Database_name,Database_accession_code,Relationship,Sf_ID,Entry_ID
BMRB,6214,Mastopran X in the other condition,15,10001
PDB,2CZP,BMRB Entry Tracking System,15,10001
PDB,1VEX,BMRB Entry Tracking System,34,10002
PDB,1WFU,BMRB Entry Tracking System,101,10006
PDB,1WFT,BMRB Entry Tracking System,120,10008
PDB,1WFW,BMRB Entry Tracking System,139,10009
PDB,2COM,BMRB Entry Tracking System,193,10011
BMRB,9500,Assigned chemical shift of actin-binding domain of troponin in Ca2+-bound state,213,10012
PDB,1VDI,BMRB Entry Tracking System,213,10012
PDB,1VDJ,Solution structure of actin-binding domain of troponin in Ca2+-bound state,213,10012
PDB,1WIL,BMRB Entry Tracking System,231,10013
PDB,2F87,BMRB Entry Tracking System,252,10014
BMRB,10017,ADP-BOUND Form of Human ABCB6 C-Terminal Domain,296,10016
BMRB,10016,the Nucleotide-Free Form of Human ABCB6 C-Terminal Domain,320,10017
PDB,2FDT,BMRB Entry Tracking System,346,10018
PDB,2RQG,BMRB Entry Tracking System,369,10019
BMRB,4146,,408,10021
PDB,2E8D,BMRB Entry Tracking System,429,10022
PDB,2DW3,BMRB Entry Tracking System,471,10024
PDB,1UL7,BMRB Entry Tracking System,490,10025
PDB,1V5S,BMRB Entry Tracking System,508,10026
PDB,2E0G,BMRB Entry Tracking System,527,10027
PDB,2DWV,BMRB Entry Tracking System,556,10028
PDB,1WFV,BMRB Entry Tracking System,574,10029
PDB,1WJO,BMRB Entry Tracking System,606,10030
PDB,1WJR,BMRB Entry Tracking System,625,10031
PDB,1WJS,BMRB Entry Tracking System,644,10032
PDB,1WJZ,BMRB Entry Tracking System,663,10033
PDB,1WK0,BMRB Entry Tracking System,682,10034
PDB,1WK1,BMRB Entry Tracking System,701,10035
PDB,1WLM,BMRB Entry Tracking System,720,10036
PDB,1WJQ,BMRB Entry Tracking System,739,10037
PDB,1WJP,BMRB Entry Tracking System,758,10038
PDB,1WGQ,BMRB Entry Tracking System,779,10039
PDB,1WGR,BMRB Entry Tracking System,811,10040
PDB,1WGS,BMRB Entry Tracking System,830,10041
PDB,1WGV,BMRB Entry Tracking System,849,10042
PDB,1WGW,BMRB Entry Tracking System,868,10043
PDB,1WH5,BMRB Entry Tracking System,887,10044
PDB,1WH7,BMRB Entry Tracking System,906,10045
PDB,1WI0,BMRB Entry Tracking System,925,10046
PDB,2ECC,BMRB Entry Tracking System,944,10047
PDB,1WJI,BMRB Entry Tracking System,963,10048
PDB,1WJT,BMRB Entry Tracking System,982,10049
PDB,1WJU,BMRB Entry Tracking System,1014,10050
PDB,1WFQ,BMRB Entry Tracking System,1103,10054
PDB,1WFS,BMRB Entry Tracking System,1122,10055
PDB,1WFY,BMRB Entry Tracking System,1141,10056
PDB,1WFZ,BMRB Entry Tracking System,1160,10057
PDB,1WIK,BMRB Entry Tracking System,1181,10058
PDB,1WIN,BMRB Entry Tracking System,1200,10059
PDB,1WJK,BMRB Entry Tracking System,1232,10060
PDB,1WJL,BMRB Entry Tracking System,1251,10061
PDB,1UE9,BMRB Entry Tracking System,1288,10063
PDB,1UEW,BMRB Entry Tracking System,1307,10064
PDB,1UFN,BMRB Entry Tracking System,1327,10065
PDB,1UFX,BMRB Entry Tracking System,1346,10066
PDB,1UHT,BMRB Entry Tracking System,1365,10067
PDB,1UJO,BMRB Entry Tracking System,1384,10068
PDB,1UJS,BMRB Entry Tracking System,1403,10069
PDB,1WEZ,BMRB Entry Tracking System,1435,10070
PDB,1WF1,BMRB Entry Tracking System,1454,10071
PDB,1WF2,BMRB Entry Tracking System,1473,10072
PDB,1WFJ,BMRB Entry Tracking System,1492,10073
PDB,1WFM,BMRB Entry Tracking System,1512,10074
PDB,1WFN,BMRB Entry Tracking System,1531,10075
PDB,1WFO,BMRB Entry Tracking System,1551,10076
PDB,1WI8,BMRB Entry Tracking System,1570,10077
PDB,1V9V,BMRB Entry Tracking System,1614,10079
PDB,1V9W,BMRB Entry Tracking System,1646,10080
PDB,1VAE,BMRB Entry Tracking System,1665,10081
PDB,1WEY,BMRB Entry Tracking System,1684,10082
PDB,1WFG,BMRB Entry Tracking System,1703,10083
PDB,1WFI,BMRB Entry Tracking System,1722,10084
PDB,1WG5,BMRB Entry Tracking System,1742,10085
PDB,1WGY,BMRB Entry Tracking System,1761,10086
PDB,1WH3,BMRB Entry Tracking System,1780,10087
PDB,1WHA,BMRB Entry Tracking System,1799,10088
PDB,1WJ1,BMRB Entry Tracking System,1818,10089
PDB,1WJJ,BMRB Entry Tracking System,1850,10090
PDB,1WJN,BMRB Entry Tracking System,1869,10091
PDB,1WH4,BMRB Entry Tracking System,1888,10092
PDB,1WH6,BMRB Entry Tracking System,1908,10093
PDB,1WH8,BMRB Entry Tracking System,1928,10094
PDB,1WH9,BMRB Entry Tracking System,1948,10095
PDB,1J0F,BMRB Entry Tracking System,1989,10097
PDB,1R79,BMRB Entry Tracking System,2009,10098
PDB,1UEM,BMRB Entry Tracking System,2030,10099
PDB,1UEP,BMRB Entry Tracking System,2063,10100
PDB,1UG7,BMRB Entry Tracking System,2083,10101
PDB,1UJT,BMRB Entry Tracking System,2102,10102
PDB,1UJU,BMRB Entry Tracking System,2124,10103
PDB,1UJX,BMRB Entry Tracking System,2143,10104
PDB,1V31,BMRB Entry Tracking System,2161,10105
PDB,1V32,BMRB Entry Tracking System,2180,10106
PDB,1V5K,BMRB Entry Tracking System,2199,10107
PDB,1V5N,BMRB Entry Tracking System,2218,10108
PDB,1V5Q,BMRB Entry Tracking System,2238,10109
PDB,1V5R,BMRB Entry Tracking System,2269,10110
PDB,1V63,BMRB Entry Tracking System,2289,10111
PDB,1V86,BMRB Entry Tracking System,2307,10112
PDB,1V5M,BMRB Entry Tracking System,2325,10113
PDB,1V5U,BMRB Entry Tracking System,2344,10114
PDB,1V88,BMRB Entry Tracking System,2363,10115
BMRB,10117,the substitution of Pro for Ala12,2382,10116
BMRB,10116,"PCP homo tetramer, mutant",2400,10117
PDB,2EXD,BMRB Entry Tracking System,2418,10118
PDB,1IUR,BMRB Entry Tracking System,2446,10119
PDB,1UFG,BMRB Entry Tracking System,2477,10120
PDB,1J26,BMRB Entry Tracking System,2496,10121
PDB,1J3T,BMRB Entry Tracking System,2515,10122
PDB,1N27,BMRB Entry Tracking System,2534,10123
PDB,1UJV,BMRB Entry Tracking System,2553,10124
PDB,1WHN,BMRB Entry Tracking System,2572,10125
PDB,1WHR,BMRB Entry Tracking System,2589,10126
PDB,1WHU,BMRB Entry Tracking System,2606,10127
PDB,1VA9,BMRB Entry Tracking System,2623,10128
PDB,1WF5,BMRB Entry Tracking System,2641,10129
PDB,1WF9,BMRB Entry Tracking System,2672,10130
PDB,1V5P,BMRB Entry Tracking System,2690,10131
BMRB,10133,1H and 15N assignment of reduced form of Pseudomonas aeruginosa cytochrome c551,2708,10132
BMRB,4578,"1H, 13C and 15N assignment of F7A/V13M/F34Y/E43Y/V78I variant of Pseudomonas aeruginosa cytochrome c551",2708,10132
BMRB,758,1H assignment of Pseudomonas aeruginosa cytochrome c551,2708,10132
BMRB,759,1H assignment of Pseudomonas aeruginosa cytochrome c551,2708,10132
BMRB,760,1H assignment of Pseudomonas aeruginosa cytochrome c551,2708,10132
BMRB,761,1H assignment of Pseudomonas aeruginosa cytochrome c551,2708,10132
BMRB,968,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2708,10132
BMRB,969,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2708,10132
BMRB,970,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2708,10132
BMRB,971,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2708,10132
PDB,2PAC,BMRB Entry Tracking System,2708,10132
BMRB,10132,1H and 15N assignment of oxidized form of Pseudomonas aeruginosa cytochrome c551,2723,10133
BMRB,4578,"1H, 13C and 15N assignment of F7A/V13M/F34Y/E43Y/V78I variant of Pseudomonas aeruginosa cytochrome c551",2723,10133
BMRB,758,1H assignment of Pseudomonas aeruginosa cytochrome c551,2723,10133
BMRB,759,1H assignment of Pseudomonas aeruginosa cytochrome c551,2723,10133
BMRB,760,1H assignment of Pseudomonas aeruginosa cytochrome c551,2723,10133
BMRB,761,1H assignment of Pseudomonas aeruginosa cytochrome c551,2723,10133
BMRB,968,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2723,10133
BMRB,969,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2723,10133
BMRB,970,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2723,10133
BMRB,971,1H and 15N assignment of Pseudomonas aeruginosa cytochrome c551 in different condition,2723,10133
PDB,2PAC,BMRB Entry Tracking System,2723,10133
BMRB,10135,1H and 15N assignment of reduced form of Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,4578,"1H, 13C and 15N assignment of F7A/V13M/F34Y/E43Y/V78I variant of homologous protein, Pseudomonas aeruginosa cytochrome c-551",2738,10134
BMRB,5086,1H assignment of reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,5087,1H assignment of oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,5088,1H assignment of reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,5089,1H assignment of oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,6033,1H and 15N assignment of C10A/C13A variant of Hydrogenobacter thermophilus cytochrome c-552,2738,10134
BMRB,10134,1H and 15N assignment of oxidized form of Hydrogenobacter thermophilus cytochrome c-552,2753,10135
BMRB,4578,"1H, 13C and 15N assignment of F7A/V13M/F34Y/E43Y/V78I variant of homologous protein, Pseudomonas aeruginosa cytochrome c-551",2753,10135
BMRB,5086,1H assignment of reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552,2753,10135
BMRB,5087,1H assignment of oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552,2753,10135
BMRB,5088,1H assignment of reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552,2753,10135
BMRB,5089,1H assignment of oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552,2753,10135
BMRB,6033,1H and 15N assignment of C10A/C13A variant of Hydrogenobacter thermophilus cytochrome c-552,2753,10135
PDB,1UFF,BMRB Entry Tracking System,2768,10136
PDB,2E4J,BMRB Entry Tracking System,2786,10137
BMRB,10139,full-length RimM (residues 1-162) in free state,2799,10138
BMRB,10140,full-length RimM and ribosomal protein S19 (rS19),2799,10138
PDB,2DOG,BMRB Entry Tracking System,2799,10138
BMRB,10138,N-terminal construct of RimM (residues 1-85),2820,10139
BMRB,10140,full-length RimM and ribosomal protein S19 (rS19),2820,10139
BMRB,10138,N-terminal construct of RimM (residues 1-85),2858,10140
BMRB,10139,full-length RimM (residues 1-162) in free state,2858,10140
PDB,2E9G,BMRB Entry Tracking System,2880,10141
PDB,2E9I,BMRB Entry Tracking System,2898,10142
PDB,2E9J,BMRB Entry Tracking System,2916,10143
PDB,2EE4,BMRB Entry Tracking System,2934,10144
PDB,2EE5,BMRB Entry Tracking System,2954,10145
PDB,2EE6,BMRB Entry Tracking System,2974,10146
PDB,2EE7,BMRB Entry Tracking System,2992,10147
PDB,2EE8,BMRB Entry Tracking System,3010,10148
PDB,2E9K,BMRB Entry Tracking System,3030,10149
PDB,2ELK,BMRB Entry Tracking System,3061,10150
PDB,2EN6,BMRB Entry Tracking System,3079,10151
PDB,2EN7,BMRB Entry Tracking System,3099,10152
PDB,2EOV,BMRB Entry Tracking System,3119,10153
PDB,2EOY,BMRB Entry Tracking System,3139,10154
PDB,2EP2,BMRB Entry Tracking System,3159,10155
PDB,2YTS,BMRB Entry Tracking System,3179,10156
PDB,2EOS,BMRB Entry Tracking System,3199,10157
PDB,2EOU,BMRB Entry Tracking System,3219,10158
PDB,2EE9,BMRB Entry Tracking System,3239,10159
PDB,2EEA,BMRB Entry Tracking System,3270,10160
PDB,2EEB,BMRB Entry Tracking System,3288,10161
PDB,2EEC,BMRB Entry Tracking System,3306,10162
PDB,2EED,BMRB Entry Tracking System,3324,10163
PDB,2EEE,BMRB Entry Tracking System,3342,10164
PDB,2EEF,BMRB Entry Tracking System,3360,10165
PDB,2EM1,BMRB Entry Tracking System,3378,10166
PDB,2EM2,BMRB Entry Tracking System,3398,10167
PDB,2EM3,BMRB Entry Tracking System,3418,10168
PDB,2EN8,BMRB Entry Tracking System,3438,10169
PDB,2EN9,BMRB Entry Tracking System,3471,10170
PDB,2ENA,BMRB Entry Tracking System,3491,10171
PDB,2ENC,BMRB Entry Tracking System,3511,10172
PDB,2ENE,BMRB Entry Tracking System,3531,10173
PDB,2ENF,BMRB Entry Tracking System,3551,10174
PDB,2ENH,BMRB Entry Tracking System,3571,10175
PDB,2YTM,BMRB Entry Tracking System,3591,10176
PDB,2YTP,BMRB Entry Tracking System,3611,10177
PDB,2YTT,BMRB Entry Tracking System,3631,10178
PDB,2EM4,BMRB Entry Tracking System,3651,10179
PDB,2EM7,BMRB Entry Tracking System,3684,10180
PDB,2EM9,BMRB Entry Tracking System,3704,10181
PDB,2EME,BMRB Entry Tracking System,3724,10182
PDB,2EMF,BMRB Entry Tracking System,3744,10183
PDB,2EMG,BMRB Entry Tracking System,3764,10184
PDB,2YTF,BMRB Entry Tracking System,3784,10185
PDB,2YTG,BMRB Entry Tracking System,3804,10186
PDB,2YTI,BMRB Entry Tracking System,3844,10188
PDB,2EOM,BMRB Entry Tracking System,3864,10189
PDB,2EOP,BMRB Entry Tracking System,3917,10191
PDB,2EOQ,BMRB Entry Tracking System,3937,10192
PDB,2YUM,BMRB Entry Tracking System,3957,10193
PDB,2YUO,BMRB Entry Tracking System,3975,10194
PDB,2YUP,BMRB Entry Tracking System,3993,10195
PDB,2EM5,BMRB Entry Tracking System,4011,10196
PDB,2EM6,BMRB Entry Tracking System,4031,10197
PDB,2EM8,BMRB Entry Tracking System,4051,10198
PDB,2EMA,BMRB Entry Tracking System,4071,10199
PDB,2EMB,BMRB Entry Tracking System,4117,10200
PDB,2EMC,BMRB Entry Tracking System,4137,10201
PDB,2EMH,BMRB Entry Tracking System,4157,10202
PDB,2EMI,BMRB Entry Tracking System,4177,10203
PDB,2EMJ,BMRB Entry Tracking System,4197,10204
PDB,2EMK,BMRB Entry Tracking System,4217,10205
PDB,2EOH,BMRB Entry Tracking System,4237,10206
PDB,2EOW,BMRB Entry Tracking System,4257,10207
PDB,2EOX,BMRB Entry Tracking System,4277,10208
PDB,2EOZ,BMRB Entry Tracking System,4297,10209
PDB,2EP0,BMRB Entry Tracking System,4330,10210
PDB,2YUQ,BMRB Entry Tracking System,4350,10211
PDB,2CUD,BMRB Entry Tracking System,4368,10212
PDB,2E29,BMRB Entry Tracking System,4386,10213
PDB,2YSE,BMRB Entry Tracking System,4406,10214
PDB,2ZAJ,BMRB Entry Tracking System,4424,10215
PDB,2EOF,BMRB Entry Tracking System,4442,10216
PDB,2EOG,BMRB Entry Tracking System,4462,10217
PDB,2EOJ,BMRB Entry Tracking System,4482,10218
PDB,2EOK,BMRB Entry Tracking System,4502,10219
PDB,2EON,BMRB Entry Tracking System,4535,10220
PDB,2EOR,BMRB Entry Tracking System,4555,10221
PDB,2YTQ,BMRB Entry Tracking System,4575,10222
PDB,2YTR,BMRB Entry Tracking System,4595,10223
PDB,2EMV,BMRB Entry Tracking System,4615,10224
PDB,2EMW,BMRB Entry Tracking System,4635,10225
PDB,2EMX,BMRB Entry Tracking System,4655,10226
PDB,2EMY,BMRB Entry Tracking System,4675,10227
PDB,2EMZ,BMRB Entry Tracking System,4695,10228
PDB,2EN0,BMRB Entry Tracking System,4715,10229
PDB,2EN1,BMRB Entry Tracking System,4748,10230
PDB,2EN2,BMRB Entry Tracking System,4768,10231
PDB,2EN3,BMRB Entry Tracking System,4788,10232
PDB,2EN4,BMRB Entry Tracking System,4808,10233
PDB,2YU8,BMRB Entry Tracking System,4828,10234
PDB,1WGU,BMRB Entry Tracking System,4848,10235
PDB,2ROZ,BMRB Entry Tracking System,4866,10236
PDB,2YSZ,BMRB Entry Tracking System,4885,10237
PDB,2YT0,BMRB Entry Tracking System,4903,10238
PDB,2YT1,BMRB Entry Tracking System,4921,10239
PDB,1X69,BMRB Entry Tracking System,4953,10240
PDB,1X6B,BMRB Entry Tracking System,4971,10241
PDB,1X6D,BMRB Entry Tracking System,4989,10242
PDB,1X6E,BMRB Entry Tracking System,5007,10243
PDB,1X6F,BMRB Entry Tracking System,5027,10244
PDB,1X6G,BMRB Entry Tracking System,5047,10245
PDB,1X6H,BMRB Entry Tracking System,5065,10246
PDB,2CO8,BMRB Entry Tracking System,5085,10247
PDB,1WZ6,BMRB Entry Tracking System,5105,10248
PDB,1X05,BMRB Entry Tracking System,5123,10249
PDB,1X1F,BMRB Entry Tracking System,5154,10250
PDB,1X1G,BMRB Entry Tracking System,5172,10251
PDB,2CO9,BMRB Entry Tracking System,5190,10252
PDB,2COA,BMRB Entry Tracking System,5208,10253
PDB,2COC,BMRB Entry Tracking System,5226,10254
PDB,2COD,BMRB Entry Tracking System,5244,10255
PDB,2COF,BMRB Entry Tracking System,5262,10256
PDB,2DJR,BMRB Entry Tracking System,5280,10257
PDB,2DJS,BMRB Entry Tracking System,5300,10258
PDB,2DJT,BMRB Entry Tracking System,5318,10259
PDB,2DJU,BMRB Entry Tracking System,5336,10260
PDB,2DJV,BMRB Entry Tracking System,5354,10261
PDB,2DKM,BMRB Entry Tracking System,5372,10262
PDB,2DN7,BMRB Entry Tracking System,5390,10263
PDB,1X5B,BMRB Entry Tracking System,5408,10264
PDB,2EDX,BMRB Entry Tracking System,5426,10265
PDB,2EDY,BMRB Entry Tracking System,5444,10266
PDB,2EDZ,BMRB Entry Tracking System,5462,10267
PDB,2EE0,BMRB Entry Tracking System,5480,10268
PDB,2EE1,BMRB Entry Tracking System,5498,10269
PDB,2EE2,BMRB Entry Tracking System,5529,10270
PDB,2EE3,BMRB Entry Tracking System,5547,10271
PDB,2EKH,BMRB Entry Tracking System,5565,10272
PDB,2EKI,BMRB Entry Tracking System,5583,10273
PDB,2EKJ,BMRB Entry Tracking System,5601,10274
PDB,2YU0,BMRB Entry Tracking System,5619,10275
PDB,2D9T,BMRB Entry Tracking System,5637,10276
PDB,2D9U,BMRB Entry Tracking System,5655,10277
PDB,2D9V,BMRB Entry Tracking System,5673,10278
PDB,2D9W,BMRB Entry Tracking System,5691,10279
PDB,2D9X,BMRB Entry Tracking System,5722,10280
PDB,2CUE,BMRB Entry Tracking System,5740,10281
PDB,2CUF,BMRB Entry Tracking System,5758,10282
PDB,2DA1,BMRB Entry Tracking System,5776,10283
PDB,2DA2,BMRB Entry Tracking System,5794,10284
PDB,2DA3,BMRB Entry Tracking System,5812,10285
PDB,2DA4,BMRB Entry Tracking System,5830,10286
PDB,2DA5,BMRB Entry Tracking System,5848,10287
PDB,2DA6,BMRB Entry Tracking System,5866,10288
PDB,2DA7,BMRB Entry Tracking System,5884,10289
PDB,2DJN,BMRB Entry Tracking System,5915,10290
PDB,2DMN,BMRB Entry Tracking System,5933,10291
PDB,2DMP,BMRB Entry Tracking System,5951,10292
PDB,2DMQ,BMRB Entry Tracking System,5969,10293
PDB,2DMS,BMRB Entry Tracking System,5987,10294
PDB,2DMT,BMRB Entry Tracking System,6005,10295
PDB,2DMU,BMRB Entry Tracking System,6023,10296
PDB,2E19,BMRB Entry Tracking System,6041,10297
PDB,2YS9,BMRB Entry Tracking System,6059,10298
PDB,2DB8,BMRB Entry Tracking System,6077,10299
PDB,2DBJ,BMRB Entry Tracking System,6121,10300
PDB,2DBK,BMRB Entry Tracking System,6139,10301
PDB,2DBM,BMRB Entry Tracking System,6157,10302
PDB,2EML,BMRB Entry Tracking System,6175,10303
PDB,2EMM,BMRB Entry Tracking System,6195,10304
PDB,2EMP,BMRB Entry Tracking System,6215,10305
PDB,2YRM,BMRB Entry Tracking System,6235,10306
PDB,2YTD,BMRB Entry Tracking System,6255,10307
PDB,2YTE,BMRB Entry Tracking System,6275,10308
PDB,2YTJ,BMRB Entry Tracking System,6295,10309
PDB,2YTK,BMRB Entry Tracking System,6328,10310
PDB,2D9Y,BMRB Entry Tracking System,6348,10311
PDB,2D9Z,BMRB Entry Tracking System,6366,10312
PDB,2DA0,BMRB Entry Tracking System,6384,10313
PDB,2DHI,BMRB Entry Tracking System,6402,10314
PDB,2DHJ,BMRB Entry Tracking System,6420,10315
PDB,2DHK,BMRB Entry Tracking System,6438,10316
PDB,2DKP,BMRB Entry Tracking System,6456,10317
PDB,2DN6,BMRB Entry Tracking System,6492,10319
PDB,2DI9,BMRB Entry Tracking System,6523,10320
PDB,2DIB,BMRB Entry Tracking System,6541,10321
PDB,2DIC,BMRB Entry Tracking System,6559,10322
PDB,2DJ4,BMRB Entry Tracking System,6577,10323
PDB,2DLG,BMRB Entry Tracking System,6595,10324
PDB,2DMB,BMRB Entry Tracking System,6613,10325
PDB,2DMC,BMRB Entry Tracking System,6631,10326
PDB,2DS4,BMRB Entry Tracking System,6649,10327
PDB,2D7M,BMRB Entry Tracking System,6667,10328
PDB,2D7N,BMRB Entry Tracking System,6685,10329
PDB,2D7O,BMRB Entry Tracking System,6716,10330
PDB,2D7P,BMRB Entry Tracking System,6734,10331
PDB,2D7Q,BMRB Entry Tracking System,6752,10332
PDB,2DI7,BMRB Entry Tracking System,6770,10333
PDB,2DI8,BMRB Entry Tracking System,6788,10334
PDB,2DIA,BMRB Entry Tracking System,6806,10335
PDB,1WWY,BMRB Entry Tracking System,6824,10336
PDB,2E5K,BMRB Entry Tracking System,6858,10337
PDB,2RLG,BMRB Entry Tracking System,7335,11002
PDB,2RLH,BMRB Entry Tracking System,7352,11003
PDB,2RLJ,BMRB Entry Tracking System,7369,11004
PDB,2RQZ,BMRB Entry Tracking System,7404,11006
PDB,2RLY,BMRB Entry Tracking System,7423,11007
PDB,2RM0,BMRB Entry Tracking System,7446,11008
PDB,2RM4,BMRB Entry Tracking System,7469,11009
PDB,2VC8,Human Homologue,7469,11009
PDB,2RMK,BMRB Entry Tracking System,7501,11010
PDB,1OQ3,the structure of the S46V mutant of CopA,7526,11011
PDB,2RML,BMRB Entry Tracking System,7526,11011
PDB,1KIS,Lower affinity aptamer - HIV TAR kissing complex,7580,11014
PDB,2RN1,BMRB Entry Tracking System,7580,11014
PDB,2RN5,BMRB Entry Tracking System,7610,11016
PDB,2RN8,BMRB Entry Tracking System,7668,11018
BMRB,11020,Chemical shifts of of the Cu(I) form of human Cox17,7686,11019
PDB,2RN9,BMRB Entry Tracking System,7686,11019
PDB,2rnb,Solution structure of the Cu(I) form of human Cox17,7686,11019
BMRB,11019,Chemical shifts of of the apo form of human Cox17,7722,11020
PDB,2rn9,Solution structure of the apo form of human Cox17,7722,11020
PDB,2RNB,BMRB Entry Tracking System,7722,11020
PDB,1UAO,Solution structure of chignolin,7749,11021
PDB,2ZEI,"CRYSTAL STRUCTURE OF THE MUTANT OF CHIGNOLIN, CLN025",7749,11021
PDB,2RNG,BMRB Entry Tracking System,7768,11022
PDB,2RNJ,BMRB Entry Tracking System,7784,11024
BMRB,11043,NMR assignment for the mutant protein on a different condition,7802,11026
PDB,2RMO,BMRB Entry Tracking System,7802,11026
BMRB,11064,A more extended version of 11028,7836,11028
PDB,2RNM,Structure of the HET-s(218-289) amyloid fibrils.,7836,11028
PDB,,A better resolved version of 2RNM,7836,11028
PDB,1V66,Entry contains the 3D-structure of human homologue of this protein.,7856,11029
PDB,2RNN,BMRB Entry Tracking System,7856,11029
PDB,1V66,Entry contains the 3D-structure of human homologue of this protein.,7879,11030
PDB,2RNO,BMRB Entry Tracking System,7879,11030
BMRB,15285,N-Me-Lys11,25804,15282
PDB,2rm8,Entry containing coordinate and constraints for this molecular system,7902,11031
BMRB,11033,"the presumed chromodomain of the yeast histone acetyl transferase protein, Esa1",7919,11032
EMBL,CAA99465.1,hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).,7919,11032
EMBL,Z75152,S.cerevisiae chromosome XV reading frame ORF YOR244w.,7919,11032
NCBI Protein,NP_014887.1,"Histone acetyltransferase catalytic subunit of the native multisubunit complex
(NuA4), Esa1p [Saccharomyces cerevisiae]",7919,11032
Protein Information Resource,S67137,hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).,7919,11032
Saccharomyces Genome Database,S000005770,ESA1/YOR244W,7919,11032
Swiss-Prot,Q08649,Histone acetyltransferase ESA1,7919,11032
BMRB,11032,"the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1",7938,11033
EMBL,CAA99465.1,hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).,7938,11033
EMBL,Z75152,S.cerevisiae chromosome XV reading frame ORF YOR244w.,7938,11033
NCBI Protein,NP_014887.1,"Histone acetyltransferase catalytic subunit of the native multisubunit complex 
(NuA4), Esa1p [Saccharomyces cerevisiae]",7938,11033
PDB,2RNZ,BMRB Entry Tracking System,7938,11033
Protein Information Resource,S67137,hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).,7938,11033
Saccharomyces Genome Database,S000005770,ESA1/YOR244W,7938,11033
Swiss-Prot,Q08649,Histone acetyltransferase ESA1,7938,11033
PDB,2RO5,BMRB Entry Tracking System,7957,11034
BMRB,11037,Entry containing chemical shift data for the same protein in cell,7974,11035
PDB,2roe,Entry containing coordinates for the same protein in vitro,7974,11035
PDB,2rog,Entry containing coordinates for the same protein in cell,7974,11035
BMRB,11035,Entry containing chemical shift data for the same protein in vitro,8009,11037
PDB,2roe,Entry containing coordinates for the same protein in vitro,8009,11037
PDB,2rog,Entry containing coordinates for the same protein in cell,8009,11037
PDB,2ROH,BMRB Entry Tracking System,8025,11038
PDB,2ROL,BMRB Entry Tracking System,8060,11040
EMBL,P35670,Wilson protein,8079,11041
PDB,2ROP,BMRB Entry Tracking System,8079,11041
PDB,2KHE,BMRB Entry Tracking System,8095,11042
BMRB,11026,NMR assignment for the mutant protein on a different condition,8115,11043
PDB,2ROT,BMRB Entry Tracking System,8115,11043
PDB,2ROO,BMRB Entry Tracking System,8133,11044
BMRB,11046,Structure of d(TACG) bound to structurally distinct recombinase hsRad51,8150,11045
BMRB,11047,Structure of d(TACG) bound to structurally distinct recombinase ttRecO,8150,11045
BMRB,11048,Structure of d(TACG) bound to structurally distinct recombinase ecRecT,8150,11045
PDB,2RPD,BMRB Entry Tracking System,8150,11045
BMRB,11045,Structure of d(TACG) bound to structurally distinct recombinase Mhr1p,8165,11046
BMRB,11047,Structure of d(TACG) bound to structurally distinct recombinase ttRecO,8165,11046
BMRB,11048,Structure of d(TACG) bound to structurally distinct recombinase ecRecT,8165,11046
PDB,2RPE,BMRB Entry Tracking System,8165,11046
BMRB,11045,Structure of d(TACG) bound to structurally distinct recombinase Mhr1p,8180,11047
BMRB,11046,Structure of d(TACG) bound to structurally distinct recombinase hsRad51,8180,11047
BMRB,11048,Structure of d(TACG) bound to structurally distinct recombinase ecRecT,8180,11047
BMRB,11045,Structure of d(TACG) bound to structurally distinct recombinase Mhr1p,8195,11048
BMRB,11046,Structure of d(TACG) bound to structurally distinct recombinase hsRad51,8195,11048
BMRB,11047,Structure of d(TACG) bound to structurally distinct recombinase ttRecO,8195,11048
PDB,2RPH,BMRB Entry Tracking System,8195,11048
PDB,2rmy,Structure of the N-terminal BARpeptide in SDS micelles,8210,11049
PDB,2RND,BMRB Entry Tracking System,8210,11049
BMRB,11049,NMR Assignment of the N-terminal BARpeptide in DPC micelles,8238,11050
PDB,2RMY,BMRB Entry Tracking System,8238,11050
PDB,2rnd,Structure of the N-terminal BARpeptide in DPC micelles,8238,11050
BMRB,11052,"two-disulfide variant of lysozyme 2SS[6-127, 64-80] with Cys6-Cys127 and
Cys64-Cys80",8252,11051
BMRB,11051,0SS-variant of lysozyme lacking all of the disulfide bridges,8268,11052
PDB,2RPS,BMRB Entry Tracking System,8302,11054
PDB,1X0N,NMR structure of Grb2 SH2 domain complexed with the inhibitor,8323,11055
BMRB,11059,Chemical shift data for PACAP27,8374,11058
PDB,,,8374,11058
BMRB,11058,Chemical shift data for PACAP21 which is PACAP27's C-terminal truncated form bound to membranes,8392,11059
PDB,2RPB,BMRB Entry Tracking System,8411,11060
PDB,2RPZ,BMRB Entry Tracking System,8432,11061
PDB,2RQ0,BMRB Entry Tracking System,8454,11062
BMRB,11028,Solid-state NMR assignment of the HET-s(218-289) amyloid fibrils.,8484,11064
PDB,2LBU,BMRB Entry Tracking System,8484,11064
PDB,2RNM,Structure of the HET-s(218-289) amyloid fibrils.,8484,11064
PDB,1GG3,,8507,11065
PDB,2RQ1,BMRB Entry Tracking System,8507,11065
PDB,1N9P,"Crystal structure of the cytoplasmic domain of G-protein activated inward
rectifier potassium channel 1",8528,11067
PDB,1U4E,Crystal structure of cytoplasmic domains of GIRK1 channel,8528,11067
PDB,2QKS,Crystal structure of a Kir3.1-prokaryotic Kir channel chimera,8528,11067
BMRB,11069,solution structure of 1-28 GBP (growth-blocking peptide),8544,11068
BMRB,11070,DPC micelle bound structure of 1-28 GBP (growth-blocking peptide),8544,11068
BMRB,11068,solution structure of 1-23 GBP (growth-blocking peptide),8558,11069
BMRB,11070,DPC micelle bound structure of 1-28 GBP (growth-blocking peptide),8558,11069
BMRB,11068,solution structure of 1-23 GBP (growth-blocking peptide),8587,11070
BMRB,11069,solution structure of 1-28 GBP (growth-blocking peptide),8587,11070
PDB,2RQ2,BMRB Entry Tracking System,8603,11072
PDB,2YUR,BMRB Entry Tracking System,10333,11159
BMRB,16021,NMR assignments of juvenile hormone binding protein in complex with JH III,8621,11073
PDB,2RQF,BMRB Entry Tracking System,8621,11073
PDB,2RPA,Solution structure of N-terminal domain of microtubule severing enzyme,8663,11075
PDB,2I9S,The solution structure of the core of mesoderm development (MESD),8684,11076
PDB,2RQK,BMRB Entry Tracking System,8684,11076
PDB,2RQM,NMR Solution Structure of Mesoderm Development (MESD) - open conformation,8684,11076
PDB,2RQL,BMRB Entry Tracking System,8714,11077
PDB,2Z5V,BMRB Entry Tracking System,8734,11078
PDB,2RQS,BMRB Entry Tracking System,8768,11080
BMRB,11082,"Chemical shift assignments of the complex between the DDEF1 SH3 domain and the 
APC SAMP1 motif",8791,11081
PDB,2RQT,BMRB Entry Tracking System,8791,11081
PDB,2RQU,"Solution structure of the complex between the DDEF1 SH3 domain and the APC 
SAMP1 motif",8791,11081
BMRB,11081,Chemical shift assignments of the the human DDEF1 SH3 domain,8814,11082
PDB,2RQT,Solution structure of the human DDEF1 SH3 domain,8814,11082
PDB,2RQU,BMRB Entry Tracking System,8814,11082
PDB,2ELL,BMRB Entry Tracking System,8837,11083
PDB,1WYN,BMRB Entry Tracking System,8855,11084
PDB,1WYL,BMRB Entry Tracking System,8873,11085
PDB,1WYO,BMRB Entry Tracking System,8891,11086
PDB,2YS3,BMRB Entry Tracking System,8909,11087
PDB,2YS1,BMRB Entry Tracking System,8927,11088
PDB,2YRY,BMRB Entry Tracking System,8945,11089
PDB,2YS4,BMRB Entry Tracking System,8979,11090
PDB,2E6J,BMRB Entry Tracking System,8997,11091
PDB,2EFI,BMRB Entry Tracking System,9015,11092
PDB,2E6I,BMRB Entry Tracking System,9033,11093
BMRB,11095,Chemical shift assignments of the chimera of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK,9053,11094
PDB,2YS5,BMRB Entry Tracking System,9053,11094
PDB,2yt2,Solution structure of the chimera of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK,9053,11094
BMRB,11094,Chemical shift assignments of the complex of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK,9072,11095
PDB,2ys5,Solution structure of the complex of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of hALK,9072,11095
PDB,2YT2,BMRB Entry Tracking System,9072,11095
PDB,2ED7,BMRB Entry Tracking System,9090,11096
PDB,2EDD,BMRB Entry Tracking System,9108,11097
PDB,2EDE,BMRB Entry Tracking System,9126,11098
PDB,2EDB,BMRB Entry Tracking System,9144,11099
PDB,2DML,BMRB Entry Tracking System,9178,11100
PDB,2DJ1,BMRB Entry Tracking System,9196,11101
PDB,2DMM,BMRB Entry Tracking System,9214,11102
PDB,2ED8,BMRB Entry Tracking System,9232,11103
PDB,2DJ2,BMRB Entry Tracking System,9250,11104
PDB,2DJ0,BMRB Entry Tracking System,9268,11105
PDB,2DMK,BMRB Entry Tracking System,9286,11106
PDB,2DIZ,BMRB Entry Tracking System,9304,11107
PDB,2DIY,BMRB Entry Tracking System,9322,11108
PDB,2DJ3,BMRB Entry Tracking System,9340,11109
PDB,2CUM,BMRB Entry Tracking System,9374,11110
PDB,1X5K,BMRB Entry Tracking System,9392,11111
PDB,1X5I,BMRB Entry Tracking System,9410,11112
PDB,1X5E,BMRB Entry Tracking System,9428,11113
PDB,1X5C,BMRB Entry Tracking System,9446,11114
PDB,2E61,free state structure of zf-CW,9464,11115
PDB,2RR4,BMRB Entry Tracking System,9464,11115
PDB,1X5D,BMRB Entry Tracking System,9488,11116
PDB,1X5A,BMRB Entry Tracking System,9506,11117
PDB,1X5J,BMRB Entry Tracking System,9524,11118
PDB,1X5F,BMRB Entry Tracking System,9542,11119
PDB,1X5H,BMRB Entry Tracking System,9576,11120
PDB,1X5G,BMRB Entry Tracking System,9594,11121
PDB,2DBA,BMRB Entry Tracking System,9612,11122
PDB,2YUS,BMRB Entry Tracking System,9630,11123
PDB,1WYP,BMRB Entry Tracking System,9648,11124
PDB,1X4X,BMRB Entry Tracking System,9666,11125
PDB,1WYQ,BMRB Entry Tracking System,9684,11126
PDB,1X4Z,BMRB Entry Tracking System,9702,11127
PDB,1X4Y,BMRB Entry Tracking System,9720,11128
PDB,1WYR,BMRB Entry Tracking System,9738,11129
PDB,2CTD,BMRB Entry Tracking System,9772,11130
PDB,1X4U,BMRB Entry Tracking System,9792,11131
PDB,2CTO,BMRB Entry Tracking System,9812,11132
PDB,2D85,BMRB Entry Tracking System,9830,11133
PDB,2D7L,BMRB Entry Tracking System,9848,11134
PDB,2CTJ,BMRB Entry Tracking System,9866,11135
PDB,2CTK,BMRB Entry Tracking System,9884,11136
PDB,2CTM,BMRB Entry Tracking System,9902,11137
PDB,2CTL,BMRB Entry Tracking System,9920,11138
PDB,2CTE,BMRB Entry Tracking System,9938,11139
PDB,2CTF,BMRB Entry Tracking System,9972,11140
PDB,2D86,BMRB Entry Tracking System,9990,11141
PDB,2D87,BMRB Entry Tracking System,10008,11142
PDB,2D88,BMRB Entry Tracking System,10026,11143
PDB,2YUA,BMRB Entry Tracking System,10044,11144
PDB,2D89,BMRB Entry Tracking System,10062,11145
PDB,2E9H,BMRB Entry Tracking System,10080,11146
PDB,2YRQ,BMRB Entry Tracking System,10100,11147
PDB,2YRP,BMRB Entry Tracking System,10118,11148
PDB,2RR5,Structural study of the UBA domain of p62 and its interaction with ubiquitin,10136,11149
PDB,3AH0,Free-form,10136,11149
PDB,2YS0,BMRB Entry Tracking System,10168,11150
PDB,2YUU,BMRB Entry Tracking System,10186,11151
PDB,2YRZ,BMRB Entry Tracking System,10206,11152
PDB,2ED1,BMRB Entry Tracking System,10224,11153
PDB,2ECZ,BMRB Entry Tracking System,10242,11154
PDB,2ED0,BMRB Entry Tracking System,10260,11155
PDB,2YUN,BMRB Entry Tracking System,10277,11156
PDB,2YS2,BMRB Entry Tracking System,10295,11157
PDB,2YUL,BMRB Entry Tracking System,10315,11158
PDB,2YUK,BMRB Entry Tracking System,10369,11160
PDB,2ECW,BMRB Entry Tracking System,10387,11161
PDB,2ECT,BMRB Entry Tracking System,10407,11162
PDB,2ECV,BMRB Entry Tracking System,10427,11163
PDB,2ECY,BMRB Entry Tracking System,10447,11164
PDB,2EOI,BMRB Entry Tracking System,10467,11165
PDB,2EOL,BMRB Entry Tracking System,10487,11166
PDB,2EOE,BMRB Entry Tracking System,10507,11167
PDB,2YTN,BMRB Entry Tracking System,10527,11168
PDB,2EP1,BMRB Entry Tracking System,10547,11169
PDB,2EP3,BMRB Entry Tracking System,10583,11170
PDB,2YTO,BMRB Entry Tracking System,10603,11171
PDB,2DAG,BMRB Entry Tracking System,10642,11173
PDB,2RR8,BMRB Entry Tracking System,10660,11175
PDB,1UGV,BMRB Entry Tracking System,10708,11178
PDB,1WI7,BMRB Entry Tracking System,10726,11179
PDB,1WIE,BMRB Entry Tracking System,10744,11180
PDB,1WJ3,BMRB Entry Tracking System,10762,11181
PDB,2CSS,BMRB Entry Tracking System,10780,11182
PDB,2CSP,BMRB Entry Tracking System,10799,11183
PDB,2CSQ,BMRB Entry Tracking System,10817,11184
PDB,2CSI,BMRB Entry Tracking System,10835,11185
PDB,2D92,BMRB Entry Tracking System,10853,11186
PDB,2DAZ,BMRB Entry Tracking System,10871,11187
PDB,2DB5,BMRB Entry Tracking System,10889,11188
PDB,2DLU,BMRB Entry Tracking System,10907,11189
PDB,2DMZ,BMRB Entry Tracking System,10925,11190
PDB,2DM8,BMRB Entry Tracking System,10944,11191
PDB,2DLT,BMRB Entry Tracking System,10962,11192
PDB,2EGA,BMRB Entry Tracking System,10980,11193
PDB,2EGC,BMRB Entry Tracking System,10998,11194
PDB,2DLS,BMRB Entry Tracking System,11016,11195
PDB,2EGE,BMRB Entry Tracking System,11034,11196
PDB,2EHR,BMRB Entry Tracking System,11052,11197
PDB,1UM7,BMRB Entry Tracking System,11070,11198
PDB,1WF7,BMRB Entry Tracking System,11088,11199
PDB,1VA8,BMRB Entry Tracking System,11132,11200
PDB,1WH1,BMRB Entry Tracking System,11150,11201
PDB,1WF8,BMRB Entry Tracking System,11168,11202
PDB,1X5M,BMRB Entry Tracking System,11186,11203
PDB,1X5N,BMRB Entry Tracking System,11204,11204
PDB,2COT,BMRB Entry Tracking System,11222,11205
PDB,1X5R,BMRB Entry Tracking System,11242,11206
PDB,1X5Q,BMRB Entry Tracking System,11261,11207
PDB,1X5L,BMRB Entry Tracking System,11280,11208
PDB,1X43,BMRB Entry Tracking System,11299,11209
PDB,1X45,BMRB Entry Tracking System,11317,11210
PDB,1X44,BMRB Entry Tracking System,11335,11211
PDB,2DAV,BMRB Entry Tracking System,11354,11212
PDB,2D8H,BMRB Entry Tracking System,11373,11213
PDB,2D8J,BMRB Entry Tracking System,11391,11214
PDB,2D8I,BMRB Entry Tracking System,11409,11215
PDB,2D90,BMRB Entry Tracking System,11427,11216
PDB,2DL4,BMRB Entry Tracking System,11446,11217
PDB,2EEL,BMRB Entry Tracking System,11464,11218
PDB,2DL3,BMRB Entry Tracking System,11482,11219
PDB,2DL7,BMRB Entry Tracking System,11501,11220
PDB,2E6Q,BMRB Entry Tracking System,11519,11221
PDB,2DL5,BMRB Entry Tracking System,11537,11222
PDB,2DL9,BMRB Entry Tracking System,11555,11223
PDB,2EQI,BMRB Entry Tracking System,11573,11224
PDB,2DL8,BMRB Entry Tracking System,11591,11225
PDB,2E7K,BMRB Entry Tracking System,11609,11226
PDB,2E7H,BMRB Entry Tracking System,11627,11227
PDB,2YSQ,BMRB Entry Tracking System,11645,11228
PDB,2E6P,BMRB Entry Tracking System,11663,11229
PDB,2E7B,BMRB Entry Tracking System,11681,11230
PDB,2YRL,BMRB Entry Tracking System,11699,11231
PDB,2E7M,BMRB Entry Tracking System,11718,11232
PDB,2DLP,BMRB Entry Tracking System,11736,11233
PDB,2YSL,BMRB Entry Tracking System,11754,11234
PDB,2E7C,BMRB Entry Tracking System,11774,11235
PDB,2YR3,BMRB Entry Tracking System,11792,11236
PDB,2YSM,BMRB Entry Tracking System,11810,11237
PDB,2YRH,BMRB Entry Tracking System,11831,11238
PDB,2YRJ,BMRB Entry Tracking System,11851,11239
PDB,2COO,BMRB Entry Tracking System,11871,11240
PDB,2DLM,BMRB Entry Tracking System,11889,11242
PDB,2EQR,BMRB Entry Tracking System,11907,11244
PDB,1UH6,BMRB Entry Tracking System,11925,11245
PDB,1WLN,BMRB Entry Tracking System,11943,11246
PDB,2CSW,BMRB Entry Tracking System,11961,11247
PDB,2YUB,BMRB Entry Tracking System,11980,11248
BMRB,11071,Assignment of Apo-form GrxS14 from Populus trichocarpa,11998,11249
PDB,2RRE,BMRB Entry Tracking System,12019,11250
PDB,2RRF,BMRB Entry Tracking System,12040,11251
PDB,2RRD,BMRB Entry Tracking System,12058,11252
PDB,1V5O,BMRB Entry Tracking System,12077,11253
PDB,1V6E,BMRB Entry Tracking System,12095,11254
PDB,1V95,BMRB Entry Tracking System,12113,11255
PDB,1WGG,BMRB Entry Tracking System,12131,11256
PDB,1WGH,BMRB Entry Tracking System,12149,11257
PDB,1WGK,BMRB Entry Tracking System,12167,11258
PDB,1WGL,BMRB Entry Tracking System,12185,11259
PDB,1WGN,BMRB Entry Tracking System,12203,11260
PDB,1WX7,BMRB Entry Tracking System,12221,11261
PDB,1WX8,BMRB Entry Tracking System,12239,11262
PDB,1WX9,BMRB Entry Tracking System,12257,11263
PDB,1WXA,BMRB Entry Tracking System,12275,11264
PDB,1WXM,BMRB Entry Tracking System,12293,11265
PDB,1WY8,BMRB Entry Tracking System,12311,11266
PDB,1WZ0,BMRB Entry Tracking System,12329,11267
PDB,1X1M,BMRB Entry Tracking System,12347,11268
PDB,2DAE,BMRB Entry Tracking System,12365,11269
PDB,2DAF,BMRB Entry Tracking System,12396,11270
PDB,2DAH,BMRB Entry Tracking System,12414,11271
PDB,2DAJ,BMRB Entry Tracking System,12432,11272
PDB,2DAL,BMRB Entry Tracking System,12450,11273
PDB,2DAM,BMRB Entry Tracking System,12468,11274
PDB,2DHX,BMRB Entry Tracking System,12486,11275
PDB,2DHY,BMRB Entry Tracking System,12504,11276
PDB,2DHZ,BMRB Entry Tracking System,12522,11277
PDB,2DI0,BMRB Entry Tracking System,12540,11278
PDB,2DZI,BMRB Entry Tracking System,12558,11279
PDB,2DZJ,BMRB Entry Tracking System,12589,11280
PDB,2DZK,BMRB Entry Tracking System,12607,11281
PDB,2DZL,BMRB Entry Tracking System,12625,11282
PDB,2DZM,BMRB Entry Tracking System,12643,11283
PDB,1WXT,BMRB Entry Tracking System,12661,11284
PDB,1WXU,BMRB Entry Tracking System,12679,11285
PDB,1X3A,BMRB Entry Tracking System,12697,11286
PDB,1X3C,BMRB Entry Tracking System,12715,11287
PDB,1X3D,BMRB Entry Tracking System,12735,11288
PDB,1X3H,BMRB Entry Tracking System,12753,11289
PDB,1X5X,BMRB Entry Tracking System,12786,11290
PDB,1X5Y,BMRB Entry Tracking System,12804,11291
PDB,1X5Z,BMRB Entry Tracking System,12822,11292
PDB,2CU8,BMRB Entry Tracking System,12840,11293
PDB,2DAW,BMRB Entry Tracking System,12860,11294
PDB,2DAX,BMRB Entry Tracking System,12878,11295
PDB,2DAY,BMRB Entry Tracking System,12896,11296
PDB,2DIG,BMRB Entry Tracking System,12914,11297
PDB,2DII,BMRB Entry Tracking System,12932,11298
PDB,2DIL,BMRB Entry Tracking System,12950,11299
PDB,2DIM,BMRB Entry Tracking System,12968,11300
PDB,2DIN,BMRB Entry Tracking System,12986,11301
PDB,2DMD,BMRB Entry Tracking System,13004,11302
PDB,2DMF,BMRB Entry Tracking System,13024,11303
PDB,2DOC,BMRB Entry Tracking System,13042,11304
PDB,1V6G,BMRB Entry Tracking System,13060,11305
PDB,1V87,BMRB Entry Tracking System,13080,11306
PDB,1WIM,BMRB Entry Tracking System,13100,11307
PDB,1WIR,BMRB Entry Tracking System,13120,11308
PDB,1WJV,BMRB Entry Tracking System,13140,11309
PDB,1WJW,BMRB Entry Tracking System,13160,11310
PDB,1X3B,BMRB Entry Tracking System,13178,11311
PDB,1X5W,BMRB Entry Tracking System,13196,11312
PDB,2CSY,BMRB Entry Tracking System,13216,11313
PDB,2CSZ,BMRB Entry Tracking System,13236,11314
PDB,2CT0,BMRB Entry Tracking System,13256,11315
PDB,2CT1,BMRB Entry Tracking System,13276,11316
PDB,2CT2,BMRB Entry Tracking System,13296,11317
PDB,2CT4,BMRB Entry Tracking System,13316,11318
PDB,2CT5,BMRB Entry Tracking System,13334,11319
PDB,2CT6,BMRB Entry Tracking System,13354,11320
PDB,2CT7,BMRB Entry Tracking System,13372,11321
PDB,2CU7,BMRB Entry Tracking System,13392,11322
PDB,2D8Q,BMRB Entry Tracking System,13410,11323
PDB,2D8S,BMRB Entry Tracking System,13450,11325
PDB,2D8T,BMRB Entry Tracking System,13470,11326
PDB,2D8U,BMRB Entry Tracking System,13490,11327
PDB,2D8V,BMRB Entry Tracking System,13510,11328
PDB,2DAT,BMRB Entry Tracking System,13530,11329
PDB,2DB9,BMRB Entry Tracking System,13561,11330
PDB,2DJA,BMRB Entry Tracking System,13579,11331
PDB,2DJB,BMRB Entry Tracking System,13599,11332
PDB,2DKT,BMRB Entry Tracking System,13619,11333
PDB,2DME,BMRB Entry Tracking System,13639,11334
PDB,2EA5,BMRB Entry Tracking System,13657,11335
PDB,2EA6,BMRB Entry Tracking System,13677,11336
PDB,2EBK,BMRB Entry Tracking System,13697,11337
PDB,2EBM,BMRB Entry Tracking System,13715,11338
PDB,2ECG,BMRB Entry Tracking System,13733,11339
PDB,2ECI,BMRB Entry Tracking System,13766,11340
PDB,2ECJ,BMRB Entry Tracking System,13786,11341
PDB,2ECL,BMRB Entry Tracking System,13806,11342
PDB,2ECM,BMRB Entry Tracking System,13826,11343
PDB,2ECN,BMRB Entry Tracking System,13846,11344
PDB,2ELJ,BMRB Entry Tracking System,13866,11345
PDB,2RPJ,BMRB Entry Tracking System,13884,11346
PDB,2YQL,BMRB Entry Tracking System,13902,11347
PDB,2E63,BMRB Entry Tracking System,13922,11348
PDB,1X4K,BMRB Entry Tracking System,13940,11349
PDB,1X4L,BMRB Entry Tracking System,13973,11350
PDB,2YUE,BMRB Entry Tracking System,13993,11351
PDB,1WES,BMRB Entry Tracking System,14011,11352
PDB,1X4I,BMRB Entry Tracking System,14031,11353
PDB,1WEN,BMRB Entry Tracking System,14051,11354
PDB,2DK4,BMRB Entry Tracking System,14071,11355
PDB,1UJY,BMRB Entry Tracking System,14089,11356
PDB,2DK7,BMRB Entry Tracking System,14107,11357
BMRB,11359,Assigned chemical shifts of the zf-CW domain with H3 dimethyl K4 peptide,14125,11358
BMRB,11360,Assigned chemical shifts of the zf-CW domain with H3 trimethyl K4 peptide,14125,11358
BMRB,11361,Assigned chemical shifts of the zf-CW domain with H4 trimethyl K20 peptide,14125,11358
BMRB,11362,Assigned chemical shifts of the zf-CW domain in zinc finger CW-type PWWP domain protein 1,14125,11358
PDB,2E61,BMRB Entry Tracking System,14125,11358
BMRB,11358,Assigned chemical shifts of the zf-CW domain with H3 peptide,14146,11359
BMRB,11360,Assigned chemical shifts of the zf-CW domain with H3 trimethyl K4 peptide,14146,11359
BMRB,11361,Assigned chemical shifts of the zf-CW domain with H4 trimethyl K20 peptide,14146,11359
BMRB,11362,Assigned chemical shifts of the zf-CW domain in zinc finger CW-type PWWP domain protein 1,14146,11359
PDB,2E61,BMRB Entry Tracking System,14146,11359
BMRB,11358,Assigned chemical shifts of the zf-CW domain with H3 peptide,14181,11360
BMRB,11359,Assigned chemical shifts of the zf-CW domain with H3 dimethyl K4 peptide,14181,11360
BMRB,11361,Assigned chemical shifts of the zf-CW domain with H4 trimethyl K20 peptide,14181,11360
BMRB,11362,Assigned chemical shifts of the zf-CW domain in zinc finger CW-type PWWP domain protein 1,14181,11360
PDB,2E61,BMRB Entry Tracking System,14181,11360
BMRB,11358,Assigned chemical shifts of the zf-CW domain with H3 peptide,14203,11361
BMRB,11359,Assigned chemical shifts of the zf-CW domain with H3 dimethyl K4 peptide,14203,11361
BMRB,11360,Assigned chemical shifts of the zf-CW domain with H3 trimethyl K4 peptide,14203,11361
BMRB,11362,Assigned chemical shifts of the zf-CW domain in zinc finger CW-type PWWP domain protein 1,14203,11361
PDB,2E61,BMRB Entry Tracking System,14203,11361
BMRB,11358,Assigned chemical shifts of the zf-CW domain with H3 peptide,14225,11362
BMRB,11359,Assigned chemical shifts of the zf-CW domain with H3 dimethyl K4 peptide,14225,11362
BMRB,11360,Assigned chemical shifts of the zf-CW domain with H3 trimethyl K4 peptide,14225,11362
BMRB,11361,Assigned chemical shifts of the zf-CW domain with H4 trimethyl K20 peptide,14225,11362
PDB,2E61,BMRB Entry Tracking System,14225,11362
PDB,1X4S,BMRB Entry Tracking System,14245,11363
PDB,2DT6,BMRB Entry Tracking System,14265,11364
PDB,2DT7,BMRB Entry Tracking System,14285,11365
BMRB,11367,Assigned chemical shifts of the human spliceosomal protein SF3b155,14306,11366
PDB,2FHO,BMRB Entry Tracking System,14306,11366
BMRB,11366,Assigned chemical shifts of the human spliceosomal protein complex p14-SF3b155,14326,11367
PDB,2FHO,BMRB Entry Tracking System,14326,11367
PDB,2YSO,BMRB Entry Tracking System,14345,11368
PDB,2YSP,BMRB Entry Tracking System,14365,11369
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14398,11370
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14398,11370
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14398,11370
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14398,11370
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14398,11370
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14398,11370
PDB,2RNE,BMRB Entry Tracking System,14398,11370
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14412,11371
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14412,11371
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14412,11371
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14412,11371
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14412,11371
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14412,11371
PDB,2RNE,BMRB Entry Tracking System,14412,11371
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14426,11372
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14426,11372
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14426,11372
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14426,11372
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14426,11372
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14426,11372
PDB,2RNE,BMRB Entry Tracking System,14426,11372
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14440,11373
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14440,11373
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14440,11373
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14440,11373
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14440,11373
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14440,11373
PDB,2RNE,BMRB Entry Tracking System,14440,11373
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14454,11374
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14454,11374
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14454,11374
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14454,11374
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14454,11374
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14454,11374
PDB,2RNE,BMRB Entry Tracking System,14454,11374
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14469,11375
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14469,11375
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14469,11375
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14469,11375
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14469,11375
BMRB,11376,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1,14469,11375
PDB,2RNE,BMRB Entry Tracking System,14469,11375
BMRB,11370,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated",14484,11376
BMRB,11371,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant",14484,11376
BMRB,15287,N-Me-Phe12,25804,15282
BMRB,11372,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant",14484,11376
BMRB,11373,"Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant",14484,11376
BMRB,11374,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC),14484,11376
BMRB,11375,Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU),14484,11376
PDB,2RNE,BMRB Entry Tracking System,14484,11376
PDB,2EPP,BMRB Entry Tracking System,14498,11377
PDB,2EPQ,BMRB Entry Tracking System,14518,11378
PDB,2EPR,BMRB Entry Tracking System,14538,11379
PDB,2EPS,BMRB Entry Tracking System,14571,11380
BMRB,11406,Assigned chemical shifts of RNA binding domain 3 in RNA (CUGCUG),15092,11405
BMRB,11407,Assigned chemical shifts of RNA binding domain 3 in RNA (UAUAUA),15092,11405
BMRB,11408,Assigned chemical shifts of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15092,11405
PDB,2rq4,Refinement of RNA binding domain 3 in CUG triplet repeat RNA-binding protein 1,15092,11405
PDB,2rqc,Solution Structure of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15092,11405
BMRB,11405,Assigned chemical shifts of RNA binding domain 3,15111,11406
BMRB,11407,Assigned chemical shifts of RNA binding domain 3 in RNA (UAUAUA),15111,11406
BMRB,11408,Assigned chemical shifts of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15111,11406
PDB,2rq4,Refinement of RNA binding domain 3 in CUG triplet repeat RNA-binding protein 1,15111,11406
PDB,2rqc,Solution Structure of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15111,11406
BMRB,11405,Assigned chemical shifts of RNA binding domain 3,15131,11407
BMRB,11406,Assigned chemical shifts of RNA binding domain 3 in RNA (CUGCUG),15131,11407
BMRB,11408,Assigned chemical shifts of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15131,11407
PDB,2rq4,Refinement of RNA binding domain 3 in CUG triplet repeat RNA-binding protein 1,15131,11407
PDB,2rqc,Solution Structure of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15131,11407
BMRB,11405,Assigned chemical shifts of RNA binding domain 3,15151,11408
BMRB,11406,Assigned chemical shifts of RNA binding domain 3 in RNA (CUGCUG),15151,11408
BMRB,11407,Assigned chemical shifts of RNA binding domain 3 in RNA (UAUAUA),15151,11408
PDB,2rq4,Refinement of RNA binding domain 3 in CUG triplet repeat RNA-binding protein 1,15151,11408
PDB,2rqc,Solution Structure of RNA-binding domain 3 of CUGBP1 in complex with RNA (UG)3,15151,11408
BMRB,11410,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GACUUCAACAAGUC),15172,11409
BMRB,11411,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (AAAAAA),15172,11409
BMRB,11412,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (UCAAU),15172,11409
PDB,2rra,Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15172,11409
BMRB,11409,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15192,11410
BMRB,11411,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (AAAAAA),15192,11410
BMRB,11412,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (UCAAU),15192,11410
PDB,2rra,Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15192,11410
BMRB,11409,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15212,11411
BMRB,11410,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GACUUCAACAAGUC),15212,11411
BMRB,11412,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (UCAAU),15212,11411
PDB,2rra,Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15212,11411
BMRB,11409,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15232,11412
BMRB,11410,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GACUUCAACAAGUC),15232,11412
BMRB,11411,Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (AAAAAA),15232,11412
PDB,2rra,Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA),15232,11412
PDB,2DMX,BMRB Entry Tracking System,15331,11417
PDB,2RRH,BMRB Entry Tracking System,15349,11419
PDB,2RRI,BMRB Entry Tracking System,15365,11420
PDB,2RRK,BMRB Entry Tracking System,15381,11422
PDB,2RRL,BMRB Entry Tracking System,15405,11423
PDB,2RRM,BMRB Entry Tracking System,15426,11424
PDB,2RRN,BMRB Entry Tracking System,15460,11426
BMRB,4011,Chemical shift assignments of the wild-type starch-binding domain of Aspersillus niger glucoamylase,15495,11428
PDB,1KUM,Solution structure of the wild-type starch-binding domain of Aspergillus niger glucoamylase,15495,11428
BMRB,11430,SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HMGB2,15510,11429
BMRB,11431,SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HMGB2 (H22Y),15510,11429
BMRB,11429,SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HMGB2,15524,11430
BMRB,11431,SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HMGB2 (H22Y),15524,11430
BMRB,11429,SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HMGB2,15538,11431
BMRB,11430,SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HMGB2,15538,11431
PDB,2RRQ,BMRB Entry Tracking System,15598,11437
BMRB,11437,DNA oligomer containing propylene cross-linked cyclic 2' -deoxyuridylate dimer,15619,11438
PDB,2rrq,DNA oligomer containing propylene cross-linked cyclic 2' -deoxyuridylate dimer,15619,11438
PDB,2RRR,BMRB Entry Tracking System,15619,11438
PDB,2RRS,BMRB Entry Tracking System,15639,11439
PDB,2RRT,BMRB Entry Tracking System,15666,11440
PDB,2RRU,BMRB Entry Tracking System,15714,11443
BMRB,15291,N-Me-Gly13,25804,15282
PDB,3B0F,Crystal structure of the UBA domain of p62 and its interaction with ubiquitin,15714,11443
PDB,2RS2,BMRB Entry Tracking System,15747,11450
PDB,2NUL,,15764,11451
PDB,2LIY,BMRB Entry Tracking System,15781,11452
PDB,1whq,,15832,11456
PDB,2RS6,BMRB Entry Tracking System,15832,11456
PDB,1uil,,15848,11457
PDB,2RS7,BMRB Entry Tracking System,15848,11457
PDB,2cpj,,15864,11458
PDB,2RS8,BMRB Entry Tracking System,15864,11458
BMRB,11051,Disulfide-free variant of hen lysozyme: 0SS,15878,11459
BMRB,11052,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80]",15878,11459
BMRB,11460,One-disulfide variant of hen lysozyme: 1SS[30-115],15878,11459
BMRB,11461,One-disulfide variant of hen lysozyme: 1SS[64-80],15878,11459
BMRB,11462,One-disulfide variant of hen lysozyme: 1SS[76-94],15878,11459
BMRB,11051,Disulfide-free variant of hen lysozyme: 0SS,15893,11460
BMRB,11052,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80]",15893,11460
BMRB,11459,One-disulfide variant of hen lysozyme: 1SS[6-127],15893,11460
BMRB,11461,One-disulfide variant of hen lysozyme: 1SS[64-80],15893,11460
BMRB,11462,One-disulfide variant of hen lysozyme: 1SS[76-94],15893,11460
BMRB,11051,Disulfide-free variant of hen lysozyme: 0SS,15908,11461
BMRB,11052,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80]",15908,11461
BMRB,11459,One-disulfide variant of hen lysozyme: 1SS[6-127],15908,11461
BMRB,11460,One-disulfide variant of hen lysozyme: 1SS[30-115],15908,11461
BMRB,11462,One-disulfide variant of hen lysozyme: 1SS[76-94],15908,11461
BMRB,11051,Disulfide-free variant of hen lysozyme: 0SS,15923,11462
BMRB,11052,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80]",15923,11462
BMRB,11459,One-disulfide variant of hen lysozyme: 1SS[6-127],15923,11462
BMRB,11460,One-disulfide variant of hen lysozyme: 1SS[30-115],15923,11462
BMRB,11461,One-disulfide variant of hen lysozyme: 1SS[64-80],15923,11462
PDB,2D9E,Bromodomain in free state,15938,11463
PDB,2RS9,BMRB Entry Tracking System,15938,11463
PDB,2RSC,BMRB Entry Tracking System,15986,11468
PDB,2RSD,BMRB Entry Tracking System,16005,11469
PDB,2RSE,BMRB Entry Tracking System,16068,11471
PDB,1UJR,free state structure,16083,11472
PDB,2RSF,BMRB Entry Tracking System,16083,11472
PDB,2RSG,BMRB Entry Tracking System,16104,11473
PDB,2RSH,BMRB Entry Tracking System,16374,11486
PDB,2RSI,BMRB Entry Tracking System,16394,11487
PDB,2RSJ,BMRB Entry Tracking System,16414,11488
PDB,2RSK,BMRB Entry Tracking System,16434,11489
PDB,2RSM,BMRB Entry Tracking System,16488,11491
BMRB,11497,Solution structure of the chromodomain of Swi6,16572,11496
PDB,2RSN,BMRB Entry Tracking System,16572,11496
BMRB,11496,Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide,16594,11497
PDB,2RSO,BMRB Entry Tracking System,16594,11497
BMRB,11472,The same citation,16628,11499
BMRB,11500,The same citation,16628,11499
BMRB,11501,The same citation,16628,11499
PDB,1UJR,NMR structure,16628,11499
BMRB,11472,The same citation,16675,11500
BMRB,11499,The same citation,16675,11500
BMRB,11501,The same citation,16675,11500
PDB,2DK6,NMR structure,16675,11500
BMRB,11472,The same citation,16694,11501
BMRB,11499,The same citation,16694,11501
BMRB,11500,The same citation,16694,11501
PDB,1X4R,NMR structure,16694,11501
PDB,2CRL,"apo form of the first domain of the human copper chaperone for SOD1, CCS",16713,11502
PDB,2RSQ,BMRB Entry Tracking System,16713,11502
PDB,1V80,ubiquitin at 30 bar,16759,11505
PDB,1V81,ubiquitin at 3 kbar,16759,11505
PDB,2RSU,BMRB Entry Tracking System,16759,11505
PDB,2RSX,BMRB Entry Tracking System,16798,11507
PDB,2RSY,BMRB Entry Tracking System,16814,11508
BMRB,11514,"NMR chemical shift of carbohydrate binding module, C2, derived from GH8 chitosanase from Paenibacillus fukuinensis D2",16884,11513
BMRB,11513,"NMR chemical shift of carbohydrate binding module, C1, derived from GH8 chitosanase/glucanase from Paenibacillus fukuinensis D2",16899,11514
BMRB,11520,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition,16945,11519
BMRB,11521,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition with the segment B1 of streptococcal protein G,16945,11519
BMRB,11519,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the diluted condition,16975,11520
BMRB,11521,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition with the segment B1 of streptococcal protein G,16975,11520
BMRB,11519,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the diluted condition,16992,11521
BMRB,11520,The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition,16992,11521
PDB,2RT6,BMRB Entry Tracking System,17060,11525
PDB,1WOC,,17094,11527
PDB,2rt9,BMRB Entry Tracking System,17130,11529
PDB,2RTT,BMRB Entry Tracking System,17178,11531
PDB,2RTZ,BMRB Entry Tracking System,17258,11536
PDB,2RU0,BMRB Entry Tracking System,17274,11537
BMRB,11539,Tachyplesin I in water,17290,11538
PDB,2MDB,Tachyplesin I in the presence of lipopolysaccharide,17290,11538
BMRB,11538,Tachyplesin I in the presence of lipopolysaccharide,17306,11539
PDB,2RTV,Tachyplesin I in water,17306,11539
BMRB,19609,Solution Structure of Protein-RNA Ternary Complex,17352,11541
PDB,2RU2,BMRB Entry Tracking System,17384,11543
BMRB,11548,DESIGNED ARMADILLO REPEAT PROTEIN FRAGMENT (MAII),17403,11544
PDB,2RSU,alternatively folded state is 70% populated,17460,11547
BMRB,11544,Solution structure of the complex formed in solution by a split Armadillo repeat protein (YIIM2-MAII),17477,11548
BMRB,11552,Structure of anoplin mutant R5W in DPC micelles,17545,11551
BMRB,11553,Structure of anoplin double mutant R5K T8W in DPC micelles,17545,11551
BMRB,11554,Structure of anoplin double mutant R5F T8W in DPC micelles,17545,11551
BMRB,11551,Structure of antimicrobial peptide anoplin in DPC micelles,17563,11552
BMRB,11553,Structure of anoplin double mutant R5K T8W in DPC micelles,17563,11552
BMRB,11554,Structure of anoplin double mutant R5F T8W in DPC micelles,17563,11552
BMRB,11551,Structure of antimicrobial peptide anoplin in DPC micelles,17581,11553
BMRB,11552,Structure of anoplin mutant R5W in DPC micelles,17581,11553
BMRB,11554,Structure of anoplin double mutant R5F T8W in DPC micelles,17581,11553
BMRB,11551,Structure of antimicrobial peptide anoplin in DPC micelles,17599,11554
BMRB,11552,Structure of anoplin mutant R5W in DPC micelles,17599,11554
BMRB,11553,Structure of anoplin double mutant R5K T8W in DPC micelles,17599,11554
BMRB,11558,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 without sulfate ion",17649,11557
BMRB,11559,Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion,17649,11557
BMRB,11560,Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant with sulfate ion,17649,11557
BMRB,11557,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion",17666,11558
BMRB,11559,Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion,17666,11558
BMRB,11560,Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant with sulfate ion,17666,11558
BMRB,11557,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion",17683,11559
BMRB,11558,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 without sulfate ion",17683,11559
BMRB,11560,Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant with sulfate ion,17683,11559
PDB,2RUC,BMRB Entry Tracking System,17683,11559
BMRB,11557,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion",17716,11560
BMRB,11558,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 without sulfate ion",17716,11560
BMRB,11559,Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion,17716,11560
PDB,2RUD,BMRB Entry Tracking System,17716,11560
BMRB,11562,"1H , 13C and 15N Assigned Chemical Shifts for PDI (reduced form)",17736,11561
PDB,2RUE,BMRB Entry Tracking System,17736,11561
PDB,2kp1,Solution structure of the identical a' domain (UNP residues: 354-469) in oxidized form at 310K,17736,11561
PDB,2kp2,Solution structure of b' domain (UNP resudiues: 228-355) at 310K,17736,11561
BMRB,11561,"1H , 13C and 15N Assigned Chemical Shifts for PDI (oxidized form)",17755,11562
PDB,2RUF,BMRB Entry Tracking System,17755,11562
PDB,2kp1,Solution structure of the identical a' domain (UNP residues: 354-469) in oxidized form at 310K,17755,11562
PDB,2kp2,Solution structure of b' domain (UNP resudiues: 228-355) at 310K,17755,11562
PDB,2RUG,BMRB Entry Tracking System,17774,11563
BMRB,11565,L94P-RPEL1 motif of MKL1,17793,11564
BMRB,11566,L105P-RPEL1 motif of MKL1,17793,11564
BMRB,11567,RPEL2 motif of MKL1,17793,11564
BMRB,11568,RPEL3 motif of MKL1,17793,11564
BMRB,11564,RPEL motif of MKL1,17806,11565
BMRB,11566,L105P-RPEL1 motif of MKL1,17806,11565
BMRB,11567,RPEL2 motif of MKL1,17806,11565
BMRB,11568,RPEL3 motif of MKL1,17806,11565
BMRB,11564,RPEL motif of MKL1,17820,11566
BMRB,11565,L94P-RPEL1 motif of MKL1,17820,11566
BMRB,11567,RPEL2 motif of MKL1,17820,11566
BMRB,11568,RPEL3 motif of MKL1,17820,11566
BMRB,11564,RPEL motif of MKL1,17834,11567
BMRB,11565,L94P-RPEL1 motif of MKL1,17834,11567
BMRB,11566,L105P-RPEL1 motif of MKL1,17834,11567
BMRB,11568,RPEL3 motif of MKL1,17834,11567
BMRB,11564,RPEL motif of MKL1,17848,11568
BMRB,11565,L94P-RPEL1 motif of MKL1,17848,11568
BMRB,11566,L105P-RPEL1 motif of MKL1,17848,11568
BMRB,11567,RPEL2 motif of MKL1,17848,11568
PDB,2RUH,BMRB Entry Tracking System,17862,11569
PDB,2RUI,BMRB Entry Tracking System,17883,11570
PDB,2EKX,Entry containing three dimensional structure.,17931,11573
PDB,1UEZ,,17949,11574
BMRB,11575,SOLUTION STRUCTURE OF THE SECOND PDZ DOMAIN OF HUMAN KIAA1526 PROTEIN,17949,11574
PDB,1UEZ,,17966,11575
BMRB,11574,SOLUTION STRUCTURE OF THE FIRST PDZ DOMAIN OF HUMAN KIAA1526 PROTEIN,17966,11575
PDB,2RUK,BMRB Entry Tracking System,17983,11578
BMRB,11581,Pre transmembrane domain in DPC micelles,18020,11580
BMRB,11582,Internal fusion peptide in DPC micelles,18020,11580
PDB,2RUM,BMRB Entry Tracking System,18020,11580
BMRB,11580,Fusion peptide in DPC micelles,18035,11581
BMRB,11582,Internal fusion peptide in DPC micelles,18035,11581
PDB,2RUN,BMRB Entry Tracking System,18035,11581
BMRB,11580,Fusion peptide in DPC micelles,18050,11582
BMRB,11581,Pre-transmembrane domain in DPC micelles,18050,11582
PDB,2RUO,BMRB Entry Tracking System,18050,11582
PDB,2RUP,BMRB Entry Tracking System,18065,11583
BMRB,15292,N-Me-Ser14,25804,15282
BMRB,11585,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for c-Myb R2R3 V103L/C130I",18081,11584
BMRB,11584,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for c-Myb R2R3 C130I",18095,11585
BMRB,11588,Solution structure of Human Pin1 PPIase C113S mutant,18109,11587
PDB,2RUQ,BMRB Entry Tracking System,18109,11587
BMRB,11587,Solution structure of human Pin1 PPIase mutant C113A,18129,11588
PDB,2RUR,BMRB Entry Tracking System,18129,11588
PDB,2RV8,BMRB Entry Tracking System,18178,11590
BMRB,11592,Solution structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5,18203,11591
PDB,2RV9,BMRB Entry Tracking System,18203,11591
BMRB,11591,Solution structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5,18220,11592
PDB,2RVA,BMRB Entry Tracking System,18220,11592
PDB,2RVB,BMRB Entry Tracking System,18253,11594
PDB,2RVC,BMRB Entry Tracking System,18278,11595
PDB,5AUI,,18292,11596
PDB,5AUK,,18292,11596
PDB,2RVF,BMRB Entry Tracking System,18309,11597
PDB,2RVH,BMRB Entry Tracking System,18330,11599
PDB,2RVJ,BMRB Entry Tracking System,18376,11601
PDB,2RV0,BMRB Entry Tracking System,18391,11607
PDB,2RVP,BMRB Entry Tracking System,18411,11608
PDB,2RVQ,BMRB Entry Tracking System,18432,11609
BMRB,6235,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the SNARE complex PubMed: 15733924",18828,12003
PDB,2N1T,Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution Pubmed: 26030874,18828,12003
BMRB,12011,"Backbone 1H, 13C, 15N chemical shift assignments for FliGc A282T mutated protein",18884,12010
BMRB,12010,"Backbone 1H, 13C, 15N chemical shift assignments for FliGc protein",18901,12011
BMRB,4588,proton and nitrogen chemical shift of the chitin-binding domain of chitinase A1,18962,12019
BMRB,4742,proton and nitrogen chemical shift of the chitin-binding domain of chitinase A1,18962,12019
PDB,1ed7,solution structure of of the chitin-binding domain of chitinase A1,18962,12019
BMRB,19683,same molecule,19021,12022
PDB,2MIJ,same chemical composition,19021,12022
PDB,3B08,The same molecular assembly,19054,12026
BMRB,12036,Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1,19119,12035
BMRB,12037,Backbone assignment for the segmental-labeled acidic region (L24G mutant) in the DNA-binding domain of Drosophila melanogaster SSRP1,19119,12035
BMRB,12038,Backbone assignment for the segmental-labeled acidic region in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19119,12035
BMRB,12039,Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19119,12035
BMRB,12035,Backbone assignment for the segmental-labeled acidic region in the DNA-binding domain of Drosophila melanogaster SSRP1,19135,12036
BMRB,12037,Backbone assignment for the segmental-labeled acidic region (L24G mutant) in the DNA-binding domain of Drosophila melanogaster SSRP1,19135,12036
BMRB,12038,Backbone assignment for the segmental-labeled acidic region in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19135,12036
BMRB,12039,Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19135,12036
BMRB,12035,Backbone assignment for the segmental-labeled acidic region in the DNA-binding domain of Drosophila melanogaster SSRP1,19151,12038
BMRB,12036,Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1,19151,12038
BMRB,12037,Backbone assignment for the segmental-labeled acidic region (L24G mutant) in the DNA-binding domain of Drosophila melanogaster SSRP1,19151,12038
BMRB,12039,Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19151,12038
BMRB,12035,Backbone assignment for the segmental-labeled acidic region in the DNA-binding domain of Drosophila melanogaster SSRP1,19167,12039
BMRB,12036,Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1,19167,12039
BMRB,12037,Backbone assignment for the segmental-labeled acidic region (L24G mutant) in the DNA-binding domain of Drosophila melanogaster SSRP1,19167,12039
BMRB,12038,Backbone assignment for the segmental-labeled acidic region in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1,19167,12039
PDB,2JM0,BMRB Entry Tracking System,20791,15000
PDB,2LD1,BMRB Entry Tracking System,20816,15001
PDB,2NPR,BMRB Entry Tracking System,20882,15007
BMRB,15009,Spo0F I90A mutant,20898,15008
BMRB,15010,Spo0F L66A mutant,20898,15008
BMRB,15011,Spo0F Y13A mutant,20898,15008
PDB,1FSP,Strucutral coordinates of wild-type Spo0F from Bacillus subtilis,20898,15008
BMRB,15008,Spo0F H101A mutant,20912,15009
BMRB,15010,Spo0F L66A mutant,20912,15009
BMRB,15011,Spo0F Y13A mutant,20912,15009
PDB,1FSP,Strucutral coordinates of wild-type Spo0F from Bacillus subtilis,20912,15009
BMRB,15008,Spo0F H101A mutant,20926,15010
BMRB,15009,Spo0F I90A mutant,20926,15010
BMRB,15011,Spo0F Y13A mutant,20926,15010
PDB,1FSP,Strucutral coordinates of wild-type Spo0F from Bacillus subtilis,20926,15010
BMRB,15008,Spo0F H101A mutant,20940,15011
BMRB,15009,Spo0F I90A mutant,20940,15011
BMRB,15010,Spo0F L66A mutant,20940,15011
PDB,1FSP,Strucutral coordinates of wild-type Spo0F from Bacillus subtilis,20940,15011
PDB,1TUC,,20968,15013
PDB,2JMA,,20968,15013
PDB,2JMC,BMRB Entry Tracking System,20968,15013
PDB,1CHC,RING domain from equine herpes virus-1,20991,15014
PDB,1E4U,N-terminal RING domain from human NOT4,20991,15014
PDB,1JM7,BRCA1/BARD1 RING heterodimer,20991,15014
PDB,1LB4,TNF RECEPTOR-ASSOCIATED FACTOR 6,20991,15014
PDB,1TK7,Structure of Su(dx) WW3-4 tandem domain in apo form,21017,15016
PDB,2JMF,BMRB Entry Tracking System,21017,15016
BMRB,7340,thermally stable DAGK mutant,21037,15019
PDB,2IFS,BMRB Entry Tracking System,21053,15020
PDB,2I7U,BMRB Entry Tracking System,21073,15021
BMRB,15035,h6CarA(Nter),21094,15023
PDB,2JML,BMRB Entry Tracking System,21094,15023
PDB,2NVJ,BMRB Entry Tracking System,21110,15025
BMRB,15027,B-DNA Dodecamer,21125,15026
BMRB,15026,IQ-modified Dodecame,21150,15027
BMRB,7108,"Trx monomer, reduced",21173,15028
BMRB,7109,"Trx monomer, oxidized",21173,15028
PDB,2IPA,BMRB Entry Tracking System,21173,15028
PDB,2JMR,BMRB Entry Tracking System,21222,15032
BMRB,15023,CarA(Nter),21268,15035
PDB,2IZ3,BMRB Entry Tracking System,21299,15037
PDB,2OFN,BMRB Entry Tracking System,21313,15038
PDB,2JMK,BMRB Entry Tracking System,21329,15039
PDB,2I1E,BMRB Entry Tracking System,21348,15040
PDB,2I1F,BMRB Entry Tracking System,21363,15041
PDB,2I1G,BMRB Entry Tracking System,21378,15042
PDB,2I1H,BMRB Entry Tracking System,21393,15043
PDB,2I1I,BMRB Entry Tracking System,21408,15044
PDB,2JMM,BMRB Entry Tracking System,21423,15045
PDB,2OV6,BMRB Entry Tracking System,21439,15046
BMRB,4375,more complete shift set at slightly different conditions,21453,15047
PDB,2I1D,BMRB Entry Tracking System,21522,15051
BMRB,15053,"prion protein fragment 173-195, mutant",21537,15052
BMRB,15054,prion protein fragment 180-195,21537,15052
BMRB,15052,prion protein fragment 173-195,21552,15053
BMRB,15054,prion protein fragment 180-195,21552,15053
BMRB,15052,prion protein fragment 173-195,21567,15054
BMRB,15053,"prion protein fragment 173-195, mutant",21567,15054
PDB,1L8Q,Structure of the remainder of the protein,21582,15055
PDB,2JMP,BMRB Entry Tracking System,21582,15055
PDB,2JMS,BMRB Entry Tracking System,21648,15058
PDB,2O10,BMRB Entry Tracking System,21668,15059
PDB,2O13,BMRB Entry Tracking System,21668,15059
PDB,2H80,human DLC2 SAM domain,21684,15060
PDB,2JMU,BMRB Entry Tracking System,21720,15063
BMRB,15065,2-PGA-bound WT cTIM,21744,15064
BMRB,15066,apo PGG/GGG cTIM,21744,15064
BMRB,15067,2-PGA-bound PGG/GGG cTIM,21744,15064
BMRB,15064,apo WT cTIM,21768,15065
BMRB,15066,apo PGG/GGG cTIM,21768,15065
BMRB,15067,2-PGA-bound PGG/GGG cTIM,21768,15065
BMRB,15064,apo WT cTIM,21795,15066
BMRB,15065,2-PGA-bound WT cTIM,21795,15066
BMRB,15067,2-PGA-bound PGG/GGG cTIM,21795,15066
BMRB,15064,apo WT cTIM,21820,15067
BMRB,15065,2-PGA-bound WT cTIM,21820,15067
BMRB,15066,apo PGG/GGG cTIM,21820,15067
PDB,2I2J,BMRB Entry Tracking System,21842,15068
PDB,2I2H,BMRB Entry Tracking System,21859,15069
BMRB,15071,apo Corynebacterium diptheriae heme oxygenase,21876,15070
BMRB,15073,"complex form, Corynebacterium diptheriae heme oxygenase",21876,15070
BMRB,15070,apo cd-HO-G135A,21891,15071
BMRB,15073,"complex form, Corynebacterium diptheriae heme oxygenase",21891,15071
BMRB,6564,Chemical Shift Assignment for OSCP-NT (1-120),21906,15072
PDB,2JMX,BMRB Entry Tracking System,21906,15072
BMRB,15070,apo cd-HO-G135A,21925,15073
BMRB,15071,apo Corynebacterium diptheriae heme oxygenase,21925,15073
PDB,2JMO,BMRB Entry Tracking System,21942,15074
BMRB,15077,B-DNA Dodecamer,21980,15076
BMRB,15078,LC8 / IC complex,21980,15076
BMRB,15076,LC8 dimer,21994,15077
BMRB,15078,LC8 / IC complex,21994,15077
BMRB,15076,LC8 dimer,22009,15078
BMRB,15077,LC8 / Swa complex,22009,15078
BMRB,15081,Chemical shifts of human U2 Stem I,22049,15080
PDB,2O32,BMRB Entry Tracking System,22049,15080
PDB,2O33,BMRB Entry Tracking System,22049,15080
BMRB,15080,Chemical shifts of yeast U2 Stem I,22072,15081
PDB,2O32,BMRB Entry Tracking System,22072,15081
PDB,2O33,BMRB Entry Tracking System,22072,15081
BMRB,7355,fabp_clof bound,22094,15082
BMRB,7356,fenofibricAcid bound,22094,15082
BMRB,7357,tolfenamic bound,22094,15082
PDB,2O8K,BMRB Entry Tracking System,22108,15083
PDB,2O9L,BMRB Entry Tracking System,22108,15083
PDB,2JN3,BMRB Entry Tracking System,22133,15084
PDB,2JN4,BMRB Entry Tracking System,22158,15085
PDB,2JN6,BMRB Entry Tracking System,22179,15086
PDB,2JN7,BMRB Entry Tracking System,22215,15088
PDB,2es9,NESG Xray structure,22234,15089
PDB,2JN8,BMRB Entry Tracking System,22234,15089
PDB,2MA8,BMRB Entry Tracking System,22264,15090
PDB,1NAQ,,22336,15094
PDB,2JN5,BMRB Entry Tracking System,22355,15095
PDB,2cka,,22394,15098
PDB,2JMY,BMRB Entry Tracking System,22409,15099
BMRB,15104,NW domain 8,22490,15103
PDB,2NX6,BMRB Entry Tracking System,22490,15103
BMRB,15103,NW domain 6,22508,15104
PDB,2NX7,BMRB Entry Tracking System,22508,15104
BMRB,15106,"Clip, second domain",22526,15105
PDB,2IKD,BMRB Entry Tracking System,22526,15105
BMRB,15105,"Clip, first domain",22543,15106
PDB,2IKE,BMRB Entry Tracking System,22543,15106
PDB,2E4E,BMRB Entry Tracking System,22560,15107
PDB,2IMU,BMRB Entry Tracking System,22577,15108
PDB,2JNG,BMRB Entry Tracking System,22592,15109
PDB,2HDM,BMRB Entry Tracking System,22613,15110
PDB,2JNH,BMRB Entry Tracking System,22632,15111
PDB,2K4W,structure entry,22649,15112
PDB,2IHX,BMRB Entry Tracking System,22671,15113
BMRB,15116,HIV-1 V7R-myrMA,22697,15114
PDB,2JNI,BMRB Entry Tracking System,22716,15115
BMRB,15114,HIV-1 L8A-myrMA,22734,15116
BMRB,4317,Corresponding chemical shift data for free NS1A (1-73),22753,15117
PDB,1ns1,structure of dsRNA binding domain of NS1,22753,15117
PDB,2JNP,BMRB Entry Tracking System,22787,15120
PDB,2JNR,BMRB Entry Tracking System,22867,15124
PDB,2JNS,BMRB Entry Tracking System,22884,15125
PDB,2OQ3,BMRB Entry Tracking System,22902,15126
PDB,2HX6,Coordinates,22921,15127
PDB,2JNU,BMRB Entry Tracking System,22945,15128
PDB,2JNY,BMRB Entry Tracking System,23037,15133
PDB,2JNZ,BMRB Entry Tracking System,23058,15134
BMRB,15136,"ENSA, free form",23076,15135
BMRB,15135,"ENSA, in SDS",23092,15136
PDB,1A43,DIMERIC PROTEIN,23108,15137
PDB,2JO0,BMRB Entry Tracking System,23108,15137
BMRB,5877,15N shifts and HN dipolar couplings for an aligned sample,23125,15138
PDB,2EEM,BMRB Entry Tracking System,23180,15140
PDB,2E8J,BMRB Entry Tracking System,23210,15142
PDB,1LiP,entry containing coordinates for LTP1 without post-translational modification,23227,15143
PDB,1AEY,NMR structure,23246,15144
PDB,1SHG,crystallographic structure,23246,15144
PDB,1U06,crystallographic structure,23246,15144
PDB,2OYV,BMRB Entry Tracking System,23291,15145
PDB,2OYW,BMRB Entry Tracking System,23291,15145
BMRB,15149,HMGB1 Full Length,23311,15148
BMRB,15148,HMGB1 AB boxes + basic tail,23326,15149
PDB,2OSG,,23354,15150
PDB,2OT2,BMRB Entry Tracking System,23376,15152
BMRB,15159,phosphoit30,23394,15153
PDB,2JO9,BMRB Entry Tracking System,23394,15153
PDB,2JOA,BMRB Entry Tracking System,23417,15154
BMRB,16873,NMR determination of protein pKa values in the solid state,23445,15156
PDB,2gi9,X-ray Structure,23445,15156
PDB,2OJ7,BMRB Entry Tracking System,23468,15157
PDB,2OJ8,BMRB Entry Tracking System,23468,15157
PDB,2JO7,BMRB Entry Tracking System,23489,15158
BMRB,15153,WW3-PPPPYP,23513,15159
PDB,2JO9,,23513,15159
PDB,2JOC,BMRB Entry Tracking System,23513,15159
PDB,2I5O,BMRB Entry Tracking System,23547,15160
PDB,2OD1,Solution structure of the MYND domain from human AML1-ETO,23570,15161
BMRB,15168,LARG PDZ domain,23603,15163
BMRB,7375,ATP7A (complex with Cu),23624,15164
PDB,2JOD,BMRB Entry Tracking System,23639,15166
BMRB,15163,LARG PDZ domain in complex with C-terminal octa-peptide of Plexin B1,23704,15168
PDB,2OMJ,Entry containing atom coordinates for this domain,23704,15168
PDB,1jrj,molecule with an analagous C-terminus.,23721,15169
PDB,1l2y,"less stable, but identical motif.",23721,15169
PDB,2JOF,BMRB Entry Tracking System,23721,15169
PDB,2OD1,Solution structure of the MYND domain from human AML1-ETO,23811,15173
PDB,2ODD,"Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor",23811,15173
BMRB,15175,[D-Phe44]iota-RXIA,23827,15174
PDB,2P4L,BMRB Entry Tracking System,23827,15174
BMRB,15174,[D-Phe44]iota-RXIA,23844,15175
BMRB,15865,Detailed Structural Characterization of Unbound Protein Phosphatase 1 Inhibitors,23862,15176
BMRB,5906,"dopamine and cAMP-regulated phosphoprotein, Mr. 32000",23862,15176
BMRB,7376,CzrA in complex with Zinc ion,23878,15177
BMRB,7377,CzrA in complex with DNA,23878,15177
PDB,1R1U,,23878,15177
PDB,1R1V,,23878,15177
BMRB,4720,Inhibitor-2,23912,15179
BMRB,6927,Spinophilin PDZ domain (493-602),23942,15180
BMRB,15183,CaM/CaMKKap,23980,15184
BMRB,15185,Cam/eNOSp,23980,15184
BMRB,15186,Cam/smMLCKp,23980,15184
BMRB,15187,CaM/PDEs,23980,15184
BMRB,15188,calmodulin,23980,15184
BMRB,15183,CaM/CaMKKap,24000,15185
BMRB,15184,CaM/CaMK1p,24000,15185
BMRB,15186,Cam/smMLCKp,24000,15185
BMRB,15187,CaM/PDEs,24000,15185
BMRB,15188,calmodulin,24000,15185
BMRB,15183,CaM/CaMKKap,24020,15186
BMRB,15184,CaM/CaMK1p,24020,15186
BMRB,15185,Cam/eNOSp,24020,15186
BMRB,15187,CaM/PDEs,24020,15186
BMRB,15188,calmodulin,24020,15186
BMRB,4970,kinase calmodulin binding domain,24020,15186
BMRB,5227,smMLCK:CaM complex,24020,15186
BMRB,15183,CaM/CaMKKap,24040,15187
BMRB,15184,CaM/CaMK1p,24040,15187
BMRB,15185,Cam/eNOSp,24040,15187
BMRB,15186,Cam/smMLCKp,24040,15187
BMRB,15188,calmodulin,24040,15187
BMRB,15183,CaM/CaMKKap,24061,15188
BMRB,15184,CaM/CaMK1p,24061,15188
BMRB,15185,Cam/eNOSp,24061,15188
BMRB,15186,Cam/smMLCKp,24061,15188
BMRB,15187,CaM/PDEs,24061,15188
BMRB,6541,Ca-bound calmodulin,24061,15188
PDB,2JOP,BMRB Entry Tracking System,24079,15189
PDB,2JOQ,BMRB Entry Tracking System,24114,15190
TargetDB,PT2,,24114,15190
PDB,2060,X-ray structure CaM-nNOSp,24143,15191
PDB,2BAF,,24160,15192
PDB,2JOR,BMRB Entry Tracking System,24160,15192
PDB,2KAO,structure entry,24174,15193
PDB,2EFZ,BMRB Entry Tracking System,24204,15195
PDB,2K7B,BMRB Entry Tracking System,24239,15197
PDB,2K7C,BMRB Entry Tracking System,24239,15197
BMRB,6622,Backbone assignment for HEWL-SMe,24253,15198
PDB,2JOW,BMRB Entry Tracking System,24402,15206
PDB,2JOX,BMRB Entry Tracking System,24441,15208
PDB,2JOY,BMRB Entry Tracking System,24487,15210
PDB,2JOZ,BMRB Entry Tracking System,24509,15211
PDB,1p7d,Int c75-DNA complex,24545,15213
PDB,2JP1,BMRB Entry Tracking System,24574,15215
PDB,2jn9,rcsb100045,24595,15217
PDB,2JP5,BMRB Entry Tracking System,24628,15218
BMRB,15224,AB_G_beta,24701,15223
BMRB,15227,alpha anomer,24701,15223
BMRB,15228,beta anomer,24701,15223
BMRB,15223,AB_G_alpha,24718,15224
BMRB,15227,alpha anomer,24718,15224
BMRB,15228,beta anomer,24718,15224
PDB,2UVS,BMRB Entry Tracking System,24754,15226
BMRB,15223,AB_G_alpha,24768,15227
BMRB,15224,AB_G_beta,24768,15227
BMRB,15228,beta anomer,24768,15227
PDB,2O7Y,,24768,15227
PDB,2O7Z,,24787,15228
PDB,2NXU,BMRB Entry Tracking System,24805,15229
PDB,2PQE,BMRB Entry Tracking System,24872,15232
BMRB,15234,D122Y mutant,24886,15233
BMRB,15235,hfraW155R,24886,15233
BMRB,15236,CyaYG26KD27SD31K,24886,15233
BMRB,15237,CyaYD31K,24886,15233
BMRB,15244,CyaYE19KD22K,24886,15233
BMRB,15233,hfraG130V,24902,15234
BMRB,15235,hfraW155R,24902,15234
BMRB,15236,CyaYG26KD27SD31K,24902,15234
BMRB,15237,CyaYD31K,24902,15234
BMRB,15244,CyaYE19KD22K,24902,15234
BMRB,15233,hfraG130V,24918,15235
BMRB,15234,D122Y mutant,24918,15235
BMRB,15236,CyaYG26KD27SD31K,24918,15235
BMRB,15237,CyaYD31K,24918,15235
BMRB,15244,CyaYE19KD22K,24918,15235
BMRB,15233,hfraG130V,24933,15236
BMRB,15234,D122Y mutant,24933,15236
BMRB,15235,hfraW155R,24933,15236
BMRB,15237,CyaYD31K,24933,15236
BMRB,15244,CyaYE19KD22K,24933,15236
BMRB,15233,hfraG130V,24949,15237
BMRB,15234,D122Y mutant,24949,15237
BMRB,15235,hfraW155R,24949,15237
BMRB,15236,CyaYG26KD27SD31K,24949,15237
BMRB,15244,CyaYE19KD22K,24949,15237
BMRB,15239,AB_C_beta,24965,15238
PDB,2O80,,24965,15238
BMRB,15238,AB_C_alpha,24984,15239
PDB,2O82,,24984,15239
PDB,2JPD,BMRB Entry Tracking System,25002,15240
PDB,2JPE,BMRB Entry Tracking System,25040,15242
PDB,2HR9,Solution NMR structure,25061,15243
BMRB,15233,hfraG130V,25076,15244
BMRB,15234,D122Y mutant,25076,15244
BMRB,15235,hfraW155R,25076,15244
BMRB,15236,CyaYG26KD27SD31K,25076,15244
BMRB,15237,CyaYD31K,25076,15244
PDB,2PPZ,BMRB Entry Tracking System,25092,15245
PDB,2JPI,BMRB Entry Tracking System,25106,15246
PDB,2V9H,BMRB Entry Tracking System,25120,15247
BMRB,15250,subtilisin Sbt70,25137,15248
PDB,1spb,crystal structure of prodomain bound Sbt70,25137,15248
BMRB,16628,Chemical shifts of MloK1_CNBD monomer,25153,15249
BMRB,15248,Sbt70 in prodomain-bound state,25169,15250
PDB,1sua,x-ray crystal structure of Sbt70,25169,15250
PDB,2JPN,BMRB Entry Tracking System,25185,15252
BMRB,15255,SH3,25223,15254
BMRB,15254,PrSH3,25242,15255
PDB,1GM0,Bombyx mori pheromone-binding protein at pH 4.5.,25260,15256
PDB,1LS8,Bombyx mori pheromone-binding protein at pH 6.5.,25260,15256
PDB,1QWV,Antheraea polyphemus pheromone-binding protein 1 at pH 6.3,25260,15256
PDB,1TWO,Antheraea polyphemus pheromone-binding protein 1 at pH 5.2.,25260,15256
PDB,2JPO,BMRB Entry Tracking System,25260,15256
PDB,2JPP,BMRB Entry Tracking System,25280,15257
PDB,2JPJ,BMRB Entry Tracking System,25358,15259
PDB,2JPL,BMRB Entry Tracking System,25358,15259
PDB,2JPK,BMRB Entry Tracking System,25381,15261
PDB,2JPM,BMRB Entry Tracking System,25381,15261
PDB,1zyn,,25419,15264
PDB,1zyp,,25419,15264
PDB,2JPU,BMRB Entry Tracking System,25439,15265
PDB,1MO2,PW2 structure in SDS micelles,25478,15267
PDB,2JQ2,BMRB Entry Tracking System,25478,15267
PDB,2JQ3,BMRB Entry Tracking System,25494,15268
PDB,2JQ4,BMRB Entry Tracking System,25516,15269
PDB,2JQ5,BMRB Entry Tracking System,25540,15270
BMRB,6160,"Same domain, homonuclear",25566,15271
PDB,1oc0,Complex of same domain,25566,15271
PDB,1s4g,"Same domain, wrong disulfides",25566,15271
PDB,1ssu,"Same domain, wrong disulfides",25566,15271
PDB,2JQ8,BMRB Entry Tracking System,25566,15271
BMRB,15273,conopeptide mr12 mutant,25585,15272
PDB,2JQB,BMRB Entry Tracking System,25585,15272
PDB,2YYF,"Purification and structural characterization of a D-amino acid containing conopeptide, marmophine, from Conus marmoreus",25585,15272
BMRB,15272,M cono-toxin mr12,25606,15273
PDB,2EFZ,M conotoxin Mr3.4,25606,15273
PDB,2JQC,BMRB Entry Tracking System,25606,15273
PDB,2YYF,M conotoxin mr12,25606,15273
PDB,2JQE,BMRB Entry Tracking System,25643,15275
PDB,1CD0,X-ray structure of the human lambda-VI light chain dimer JTO,25663,15276
BMRB,15278,sLbpro,25682,15277
PDB,1QMY,,25682,15277
PDB,1QOL,,25682,15277
PDB,2JQF,BMRB Entry Tracking System,25682,15277
BMRB,15277,Lbpro,25704,15278
PDB,1QMY,,25704,15278
PDB,1QOL,,25704,15278
PDB,2JQG,BMRB Entry Tracking System,25704,15278
PDB,2JQ6,BMRB Entry Tracking System,25727,15279
BMRB,6709,reduced form of the N-terminal domain of PilB,25745,15280
PDB,2o0q,Xray crystal structure,25760,15281
BMRB,15284,N-Me-Leu8,25804,15282
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25804,15282
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25804,15282
BMRB,5839,"T1, T2, and NOE of GB3",25819,15283
PDB,1IGD,,25819,15283
PDB,2OED,,25819,15283
BMRB,15282,N-Me-Phe5,25835,15284
BMRB,15285,N-Me-Lys11,25835,15284
BMRB,15287,N-Me-Phe12,25835,15284
BMRB,15291,N-Me-Gly13,25835,15284
BMRB,15292,N-Me-Ser14,25835,15284
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25835,15284
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25835,15284
BMRB,15282,N-Me-Phe5,25851,15285
BMRB,15284,N-Me-Leu8,25851,15285
BMRB,15287,N-Me-Phe12,25851,15285
BMRB,15291,N-Me-Gly13,25851,15285
BMRB,15292,N-Me-Ser14,25851,15285
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25851,15285
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25851,15285
BMRB,15282,N-Me-Phe5,25881,15287
BMRB,15284,N-Me-Leu8,25881,15287
BMRB,15285,N-Me-Lys11,25881,15287
BMRB,15291,N-Me-Gly13,25881,15287
BMRB,15292,N-Me-Ser14,25881,15287
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25881,15287
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25881,15287
PDB,2JQO,BMRB Entry Tracking System,25896,15288
BMRB,15300,THAP domain 1-90 from human THAP1 protein,25917,15289
PDB,2JQQ,BMRB Entry Tracking System,25938,15290
BMRB,15282,N-Me-Phe5,25962,15291
BMRB,15284,N-Me-Leu8,25962,15291
BMRB,15285,N-Me-Lys11,25962,15291
BMRB,15287,N-Me-Phe12,25962,15291
BMRB,15292,N-Me-Ser14,25962,15291
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25962,15291
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25962,15291
BMRB,15282,N-Me-Phe5,25977,15292
BMRB,15284,N-Me-Leu8,25977,15292
BMRB,15285,N-Me-Lys11,25977,15292
BMRB,15287,N-Me-Phe12,25977,15292
BMRB,15291,N-Me-Gly13,25977,15292
BMRB,15293,N-Me-Leu8/N-Me-Ser14,25977,15292
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25977,15292
BMRB,15282,N-Me-Phe5,25992,15293
BMRB,15284,N-Me-Leu8,25992,15293
BMRB,15285,N-Me-Lys11,25992,15293
BMRB,15287,N-Me-Phe12,25992,15293
BMRB,15291,N-Me-Gly13,25992,15293
BMRB,15292,N-Me-Ser14,25992,15293
BMRB,15294,N-Me-Val1/N-Me-Leu8/N-Me-Ser14,25992,15293
BMRB,15282,N-Me-Phe5,26008,15294
BMRB,15284,N-Me-Leu8,26008,15294
BMRB,15285,N-Me-Lys11,26008,15294
BMRB,15287,N-Me-Phe12,26008,15294
BMRB,15291,N-Me-Gly13,26008,15294
BMRB,15292,N-Me-Ser14,26008,15294
BMRB,15293,N-Me-Leu8/N-Me-Ser14,26008,15294
PDB,2JQV,BMRB Entry Tracking System,26025,15295
PDB,1K2H,apo-S100A1,26045,15296
PDB,1ZFS,Ca-S100A1,26045,15296
PDB,2Z3S,BMRB Entry Tracking System,26078,15299
BMRB,15289,THAP domain 1-81 from human THAP1 protein,26093,15300
BMRB,7390,reduced form,26114,15301
PDB,1AYF,,26114,15301
PDB,1YCC,,26114,15301
PDB,2JQW,BMRB Entry Tracking System,26142,15302
BMRB,4156,b domain of human PDI,26157,15303
PDB,1BJX,b domain of human PDI,26157,15303
PDB,2B5E,yeast PDI,26157,15303
PDB,1zvd,Smurf2 HECT domain,26210,15306
PDB,2JR0,BMRB Entry Tracking System,26246,15312
PDB,2KN6,BMRB Entry Tracking System,26263,15313
PDB,2JR1,BMRB Entry Tracking System,26279,15314
PDB,2Z4F,BMRB Entry Tracking System,26299,15315
BMRB,7391,denatured protein,26318,15316
PDB,2JR3,BMRB Entry Tracking System,26385,15318
PDB,2JR4,BMRB Entry Tracking System,26401,15319
PDB,2JR5,BMRB Entry Tracking System,26422,15320
PDB,2HO9,Solution Structure of Chemotaxis Protein CheW from Escherichia coli,26445,15322
PDB,2JR8,BMRB Entry Tracking System,26459,15323
PDB,2JRA,BMRB Entry Tracking System,26474,15324
PDB,2JRB,BMRB Entry Tracking System,26496,15325
PDB,2HGK,BMRB Entry Tracking System,26527,15327
PDB,2JRF,BMRB Entry Tracking System,26545,15329
BMRB,15358,caenopore5 trans monomer,26570,15330
PDB,2JR4,,26586,15331
PDB,2JRG,BMRB Entry Tracking System,26586,15331
PDB,2JRH,BMRB Entry Tracking System,26609,15332
PDB,2JRL,BMRB Entry Tracking System,26649,15334
PDB,2JR4,,26901,15342
PDB,2jrg,,26901,15342
PDB,2JRQ,BMRB Entry Tracking System,26901,15342
PDB,2JRT,BMRB Entry Tracking System,26953,15344
PDB,2JRK,BMRB Entry Tracking System,26974,15345
PDB,2K8S,BMRB Entry Tracking System,27011,15347
GB,GI:11321605,GenBank NCBI identification,27032,15348
PDB,2JRZ,BMRB Entry Tracking System,27032,15348
SP,P41229,Swissprot,27032,15348
PDB,2JS0,BMRB Entry Tracking System,27056,15349
PDB,2GSV,Crystal structure of SR478,27075,15350
PDB,2JS1,BMRB Entry Tracking System,27075,15350
PDB,2JS2,BMRB Entry Tracking System,27111,15351
BMRB,15354,protein Q60C73_METCA,27130,15352
PDB,2JS3,BMRB Entry Tracking System,27130,15352
PDB,2JS4,BMRB Entry Tracking System,27152,15353
BMRB,15352,rpt8 dimer,27177,15354
PDB,2JS5,BMRB Entry Tracking System,27177,15354
PDB,2JS7,BMRB Entry Tracking System,27215,15356
PDB,2KHS,BMRB Entry Tracking System,27245,15357
BMRB,15330,caenopore5 cis monomer,27259,15358
PDB,2JSA,BMRB Entry Tracking System,27259,15358
PDB,2JSB,BMRB Entry Tracking System,27275,15359
PDB,2JSD,BMRB Entry Tracking System,27309,15361
PDB,2JR4,,27338,15362
PDB,2JRG,,27338,15362
PDB,2JRQ,,27338,15362
PDB,2JSG,BMRB Entry Tracking System,27338,15362
PDB,1NC8,NMR STRUCTURE OF THE HIV-2 NUCLEOCAPSID PROTEIN: FRAGMENT: RESIDUES 1-29,27381,15364
PDB,2DI2,NMR STRUCTURE OF THE HIV-2 NUCLEOCAPSID PROTEIN N11A MUTANT (1NC8 MUTANT): FRAGMENT: RESIDUS 1-29,27381,15364
PDB,2E1X,NMR STRUCTURE OF THE HIV-2 NUCLEOCAPSID PROTEIN: FRAGMENT: RESIDUES 23-49,27381,15364
BMRB,6116,Human eRF1 N-domain,27403,15366
BMRB,6763,Human eRF1 middle domain,27403,15366
BMRB,15368,mutant at residue 10,27427,15367
BMRB,15436,mutant at residue 6,27427,15367
BMRB,15367,mutant at residue 5,27441,15368
BMRB,15436,mutant at residue 6,27441,15368
PDB,2JSN,BMRB Entry Tracking System,27470,15370
PDB,2JSO,BMRB Entry Tracking System,27489,15371
PDB,2JSP,BMRB Entry Tracking System,27530,15373
BMRB,15375,complex with nickel,27557,15374
PDB,2KKD,,27557,15374
PDB,2QKZ,,27557,15374
PDB,2QL0,BMRB Entry Tracking System,27557,15374
BMRB,15374,complex with zinc,27579,15375
PDB,2KKD,BMRB Entry Tracking System,27579,15375
PDB,2QKZ,,27579,15375
PDB,2QL0,,27579,15375
PDB,2O4Y,,27604,15376
PDB,2JR7,BMRB Entry Tracking System,27624,15377
BMRB,15156,Solid-state NMR of GB1 T2Q: 13C and 15N chemical shift assignment,27692,15380
PDB,2GI9,GB1 T2Q orthorhombic crystal structure determined by x-ray single crystal diffraction,27692,15380
PDB,2JSV,Ensemble of solid-state NMR GB1 structures,27692,15380
PDB,2QMT,GB1 T2Q trigonal crystal structure determined by x-ray single crystal diffraction,27692,15380
PDB,2JSX,BMRB Entry Tracking System,27709,15381
PDB,2JOT,BMRB Entry Tracking System,27731,15382
PDB,2JST,BMRB Entry Tracking System,27767,15384
PDB,2JT0,BMRB Entry Tracking System,27789,15385
PDB,2JT3,BMRB Entry Tracking System,27845,15388
PDB,1ibn,wild-type HA fusion domain in ph 5,27897,15390
PDB,1ibo,wild-type HA fusion domain in ph 7.4,27897,15390
PDB,2JRD,BMRB Entry Tracking System,27897,15390
BMRB,15392,KIA7F tetramer,27914,15391
BMRB,15391,KIA7 temramer,27932,15392
PDB,1YFQ,,27950,15393
PDB,2JSS,BMRB Entry Tracking System,27950,15393
PDB,2JOH,BMRB Entry Tracking System,27983,15394
BMRB,15396,MMP-3 with INHIBITOR VII,27999,15395
PDB,2JNP,,27999,15395
PDB,2JT5,BMRB Entry Tracking System,27999,15395
BMRB,15395,MMP-3 with MLC88,28019,15396
PDB,2JNP,,28019,15396
PDB,2JT6,BMRB Entry Tracking System,28019,15396
BMRB,15398,CBP in the free state,28039,15397
BMRB,5228,"ACTR in complex with the CREB binding protein, CBP",28039,15397
BMRB,15397,ACTR in the free state,28055,15398
BMRB,5228,"ACTR in complex with the CREB binding protein, CBP",28055,15398
PDB,2JOM,BMRB Entry Tracking System,28071,15399
PDB,2JT8,BMRB Entry Tracking System,28086,15400
BMRB,15402,complex with calcium ion,28105,15401
BMRB,15401,free form,28124,15402
PDB,2JOO,BMRB Entry Tracking System,28178,15405
PDB,2JTE,BMRB Entry Tracking System,28212,15407
PDB,2LD9,BMRB Entry Tracking System,28284,15410
PDB,2JSW,BMRB Entry Tracking System,28300,15411
PDB,2QDQ,Entry containing the structure of the following domain or dimerisation domain,28300,15411
PDB,2JTM,BMRB Entry Tracking System,28351,15415
PDB,2JTP,BMRB Entry Tracking System,28368,15417
PDB,1JWD,Entry containing restraints of S100A6,28398,15418
PDB,2JTT,BMRB Entry Tracking System,28398,15418
PDB,2JTV,BMRB Entry Tracking System,28422,15419
BMRB,15425,mutant KChIP4a(Delta1-42),28490,15422
PDB,2JTY,BMRB Entry Tracking System,28509,15423
BMRB,15422,KChIP4a,28538,15425
PDB,2JTZ,BMRB Entry Tracking System,28572,15427
BMRB,4098,resonance assignments and secondary structure,28591,15429
PDB,2JU3,BMRB Entry Tracking System,28591,15429
PDB,2JU4,BMRB Entry Tracking System,28628,15430
PDB,2JU5,BMRB Entry Tracking System,28649,15431
BMRB,15429,Solution-State Structures of apo-LFABP (Liver Fatty Acid-Binding Protein),28663,15433
BMRB,4098,resonance assignments and secondary structure,28663,15433
PDB,2JU7,BMRB Entry Tracking System,28663,15433
PDB,2ju3,Solution-State Structures of apo-LFABP (Liver Fatty Acid-Binding Protein),28663,15433
BMRB,15429,Solution-State Structures of apo-LFABP (Liver Fatty Acid-Binding Protein),28690,15434
BMRB,15433,"Solution-State Structures of Oleate-Liganded LFABP, Protein Only",28690,15434
BMRB,4098,resonance assignments and secondary structure,28690,15434
PDB,2JU8,BMRB Entry Tracking System,28690,15434
PDB,2ju3,Solution-State Structures of apo-LFABP (Liver Fatty Acid-Binding Protein),28690,15434
PDB,2ju7,"Solution-State Structures of Oleate-Liganded LFABP, Protein Only",28690,15434
BMRB,15367,RgIA,28721,15435
BMRB,15368,RgIA (mutant),28721,15435
BMRB,15436,alpha-RgIA,28721,15435
BMRB,15367,RgIA,28737,15436
BMRB,15368,RgIA (mutant),28737,15436
BMRB,15435,RgIA,28737,15436
BMRB,5687,sibling protein S824,28751,15437
PDB,1p68,sibling protein S824,28751,15437
PDB,2JUA,BMRB Entry Tracking System,28751,15437
PDB,2JUB,BMRB Entry Tracking System,28780,15438
PDB,2JUC,BMRB Entry Tracking System,28795,15439
PDB,2M2K,BMRB Entry Tracking System,28827,15440
PDB,2JUG,BMRB Entry Tracking System,28859,15442
PDB,2JUH,BMRB Entry Tracking System,28896,15444
BMRB,7413,"HMGB1, delta25",30048,15502
BMRB,7249,Assigned chemical shifts,28918,15445
PDB,1e7k,15.5K-U4SL complex,28918,15445
PDB,2jnb,Structure coordinate file,28918,15445
PDB,2ozb,15.5K-U4SL-hPrp31 complex,28918,15445
BMRB,15986,89FnI-collagen complex,28959,15447
PDB,2PNG,BMRB Entry Tracking System,28994,15449
PDB,2JUM,BMRB Entry Tracking System,29024,15450
PDB,2JUO,BMRB Entry Tracking System,29047,15451
PDB,1D1J,,29076,15452
PDB,2JUP,BMRB Entry Tracking System,29093,15453
BMRB,15455,AbaA3-DKP-insulin,29115,15454
PDB,2JUU,BMRB Entry Tracking System,29115,15454
BMRB,15454,ALOA3-DKP-insulin,29140,15455
PDB,2JUV,BMRB Entry Tracking System,29140,15455
PDB,2JUW,BMRB Entry Tracking System,29165,15456
BMRB,15458,F0 domain (residues 1-85),29195,15457
BMRB,15615,F0F1 double domain,29195,15457
BMRB,15616,F1,29195,15457
BMRB,15625,Residues 1815-1973,29195,15457
BMRB,16930,F2 domain (residues 196-309),29195,15457
BMRB,16932,F2F3 domain (residues 196-405),29195,15457
BMRB,16959,F1F2 double domain (residues 86-303),29195,15457
BMRB,17070,domain C,29195,15457
PDB,2KBB,BMRB Entry Tracking System,29195,15457
PDB,2KMA,structure entry,29195,15457
BMRB,15457,"domain, 1655-1822",29217,15458
BMRB,15615,F0F1 double domain,29217,15458
BMRB,15616,F1,29217,15458
BMRB,15625,Residues 1815-1973,29217,15458
BMRB,16930,F2 domain (residues 196-309),29217,15458
BMRB,16932,F2F3 domain (residues 196-405),29217,15458
BMRB,16959,F1F2 double domain (residues 86-303),29217,15458
BMRB,17070,domain C,29217,15458
PDB,2KBB,structure entry,29217,15458
PDB,2KMA,structure entry,29217,15458
BMRB,7406,ccc2 (complex form),29279,15461
PDB,2JUZ,BMRB Entry Tracking System,29296,15462
PDB,2JV1,BMRB Entry Tracking System,29336,15464
PDB,2JV2,BMRB Entry Tracking System,29351,15465
PDB,2JV4,BMRB Entry Tracking System,29370,15466
BMRB,7234,beta phosphoglucosmutase complex with glucose-6-phosphate and MgF3-,29389,15467
BMRB,7235,beta phosphoglucomutase open form,29389,15467
BMRB,15618,"NMR assignment of the domain 527-651 from the SARS-CoV nonstructural protein
nsp3",29432,15469
PDB,2jzd,"NMR structure of the domain 527-651 from the SARS-CoV nonstructural protein
nsp3, ensemble of 20 energy minimized conformers",29432,15469
PDB,2jze,"NMR structure of the domain 527-651 from the SARS-CoV nonstructural protein
nsp3, SINGLE CONFORMER",29432,15469
PDB,2JZF,"NMR structure of the domain 513-651 from the SARS-CoV nonstructural protein
nsp3, SINGLE CONFORMER",29432,15469
PDB,2JVA,BMRB Entry Tracking System,29478,15471
BMRB,4886,Backbone 1H and 15N chemical shifts assignments of folded Azotobacter vinelandii C69A apoflavodoxin,29516,15474
PDB,2K14,Solution Structure of the Soluble Domain of the NfeD Protein YuaF from Bacillus subtilis,29533,15475
PDB,2HEP,structure of full length ynzC,29552,15476
PDB,2JVD,BMRB Entry Tracking System,29552,15476
PDB,2JVE,BMRB Entry Tracking System,29580,15477
PDB,2JVF,BMRB Entry Tracking System,29601,15478
BMRB,3078,wild type assignments,29636,15480
BMRB,3079,microglobulin,29636,15480
PDB,1JNJ,solution structure of wild-type beta2-microglobulin,29636,15480
PDB,2VB5,BMRB Entry Tracking System,29636,15480
PDB,2P8V,On hold - Huang et al. Crystal structure of human Homer3 EVH1 domain,29650,15481
,gi:21361157,GenBank NCBI identification,29650,15481
,Q9NSC5,Swissprot ID,29650,15481
TargetDB,RhR95,,29668,15482
BMRB,15487,Npl3p RRM2,29726,15485
PDB,2JVO,BMRB Entry Tracking System,29726,15485
BMRB,15485,Npl3p RRM1,29765,15487
PDB,2JVR,BMRB Entry Tracking System,29765,15487
PDB,1IEP,"Crystal structure of ABL kinase domain in complex with imatinib (Nagar et al. 2002, Can. Res.)",29786,15488
PDB,2JVV,BMRB Entry Tracking System,29832,15490
PDB,2JVW,BMRB Entry Tracking System,29848,15491
BMRB,15493,fluorowillardiine-S1S2,29874,15492
BMRB,15494,bromowillardiine-S1S2,29874,15492
BMRB,15495,iodowillardiine-S1S2,29874,15492
BMRB,15496,kainate-S1S2,29874,15492
BMRB,15492,willardiine-S1S2,29891,15493
BMRB,15494,bromowillardiine-S1S2,29891,15493
BMRB,15495,iodowillardiine-S1S2,29891,15493
BMRB,15496,kainate-S1S2,29891,15493
BMRB,15492,willardiine-S1S2,29908,15494
BMRB,15493,fluorowillardiine-S1S2,29908,15494
BMRB,15495,iodowillardiine-S1S2,29908,15494
BMRB,15496,kainate-S1S2,29908,15494
BMRB,15492,willardiine-S1S2,29925,15495
BMRB,15493,fluorowillardiine-S1S2,29925,15495
BMRB,15494,bromowillardiine-S1S2,29925,15495
BMRB,15496,kainate-S1S2,29925,15495
BMRB,15492,willardiine-S1S2,29942,15496
BMRB,15493,fluorowillardiine-S1S2,29942,15496
BMRB,15494,bromowillardiine-S1S2,29942,15496
BMRB,15495,iodowillardiine-S1S2,29942,15496
BMRB,7407,MxiD - MxiM complex,29959,15497
BMRB,15500,mutant zinc fingers of the NEMO protein,29990,15499
PDB,2JVX,BMRB Entry Tracking System,29990,15499
PDB,2jvy,mutant zinc fingers of the NEMO protein,29990,15499
BMRB,15499,wild type zinc fingers of the NEMO protein,30009,15500
PDB,2jvx,wild type zinc fingers of the NEMO protein,30009,15500
PDB,2JVY,BMRB Entry Tracking System,30009,15500
BMRB,7408,"HMGB1, ABprime",30048,15502
BMRB,7409,"HMGB1, delta5",30048,15502
BMRB,7410,"HMGB1, delta10",30048,15502
BMRB,7411,"HMGB1, delta15",30048,15502
BMRB,7412,"HMGB1, delta20",30048,15502
BMRB,15504,MxiM - MxiD (553-570) complex,30063,15503
BMRB,15503,MxiM,30078,15504
PDB,2JW1,BMRB Entry Tracking System,30078,15504
EMDB,2vcd,PDB files; coordinates,30127,15507
BMRB,7021,NMR data for free protein,30127,15507
PDB,2JUF,BMRB Entry Tracking System,30161,15509
TargetDB,HR3443B,,30161,15509
PDB,2JW8,BMRB Entry Tracking System,30216,15511
PDB,2LQR,BMRB Entry Tracking System,30232,15512
PDB,1ZTR,,30364,15520
PDB,1FTT,NMR solution structure,30385,15521
BMRB,15525,Ral binding domain of RLIP76 in complex with RalB,30421,15524
PDB,2KWH,BMRB Entry Tracking System,30421,15524
BMRB,15524,Ral binding domain of RLIP76,30436,15525
PDB,2FFG,,30521,15529
PDB,2P3M,atomic coordinates,30554,15530
BMRB,15533,wt1-zf14-14mer,30592,15532
PDB,2JP9,BMRB Entry Tracking System,30592,15532
BMRB,15532,wt1-17mer,30610,15533
PDB,2JPA,BMRB Entry Tracking System,30610,15533
PDB,2JWS,BMRB Entry Tracking System,30646,15535
PDB,1ENH,Crystal structure of the protein,30663,15536
PDB,2JWT,BMRB Entry Tracking System,30663,15536
PDB,2JWU,BMRB Entry Tracking System,30684,15537
PDB,1OOA,Crystal structure of NF-kB (p50)2 bound to RNA,30701,15538
PDB,2JWV,BMRB Entry Tracking System,30701,15538
PDB,1FPO,X-ray crystal structure of HscB,30758,15541
PDB,2JX2,BMRB Entry Tracking System,30819,15543
PDB,2JX5,BMRB Entry Tracking System,30887,15547
PDB,2JX8,BMRB Entry Tracking System,30943,15550
PDB,2JX9,BMRB Entry Tracking System,30996,15553
PDB,2JXA,BMRB Entry Tracking System,30996,15553
PDB,1eh2,Apo EH domain,31017,15554
PDB,1ff1,low affinity complex,31017,15554
PDB,2JXC,BMRB Entry Tracking System,31017,15554
PDB,2JXD,BMRB Entry Tracking System,31045,15555
PDB,2JXF,BMRB Entry Tracking System,31087,15559
PDB,1eij,NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615,31136,15562
PDB,2cru,Solution structure of programmed cell death 5,31136,15562
PDB,2fh0,NMR Ensemble of The Yeast Saccharomyces cerevisiae protein Ymr074cp core region,31136,15562
PDB,2JW5,protein structure,31233,15566
PDB,2JXO,BMRB Entry Tracking System,31254,15567
BMRB,15572,RNA DUPLEX CONTAINING SINGLE ADENOSINE BULGE,31355,15571
PDB,2JXQ,BMRB Entry Tracking System,31355,15571
BMRB,15571,RNA DUPLEX,31376,15572
PDB,2JXS,BMRB Entry Tracking System,31376,15572
PDB,2JXU,BMRB Entry Tracking System,31425,15574
PDB,2JXW,BMRB Entry Tracking System,31439,15575
PDB,2JXX,BMRB Entry Tracking System,31463,15576
PDB,2JXY,BMRB Entry Tracking System,31509,15578
BMRB,15580,NS4A,31530,15579
BMRB,15582,NS3,31530,15579
BMRB,16886,NS2 [27-59],31530,15579
BMRB,16892,NS2 [60-99],31530,15579
PDB,2JY0,BMRB Entry Tracking System,31530,15579
BMRB,15579,NS2,31547,15580
BMRB,15582,NS3,31547,15580
BMRB,15579,NS2,31577,15582
BMRB,15580,NS4A,31577,15582
PDB,2JY9,BMRB Entry Tracking System,31609,15584
PDB,2JYA,BMRB Entry Tracking System,31633,15585
PDB,2JY7,BMRB Entry Tracking System,31717,15591
PDB,2K0B,BMRB Entry Tracking System,31717,15591
PDB,2JY8,BMRB Entry Tracking System,31737,15592
PDB,2jyc,,31758,15593
BMRB,6699,La3+ monosubstituted calbindin D9k,31781,15594
PDB,2BCA,,31781,15594
PDB,1HA6,Mouse MIP-3alpha/CCL20,31825,15596
PDB,1M8A,Human MIP-3alpha X-ray structure,31825,15596
PDB,2HCI,Human MIP-3alpha X-ray structure,31825,15596
PDB,2JYO,BMRB Entry Tracking System,31825,15596
BMRB,15598,protein in reduced form,31844,15597
BMRB,15597,protein in oxidized form,31865,15598
BMRB,6625,Pi-bound form PHPT1,31885,15599
PDB,2OZX,Pi-free structure,31885,15599
PDB,2KPH,BMRB Entry Tracking System,31900,15601
PDB,2jz2,,31980,15604
TargetDB,SgR42,,31980,15604
PDB,2PV6,,32008,15605
BMRB,6140,backbone chemical shifts of uniformly labeled At3g16450.1,32050,15607
PDB,2JZ4,BMRB Entry Tracking System,32050,15607
TargetDB,GO.12798,At3g16450.1,32050,15607
PDB,2JZ5,BMRB Entry Tracking System,32067,15608
PDB,2JZ6,BMRB Entry Tracking System,32089,15609
PDB,2JZA,BMRB Entry Tracking System,32145,15611
TargetDB,EwR120,,32145,15611
PDB,2K4L,BMRB Entry Tracking System,32189,15613
PDB,2JZB,BMRB Entry Tracking System,32207,15614
BMRB,15457,"domain, 1655-1822",32224,15615
BMRB,15458,F0 domain (residues 1-85),32224,15615
BMRB,15616,F1,32224,15615
BMRB,15625,Residues 1815-1973,32224,15615
BMRB,16930,F2 domain (residues 196-309),32224,15615
BMRB,16932,F2F3 domain (residues 196-405),32224,15615
BMRB,16959,F1F2 double domain (residues 86-303),32224,15615
BMRB,17070,domain C,32224,15615
PDB,2KBB,structure entry,32224,15615
PDB,2KMA,BMRB Entry Tracking System,32224,15615
BMRB,15457,"domain, 1655-1822",32245,15616
BMRB,15458,F0 domain (residues 1-85),32245,15616
BMRB,15615,F0F1  double domain,32245,15616
BMRB,15625,Residues 1815-1973,32245,15616
BMRB,16930,F2 domain (residues 196-309),32245,15616
BMRB,16932,F2F3 domain (residues 196-405),32245,15616
BMRB,16959,F1F2 double domain (residues 86-303),32245,15616
BMRB,17070,domain C,32245,15616
PDB,2KBB,structure entry,32245,15616
PDB,2KMA,structure entry,32245,15616
PDB,2JZC,BMRB Entry Tracking System,32266,15617
BMRB,15469,NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3,32288,15618
PDB,2JZD,BMRB Entry Tracking System,32288,15618
PDB,2JZF,"NMR structure of the domain 513-651 of the SARS-CoV nonstructural protein nsp3, single conformer",32288,15618
PDB,2RNK,"NMR structure of the domain 513-651 of the SARS-CoV nonstructural protein nsp3, ensemble of twenty energy minimized structures",32288,15618
BMRB,15621,peptide modified by apha-D-mannopyranose,32319,15620
BMRB,15620,unmodified peptide,32335,15621
PDB,2JOB,BMRB Entry Tracking System,32352,15622
PDB,2K7D,BMRB Entry Tracking System,32370,15623
BMRB,6023,"1H, 15N, and 13C resonance assignments of calmodulin complexed with the calmodulin-binding domain of calcineurin",32386,15624
PDB,2JZI,BMRB Entry Tracking System,32386,15624
BMRB,15457,"domain, 1655-1822",32405,15625
BMRB,15458,F0 domain (residues 1-85),32405,15625
BMRB,15615,F0F1  double domain,32405,15625
BMRB,15616,F1,32405,15625
BMRB,16930,F2 domain (residues 196-309),32405,15625
BMRB,16932,F2F3 domain (residues 196-405),32405,15625
BMRB,16959,F1F2 double domain (residues 86-303),32405,15625
BMRB,17070,domain C,32405,15625
PDB,2KBB,structure entry,32405,15625
PDB,2KMA,structure entry,32405,15625
PDB,2K01,BMRB Entry Tracking System,32529,15633
PDB,2K02,BMRB Entry Tracking System,32549,15634
BMRB,15633,SDF1 dimer,32564,15635
BMRB,15636,"CXCL12/SDF1-alpha, CXCR4",32564,15635
BMRB,15637,"CXCL12/SDF1-alpha, CXCR4 containing a sulfotyrosine",32564,15635
PDB,2K03,BMRB Entry Tracking System,32564,15635
BMRB,15633,SDF1 dimer,32587,15636
BMRB,15635,"CXCL12/SDF1-alpha, CXCR4 containing a sulfotyrosine",32587,15636
BMRB,15637,"CXCL12/SDF1-alpha, CXCR4 containing a sulfotyrosine",32587,15636
PDB,2K04,BMRB Entry Tracking System,32587,15636
BMRB,15633,SDF1 dimer,32609,15637
BMRB,15635,"CXCL12/SDF1-alpha, CXCR4 containing a sulfotyrosine",32609,15637
BMRB,15636,"CXCL12/SDF1-alpha, CXCR4",32609,15637
PDB,2K05,BMRB Entry Tracking System,32609,15637
PDB,2K06,BMRB Entry Tracking System,32699,15642
PDB,2K0A,BMRB Entry Tracking System,32730,15644
PDB,2K0D,BMRB Entry Tracking System,32752,15645
BMRB,15648,"HSV-1 gH protein, R642S gH626-644 fusion peptide",32795,15647
BMRB,15649,"HSV-1_gH_protein,_L627S_gH626-644_fusion_peptide",32795,15647
BMRB,15647,"HSV-1 gH protein, gH626-644 fusion peptide",32809,15648
BMRB,15649,"HSV-1_gH_protein,_L627S_gH626-644_fusion_peptide",32809,15648
BMRB,15647,"HSV-1 gH protein, gH626-644 fusion peptide",32824,15649
BMRB,15648,"HSV-1 gH protein, R642S gH626-644 fusion peptide",32824,15649
BMRB,7416,calmodulin with Terbium(III),32839,15650
BMRB,7417,calmodulin with Dysprosium(III),32839,15650
BMRB,7418,calmodulin with Thulium(III),32839,15650
PDB,2K0L,BMRB Entry Tracking System,32861,15651
BMRB,15659,act_ACP,33021,15658
BMRB,15658,act_holo-acp,33037,15659
PDB,1AF8,The new entry has refined and improved coordinates,33037,15659
PDB,2AF8,The new entry has refined and improved coordinates,33037,15659
PDB,2K0Y,BMRB Entry Tracking System,33037,15659
PDB,2KO5,Structure,33064,15660
PDB,2M1S,BMRB Entry Tracking System,33064,15660
PDB,2LC5,BMRB Entry Tracking System,33134,15663
PDB,2K10,BMRB Entry Tracking System,33172,15665
BMRB,15671,TAF3-PHD_H3K4me3,33249,15670
PDB,2K16,BMRB Entry Tracking System,33249,15670
BMRB,15670,TAF3-PHD,33271,15671
PDB,2K17,BMRB Entry Tracking System,33271,15671
PDB,2K19,BMRB Entry Tracking System,33310,15673
PDB,2K1B,BMRB Entry Tracking System,33330,15674
PDB,1FO7,E200K variant of the human prion protein,33348,15676
PDB,1QM1,wild type human prion protein,33348,15676
PDB,2K1D,BMRB Entry Tracking System,33348,15676
PDB,2K1E,BMRB Entry Tracking System,33362,15677
PDB,2KB1,BMRB Entry Tracking System,33362,15677
PDB,2K1H,BMRB Entry Tracking System,33383,15678
PDB,2K1M,BMRB Entry Tracking System,33404,15679
BMRB,15685,EGF2 - MIC1 complex,33455,15682
BMRB,15692,TgMIC1-CT TgMIC16-EGF2 complex,33455,15682
BMRB,6376,C-terminal domain from TgMIC1,33455,15682
BMRB,15682,unbound EGF2,33531,15685
BMRB,15692,TgMIC1-CT TgMIC16-EGF2 complex,33531,15685
BMRB,6376,C-terminal domain from TgMIC1,33531,15685
PDB,2bvb,,33531,15685
PDB,2K22,BMRB Entry Tracking System,33550,15687
PDB,2K24,BMRB Entry Tracking System,33565,15688
PDB,2K25,BMRB Entry Tracking System,33579,15689
BMRB,6266,Cu(I)-HAH1,33593,15690
PDB,1KVJ,Cu(I)-MNK1,33593,15690
PDB,1TL4,Cu(I)-HAH1,33593,15690
PDB,3CJK,HAH1-Cd(II)-MNK1,33593,15690
PDB,2K29,BMRB Entry Tracking System,33623,15691
BMRB,15682,unbound EGF2,33642,15692
BMRB,15685,EGF2 - MIC1 complex,33642,15692
BMRB,6376,C-terminal domain from TgMIC1,33642,15692
PDB,2bvb,,33642,15692
PDB,2K27,BMRB Entry Tracking System,33658,15693
PDB,2K28,BMRB Entry Tracking System,33694,15695
PDB,2K2A,BMRB Entry Tracking System,33730,15698
PDB,2K2C,BMRB Entry Tracking System,33750,15700
PDB,2K2D,BMRB Entry Tracking System,33777,15701
PDB,2FVT,similar protein / homologue,33805,15702
PDB,2GM2,similar protein / homologue,33805,15702
PDB,2K2E,BMRB Entry Tracking System,33805,15702
PDB,3CPK,X-ray structure of this protein,33805,15702
PDB,2K2F,BMRB Entry Tracking System,33849,15704
BMRB,6087,HCV p7,39028,15951
BMRB,7422,Complex with diamagnetic Lutetium,33867,15705
PDB,2K2J,BMRB Entry Tracking System,33908,15707
PDB,2K2M,BMRB Entry Tracking System,33958,15710
BMRB,15712,"SOD1, mutant A4V",33976,15711
BMRB,15713,"SOD1, mutant G85R",33976,15711
BMRB,15714,"SOD1, mutant D90A",33976,15711
BMRB,15711,"SOD1, wild type",33991,15712
BMRB,15713,"SOD1, mutant G85R",33991,15712
BMRB,15714,"SOD1, mutant D90A",33991,15712
BMRB,15711,"SOD1, wild type",34006,15713
BMRB,15712,"SOD1, mutant A4V",34006,15713
BMRB,15713,"SOD1, mutant D90A",34006,15713
BMRB,15711,"SOD1, wild type",34021,15714
BMRB,15712,"SOD1, mutant A4V",34021,15714
BMRB,15713,"SOD1, mutant G85R",34021,15714
PDB,2LB9,BMRB Entry Tracking System,34075,15717
PDB,2K2O,BMRB Entry Tracking System,34107,15718
BMRB,4880,N-terminus of Calponin,34128,15719
PDB,2K2P,BMRB Entry Tracking System,34167,15721
PDB,2K87,BMRB Entry Tracking System,34208,15723
BMRB,5571,chemical shift assignments oxidized flavodoxin,34226,15724
BMRB,5540,chemical shift assignments reduced flavodoxin,34226,15724
BMRB,15725,3J coupling constants chi1-torsion oxidized flavodoxin,34226,15724
BMRB,15724,3J coupling constants phi-torsion oxidized flavodoxin,34255,15725
BMRB,15904,1J coupling constants related to the Ca carbons in oxidized Flavodoxin,34255,15725
BMRB,16579,2J coupling constants in oxidized Flavodoxin,34255,15725
BMRB,26018,3J coupling constants related to the psi-torsions in oxidized Flavodoxin,34255,15725
BMRB,5540,chemical shift assignments reduced flavodoxin,34255,15725
BMRB,5571,chemical shift assignments oxidized flavodoxin,34255,15725
BMRB,15727,assignment of the N-terminal region of human La protein in complex with RNA,34295,15726
BMRB,5719,Full assignment of the central RRM of La protein,34295,15726
BMRB,6044,Full assignment of La motif of La protein,34295,15726
BMRB,15726,Backbone assignment of apo La NTD,34316,15727
PDB,2K1K,BMRB Entry Tracking System,34338,15728
PDB,2K2X,BMRB Entry Tracking System,34364,15729
PDB,2K2Y,BMRB Entry Tracking System,34393,15730
PDB,2K2Z,BMRB Entry Tracking System,34409,15731
BMRB,15737,"AcrA(61-210DD), N-glycosylated form",34485,15735
PDB,2K32,BMRB Entry Tracking System,34485,15735
BMRB,15735,nonglycosylated form,34521,15737
PDB,2K32,nonglycosylated form,34521,15737
PDB,2K33,BMRB Entry Tracking System,34521,15737
PDB,2K36,BMRB Entry Tracking System,34590,15740
PDB,2K37,BMRB Entry Tracking System,34628,15742
PDB,2KP5,BMRB Entry Tracking System,34645,15743
PDB,2L7B,BMRB Entry Tracking System,34663,15744
PDB,2JYM,BMRB Entry Tracking System,34677,15745
BMRB,15749,Same protein in PBS Buffer and 90% H2O/10% D2O,34734,15748
BMRB,15748,Same protein in methanol,34752,15749
PDB,2K1I,This entry contains an ensemble of ten structures of this system,34811,15751
BMRB,15753,ILTat1.24 C1,34826,15752
PDB,1XU6,Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2,34826,15752
PDB,2JWH,BMRB Entry Tracking System,34826,15752
BMRB,15752,ILTat1.24 C2,34842,15753
PDB,1XU6,Structure of the C-terminal domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2,34842,15753
PDB,2JWG,BMRB Entry Tracking System,34842,15753
PDB,2K2I,structure of the protein,34858,15755
PDB,2CG6,Crystal structure (form I),34878,15756
PDB,2CG7,Crystal structure (form I),34878,15756
PDB,2CKU,Solution structure,34878,15756
PDB,1fbr,,34910,15758
PDB,2k1o,,34970,15761
PDB,2K3I,BMRB Entry Tracking System,34991,15762
PDB,2K3J,BMRB Entry Tracking System,35014,15763
BMRB,16768,chemical shifts in 90% TFE/10% H2O,35093,15767
BMRB,16767,chemical shifts in 90% H2O/10% D2O,35107,15768
NCBI,CAA50383,,35152,15770
PDB,2K3M,BMRB Entry Tracking System,35198,15774
PDB,2LP1,BMRB Entry Tracking System,35229,15775
PDB,2K3R,BMRB Entry Tracking System,35243,15776
PDB,2K3T,BMRB Entry Tracking System,35265,15777
PDB,1XEE,Solution structure of free CHIPS(31-121).,35284,15778
PDB,2E79,,35319,15779
BMRB,15781,5'-R(*GP*UP*CP*GP*UP*GP*CP*UP*G)-3',35346,15780
PDB,2K3Z,BMRB Entry Tracking System,35346,15780
BMRB,15780,5'-R(*GP*UP*CP*GP*AP*GP*CP*UP*G)-3',35366,15781
PDB,2K41,BMRB Entry Tracking System,35366,15781
BMRB,15785,C2A,35401,15783
PDB,2K43,BMRB Entry Tracking System,35401,15783
PDB,2BA3,Structure,35417,15784
BMRB,15783,FGF-1,35436,15785
PDB,2K45,BMRB Entry Tracking System,35436,15785
PDB,2QDX,crystal structure,35494,15788
PDB,2VRG,Structure and NOE restraint data (on hold until publication),35514,15789
PDB,2K48,BMRB Entry Tracking System,35536,15790
PDB,2K49,BMRB Entry Tracking System,35555,15791
PDB,2K4B,BMRB Entry Tracking System,35596,15793
PDB,2JVL,NMR structure of the C-terminal domain of multiprotein bridging factor 1 (MBF1) of Trichoderma reesei,35617,15795
PDB,1FBV,c-Cbl UbcH7 crystal structure,35636,15796
PDB,2K4D,BMRB Entry Tracking System,35636,15796
BMRB,15798,Tpx in the oxidized state,35656,15797
PDB,2JSZ,BMRB Entry Tracking System,35656,15797
BMRB,15797,Tpx in the reduced state,35676,15798
PDB,2JSY,BMRB Entry Tracking System,35676,15798
PDB,2K4J,BMRB Entry Tracking System,35740,15801
BMRB,15525,RalB-GMPPNP,35780,15803
PDB,2K4M,BMRB Entry Tracking System,35800,15804
TargetDB,TR8,,35800,15804
PDB,2K4N,BMRB Entry Tracking System,35830,15805
PDB,2K4Q,BMRB Entry Tracking System,35870,15807
PDB,2K4V,BMRB Entry Tracking System,35946,15810
PDB,2K4X,BMRB Entry Tracking System,35971,15811
PDB,2K4Y,BMRB Entry Tracking System,35996,15812
BMRB,15814,domain 5 of Dictyostelium ABP-120,36018,15813
PDB,2K4Z,BMRB Entry Tracking System,36053,15816
BMRB,15818,HPLC-12 (solid state),36074,15817
BMRB,15817,HPLC-12,36089,15818
PDB,2K54,BMRB Entry Tracking System,36260,15823
PDB,2K5C,BMRB Entry Tracking System,36388,15828
BMRB,15831,Y receptors N-Y2,36469,15830
BMRB,15832,Y receptors N-Y5,36469,15830
BMRB,15830,Y receptors N-Y1,36486,15831
BMRB,15832,Y receptors N-Y5,36486,15831
BMRB,15830,Y receptors N-Y1,36502,15832
BMRB,15831,Y receptors N-Y2,36502,15832
PDB,2K5F,BMRB Entry Tracking System,36544,15834
TargetDB,CtR121,,36544,15834
PDB,2K5G,BMRB Entry Tracking System,36570,15835
PDB,2K5H,BMRB Entry Tracking System,36594,15836
PDB,2K5J,BMRB Entry Tracking System,36641,15839
PDB,2K5L,BMRB Entry Tracking System,36695,15841
PDB,2K5N,BMRB Entry Tracking System,36719,15843
PDB,2K5O,BMRB Entry Tracking System,36785,15845
PDB,2K5R,BMRB Entry Tracking System,36838,15847
PDB,2K5W,BMRB Entry Tracking System,36941,15850
PDB,2K60,BMRB Entry Tracking System,36972,15851
BMRB,7423,3CaYb and CaM and DAPk complex,36996,15852
BMRB,7424,3CaTb and CaM and DAPk complex,36996,15852
BMRB,7425,3CaTm and CaM and DAPk complex,36996,15852
PDB,2K61,BMRB Entry Tracking System,36996,15852
PDB,2JN3,NMR solution structure of cl_BABP with two putative cholate ligands,37039,15854
PDB,2KG4,BMRB Entry Tracking System,37056,15855
BMRB,15857,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 and IBS1 of the group II intron Sc.ai5(gamma),37081,15856
BMRB,15858,NMR data related to NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37081,15856
BMRB,15859,NMR data related to NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37081,15856
BMRB,5962,NMR data related to solution structure of domain 5 from the ai5(gamma) group II intron,37081,15856
BMRB,6756,NMR data related to solution structure of domain 6 from the ai5(gamma)group II intron,37081,15856
PDB,1KXK,Crystal Structure of a RNA Molecule Containing Domain 5 and 6 of the Yeast ai5g Group II Self-splicing Intron,37081,15856
PDB,1R2P,Solution structure of domain 5 from the ai5(gamma) group II intron,37081,15856
PDB,2AHT,Solution structure of domain 6 from the ai5(gamma)group II intron,37081,15856
PDB,2K63,BMRB Entry Tracking System,37081,15856
PDB,2K64,NMR solution structure of the d3'-hairpin including EBS1 together with IBS1 of the group II intron Sc.ai5(gamma),37081,15856
PDB,2K65,NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37081,15856
PDB,2K66,NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37081,15856
PDB,3BWP,Crystal structure of a self-spliced group II intron,37081,15856
BMRB,15856,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 of the group II intron Sc.ai5(gamma),37114,15857
BMRB,15858,NMR data related to NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37114,15857
BMRB,15859,NMR data related to NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37114,15857
BMRB,5962,NMR data related to solution structure of domain 5 from the ai5(gamma) group II intron,37114,15857
BMRB,6756,NMR data related to solution structure of domain 6 from the ai5(gamma)group II intron,37114,15857
PDB,1KXK,Crystal Structure of a RNA Molecule Containing Domain 5 and 6 of the Yeast ai5g Group II Self-splicing Intron,37114,15857
PDB,1R2P,Solution structure of domain 5 from the ai5(gamma) group II intron,37114,15857
PDB,2AHT,Solution structure of domain 6 from the ai5(gamma)group II intron,37114,15857
PDB,2K63,NMR solution structure of the d3'-hairpin including the exon binding site 1 (EBS1) of the group II intron Sc.ai5(gamma),37114,15857
PDB,2K64,BMRB Entry Tracking System,37114,15857
PDB,2K65,NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37114,15857
PDB,2K66,NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37114,15857
PDB,3BWP,Crystal structure of a self-spliced group II intron,37114,15857
BMRB,15856,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 of the group II intron Sc.ai5(gamma),37144,15858
BMRB,15857,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 and IBS1 of the group II intron Sc.ai5(gamma),37144,15858
BMRB,15858,NMR data related to NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37144,15858
BMRB,15859,NMR data related to NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37144,15858
BMRB,5962,NMR data related to solution structure of domain 5 from the ai5(gamma) group II intron,37144,15858
BMRB,6756,NMR data related to solution structure of domain 6 from the ai5(gamma)group II intron,37144,15858
PDB,1KXK,Crystal Structure of a RNA Molecule Containing Domain 5 and 6 of the Yeast ai5g Group II Self-splicing Intron,37144,15858
PDB,1R2P,Solution structure of domain 5 from the ai5(gamma) group II intron,37144,15858
PDB,2AHT,Solution structure of domain 6 from the ai5(gamma)group II intron,37144,15858
PDB,2K63,NMR solution structure of the d3'-hairpin including the exon binding site 1 (EBS1) of the group II intron Sc.ai5(gamma),37144,15858
PDB,2K64,NMR solution structure of the d3'-hairpin including EBS1 and IBS1 of the group II intron Sc.ai5(gamma),37144,15858
PDB,2K65,BMRB Entry Tracking System,37144,15858
PDB,2K8J,BMRB Entry Tracking System,39028,15951
PDB,2K66,NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37144,15858
PDB,3BWP,Crystal structure of a self-spliced group II intron,37144,15858
BMRB,15856,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 of the group II intron Sc.ai5(gamma),37168,15859
BMRB,15857,NMR data related to NMR solution structure of the d3'-hairpin including EBS1 and IBS1 of the group II intron Sc.ai5(gamma),37168,15859
BMRB,15858,NMR data related to NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37168,15859
BMRB,15859,NMR data related to NMR solution structure of the d3'-stem closed by a GAAA tetraloop of the group II intron Sc.ai5(gamma),37168,15859
BMRB,5962,NMR data related to solution structure of domain 5 from the ai5(gamma) group II intron,37168,15859
BMRB,6756,NMR data related to solution structure of domain 6 from the ai5(gamma)group II intron,37168,15859
PDB,1KXK,Crystal Structure of a RNA Molecule Containing Domain 5 and 6 of the Yeast ai5g Group II Self-splicing Intron,37168,15859
PDB,1R2P,Solution structure of domain 5 from the ai5(gamma) group II intron,37168,15859
PDB,2AHT,Solution structure of domain 6 from the ai5(gamma)group II intron,37168,15859
PDB,2K63,NMR solution structure of the d3'-hairpin including the exon binding site 1 (EBS1) of the group II intron Sc.ai5(gamma),37168,15859
PDB,2K64,NMR solution structure of the d3'-hairpin including EBS1 together with IBS1 of the group II intron Sc.ai5(gamma),37168,15859
PDB,2K65,NMR solution structure of the exon/intron binding site 1 (EBS1/IBS1) of the group II intron Sc.ai5(gamma),37168,15859
PDB,2K66,BMRB Entry Tracking System,37168,15859
PDB,3BWP,Crystal structure of a self-spliced group II intron,37168,15859
PDB,2K67,BMRB Entry Tracking System,37207,15860
PDB,2K68,BMRB Entry Tracking System,37207,15860
PDB,2K69,BMRB Entry Tracking System,37207,15860
PDB,2FMC,solution structure of EAS,37233,15863
PDB,2K6A,BMRB Entry Tracking System,37233,15863
PDB,1YYB,Solution structure of 1-26 fragment of human programmed cell death 5 protein,37254,15864
PDB,2K6B,BMRB Entry Tracking System,37254,15864
BMRB,15176,NMR assignment of DARPP-32 residues 1-118,37271,15865
PDB,2K6D,BMRB Entry Tracking System,37287,15866
BMRB,15867,Urea-denatured GED,37322,15868
PDB,2K6I,BMRB Entry Tracking System,37371,15870
PDB,1QQV,Solution Structure of the Headpiece Domain of Chicken Villin,37408,15873
PDB,1QZP,NMR Structure of the Human Dematin Headpiece Domain,37408,15873
PDB,1UJS,Solution Structure of the Villin Headpiece Domain of Human Actin-Binding LIM protein homolog,37408,15873
PDB,1UNC,Solution Structure of the Human Villin C-Terminal Headpiece Subdomain,37408,15873
PDB,1UND,Solution Structure of the Human Advillin C-Terminal Subdomain,37408,15873
PDB,1VII,"Thermostable Subdomain from Chicken Villin Headpiece, NMR, Minimized Average Structure",37408,15873
PDB,1WY3,"Chicken Villin Subdomain HP-35, K65(NLE), N68H, pH 7.0",37408,15873
PDB,1WY4,"Chicken Villin Subdomain HP-35, K65(NLE), N68H, pH 5.1",37408,15873
PDB,1YRF,"Chicken Villin Subdomain HP-35, N68H, pH 6.7",37408,15873
PDB,1YRI,"Chicken Villin Subdomain HP-35, N68H, pH 6.4",37408,15873
PDB,1YU5,Crystal Structure of the Headpiece Domain of Chicken Villin,37408,15873
PDB,1YU7,Crystal Structure of the W64A Mutant of Villin Headpiece,37408,15873
PDB,1YU8,Crystal Structure of the R37A Mutant of Villin Headpiece,37408,15873
PDB,1ZV6,NMR Structure of the human Dematin Headpiece S74E Mutant,37408,15873
PDB,2JM0,Solution Structure of Chicken Villin Headpiece Subdomain Containing a Fluorinated Sidechain in the Core,37408,15873
PDB,2K6M,BMRB Entry Tracking System,37408,15873
PDB,2PPZ,NMR Solution Structure of the Villin Headpiece Mutant G34L,37408,15873
PDB,1QQV,Solution Structure of the Headpiece Domain of Chicken Villin,37432,15874
PDB,1QZP,NMR Structure of the Human Dematin Headpiece Domain,37432,15874
PDB,1UJS,Solution Structure of the Villin Headpiece Domain of Human Actin-Binding LIM protein homolog,37432,15874
PDB,1UNC,Solution Structure of the Human Villin C-Terminal Headpiece Subdomain,37432,15874
PDB,1UND,Solution Structure of the Human Advillin C-Terminal Subdomain,37432,15874
PDB,1VII,"Thermostable Subdomain from Chicken Villin Headpiece, NMR, Minimized Average Structure",37432,15874
PDB,1WY3,"Chicken Villin Subdomain HP-35, K65(NLE), N68H, pH 7.0",37432,15874
PDB,1WY4,"Chicken Villin Subdomain HP-35, K65(NLE), N68H, pH 5.1",37432,15874
PDB,1YRF,"Chicken Villin Subdomain HP-35, N68H, pH 6.7",37432,15874
PDB,1YRI,"Chicken Villin Subdomain HP-35, N68H, pH 6.4",37432,15874
PDB,1YU5,Crystal Structure of the Headpiece Domain of Chicken Villin,37432,15874
PDB,1YU7,Crystal Structure of the W64A Mutant of Villin Headpiece,37432,15874
PDB,1YU8,Crystal Structure of the R37A Mutant of Villin Headpiece,37432,15874
PDB,1ZV6,NMR Structure of the human Dematin Headpiece S74E Mutant,37432,15874
PDB,2JM0,Solution Structure of Chicken Villin Headpiece Subdomain Containing a Fluorinated Sidechain in the Core,37432,15874
PDB,2K6N,BMRB Entry Tracking System,37432,15874
PDB,2PPZ,NMR Solution Structure of the Villin Headpiece Mutant G34L,37432,15874
PDB,2FBS,N-terminal fragment of LL-37,37475,15876
PDB,2FBU,C-terminal fragment of LL-37,37475,15876
PDB,2K6O,BMRB Entry Tracking System,37475,15876
PDB,1ugm,,37490,15877
PDB,2K6Q,BMRB Entry Tracking System,37490,15877
PDB,2zjd,,37490,15877
BMRB,7426,YopE free state,37511,15878
BMRB,7427,n-terminal YopE effector domain,37511,15878
PDB,1FME,beta-beta-alpha fold,37526,15879
PDB,1FSV,beta-beta-alpha fold,37526,15879
PDB,2K6R,BMRB Entry Tracking System,37526,15879
PDB,2K6S,BMRB Entry Tracking System,37560,15880
PDB,2pe8,SPF45 UHM domain,37596,15882
PDB,1byy,,40418,16032
BMRB,15887,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with U2AF65(85-112)",37641,15885
BMRB,15888,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF1 (1-25)",37641,15885
BMRB,15889,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (194-229)",37641,15885
BMRB,15890,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (317-357)",37641,15885
BMRB,15891,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with Prp16 (201-238)",37641,15885
PDB,2DNY,NMR structure of the same domain,37641,15885
PDB,3dxb,crystal structure of the same domain,37641,15885
BMRB,15885,backbone assignment of the UHM domain of Puf60,37660,15887
BMRB,15888,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF1 (1-25)",37660,15887
BMRB,15889,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (194-229)",37660,15887
BMRB,15890,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (317-357)",37660,15887
BMRB,15891,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with Prp16 (201-238)",37660,15887
PDB,1jmt,The peptide ligand U2AF65(85-112) in 1jmt is the same as the ligand titrated to Puf60(UHM) in this entry,37660,15887
PDB,2DNY,NMR structure of the UHM domain of Puf60,37660,15887
PDB,3dxb,crystal structure of the UHM domain of Puf60,37660,15887
BMRB,15885,backbone assignment of the UHM domain of Puf60,37678,15888
BMRB,15887,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with U2AF65(85-112)",37678,15888
BMRB,15889,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (194-229)",37678,15888
BMRB,15890,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (317-357)",37678,15888
BMRB,15891,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with Prp16 (201-238)",37678,15888
PDB,1opi,The peptide ligand SF1(1-25) in 1opi is the same as the ligand titrated to Puf60(UHM) in this entry,37678,15888
PDB,2DNY,NMR structure of the UHM domain of Puf60,37678,15888
PDB,3dxb,crystal structure of the UHM domain of Puf60,37678,15888
BMRB,15885,backbone assignment of the UHM domain of Puf60,37696,15889
BMRB,15887,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with U2AF65(85-112)",37696,15889
BMRB,15888,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF1 (1-25)",37696,15889
BMRB,15890,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155 (317-357)",37696,15889
BMRB,15891,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with Prp16 (201-238)",37696,15889
PDB,2DNY,NMR structure of the UHM domain of Puf60,37696,15889
PDB,3dxb,crystal structure of the UHM domain of Puf60,37696,15889
BMRB,15885,backbone assignment of the UHM domain of Puf60,37727,15890
BMRB,15887,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with U2AF65(85-112)",37727,15890
BMRB,15888,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF1(1-25)",37727,15890
BMRB,15889,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155(194-229)",37727,15890
BMRB,15891,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with Prp16 (201-238)",37727,15890
PDB,2DNY,NMR structure of the UHM domain of Puf60,37727,15890
PDB,3dxb,crystal structure of the UHM domain of Puf60,37727,15890
BMRB,15885,backbone assignment of the UHM domain of Puf60,37745,15891
BMRB,15887,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with U2AF65(85-112)",37745,15891
BMRB,15888,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF1(1-25)",37745,15891
BMRB,15889,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155(194-229)",37745,15891
BMRB,15890,"1H, 15N chemical shifts of the UHM domain of Puf60 in complex with SF3b155(317-357)",37745,15891
PDB,2DNY,NMR structure of the UHM domain of Puf60,37745,15891
PDB,3dxb,crystal structure of the UHM domain of Puf60,37745,15891
PDB,2K6V,BMRB Entry Tracking System,37779,15893
BMRB,15895,assignment of apo form (cis-P14),37799,15894
BMRB,15896,assignment of copper form (trans-P14),37799,15894
BMRB,15897,assignment of copper form (cis-P14),37799,15894
PDB,2K6W,BMRB Entry Tracking System,37799,15894
BMRB,15894,assignment of apo form (trans-P14),37819,15895
BMRB,15896,assignment of copper form (trans-P14),37819,15895
BMRB,15897,assignment of copper form (cis-P14),37819,15895
PDB,2k6w,,37819,15895
BMRB,15894,assignment of apo form (trans-P14),37839,15896
BMRB,15895,assignment of apo form (cis-P14),37839,15896
BMRB,15897,assignment of copper form (cis-P14),37839,15896
PDB,2k6w,structure of apo form (trans-P14),37839,15896
PDB,2k6y,structure of apo form (cis-P14),37839,15896
PDB,2K6Z,BMRB Entry Tracking System,37839,15896
BMRB,15894,assignment of apo form (trans-P14),37861,15897
BMRB,15895,assignment of apo form (cis-P14),37861,15897
BMRB,15896,assignment of copper form (trans-P14),37861,15897
PDB,2k6w,structure of apo form (trans-P14),37861,15897
PDB,2k6y,structure of apo form (cis-P14),37861,15897
PDB,2k6z,solution structures of copper form (trans P14),37861,15897
PDB,2K70,BMRB Entry Tracking System,37861,15897
PDB,2K71,,37883,15898
RCSB,100756,,37883,15898
PDB,2K72,BMRB Entry Tracking System,37933,15900
BMRB,15724,3J coupling constants related to phi-torsions in oxidized flavodoxin,38038,15904
BMRB,15725,3J coupling constants related to chi1-torsions in oxidized flavodoxin,38038,15904
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,38038,15904
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,38038,15904
BMRB,15907,1J coupling constants related to the Ca carbons in human Ubiquitin,38038,15904
PDB,1qg9,,40418,16032
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,38038,15904
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,38038,15904
BMRB,5540,"1H, 13C and 15N chemical shift assignments for reduced flavodoxin",38038,15904
BMRB,5571,"1H, 13C and 15N chemical shift assignments for oxidized flavodoxin",38038,15904
BMRB,133,1H chemical shift assignments for Ribonuclease T1,38076,15905
BMRB,15904,1J coupling constants related to the Ca carbons in oxidised Flavodxin,38076,15905
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,38076,15905
BMRB,15907,1J coupling constants related to the Ca carbons in human Ubiquitin,38076,15905
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,38076,15905
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,38076,15905
BMRB,1658,15N chemical shift assignments for Ribonuclease T1,38076,15905
BMRB,15904,1J coupling constants related to the Ca carbons in oxidised Flavodxin,38108,15906
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,38108,15906
BMRB,15907,1J coupling constants related to the Ca carbons in human Ubiquitin,38108,15906
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,38108,15906
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,38108,15906
BMRB,4342,"1H, 15N, 13C chemical-shift assignments for Frataxin C-terminal domain (90-210)",38108,15906
BMRB,15410,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for human ubiquitin",38136,15907
BMRB,15904,1J coupling constants related to the Ca carbons in oxidised Flavodxin,38136,15907
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,38136,15907
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,38136,15907
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,38136,15907
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,38136,15907
BMRB,6466,"1H, 15N, 13C chemical-shift assignments for human Ubiquitin",38136,15907
BMRB,6488,3J(HA-N) and 3J(HN-CO) coupling constants in Ubiquitin,38136,15907
BMRB,15904,1J coupling constants related to the Ca carbons in oxidised Flavodxin,38169,15908
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,38169,15908
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,38169,15908
BMRB,15907,1J coupling constants related to the Ca carbons in Ubiquitin,38169,15908
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,38169,15908
BMRB,5352,"1H, 13C and 15N resonance assignment of Bacillus agaradhaerens xylanase",38169,15908
BMRB,15904,1J coupling constants related to the Ca carbons in oxidised Flavodxin,38205,15909
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,38205,15909
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,38205,15909
BMRB,15907,1J coupling constants related to the Ca carbons in Ubiquitin,38205,15909
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,38205,15909
BMRB,5618,"Backbone 1H, 13C, 15N and Side Chain 13C Chemical Shift Assignments for DFPase from Loligo vulgaris",38205,15909
PDB,1awj,SH3 peptide complex,38297,15912
PDB,1luk,cis SH2 domain,38297,15912
PDB,1lun,trans SH2 domain,38297,15912
PDB,2etz,SH2 peptide complex,38297,15912
PDB,2K79,BMRB Entry Tracking System,38297,15912
PDB,2rna,SH3 domain,38297,15912
PDB,2K78,BMRB Entry Tracking System,38320,15913
PDB,2K7E,BMRB Entry Tracking System,38364,15915
PDB,2K7I,BMRB Entry Tracking System,38394,15916
BMRB,6024,wt TEM-1 beta-lactamase,38420,15917
BMRB,6357,"wt TEM-1 beta-lactamase, corrected",38420,15917
BMRB,15934,M-crystallin (calcium bound form) in presence of 6 M Gdn-Hcl,38439,15918
BMRB,6904,M-Crystallin Ca2+ loaded (HOLO) monomer,38439,15918
PDB,2K7L,BMRB Entry Tracking System,38457,15919
PDB,2K7N,BMRB Entry Tracking System,38506,15922
PDB,1B4C,apo-S100B,38520,15923
PDB,1QLK,"Ca2+-S100B, no RDC",38520,15923
PDB,2K7O,BMRB Entry Tracking System,38520,15923
BMRB,15925,domains 18-19,38542,15924
PDB,2K7P,BMRB Entry Tracking System,38542,15924
BMRB,15924,domains 16-17,38562,15925
PDB,2K7Q,BMRB Entry Tracking System,38562,15925
PDB,2K7R,BMRB Entry Tracking System,38583,15926
PDB,1X0O,ARNT PAS-B Wildtype,38623,15928
PDB,2K7S,BMRB Entry Tracking System,38623,15928
BMRB,4870,4.2 sigma70,38642,15930
PDB,2K7V,BMRB Entry Tracking System,38659,15931
PDB,2K7Z,BMRB Entry Tracking System,38673,15932
BMRB,15918,M-crystallin (calcium bound form) in presence of 4 M Gdn-Hcl,38708,15934
BMRB,6904,M-Crystallin Ca2+ loaded (HOLO) monomer,38708,15934
BMRB,15930,chemical shifts and relaxation parameters of 4 sigma70,38757,15936
BMRB,4870,4 sigma70,38757,15936
PDB,2K85,BMRB Entry Tracking System,38804,15938
PDB,2K86,BMRB Entry Tracking System,38822,15939
PDB,2K8D,BMRB Entry Tracking System,38862,15941
PDB,2K8E,BMRB Entry Tracking System,38897,15943
PDB,2K8F,BMRB Entry Tracking System,38920,15944
PDB,2K76,BMRB Entry Tracking System,38962,15946
PDB,2KIZ,BMRB Entry Tracking System,38979,15948
BMRB,5455,PRL-1 WT NMR Assignments,38995,15949
BMRB,6080,PRL-1 WT NMR Assignments,38995,15949
PDB,1r6h,Crystal Structure of PRL-3,38995,15949
PDB,1v3a,Crystal Structure of PRL-3,38995,15949
PDB,1xm2,Crystal Structure of PRL-1 C104S,38995,15949
PDB,1zck,Crystal Structure of WT PRL-1,38995,15949
PDB,1zcl,Crystal Structure of PRL-1 C104S,38995,15949
PDB,2K8I,BMRB Entry Tracking System,39013,15950
PDB,2K3G,BMRB Entry Tracking System,39114,15956
PDB,2K8Q,BMRB Entry Tracking System,39152,15958
BMRB,7429,Bound Form,39178,15959
BMRB,15963,HasAp Full-Length polypeptide,39224,15962
BMRB,15962,HasAp truncated polypeptide,39249,15963
BMRB,7430,Reduced ERp18,39274,15964
PDB,2K8V,BMRB Entry Tracking System,39274,15964
BMRB,4995,Solution NMR Structure and Folding Dynamics of TM1bZip,39297,15965
PDB,1IHQ,"structure of unbound TM1b(1-19)Zip, a peptide model of the N terminus of non-muscle tropomyosin",39297,15965
PDB,2K8X,BMRB Entry Tracking System,39297,15965
PDB,2HI7,Crystal structure of DsbB-DsbA complex,39319,15966
PDB,2K73,BMRB Entry Tracking System,39319,15966
PDB,3E9J,Crystal structure of charge transfer complex of DsbB,39319,15966
BMRB,7432,"Chemical shifts, T1, T2, and NOE of IscU(D39A)",39339,15967
PDB,1qgt,Crystal structure of recombinant T= 4 capsid like particles formed by human hepatitis virus core protein (strain cw),39372,15969
PDB,2g33,Crystal structure of recombinant T= 4 capsid like particles formed by human hepatitis virus core protein (sub-type adyw),39372,15969
BMRB,15930,RNA polymerase sigma70 domain,39465,15975
BMRB,15936,RNA polymerase sigma70 subunit recorded at TFE,39465,15975
BMRB,4870,RNA polymerase sigma70 subunit,39465,15975
BMRB,18121,CdnL N-terminal domain 1-68 residues,39483,15977
BMRB,18151,CdnL 1-164 residues,39483,15977
PDB,2LT3,BMRB Entry Tracking System,39483,15977
PDB,1ZD0,,39546,15981
PDB,2K8Y,BMRB Entry Tracking System,39546,15981
PDB,2K9E,BMRB Entry Tracking System,39562,15983
BMRB,15447,8F19F1 module pair from Fibronectin,39581,15986
PDB,3EJH,Crystal Structure of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I Collagen Peptide,39581,15986
PDB,2K9I,BMRB Entry Tracking System,39606,15987
BMRB,6375,TonB C-terminal Domain monomer,39621,15988
PDB,1U07,,39621,15988
PDB,1XX3,,39621,15988
PDB,2GRX,,39621,15988
PDB,2GSK,,39621,15988
PDB,2K9K,BMRB Entry Tracking System,39621,15988
PDB,2K9N,BMRB Entry Tracking System,39636,15989
PDB,2KDZ,structure entry,39636,15989
PDB,2K9O,BMRB Entry Tracking System,39693,15992
BMRB,15994,XD Complex with C-Terminal Part of the Nucloeprotein.,39711,15993
BMRB,15993,XD,39728,15994
PDB,2K9P,BMRB Entry Tracking System,39745,15995
PDB,2WCY,BMRB Entry Tracking System,39766,15996
PDB,1BL0,homolog MarA,39884,16001
PDB,1D5Y,homolog Rob,39884,16001
PDB,2K9S,BMRB Entry Tracking System,39884,16001
PDB,2K9U,BMRB Entry Tracking System,39907,16002
PDB,2k1k,EphA1 pH 4.3,39937,16005
PDB,2k1l,EphA1 pH 6.3,39937,16005
PDB,2K9Y,BMRB Entry Tracking System,39937,16005
PDB,2K9Z,BMRB Entry Tracking System,39957,16006
PDB,2KA0,BMRB Entry Tracking System,39979,16007
BMRB,16011,ribonuclease A in 8 M urea,40040,16010
BMRB,2928,ribonuclease A,40040,16010
BMRB,4031,bovine pancreatic ribonuclease A,40040,16010
BMRB,4032,"bovine pancreatic [C65S,C72S] ribonuclease A",40040,16010
BMRB,443,ribonuclease A,40040,16010
PDB,2aas,,40040,16010
BMRB,1072,ribonuclease A,40055,16011
BMRB,16010,Ribonuclease A in 40% Acetic Acid,40055,16011
BMRB,2928,ribonuclease A,40055,16011
BMRB,4031,bovine pancreatic ribonuclease A,40055,16011
BMRB,4032,"bovine pancreatic [C65S,C72S] ribonuclease A",40055,16011
BMRB,443,ribonuclease A,40055,16011
PDB,2aas,,40055,16011
PDB,2KA1,BMRB Entry Tracking System,40070,16012
PDB,2KA4,BMRB Entry Tracking System,40088,16014
PDB,2KA6,BMRB Entry Tracking System,40106,16015
PDB,1zko,X-ray structure,40124,16016
PDB,2KA7,BMRB Entry Tracking System,40124,16016
PDB,2KA5,BMRB Entry Tracking System,40163,16019
PDB,2KAD,BMRB Entry Tracking System,40182,16020
BMRB,11073,A more extended version of 16021,40203,16021
BMRB,15391,Tetrameric structure of KIA7 peptide,40221,16022
BMRB,15392,Tetrameric structure of KIA7F peptide,40221,16022
BMRB,16023,Tetramer of KIA7H peptide,40221,16022
PDB,2KAG,BMRB Entry Tracking System,40221,16022
PDB,2jo4,Tetrameric structure of KIA7 peptide,40221,16022
BMRB,15391,Tetrameric structure of KIA7 peptide,40242,16023
BMRB,15392,Tetrameric structure of KIA7F peptide,40242,16023
BMRB,16022,Tetramer of KIA7W peptide,40242,16023
PDB,2KAH,BMRB Entry Tracking System,40242,16023
PDB,2jo4,Tetrameric structure of KIA7 peptide,40242,16023
PDB,2kag,Not online yet,40242,16023
PDB,2KAJ,BMRB Entry Tracking System,40264,16024
PDB,2KAK,BMRB Entry Tracking System,40284,16025
BMRB,16027,"INSULIN A CHAIN, INSULIN B CHAIN (mutant)",40303,16026
BMRB,16026,"INSULIN A CHAIN, INSULIN B CHAIN (mutant)",40320,16027
PDB,2K91,BMRB Entry Tracking System,40320,16027
PDB,1DHL,delta-hemolysin (theoretical model),40336,16028
PDB,1DTC,synthethic acetyl-delta-toxin peptide dissolved in CD3OH/H2O (2:1),40336,16028
PDB,2DHL,delta-hemolysin (theoretical model),40336,16028
PDB,2DTB,synthethic delta-toxin peptide dissolved in CD3OH/H2O (2:1),40336,16028
PDB,2KAM,BMRB Entry Tracking System,40336,16028
PDB,3DHL,delta-hemolysin (theoretical model),40336,16028
PDB,2KAN,BMRB Entry Tracking System,40355,16029
TargetDB,AR3433A,,40355,16029
PDB,2KAT,BMRB Entry Tracking System,40379,16030
PDB,1byy,SODIUM CHANNEL IIA INACTIVATION GATE,40401,16031
PDB,1qg9,SECOND REPEAT (IS2MIC) FROM VOLTAGE-GATED SODIUM CHANNEL,40401,16031
PDB,2KAV,BMRB Entry Tracking System,40418,16032
BMRB,16034,Ca complex form,40441,16033
PDB,2KAX,BMRB Entry Tracking System,40441,16033
BMRB,16033,apo form,40464,16034
PDB,2KAY,BMRB Entry Tracking System,40464,16034
PDB,2KB2,BMRB Entry Tracking System,40503,16037
BMRB,16039,"NMR structure of the unphosphorylated form of OdhI,OdhI.",40525,16038
PDB,2KB3,BMRB Entry Tracking System,40525,16038
BMRB,16038,"NMR Structure of the phosphorylated form of OdhI, pOdhI.",40542,16039
PDB,2KB4,BMRB Entry Tracking System,40542,16039
PDB,2KB6,BMRB Entry Tracking System,40557,16040
BMRB,16046,human brain-type fatty acid binding protein (hb-FABP bound to docosahexaenoic acid (DHA)),40591,16042
BMRB,16047,human brain-type fatty acid binding protein (hb-FABP bound to elaidic acid),40591,16042
BMRB,16048,human brain-type fatty acid binding protein (hb-FABP bound to oleic acid (OLA)),40591,16042
BMRB,16049,human brain-type fatty acid binding protein (hb-FABP bound to linoleic acid (LNA)),40591,16042
BMRB,5320,1H and 15N assignments,40591,16042
PDB,1JJX,solution structure,40591,16042
PDB,2KBI,BMRB Entry Tracking System,40642,16045
BMRB,16042,apo human brain-type fatty acid binding protein,40659,16046
BMRB,16047,human brain-type fatty acid binding protein (hb-FABP bound to elaidic acid),40659,16046
BMRB,16048,human brain-type fatty acid binding protein (hb-FABP bound to oleic acid (OLA)),40659,16046
BMRB,16049,human brain-type fatty acid binding protein (hb-FABP bound to linoleic acid (LNA)),40659,16046
PDB,1FDQ,DHA-bound human brain-type fatty acid binding protein,40659,16046
PDB,1JJX,apo human brain-type fatty acid binding protein,40659,16046
BMRB,16042,human brain-type fatty acid binding protein (hb-FABP),40675,16047
BMRB,16046,human brain-type fatty acid binding protein (hb-FABP bound to docosahexaenoic acid (DHA)),40675,16047
BMRB,16048,human brain-type fatty acid binding protein (hb-FABP bound to oleic acid (OLA)),40675,16047
BMRB,16049,human brain-type fatty acid binding protein (hb-FABP bound to linoleic acid (LNA)),40675,16047
BMRB,16042,human brain-type fatty acid binding protein (hb-FABP),40691,16048
BMRB,16046,human brain-type fatty acid binding protein (hb-FABP bound to docosahexaenoic acid (DHA)),40691,16048
BMRB,16047,human brain-type fatty acid binding protein (hb-FABP bound to elaidic acid),40691,16048
BMRB,16049,human brain-type fatty acid binding protein (hb-FABP bound to linoleic acid (LNA)),40691,16048
BMRB,16042,human brain-type fatty acid binding protein (hb-FABP),40707,16049
BMRB,16046,human brain-type fatty acid binding protein (hb-FABP bound to docosahexaenoic acid (DHA)),40707,16049
BMRB,16047,human brain-type fatty acid binding protein (hb-FABP bound to elaidic acid),40707,16049
BMRB,16048,human brain-type fatty acid binding protein (hb-FABP bound to oleic acid (OLA)),40707,16049
PDB,1ZFS,,40723,16050
PDB,2K2F,,40723,16050
PDB,2KBM,BMRB Entry Tracking System,40723,16050
PDB,2KBN,BMRB Entry Tracking System,40741,16051
PDB,2KEN,BMRB Entry Tracking System,40741,16051
PDB,2KBT,BMRB Entry Tracking System,40783,16053
BMRB,16055,5'-D(P*TP*CP*GP*TP*TP*GP*CP*T)-3',40802,16054
PDB,2k8z,structure of the lineal anolgue d(TCGTTGCT),40802,16054
PDB,2K90,BMRB Entry Tracking System,40802,16054
BMRB,16054,5'-D(TP*CP*GP*TP*TP*GP*CP*T)-3',40819,16055
PDB,2k8z,structure of the lineal anolgue d(TCGTTGCT),40819,16055
PDB,2k90,structure of the lineal analogue d(TGCTTCGT),40819,16055
PDB,2K97,BMRB Entry Tracking System,40819,16055
PDB,2KBZ,BMRB Entry Tracking System,40857,16057
PDB,2KC0,BMRB Entry Tracking System,40873,16058
PDB,2KC5,BMRB Entry Tracking System,40937,16061
BMRB,7326,Chemical shifts of En-1 at 25 C,40958,16062
PDB,2KC6,BMRB Entry Tracking System,40958,16062
PDB,2nsv,Structure of En-1 at 25 C,40958,16062
PDB,2KBX,BMRB Entry Tracking System,40978,16063
PDB,2KC7,BMRB Entry Tracking System,40995,16064
TargetDB,BfR218,Putative uncharacterized protein.,40995,16064
BMRB,16066,RelE,41026,16065
BMRB,16067,RelBc,41026,16065
PDB,2KC8,BMRB Entry Tracking System,41026,16065
BMRB,16065,RelE:RelBc complex,41053,16066
BMRB,16067,RelBc,41053,16066
PDB,2KC9,BMRB Entry Tracking System,41053,16066
BMRB,16065,RelE:RelBc complex,41076,16067
BMRB,16066,RelE,41076,16067
PDB,2KCA,BMRB Entry Tracking System,41092,16068
PDB,3CNR,Crystal structure for the protein that is used in this study,41112,16069
PDB,2kbu,variant of pin1 WW domain with beta turn mimic,41130,16070
BMRB,16075,mPrP90 (P102L),41151,16071
BMRB,16076,mPrP90 (M129V),41151,16071
BMRB,16077,mPrP90 (P105L),41151,16071
BMRB,16078,mPrP90 (A117V),41151,16071
BMRB,16079,mPrP90 (3AV),41151,16071
BMRB,16080,mPrP90 (2II),41151,16071
PDB,2KCD,BMRB Entry Tracking System,41165,16072
PDB,2KCG,BMRB Entry Tracking System,41195,16073
PDB,2KCH,BMRB Entry Tracking System,41209,16074
BMRB,16071,mPrP90,41223,16075
BMRB,16076,mPrP90 (P102L),41223,16075
BMRB,16077,mPrP90 (P105L),41223,16075
BMRB,16078,mPrP90 (A117V),41223,16075
BMRB,16079,mPrP90 (3AV),41223,16075
BMRB,16080,mPrP90 (2II),41223,16075
BMRB,16071,mPrP90,41237,16076
BMRB,16075,mPrP90 (M129V),41237,16076
BMRB,16077,mPrP90 (P105L),41237,16076
BMRB,16078,mPrP90 (A117V),41237,16076
BMRB,16079,mPrP90 (3AV),41237,16076
BMRB,16080,mPrP90 (2II),41237,16076
BMRB,16071,mPrP90,41251,16077
BMRB,16075,mPrP90 (M129V),41251,16077
BMRB,16076,mPrP90 (P102L),41251,16077
BMRB,16078,mPrP90 (A117V),41251,16077
BMRB,16079,mPrP90 (3AV),41251,16077
BMRB,16080,mPrP90 (2II),41251,16077
PDB,2JPO,BMRB Entry Tracking System,41251,16077
BMRB,16071,mPrP90,41265,16078
BMRB,16075,mPrP90 (M129V),41265,16078
BMRB,16076,mPrP90 (P102L),41265,16078
BMRB,16077,mPrP90 (P105L),41265,16078
BMRB,16079,mPrP90 (3AV),41265,16078
BMRB,16080,mPrP90 (2II),41265,16078
BMRB,16071,mPrP90,41279,16079
BMRB,16075,mPrP90 (M129V),41279,16079
BMRB,16076,mPrP90 (P102L),41279,16079
BMRB,16077,mPrP90 (P105L),41279,16079
BMRB,16078,mPrP90 (A117V),41279,16079
BMRB,16080,mPrP90 (2II),41279,16079
BMRB,16071,mPrP90,41293,16080
BMRB,16075,mPrP90 (M129V),41293,16080
BMRB,16076,mPrP90 (P102L),41293,16080
BMRB,16077,mPrP90 (P105L),41293,16080
BMRB,16078,mPrP90 (A117V),41293,16080
BMRB,16079,mPrP90 (3AV),41293,16080
PDB,2KCJ,BMRB Entry Tracking System,41307,16082
PDB,2KCK,BMRB Entry Tracking System,41322,16083
PDB,2KCL,BMRB Entry Tracking System,41345,16084
PDB,2KCN,BMRB Entry Tracking System,41383,16087
PDB,2kbu,variant of pin1 WW domain with beta turn mimic,41398,16088
PDB,2KCO,BMRB Entry Tracking System,41419,16089
PDB,1aa0,X-Ray Structure of Bacterionphage T4 Fibritin,41442,16090
PDB,1RFO,Solution Structure of Trimeric Foldon Domain from Bacteriophage T4 Fibritin,41442,16090
PDB,1U0P,"Solution Structrue of the Monomeric A-state Form of Foldon, the Trimerization Domain from Bacteriophage T4 Fibritin",41442,16090
PDB,2KBL,BMRB Entry Tracking System,41442,16090
PDB,2KCP,BMRB Entry Tracking System,41461,16091
PDB,2KCQ,BMRB Entry Tracking System,41487,16093
PDB,2KCR,BMRB Entry Tracking System,41510,16094
BMRB,18380,dvCcmE'(44-128),41527,16096
PDB,2KCT,BMRB Entry Tracking System,41527,16096
PDB,2KCU,BMRB Entry Tracking System,41559,16097
PDB,3E0H,,41559,16097
PDB,2KCW,BMRB Entry Tracking System,41586,16098
PDB,2KCX,BMRB Entry Tracking System,41604,16099
PDB,2KCZ,BMRB Entry Tracking System,41646,16100
PDB,2KD0,BMRB Entry Tracking System,41673,16101
PDB,2KD1,BMRB Entry Tracking System,41695,16102
PDB,2KD2,BMRB Entry Tracking System,41726,16103
PDB,2KD7,BMRB Entry Tracking System,41781,16107
TargetDB,BtR324B,,41781,16107
PDB,2KDB,BMRB Entry Tracking System,41828,16109
PDB,2KDD,BMRB Entry Tracking System,41853,16110
PDB,2KPY,BMRB Entry Tracking System,41877,16111
PDB,2k44,Solution structure of a K+-channel voltage-sensor paddle domain,41894,16112
PDB,2HFI,NMR structure,41908,16113
PDB,2KDI,BMRB Entry Tracking System,41927,16114
BMRB,15535,Ga88,41966,16116
BMRB,15537,Gb88,41966,16116
BMRB,16117,Gb95,41966,16116
BMRB,6945,GaWT,41966,16116
BMRB,7280,GbWT,41966,16116
PDB,2KDL,BMRB Entry Tracking System,41966,16116
BMRB,15535,Ga88,41983,16117
BMRB,15537,Gb88,41983,16117
BMRB,16116,Ga95,41983,16117
BMRB,6945,GaWT,41983,16117
BMRB,7280,GbWT,41983,16117
PDB,2KDM,BMRB Entry Tracking System,41983,16117
PDB,2KDN,BMRB Entry Tracking System,42000,16118
PDB,2KDO,BMRB Entry Tracking System,42021,16119
PDB,2JXF,The solution structure of HCV NS4B(40-69),42084,16122
PDB,2KDR,BMRB Entry Tracking System,42084,16122
BMRB,16125,RppH mutant E53A,42112,16124
PDB,2KDX,BMRB Entry Tracking System,42130,16126
PDB,2KDP,BMRB Entry Tracking System,42147,16127
PDB,2KE4,BMRB Entry Tracking System,42170,16129
BMRB,16131,Tdom40-76,42190,16130
BMRB,16133,TolAIII,42190,16130
BMRB,16134,TolAIII+tdom,42190,16130
BMRB,16130,Tdom 40-76 TolAIII complex,42206,16131
BMRB,16133,TolAIII,42206,16131
BMRB,16134,TolAIII+tdom,42206,16131
BMRB,16130,Tdom 40-76 TolAIII complex,42221,16133
BMRB,16131,Tdom40-76,42221,16133
BMRB,16134,TolAIII+tdom,42221,16133
BMRB,16130,Tdom 40-76 TolAIII complex,42236,16134
BMRB,16131,Tdom40-76,42236,16134
BMRB,16133,TolAIII,42236,16134
PDB,2KMT,BMRB Entry Tracking System,42252,16135
PDB,2W9O,BMRB Entry Tracking System,42269,16136
PDB,2KE7,BMRB Entry Tracking System,42286,16137
BMRB,15860,"NMR data related to NMR solutions structure of modified DNA containing imidazole nucleosides at acidic, neutral and basic pH",42302,16138
PDB,2K67,NMR solutions structure of modified DNA containing imidazole nucleosides at acidic  pH,42302,16138
PDB,2K68,NMR solutions structure of modified DNA containing imidazole nucleosides at neutral pH,42302,16138
PDB,2K69,NMR solutions structure of modified DNA containing imidazole nucleosides at basic pH,42302,16138
PDB,2KE8,NMR solution structure of metal-modified DNA,42302,16138
PDB,2M54,BMRB Entry Tracking System,42302,16138
PDB,2KE9,BMRB Entry Tracking System,42325,16139
PDB,2KEA,BMRB Entry Tracking System,42358,16141
BMRB,16143,Structure of SDF-1/CXCL12,42374,16142
BMRB,16145,Structure of SDF-1/CXCL12,42374,16142
PDB,2KEC,BMRB Entry Tracking System,42374,16142
BMRB,16142,Structure of SDF-1/CXCL12,42393,16143
BMRB,16145,Structure of SDF-1/CXCL12,42393,16143
PDB,2KED,BMRB Entry Tracking System,42393,16143
BMRB,16142,Structure of SDF-1/CXCL12,42431,16145
BMRB,16143,Structure of SDF-1/CXCL12,42431,16145
PDB,2KEE,BMRB Entry Tracking System,42431,16145
BMRB,16149,Plantaricin K in TFE,42484,16148
BMRB,16239,Plantaricin J in DPC-micelles,42484,16148
BMRB,16241,Plantaricin J in TFE,42484,16148
PDB,2KEG,BMRB Entry Tracking System,42484,16148
BMRB,16148,Plantaricin K in DPC-micelles,42503,16149
BMRB,16239,Plantaricin J in DPC-micelles,42503,16149
BMRB,16241,Plantaricin J in TFE,42503,16149
PDB,2KEH,BMRB Entry Tracking System,42503,16149
BMRB,16136,NMR data of wild type jerdostatin,42522,16150
PDB,2W9U,BMRB Entry Tracking System,42522,16150
PDB,2w9o,Coordinates of wild type jerdostatin,42522,16150
PDB,2w9v,Coordinates of jerdostatin with deletion of residues N45G46,42522,16150
PDB,2w9w,Coordinates of jerdostatin mutant R24K with deletion of residues N45G46,42522,16150
BMRB,16136,NMR data of wild type jerdostatin,42539,16151
PDB,2W9V,BMRB Entry Tracking System,42539,16151
PDB,2w9o,Coordinates of wild type jerdostatin,42539,16151
PDB,2w9u,Coordinates of jerdostatin mutant R24K,42539,16151
PDB,2w9w,Coordinates of jerdostatin mutant R24K with deletion of residues N45G46,42539,16151
BMRB,16136,NMR data of wild type jerdostatin,42556,16152
PDB,2w9o,Coordinates of wild type jerdostatin,42556,16152
PDB,2w9u,Coordinates of jerdostatin mutant R24K,42556,16152
PDB,2w9v,Coordinates of wild type jerdostatin with deletion of residues N45G46,42556,16152
PDB,2W9W,BMRB Entry Tracking System,42556,16152
PDB,2KEL,BMRB Entry Tracking System,42573,16153
PDB,2kbn,NMR structure refined without RDC constraints,42598,16154
PDB,2KEN,BMRB Entry Tracking System,42598,16154
PDB,2KEO,BMRB Entry Tracking System,42626,16155
PDB,2KES,BMRB Entry Tracking System,42648,16156
PDB,2KER,BMRB Entry Tracking System,42667,16157
BMRB,15552,Assigments of cytoplasmic tail of the human beta3 integrin,42691,16158
BMRB,16159,Beta-1D,42691,16158
BMRB,16162,Beta-1A-His6,42691,16158
BMRB,15552,Assigments of cytoplasmic tail of the human beta3 integrin,42708,16159
BMRB,16158,Beta-1A,42708,16159
BMRB,16162,Beta-1A-His6,42708,16159
PDB,2KEY,BMRB Entry Tracking System,42758,16161
BMRB,15552,Assigments of cytoplasmic tail of the human beta3 integrin,42785,16162
BMRB,16158,Beta-1A,42785,16162
BMRB,16159,Beta-1D,42785,16162
PDB,2KEP,BMRB Entry Tracking System,42826,16164
,AB047639,"GENBANK Hepatitis C virus (isolate JFH-1) genomic RNA, complete genome.",42854,16165
,Q99IB8,SWISS-PROT POLG_HCVJF,42854,16165
BMRB,16168,"STRUCTURE OF THE NA,K-ATPASE REGULATORY PROTEIN FXYD1 IN MICELLES",42884,16167
PDB,2JP3,Solution Structure of the human FXYD4 (CHIF) protein in SDS micelles,42884,16167
BMRB,16167,NMR data for FXYD4 in micelles,42900,16168
PDB,2JO1,BMRB Entry Tracking System,42900,16168
PDB,2JP3,Solution Structure of the human FXYD4 (CHIF) protein in SDS micelles,42900,16168
BMRB,16170,Barnase high pressure structure,42918,16169
BMRB,16171,"Barnase bound to d(CGAC), low pressure",42918,16169
BMRB,16172,"Barnase bound to d(CGAC), high pressure",42918,16169
PDB,1a2p,wild type barnase,42918,16169
BMRB,16169,Barnase low pressure reference,42932,16170
BMRB,16171,"Barnase bound to d(CGAC), low pressure",42932,16170
BMRB,16172,"Barnase bound to d(CGAC), high pressure",42932,16170
PDB,1a2p,wild type barnase,42932,16170
PDB,2kf3,low pressure structure,42932,16170
PDB,2KF4,BMRB Entry Tracking System,42932,16170
BMRB,16169,Barnase low pressure reference,42946,16171
BMRB,16170,Barnase high pressure structure,42946,16171
BMRB,16172,Barnase bound to d(CGAC) high pressure,42946,16171
PDB,1a2p,wild type barnase,42946,16171
PDB,2KF5,BMRB Entry Tracking System,42946,16171
BMRB,16169,Barnase low pressure reference,42960,16172
BMRB,16170,Barnase high pressure structure,42960,16172
BMRB,16171,"Barnase bound to d(CGAC), low pressure",42960,16172
PDB,1a2p,wild type barnase,42960,16172
PDB,2kf5,low pressure structure,42960,16172
PDB,2KF6,BMRB Entry Tracking System,42960,16172
PDB,2KFB,BMRB Entry Tracking System,42974,16173
PDB,2KFD,BMRB Entry Tracking System,43032,16176
BMRB,17069,Backbone dynamics of E73 from SSV-RH,43052,16177
PDB,2KFE,BMRB Entry Tracking System,43069,16178
PDB,2OJM,Solution structure and cell selectivity of Piscidin 1 and its analogues,43069,16178
BMRB,16180,C-terminal domain of EHD1 in complex with FNYESTNPFTAK,43086,16179
BMRB,16181,C-terminal domain of EHD1 in complex with FNYESTGPFTAK,43086,16179
PDB,2KFF,BMRB Entry Tracking System,43086,16179
BMRB,16179,C-terminal domain of EHD1 in complex with FNYESTNPFTAK,43107,16180
BMRB,16181,C-terminal domain of EHD1 in complex with FNYESTGPFTAK,43107,16180
PDB,2KFG,BMRB Entry Tracking System,43107,16180
BMRB,16179,C-terminal domain of EHD1 in complex with FNYESTNPFTAK,43128,16181
BMRB,16180,C-terminal domain of EHD1 in complex with FNYESTNPFTAK,43128,16181
PDB,2KFH,BMRB Entry Tracking System,43128,16181
PDB,2KFL,BMRB Entry Tracking System,43164,16183
PDB,2KFM,BMRB Entry Tracking System,43186,16184
PDB,2KFO,BMRB Entry Tracking System,43208,16185
PDB,2KFQ,BMRB Entry Tracking System,43279,16187
PDB,2KFS,BMRB Entry Tracking System,43295,16188
PDB,2KFV,BMRB Entry Tracking System,43315,16189
PDB,2KFX,BMRB Entry Tracking System,43333,16190
PDB,2KLE,BMRB Entry Tracking System,43356,16191
BMRB,6745,"Backbone 1H, 13C, and 15N chemical shift assignments of human HnRNP F qRRM12",43373,16192
PDB,2HGL,NMR structure of the first qRRM domain of human hnRNP F,43373,16192
PDB,2brz,fruit brazzein,43798,16215
BMRB,6745,"Backbone 1H, 13C, and 15N chemical shift assignments of human HnRNP F qRRM12",43391,16193
PDB,2HGM,NMR structure of the second qRRM domain of human hnRNP F,43391,16193
PDB,2KG0,BMRB Entry Tracking System,43391,16193
PDB,2HGN,NMR structure of the third qRRM domain of human hnRNP F,43411,16194
PDB,2KG1,BMRB Entry Tracking System,43411,16194
PDB,2LG1,BMRB Entry Tracking System,43431,16195
BMRB,16197,NMR Solution Structures of malonyl ACP from the actinorhodin polyketide synthase in Streptomyces coelicolor,43447,16196
BMRB,16199,"NMR Solution Structures of butyryl-ACP (a non-polar, non pathway intermediate) from Streptomyces coelicolor",43447,16196
BMRB,16200,NMR Solution Structures of hexanoyl ACP (a non natural intermediate) from Streptomyces coelicolor,43447,16196
BMRB,16201,NMR Solution Structures of octanoyl ACP (a non-natural intermediate) from Streptomyces coelicolor,43447,16196
BMRB,16202,"NMR Solution Structures of 3-oxo-butyl-ACP, an intermediate mimic from Streptomyces coelicolor",43447,16196
BMRB,16203,"NMR Solution Structures of 3,5-dioxohexyl ACP (a triketide mimic) from Streptomyces coelicolor",43447,16196
PDB,2k0x,Solution Structure of the holo Acyl Carrier Protein from the Actinorhodin polyketide pathway in Streptomyces coelicolor,43447,16196
PDB,2k0y,Solution Structure of the apo Acyl Carrier Protein from the Actinorhodin polyketide pathway in Streptomyces coelicolor,43447,16196
PDB,2KG6,BMRB Entry Tracking System,43447,16196
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43465,16197
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43465,16197
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43465,16197
BMRB,16199,"NMR Solution Structures of butyryl-ACP (a non-polar, non pathway intermediate) from Streptomyces coelicolor",43465,16197
BMRB,16200,NMR Solution Structures of hexanoyl ACP (a non natural intermediate) from Streptomyces coelicolor,43465,16197
BMRB,16201,NMR Solution Structures of octanoyl ACP (a non-natural intermediate) from Streptomyces coelicolor,43465,16197
BMRB,16202,"NMR Solution Structures of 3-oxo-butyl-ACP, an intermediate mimic from Streptomyces coelicolor",43465,16197
BMRB,16203,"NMR Solution Structures of 3,5-dioxohexyl ACP (a triketide mimic) from Streptomyces coelicolor",43465,16197
PDB,2k0x,NMR Solution structures of holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor,43465,16197
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43465,16197
PDB,2kg6,NMR Solution structures of acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor,43465,16197
PDB,2KG8,BMRB Entry Tracking System,43465,16197
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,16197,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,16200,NMR Solution Structures of hexanoyl ACP (a non natural intermediate) from the actinorhodin polyketide synthase in Streptomyces coelicolor,43497,16199
BMRB,16201,"1H, 13C and 15N NMR assignments for octanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,16202,"1H, 13C and 15N NMR assignments for 3-xoxbutyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43497,16199
BMRB,16203,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),43497,16199
PDB,2k0x,NMR Solutions structure of holo ACP from the actinorhodin pathway of Streptomyces coelicolor,43497,16199
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43497,16199
PDB,2kg6,NMR Solutions structure of acetyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43497,16199
PDB,2kg8,NMR Solutions structure of malonyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43497,16199
PDB,2KG9,BMRB Entry Tracking System,43497,16199
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43541,16200
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43541,16200
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43541,16200
BMRB,16197,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43541,16200
BMRB,16199,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43541,16200
BMRB,16201,NMR Solution Structures of octanoyl ACP (a non-natural intermediate) from the actinorhodin polyketide synthase in Streptomyces coelicolor,43541,16200
BMRB,16202,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),43541,16200
BMRB,16203,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),43541,16200
PDB,2k0x,NMR Solutions structure of holo ACP from the actinorhodin pathway of Streptomyces coelicolor,43541,16200
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43541,16200
PDB,2kg6,NMR Solutions structure of acetyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43541,16200
PDB,2kg8,NMR Solutions structure of malonyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43541,16200
PDB,2kg9,NMR Solutions structure of butyryl ACP from the actinorhodin pathway of Streptomyces coelicolor,43541,16200
PDB,2KGA,BMRB Entry Tracking System,43541,16200
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,16197,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,16199,"1H, 13C and 15N NMR assignments for butyryl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,16200,"1H, 13C and 15N NMR assignments for hexanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43559,16201
BMRB,16202,NMR Solution Structures of 3-oxo-butyl-ACP  from the actinorhodin polyketide synthase in Streptomyces coelicolor,43559,16201
BMRB,16203,NMR Solution Structures of 3-oxo-butyl-ACP from the actinorhodin polyketide synthase in Streptomyces coelicolor,43559,16201
PDB,2k0x,NMR Solutions structure of holo ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
PDB,2kg6,NMR Solutions structure of acetyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
PDB,2kg8,NMR Solutions structure of malonyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
PDB,2kg9,NMR Solutions structure of butyryl ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
PDB,2kga,NMR Solutions structure of hexanoyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43559,16201
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16197,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16199,"1H, 13C and 15N NMR assignments for butyryl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16200,"1H, 13C and 15N NMR assignments for hexanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16201,"1H, 13C and 15N NMR assignments for octanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43577,16202
BMRB,16203,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),43577,16202
PDB,2k0x,NMR Solutions structure of holo ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2kg6,NMR Solutions structure of acetyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2kg8,NMR Solutions structure of malonyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2kg9,NMR Solutions structure of butyryl ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2kga,NMR Solutions structure of hexanoyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2kgc,NMR Solutions structure of octanoyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43577,16202
PDB,2KGD,BMRB Entry Tracking System,43577,16202
BMRB,15658,"1H, 13C and 15N NMR assignments for holo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,15659,"1H, 13C and 15N NMR assignments for apo ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16196,"1H, 13C and 15N NMR assignments for acetyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16197,"1H, 13C and 15N NMR assignments for malonyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16199,"1H, 13C and 15N NMR assignments for butyryl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16200,"1H, 13C and 15N NMR assignments for hexanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16201,"1H, 13C and 15N NMR assignments for octanoyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
BMRB,16202,"1H, 13C and 15N NMR assignments for 3-xoxbutyl ACP from the actinorhodin polyketide synthase of Streptomyces coelicolor",43595,16203
PDB,2k0x,NMR Solutions structure of holo ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2k0y,NMR Solutions structure of apo ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kg6,NMR Solutions structure of acetyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kg8,NMR Solutions structure of malonyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kg9,NMR Solutions structure of butyryl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kga,NMR Solutions structure of hexanoyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kgc,NMR Solutions structure of octanoyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2kgd,NMR Solutions structure of 3-oxobutyl ACP from the actinorhodin pathway of Streptomyces coelicolor,43595,16203
PDB,2wbr,,43642,16206
BMRB,16208,NmerA holo form (complex with Mercury ion),43658,16207
PDB,2KT2,BMRB Entry Tracking System,43658,16207
BMRB,16207,NmerA apo form,43672,16208
PDB,2KT3,BMRB Entry Tracking System,43672,16208
BMRB,16210,JARID1A C-terminal PHD finger in complex with H3(1-9)K4me3,43688,16209
PDB,2KGG,BMRB Entry Tracking System,43688,16209
PDB,2KGI,BMRB Entry Tracking System,43706,16210
PDB,2KGJ,BMRB Entry Tracking System,43727,16211
PDB,2K8Z,BMRB Entry Tracking System,43741,16212
BMRB,7248,Conseverd region of Mesd,43758,16213
PDB,2KGO,BMRB Entry Tracking System,43772,16214
PDB,1brz,fruit brazzein,43798,16215
PDB,2LY5,BMRB Entry Tracking System,43798,16215
BMRB,16218,apoMb(1-119) fragment,43844,16217
BMRB,16217,apoMb(1-119) fragment in the presence of DnaK-beta,43860,16218
PDB,2KGT,BMRB Entry Tracking System,43877,16219
BMRB,16223,5'-D(*DCP*DTP*(FAG)P*DA)-3',43917,16222
PDB,2KH3,BMRB Entry Tracking System,43917,16222
BMRB,16222,5'-D(*DCP*DTP*DAP*DTP*(FAG)P*DAP*DTP*DTP*DCP*DA)-3',43940,16223
PDB,2KH4,BMRB Entry Tracking System,43940,16223
BMRB,16222,FAG mutant in chain 1 of 10 residue DNA,43961,16225
BMRB,16223,FAG mutant in single chain of 4 residue DNA,43961,16225
BMRB,16226,TG mutant at 6 in chain 1 of 12 residue DNA,43961,16225
PDB,2KH6,BMRB Entry Tracking System,43961,16225
PDB,2KH7,BMRB Entry Tracking System,43986,16226
PDB,2KH8,BMRB Entry Tracking System,43986,16226
BMRB,7070,RRMs 1 and 2 of Prp24 from S. cerevisiae,44046,16230
PDB,2KH9,BMRB Entry Tracking System,44046,16230
PDB,2KHA,BMRB Entry Tracking System,44076,16231
PDB,2LBO,BMRB Entry Tracking System,44090,16233
PDB,1NB1,macrocyclic parent,44123,16235
PDB,2KHB,BMRB Entry Tracking System,44123,16235
PDB,2KHC,BMRB Entry Tracking System,44137,16236
PDB,2KGS,BMRB Entry Tracking System,44151,16237
PDB,2KHD,BMRB Entry Tracking System,44173,16238
BMRB,16148,Plantaricin K in DPC-micelles,44200,16239
BMRB,16149,Plantaricin K in TFE,44200,16239
BMRB,16241,Plantaricin J in TFE,44200,16239
PDB,2KHF,BMRB Entry Tracking System,44200,16239
PDB,2KFW,BMRB Entry Tracking System,44234,16240
BMRB,16148,Plantaricin K in DPC-micelles,44255,16241
BMRB,16149,Plantaricin K in TFE,44255,16241
BMRB,16239,Plantaricin J in DPC-micelles,44255,16241
PDB,2KHG,BMRB Entry Tracking System,44255,16241
BMRB,16230,Prp24-RRM2 bound to AGAGAU from U6 snRNA,44275,16243
BMRB,7070,PRP24 (RRM 1 and 2),44275,16243
PDB,2KH9,BMRB Entry Tracking System,44275,16243
BMRB,16230,Prp24-RRM2 bound to AGAGAU from U6 snRNA,44292,16244
BMRB,7070,PRP24 (RRM 1 and 2),44292,16244
PDB,2KH9,BMRB Entry Tracking System,44292,16244
BMRB,7070,RRMs 1 and 2 of Prp24 from S. cerevisiae,44328,16246
PDB,2KH9,BMRB Entry Tracking System,44328,16246
PDB,2KHK,BMRB Entry Tracking System,44345,16247
PDB,2KFU,BMRB Entry Tracking System,44362,16248
BMRB,17131,NMR Assignment of the N-terminal domain of Araneus diadematus spider silk protein,44379,16249
PDB,2KHM,BMRB Entry Tracking System,44379,16249
PDB,2KHN,BMRB Entry Tracking System,44403,16250
PDB,2KHQ,BMRB Entry Tracking System,44430,16251
TargetDB,SyR103B,,44430,16251
PDB,2L7Z,BMRB Entry Tracking System,44458,16252
PDB,2KHR,BMRB Entry Tracking System,44472,16253
PDB,2KHT,BMRB Entry Tracking System,44493,16254
PDB,2KHV,BMRB Entry Tracking System,44512,16255
PDB,2KHX,BMRB Entry Tracking System,44537,16256
PDB,2KHZ,BMRB Entry Tracking System,44568,16258
BMRB,15552,Assigments of related molecules.,44592,16259
BMRB,16158,Assigments of related molecules.,44592,16259
BMRB,16159,Assigments of related molecules.,44592,16259
BMRB,16162,Assigments of related molecules.,44592,16259
PDB,2KI3,BMRB Entry Tracking System,44613,16260
PDB,2KM6,BMRB Entry Tracking System,44663,16263
PDB,2KHP,BMRB Entry Tracking System,44680,16264
BMRB,15264,Assignments for the reduced form of the N-terminal domain of AhpF,44701,16265
PDB,1HYU,,44701,16265
PDB,1ZYN,,44701,16265
PDB,1ZYP,,44701,16265
TargetDB,AtT7,,44744,16267
PDB,2KI9,BMRB Entry Tracking System,44779,16268
PDB,2KIC,BMRB Entry Tracking System,44795,16269
PDB,1ija,apo-SrtA,44810,16270
PDB,1t2p,apo-SrtA,44810,16270
PDB,2KID,BMRB Entry Tracking System,44810,16270
PDB,2KIE,BMRB Entry Tracking System,44840,16271
PDB,2KIF,BMRB Entry Tracking System,44857,16272
PDB,2KIG,BMRB Entry Tracking System,44886,16273
BMRB,20029,Apelin17-35C,44917,16275
BMRB,20030,Apelin17_5C confA,44917,16275
BMRB,20031,Apelin17_5C confB,44917,16275
BMRB,20082,Apelin17 bound to SDS micelles,44917,16275
BMRB,16278,NMR structure of the H103G mutant SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state,44939,16276
PDB,2KII,BMRB Entry Tracking System,44939,16276
PDB,2KIJ,BMRB Entry Tracking System,44962,16277
BMRB,16276,SO2144 H-NOX domain in the Fe(II)CO ligation state,44984,16278
PDB,2kii,,44984,16278
PDB,2KIL,BMRB Entry Tracking System,44984,16278
BMRB,16280,free DNA,45040,16281
BMRB,16280,shorter oligo,45057,16282
PDB,2KIM,BMRB Entry Tracking System,45072,16283
PDB,2kif,,45072,16283
BMRB,16295,"reduced yeast TOR1 FATC domain bound to DPC micelles, 298K",45099,16284
BMRB,6228,"oxidized yeast TOR1 FATC domain in solution, 298K",45099,16284
PDB,1w1n,"oxidized yeast TOR1 FATC domain in solution, 298K",45099,16284
PDB,2KIO,BMRB Entry Tracking System,45099,16284
PDB,2kit,"reduced yeast TOR1 FATC domain bound to DPC micelles, 298K",45099,16284
PDB,2KG2,BMRB Entry Tracking System,45122,16285
BMRB,16280,shorter oligo,45137,16286
BMRB,16282,free oligo,45152,16287
BMRB,16286,free oligo,45169,16288
BMRB,16282,same study,45186,16289
BMRB,16289,free oligo,45201,16290
BMRB,16282,free oligo,45218,16291
BMRB,16292,d(CGAGCTCG)2 plus Ru ligand 1:2 assignments,45218,16291
BMRB,16291,"similar oligo, same ligand",45235,16292
PDB,2KIS,BMRB Entry Tracking System,45252,16293
PDB,2ALG,entry containing coordinates for peach Pru p 3,45268,16294
BMRB,16284,"oxidized yeast TOR1 FATC domain bound to DPC micelles, 318K",45287,16295
BMRB,6228,"oxidized yeast TOR1 FATC domain in solution, 298K",45287,16295
PDB,1w1n,"oxidized yeast TOR1 FATC domain in solution, 298K",45287,16295
PDB,2kio,"oxidized yeast TOR1 FATC domain bound to DPC micelles, 318K",45287,16295
PDB,2KIT,BMRB Entry Tracking System,45287,16295
PDB,2KIV,BMRB Entry Tracking System,45324,16297
PDB,2KIW,BMRB Entry Tracking System,45339,16298
BMRB,16301,free SaS,45384,16300
BMRB,16302,aS-SLAS,45384,16300
BMRB,16303,SaS-SLAS,45384,16300
BMRB,16304,bS-SLAS,45384,16300
BMRB,16342,aSyn-pH3,45384,16300
BMRB,16547,aSyn E46K-pH6,45384,16300
BMRB,16904,aSyn,45384,16300
BMRB,6968,aSyn-protonless,45384,16300
BMRB,7244,gSyn,45384,16300
BMRB,16300,free aS,45398,16301
BMRB,16302,aS-SLAS,45398,16301
BMRB,16303,SaS-SLAS,45398,16301
BMRB,16304,bS-SLAS,45398,16301
BMRB,16300,free aS,45412,16302
BMRB,16301,free SaS,45412,16302
BMRB,16303,SaS-SLAS,45412,16302
BMRB,16304,bS-SLAS,45412,16302
PDB,2KKW,structure,45412,16302
BMRB,16300,free aS,45426,16303
BMRB,16301,free SaS,45426,16303
BMRB,16302,aS-SLAS,45426,16303
BMRB,16304,bS-SLAS,45426,16303
BMRB,16300,free aS,45440,16304
BMRB,16301,free SaS,45440,16304
BMRB,16302,aS-SLAS,45440,16304
BMRB,16303,SaS-SLAS,45440,16304
BMRB,16307,in complex with HEM,45471,16306
PDB,2KSC,BMRB Entry Tracking System,45471,16306
BMRB,16306,in complex with HEME B/C,45502,16307
BMRB,16310,apo cL-BABP T91C,45537,16309
PDB,2KJ4,BMRB Entry Tracking System,45569,16311
PDB,2KJ5,BMRB Entry Tracking System,45587,16312
PDB,2KJ8,BMRB Entry Tracking System,45657,16315
PDB,2KJ9,BMRB Entry Tracking System,45678,16316
PDB,2KLL,BMRB Entry Tracking System,45699,16317
PDB,2KJE,BMRB Entry Tracking System,45723,16318
PDB,2KJF,BMRB Entry Tracking System,45744,16319
PDB,2KJG,BMRB Entry Tracking System,45772,16320
PDB,2KJH,BMRB Entry Tracking System,45789,16321
BMRB,7433,Extracellular CD147 Isoform-3,45806,16322
PDB,2KJK,BMRB Entry Tracking System,45842,16325
PDB,2joh,,45880,16328
BMRB,16330,"SaDsbA Oxidoreductase, Reduced Form",45894,16329
BMRB,16329,"SaDsbA Oxidoreductase, Oxidised Form",45923,16330
BMRB,16333,At condition of pH 6.8,45938,16332
PDB,2KJN,BMRB Entry Tracking System,45938,16332
BMRB,16332,lah4 in a pH of 4.3,45952,16333
PDB,2KJP,BMRB Entry Tracking System,45980,16335
PDB,2KJR,BMRB Entry Tracking System,46038,16338
PDB,2KJL,BMRB Entry Tracking System,46065,16339
BMRB,247,proton assignment of wild type,46098,16340
PDB,1B1G,NMR structure ensemble,46098,16340
PDB,4ICB,X-Ray crystal structure,46098,16340
BMRB,16300,aSyn,46132,16342
BMRB,16547,aSyn E46K-pH6,46132,16342
BMRB,16904,alpha-synuclei,46132,16342
BMRB,5744,Broken Alpha-helix in Folded Alpha-synuclein,46132,16342
BMRB,6968,NOE's of unfolded alpha-synuclein,46132,16342
BMRB,7244,gSyn,46132,16342
BMRB,16324,Dynamics of Insulin,46152,16343
BMRB,16345,Solution structure of the permutant S6p3.,46171,16344
PDB,1RIS,Crystal structure of S6.,46171,16344
PDB,2KJV,BMRB Entry Tracking System,46171,16344
PDB,2KJW,Solution structure of the permutant S6p3.,46171,16344
BMRB,16344,Solution structure of parent protein S6.,46194,16345
PDB,1RIS,Crystal structure of parent protein S6.,46194,16345
PDB,2kjv,Solution structure of parent protein S6.,46194,16345
PDB,2KJW,BMRB Entry Tracking System,46194,16345
PDB,2KJZ,BMRB Entry Tracking System,46218,16347
PDB,2KK0,BMRB Entry Tracking System,46241,16348
PDB,2KK1,BMRB Entry Tracking System,46266,16349
PDB,2jms,En-6 structure,46303,16350
PDB,2kc6,En-1 structure at -1.5 C,46303,16350
PDB,2KK2,BMRB Entry Tracking System,46303,16350
PDB,2nsv,En-1 structure,46303,16350
PDB,2nsw,En-2 structure,46303,16350
PDB,2KK4,BMRB Entry Tracking System,46322,16352
PDB,2KK6,BMRB Entry Tracking System,46346,16353
PDB,2KK7,BMRB Entry Tracking System,46373,16354
PDB,2KK8,BMRB Entry Tracking System,46390,16355
PDB,2KKA,BMRB Entry Tracking System,46425,16356
PDB,2KKE,BMRB Entry Tracking System,46440,16357
PDB,2KKC,BMRB Entry Tracking System,46519,16361
BMRB,15927,"1H, 13C and 15N NMR resonance assignments of the actinoporin Sticholysin I",46534,16362
BMRB,16630,"1H, 13C and 15N NMR assignments of StnII-Y111N, a mutant of the sea anemone actinoporin Sticholysin II",46534,16362
PDB,1JJS,another ligand free structure,46550,16363
PDB,1KBH,ligand bound structure,46550,16363
PDB,1zoq,ligand bound structure,46550,16363
PDB,2c52,ligand bound structure,46550,16363
PDB,2KKJ,BMRB Entry Tracking System,46550,16363
PDB,2KKL,BMRB Entry Tracking System,46565,16364
PDB,2KKM,BMRB Entry Tracking System,46595,16365
PDB,2KKN,BMRB Entry Tracking System,46616,16366
PDB,2KKQ,BMRB Entry Tracking System,46687,16370
PDB,2KKS,BMRB Entry Tracking System,46715,16371
PDB,2KKU,BMRB Entry Tracking System,46740,16372
PDB,2KKV,BMRB Entry Tracking System,46766,16373
BMRB,16375,Solution Structure of C-terminal domain of oxidized NleG2-3,46795,16374
BMRB,16501,(1-153)Apomyoglobin,49389,16500
BMRB,16374,Solution Structure of C-terminal domain of reduced NleG2-3,46822,16375
PDB,2KKZ,BMRB Entry Tracking System,46849,16376
PDB,2KL1,BMRB Entry Tracking System,46908,16378
PDB,1zko,X-ray structure,46961,16380
PDB,2KL2,BMRB Entry Tracking System,46961,16380
PDB,2K4T,BMRB Entry Tracking System,46983,16381
PDB,2KL3,BMRB Entry Tracking System,46997,16382
TargetDB,NsR437A,,46997,16382
PDB,2KL5,BMRB Entry Tracking System,47030,16384
PDB,2KL6,BMRB Entry Tracking System,47054,16385
PDB,2KL7,BMRB Entry Tracking System,47095,16386
PDB,2KL8,BMRB Entry Tracking System,47122,16387
PDB,2KLB,BMRB Entry Tracking System,47154,16388
PDB,2KLA,BMRB Entry Tracking System,47174,16389
PDB,2KLC,BMRB Entry Tracking System,47207,16390
BMRB,6024,Entry containing chemical shift data for this molecular system,47255,16392
BMRB,16394,deltaF508 CFTR NBD1-RE,47283,16393
BMRB,16393,CFTR NBD1-RE,47300,16394
PDB,2KLQ,BMRB Entry Tracking System,47331,16396
PDB,2KKR,BMRB Entry Tracking System,47350,16397
BMRB,16407,w2w11 counterpart,47384,16399
PDB,2KLW,BMRB Entry Tracking System,47413,16400
PDB,2KLX,BMRB Entry Tracking System,47475,16403
BMRB,6711,"1H, 13C, and 15N Chemical Shift Assignments for Human Ubc7",47495,16404
PDB,2KLY,BMRB Entry Tracking System,47495,16404
PDB,2KLZ,BMRB Entry Tracking System,47513,16405
PDB,1FKL,,47531,16406
BMRB,16399,w4w9 counterpart,47550,16407
PDB,2K0Q,"apo-CopK protein, solution structure",47564,16408
PDB,2KM0,BMRB Entry Tracking System,47564,16408
BMRB,7234,"Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-",47587,16409
PDB,1z4n,beta phosphoglucomutase in complex with alpha-galactose 1-phosphate,47587,16409
PDB,1z4o,beta phosphoglucomutase in complex with alpha-galactose 1-phosphate,47587,16409
PDB,2wf5,beta phosphoglucomutase in a ternary complex with glucose 6-phosphate and MgF3-,47587,16409
PDB,2KM4,BMRB Entry Tracking System,47611,16411
PDB,2LJK,BMRB Entry Tracking System,47646,16413
PDB,2KM8,BMRB Entry Tracking System,47884,16425
PDB,2JV3,,47911,16426
PDB,2KMD,BMRB Entry Tracking System,47911,16426
PDB,2KMJ,BMRB Entry Tracking System,47997,16431
BMRB,16436,LDTI - IIa,48028,16435
BMRB,16437,LDTI - IIb,48028,16435
BMRB,16438,LDTI - IIc,48028,16435
BMRB,16435,"LDTI, apo- form",48047,16436
BMRB,16437,LDTI - IIb,48047,16436
BMRB,16438,LDTI - IIc,48047,16436
PDB,2KMO,BMRB Entry Tracking System,48047,16436
BMRB,16435,"LDTI, apo- form",48066,16437
BMRB,16436,LDTI - IIa,48066,16437
BMRB,16438,LDTI - IIc,48066,16437
PDB,2KMP,BMRB Entry Tracking System,48066,16437
BMRB,16435,"LDTI, apo- form",48085,16438
BMRB,16436,LDTI - IIa,48085,16438
BMRB,16437,LDTI - IIb,48085,16438
PDB,2KMP,BMRB Entry Tracking System,48085,16438
PDB,2KMS,BMRB Entry Tracking System,48104,16439
BMRB,16441,ATP-bound N- domain,48125,16440
PDB,2KMV,BMRB Entry Tracking System,48125,16440
BMRB,16440,ATP-free N- domain,48148,16441
PDB,2kmv,ATP-free N- domain,48148,16441
PDB,2KMW,BMRB Entry Tracking System,48173,16442
BMRB,18343,free 10nts ssDNA,48292,16449
PDB,1z00,,48292,16449
PDB,2aq0,,48292,16449
PDB,2KN7,BMRB Entry Tracking System,48292,16449
PDB,2KN8,BMRB Entry Tracking System,48343,16452
BMRB,5159,,48503,16459
PDB,1xke,,48503,16459
BMRB,4257,VPR chemical shift assignments,48552,16461
PDB,1X9V,Dimeric structure of the C-terminal domain of Vpr,48552,16461
PDB,1LVE,"x-ray structure of immunoglobulin light chain, LEN",48589,16463
PDB,2KNE,BMRB Entry Tracking System,48629,16465
PDB,2KNF,BMRB Entry Tracking System,48651,16466
PDB,2KNH,BMRB Entry Tracking System,48665,16467
PDB,1LMM,,48682,16468
BMRB,133,1H chemical-shift assignments for Ribonuclease T1,48700,16469
BMRB,15905,"1J(CA,X) coupling constants in Ribonuclease T1",48700,16469
BMRB,1658,15N chemical-shift assignments for Ribonuclease T1,48700,16469
BMRB,16580,2J coupling constants in Ribonuclease T1 from Aspergillus oryzae,48700,16469
PDB,2KNO,BMRB Entry Tracking System,48776,16472
PDB,2KNR,BMRB Entry Tracking System,48840,16476
PDB,2KNU,BMRB Entry Tracking System,48870,16477
PDB,2KNA,BMRB Entry Tracking System,48888,16478
PDB,2LGP,BMRB Entry Tracking System,48933,16480
PDB,2VY0,,48957,16481
PDB,2KNY,BMRB Entry Tracking System,49007,16483
PDB,2KNZ,BMRB Entry Tracking System,49039,16484
BMRB,15300,NMR assignment of free THAP domain of THAP1,49055,16485
PDB,2JTG,Solution structure of the THAP-zinc finger of THAP1,49055,16485
PDB,2KO0,BMRB Entry Tracking System,49055,16485
PDB,3ibw,X-ray structure,49080,16486
TargetDB,CtR148A,,49080,16486
PDB,2KO6,BMRB Entry Tracking System,49155,16490
PDB,2KO7,BMRB Entry Tracking System,49179,16491
PDB,2KO8,BMRB Entry Tracking System,49204,16492
BMRB,16494,aFGF,49226,16493
BMRB,16493,Entry containing chemical shifts for aFGF in its complex with MIHS,49245,16494
PDB,2KNC,BMRB Entry Tracking System,49276,16496
PDB,2K9J,BMRB Entry Tracking System,49299,16497
PDB,2KOB,BMRB Entry Tracking System,49315,16498
BMRB,16500,(1-119)Apomyoglobin,49362,16499
BMRB,16501,(1-153)Apomyoglobin,49362,16499
BMRB,16499,(1-77)Apomyoglobin,49389,16500
BMRB,16499,(1-77)Apomyoglobin,49403,16501
BMRB,16500,(1-119)Apomyoglobin,49403,16501
BMRB,16493,Entry containing chemical shifts for aFGF in its complex with MIHS,49417,16502
BMRB,16494,Entry containing chemical shifts for free aFGF,49417,16502
PDB,1RML,Coordinates for NMR solution structure of aFGF-NTS complex,49417,16502
PDB,2KOE,BMRB Entry Tracking System,49453,16504
PDB,2KKG,BMRB Entry Tracking System,49469,16505
BMRB,16529,octanoyl-ACP,49488,16506
BMRB,16530,decanoyl-ACP,49488,16506
BMRB,16531,dodecanoyl-ACP,49488,16506
BMRB,16532,tetradecanoyl-ACP,49488,16506
BMRB,16533,hexadecanoyl-ACP,49488,16506
PDB,2KOH,BMRB Entry Tracking System,49505,16507
BMRB,6374,free AIRE-PHD1,49574,16510
PDB,1XWH,free AIRE-PHD1,49574,16510
PDB,2KE1,BMRB Entry Tracking System,49574,16510
BMRB,16522,A Doppel alpha-helix Peptide Fragment,49592,16511
PDB,2KOJ,BMRB Entry Tracking System,49640,16515
TargetDB,BrabA.00007.a,,49675,16517
PDB,3E0U,X-ray structure of T. cruzi GPXI,49695,16518
PDB,2KOL,BMRB Entry Tracking System,49710,16519
PDB,2KOM,BMRB Entry Tracking System,49743,16520
BMRB,16511,A Doppel alpha-helix Peptide Fragment,49793,16522
PDB,1COL,Refined crystallographic structure of the pore-forming domain of colicin A,49813,16523
BMRB,16525,NMR solution structures of 3-hydroxyoctanoyl-ACP with SYO,49831,16524
BMRB,16526,NMR solution structures of 3-hydroxyoctanoyl-ACP with SHO,49831,16524
BMRB,16527,NMR solution structures of 3-hydroxyoctanoyl-ACP with SOD,49831,16524
BMRB,16528,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXO,49831,16524
PDB,2KOO,BMRB Entry Tracking System,49831,16524
PDB,2kop,ACP with other bound intermediate,49831,16524
PDB,2koq,ACP with other bound intermediate,49831,16524
PDB,2kor,ACP with other bound intermediate,49831,16524
PDB,2kos,ACP with other bound intermediate,49831,16524
BMRB,16524,Modified Fatty Acid Synthase Acyl Carrier Protein with SXH,49851,16525
BMRB,16526,Modified Fatty Acid Synthase Acyl Carrier Protein with SHO,49851,16525
BMRB,16527,Modified Fatty Acid Synthase Acyl Carrier Protein with SOD,49851,16525
BMRB,16528,Modified Fatty Acid Synthase Acyl Carrier Protein with SXO,49851,16525
PDB,2koo,ACP with other bound intermediate,49851,16525
PDB,2KOP,BMRB Entry Tracking System,49851,16525
PDB,2koq,ACP with other bound intermediate,49851,16525
PDB,2kor,ACP with other bound intermediate,49851,16525
PDB,2kos,ACP with other bound intermediate,49851,16525
BMRB,16524,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXH,49870,16526
BMRB,16525,NMR solution structures of 3-hydroxyoctanoyl-ACP with SYO,49870,16526
BMRB,16527,NMR solution structures of 3-hydroxyoctanoyl-ACP with SOD,49870,16526
BMRB,16528,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXO,49870,16526
PDB,2koo,ACP with other bound intermediate,49870,16526
PDB,2kop,ACP with other bound intermediate,49870,16526
PDB,2KOQ,BMRB Entry Tracking System,49870,16526
PDB,2kor,ACP with other bound intermediate,49870,16526
PDB,2kos,ACP with other bound intermediate,49870,16526
BMRB,16524,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXH,49891,16527
BMRB,16525,NMR solution structures of 3-hydroxyoctanoyl-ACP with SYO,49891,16527
BMRB,16526,NMR solution structures of 3-hydroxyoctanoyl-ACP with SHO,49891,16527
BMRB,16528,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXO,49891,16527
PDB,2koo,ACP with other bound intermediate,49891,16527
PDB,2kop,ACP with other bound intermediate,49891,16527
PDB,2koq,ACP with other bound intermediate,49891,16527
PDB,2KOR,BMRB Entry Tracking System,49891,16527
PDB,2kos,ACP with other bound intermediate,49891,16527
BMRB,16524,NMR solution structures of 3-hydroxyoctanoyl-ACP with SXH,49910,16528
BMRB,16525,NMR solution structures of 3-hydroxyoctanoyl-ACP with SYO,49910,16528
BMRB,16526,NMR solution structures of 3-hydroxyoctanoyl-ACP with SHO,49910,16528
BMRB,16527,NMR solution structures of 3-hydroxyoctanoyl-ACP with SOD,49910,16528
PDB,2koo,ACP with other bound intermediate,49910,16528
PDB,2kop,ACP with other bound intermediate,49910,16528
PDB,2koq,ACP with other bound intermediate,49910,16528
PDB,2kor,ACP with other bound intermediate,49910,16528
PDB,2KOS,BMRB Entry Tracking System,49910,16528
BMRB,16506,butyryl-ACP,49929,16529
BMRB,16530,decanoyl-ACP,49929,16529
BMRB,16531,dodecanoyl-ACP,49929,16529
BMRB,16532,tetradecanoyl-ACP,49929,16529
BMRB,16533,hexadecanoyl-ACP,49929,16529
BMRB,16506,butyryl-ACP,49959,16530
BMRB,16529,octanoyl-ACP,49959,16530
BMRB,16531,dodecanoyl-ACP,49959,16530
BMRB,16532,tetradecanoyl-ACP,49959,16530
BMRB,16533,hexadecanoyl-ACP,49959,16530
BMRB,16506,butyryl-ACP,49976,16531
BMRB,16529,octanoyl-ACP,49976,16531
BMRB,16530,decanoyl-ACP,49976,16531
BMRB,16532,tetradecanoyl-ACP,49976,16531
BMRB,16533,hexadecanoyl-ACP,49976,16531
BMRB,16506,butyryl-ACP,49993,16532
BMRB,16529,octanoyl-ACP,49993,16532
BMRB,16530,decanoyl-ACP,49993,16532
BMRB,16531,dodecanoyl-ACP,49993,16532
BMRB,16533,hexadecanoyl-ACP,49993,16532
BMRB,16506,butyryl-ACP,50010,16533
BMRB,16529,octanoyl-ACP,50010,16533
BMRB,16530,decanoyl-ACP,50010,16533
BMRB,16531,dodecanoyl-ACP,50010,16533
BMRB,16532,tetradecanoyl-ACP,50010,16533
PDB,2KOU,BMRB Entry Tracking System,50027,16534
PDB,2ARF,wild type N-domain,50041,16536
PDB,2KOY,BMRB Entry Tracking System,50041,16536
BMRB,17260,UCHL1 S18Y variant,50057,16537
BMRB,16542,Complete Tandem MA-3 Region,50075,16538
BMRB,16540,Solution structure of nasonin-1M,50096,16539
PDB,2KOZ,BMRB Entry Tracking System,50096,16539
BMRB,16539,Solution structure of nasonin-1,50128,16540
PDB,2KP0,BMRB Entry Tracking System,50128,16540
BMRB,16538,Middle MA-3 Domain,50161,16542
BMRB,16300,aSyn,50177,16543
BMRB,16342,aSyn-pH3,50177,16543
BMRB,16546,1H/15N chemical shift assignments for disordered A30P alpha-synuclein at pH 6.0,50177,16543
BMRB,16547,1H/15N chemical shift assignments for disordered E46K alpha-synuclein at pH 6.0,50177,16543
BMRB,16548,1H/15N chemical shift assignments for disordered A53T alpha-synuclein at pH 6.0,50177,16543
BMRB,16904,alpha-synuclei,50177,16543
BMRB,6968,aSyn-protonless,50177,16543
BMRB,7244,gSyn,50177,16543
PDB,2KMU,BMRB Entry Tracking System,50191,16544
PDB,2KP6,BMRB Entry Tracking System,50209,16545
BMRB,16300,aSyn,50234,16546
BMRB,16342,aSyn-pH3,50234,16546
BMRB,16543,1H/15N chemical shift assignments for disordered alpha-synuclein at pH 6.0,50234,16546
BMRB,16547,1H/15N chemical shift assignments for disordered E46K alpha-synuclein at pH 6.0,50234,16546
BMRB,16548,1H/15N chemical shift assignments for disordered A53T alpha-synuclein at pH 6.0,50234,16546
BMRB,16904,alpha-synuclei,50234,16546
BMRB,6968,aSyn-protonless,50234,16546
BMRB,7244,gSyn,50234,16546
BMRB,16300,aSyn,50248,16547
BMRB,16342,aSyn-pH3,50248,16547
BMRB,16543,1H/15N chemical shift assignments for disordered alpha-synuclein at pH 6.0,50248,16547
BMRB,16546,1H/15N chemical shift assignments for disordered A30P alpha-synuclein at pH 6.0,50248,16547
BMRB,16548,1H/15N chemical shift assignments for disordered A53T alpha-synuclein at pH 6.0,50248,16547
BMRB,16904,alpha-synuclei,50248,16547
BMRB,6968,aSyn-protonless,50248,16547
BMRB,7244,gSyn,50248,16547
BMRB,16300,aSyn,50262,16548
BMRB,16342,aSyn-pH3,50262,16548
BMRB,16543,1H/15N chemical shift assignments for disordered alpha-synuclein at pH 6.0,50262,16548
BMRB,16546,1H/15N chemical shift assignments for disordered A30P alpha-synuclein at pH 6.0,50262,16548
BMRB,16547,1H/15N chemical shift assignments for disordered E46K alpha-synuclein at pH 6.0,50262,16548
BMRB,16904,alpha-synuclei,50262,16548
BMRB,6968,aSyn-protonless,50262,16548
BMRB,7244,gSyn,50262,16548
PDB,2KP7,BMRB Entry Tracking System,50276,16549
BMRB,16551,ARNO-(375-400) phosphorylated at Ser392,50315,16550
PDB,2KPA,BMRB Entry Tracking System,50315,16550
BMRB,16550,ARNO-(375-400) apo form,50329,16551
PDB,2KPB,BMRB Entry Tracking System,50329,16551
PDB,2KPJ,BMRB Entry Tracking System,50407,16557
BMRB,16559,MAGI-1 PDZ1 / E6CT,50433,16558
PDB,2KPK,BMRB Entry Tracking System,50433,16558
BMRB,16558,MAGI-1 PDZ1,50456,16559
PDB,2KPL,BMRB Entry Tracking System,50456,16559
PDB,2KPM,BMRB Entry Tracking System,50491,16560
TargetDB,NeR103A,,50491,16560
PDB,2KPN,BMRB Entry Tracking System,50518,16561
BMRB,18558,RDC and peaklist data,50559,16562
PDB,2KPO,BMRB Entry Tracking System,50559,16562
PDB,2LV8,NMR structure refined with RDC data,50559,16562
PDB,2KPP,BMRB Entry Tracking System,50592,16563
PDB,2KPQ,BMRB Entry Tracking System,50615,16564
BMRB,16566,Complex of WT_yeast_TIM with D-glycerol_3-phosphate,50639,16565
BMRB,16565,apo form of WT_yeast_TIM,50656,16566
PDB,2KPS,,50754,16570
PDB,2KPU,BMRB Entry Tracking System,50754,16570
PDB,2KPW,BMRB Entry Tracking System,50794,16572
BMRB,16575,NEDD4-VP40,50836,16574
BMRB,16574,NEDD4-GAP-PRO,50856,16575
PDB,2KQ1,BMRB Entry Tracking System,50875,16576
PDB,2LD5,BMRB Entry Tracking System,50898,16577
PDB,2KQ2,BMRB Entry Tracking System,50915,16578
BMRB,15724,3J coupling constants related to phi-torsions in oxidized flavodoxin,50942,16579
BMRB,15725,3J coupling constants related to chi1-torsions in oxidized flavodoxin,50942,16579
BMRB,15904,1J coupling constants related to the Ca carbons in oxidized Flavodoxin,50942,16579
BMRB,16580,2J coupling constants in Ribonuclease T1,50942,16579
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,50942,16579
BMRB,16582,2J coupling constants in human Ubiquitin,50942,16579
BMRB,16583,2J coupling constants in Xylanase,50942,16579
BMRB,16584,2J coupling constants in DFPase,50942,16579
BMRB,5540,"1H, 13C and 15N chemical shift assignments for reduced flavodoxin",50942,16579
BMRB,5571,"1H, 13C and 15N chemical shift assignments for oxidized flavodoxin",50942,16579
BMRB,133,1H chemical shift assignments for Ribonuclease T1,50984,16580
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,50984,16580
BMRB,16469,3J coupling constants related to the phi-torsions in Ribonuclease T1,50984,16580
BMRB,16579,2J coupling constants in oxidised Flavodxin,50984,16580
BMRB,1658,15N chemical shift assignments for Ribonuclease T1,50984,16580
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,50984,16580
BMRB,16582,2J coupling constants in human Ubiquitin,50984,16580
BMRB,16583,2J coupling constants in Xylanase,50984,16580
BMRB,16584,2J coupling constants in DFPase,50984,16580
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,51031,16581
BMRB,16579,2J coupling constants in oxidised Flavodxin,51031,16581
BMRB,16580,2J coupling constants in Ribonuclease T1,51031,16581
BMRB,16582,2J coupling constants in human Ubiquitin,51031,16581
BMRB,16583,2J coupling constants in Xylanase,51031,16581
BMRB,16584,2J coupling constants in DFPase,51031,16581
BMRB,4342,"1H, 15N, 13C chemical-shift assignments for Frataxin C-terminal domain (90-210)",51031,16581
BMRB,15410,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for human ubiquitin",51048,16582
BMRB,15907,1J coupling constants related to the Ca carbons in human Ubiquitin,51048,16582
BMRB,16579,2J coupling constants in oxidised Flavodxin,51048,16582
BMRB,16580,2J coupling constants in Ribonuclease T1,51048,16582
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,51048,16582
BMRB,16583,2J coupling constants in Xylanase,51048,16582
BMRB,16584,2J coupling constants in DFPase,51048,16582
BMRB,6466,"1H, 15N, 13C chemical-shift assignments for human Ubiquitin",51048,16582
BMRB,6488,3J(HA-N) and 3J(HN-CO) coupling constants in Ubiquitin,51048,16582
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,51092,16583
BMRB,16579,2J coupling constants in oxidised Flavodxin,51092,16583
BMRB,16580,2J coupling constants in Ribonuclease T1,51092,16583
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,51092,16583
BMRB,16582,2J coupling constants in Ubiquitin,51092,16583
BMRB,16584,2J coupling constants in DFPase,51092,16583
BMRB,5352,"1H, 13C and 15N resonance assignment of Bacillus agaradhaerens xylanase",51092,16583
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,51126,16584
BMRB,16579,2J coupling constants in oxidised Flavodxin,51126,16584
BMRB,16580,2J coupling constants in Ribonuclease T1,51126,16584
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,51126,16584
BMRB,16582,2J coupling constants in Ubiquitin,51126,16584
BMRB,16583,2J coupling constants in Xylanase,51126,16584
BMRB,5618,"Backbone 1H, 13C, 15N and Side Chain 13C Chemical Shift Assignments for DFPase from Loligo vulgaris",51126,16584
PDB,2KQ3,BMRB Entry Tracking System,51156,16585
BMRB,7434,3F5 PABPN1 peptide complex,51172,16586
BMRB,15480,w60g-b2m,51187,16587
PDB,1JNJ,,51187,16587
PDB,2VB5,,51187,16587
PDB,2KQ5,BMRB Entry Tracking System,51225,16589
PDB,2KQ6,BMRB Entry Tracking System,51240,16590
PDB,2KQ8,BMRB Entry Tracking System,51275,16592
BMRB,5011,Wild type apoflavodoxin from Anabaena PCC 7119,51306,16593
PDB,1FTG,Crystal structure for wild type apoflavodoxin from Anabaena PCC 7119,51306,16593
PDB,2KQ9,BMRB Entry Tracking System,51322,16594
BMRB,16597,Membrane-Associated Influenza Virus Fusion Peptide,51350,16595
PDB,2KQB,BMRB Entry Tracking System,51364,16596
PDB,2KQC,BMRB Entry Tracking System,51364,16596
PDB,2KQD,BMRB Entry Tracking System,51364,16596
PDB,2KQE,BMRB Entry Tracking System,51364,16596
BMRB,16595,HIV Fusion Peptide in Cholesterol-Rich Membranes,51385,16597
BMRB,6024,TEM-1 E28G (chemical shifts),51400,16598
BMRB,6357,TEM-1 WT (chemical shifts),51400,16598
BMRB,6838,PSE-4 (chemical shifts + dynamics),51400,16598
BMRB,7236,TEM-1 Y105W (chemical shifts),51400,16598
BMRB,7237,TEM-1 Y105G (chemical shifts),51400,16598
BMRB,7238,TEM-1 Y105N (chemical shifts),51400,16598
BMRB,7239,TEM-1 Y105D (chemical shifts),51400,16598
BMRB,17282,apo-IscU(WT),51504,16603
BMRB,7432,"Previous assignment information and 15N R1, R2, and heteronuclear NOE information",51504,16603
PDB,1r9p,NMR solution structure of Haemophilus influenzae Zn-bound IscU,51504,16603
PDB,2KQK,BMRB Entry Tracking System,51504,16603
BMRB,16609,artificial neomycin-sensing riboswitch in complex with ribostamycin,51528,16604
PDB,2KQL,BMRB Entry Tracking System,51554,16605
PDB,2KQM,BMRB Entry Tracking System,51575,16606
PDB,2KQN,BMRB Entry Tracking System,51594,16607
PDB,2KQP,BMRB Entry Tracking System,51613,16608
BMRB,16604,artificial neomycin-sensing riboswitch in complex with tobramycin,51630,16609
PDB,2KQR,BMRB Entry Tracking System,51670,16610
PDB,2ASQ,Solution structure of complex between SUMO-1 and SIM from PIASx,51689,16611
PDB,2RPQ,Solution structure of complex between SUMO-3 and SIM from MCAF1,51689,16611
PDB,1NYJ,"Oriented 15N SSNMR Model, apo",51712,16612
PDB,2H95,Oriented 15N SSNMR Model with Amantadine,51712,16612
PDB,2KAD,Chemical-Shift Constrained Model with Amantadine,51712,16612
PDB,2KQT,BMRB Entry Tracking System,51712,16612
PDB,2RLF,Solution NMR Model with Rimantadine,51712,16612
PDB,3BKD,"X-Ray Crystal Structure at high pH, apo",51712,16612
PDB,3C9J,X-Ray crystal structure with Amantadine,51712,16612
PDB,2JOM,,51793,16616
PDB,2KQY,BMRB Entry Tracking System,51807,16617
PDB,3FS7,Crystal structure of same protein in calcium-bound form,51807,16617
PDB,2KR1,BMRB Entry Tracking System,51872,16620
PDB,2M9Z,BMRB Entry Tracking System,51896,16621
PDB,2rmo,,51910,16622
PDB,2KR5,BMRB Entry Tracking System,51946,16624
BMRB,15249,CNBD in complex with cAMP,51997,16628
PDB,2KR7,BMRB Entry Tracking System,52015,16629
BMRB,15927,"1H, 13C and 15N NMR resonance assignments of the actinoporin Sticholysin I",52044,16630
BMRB,16362,"1H, 13C and 15N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II",52044,16630
PDB,1nty,,52061,16632
PDB,2KRA,BMRB Entry Tracking System,52102,16633
BMRB,15560,L67V mutation,52119,16634
PDB,2IN0,,52119,16634
PDB,2IN8,L67V mutation,52119,16634
PDB,2IN9,,52119,16634
PDB,2KRF,BMRB Entry Tracking System,52160,16636
BMRB,16716,NI3C_Mut5 DARPin,53877,16717
PDB,2JXO,NMR structure of canonical PDZ domain (150-240),52180,16637
PDB,2KJD,BMRB Entry Tracking System,52180,16637
PDB,2OZF,X-ray structure of canonical PDZ domain (150-239),52180,16637
PDB,2KRG,Structure of NHERF1 (150-358) in this study.,52199,16638
PDB,2KRI,BMRB Entry Tracking System,52219,16639
PDB,2KRK,BMRB Entry Tracking System,52256,16640
PDB,2J6K,Entry containing initial coordinates refined in this molecular system,52281,16641
PDB,2J6O,Entry containing initial coordinates refined in this molecular system,52281,16641
PDB,2KRM,BMRB Entry Tracking System,52281,16641
PDB,2FEI,SH3-B of CMS,52297,16642
PDB,2JTE,SH3-C of CD2AP,52297,16642
PDB,2KRN,BMRB Entry Tracking System,52297,16642
PDB,2O2O,SH3-B of CIN85,52297,16642
PDB,2JTE,Entry containing NOe constraints and initial coordinates refined in this study,52312,16643
PDB,2K9G,SH3-C of CIN85,52312,16643
PDB,2KRO,BMRB Entry Tracking System,52312,16643
PDB,2KRR,BMRB Entry Tracking System,52328,16646
PDB,2KRT,BMRB Entry Tracking System,52400,16648
PDB,2KRU,BMRB Entry Tracking System,52441,16649
TargetDB,CtR69A,,52441,16649
PDB,2KRX,BMRB Entry Tracking System,52482,16652
PDB,2L97,BMRB Entry Tracking System,52510,16653
BMRB,16644,RNA (5'-R(*CP*UP*CP*GP*GP*CP*UP*AP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52524,16654
BMRB,16645,RNA 5'-R(*CP*UP*CP*GP*GP*CP*UP*IP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3',52524,16654
BMRB,16650,RNA (5'-R(*CP*UP*CP*GP*GP*(N)P*UP*IP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52524,16654
BMRB,16651,RNA (5'-R(*CP*UP*CP*GP*GP*(N)P*UP*AP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52524,16654
BMRB,16655,RNA (5'-R(*(PSU)P*CP*GP*GP*GP*CP*CP*CP*AP*UP*AP*CP*CP*CP*CP*GP*A)-3'),52524,16654
BMRB,16644,RNA (5'-R(*CP*UP*CP*GP*GP*CP*UP*AP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52548,16655
BMRB,16645,RNA 5'-R(*CP*UP*CP*GP*GP*CP*UP*IP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3',52548,16655
BMRB,16650,RNA (5'-R(*CP*UP*CP*GP*GP*(N)P*UP*IP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52548,16655
BMRB,16651,RNA (5'-R(*CP*UP*CP*GP*GP*(N)P*UP*AP*CP*GP*AP*AP*CP*CP*GP*AP*G)-3'),52548,16655
BMRB,16654,RNA (5'-R(*(PSU)P*CP*GP*GP*GP*CP*CP*(N)P*AP*UP*AP*CP*CP*CP*CP*GP*A)-3'),52548,16655
PDB,2KRZ,BMRB Entry Tracking System,52548,16655
PDB,2KS0,BMRB Entry Tracking System,52572,16656
BMRB,16659,pSic1,52603,16657
PDB,2jwa,,52646,16658
BMRB,20115,Substance P 40 structures in water pH 5.5 298 K,52724,16660
BMRB,20116,Substance P in DMPC:CHAPS q=0.25 bicelles,52724,16660
BMRB,20117,Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles,52724,16660
PDB,2KS9,BMRB Entry Tracking System,52724,16660
BMRB,6516,NMR structure of ACP without the transit peptide,52741,16661
PDB,3gzm,Xray structure of ACP without the transit peptide,52741,16661
PDB,2KSH,BMRB Entry Tracking System,52758,16662
PDB,2KQQ,BMRB Entry Tracking System,52784,16663
BMRB,16662,apo Sterol Carrier Protein - 2 from Aedes aegypti (AeSCP-2),52816,16665
BMRB,16669,RhoA-GTPgS,52874,16668
BMRB,16668,RhoA-GDP,52894,16669
PDB,1PN5,,52914,16670
PDB,2KSP,BMRB Entry Tracking System,52928,16671
PDB,2KSR,BMRB Entry Tracking System,52948,16672
PDB,2KSU,BMRB Entry Tracking System,52981,16674
PDB,2KSV,BMRB Entry Tracking System,53005,16675
PDB,2LAG,BMRB Entry Tracking System,53038,16677
PDB,2KSY,BMRB Entry Tracking System,53057,16678
PDB,2LFU,BMRB Entry Tracking System,53079,16679
PDB,2KT0,BMRB Entry Tracking System,53093,16680
PDB,2KT1,BMRB Entry Tracking System,53107,16681
PDB,2KT4,BMRB Entry Tracking System,53135,16682
PDB,2F3J,REF in free form,53155,16683
PDB,2KT5,BMRB Entry Tracking System,53155,16683
PDB,3L48,corresponding X-ray crystal structure,53174,16684
PDB,2kt7,,53226,16686
TargetDB,LmR64A,,53226,16686
PDB,1YW5,THE STRUCTURE OF THE CANDIDA ALBICANS ESS1 PROLYL  ISOMERASE REVEALS A WELL-ORDERED LINKER THAT RESTRICTS DOMAIN MOBILITY,53361,16690
PDB,2KT9,BMRB Entry Tracking System,53375,16691
PDB,2KTA,BMRB Entry Tracking System,53424,16692
PDB,2KTC,BMRB Entry Tracking System,53449,16693
PDB,2KTB,BMRB Entry Tracking System,53465,16694
BMRB,16683,REF 54-155 with ICP27 103-138,53515,16696
PDB,2F3J,REF in free form,53515,16696
PDB,2KT5,BMRB Entry Tracking System,53515,16696
BMRB,16683,REF 54-155 with ICP27 103-138,53529,16697
PDB,2F3J,REF in free form,53529,16697
PDB,2KT5,BMRB Entry Tracking System,53529,16697
BMRB,16683,REF 54-155 with ICP27 103-138,53543,16698
BMRB,7435,REF 54-155 with ORF57_8-120,53543,16698
PDB,2F3J,REF in free form,53543,16698
PDB,2KT5,BMRB Entry Tracking System,53543,16698
PDB,2LGZ,BMRB Entry Tracking System,53606,16701
BMRB,16704,SPI2(T7Y),53621,16703
BMRB,16705,SPI2(T7A),53621,16703
BMRB,16703,SPI2,53639,16704
BMRB,16705,SPI2(T7A),53639,16704
BMRB,16703,SPI2,53657,16705
BMRB,16704,SPI2(T7Y),53657,16705
PDB,1tpx,,53675,16706
PDB,1tqb,,53675,16706
PDB,1xyu,,53675,16706
PDB,1y2s,,53675,16706
BMRB,16709,Lch-beta peptide,53690,16707
BMRB,16707,Lch-alpha peptide,53727,16709
PDB,2KTN,BMRB Entry Tracking System,53727,16709
PDB,2KTS,BMRB Entry Tracking System,53763,16711
BMRB,16713,reduced desulthioredoxin,53782,16712
BMRB,16712,oxidized desulthioredoxin,53796,16713
PDB,2Y95,BMRB Entry Tracking System,53810,16714
PDB,2LAV,BMRB Entry Tracking System,53841,16715
BMRB,16717,NI3C DARPin,53860,16716
BMRB,16718,NI2C DARPin,53860,16716
BMRB,16718,NI2C DARPin,53877,16717
BMRB,16716,NI3C_Mut5 DARPin,53894,16718
BMRB,16717,NI3C DARPin,53894,16718
PDB,2L95,BMRB Entry Tracking System,53911,16719
BMRB,16722,mouse prion protein mutant D167S,53943,16720
BMRB,16723,"mouse prion protein double mutant D167S, N173K",53943,16720
PDB,2KU4,BMRB Entry Tracking System,53943,16720
PDB,2KU3,BMRB Entry Tracking System,53959,16721
BMRB,16720,Horse prion protein,53981,16722
BMRB,16723,"mouse prion protein double mutant D167S, N173K",53981,16722
PDB,2KU5,BMRB Entry Tracking System,53981,16722
BMRB,16720,mouse prion protein mutant D167S,53997,16723
BMRB,16722,"mouse prion protein double mutant D167S, N173K",53997,16723
PDB,2KU6,BMRB Entry Tracking System,53997,16723
PDB,2KUC,BMRB Entry Tracking System,54072,16731
TargetDB,NYSGXRC-11211c,,54072,16731
BMRB,16733,PASTA domain 2 and 3 of PknB,54088,16732
BMRB,16734,PASTA domain 3 and 4 of PknB,54088,16732
PDB,2KUD,BMRB Entry Tracking System,54088,16732
BMRB,16732,PASTA domain 1 and 2 of PknB,54104,16733
BMRB,16734,PASTA domain 3 and 4 of PknB,54104,16733
PDB,2KUE,BMRB Entry Tracking System,54104,16733
BMRB,16732,PASTA domain 1 and 2 of PknB,54120,16734
BMRB,16733,PASTA domain 2 and 3 of PknB,54120,16734
PDB,2KUF,BMRB Entry Tracking System,54120,16734
PDB,2KKC,Monomeric structure of p62 PB1,54150,16736
PDB,2RPV,Structure of the LBT attached to GB1,54150,16736
PDB,2KXI,BMRB Entry Tracking System,54170,16737
PDB,2KUL,BMRB Entry Tracking System,54195,16738
PDB,1ZFU,NMR solution structure,54215,16739
BMRB,16741,Backbone assignments for Paracoccus denitrificans amicyanin-CuI.,54242,16740
BMRB,16740,Amide assignments for Paracoccus denitrificans amicyanin-ZnII.,54259,16741
PDB,2KUN,BMRB Entry Tracking System,54290,16743
PDB,2KUO,BMRB Entry Tracking System,54311,16744
PDB,2KUS,BMRB Entry Tracking System,54340,16745
PDB,2KUT,BMRB Entry Tracking System,54358,16746
PDB,2KUY,BMRB Entry Tracking System,54383,16747
BMRB,17343,NOXO1b,54413,16749
PDB,2KUG,BMRB Entry Tracking System,54702,16764
PDB,2KUH,BMRB Entry Tracking System,54702,16764
PDB,2KV3,BMRB Entry Tracking System,54738,16767
PDB,2KV4,BMRB Entry Tracking System,54754,16768
PDB,2KV7,BMRB Entry Tracking System,54798,16770
PDB,1KUP,,54822,16771
PDB,1KUZ,,54822,16771
PDB,1M8O,,54822,16771
PDB,2K9J,,54822,16771
PDB,2KV9,BMRB Entry Tracking System,54822,16771
BMRB,16773,CI-MPR domain5 (complex form),54841,16772
PDB,2KVA,BMRB Entry Tracking System,54841,16772
BMRB,16772,CI-MPR domain5 (apo form),54860,16773
PDB,2KVB,BMRB Entry Tracking System,54860,16773
PDB,2KVC,BMRB Entry Tracking System,54879,16774
PDB,2KVM,BMRB Entry Tracking System,54919,16778
PDB,2LXD,BMRB Entry Tracking System,54943,16779
PDB,2KVO,BMRB Entry Tracking System,54994,16782
BMRB,16785,conotoxin_cis-mr3c,55062,16784
BMRB,16786,cis-conomarphin,55062,16784
PDB,2JQC,A L-amino acid mutant of a D-amino acid containing conopeptide,55062,16784
PDB,2YYF,"A D-amino acid containing conopeptide, marmophine, from Conus marmoreus",55062,16784
BMRB,16784,conotoxin_mr3c,55081,16785
BMRB,16786,cis-conomarphin,55081,16785
PDB,2JQC,A L-amino acid mutant of a D-amino acid containing conopeptide,55081,16785
PDB,2YYF,"A D-amino acid containing conopeptide, marmophine, from Conus marmoreus",55081,16785
BMRB,16784,conotoxin_mr3c,55100,16786
BMRB,16785,conotoxin_cis-mr3c,55100,16786
PDB,2JQC,A L-amino acid mutant of a D-amino acid containing conopeptide,55100,16786
PDB,2YYF,"A D-amino acid containing conopeptide, marmophine, from Conus marmoreus",55100,16786
BMRB,16804,oxidized Rieske Protein,55120,16787
PDB,2KVQ,BMRB Entry Tracking System,55136,16788
PDB,2KVR,BMRB Entry Tracking System,55156,16789
PDB,2x8n,,55174,16790
PDB,2KVT,BMRB Entry Tracking System,55203,16791
PDB,2KVU,BMRB Entry Tracking System,55227,16792
PDB,2KVS,BMRB Entry Tracking System,55252,16794
PDB,2KVV,BMRB Entry Tracking System,55293,16795
PDB,2KLQ,,55318,16796
PDB,2KVH,BMRB Entry Tracking System,55344,16797
BMRB,16799,(JFH-1) in presence of 50%TFE,55364,16798
BMRB,16800,(Con1) in presence of 50%TFE,55364,16798
BMRB,16798,5A (NS5A) protein from Hepatitis C Virus (JFH-1),55379,16799
BMRB,16800,(Con1) in presence of 50%TFE,55379,16799
BMRB,16798,5A (NS5A) protein from Hepatitis C Virus (JFH-1),55394,16800
BMRB,16799,(JFH-1) in presence of 50%TFE,55394,16800
PDB,2KT7,another domain from same polypeptide and with a similar fold,55409,16801
PDB,2KVZ,BMRB Entry Tracking System,55409,16801
BMRB,16787,reduced Rieske Protein,55460,16804
PDB,2KW2,BMRB Entry Tracking System,55476,16805
PDB,3lmo,,55476,16805
PDB,2KW5,BMRB Entry Tracking System,55503,16806
BMRB,16578,apo form,55544,16807
PDB,2kq2,apo form,55544,16807
PDB,2KW4,BMRB Entry Tracking System,55544,16807
BMRB,16816,NESG target HR4547E,55570,16808
PDB,2KW6,BMRB Entry Tracking System,55570,16808
PDB,1awj,SH3 peptide complex,55603,16809
PDB,1luk,cis SH2 domain,55603,16809
PDB,1lun,trans SH2 domain,55603,16809
PDB,2etz,SH2 peptide complex,55603,16809
PDB,2rna,SH3 domain,55603,16809
PDB,2KW7,BMRB Entry Tracking System,55624,16810
TargetDB,PgR37A,,55624,16810
PDB,2KW8,BMRB Entry Tracking System,55651,16811
PDB,2KAE,BMRB Entry Tracking System,55677,16812
PDB,2KNB,BMRB Entry Tracking System,55696,16813
BMRB,16815,mouse testis zinc finger protein,55720,16814
BMRB,16814,mouse testis zinc finger protein,55740,16815
BMRB,16792,without RDC,55759,16816
BMRB,16808,NESG target HR3057H,55759,16816
PDB,2KW9,BMRB Entry Tracking System,55759,16816
PDB,2kvu,without RDC,55759,16816
PDB,2KSG,BMRB Entry Tracking System,55787,16817
BMRB,16727,monomeric culbertcidin,55817,16819
PDB,2ku8,monomeric culbertcidin,55817,16819
BMRB,16091,NMR chemical shifts,55834,16820
PDB,2kcp,NMR structure refined without RDC constraints,55834,16820
PDB,2KCY,BMRB Entry Tracking System,55834,16820
BMRB,16084,NMR chemical shifts,55860,16821
PDB,2kcl,NMR structure refined without RDC constraints,55860,16821
PDB,2KCV,BMRB Entry Tracking System,55860,16821
PDB,2K42,BMRB Entry Tracking System,55906,16824
PDB,2KNG,BMRB Entry Tracking System,55927,16831
PDB,2KTL,BMRB Entry Tracking System,55941,16832
PDB,2LOY,BMRB Entry Tracking System,55956,16833
PDB,2KAL,BMRB Entry Tracking System,56000,16834
PDB,2KWC,BMRB Entry Tracking System,56025,16835
PDB,1BOY,,56059,16838
PDB,1TFH,,56059,16838
PDB,2HFT,,56059,16838
PDB,2KUM,BMRB Entry Tracking System,56075,16839
PDB,2L9C,BMRB Entry Tracking System,56097,16840
BMRB,4830,The Hairpin Structure of the (6)F1(1)F2(2)F2 Fragment from Human Fibronectin Enhances Gelatin Binding,56116,16841
PDB,1E88,The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.,56116,16841
PDB,2LDO,BMRB Entry Tracking System,56138,16842
PDB,2K3B,BMRB Entry Tracking System,56160,16843
PDB,2KKD,BMRB Entry Tracking System,56252,16849
PDB,2QL0,NMR stucture of the Zn substituted form of the same protein,56252,16849
PDB,8RXN,X-ray stucture of same protein but with native Fe centre,56252,16849
PDB,2KWF,BMRB Entry Tracking System,56294,16851
PDB,2KWG,BMRB Entry Tracking System,56314,16852
BMRB,15479,Chemical shifts for cytoplasmic domains of human CD4,56342,16853
PDB,2KLU,BMRB Entry Tracking System,56342,16853
PDB,2KWL,BMRB Entry Tracking System,56376,16856
PDB,2KB9,BMRB Entry Tracking System,56392,16857
PDB,2VJ2,crystal structure of DSL/EGF1/EGF2/EGF3,56392,16857
BMRB,16859,DPF3b bound histone N-terminal H3,56409,16858
BMRB,16861,DPF3b bound histone H4 acetylated lys 16,56409,16858
BMRB,16865,DPF3b bound histone H4 acetylated serine 1,56409,16858
BMRB,16878,DPF3b bound Histone H3 1-20Cys,56409,16858
BMRB,16858,DPF3b bound histone H3 acetylated lys 14,56439,16859
BMRB,16861,DPF3b bound histone H4 acetylated lys 16,56439,16859
BMRB,16865,DPF3b bound histone H4 acetylated serine 1,56439,16859
BMRB,16878,DPF3b bound Histone H3 1-20Cys,56439,16859
PDB,2KJS,before NH RDC refinement,56469,16860
PDB,2KWM,before NH RDC refinement,56469,16860
BMRB,16858,DPF3b bound histone H3 acetylated lys 14,56523,16861
BMRB,16859,DPF3b bound histone N-terminal H3,56523,16861
BMRB,16865,DPF3b bound histone H4 acetylated serine 1,56523,16861
BMRB,16878,DPF3b bound Histone H3 1-20Cys,56523,16861
PDB,2KWN,BMRB Entry Tracking System,56523,16861
PDB,2LAN,BMRB Entry Tracking System,56553,16862
PDB,2MA0,BMRB Entry Tracking System,56590,16864
BMRB,16858,DPF3b bound histone H3 acetylated lys 14,56607,16865
BMRB,16859,DPF3b bound histone N-terminal H3,56607,16865
BMRB,16861,DPF3b bound histone H4 acetylated lys 16,56607,16865
BMRB,16878,DPF3b bound Histone H3 1-20Cys,56607,16865
PDB,2KWO,BMRB Entry Tracking System,56607,16865
BMRB,16867,VAMP7(1-180),56639,16866
BMRB,16866,VAMP7(1-118),56653,16867
PDB,2KWP,BMRB Entry Tracking System,56667,16868
BMRB,17201,little finger domain of Dpo4,56684,16869
PDB,2JWE,BMRB Entry Tracking System,56718,16871
PDB,2KWQ,BMRB Entry Tracking System,56741,16872
BMRB,15156,beta-1 immunoglobulin binding domain of protein G (GB1),56766,16873
PDB,1GB1,,56766,16873
PDB,1IBX,,56766,16873
PDB,1PGB,,56766,16873
PDB,1PN5,,56766,16873
PDB,2CWB,,56766,16873
PDB,2DEN,,56766,16873
PDB,2GB1,,56766,16873
PDB,2GI9,,56766,16873
PDB,2I2Y,,56766,16873
PDB,2I38,,56766,16873
PDB,2JSV,,56766,16873
PDB,2JU6,,56766,16873
PDB,2K0P,,56766,16873
PDB,2KBT,,56766,16873
PDB,2KHU,,56766,16873
PDB,2KHW,,56766,16873
PDB,2KLK,,56766,16873
PDB,2KQ4,,56766,16873
PDB,2PLP,,56766,16873
PDB,2QMT,,56766,16873
PDB,2RMM,,56766,16873
PDB,3GB1,,56766,16873
PDB,IPGA,,56766,16873
PDB,2a9x,BIV TAR and cyclic peptide mimicking BIV Tat,56827,16877
PDB,2ns4,Unbound L-22 solution structure,56827,16877
BMRB,16858,DPF3b bound histone H3 acetylated lys 14,56854,16878
BMRB,16859,DPF3b bound histone N-terminal H3,56854,16878
BMRB,16861,DPF3b bound histone H4 acetylated lys 16,56854,16878
BMRB,16865,DPF3b bound histone H4 acetylated serine 1,56854,16878
PDB,2KFT,BMRB Entry Tracking System,56854,16878
BMRB,16885,Solution Structure of UBM1,56891,16880
PDB,2KHU,,56891,16880
PDB,2KHW,,56891,16880
PDB,2KWU,BMRB Entry Tracking System,56891,16880
PDB,2KF2,BMRB Entry Tracking System,56917,16881
BMRB,16953,GGUAGGCCA,58282,16952
PDB,2KHU,BMRB Entry Tracking System,56939,16882
BMRB,16880,Solution Structure of UBM2,56988,16885
PDB,2KWU,,56988,16885
PDB,2KWV,BMRB Entry Tracking System,56988,16885
BMRB,15579,HCV NS2 [1-27],57014,16886
BMRB,16892,HCV NS2 [60-99],57014,16886
PDB,1JY0,HCV NS2 [1-27],57014,16886
PDB,2KWT,BMRB Entry Tracking System,57014,16886
BMRB,16888,HIV-2 myristoylated Matrix protein,57030,16887
BMRB,16889,"HIV-2 myrMA bound to di-C4-PI(4,5)P2",57030,16887
PDB,2K4E,BMRB Entry Tracking System,57030,16887
BMRB,16887,"myristoylated HIV-2 MA protein and PI(4,5)P2",57047,16888
BMRB,16889,"HIV-2 myrMA bound to di-C4-PI(4,5)P2",57047,16888
PDB,2K4H,BMRB Entry Tracking System,57047,16888
BMRB,16887,"myristoylated HIV-2 MA protein and PI(4,5)P2",57065,16889
BMRB,16888,HIV-2 myristoylated Matrix protein,57065,16889
PDB,2K4I,BMRB Entry Tracking System,57065,16889
BMRB,15579,HCV NS2 [1-27],57119,16892
BMRB,16886,HCV NS2 [27-59],57119,16892
PDB,2JY0,,57119,16892
PDB,2KWT,,57119,16892
PDB,2KWZ,BMRB Entry Tracking System,57119,16892
BMRB,16894,MDM4-nutlin3 complex,57135,16893
BMRB,16900,MDM4-p53 complex,57135,16893
BMRB,16893,MDM4 N-terminal domain,57150,16894
BMRB,16900,MDM4-p53 complex,57150,16894
PDB,2KX0,BMRB Entry Tracking System,57167,16895
PDB,2KX2,BMRB Entry Tracking System,57191,16897
BMRB,16893,MDM4 N-terminal domain,57265,16900
BMRB,16894,MDM4 N-terminal domain,57265,16900
PDB,2h8b,independent structure assignment,57282,16901
PDB,2K6T,BMRB Entry Tracking System,57282,16901
BMRB,16300,aSyn,57332,16904
BMRB,16342,aSyn-pH3,57332,16904
BMRB,16547,aSyn E46K-pH6,57332,16904
BMRB,6968,aSyn-protonless,57332,16904
BMRB,7244,gSyn,57332,16904
PDB,2LPM,BMRB Entry Tracking System,57351,16905
PDB,2KXC,BMRB Entry Tracking System,57426,16909
PDB,3LLO,Crystal structure of the STAS domain of motor protein prestin (anion transporter SLC26A5),57445,16910
BMRB,17999,Chemical Shift Assignments from PfEMP1: Full-length,57465,16911
PDB,2LKL,BMRB Entry Tracking System,57465,16911
BMRB,19284,"T1, T2, and NOE data",57486,16912
PDB,2M4K,BMRB Entry Tracking System,57486,16912
PDB,2KXG,BMRB Entry Tracking System,57503,16913
PDB,2KXK,BMRB Entry Tracking System,57532,16915
BMRB,16919,apo-form of spMDD,57551,16916
BMRB,16918,Mg(2+)-bound CKI1RD,57572,16917
PDB,3MM4,,57572,16917
BMRB,16917,CKI1RD,57595,16918
PDB,3MMN,,57595,16918
BMRB,16916,spMDD in complex with ligands,57620,16919
PDB,2KXN,BMRB Entry Tracking System,57648,16920
PDB,2KSF,BMRB Entry Tracking System,57687,16922
PDB,2KXQ,BMRB Entry Tracking System,57703,16923
BMRB,18810,Trypanosoma brucei FKBP12,57719,16925
PDB,2KXX,BMRB Entry Tracking System,57743,16926
PDB,2KXY,BMRB Entry Tracking System,57760,16927
PDB,2KXV,BMRB Entry Tracking System,57795,16929
BMRB,15457,"domain, 1655-1822",57828,16930
BMRB,15458,F0 domain (residues 1-85),57828,16930
BMRB,15615,F0F1  double domain,57828,16930
BMRB,15616,F1,57828,16930
BMRB,15625,Residues 1815-1973,57828,16930
BMRB,16932,F2F3 domain (residues 196-405),57828,16930
BMRB,16959,F1F2 double domain (residues 86-303),57828,16930
BMRB,17070,domain C,57828,16930
PDB,2KBB,structure entry,57828,16930
PDB,2KMA,structure entry,57828,16930
BMRB,16933,FKBP12-rapamycin-FRB,57843,16931
BMRB,15457,"domain, 1655-1822",57875,16932
BMRB,15458,F0 domain (residues 1-85),57875,16932
BMRB,15615,F0F1  double domain,57875,16932
BMRB,15616,F1,57875,16932
BMRB,15625,Residues 1815-1973,57875,16932
BMRB,16932,F2F3 domain (residues 196-405),57875,16932
BMRB,16959,F1F2 double domain (residues 86-303),57875,16932
BMRB,17070,domain C,57875,16932
PDB,2KBB,structure entry,57875,16932
PDB,2KMA,structure entry,57875,16932
BMRB,16931,FKBP12-rapamycin,57890,16933
PDB,2KY4,BMRB Entry Tracking System,57914,16934
TargetDB,NsR123E,,57914,16934
PDB,2KY5,BMRB Entry Tracking System,57949,16935
PDB,1IG4,MBD1 bound to methylated DNA,57968,16936
PDB,2KY8,BMRB Entry Tracking System,57968,16936
PDB,3C2I,MeCP2 bound to methylated DNA,57968,16936
BMRB,17648,A30P alpha-synuclein fibrils,58011,16939
BMRB,17649,A53T alpha-synuclein fibrils,58011,16939
BMRB,17654,E46K alpha-synuclein fibrils,58011,16939
PDB,2A9X,BIV TAR and BIV Tat mimic,58053,16941
PDB,2KDQ,HIV-1 and peptide mimic of Tat protein,58053,16941
PDB,2KX5,BMRB Entry Tracking System,58053,16941
TargetDB,SR518,,58077,16942
PDB,2KYB,BMRB Entry Tracking System,58134,16944
BMRB,16955,calcium-bound CPV3,58159,16945
PDB,2KYC,BMRB Entry Tracking System,58159,16945
PDB,2KSD,BMRB Entry Tracking System,58191,16947
BMRB,16951,GACGAGCGUCA,58241,16950
BMRB,16952,GACUAGAGUCA,58241,16950
BMRB,16953,GGUAGGCCA,58241,16950
PDB,2KXZ,BMRB Entry Tracking System,58241,16950
BMRB,16950,GACAAGUGUCA,58262,16951
BMRB,16952,GACUAGAGUCA,58262,16951
BMRB,16953,GGUAGGCCA,58262,16951
PDB,2KY0,BMRB Entry Tracking System,58262,16951
BMRB,16950,GACAAGUGUCA,58282,16952
BMRB,16951,GACGAGCGUCA,58282,16952
PDB,2KY1,BMRB Entry Tracking System,58282,16952
BMRB,16950,GACAAGUGUCA,58302,16953
BMRB,16951,GACGAGCGUCA,58302,16953
BMRB,16952,GACUAGAGUCA,58302,16953
PDB,2KY2,BMRB Entry Tracking System,58302,16953
PDB,2KYG,BMRB Entry Tracking System,58321,16954
BMRB,16945,calcium-free CPV3,58343,16955
PDB,2KYF,BMRB Entry Tracking System,58343,16955
BMRB,15716,"1H, 15N, 13C resonance assignment of the AlgE6R1 subunit from the Azotobacter vinelandii Mannuronan C5-epimerase",58359,16956
BMRB,6390,NMR assignment of the R-module from the Azotobacter vinelandii mannuronan C5-epimerase AlgE4,58359,16956
PDB,2KYH,BMRB Entry Tracking System,58380,16957
BMRB,15457,"domain, 1655-1822",58425,16959
BMRB,15458,F0 domain (residues 1-85),58425,16959
BMRB,15615,F0F1  double domain,58425,16959
BMRB,15616,F1,58425,16959
BMRB,15625,Residues 1815-1973,58425,16959
BMRB,16930,F2 domain (residues 196-309),58425,16959
BMRB,16932,F2F3 domain (residues 196-405),58425,16959
BMRB,17070,domain C,58425,16959
PDB,2KBB,structure entry,58425,16959
PDB,2KMA,structure entry,58425,16959
PDB,2WH9,BMRB Entry Tracking System,58454,16960
PDB,2KYI,BMRB Entry Tracking System,58471,16961
BMRB,15904,1J coupling constants related to the Ca carbons in oxidized Flavodxin,58502,16962
BMRB,15905,1J coupling constants related to the Ca carbons in Ribonuclease T1,58502,16962
BMRB,15906,1J coupling constants related to the Ca carbons in Frataxin C-terminal domain,58502,16962
BMRB,15907,1J coupling constants related to the Ca carbons in Ubiquitin,58502,16962
BMRB,15908,1J coupling constants related to the Ca carbons in Xylanase,58502,16962
BMRB,15909,1J coupling constants related to the Ca carbons in DFPase,58502,16962
BMRB,15964,chemical shift assignments oxidized ERp18,58502,16962
BMRB,16579,2J coupling constants in oxidized Flavodoxin,58502,16962
BMRB,16580,2J coupling constants in Ribonuclease T1,58502,16962
BMRB,16581,2J coupling constants in Frataxin C-terminal domain,58502,16962
BMRB,16582,2J coupling constants in Ubiquitin,58502,16962
BMRB,16583,2J coupling constants in Xylanase,58502,16962
BMRB,16584,2J coupling constants in DFPase,58502,16962
PDB,2KYJ,BMRB Entry Tracking System,58549,16963
BMRB,16965,HET-s(1-227) solid state,58565,16964
BMRB,16964,HET-s(1-227) solution state,58580,16965
PDB,2KYL,BMRB Entry Tracking System,58609,16967
PDB,2h8b,cross-linked derivative,58631,16968
PDB,2k6t,cross-linked derivative determine under the same experimental conditions,58631,16968
PDB,2K6U,BMRB Entry Tracking System,58631,16968
PDB,2KYM,BMRB Entry Tracking System,58690,16970
PDB,2L8B,BMRB Entry Tracking System,58711,16971
PDB,2L8K,BMRB Entry Tracking System,58726,16977
PDB,1BRZ,"WT-brazzein, original structure",58747,16978
PDB,2KGQ,"WT-brazzein, revised structure",58747,16978
PDB,2KYQ,BMRB Entry Tracking System,58747,16978
PDB,2KYR,BMRB Entry Tracking System,58775,16979
PDB,2KYD,BMRB Entry Tracking System,58815,16980
BMRB,16984,Complex form,58852,16982
PDB,1GUB,,58852,16982
PDB,2KYU,BMRB Entry Tracking System,58866,16983
BMRB,16982,Apo form,58882,16984
PDB,1GUD,,58882,16984
PDB,2KXE,BMRB Entry Tracking System,58898,16986
TargetDB,PtR41O,,58915,16988
PDB,2KYX,BMRB Entry Tracking System,58951,16989
TargetDB,NeR70A,,58979,16991
PDB,2KZ2,BMRB Entry Tracking System,59026,16994
PDB,2KZ0,BMRB Entry Tracking System,59051,16995
PDB,2KZ3,BMRB Entry Tracking System,59070,16996
PDB,2KZ4,BMRB Entry Tracking System,59087,16997
PDB,2KZ5,BMRB Entry Tracking System,59110,16998
PDB,2KZ6,BMRB Entry Tracking System,59156,16999
PDB,2KZ9,BMRB Entry Tracking System,59192,17000
PDB,1HYK,minimized human agouti related protein,59208,17001
PDB,1MR0,agouti-related protein,59208,17001
PDB,1Y7J,agouti signaling protein,59208,17001
PDB,1Y7K,agouti signaling protein,59208,17001
PDB,2KZA,BMRB Entry Tracking System,59208,17001
PDB,2KZC,BMRB Entry Tracking System,59228,17002
PDB,1PII,Entry containing crystal structure of the full-length phosphorybosilanthranilate isomerase (PRAI) from Eschericia coli,59261,17005
PDB,2KZH,BMRB Entry Tracking System,59261,17005
BMRB,17007,Alpha-mannosidase binding domain of Atg34,59286,17006
PDB,2KZB,BMRB Entry Tracking System,59286,17006
BMRB,17006,Alpha-mannosidase binding domain of ATG19,59304,17007
PDB,2KZK,BMRB Entry Tracking System,59304,17007
BMRB,5619,Resonance assignments for SR10,59322,17008
PDB,1xm0,,59322,17008
PDB,2KZN,BMRB Entry Tracking System,59322,17008
PDB,3FMY,,59364,17009
PDB,3GN5,,59364,17009
BMRB,17012,mutant L75F Tryptophan Repressor,59380,17010
BMRB,17013,mutant A77V Tryptophan Repressor,59380,17010
BMRB,17041,Tryptophan repressor protein in holo-form,59380,17010
BMRB,17046,Tryptophan repressor L75F mutant in holo-form,59380,17010
BMRB,17047,Tryptophan repressor A77V mutant protein in holo-form,59380,17010
PDB,2KZQ,BMRB Entry Tracking System,59403,17011
BMRB,17010,Wild Type Tryptophan Repressor,59418,17012
BMRB,17013,mutant A77V Tryptophan Repressor,59418,17012
BMRB,17041,Tryptophan repressor protein in holo-form,59418,17012
BMRB,17046,Tryptophan repressor L75F mutant in holo-form,59418,17012
BMRB,17047,Tryptophan repressor A77V mutant protein in holo-form,59418,17012
BMRB,17010,Wild Type Tryptophan Repressor,59439,17013
BMRB,17012,mutant L75F Tryptophan Repressor,59439,17013
BMRB,17041,Tryptophan repressor protein in holo-form,59439,17013
BMRB,17046,Tryptophan repressor L75F mutant in holo-form,59439,17013
BMRB,17047,Tryptophan repressor A77V mutant protein in holo-form,59439,17013
PDB,2K38,BMRB Entry Tracking System,59476,17015
PDB,2KXP,solution NMR structure of V-1 bound to capping protein (CP),59492,17016
PDB,2KZ7,BMRB Entry Tracking System,59492,17016
PDB,2KZU,BMRB Entry Tracking System,59563,17019
PDB,2KZV,BMRB Entry Tracking System,59592,17020
BMRB,17024,Znf_A20:ubiquitin complex,59686,17023
PDB,2KZY,BMRB Entry Tracking System,59686,17023
BMRB,17023,free ZNF216 A20,59707,17024
PDB,2kzy,free ZNF216 A20,59707,17024
PDB,2L01,BMRB Entry Tracking System,59733,17025
TargetDB,BvR153,,59733,17025
TargetDB,BtR375,,59766,17026
PDB,2L04,BMRB Entry Tracking System,59816,17028
PDB,2L05,BMRB Entry Tracking System,59851,17030
PDB,2KGQ,"WT-brazzein, revised structure",59924,17032
PDB,2KYQ,CKR-brazzein,59924,17032
PDB,2L07,BMRB Entry Tracking System,59924,17032
PDB,2L08,BMRB Entry Tracking System,59951,17033
PDB,2L09,BMRB Entry Tracking System,59995,17035
PDB,2L0C,BMRB Entry Tracking System,60055,17038
PDB,2L0D,BMRB Entry Tracking System,60087,17039
PDB,2L0E,BMRB Entry Tracking System,60132,17040
BMRB,17010,Wild Type Tryptophan Repressor,60152,17041
BMRB,17012,mutant L75F Tryptophan Repressor,60152,17041
BMRB,17013,mutant A77V Tryptophan Repressor,60152,17041
BMRB,17046,Tryptophan repressor L75F mutant in holo-form,60152,17041
BMRB,17047,Tryptophan repressor A77V mutant protein in holo-form,60152,17041
PDB,2xdi,,60152,17041
PDB,2KM4,Solution structure of Rtt103 CTD-interacting domain,60208,17044
PDB,2L0I,BMRB Entry Tracking System,60208,17044
PDB,2LPE,BMRB Entry Tracking System,60223,17045
BMRB,17010,Wild Type Tryptophan Repressor,60241,17046
BMRB,17012,mutant L75F Tryptophan Repressor,60241,17046
BMRB,17013,mutant A77V Tryptophan Repressor,60241,17046
BMRB,17041,Tryptophan repressor protein in holo-form,60241,17046
BMRB,17047,Tryptophan repressor A77V mutant protein in holo-form,60241,17046
PDB,2xdi,,60241,17046
BMRB,17010,Wild Type Tryptophan Repressor,60267,17047
BMRB,17012,mutant L75F Tryptophan Repressor,60267,17047
BMRB,17013,mutant A77V Tryptophan Repressor,60267,17047
BMRB,17041,Tryptophan repressor protein in holo-form,60267,17047
BMRB,17046,Tryptophan repressor L75F mutant in holo-form,60267,17047
PDB,2xdi,,60267,17047
PDB,2e5p,human homolog,60322,17050
PDB,2e5q,human homolog,60322,17050
PDB,2eqj,human homolog,60322,17050
PDB,2XK0,BMRB Entry Tracking System,60322,17050
BMRB,17063,hPgn (K57D)rK3,60518,17062
PDB,2L0S,BMRB Entry Tracking System,60518,17062
BMRB,17062,hPgn rK3,60538,17063
BMRB,7312,VHS domain monomer of STAM1,60575,17065
PDB,2L0W,BMRB Entry Tracking System,60590,17066
PDB,2k3j,Solution structure of human Mia40,60609,17067
PDB,2L0Y,BMRB Entry Tracking System,60609,17067
PDB,2rn9,Solution structure of human apoCox17,60609,17067
BMRB,6356,Yfh1 298K chemical shift assignment,60629,17068
PDB,2ga5,Yfh1 298K solution structure,60629,17068
BMRB,16177,Chemical shift assignments for E73 from SSV-RH,60643,17069
BMRB,15457,"domain, 1655-1822",60676,17070
BMRB,15458,F0 domain (residues 1-85),60676,17070
BMRB,15615,F0F1  double domain,60676,17070
BMRB,15616,F1,60676,17070
BMRB,15625,Residues 1815-1973,60676,17070
BMRB,16930,F2 domain (residues 196-309),60676,17070
BMRB,16932,F2F3 domain (residues 196-405),60676,17070
BMRB,16959,F1F2 double domain (residues 86-303),60676,17070
PDB,2KBB,structure entry,60676,17070
PDB,2KMA,structure entry,60676,17070
PDB,2L10,BMRB Entry Tracking System,60676,17070
BMRB,17072,Cbx7 H3K9me3 complex,60697,17071
BMRB,17079,Cbx7 H3K9me3 complex,60697,17071
PDB,2L11,BMRB Entry Tracking System,60697,17071
BMRB,17071,Cbx3 H3K9me3 complex,60723,17072
BMRB,17079,Cbx3 H3K9me3 complex,60723,17072
PDB,2L12,BMRB Entry Tracking System,60723,17072
PDB,2L14,BMRB Entry Tracking System,60750,17073
BMRB,17076,SynArsC in TRIS buffer,60769,17074
BMRB,17077,Disulfide bound SynArsC,60769,17074
BMRB,17074,SynArsC in PBS buffer,60803,17076
BMRB,17077,Disulfide bound SynArsC,60803,17076
BMRB,17074,SynArsC in PBS buffer,60820,17077
BMRB,17076,SynArsC in TRIS buffer,60820,17077
BMRB,17071,Cbx3 H3K9me3 complex,60860,17079
BMRB,17072,Cbx7 H3K9me3 complex,60860,17079
PDB,2L1B,BMRB Entry Tracking System,60860,17079
BMRB,17082,Prion Protein with 175A mutation,60909,17081
BMRB,17084,Prion Protein,60909,17081
BMRB,17087,"Prion Protein with Y169A, Y225A, Y226A mutation",60909,17081
PDB,2L1D,BMRB Entry Tracking System,60909,17081
BMRB,17081,Prion Protein with Y169G Mutation,60931,17082
BMRB,17084,Prion Protein,60931,17082
BMRB,17087,"Prion Protein with Y169A, Y225A, and Y226A mutation",60931,17082
PDB,2L1E,BMRB Entry Tracking System,60931,17082
PDB,2L1F,BMRB Entry Tracking System,60953,17083
BMRB,17081,Prion Protein with Mutation Y169G,60969,17084
BMRB,17082,Prion Protein with Mutation F175A,60969,17084
BMRB,17087,"Prion Protein with mutation Y169A, Y225A, and Y226A",60969,17084
PDB,2L1I,BMRB Entry Tracking System,60989,17085
PDB,1HYK,minimized human agouti related protein,61009,17086
PDB,1MR0,agouti-related protein,61009,17086
PDB,1Y7J,agouti signaling protein,61009,17086
PDB,1Y7K,agouti signaling protein,61009,17086
BMRB,17081,Prion Protein with Mutation Y169G,61027,17087
BMRB,17082,Prion Protein with Mutation F175A,61027,17087
BMRB,17084,Prion Protein,61027,17087
PDB,2L1K,BMRB Entry Tracking System,61027,17087
PDB,2kye,Solution structure of the pseudouridine modified P6.1 hairpin of human telomerase RNA,61049,17088
PDB,1TUC,"ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20",61074,17089
PDB,2JMC,Chimer between Spc-SH3 and P41,61074,17089
PDB,2KXD,BMRB Entry Tracking System,61074,17089
PDB,2L1N,BMRB Entry Tracking System,61102,17090
PDB,2L1O,BMRB Entry Tracking System,61122,17091
BMRB,7093,mMjCM in complex with a TSA,61164,17093
PDB,1dtl,CRYSTAL STRUCTURE OF CALCIUM-SATURATED (3CA2+) CARDIAC TROPONIN C COMPLEXED WITH THE CALCIUM SENSITIZER BEPRIDIL AT 2.15 A RESOLUTION,61367,17103
PDB,1lxf,Structure of the Regulatory N-domain of Human Cardiac Troponin C in Complex with Human Cardiac Troponin-I(147-163) and Bepridil,61367,17103
PDB,1wrk,Crystal structure of the N-terminal domain of human cardiac troponin C in complex with trifluoperazine (orthrombic crystal form),61367,17103
PDB,1ytz,Crystal structure of skeletal muscle troponin in the Ca2+-activated state,61367,17103
PDB,2kfx,Structure of the N-terminal domain of human cardiac troponin C bound to calcium ion and to the inhibitor W7,61367,17103
PDB,2krd,Solution Structure of the Regulatory Domain of Human Cardiac Troponin C in Complex with the Switch Region of cardiac Troponin I and W7,61367,17103
PDB,2L1R,BMRB Entry Tracking System,61367,17103
PDB,2L1S,BMRB Entry Tracking System,61387,17104
PDB,2L1T,BMRB Entry Tracking System,61405,17105
PDB,2L1V,BMRB Entry Tracking System,61424,17106
BMRB,17108,"ILE-A2-LEU, VAL-A3-LEU 2 HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO",61450,17107
PDB,2L1Y,BMRB Entry Tracking System,61450,17107
BMRB,17107,"GLY-B20-D-ALA, GLY-B23 2 PRO-B28-LYS, LYS-B29-PRO",61466,17108
PDB,2L1Z,BMRB Entry Tracking System,61466,17108
PDB,1GP0,Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur,61497,17110
PDB,2CNJ,NMR STUDIES ON THE INTERACTION OF INSULIN-GROWTH FACTOR II (IGF-II) WITH IGF2R DOMAIN 11,61497,17110
PDB,2L22,BMRB Entry Tracking System,61519,17111
BMRB,17113,PKC-delta C1A,61533,17112
BMRB,17112,C1B Subdomains of PKC-delta,61553,17113
PDB,1LUD,SOLUTION STRUCTURE OF L.CASEI DIHYDROFOLATE REDUCTASE COMPLEXED WITH TRIMETHOPRIM AND NADPH,61755,17125
PDB,1YHO,SOLUTION STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH TRIMETHOPRIM AND NADPH,61755,17125
PDB,2HM9,SOLUTION STRUCTURE OF L.CASEI DIHYDROFOLATE REDUCTASE COMPLEXED WITH TRIMETHOPRIM,61755,17125
PDB,2HQP,SOLUTION STRUCTURE OF L.CASEI DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH,61755,17125
PDB,2L28,BMRB Entry Tracking System,61755,17125
PDB,2L29,BMRB Entry Tracking System,61804,17127
PDB,1GP0,xray structure ofhuman IGF2R domain 11,61829,17128
PDB,2CNJ,solution structure of human IGF2R domain 11,61829,17128
BMRB,16249,NMR Assignment of the C-terminal domain of Araneus diadematus spider silk protein,61904,17131
PDB,2khm,Solution Structure of the C-terminal domain of Araneus diadematus spider silk protein,61904,17131
PDB,3lr2,Crystal Structure of the N-terminal domain of E. australis spider silk protein,61904,17131
PDB,1GP0,HUMAN IGF2R DOMAIN 11,61963,17134
PDB,2CNJ,NMR STUDIES ON THE INTERACTION OF INSULIN-GROWTH FACTOR II (IGF-II) WITH IGF2R DOMAIN 11,61963,17134
PDB,2L2L,BMRB Entry Tracking System,62029,17138
BMRB,17146,reduced forms of ApcA,62106,17144
BMRB,17147,Pitx2 homeodomain Wild-Type,62128,17145
PDB,2L7M,BMRB Entry Tracking System,62128,17145
BMRB,17144,oxidized (paramagnetic) form of ApcA,62144,17146
BMRB,17145,Pitx2 homeodomain R24H mutant,62166,17147
PDB,2L7F,BMRB Entry Tracking System,62166,17147
PDB,1SHF,Structure of the native Fyn SH3 domain from H. sapiens,62213,17149
PDB,3CQT,Structure of the native Fyn SH3 domain mutant N53I/V55L from G. gallus,62213,17149
PDB,2L2Q,BMRB Entry Tracking System,62246,17150
PDB,2L2R,BMRB Entry Tracking System,62288,17152
BMRB,17154,Thiostrepton (oxidized 9:CA-CB),62302,17153
BMRB,17155,Thiostrepton (epimer 9:CA),62302,17153
BMRB,17156,Thiostrepton (reduced 14:N-CA),62302,17153
PDB,1E9W,,62302,17153
PDB,2JQ7,,62302,17153
PDB,2L2W,BMRB Entry Tracking System,62302,17153
BMRB,17153,Thiostrepton,62327,17154
BMRB,17155,Thiostrepton (epimer 9:CA),62327,17154
BMRB,17156,Thiostrepton (reduced 14:N-CA),62327,17154
PDB,1E9W,,62327,17154
PDB,2JQ7,,62327,17154
PDB,2L2X,BMRB Entry Tracking System,62327,17154
BMRB,17153,Thiostrepton,62352,17155
BMRB,17154,Thiostrepton (oxidized 9:CA-CB),62352,17155
BMRB,17156,Thiostrepton (reduced 14:N-CA),62352,17155
PDB,1E9W,,62352,17155
PDB,2JQ7,,62352,17155
PDB,2L2Y,BMRB Entry Tracking System,62352,17155
BMRB,17153,Thiostrepton,62377,17156
BMRB,17154,Thiostrepton (oxidized 9:CA-CB),62377,17156
BMRB,17155,Thiostrepton (epimer 9:CA),62377,17156
PDB,1E9W,,62377,17156
PDB,2JQ7,,62377,17156
PDB,2L2Z,BMRB Entry Tracking System,62377,17156
BMRB,17158,PARP-1 Finger 2,62402,17157
PDB,2L30,BMRB Entry Tracking System,62402,17157
BMRB,17157,PARP-1 Finger 1,62421,17158
PDB,2L31,BMRB Entry Tracking System,62421,17158
PDB,2LHS,BMRB Entry Tracking System,62455,17160
PDB,2L9B,BMRB Entry Tracking System,62473,17161
BMRB,17163,photochromic fluorescent protein Dronpa in the dark state,62500,17162
BMRB,17163,photochromic fluorescent protein Dronpa in the bright state,62516,17163
BMRB,17166,"IMMUNGLOBULIN, RESIDUES 27-119",62532,17165
PDB,2XKS,BMRB Entry Tracking System,62532,17165
BMRB,17165,BETA2-MICROGLOBULIN,62560,17166
PDB,2XKU,BMRB Entry Tracking System,62560,17166
PDB,2LO6,BMRB Entry Tracking System,62675,17173
PDB,2L1D,MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTION Y169G,62692,17174
PDB,2L1E,MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTION F175A,62692,17174
PDB,2L1H,MOUSE PRION PROTEIN FRAGMENT 121-231 AT 20 C,62692,17174
PDB,2L1K,"MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTIONS Y169A, Y225A, AND Y226A",62692,17174
PDB,2L39,BMRB Entry Tracking System,62692,17174
PDB,2L3A,BMRB Entry Tracking System,62712,17175
PDB,2L3E,BMRB Entry Tracking System,62998,17188
BMRB,17190,RPP30/Pop5 complex,63027,17189
BMRB,17189,Free RPP30,63058,17190
PDB,2L3H,BMRB Entry Tracking System,63154,17193
PDB,2L3I,BMRB Entry Tracking System,63170,17194
BMRB,17362,E2-25K monomer,63187,17195
PDB,2L3M,BMRB Entry Tracking System,63207,17196
PDB,2L3N,BMRB Entry Tracking System,63225,17199
PDB,2L3R,BMRB Entry Tracking System,63256,17200
BMRB,16869,catalytic core of Dpo4,63284,17201
PDB,2L3T,BMRB Entry Tracking System,63301,17202
PDB,2L3V,BMRB Entry Tracking System,63315,17203
TargetDB,SnR168A,,63383,17207
BMRB,17209,NBD(1-388) (apo form),63420,17208
BMRB,17210,NBD(1-392) (ATP-bound state),63420,17208
BMRB,6229,Entry containing backbone chemical shift assignments for the NBD of thermus thermophilus DnaK,63420,17208
BMRB,17208,NBD(1-388) (ADP-bound state),63446,17209
BMRB,17210,NBD(1-392) (ATP-bound state),63446,17209
BMRB,6229,Entry containing backbone chemical shift assignments for the NBD of thermus thermophilus DnaK,63446,17209
BMRB,17208,NBD(1-388) (ADP-bound state),63466,17210
BMRB,17209,NBD(1-388) (apo form),63466,17210
BMRB,6229,Entry containing backbone chemical shift assignments for the NBD of thermus thermophilus DnaK,63466,17210
BMRB,17081,Mouse prion protein (121-231) with the mutation Y169G,63526,17213
BMRB,17082,Mouse prion protein (121-231) with the mutation F175A,63526,17213
BMRB,17084,Mouse prion protein (121-231) at 20 C degrees,63526,17213
BMRB,17087,"Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A",63526,17213
BMRB,17174,Mouse prion protein (121-231) at 37 C degrees,63526,17213
PDB,2l1d,Mouse prion protein (121-231) with the mutation Y169G,63526,17213
PDB,2l1e,Mouse prion protein (121-231) with the mutation F175A,63526,17213
PDB,2l1h,Mouse prion protein (121-231) at 20 C degrees,63526,17213
PDB,2l1k,"Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A",63526,17213
PDB,2l39,Mouse prion protein (121-231) at 37 C degrees,63526,17213
PDB,2L40,BMRB Entry Tracking System,63526,17213
BMRB,17229,ZNF_DNA,63815,17228
BMRB,17230,ZNF-PtDNA,63815,17228
PDB,2L44,BMRB Entry Tracking System,63815,17228
BMRB,17228,ZNF,63833,17229
BMRB,17230,ZNF-PtDNA,63833,17229
PDB,2L45,BMRB Entry Tracking System,63833,17229
BMRB,17233,PlyG,63879,17232
PDB,2L47,BMRB Entry Tracking System,63879,17232
BMRB,17232,PlyG (E.C.3.5.1.28),63900,17233
PDB,2L48,BMRB Entry Tracking System,63900,17233
PDB,2L4A,BMRB Entry Tracking System,63919,17234
PDB,2L4B,BMRB Entry Tracking System,63938,17235
PDB,2KMZ,BMRB Entry Tracking System,63981,17237
BMRB,17239,UBA+Ub complex,63997,17238
PDB,2L4E,BMRB Entry Tracking System,63997,17238
PDB,3BQ3,Crystal structure of full-length Dcn1,63997,17238
BMRB,17238,UBA,64020,17239
PDB,2L4F,BMRB Entry Tracking System,64020,17239
PDB,3BQ3,Crystal structure of full-length Dcn1,64020,17239
PDB,1IBN,HA fusion peptide WT,64055,17240
PDB,1XOO,HA fusion peptide G1S,64055,17240
PDB,1XOP,HA fusion peptide G1V,64055,17240
PDB,2JRD,HA fusion peptide F9A,64055,17240
PDB,2L4G,BMRB Entry Tracking System,64055,17240
PDB,2L4J,BMRB Entry Tracking System,64073,17241
BMRB,17268,"Thioredoxin C, oxidized form",64090,17242
PDB,2L4Q,BMRB Entry Tracking System,64090,17242
PDB,2KDH,BMRB Entry Tracking System,64109,17243
PDB,2L4N,BMRB Entry Tracking System,64150,17245
PDB,2L4O,BMRB Entry Tracking System,64168,17246
PDB,2kmz,human Fn14 solution NMR structure,64198,17247
PDB,2KN0,BMRB Entry Tracking System,64198,17247
BMRB,17247,xenopus Fn14,64277,17252
PDB,2kmz,human Fn14 solution NMR structure,64277,17252
PDB,2kn0,xenopus Fn14 solution NMR structure,64277,17252
PDB,2KN1,BMRB Entry Tracking System,64277,17252
BMRB,17255,GIP/Glutaminase L peptide complex,64310,17254
PDB,2L4S,BMRB Entry Tracking System,64310,17254
BMRB,17254,GIP apo,64327,17255
PDB,214S,,64327,17255
PDB,2L4T,BMRB Entry Tracking System,64327,17255
PDB,2L4U,BMRB Entry Tracking System,64345,17256
PDB,2L4W,BMRB Entry Tracking System,64359,17257
PDB,3OV5,Entry containing the x-ray crystal structure for the XAC2622 globular domain,64359,17257
PDB,2L4V,,64385,17258
BMRB,16537,UCH-L1,64417,17260
PDB,2LEN,BMRB Entry Tracking System,64417,17260
BMRB,17262,Calcium bound S100A16,64432,17261
PDB,2L50,BMRB Entry Tracking System,64432,17261
BMRB,17261,APO S100A16,64457,17262
PDB,2L51,BMRB Entry Tracking System,64457,17262
PDB,2L52,BMRB Entry Tracking System,64484,17263
PDB,2ix7,,64512,17264
PDB,2L53,BMRB Entry Tracking System,64512,17264
PDB,1M3V,,64533,17265
PDB,1RUT,,64533,17265
PDB,2L4Z,BMRB Entry Tracking System,64533,17265
PDB,2L55,BMRB Entry Tracking System,64558,17266
PDB,2L57,BMRB Entry Tracking System,64586,17267
TargetDB,NYSGXRC-11217h,,64586,17267
BMRB,17242,"Thioredoxin C, reduced form",64603,17268
PDB,2L59,BMRB Entry Tracking System,64603,17268
PDB,2L5E,BMRB Entry Tracking System,64634,17270
PDB,2L5G,BMRB Entry Tracking System,64652,17271
BMRB,17273,human PIWI-like 1 PAZ domain with ssRNA (5'-pUGACA),64673,17272
PDB,2L5C,BMRB Entry Tracking System,64673,17272
BMRB,17272,human PIWI-like 1 PAZ domain,64696,17273
PDB,2L5D,BMRB Entry Tracking System,64696,17273
PDB,2L5L,BMRB Entry Tracking System,64751,17275
TargetDB,NYSGXRC-11218b,,64751,17275
PDB,2L5O,BMRB Entry Tracking System,64782,17277
TargetDB,NYSGXRC-11210e,,64782,17277
PDB,2L5P,BMRB Entry Tracking System,64816,17279
PDB,2L5R,BMRB Entry Tracking System,64875,17281
PDB,1R9P,Solution structure of Zn-bound IscU,64892,17282
PDB,2KQK,Solution structure of apo-IscU(D39A),64892,17282
PDB,2L4X,BMRB Entry Tracking System,64892,17282
PDB,2Z7E,Solution structure of holo-IscU,64892,17282
PDB,3LVL,Complex crystal structure of IscU and IscS,64892,17282
PDB,2LJ6,BMRB Entry Tracking System,64918,17283
PDB,2L5T,BMRB Entry Tracking System,64937,17284
PDB,2L5V,BMRB Entry Tracking System,64974,17286
BMRB,7131,Solution structure of IGF2R domain 11,64988,17287
PDB,2CNJ,NMR STUDIES ON THE INTERACTION OF INSULIN-GROWTH FACTOR II (IGF-II) WITH IGF2R DOMAIN 11,64988,17287
PDB,2LLA,BMRB Entry Tracking System,64988,17287
PDB,2MF2,BMRB Entry Tracking System,65010,17288
PDB,2L5Y,BMRB Entry Tracking System,65025,17289
PDB,2L5Z,BMRB Entry Tracking System,65093,17292
BMRB,17295,g-Ec-1 with Zn,65143,17294
PDB,2L61,BMRB Entry Tracking System,65143,17294
BMRB,17294,g-Ec-1 with Cd,65163,17295
PDB,2L62,BMRB Entry Tracking System,65163,17295
BMRB,17297,GLP-2 in DHPC micelles,65183,17296
PDB,2L63,BMRB Entry Tracking System,65183,17296
BMRB,17296,"GLP-2 in 2,2,2 trifluroethanol",65197,17297
PDB,2L64,BMRB Entry Tracking System,65197,17297
PDB,2MDT,BMRB Entry Tracking System,65211,17298
BMRB,17300,reduced thioredoxin,65226,17299
BMRB,17299,oxidized thioredoxin,65240,17300
BMRB,15429,rat apo L-FABP assignment,65271,17302
BMRB,15433,rat holo L-FABP assignment,65271,17302
BMRB,17303,human apo L-FABP assignment,65271,17302
PDB,1LFO,rat holo L-FABP X-ray structure,65271,17302
PDB,2F73,human L-FABP X-ray structure,65271,17302
PDB,2JU3,rat apo L-FABP solution structure,65271,17302
PDB,2JU7,rat holo L-FABP solution structure,65271,17302
PDB,2L67,BMRB Entry Tracking System,65271,17302
PDB,2PY1,human L-FABP solution structure,65271,17302
BMRB,15429,rat apo L-FABP assignment,65291,17303
BMRB,15433,rat holo L-FABP assignment,65291,17303
BMRB,17302,human apo L-FABP assignment,65291,17303
PDB,1LFO,rat holo L-FABP X-ray structure,65291,17303
PDB,2F73,human L-FABP X-ray structure,65291,17303
PDB,2JU3,rat apo L-FABP solution structure,65291,17303
PDB,2JU7,rat holo L-FABP solution structure,65291,17303
PDB,2LKK,BMRB Entry Tracking System,65291,17303
PDB,2PY1,human L-FABP solution structure,65291,17303
PDB,2L69,BMRB Entry Tracking System,65311,17304
PDB,2L6A,BMRB Entry Tracking System,65338,17305
PDB,2L6B,BMRB Entry Tracking System,65358,17306
PDB,2L6E,BMRB Entry Tracking System,65383,17307
PDB,2L6I,BMRB Entry Tracking System,65425,17309
BMRB,17125,Chemical shifts of apo-lcDHFR,65446,17310
BMRB,17311,Chemical shifts of lcDHFR-NDP complex,65446,17310
BMRB,5396,Chemical shifts of lcDHFR-TMP-NADPH complex,65446,17310
PDB,1LUD,Solution structure of lcDHFR-TMP-NADPH complex,65446,17310
PDB,2HM9,Solution structure of this complex,65446,17310
PDB,2HQP,Solution structure of lcDHFR-NADPH complex,65446,17310
PDB,2L28,Solution structure of apo-lcDHFR,65446,17310
BMRB,17125,Chemical shifts of apo-lcDHFR,65471,17311
BMRB,17310,Chemical shifts of lcDHFR-TRR complex,65471,17311
BMRB,5396,Chemical shifts of lcDHFR-TMP-NADPH complex,65471,17311
PDB,1LUD,Solution structure of lcDHFR-TMP-NADPH complex,65471,17311
PDB,2HM9,Solution structure of lcDHFR-TMP complex,65471,17311
PDB,2HQP,Solution structure of this complex,65471,17311
PDB,2L28,Solution structure of apo-lcDHFR,65471,17311
PDB,2L6K,BMRB Entry Tracking System,65538,17314
PDB,2L6M,BMRB Entry Tracking System,65552,17315
PDB,2KZL,BMRB Entry Tracking System,65575,17316
PDB,2L6N,BMRB Entry Tracking System,65591,17318
PDB,2L6P,BMRB Entry Tracking System,65610,17319
PDB,2L6O,BMRB Entry Tracking System,65629,17320
BMRB,17322,(W protein of bacteriophage lambda) at acidic pH,65648,17321
PDB,2L6Q,BMRB Entry Tracking System,65648,17321
BMRB,17321,(W protein of bacteriophage lambda) at neutral pH,65665,17322
PDB,2L6R,BMRB Entry Tracking System,65665,17322
PDB,2MC3,BMRB Entry Tracking System,65711,17324
BMRB,17559,Assignment of the stem loop 2 of RsmZ,65749,17326
BMRB,17560,Assignment of the stem loop 4 of RsmZ,65749,17326
BMRB,17566,22 nt artificial stemloop TASL1,65749,17326
BMRB,17567,26 nt artificial stemloop TASL2,65749,17326
BMRB,17568,30 nt artificial stemloop TASL3,65749,17326
BMRB,17329,calcium bound CIB1,65786,17328
PDB,1XO5,crystal str. of Ca-CIB1,65786,17328
PDB,2L4I,solution str. of Ca-CIB1,65786,17328
BMRB,17328,magnesium bound CIB1,65806,17329
PDB,1XO5,crystal structure of CIB1,65806,17329
PDB,1Y1A,crystal structure of CIB1,65806,17329
PDB,2L4H,BMRB Entry Tracking System,65806,17329
BMRB,17331,Solution structure of GIP in bicellular media,65825,17330
PDB,1T5Q,Solution structure of GIP(1-30) amide in TFE/Water,65825,17330
PDB,2B4N,Solution structure of GIP,65825,17330
PDB,2L70,BMRB Entry Tracking System,65825,17330
PDB,2OBU,Solution structure of GIP in TFE/Water,65825,17330
BMRB,17331,Solution structure of GIP in micellular media,65841,17331
PDB,1T5Q,Solution structure of GIP(1-30) amide in TFE/Water,65841,17331
PDB,2B4N,Solution structure of GIP,65841,17331
PDB,2L71,BMRB Entry Tracking System,65841,17331
PDB,2OBU,Solution structure of GIP in TFE/Water,65841,17331
BMRB,16749,Noxo1b PX domain,65994,17343
PDB,2L73,BMRB Entry Tracking System,65994,17343
PDB,2L75,BMRB Entry Tracking System,66010,17344
BMRB,17347,PAP248-286 in 30% TFE,66061,17346
PDB,2L77,BMRB Entry Tracking System,66061,17346
BMRB,17346,PAP248-286 in 50% TFE,66080,17347
PDB,2L79,BMRB Entry Tracking System,66080,17347
PDB,1SJ8,Structure of the VBS1-VBS2A domains of talin,66099,17350
PDB,2L7D,BMRB Entry Tracking System,66116,17351
PDB,2L7E,BMRB Entry Tracking System,66136,17352
BMRB,17354,high calcium androcam,66152,17353
PDB,2LMT,BMRB Entry Tracking System,66152,17353
BMRB,17353,high calcium androcam,66170,17354
PDB,2LMV,BMRB Entry Tracking System,66170,17354
PDB,2L9F,BMRB Entry Tracking System,66188,17355
PDB,2L7C,BMRB Entry Tracking System,66206,17356
PDB,2L7J,BMRB Entry Tracking System,66240,17358
BMRB,5286,Backbone assignments of CaM:CaMKIp complex,66307,17360
PDB,1MXE,X-ray structure of Ca2+/CaM bound to CaMKIp,66307,17360
PDB,2L7L,BMRB Entry Tracking System,66307,17360
BMRB,17195,UBA Domain of E2-25K,66354,17362
PDB,3E46,Crystal stucture of E2-25K,66354,17362
PDB,3F92,Crystal stucture of E2-25K,66354,17362
PDB,2L7N,BMRB Entry Tracking System,66371,17363
PDB,2L7P,BMRB Entry Tracking System,66414,17365
BMRB,17369,MS2 (bound form),66448,17368
PDB,1AOT,,66448,17368
PDB,1G83,,66448,17368
BMRB,17368,MS2 (free form),66465,17369
PDB,1AOT,,66465,17369
PDB,2L7R,BMRB Entry Tracking System,66542,17371
PDB,2LJ8,BMRB Entry Tracking System,66581,17374
BMRB,15501,human PCNA trimer,66595,17375
BMRB,17376,hPCNA trimer Complexed with a 12 Amino Acids Peptide,66595,17375
PDB,1AXC,,66595,17375
PDB,1U76,,66595,17375
PDB,1U7B,,66595,17375
PDB,1UL1,,66595,17375
PDB,1VYJ,,66595,17375
PDB,1VYM,,66595,17375
PDB,1W60,,66595,17375
PDB,2ZVK,,66595,17375
PDB,2ZVL,,66595,17375
PDB,2ZVM,,66595,17375
BMRB,15501,human PCNA trimer,66613,17376
BMRB,17375,hPCNA trimer Complexed with a 20 Amino Acids Peptide,66613,17376
PDB,1AXC,,66613,17376
PDB,1U76,,66613,17376
PDB,1U7B,,66613,17376
PDB,1UL1,,66613,17376
PDB,1VYJ,,66613,17376
PDB,1VYM,,66613,17376
PDB,1W60,,66613,17376
PDB,2ZVK,,66613,17376
PDB,2ZVL,,66613,17376
PDB,2ZVM,,66613,17376
PDB,2L7T,BMRB Entry Tracking System,66631,17377
PDB,3PVL,MyTH4-FERM-SH3/CEN1 complex,66631,17377
PDB,2L7V,BMRB Entry Tracking System,66668,17379
PDB,2L7Y,BMRB Entry Tracking System,66705,17381
PDB,2L7X,BMRB Entry Tracking System,66737,17383
PDB,2OIQ,crystal structure of SrcKD in complex with Imatinib,66758,17384
PDB,2L80,BMRB Entry Tracking System,66842,17388
PDB,2L81,BMRB Entry Tracking System,66862,17389
PDB,2L82,BMRB Entry Tracking System,66918,17390
PDB,2L83,BMRB Entry Tracking System,66955,17391
PDB,2L84,BMRB Entry Tracking System,66971,17392
PDB,2L85,BMRB Entry Tracking System,66999,17393
PDB,2L86,BMRB Entry Tracking System,67027,17394
PDB,2L87,BMRB Entry Tracking System,67046,17395
PDB,2L8E,BMRB Entry Tracking System,67063,17396
PDB,2F8U,,67084,17397
PDB,2L88,BMRB Entry Tracking System,67084,17397
PDB,2L89,BMRB Entry Tracking System,67102,17398
PDB,2L8A,BMRB Entry Tracking System,67118,17399
PDB,3PZT,Structure of the catalytic domain of cellulase 5A from Bacillus subtilis 168 in complex with maganese(II) ion,67118,17399
PDB,3PZU,P212121 crystal form of the catalytic domain of cellulase 5A from Bacillus subtilis 168,67118,17399
PDB,3PZV,C2 crystal form of the catalytic domain of cellulase 5A from Bacillus subtilis 168,67118,17399
BMRB,17413,Complex with L-tryptophan,67138,17400
PDB,2L8U,BMRB Entry Tracking System,67153,17401
PDB,2L8W,BMRB Entry Tracking System,67153,17401
PDB,2L8D,BMRB Entry Tracking System,67169,17402
PDB,3ZUA,BMRB Entry Tracking System,67191,17403
PDB,4AKA,BMRB Entry Tracking System,67231,17405
PDB,2L8F,BMRB Entry Tracking System,67246,17406
PDB,2LP0,BMRB Entry Tracking System,67269,17407
PDB,2L8H,BMRB Entry Tracking System,67293,17408
PDB,2L8I,BMRB Entry Tracking System,67315,17409
PDB,2L8J,BMRB Entry Tracking System,67370,17412
BMRB,17400,protein of apo form,67396,17413
PDB,2L8L,BMRB Entry Tracking System,67412,17414
BMRB,5759,oxidized CYP101A1,67428,17415
PDB,2LQD,BMRB Entry Tracking System,67428,17415
PDB,3CPP,reduced and CO-bound CYP101A1,67428,17415
PDB,2LCJ,BMRB Entry Tracking System,67485,17418
PDB,2L8N,BMRB Entry Tracking System,67505,17419
PDB,2L8O,BMRB Entry Tracking System,67525,17420
BMRB,15593,unbound C6orf130,67541,17421
PDB,2JYC,unbound C6orf130,67541,17421
PDB,2L8R,BMRB Entry Tracking System,67541,17421
BMRB,17423,DNA duplex,67562,17422
PDB,2L8P,BMRB Entry Tracking System,67562,17422
BMRB,17422,CDV DNA duplex,67584,17423
PDB,2L8P,CDV DNA duplex,67584,17423
PDB,2L8Q,BMRB Entry Tracking System,67584,17423
PDB,2L8S,BMRB Entry Tracking System,67605,17424
PDB,2L8T,BMRB Entry Tracking System,67622,17425
PDB,2L8V,BMRB Entry Tracking System,67687,17429
PDB,2L8X,BMRB Entry Tracking System,67732,17430
PDB,2L8Y,BMRB Entry Tracking System,67751,17431
PDB,2L90,BMRB Entry Tracking System,67771,17432
PDB,2L91,BMRB Entry Tracking System,67787,17433
BMRB,17435,C-terminal domain of Salmonella H-NS,67801,17434
PDB,2L92,BMRB Entry Tracking System,67801,17434
PDB,2L93,C-terminal domain of Salmonella H-NS,67801,17434
BMRB,17434,C-terminal domain of H-NS like protein Bv3F,67815,17435
PDB,2L92,C-terminal domain of H-NS like protein Bv3F,67815,17435
PDB,2L93,BMRB Entry Tracking System,67815,17435
PDB,1Z2J,RNA structure with no ligand bound,67829,17436
PDB,2L94,BMRB Entry Tracking System,67829,17436
BMRB,17441,LAK160-P12,67878,17438
BMRB,17442,LAK160-P710,67878,17438
PDB,2L96,BMRB Entry Tracking System,67878,17438
PDB,2L99,LAK160-P710,67878,17438
PDB,2L9A,LAK160-P12,67878,17438
PDB,2kdh,,67927,17440
PDB,2L98,BMRB Entry Tracking System,67927,17440
BMRB,17438,LAK10-P7,67952,17441
BMRB,17442,LAK160-P712,67952,17441
PDB,2l96,LAK10-P7,67952,17441
PDB,2L99,BMRB Entry Tracking System,67952,17441
BMRB,17438,LAK160-P7,67972,17442
BMRB,17441,LAK160-P710,67972,17442
PDB,2l96,LAK160-P7,67972,17442
PDB,2l99,LAK160-P710,67972,17442
PDB,2L9A,BMRB Entry Tracking System,67972,17442
PDB,2Y4W,BMRB Entry Tracking System,67992,17443
PDB,2L9D,BMRB Entry Tracking System,68074,17448
PDB,2L9E,BMRB Entry Tracking System,68093,17449
PDB,2L9G,BMRB Entry Tracking System,68130,17450
PDB,2L9J,BMRB Entry Tracking System,68146,17451
BMRB,17145,Pitx2 homeodomain R24H,68170,17452
BMRB,17147,Pitx2 homeodomain,68170,17452
PDB,1u4l,oligomer structure based on the dimer,68189,17453
PDB,2L9H,BMRB Entry Tracking System,68189,17453
BMRB,17454,chemical shift data for wild type PMP22,68223,17455
PDB,2LAU,BMRB Entry Tracking System,68238,17456
PDB,2L9I,BMRB Entry Tracking System,68274,17458
BMRB,6468,p38 mitogen-activated protein kinase,68497,17471
PDB,1P38,,68497,17471
PDB,2Y9T,BMRB Entry Tracking System,68559,17475
PDB,2L9L,BMRB Entry Tracking System,68591,17477
PDB,2L9M,BMRB Entry Tracking System,68609,17478
PDB,2L9N,BMRB Entry Tracking System,68632,17479
PDB,2L9P,BMRB Entry Tracking System,68659,17481
BMRB,17483,Hsp12 in aqueous solution,68686,17482
PDB,2L9Q,BMRB Entry Tracking System,68686,17482
BMRB,17482,Hsp12 (in SDS micelles),68706,17483
PDB,2L9R,BMRB Entry Tracking System,68725,17484
PDB,2L9S,BMRB Entry Tracking System,68758,17485
PDB,2L9U,BMRB Entry Tracking System,68788,17488
PDB,2L9V,BMRB Entry Tracking System,68806,17489
BMRB,16230,Prp24-2 + RNA,68827,17490
BMRB,16243,Prp24-23,68827,17490
BMRB,16244,Prp24-23 + RNA,68827,17490
BMRB,16246,Prp24-2,68827,17490
BMRB,7070,Prp24-12,68827,17490
PDB,2ghp,Prp24-123,68827,17490
PDB,2go9,Prp24-12,68827,17490
PDB,2kh9,Prp24-2 + RNA,68827,17490
PDB,2L9W,BMRB Entry Tracking System,68827,17490
BMRB,16230,Prp24-2 + RNA,68855,17491
BMRB,16243,Prp24-23,68855,17491
BMRB,16244,Prp24-23 + RNA,68855,17491
BMRB,16246,Prp24-2,68855,17491
BMRB,17490,Prp24-L4W,68855,17491
BMRB,7070,Prp24-12,68855,17491
PDB,2ghp,Prp24-123,68855,17491
PDB,2go9,Prp24-12,68855,17491
PDB,2kh9,Prp24-2 + RNA,68855,17491
PDB,2l9w,Prp24-L4W,68855,17491
BMRB,17495,Thuricin CD,68873,17492
PDB,2L9X,BMRB Entry Tracking System,68873,17492
PDB,2L9Y,BMRB Entry Tracking System,68891,17493
PDB,2L9Z,BMRB Entry Tracking System,68913,17494
BMRB,17492,Thuricin CD,68933,17495
PDB,2LA0,BMRB Entry Tracking System,68933,17495
PDB,1YWU,apo PA4608,68950,17496
PDB,2L74,holo PA4608,68950,17496
PDB,3KYF,holo PP4397,68950,17496
PDB,1G6W,,69010,17499
PDB,1G6Y,,69010,17499
PDB,2LA2,BMRB Entry Tracking System,69025,17500
PDB,2LA3,BMRB Entry Tracking System,69040,17501
PDB,2LA4,BMRB Entry Tracking System,69059,17502
PDB,2LA5,BMRB Entry Tracking System,69105,17504
PDB,2LA6,BMRB Entry Tracking System,69186,17508
PDB,2LA7,BMRB Entry Tracking System,69213,17509
PDB,2LZN,BMRB Entry Tracking System,69285,17512
BMRB,3394,Jun leucine zipper domain,69324,17514
PDB,1JUN,,69324,17514
PDB,2H7H,,69324,17514
PDB,2LA8,BMRB Entry Tracking System,69341,17515
BMRB,17520,unmodified  ASL_Tyr,69363,17517
BMRB,17572,i6A37 tyrASL,69363,17517
BMRB,17573,Conformation Effects of Base Modification on the Anticodon Stem-loop of Bacillus subtilis tRNATYR,69363,17517
PDB,2LA9,BMRB Entry Tracking System,69363,17517
BMRB,17519,CBM25-2 of beta/alpha-amylase,69381,17518
PDB,2LAA,BMRB Entry Tracking System,69381,17518
BMRB,17518,Starch Binding Domain 1 of beta/alpha-amylase,69398,17519
PDB,2LAB,BMRB Entry Tracking System,69398,17519
BMRB,17517,Pseudouridine ASL_Tyr,69429,17520
BMRB,17572,i6A37 tyrASL,69429,17520
BMRB,17573,Conformation Effects of Base Modification on the Anticodon Stem-loop of Bacillus subtilis tRNATYR,69429,17520
PDB,2LAC,BMRB Entry Tracking System,69429,17520
PDB,2LAE,BMRB Entry Tracking System,69446,17521
PDB,2LNC,BMRB Entry Tracking System,69467,17523
PDB,2LAH,BMRB Entry Tracking System,69493,17524
PDB,2LAI,BMRB Entry Tracking System,69520,17525
BMRB,15312,NusB from Aquifex Aeolicus,69542,17526
BMRB,4737,Transcriptional Antiterminator NusB,69542,17526
PDB,1EY1,,69542,17526
PDB,2JR0,,69542,17526
PDB,3r2c,,69542,17526
PDB,2RR0,,69559,17527
PDB,2RR2,,69559,17527
PDB,2RR0,,69577,17528
PDB,2RR2,,69577,17528
PDB,2LAJ,BMRB Entry Tracking System,69593,17529
PDB,2LAK,BMRB Entry Tracking System,69614,17530
PDB,2LAM,BMRB Entry Tracking System,69642,17531
PDB,2LAP,BMRB Entry Tracking System,69660,17532
PDB,2LAQ,BMRB Entry Tracking System,69679,17533
PDB,2LVL,BMRB Entry Tracking System,69699,17534
PDB,2LAR,BMRB Entry Tracking System,69722,17535
PDB,2ASQ,SUMO-SIM complex,69745,17536
PDB,2LAS,BMRB Entry Tracking System,69745,17536
PDB,2LAT,BMRB Entry Tracking System,69765,17537
BMRB,17539,first WW domain of human YAP in complex with a human Smad1 doubly-phosphorilated derived peptide,69781,17538
BMRB,17540,first domain of human Yap in complex with a human Smad1 derived peptide,69781,17538
PDB,2LAW,BMRB Entry Tracking System,69781,17538
BMRB,17538,second WW domain from human YAP in complex with a human Smad1 derived peptide,69801,17539
BMRB,17540,first domain of human Yap in complex with a human Smad1 derived peptide,69801,17539
PDB,2LAX,BMRB Entry Tracking System,69801,17539
BMRB,17538,second WW domain from human YAP in complex with a human Smad1 derived peptide,69823,17540
BMRB,17539,first WW domain of human YAP in complex with a human Smad1 doubly-phosphorilated derived peptide,69823,17540
PDB,2LAY,BMRB Entry Tracking System,69823,17540
BMRB,17542,first domain of human Smurf1 in complex with a doubly phosphorylated human Smad1 derived peptide,69843,17541
BMRB,17543,first domain of human Smurf1 in complex with a human Smad1 derived peptide,69843,17541
PDB,2LAZ,BMRB Entry Tracking System,69843,17541
BMRB,17541,first domain of human Smurf1 in complex with a phosphorylated human Smad1 derived peptide,69864,17542
BMRB,17543,first domain of human Smurf1 in complex with a human Smad1 derived peptide,69864,17542
PDB,2LB0,BMRB Entry Tracking System,69864,17542
BMRB,17541,first domain of human Smurf1 in complex with a phosphorylated human Smad1 derived peptide,69885,17543
BMRB,17542,first domain of human Smurf1 in complex with a doubly phosphorylated human Smad1 derived peptide,69885,17543
PDB,2LB1,BMRB Entry Tracking System,69885,17543
BMRB,17545,first domain human PIN1 in complex with a human Smad3 derived peptide,69905,17544
PDB,2LB2,BMRB Entry Tracking System,69905,17544
BMRB,17544,second domain of human Nedd4L in complex with a doubly phosphorylated human Smad3 derived peptide,69926,17545
PDB,2LB3,BMRB Entry Tracking System,69926,17545
PDB,2LB5,BMRB Entry Tracking System,69947,17546
PDB,2LB7,BMRB Entry Tracking System,69963,17547
PDB,2LBA,BMRB Entry Tracking System,70013,17551
PDB,2LBB,BMRB Entry Tracking System,70054,17553
PDB,2LBC,BMRB Entry Tracking System,70076,17554
PDB,1SJ7,Structure of VBS1,70095,17555
PDB,2LBF,BMRB Entry Tracking System,70126,17557
PDB,2LBG,BMRB Entry Tracking System,70141,17558
BMRB,17326,20 nt RNA stem loop,70161,17559
BMRB,17560,Assignment of the stem loop 4 of RsmZ,70161,17559
BMRB,17566,22 nt artificial stemloop TASL1,70161,17559
BMRB,17567,26 nt artificial stemloop TASL2,70161,17559
BMRB,17568,30 nt artificial stemloop TASL2,70161,17559
BMRB,17326,20 nt RNA stem loop,70192,17560
BMRB,17559,Assignment of the stem loop 2 of RsmZ,70192,17560
BMRB,17566,22 nt artificial stemloop TASL1,70192,17560
BMRB,17567,26 nt artificial stemloop TASL2,70192,17560
BMRB,17568,30 nt artificial stemloop TASL2,70192,17560
PDB,2LBH,BMRB Entry Tracking System,70210,17561
PDB,2LBI,BMRB Entry Tracking System,70233,17562
BMRB,17564,Glycyl-tRNA(UCC)1B anticodon stem-loop,70251,17563
BMRB,17565,Unmodified Glycyl-tRNA(UCC) anticodon stem-loop,70251,17563
PDB,2LBJ,BMRB Entry Tracking System,70251,17563
BMRB,17563,Glycyl-tRNA(GCC) anticodon stem-loop,70268,17564
BMRB,17565,Unmodified Glycyl-tRNA(UCC) anticodon stem-loop,70268,17564
PDB,2LBK,BMRB Entry Tracking System,70268,17564
BMRB,17563,Glycyl-tRNA(GCC) anticodon stem-loop,70285,17565
BMRB,17564,Glycyl-tRNA(UCC)1B anticodon stem-loop,70285,17565
PDB,2LBL,BMRB Entry Tracking System,70285,17565
BMRB,17326,20 nt RNA stem loop,70302,17566
BMRB,17559,Assignment of the stem loop 2 of RsmZ,70302,17566
BMRB,17560,Assignment of the stem loop 4 of RsmZ,70302,17566
BMRB,17567,26 nt artificial stemloop TASL2,70302,17566
BMRB,17568,30 nt artificial stemloop TASL3,70302,17566
BMRB,17326,20 nt RNA stem loop,70318,17567
BMRB,17559,Assignment of the stem loop 2 of RsmZ,70318,17567
BMRB,17560,Assignment of the stem loop 4 of RsmZ,70318,17567
BMRB,17566,22 nt artificial stemloop TASL1,70318,17567
BMRB,17568,30 nt artificial stemloop TASL3,70318,17567
BMRB,17326,20 nt RNA stem loop,70335,17568
BMRB,17559,Assignment of the stem loop 2 of RsmZ,70335,17568
BMRB,17560,Assignment of the stem loop 4 of RsmZ,70335,17568
BMRB,17566,22 nt artificial stemloop TASL1,70335,17568
BMRB,17567,26 nt artificial stemloop TASL2,70335,17568
PDB,2LBM,BMRB Entry Tracking System,70350,17569
BMRB,17499,C-terminal domain of Ure2p in microcrystals,70386,17570
PDB,1G6Y,C-terminal domain x-ray structure,70386,17570
BMRB,17561,Unliganded Bovine Neurophysin,70401,17571
PDB,2LBN,BMRB Entry Tracking System,70401,17571
BMRB,17517,Pseudouridine ASL_Tyr,70422,17572
BMRB,17520,unmodified ASL_Tyr,70422,17572
BMRB,17573,Conformation Effects of Base Modification on the Anticodon Stem-loop of Bacillus subtilis tRNATYR,70422,17572
PDB,2LBQ,BMRB Entry Tracking System,70422,17572
BMRB,17517,Pseudouridine ASL_Tyr,70441,17573
BMRB,17520,unmodified ASL_Tyr,70441,17573
BMRB,17572,i6A37 tyrASL,70441,17573
PDB,2LBR,BMRB Entry Tracking System,70441,17573
PDB,1T4L,,70461,17574
PDB,2LBS,BMRB Entry Tracking System,70461,17574
PDB,2LBT,BMRB Entry Tracking System,70487,17575
BMRB,17582,cataract-related variant (gamma)S-G18V,70501,17576
PDB,2M3T,BMRB Entry Tracking System,70501,17576
PDB,2LBV,BMRB Entry Tracking System,70519,17577
BMRB,17579,H/ACA RNP protein Nhp2p,70539,17578
PDB,2LBW,BMRB Entry Tracking System,70539,17578
BMRB,17578,H/ACA RNP protein Nhp2p-S82W mutant,70562,17579
PDB,2LBX,BMRB Entry Tracking System,70562,17579
PDB,2LBY,BMRB Entry Tracking System,70585,17580
BMRB,17576,wild-type human (gamma)S-crystallin,70619,17582
PDB,2M3U,BMRB Entry Tracking System,70619,17582
PDB,2LBZ,BMRB Entry Tracking System,70638,17583
PDB,2LMA,BMRB Entry Tracking System,70658,17584
BMRB,17586,Rv0020c_FHA Structure,70675,17585
PDB,2LC0,BMRB Entry Tracking System,70675,17585
BMRB,17585,Rv0020c_Nter structure,70694,17586
PDB,2LC1,BMRB Entry Tracking System,70694,17586
PDB,2LC2,BMRB Entry Tracking System,70713,17588
BMRB,16230,Prp24-2 + RNA,70731,17589
BMRB,16243,Prp24-23,70731,17589
BMRB,16244,Prp24-23 + RNA,70731,17589
BMRB,16246,Prp24-2,70731,17589
BMRB,17490,Prp24-L4W,70731,17589
BMRB,17491,Prp24-L4C,70731,17589
BMRB,7070,Prp24-12,70731,17589
PDB,2ghp,Prp24-123,70731,17589
PDB,2go9,Prp24-12,70731,17589
PDB,2kh9,Prp24-2 + RNA,70731,17589
PDB,2l9w,Prp24-L4W,70731,17589
BMRB,17591,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with F-tails,70749,17590
BMRB,17592,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with DNA,70749,17590
BMRB,17590,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with D-tails,70766,17591
BMRB,17592,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with DNA,70766,17591
BMRB,17590,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with D-tails,70783,17592
BMRB,17591,Backbone assignments of Anabaena Sensory Rhodopsin Transducer with F-tails,70783,17592
PDB,2LC3,BMRB Entry Tracking System,70826,17594
PDB,2LCQ,BMRB Entry Tracking System,70850,17595
PDB,2LSH,BMRB Entry Tracking System,70876,17596
PDB,2LC4,BMRB Entry Tracking System,70914,17598
BMRB,17600,Solution structure of the isolated Par-6 PDZ domain,70933,17599
PDB,2LC6,BMRB Entry Tracking System,70933,17599
BMRB,17599,Solution structure of the Par-6 Q144C/L164C,70966,17600
PDB,2LC7,BMRB Entry Tracking System,70966,17600
PDB,2LC8,BMRB Entry Tracking System,70986,17601
BMRB,17604,T4_L99A,71023,17603
PDB,2LC9,BMRB Entry Tracking System,71023,17603
BMRB,17603,T4_L99A/G113A/R119P,71042,17604
PDB,2LCB,BMRB Entry Tracking System,71042,17604
BMRB,17607,RBBP1 tudor domain,71066,17606
PDB,2LCC,BMRB Entry Tracking System,71066,17606
BMRB,17606,RBBP1 chromobarrel domain,71081,17607
PDB,2MAM,BMRB Entry Tracking System,71081,17607
PDB,2MBG,BMRB Entry Tracking System,71100,17608
PDB,2LCE,BMRB Entry Tracking System,71119,17609
BMRB,18461,H-Ras-GppNHp bound to Ras-binding domain of cRaf1,71154,17610
PDB,2LCF,BMRB Entry Tracking System,71154,17610
PDB,2LCH,BMRB Entry Tracking System,71212,17612
PDB,2LCI,BMRB Entry Tracking System,71234,17613
PDB,1OKC,MITOCHONDRIAL ADP/ATP CARRIER,71263,17614
PDB,2LCK,BMRB Entry Tracking System,71263,17614
PDB,2LCL,BMRB Entry Tracking System,71289,17615
PDB,2LCM,BMRB Entry Tracking System,71322,17617
BMRB,17619,WALP19-P10 in SDS micelles,71336,17618
PDB,2LCN,BMRB Entry Tracking System,71336,17618
BMRB,17618,WALP19-P10 in SDS micelles,71361,17619
PDB,2LCO,BMRB Entry Tracking System,71361,17619
PDB,2Y4Q,BMRB Entry Tracking System,71411,17621
BMRB,17623,human U2AF65 uridine binding,71430,17622
PDB,2YH0,BMRB Entry Tracking System,71430,17622
BMRB,17622,human U2AF65 closed conformation,71447,17623
PDB,2YH1,BMRB Entry Tracking System,71447,17623
PDB,2YHH,BMRB Entry Tracking System,71465,17625
BMRB,17627,apo actinin-2 C-terminal EF-hand (Act2-EF34),71484,17626
BMRB,4453,Act2EF34-Zr7,71484,17626
BMRB,4454,Act2EF34-Zr7,71484,17626
PDB,1H8B,structure of Act2EF34-Zr7,71484,17626
BMRB,17626,Act2-EF34 in complex with palladin peptide,71503,17627
BMRB,4453,Act2EF34-Zr7,71503,17627
BMRB,4454,Act2EF34-Zr7,71503,17627
PDB,1H8B,Act2EF34-Zr7,71503,17627
PDB,2LCR,BMRB Entry Tracking System,71522,17628
PDB,2LCS,BMRB Entry Tracking System,71548,17629
BMRB,17631,JAZ ZF2,71570,17630
BMRB,17630,Zinc Finger Protein residues 23-117,71586,17631
PDB,2LCT,BMRB Entry Tracking System,71603,17632
PDB,2LCU,BMRB Entry Tracking System,71621,17633
BMRB,17419,,71641,17634
PDB,2L8N,,71641,17634
PDB,2LCV,BMRB Entry Tracking System,71641,17634
PDB,2LCW,BMRB Entry Tracking System,71661,17635
BMRB,17637,short Grx domain,71675,17636
PDB,2LV3,BMRB Entry Tracking System,71675,17636
BMRB,17636,Grx domain,71689,17637
BMRB,17639,"Ebolavirus GP2 at pH 7.0""",71703,17638
PDB,2LCY,BMRB Entry Tracking System,71703,17638
BMRB,17638,"Ebolavirus GP2 at pH 5.5""",71720,17639
PDB,2LCZ,BMRB Entry Tracking System,71720,17639
PDB,3P7N,EL222 molecular coordinates,71737,17640
BMRB,17068,NMR assigment of the cold denaturated state (0 C) of Yeast frataxin in solution,71756,17641
BMRB,6356,NMR assigment of the folded Yeast frataxin,71756,17641
PDB,1ekg,Mature human frataxin,71756,17641
PDB,1soy,Solution structure of the bacterial frataxin,71756,17641
PDB,2fql,Crystal structure of trimeric yeast frataxin,71756,17641
PDB,2ga5,NMR structure of the folded Yeast frataxin in solution,71756,17641
BMRB,17644,htt17 in DPC micelles,71771,17642
PDB,2LD0,BMRB Entry Tracking System,71771,17642
BMRB,17642,htt17 in 50% TFE,71803,17644
PDB,2LD2,BMRB Entry Tracking System,71803,17644
PDB,2LD3,BMRB Entry Tracking System,71817,17645
PDB,2LD4,BMRB Entry Tracking System,71838,17646
PDB,3QMN,,71863,17647
BMRB,16939,WT alpha-synuclein fibrils,71877,17648
BMRB,17649,A53T alpha-synuclein fibrils,71877,17648
BMRB,17654,E46K alpha-synuclein fibrils,71877,17648
BMRB,16939,WT alpha-synuclein fibrils,71892,17649
BMRB,17648,A30P alpha-synuclein fibrils,71892,17649
BMRB,17654,E46K alpha-synuclein fibrils,71892,17649
PDB,2LD6,BMRB Entry Tracking System,71924,17651
PDB,2LD7,BMRB Entry Tracking System,71959,17653
BMRB,16939,WT alpha-synuclein fibrils,71981,17654
BMRB,17648,A30P alpha-synuclein fibrils,71981,17654
BMRB,17649,A53T alpha-synuclein fibrils,71981,17654
PDB,1KF1,,71996,17655
PDB,2gku,,71996,17655
PDB,2JSL,,71996,17655
PDB,2kf8,,71996,17655
PDB,2km3,,71996,17655
PDB,2LD8,BMRB Entry Tracking System,71996,17655
BMRB,17658,stapled peptide SP1,72028,17657
BMRB,17659,stapled peptide SP6,72028,17657
PDB,2LDA,BMRB Entry Tracking System,72028,17657
BMRB,17657,stapled peptide SP2,72049,17658
BMRB,17659,stapled peptide SP6,72049,17658
PDB,2LDC,BMRB Entry Tracking System,72049,17658
BMRB,17657,stapled peptide SP2,72070,17659
BMRB,17658,stapled peptide SP1,72070,17659
PDB,2LDD,BMRB Entry Tracking System,72070,17659
BMRB,17662,sarafotoxin srtx-m,72123,17661
PDB,2LDE,BMRB Entry Tracking System,72123,17661
BMRB,17661,sarafotoxin srtx-i3,72142,17662
PDB,2LDF,BMRB Entry Tracking System,72142,17662
BMRB,17664,ORF57 103-120,72162,17663
BMRB,17663,ORF57 56-140,72177,17664
PDB,2LL4,BMRB Entry Tracking System,72207,17667
PDB,2LDI,BMRB Entry Tracking System,72223,17668
PDB,2OFG,the n-terminal domain of the zinc(II) ATPase ziaa in its apo form,72223,17668
PDB,2OFH,the n-terminal domain of the zinc(II) ATPase ziaa in its apo form,72223,17668
PDB,2LDJ,BMRB Entry Tracking System,72239,17669
PDB,2LDK,BMRB Entry Tracking System,72269,17670
TargetDB,AaR96,,72269,17670
PDB,2LDL,BMRB Entry Tracking System,72300,17671
PDB,2LDM,BMRB Entry Tracking System,72335,17673
PDB,2LDR,BMRB Entry Tracking System,72429,17680
PDB,2LDS,BMRB Entry Tracking System,72452,17681
PDB,2LDT,BMRB Entry Tracking System,72466,17682
PDB,2LDU,BMRB Entry Tracking System,72481,17683
PDB,2LWX,BMRB Entry Tracking System,72509,17685
PDB,2LDY,BMRB Entry Tracking System,72528,17686
PDB,2YKO,Crystal structure of human LINE-1 ORF1p timer,72528,17686
PDB,2YKP,Crystal structure of human LINE-1 ORF1p timer,72528,17686
PDB,2YKQ,Crystal structure of human LINE-1 ORF1p timer,72528,17686
PDB,2LE0,BMRB Entry Tracking System,72550,17687
TargetDB,TfR85a,,72569,17688
PDB,2LE2,BMRB Entry Tracking System,72603,17689
PDB,2LE3,BMRB Entry Tracking System,72635,17690
PDB,2LE4,BMRB Entry Tracking System,72649,17691
PDB,2YKA,BMRB Entry Tracking System,72677,17693
PDB,2LS6,BMRB Entry Tracking System,72698,17694
PDB,1UV6,Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures.,72713,17695
PDB,1YI5,Crystal structure of the a-cobratoxin-AChBP complex,72713,17695
PDB,2BG9,Refined structure of the nicotinic acetylcholine receptor at 4A resolution.,72713,17695
PDB,2QC1,Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin,72713,17695
PDB,2VL0,X-RAY STRUCTURE OF A PENTAMERIC LIGAND GATED ION CHANNEL FROM ERWINIA CHRYSANTHEMI (ELIC),72713,17695
PDB,3EAM,X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation.,72713,17695
PDB,3IGQ,Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel.,72713,17695
PDB,1Y8D,"Dimeric parallel-stranded tetraplex with 3+1 5' G-tetrad interface, single-residue chain reversal loops and A(GGGG) pentad",72733,17697
PDB,2LE6,BMRB Entry Tracking System,72733,17697
PDB,3MYA,Crystal Structure of HP67 H41F,72755,17698
PDB,3MYC,Crystal Structure of HP67 H41F,72755,17698
PDB,2LE7,BMRB Entry Tracking System,72775,17699
PDB,2LE8,BMRB Entry Tracking System,72861,17702
PDB,2LTR,BMRB Entry Tracking System,72886,17703
PDB,2LTS,BMRB Entry Tracking System,72886,17703
PDB,2LEA,BMRB Entry Tracking System,72927,17705
BMRB,17705,Protein + RNA,72947,17706
PDB,21ea,Protein + RNA,72947,17706
PDB,2LEB,BMRB Entry Tracking System,72947,17706
BMRB,17706,Protein + RNA2,72968,17707
PDB,21eb,Protein + RNA2,72968,17707
PDB,2LEC,BMRB Entry Tracking System,72968,17707
BMRB,17709,Solution-state structures of monomeric and dimeric G-quadruplexes formed by a sequence from N-myc,72989,17708
PDB,2LED,BMRB Entry Tracking System,72989,17708
BMRB,17708,Solution-state structures of monomeric and dimeric G-quadruplexes adopted by a sequence from N-myc,73004,17709
PDB,2LEE,BMRB Entry Tracking System,73004,17709
BMRB,15546,Chemical shift assignments for DsbB,73032,17710
BMRB,16327,Chemical shift assignments for DsbA,73032,17710
PDB,2hi7,,73032,17710
PDB,2LEH,BMRB Entry Tracking System,73062,17711
PDB,4BF8,BMRB Entry Tracking System,73085,17713
PDB,1QM1,,73105,17714
PDB,2LEJ,BMRB Entry Tracking System,73105,17714
PDB,2LEL,BMRB Entry Tracking System,73140,17716
PDB,2LEM,BMRB Entry Tracking System,73167,17717
BMRB,5003,Entry containing chemical shifts of staphylococcal nuclease H124L.,73190,17718
PDB,2LEO,BMRB Entry Tracking System,73208,17719
PDB,2LEP,BMRB Entry Tracking System,73237,17720
BMRB,15764,Resonance assignments for CBD1 in the free state,73253,17721
BMRB,17722,"Backbone (1H,15N,13C) chemical shifts of CBD12 in the Ca2+-bound state",73253,17721
BMRB,7008,Resonance assignments for CBD2 in the Ca2+-bound state,73253,17721
BMRB,7009,Resonance assignments for CBD1 in the Ca2+-bound state,73253,17721
BMRB,15764,Resonance assignments for CBD1 in the free state,73267,17722
BMRB,17721,"Backbone (1H, 13C, 15N) Chemical Shifts for CBD12 in the free state",73267,17722
BMRB,7008,Resonance assignments for CBD2 in the Ca2+-bound state,73267,17722
BMRB,7009,Resonance assignments for CBD1 in the Ca2+-bound state,73267,17722
PDB,2LEQ,BMRB Entry Tracking System,73283,17723
BMRB,17045,KSR1 CA1 monomer,73309,17724
BMRB,17725,KSR1 CA1-CA1a domain,73309,17724
BMRB,18740,LMPG micelle-bound CC-SAM,73309,17724
BMRB,17045,KSR1 CA1-CA1a (25-170),73325,17725
BMRB,17724,KSR1 CA1-CA1a domain (bound to SDS micelles),73325,17725
BMRB,18740,LMPG micelle-bound CC-SAM,73325,17725
PDB,2LER,BMRB Entry Tracking System,73341,17726
Uniprot,P86942,Uniprot,73341,17726
BMRB,17744,KcsA-Kv1.3 channel,73356,17727
PDB,2LES,BMRB Entry Tracking System,73356,17727
PDB,2LEV,BMRB Entry Tracking System,73387,17729
PDB,2LEW,BMRB Entry Tracking System,73430,17731
PDB,,native Crp4,73430,17731
PDB,,E15D Crp4,73430,17731
PDB,2LEX,BMRB Entry Tracking System,73446,17732
PDB,2GW9,Cryptdin-4,73473,17733
PDB,2GWP,(E15G)-Crp4,73473,17733
PDB,2LEY,BMRB Entry Tracking System,73473,17733
PDB,2LF2,BMRB Entry Tracking System,73540,17736
PDB,2jyl,Entry showing the c-terminal domain of this protein,73620,17738
PDB,2LF4,BMRB Entry Tracking System,73620,17738
PDB,2LF6,BMRB Entry Tracking System,73643,17739
PDB,3NHN,corresponding Crystal structure,73670,17740
BMRB,17742,ETS Domain within ETV6,73688,17741
PDB,2LF7,BMRB Entry Tracking System,73688,17741
BMRB,17741,ETS Domain within ETV6,73706,17742
PDB,2LF8,BMRB Entry Tracking System,73706,17742
BMRB,17727,KcsA-Kv1.3 channel,73745,17744
PDB,2LSN,BMRB Entry Tracking System,73760,17745
PDB,2LFA,BMRB Entry Tracking System,73775,17746
PDB,2LFC,BMRB Entry Tracking System,73792,17747
PDB,2LFD,BMRB Entry Tracking System,73835,17749
PDB,2LFE,BMRB Entry Tracking System,73875,17750
PDB,2LFF,BMRB Entry Tracking System,73899,17751
PDB,1RW5,Human prolactin,73924,17752
PDB,2LFG,BMRB Entry Tracking System,73924,17752
PDB,3D48,1:1 complex,73924,17752
PDB,3EW3,2:1 complex,73924,17752
PDB,3MZG,1:1 complex,73924,17752
PDB,3NPZ,2:1 complex,73924,17752
PDB,2LFH,BMRB Entry Tracking System,73947,17753
TargetDB,HR3111A,,73947,17753
PDB,2LFI,BMRB Entry Tracking System,73974,17754
BMRB,17757,HuPrP(121-230) methylated,74020,17756
BMRB,17756,HuPrP(121-230) oxidized,74037,17757
BMRB,17759,mPrP(121-232) methylated,74055,17758
BMRB,17758,mPrP(121-232) oxidized,74072,17759
PDB,2LFJ,BMRB Entry Tracking System,74119,17762
BMRB,17779,lllb,74138,17763
PDB,2LFK,BMRB Entry Tracking System,74138,17763
PDB,2LFM,BMRB Entry Tracking System,74155,17764
PDB,2FMC,Solution structure of the class I hydrophobin EAS,74169,17765
PDB,2K6A,Solution structure of EAS D15 truncation mutant,74169,17765
PDB,2LFN,BMRB Entry Tracking System,74169,17765
PDB,2JN3,entry containing coordinates of cl-BABP complexed with chenodeoxycholic acid,74205,17767
PDB,2LFO,BMRB Entry Tracking System,74205,17767
PDB,1z1z,,74229,17768
PDB,2gjv,,74229,17768
PDB,2l25,,74229,17768
PDB,2LFP,BMRB Entry Tracking System,74229,17768
PDB,3fz2,,74229,17768
PDB,3fzb,,74229,17768
BMRB,19689,a phytocystatin from Sesamum indicum L.,74299,17771
PDB,2M0J,BMRB Entry Tracking System,74299,17771
PDB,2M0K,BMRB Entry Tracking System,74299,17771
PDB,3ZTG,BMRB Entry Tracking System,74319,17772
BMRB,17776,Af1503 HAMP- EnvZ DHp; A219F variant,74379,17775
PDB,2LFR,BMRB Entry Tracking System,74379,17775
PDB,3ZRV,crystal structure (A291F variant),74379,17775
PDB,3ZRW,crystal structure (A291V variant),74379,17775
PDB,3ZRX,crystal structure,74379,17775
BMRB,17775,Af1503 HAMP- EnvZ DHp,74398,17776
PDB,2LFS,BMRB Entry Tracking System,74398,17776
PDB,3ZRV,crystal structure (A291F variant),74398,17776
PDB,3ZRW,crystal structure (A291V variant),74398,17776
PDB,3ZRX,crystal structure,74398,17776
BMRB,17763,TdPI-short,74433,17779
PDB,2LFL,BMRB Entry Tracking System,74433,17779
PDB,1QM1,,74448,17780
PDB,2LFT,BMRB Entry Tracking System,74448,17780
BMRB,17882,lsm57,74467,17781
BMRB,17881,lsm567 hexamer,74481,17782
PDB,2LFW,BMRB Entry Tracking System,74521,17784
BMRB,17787,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74564,17786
BMRB,17788,"gamma-hydroxy-1,N2-propano-2'-deoxyguanosine adduct",74564,17786
BMRB,17789,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74564,17786
BMRB,17790,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74564,17786
BMRB,17791,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74564,17786
PDB,2LFX,BMRB Entry Tracking System,74564,17786
BMRB,17786,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74579,17787
BMRB,17788,"gamma-hydroxy-1,N2-propano-2'-deoxyguanosine adduct",74579,17787
BMRB,17789,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74579,17787
BMRB,17790,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74579,17787
BMRB,17791,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74579,17787
PDB,2LFY,BMRB Entry Tracking System,74579,17787
BMRB,17786,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74594,17788
BMRB,17787,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74594,17788
BMRB,17789,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74594,17788
BMRB,17790,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74594,17788
BMRB,17791,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74594,17788
PDB,2KV6,Major conformer of the DNA-peptide conjugate,74594,17788
BMRB,17786,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74611,17789
BMRB,17787,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74611,17789
BMRB,17788,"gamma-hydroxy-1,N2-propano-2'-deoxyguanosine adduct",74611,17789
BMRB,17790,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74611,17789
BMRB,17791,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74611,17789
PDB,2LG0,BMRB Entry Tracking System,74611,17789
BMRB,17786,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74641,17790
BMRB,17787,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74641,17790
BMRB,17788,"gamma-hydroxy-1,N2-propano-2'-deoxyguanosine adduct",74641,17790
BMRB,17789,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74641,17790
BMRB,17791,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74641,17790
PDB,2LG2,BMRB Entry Tracking System,74641,17790
BMRB,17786,"(5'S)-8,5'-cyclo-2'-deoxyguanosine",74659,17791
BMRB,17787,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74659,17791
BMRB,17788,"gamma-hydroxy-1,N2-propano-2'-deoxyguanosine adduct",74659,17791
BMRB,17789,"(5'S)-8,5'-cyclo-2'-deoxyadenosine",74659,17791
BMRB,17790,"(6S,8R,11S) gamma-hydroxy-1,N2-propano-deoxyguanosine adduct",74659,17791
PDB,2LG3,BMRB Entry Tracking System,74659,17791
PDB,2LG4,BMRB Entry Tracking System,74676,17792
BMRB,17794,Abeta(1-42) reduced,74693,17793
BMRB,17795,Abeta(1-40) oxidised,74693,17793
BMRB,17796,Abeta(1-40) reduced,74693,17793
BMRB,17793,Abeta(1-42) oxidised,74708,17794
BMRB,17795,Abeta(1-40) oxidised,74708,17794
BMRB,17796,Abeta(1-40) reduced,74708,17794
BMRB,17793,Abeta(1-42) oxidised,74723,17795
BMRB,17794,Abeta(1-42) reduced,74723,17795
BMRB,17796,Abeta(1-40) reduced,74723,17795
BMRB,17793,Abeta(1-42) oxidised,74738,17796
BMRB,17794,Abeta(1-42) reduced,74738,17796
BMRB,17795,Abeta(1-40) oxidised,74738,17796
BMRB,17798,chicken AvBD2-K31A mutant,74753,17797
PDB,2LG5,BMRB Entry Tracking System,74753,17797
BMRB,17797,Chicken AvBD2 defensin,74770,17798
PDB,2LG6,BMRB Entry Tracking System,74770,17798
BMRB,17806,YP_001302112.1,74787,17799
PDB,2LG7,BMRB Entry Tracking System,74787,17799
PDB,2LGB,BMRB Entry Tracking System,74805,17803
PDB,2LGD,BMRB Entry Tracking System,74847,17805
BMRB,17799,YP_001302112.1,74871,17806
PDB,2LGE,BMRB Entry Tracking System,74871,17806
PDB,2LGF,BMRB Entry Tracking System,74891,17807
PDB,2LGG,BMRB Entry Tracking System,74920,17808
PDB,1GB1,,75004,17810
PDB,1PGA,,75004,17810
PDB,1PGB,,75004,17810
PDB,2GB1,,75004,17810
PDB,2GI9,,75004,17810
PDB,2JSV,,75004,17810
PDB,2JU6,,75004,17810
PDB,2KOP,,75004,17810
PDB,2KQ4,,75004,17810
PDB,2KWD,,75004,17810
PDB,2LGI,BMRB Entry Tracking System,75004,17810
PDB,2PLP,,75004,17810
PDB,2QMT,,75004,17810
PDB,2LGJ,BMRB Entry Tracking System,75022,17811
PDB,2LGK,BMRB Entry Tracking System,75044,17812
PDB,2LGL,BMRB Entry Tracking System,75065,17813
PDB,2LGM,BMRB Entry Tracking System,75081,17814
PDB,3KRM,Xray crystal structure,75103,17815
PDB,2LGN,BMRB Entry Tracking System,75119,17816
BMRB,15955,Green Proteorhodopsin,75136,17817
PDB,2LGO,BMRB Entry Tracking System,75154,17818
TargetDB,GilaA.00840.a,,75154,17818
PDB,2LGQ,BMRB Entry Tracking System,75208,17821
PDB,2rn9,,75208,17821
PDB,2LGT,BMRB Entry Tracking System,75229,17822
PDB,1LDJ,Cul1-Rbx1-Skp1-F boxSkp2 SCF,75261,17824
PDB,1LDK,Cul1-Rbx1-Skp1-F boxSkp2 SCF,75261,17824
PDB,1U6G,Cand1-Rbx1-Cullin1,75261,17824
PDB,2HYE,DDB1-Cul4A-Rbx1-SV5V,75261,17824
PDB,2LGV,BMRB Entry Tracking System,75261,17824
PDB,3DPL,NEDD8-Cul5-Rbx1,75261,17824
PDB,3DQV,NEDD8-Cul5-Rbx1,75261,17824
PDB,3RTR,Cul1-Rbx1,75261,17824
PDB,2LGW,BMRB Entry Tracking System,75286,17825
BMRB,15800,Galectin-1,75304,17826
PDB,2LGX,BMRB Entry Tracking System,75322,17827
BMRB,17831,oxidized nDsbD,75398,17830
PDB,3PFU,X-ray structure of reduced nDsbD,75398,17830
BMRB,17830,reduced nDsbD,75415,17831
PDB,2LH0,BMRB Entry Tracking System,75432,17832
PDB,2LH8,BMRB Entry Tracking System,75462,17834
PDB,2LH9,BMRB Entry Tracking System,75484,17835
BMRB,17837,IscU,75502,17836
BMRB,17844,IscU:IscS,75502,17836
BMRB,17836,IscU,75519,17837
BMRB,17844,IscU:IscS,75519,17837
PDB,2LHA,BMRB Entry Tracking System,75536,17838
BMRB,17840,GB98,75554,17839
BMRB,17841,"GB98-T25I,L20A",75554,17839
BMRB,17843,GB98-T25I,75554,17839
PDB,2LHC,BMRB Entry Tracking System,75554,17839
BMRB,17839,Ga98,75576,17840
BMRB,17841,"GB98-T25I,L20A",75576,17840
BMRB,17843,GB98-T25I,75576,17840
PDB,2LHD,BMRB Entry Tracking System,75576,17840
BMRB,17839,GA98,75599,17841
BMRB,17840,GB98,75599,17841
BMRB,17843,GB98-T25I,75599,17841
PDB,2LHE,BMRB Entry Tracking System,75599,17841
PDB,2LHF,BMRB Entry Tracking System,75621,17842
BMRB,17839,GA98,75636,17843
BMRB,17840,GB98,75636,17843
BMRB,17841,"GB98-T25I,L20A",75636,17843
PDB,2LHG,BMRB Entry Tracking System,75636,17843
BMRB,17836,IscU,75650,17844
BMRB,17837,IscU,75650,17844
BMRB,17846,yCc,75667,17845
BMRB,17847,hCc,75667,17845
BMRB,17848,hCc,75667,17845
BMRB,346,proton assignements,75667,17845
BMRB,923,proton assignements,75667,17845
PDB,1YIC,NMR structure,75667,17845
PDB,2YCC,X-ray structure,75667,17845
BMRB,17845,yCc,75688,17846
BMRB,17847,hCc,75688,17846
BMRB,17848,hCc,75688,17846
BMRB,345,proton assignements,75688,17846
BMRB,922,proton assignements,75688,17846
PDB,1YCC,X-ray structure,75688,17846
PDB,1YFC,NMR structure,75688,17846
BMRB,17845,yCc,75709,17847
BMRB,17846,yCc,75709,17847
BMRB,17848,hCc,75709,17847
BMRB,5828,backbone assignments for H26N/H33N mutant,75709,17847
BMRB,5830,backbone amide assignments for the wt protein,75709,17847
PDB,1AKK,NMR structure,75709,17847
PDB,1HRC,X-ray structure,75709,17847
PDB,1OCD,NMR structure,75709,17847
BMRB,17845,yCc,75730,17848
BMRB,17846,yCc,75730,17848
BMRB,17847,hCc,75730,17848
BMRB,5827,backbone assignments for H26N/H33N mutant,75730,17848
BMRB,5829,backbone amide assignments for the wt protein,75730,17848
PDB,1GIW,NMR structure,75730,17848
PDB,2FRC,NMR structure,75730,17848
BMRB,17850,yCaM,75751,17849
PDB,2LHH,BMRB Entry Tracking System,75751,17849
BMRB,17849,yCaM,75787,17850
PDB,2LHI,BMRB Entry Tracking System,75787,17850
BMRB,17852,beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate,75810,17851
BMRB,7234,"Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-",75810,17851
PDB,2wf5,Structure of beta-phosphoglucomutase inhibited with glucose-6-phosphate and trifluoromagnesate,75810,17851
PDB,2wfa,"Structure of beta-phosphoglucomutase inhibited with beryllium trifluoride, in an open conformation",75810,17851
BMRB,17851,"Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a binary complex with BeF3-",75831,17852
BMRB,7234,"Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-",75831,17852
PDB,2wf5,Structure of beta-phosphoglucomutase inhibited with glucose-6-phosphate and trifluoromagnesate,75831,17852
PDB,2wf8,"Structure of beta-phosphoglucomutase inhibited with glucose-6-phosphate, glucose-1-phosphate and beryllium trifluoride",75831,17852
PDB,2wf9,"Structure of beta-phosphoglucomutase inhibited with glucose-6-phosphate and beryllium trifluoride, crystal form 2",75831,17852
PDB,2wfa,"Structure of beta-phosphoglucomutase inhibited with beryllium trifluoride, in an open conformation",75831,17852
PDB,2LHJ,BMRB Entry Tracking System,75870,17855
PDB,2LHK,BMRB Entry Tracking System,75887,17856
BMRB,16360,chemical shifts and relaxation data for wildtype human apo-S100A1,75901,17857
PDB,2L0P,structure of human apo-S100A1,75901,17857
PDB,2M3W,BMRB Entry Tracking System,75901,17857
PDB,2LHN,BMRB Entry Tracking System,75931,17858
PDB,2LHO,BMRB Entry Tracking System,75951,17859
PDB,2LHP,BMRB Entry Tracking System,75969,17860
PDB,2LHR,BMRB Entry Tracking System,76017,17862
PDB,2LHU,BMRB Entry Tracking System,76113,17867
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
BMRB,17873,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76130,17868
PDB,2LHV,BMRB Entry Tracking System,76130,17868
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
BMRB,17873,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76149,17869
PDB,2LHW,BMRB Entry Tracking System,76149,17869
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
BMRB,17873,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76185,17870
PDB,2LHX,BMRB Entry Tracking System,76185,17870
PDB,2LHY,BMRB Entry Tracking System,76206,17871
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
BMRB,17873,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76227,17872
PDB,2LHZ,BMRB Entry Tracking System,76227,17872
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76248,17873
PDB,2LI0,BMRB Entry Tracking System,76248,17873
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
BMRB,17873,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
BMRB,17875,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76269,17874
PDB,2LI1,BMRB Entry Tracking System,76269,17874
BMRB,17868,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
BMRB,17869,Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
BMRB,17870,Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
BMRB,17872,Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
BMRB,17873,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
BMRB,17874,Mono-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat,76290,17875
PDB,2LI2,BMRB Entry Tracking System,76290,17875
PDB,2LI4,BMRB Entry Tracking System,76331,17877
BMRB,15726,assignment of the N-terminal region of human La protein,76353,17878
BMRB,15727,assignment of the N-terminal region of human La protein in complex with RNA,76353,17878
BMRB,5235,Full assignment of the RRM2 of La protein,76353,17878
BMRB,5719,Full assignment of the RRM1 of La protein,76353,17878
BMRB,6044,Full assignment of La motif of La protein,76353,17878
PDB,2KWC,,76369,17879
PDB,2LI5,BMRB Entry Tracking System,76369,17879
PDB,2LI6,BMRB Entry Tracking System,76392,17880
BMRB,17981,"calcium calmodulin, complex with PEP-19",76406,17881
BMRB,17982,"calcium calmodulin, complex with Ca",76406,17881
BMRB,17983,"calcium calmodulin, complex with Ca and PEP-19",76406,17881
PDB,2LI7,BMRB Entry Tracking System,76423,17882
PDB,2CQF,Structure of Lin28 ZnFs free form,76439,17883
PDB,2LI8,BMRB Entry Tracking System,76439,17883
PDB,1ZE7,,76466,17884
PDB,2LI9,BMRB Entry Tracking System,76466,17884
PDB,2LIA,BMRB Entry Tracking System,76493,17885
PDB,2M5R,BMRB Entry Tracking System,76510,17886
PDB,2LIB,BMRB Entry Tracking System,76526,17887
PDB,2LIC,BMRB Entry Tracking System,76549,17888
PDB,2LID,BMRB Entry Tracking System,76565,17889
BMRB,17902,lectin CCL2 (+carbohydrate),76594,17890
PDB,2LIE,BMRB Entry Tracking System,76594,17890
PDB,2LIF,BMRB Entry Tracking System,76616,17891
BMRB,17893,CylR2 homodimer at 270K,76634,17892
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76634,17892
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76634,17892
BMRB,17896,monomeric intermediate of CylR2 at 262K,76634,17892
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76634,17892
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76634,17892
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76634,17892
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76634,17892
PDB,2LYJ,BMRB Entry Tracking System,76634,17892
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76634,17892
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76634,17892
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76634,17892
BMRB,17892,NMR structure of the CylR2 homodimer at 298K,76651,17893
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76651,17893
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76651,17893
BMRB,17896,monomeric intermediate of CylR2 at 262K,76651,17893
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76651,17893
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76651,17893
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76651,17893
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76651,17893
PDB,2LYK,BMRB Entry Tracking System,76651,17893
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76651,17893
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76651,17893
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76651,17893
BMRB,17892,CylR2 homodimer at 298K,76668,17894
BMRB,17893,CylR2 homodimer at 270K,76668,17894
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76668,17894
BMRB,17896,monomeric intermediate of CylR2 at 262K,76668,17894
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76668,17894
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76668,17894
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76668,17894
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76668,17894
PDB,2LYL,BMRB Entry Tracking System,76668,17894
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76668,17894
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76668,17894
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76668,17894
BMRB,17892,NMR structure of the CylR2 homodimer at 298K,76685,17895
BMRB,17893,NMR structure of the CylR2 homodimer at 270K,76685,17895
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76685,17895
BMRB,17896,monomeric intermediate of CylR2 at 262K,76685,17895
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76685,17895
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76685,17895
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76685,17895
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76685,17895
PDB,2LYP,BMRB Entry Tracking System,76685,17895
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76685,17895
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76685,17895
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76685,17895
BMRB,17892,NMR structure of the CylR2 homodimer at 298K,76702,17896
BMRB,17893,NMR structure of the CylR2 homodimer at 270K,76702,17896
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76702,17896
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76702,17896
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76702,17896
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76702,17896
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76702,17896
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76702,17896
PDB,2LYQ,BMRB Entry Tracking System,76702,17896
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76702,17896
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76702,17896
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76702,17896
BMRB,17892,NMR structure of the CylR2 homodimer at 298K,76719,17897
BMRB,17893,NMR structure of the CylR2 homodimer at 270K,76719,17897
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76719,17897
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76719,17897
BMRB,17896,monomeric intermediate of CylR2 at 262K,76719,17897
BMRB,17898,monomeric partially-folded intermediate of CylR2 at 257K,76719,17897
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76719,17897
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76719,17897
PDB,2LYR,BMRB Entry Tracking System,76719,17897
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76719,17897
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76719,17897
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76719,17897
BMRB,17892,NMR structure of the CylR2 homodimer at 298K,76736,17898
BMRB,17893,NMR structure of the CylR2 homodimer at 270K,76736,17898
BMRB,17894,predissociated homodimer of CylR2 in equilibrium with monomer at 266K,76736,17898
BMRB,18077,AbpSH3-Srv12,79923,18065
BMRB,17895,monomer of CylR2 in equilibrium with predissociated homodimer at 266K,76736,17898
BMRB,17896,monomeric intermediate of CylR2 at 262K,76736,17898
BMRB,17897,monomeric partially-folded intermediate of CylR2 at 259K,76736,17898
PDB,1UTX,X-ray structure of the same protein at 1.9 A resolution,76736,17898
PDB,2GZU,Structure of the same protein using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings,76736,17898
PDB,2LYS,BMRB Entry Tracking System,76736,17898
PDB,2XI8,X-ray structure of the same protein at 1.21 A resolution,76736,17898
PDB,2XIU,X-ray structure of MTSL-tagged CYLR2,76736,17898
PDB,2XJ3,X-ray structure of T55C mutant of CYLR2,76736,17898
PDB,2LIO,BMRB Entry Tracking System,76781,17900
BMRB,17890,lectin CCL2 (free),76822,17902
PDB,2LIQ,BMRB Entry Tracking System,76822,17902
BMRB,17904,Yeast Iso-1-cytochrome c Mutant P71H in reduced states,76851,17903
PDB,2LIR,BMRB Entry Tracking System,76851,17903
BMRB,17903,Yeast Iso-1-cytochrome c Mutant P71H in oxidized states,76870,17904
PDB,2LIT,BMRB Entry Tracking System,76870,17904
BMRB,17907,CurA module,76906,17906
PDB,2LIU,BMRB Entry Tracking System,76906,17906
BMRB,17906,CurA module,76925,17907
PDB,2LIX,BMRB Entry Tracking System,76951,17908
BMRB,16939,alpha-synuclein fibrils,76996,17910
BMRB,17214,alpha-synuclein fibrils,76996,17910
BMRB,17648,A30P alpha-synuclein fibrils,76996,17910
BMRB,17649,A53T alpha-synuclein fibrils,76996,17910
BMRB,17654,E46K alpha-synuclein fibrils,76996,17910
PDB,2LIZ,BMRB Entry Tracking System,77012,17911
BMRB,17913,third SH3 domain of R85FL with ataxin-7 PRR,77032,17912
PDB,2LJ0,BMRB Entry Tracking System,77032,17912
BMRB,17912,third SH3 domain of R85FL,77046,17913
PDB,2LJ1,BMRB Entry Tracking System,77046,17913
PDB,1WAZ,,77060,17914
PDB,2H3O,,77060,17914
PDB,2LJ2,BMRB Entry Tracking System,77060,17914
BMRB,3433,1H and 15N assignments and secondary structure of the Src Sh3 domain,77078,17915
PDB,1SHG,Crystal Structure of SH3,77078,17915
PDB,2LJ3,BMRB Entry Tracking System,77078,17915
BMRB,17917,Tfg1,77094,17916
BMRB,17916,Tfg2,77110,17917
PDB,2LJ4,BMRB Entry Tracking System,77126,17918
PDB,2KOX,NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin,77140,17919
PDB,2LJ5,BMRB Entry Tracking System,77140,17919
BMRB,6652,GAAA tetraloop/Receptor homodimer,77168,17921
PDB,2ADT,NMR structure of a 30 kDa GAAA tetraloop receptor complex,77168,17921
PDB,2LJ7,BMRB Entry Tracking System,77204,17923
BMRB,17925,SEVI with Zn,77221,17924
BMRB,17924,SEVI without Zn,77237,17925
PDB,2LJ9,BMRB Entry Tracking System,77255,17926
PDB,2LJA,BMRB Entry Tracking System,77279,17927
TargetDB,NYSGRC-501011,,77279,17927
BMRB,17929,Influenza AM2-BM2 chimeric channel bound to rimantadine,77299,17928
PDB,2KIH,S31N mutant,77299,17928
PDB,2KIX,BM2 channel structure,77299,17928
PDB,2KWX,V27A mutant,77299,17928
PDB,2LJB,BMRB Entry Tracking System,77299,17928
PDB,2RLF,AM2 channel structure,77299,17928
BMRB,17928,influenza AM2-BM2 chimeric channel,77322,17929
PDB,2KIX,BM2 channel structure,77322,17929
PDB,2KWX,V27A mutant,77322,17929
PDB,2ljb,AM2-BM2 chimeric channel without drug,77322,17929
PDB,2LJC,BMRB Entry Tracking System,77322,17929
PDB,2RLF,AM2 channel structure,77322,17929
BMRB,17931,"biphosphorylated (747pY, 759pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions",77361,17930
BMRB,17932,monophosphorylated (747pY) beta3 integrin cytoplasmic tail under aqueous conditions,77361,17930
PDB,2LJD,BMRB Entry Tracking System,77361,17930
BMRB,17930,monophosphorylated (747pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions,77379,17931
BMRB,17932,monophosphorylated (747pY) beta3 integrin cytoplasmic tail under aqueous conditions,77379,17931
PDB,2LJE,BMRB Entry Tracking System,77379,17931
BMRB,17930,monophosphorylated (747pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions,77398,17932
BMRB,17931,"biphosphorylated (747pY, 759pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions",77398,17932
PDB,2LJF,BMRB Entry Tracking System,77398,17932
PDB,2M38,BMRB Entry Tracking System,77416,17934
PDB,2LXN,BMRB Entry Tracking System,77431,17935
PDB,2LJH,BMRB Entry Tracking System,77447,17936
BMRB,17937,Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules,77486,17938
PDB,2LJI,BMRB Entry Tracking System,77502,17939
BMRB,6468,mitogen-activated protein kinase p38 alpha,77519,17940
PDB,2LJJ,BMRB Entry Tracking System,77534,17941
BMRB,15209,hDlg in complex with a different peptide,77556,17942
PDB,2M3M,BMRB Entry Tracking System,77556,17942
BMRB,5740,Backbone assignments for the related E. coli DHFR:NADP+:folate complex,77628,17946
BMRB,16306,ferric protein,77648,17947
PDB,2ksc,ferric protein,77648,17947
PDB,2LJL,BMRB Entry Tracking System,77675,17948
PDB,2LJM,BMRB Entry Tracking System,77693,17949
PDB,4A1M,BMRB Entry Tracking System,77756,17953
BMRB,17958,"C9L,C14L-LeuA",77772,17955
PDB,2LJQ,BMRB Entry Tracking System,77772,17955
PDB,1nb1,This entry contains the all-L version of kalata B1,77788,17956
PDB,2LJS,BMRB Entry Tracking System,77788,17956
PDB,2LT2,BMRB Entry Tracking System,77806,17957
BMRB,17955,"(C9S,C14S)-leucocin A",77821,17958
PDB,2LJT,BMRB Entry Tracking System,77821,17958
PDB,2LKR,BMRB Entry Tracking System,77869,17961
PDB,2LJU,BMRB Entry Tracking System,77894,17962
PDB,3D3T,,77932,17964
BMRB,17968,N-terminal domain dimer of HPV16 E6,78001,17967
PDB,2LJX,BMRB Entry Tracking System,78001,17967
BMRB,17967,Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein,78024,17968
PDB,2ljx,Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein,78024,17968
PDB,2LJY,BMRB Entry Tracking System,78024,17968
BMRB,17970,RBM5-ZF1,78046,17969
PDB,2LK0,BMRB Entry Tracking System,78046,17969
BMRB,17969,RBM5-ZF1,78082,17970
PDB,2LK1,BMRB Entry Tracking System,78082,17970
PDB,2LK3,BMRB Entry Tracking System,78158,17972
PDB,2LK4,BMRB Entry Tracking System,78207,17974
BMRB,17976,PPARgamma LBD + MRL24,78222,17975
BMRB,17977,PPARgamma LBD + MRL20,78222,17975
BMRB,17975,PPARgamma LBD + rosigliazone,78241,17976
BMRB,17977,PPARgamma LBD + MRL20,78241,17976
BMRB,17975,PPARgamma LBD + rosigliazone,78260,17977
BMRB,17976,PPARgamma LBD + MRL24,78260,17977
BMRB,17997,Cd(II) form of Desulforedoxin,78298,17979
BMRB,5249,Backbone chemical shifts for desulforedoxin,78298,17979
BMRB,5260,Pseudocontact chemical shifts for [Fe(II)/Fe(II)]Dx,78298,17979
BMRB,5271,Pseudocontact chemical shifts for [Fe(II)/Zn(II)]Dx,78298,17979
PDB,1cfw,,78298,17979
PDB,1dcd,,78298,17979
PDB,1dhg,,78298,17979
PDB,1dxg,,78298,17979
PDB,2LK5,BMRB Entry Tracking System,78298,17979
PDB,2LK7,BMRB Entry Tracking System,78329,17980
BMRB,17881,"calcium calmodulin, apo form",78343,17981
BMRB,17982,"calcium calmodulin, complex with Ca",78343,17981
BMRB,17983,"calcium calmodulin, complex with Ca and PEP-19",78343,17981
BMRB,17881,"calcium calmodulin, apo form",78361,17982
BMRB,17981,"calcium calmodulin, complex with PEP-19",78361,17982
BMRB,17983,"calcium calmodulin, complex with Ca and PEP-19",78361,17982
BMRB,17881,"calcium calmodulin, apo form",78380,17983
BMRB,17981,"calcium calmodulin, complex with PEP-19",78380,17983
BMRB,17982,"calcium calmodulin, complex with Ca",78380,17983
PDB,2LK9,BMRB Entry Tracking System,78400,17985
PDB,1KFP,Solution structure of the antimicrobial 18-residue gomesin,78416,17986
PDB,2LO7,BMRB Entry Tracking System,78435,17987
PDB,2LKB,BMRB Entry Tracking System,78450,17988
PDB,2LW1,BMRB Entry Tracking System,78464,17989
PDB,2LKJ,BMRB Entry Tracking System,78496,17990
BMRB,17992,NMR Structure and Dynamics of Water-Solubilized Transmembrane Domains of Nicotinic Acetylcholine Receptor,78513,17991
PDB,2LKG,BMRB Entry Tracking System,78513,17991
BMRB,17991,NMR Structure and Dynamics of Water-Solubilized Transmembrane Domains of Nicotinic Acetylcholine Receptor,78530,17992
PDB,2LKH,BMRB Entry Tracking System,78530,17992
PDB,2LQ4,BMRB Entry Tracking System,78547,17993
BMRB,17964,inactive HIV-1 protease CRF01_AE,78562,17994
BMRB,17996,HIV-1 Protease subtype C,78562,17994
PDB,2LKI,BMRB Entry Tracking System,78579,17995
BMRB,17994,HIV-1 Protease subtype F,78604,17996
BMRB,17979,Zn(II) form of Desulforedoxin,78621,17997
BMRB,5249,Backbone chemical shifts for desulforedoxin,78621,17997
BMRB,5260,Pseudocontact chemical shifts for [Fe(II)/Fe(II)]Dx,78621,17997
BMRB,5271,Pseudocontact chemical shifts for [Fe(II)/Zn(II)]Dx,78621,17997
PDB,1cfw,,78621,17997
PDB,1dcd,,78621,17997
PDB,1dhg,,78621,17997
PDB,1dxg,,78621,17997
PDB,2LK6,BMRB Entry Tracking System,78621,17997
PDB,2F4E,FKBP42 domain X-ray structure,78639,17998
PDB,2IF4,FKBP42 X-ray structure,78639,17998
BMRB,16911,Chemical shift assignments of the structured core in isolation,78656,17999
PDB,2LKM,BMRB Entry Tracking System,78713,18000
PDB,2LKN,BMRB Entry Tracking System,78733,18001
PDB,2LKO,BMRB Entry Tracking System,78751,18002
PDB,2LKP,BMRB Entry Tracking System,78773,18003
BMRB,18005,Molecular System,78794,18004
BMRB,18006,Molecular System,78794,18004
BMRB,18007,Molecular System,78794,18004
BMRB,18008,Molecular System,78794,18004
PDB,4A24,BMRB Entry Tracking System,78794,18004
BMRB,18006,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78818,18005
BMRB,18007,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78818,18005
BMRB,18008,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78818,18005
PDB,4A4E,BMRB Entry Tracking System,78818,18005
BMRB,18005,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78839,18006
BMRB,18007,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78839,18006
BMRB,18008,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78839,18006
PDB,4A4F,BMRB Entry Tracking System,78839,18006
BMRB,18005,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78860,18007
BMRB,18006,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78860,18007
BMRB,18008,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78860,18007
PDB,4A4G,BMRB Entry Tracking System,78860,18007
BMRB,18005,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78881,18008
BMRB,18006,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78881,18008
BMRB,18078,AbpSH3-Srv17,79923,18065
BMRB,18007,Structural basis for dimethyl-arginine recognition by the Tudor domains of human SMN and SPF30 proteins,78881,18008
PDB,4A4H,BMRB Entry Tracking System,78881,18008
PDB,2LKQ,BMRB Entry Tracking System,78902,18009
BMRB,5537,Entry for the full length FF domain native state,78929,18010
PDB,1UZC,Entry for the full length FF domain native state,78929,18010
PDB,2KZG,Entry for the full length FF domain folding intermediate state,78929,18010
PDB,2LKS,BMRB Entry Tracking System,78929,18010
PDB,2LVV,BMRB Entry Tracking System,78949,18011
PDB,2LKT,BMRB Entry Tracking System,78963,18012
PDB,2LKV,BMRB Entry Tracking System,78987,18013
PDB,2LKW,BMRB Entry Tracking System,79009,18014
PDB,1YZ8,current entry is to replace entry 1YZ8,79025,18015
PDB,2LKX,BMRB Entry Tracking System,79025,18015
PDB,2LKZ,BMRB Entry Tracking System,79067,18017
PDB,2LL0,BMRB Entry Tracking System,79086,18018
PDB,2LL1,BMRB Entry Tracking System,79105,18019
BMRB,18021,Mg2+ bound Alpha1 I-domain,79134,18020
BMRB,18020,Apo Alpha1 I-domain,79150,18021
PDB,2LL2,BMRB Entry Tracking System,79167,18022
PDB,2LL5,BMRB Entry Tracking System,79182,18023
BMRB,18028,CaM bound to eNOS peptides,79248,18027
PDB,2LL6,BMRB Entry Tracking System,79248,18027
BMRB,18027,CaM bound to iNOS peptides,79265,18028
PDB,2LL7,BMRB Entry Tracking System,79265,18028
PDB,3o55,,79280,18029
BMRB,18030,Fap7 monomer,79311,18031
PDB,2LL8,BMRB Entry Tracking System,79332,18032
PDB,4A4T,BMRB Entry Tracking System,79385,18034
PDB,4A4U,BMRB Entry Tracking System,79401,18035
PDB,4A4S,BMRB Entry Tracking System,79417,18036
PDB,2LL9,BMRB Entry Tracking System,79495,18040
BMRB,18042,Assigned NMR chemical shifts of EDC3:DCP2,79511,18041
PDB,4A53,BMRB Entry Tracking System,79511,18041
BMRB,18041,Assigned NMR chemical shifts of EDC3-LSm domain,79526,18042
PDB,4A54,BMRB Entry Tracking System,79526,18042
PDB,2LLD,BMRB Entry Tracking System,79542,18043
BMRB,15097,Domain six is part of the larger D6-HP villin fragment,79597,18046
PDB,2LLF,BMRB Entry Tracking System,79597,18046
PDB,2LLG,BMRB Entry Tracking System,79620,18047
PDB,2LLH,BMRB Entry Tracking System,79635,18048
PDB,2VXD,,79635,18048
PDB,2LLI,BMRB Entry Tracking System,79657,18049
PDB,2LLJ,BMRB Entry Tracking System,79674,18050
PDB,2LLL,BMRB Entry Tracking System,79735,18053
BMRB,18055,AbpSH3-ArkA,79759,18054
BMRB,18056,AbpSH3-ArkB,79759,18054
BMRB,18057,AbpSH3-ArkA_H(-6)A,79759,18054
BMRB,18058,AbpSH3-ArkA_SI,79759,18054
BMRB,18059,AbpSH3-ArkA_K(-3)A,79759,18054
BMRB,18060,AbpSH3-ArkA_K(-3)R,79759,18054
BMRB,18061,AbpSH3-ArkA_K(-3)V,79759,18054
BMRB,18062,AbpSH3-ArkA_K(3)A,79759,18054
BMRB,18063,AbpSH3-ArkA_L(-7)A,79759,18054
BMRB,18064,AbpSH3-ArkA_L(-7)V,79759,18054
BMRB,18065,AbpSH3-ArkA12,79759,18054
BMRB,18066,AbpSH3-ArkA_P(-4)A,79759,18054
BMRB,18067,AbpSH3-ArkA_P(2)A,79759,18054
BMRB,18068,AbpSH3-ArkA_P(2)V,79759,18054
BMRB,18069,AbpSH3-ArkA_P(0)A,79759,18054
BMRB,18070,AbpSH3-ArkA_P(-1)A,79759,18054
BMRB,18071,AbpSH3-Prk17,79759,18054
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79759,18054
BMRB,18073,AbpSH3-PRR,79759,18054
BMRB,18074,AbpSH3-Scp12,79759,18054
BMRB,18075,AbpSH3-Scp17,79759,18054
BMRB,18076,AbpSH3-Sjl17,79759,18054
BMRB,18077,AbpSH3-Srv12,79759,18054
BMRB,18078,AbpSH3-Srv17,79759,18054
BMRB,18054,monomer (free AbpSH3),79773,18055
BMRB,18056,AbpSH3-ArkB,79773,18055
BMRB,18057,AbpSH3-ArkA_H(-6)A,79773,18055
BMRB,18058,AbpSH3-ArkA_SI,79773,18055
BMRB,18059,AbpSH3-ArkA_K(-3)A,79773,18055
BMRB,18060,AbpSH3-ArkA_K(-3)R,79773,18055
BMRB,18061,AbpSH3-ArkA_K(-3)V,79773,18055
BMRB,18062,AbpSH3-ArkA_K(3)A,79773,18055
BMRB,18063,AbpSH3-ArkA_L(-7)A,79773,18055
BMRB,18064,AbpSH3-ArkA_L(-7)V,79773,18055
BMRB,18065,AbpSH3-ArkA12,79773,18055
BMRB,18066,AbpSH3-ArkA_P(-4)A,79773,18055
BMRB,18067,AbpSH3-ArkA_P(2)A,79773,18055
BMRB,18068,AbpSH3-ArkA_P(2)V,79773,18055
BMRB,18069,AbpSH3-ArkA_P(0)A,79773,18055
BMRB,18070,AbpSH3-ArkA_P(-1)A,79773,18055
BMRB,18071,AbpSH3-Prk17,79773,18055
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79773,18055
BMRB,18073,AbpSH3-PRR,79773,18055
BMRB,18074,AbpSH3-Scp12,79773,18055
BMRB,18075,AbpSH3-Scp17,79773,18055
BMRB,18076,AbpSH3-Sjl17,79773,18055
BMRB,18077,AbpSH3-Srv12,79773,18055
BMRB,18078,AbpSH3-Srv17,79773,18055
BMRB,18054,monomer (free AbpSH3),79788,18056
BMRB,18055,AbpSH3-ArkA,79788,18056
BMRB,18057,AbpSH3-ArkA_H(-6)A,79788,18056
BMRB,18058,AbpSH3-ArkA_SI,79788,18056
BMRB,18059,AbpSH3-ArkA_K(-3)A,79788,18056
BMRB,18060,AbpSH3-ArkA_K(-3)R,79788,18056
BMRB,18061,AbpSH3-ArkA_K(-3)V,79788,18056
BMRB,18062,AbpSH3-ArkA_K(3)A,79788,18056
BMRB,18063,AbpSH3-ArkA_L(-7)A,79788,18056
BMRB,18064,AbpSH3-ArkA_L(-7)V,79788,18056
BMRB,18065,AbpSH3-ArkA12,79788,18056
BMRB,18066,AbpSH3-ArkA_P(-4)A,79788,18056
BMRB,18067,AbpSH3-ArkA_P(2)A,79788,18056
BMRB,18068,AbpSH3-ArkA_P(2)V,79788,18056
BMRB,18069,AbpSH3-ArkA_P(0)A,79788,18056
BMRB,18070,AbpSH3-ArkA_P(-1)A,79788,18056
BMRB,18071,AbpSH3-Prk17,79788,18056
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79788,18056
BMRB,18073,AbpSH3-PRR,79788,18056
BMRB,18074,AbpSH3-Scp12,79788,18056
BMRB,18075,AbpSH3-Scp17,79788,18056
BMRB,18076,AbpSH3-Sjl17,79788,18056
BMRB,18077,AbpSH3-Srv12,79788,18056
BMRB,18078,AbpSH3-Srv17,79788,18056
BMRB,18054,monomer (free AbpSH3),79803,18057
BMRB,18055,AbpSH3-ArkA,79803,18057
BMRB,18056,AbpSH3-ArkB,79803,18057
BMRB,18058,AbpSH3-ArkA_SI,79803,18057
BMRB,18059,AbpSH3-ArkA_K(-3)A,79803,18057
BMRB,18060,AbpSH3-ArkA_K(-3)R,79803,18057
BMRB,18061,AbpSH3-ArkA_K(-3)V,79803,18057
BMRB,18062,AbpSH3-ArkA_K(3)A,79803,18057
BMRB,18063,AbpSH3-ArkA_L(-7)A,79803,18057
BMRB,18064,AbpSH3-ArkA_L(-7)V,79803,18057
BMRB,18065,AbpSH3-ArkA12,79803,18057
BMRB,18066,AbpSH3-ArkA_P(-4)A,79803,18057
BMRB,18067,AbpSH3-ArkA_P(2)A,79803,18057
BMRB,18068,AbpSH3-ArkA_P(2)V,79803,18057
BMRB,18069,AbpSH3-ArkA_P(0)A,79803,18057
BMRB,18070,AbpSH3-ArkA_P(-1)A,79803,18057
BMRB,18071,AbpSH3-Prk17,79803,18057
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79803,18057
BMRB,18073,AbpSH3-PRR,79803,18057
BMRB,18074,AbpSH3-Scp12,79803,18057
BMRB,18075,AbpSH3-Scp17,79803,18057
BMRB,18076,AbpSH3-Sjl17,79803,18057
BMRB,18077,AbpSH3-Srv12,79803,18057
BMRB,18078,AbpSH3-Srv17,79803,18057
BMRB,18054,monomer (free AbpSH3),79818,18058
BMRB,18055,AbpSH3-ArkA,79818,18058
BMRB,18056,AbpSH3-ArkB,79818,18058
BMRB,18057,AbpSH3-ArkA_H(-6)A,79818,18058
BMRB,18059,AbpSH3-ArkA_K(-3)A,79818,18058
BMRB,18060,AbpSH3-ArkA_K(-3)R,79818,18058
BMRB,18061,AbpSH3-ArkA_K(-3)V,79818,18058
BMRB,18062,AbpSH3-ArkA_K(3)A,79818,18058
BMRB,18063,AbpSH3-ArkA_L(-7)A,79818,18058
BMRB,18064,AbpSH3-ArkA_L(-7)V,79818,18058
BMRB,18065,AbpSH3-ArkA12,79818,18058
BMRB,18066,AbpSH3-ArkA_P(-4)A,79818,18058
BMRB,18067,AbpSH3-ArkA_P(2)A,79818,18058
BMRB,18068,AbpSH3-ArkA_P(2)V,79818,18058
BMRB,18069,AbpSH3-ArkA_P(0)A,79818,18058
BMRB,18070,AbpSH3-ArkA_P(-1)A,79818,18058
BMRB,18071,AbpSH3-Prk17,79818,18058
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79818,18058
BMRB,18073,AbpSH3-PRR,79818,18058
BMRB,18074,AbpSH3-Scp12,79818,18058
BMRB,18075,AbpSH3-Scp17,79818,18058
BMRB,18076,AbpSH3-Sjl17,79818,18058
BMRB,18077,AbpSH3-Srv12,79818,18058
BMRB,18078,AbpSH3-Srv17,79818,18058
BMRB,18054,monomer (free AbpSH3),79833,18059
BMRB,18055,AbpSH3-ArkA,79833,18059
BMRB,18056,AbpSH3-ArkB,79833,18059
BMRB,18057,AbpSH3-ArkA_H(-6)A,79833,18059
BMRB,18058,AbpSH3-ArkA_SI,79833,18059
BMRB,18060,AbpSH3-ArkA_K(-3)R,79833,18059
BMRB,18061,AbpSH3-ArkA_K(-3)V,79833,18059
BMRB,18062,AbpSH3-ArkA_K(3)A,79833,18059
BMRB,18063,AbpSH3-ArkA_L(-7)A,79833,18059
BMRB,18064,AbpSH3-ArkA_L(-7)V,79833,18059
BMRB,18065,AbpSH3-ArkA12,79833,18059
BMRB,18066,AbpSH3-ArkA_P(-4)A,79833,18059
BMRB,18067,AbpSH3-ArkA_P(2)A,79833,18059
BMRB,18068,AbpSH3-ArkA_P(2)V,79833,18059
BMRB,18069,AbpSH3-ArkA_P(0)A,79833,18059
BMRB,18070,AbpSH3-ArkA_P(-1)A,79833,18059
BMRB,18071,AbpSH3-Prk17,79833,18059
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79833,18059
BMRB,18073,AbpSH3-PRR,79833,18059
BMRB,18074,AbpSH3-Scp12,79833,18059
BMRB,18075,AbpSH3-Scp17,79833,18059
BMRB,18076,AbpSH3-Sjl17,79833,18059
BMRB,18077,AbpSH3-Srv12,79833,18059
BMRB,18078,AbpSH3-Srv17,79833,18059
BMRB,18054,monomer (free AbpSH3),79848,18060
BMRB,18055,AbpSH3-ArkA,79848,18060
BMRB,18056,AbpSH3-ArkB,79848,18060
BMRB,18057,AbpSH3-ArkA_H(-6)A,79848,18060
BMRB,18058,AbpSH3-ArkA_SI,79848,18060
BMRB,18059,AbpSH3-ArkA_K(-3)A,79848,18060
BMRB,18061,AbpSH3-ArkA_K(-3)V,79848,18060
BMRB,18062,AbpSH3-ArkA_K(3)A,79848,18060
BMRB,18063,AbpSH3-ArkA_L(-7)A,79848,18060
BMRB,18064,AbpSH3-ArkA_L(-7)V,79848,18060
BMRB,18065,AbpSH3-ArkA12,79848,18060
BMRB,18066,AbpSH3-ArkA_P(-4)A,79848,18060
BMRB,18067,AbpSH3-ArkA_P(2)A,79848,18060
BMRB,18068,AbpSH3-ArkA_P(2)V,79848,18060
BMRB,18069,AbpSH3-ArkA_P(0)A,79848,18060
BMRB,18070,AbpSH3-ArkA_P(-1)A,79848,18060
BMRB,18071,AbpSH3-Prk17,79848,18060
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79848,18060
BMRB,18073,AbpSH3-PRR,79848,18060
BMRB,18074,AbpSH3-Scp12,79848,18060
BMRB,18075,AbpSH3-Scp17,79848,18060
BMRB,18076,AbpSH3-Sjl17,79848,18060
BMRB,18077,AbpSH3-Srv12,79848,18060
BMRB,18078,AbpSH3-Srv17,79848,18060
BMRB,18054,monomer (free AbpSH3),79863,18061
BMRB,18055,AbpSH3-ArkA,79863,18061
BMRB,18056,AbpSH3-ArkB,79863,18061
BMRB,18057,AbpSH3-ArkA_H(-6)A,79863,18061
BMRB,18058,AbpSH3-ArkA_SI,79863,18061
BMRB,18059,AbpSH3-ArkA_K(-3)A,79863,18061
BMRB,18060,AbpSH3-ArkA_K(-3)R,79863,18061
BMRB,18062,AbpSH3-ArkA_K(3)A,79863,18061
BMRB,18063,AbpSH3-ArkA_L(-7)A,79863,18061
BMRB,18064,AbpSH3-ArkA_L(-7)V,79863,18061
BMRB,18065,AbpSH3-ArkA12,79863,18061
BMRB,18066,AbpSH3-ArkA_P(-4)A,79863,18061
BMRB,18067,AbpSH3-ArkA_P(2)A,79863,18061
BMRB,18068,AbpSH3-ArkA_P(2)V,79863,18061
BMRB,18069,AbpSH3-ArkA_P(0)A,79863,18061
BMRB,18070,AbpSH3-ArkA_P(-1)A,79863,18061
BMRB,18071,AbpSH3-Prk17,79863,18061
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79863,18061
BMRB,18073,AbpSH3-PRR,79863,18061
BMRB,18074,AbpSH3-Scp12,79863,18061
BMRB,18075,AbpSH3-Scp17,79863,18061
BMRB,18076,AbpSH3-Sjl17,79863,18061
BMRB,18077,AbpSH3-Srv12,79863,18061
BMRB,18078,AbpSH3-Srv17,79863,18061
BMRB,18054,monomer (free AbpSH3),79878,18062
BMRB,18055,AbpSH3-ArkA,79878,18062
BMRB,18056,AbpSH3-ArkB,79878,18062
BMRB,18057,AbpSH3-ArkA_H(-6)A,79878,18062
BMRB,18058,AbpSH3-ArkA_SI,79878,18062
BMRB,18059,AbpSH3-ArkA_K(-3)A,79878,18062
BMRB,18060,AbpSH3-ArkA_K(-3)R,79878,18062
BMRB,18061,AbpSH3-ArkA_K(-3)V,79878,18062
BMRB,18063,AbpSH3-ArkA_L(-7)A,79878,18062
BMRB,18064,AbpSH3-ArkA_L(-7)V,79878,18062
BMRB,18065,AbpSH3-ArkA12,79878,18062
BMRB,18066,AbpSH3-ArkA_P(-4)A,79878,18062
BMRB,18067,AbpSH3-ArkA_P(2)A,79878,18062
BMRB,18068,AbpSH3-ArkA_P(2)V,79878,18062
BMRB,18069,AbpSH3-ArkA_P(0)A,79878,18062
BMRB,18070,AbpSH3-ArkA_P(-1)A,79878,18062
BMRB,18071,AbpSH3-Prk17,79878,18062
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79878,18062
BMRB,18073,AbpSH3-PRR,79878,18062
BMRB,18074,AbpSH3-Scp12,79878,18062
BMRB,18075,AbpSH3-Scp17,79878,18062
BMRB,18076,AbpSH3-Sjl17,79878,18062
BMRB,18077,AbpSH3-Srv12,79878,18062
BMRB,18078,AbpSH3-Srv17,79878,18062
BMRB,18054,monomer (free AbpSH3),79893,18063
BMRB,18055,AbpSH3-ArkA,79893,18063
BMRB,18056,AbpSH3-ArkB,79893,18063
BMRB,18057,AbpSH3-ArkA_H(-6)A,79893,18063
BMRB,18058,AbpSH3-ArkA_SI,79893,18063
BMRB,18059,AbpSH3-ArkA_K(-3)A,79893,18063
BMRB,18060,AbpSH3-ArkA_K(-3)R,79893,18063
BMRB,18061,AbpSH3-ArkA_K(-3)V,79893,18063
BMRB,18062,AbpSH3-ArkA_K(3)A,79893,18063
BMRB,18064,AbpSH3-ArkA_L(-7)V,79893,18063
BMRB,18065,AbpSH3-ArkA12,79893,18063
BMRB,18066,AbpSH3-ArkA_P(-4)A,79893,18063
BMRB,18067,AbpSH3-ArkA_P(2)A,79893,18063
BMRB,18068,AbpSH3-ArkA_P(2)V,79893,18063
BMRB,18069,AbpSH3-ArkA_P(0)A,79893,18063
BMRB,18070,AbpSH3-ArkA_P(-1)A,79893,18063
BMRB,18071,AbpSH3-Prk17,79893,18063
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79893,18063
BMRB,18073,AbpSH3-PRR,79893,18063
BMRB,18074,AbpSH3-Scp12,79893,18063
BMRB,18075,AbpSH3-Scp17,79893,18063
BMRB,18076,AbpSH3-Sjl17,79893,18063
BMRB,18077,AbpSH3-Srv12,79893,18063
BMRB,18078,AbpSH3-Srv17,79893,18063
BMRB,18054,monomer (free AbpSH3),79908,18064
BMRB,18055,AbpSH3-ArkA,79908,18064
BMRB,18056,AbpSH3-ArkB,79908,18064
BMRB,18057,AbpSH3-ArkA_H(-6)A,79908,18064
BMRB,18058,AbpSH3-ArkA_SI,79908,18064
BMRB,18059,AbpSH3-ArkA_K(-3)A,79908,18064
BMRB,18060,AbpSH3-ArkA_K(-3)R,79908,18064
BMRB,18061,AbpSH3-ArkA_K(-3)V,79908,18064
BMRB,18062,AbpSH3-ArkA_K(3)A,79908,18064
BMRB,18063,AbpSH3-ArkA_L(-7)A,79908,18064
BMRB,18065,AbpSH3-ArkA12,79908,18064
BMRB,18066,AbpSH3-ArkA_P(-4)A,79908,18064
BMRB,18067,AbpSH3-ArkA_P(2)A,79908,18064
BMRB,18068,AbpSH3-ArkA_P(2)V,79908,18064
BMRB,18069,AbpSH3-ArkA_P(0)A,79908,18064
BMRB,18070,AbpSH3-ArkA_P(-1)A,79908,18064
BMRB,18071,AbpSH3-Prk17,79908,18064
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79908,18064
BMRB,18073,AbpSH3-PRR,79908,18064
BMRB,18074,AbpSH3-Scp12,79908,18064
BMRB,18075,AbpSH3-Scp17,79908,18064
BMRB,18076,AbpSH3-Sjl17,79908,18064
BMRB,18077,AbpSH3-Srv12,79908,18064
BMRB,18078,AbpSH3-Srv17,79908,18064
BMRB,18054,monomer (free AbpSH3),79923,18065
BMRB,18055,AbpSH3-ArkA,79923,18065
BMRB,18056,AbpSH3-ArkB,79923,18065
BMRB,18057,AbpSH3-ArkA_H(-6)A,79923,18065
BMRB,18058,AbpSH3-ArkA_SI,79923,18065
BMRB,18059,AbpSH3-ArkA_K(-3)A,79923,18065
BMRB,18060,AbpSH3-ArkA_K(-3)R,79923,18065
BMRB,18061,AbpSH3-ArkA_K(-3)V,79923,18065
BMRB,18062,AbpSH3-ArkA_K(3)A,79923,18065
BMRB,18063,AbpSH3-ArkA_L(-7)A,79923,18065
BMRB,18064,AbpSH3-ArkA_L(-7)V,79923,18065
BMRB,18066,AbpSH3-ArkA_P(-4)A,79923,18065
BMRB,18067,AbpSH3-ArkA_P(2)A,79923,18065
BMRB,18068,AbpSH3-ArkA_P(2)V,79923,18065
BMRB,18069,AbpSH3-ArkA_P(0)A,79923,18065
BMRB,18070,AbpSH3-ArkA_P(-1)A,79923,18065
BMRB,18071,AbpSH3-Prk17,79923,18065
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79923,18065
BMRB,18073,AbpSH3-PRR,79923,18065
BMRB,18074,AbpSH3-Scp12,79923,18065
BMRB,18075,AbpSH3-Scp17,79923,18065
BMRB,18076,AbpSH3-Sjl17,79923,18065
BMRB,18054,monomer (free AbpSH3),79938,18066
BMRB,18055,AbpSH3-ArkA,79938,18066
BMRB,18056,AbpSH3-ArkB,79938,18066
BMRB,18057,AbpSH3-ArkA_H(-6)A,79938,18066
BMRB,18058,AbpSH3-ArkA_SI,79938,18066
BMRB,18059,AbpSH3-ArkA_K(-3)A,79938,18066
BMRB,18060,AbpSH3-ArkA_K(-3)R,79938,18066
BMRB,18061,AbpSH3-ArkA_K(-3)V,79938,18066
BMRB,18062,AbpSH3-ArkA_K(3)A,79938,18066
BMRB,18063,AbpSH3-ArkA_L(-7)A,79938,18066
BMRB,18064,AbpSH3-ArkA_L(-7)V,79938,18066
BMRB,18065,AbpSH3-ArkA12,79938,18066
BMRB,18067,AbpSH3-ArkA_P(2)A,79938,18066
BMRB,18068,AbpSH3-ArkA_P(2)V,79938,18066
BMRB,18069,AbpSH3-ArkA_P(0)A,79938,18066
BMRB,18070,AbpSH3-ArkA_P(-1)A,79938,18066
BMRB,18071,AbpSH3-Prk17,79938,18066
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79938,18066
BMRB,18073,AbpSH3-PRR,79938,18066
BMRB,18074,AbpSH3-Scp12,79938,18066
BMRB,18075,AbpSH3-Scp17,79938,18066
BMRB,18076,AbpSH3-Sjl17,79938,18066
BMRB,18077,AbpSH3-Srv12,79938,18066
BMRB,18078,AbpSH3-Srv17,79938,18066
BMRB,18054,monomer (free AbpSH3),79953,18067
BMRB,18055,AbpSH3-ArkA,79953,18067
BMRB,18056,AbpSH3-ArkB,79953,18067
BMRB,18057,AbpSH3-ArkA_H(-6)A,79953,18067
BMRB,18058,AbpSH3-ArkA_SI,79953,18067
BMRB,18059,AbpSH3-ArkA_K(-3)A,79953,18067
BMRB,18060,AbpSH3-ArkA_K(-3)R,79953,18067
BMRB,18061,AbpSH3-ArkA_K(-3)V,79953,18067
BMRB,18062,AbpSH3-ArkA_K(3)A,79953,18067
BMRB,18063,AbpSH3-ArkA_L(-7)A,79953,18067
BMRB,18064,AbpSH3-ArkA_L(-7)V,79953,18067
BMRB,18065,AbpSH3-ArkA12,79953,18067
BMRB,18066,AbpSH3-ArkA_P(-4)A,79953,18067
BMRB,18068,AbpSH3-ArkA_P(2)V,79953,18067
BMRB,18069,AbpSH3-ArkA_P(0)A,79953,18067
BMRB,18070,AbpSH3-ArkA_P(-1)A,79953,18067
BMRB,18071,AbpSH3-Prk17,79953,18067
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79953,18067
BMRB,18073,AbpSH3-PRR,79953,18067
BMRB,18074,AbpSH3-Scp12,79953,18067
BMRB,18075,AbpSH3-Scp17,79953,18067
BMRB,18076,AbpSH3-Sjl17,79953,18067
BMRB,18077,AbpSH3-Srv12,79953,18067
BMRB,18078,AbpSH3-Srv17,79953,18067
BMRB,18054,monomer (free AbpSH3),79968,18068
BMRB,18055,AbpSH3-ArkA,79968,18068
BMRB,18056,AbpSH3-ArkB,79968,18068
BMRB,18057,AbpSH3-ArkA_H(-6)A,79968,18068
BMRB,18058,AbpSH3-ArkA_SI,79968,18068
BMRB,18059,AbpSH3-ArkA_K(-3)A,79968,18068
BMRB,18060,AbpSH3-ArkA_K(-3)R,79968,18068
BMRB,18061,AbpSH3-ArkA_K(-3)V,79968,18068
BMRB,18062,AbpSH3-ArkA_K(3)A,79968,18068
BMRB,18063,AbpSH3-ArkA_L(-7)A,79968,18068
BMRB,18064,AbpSH3-ArkA_L(-7)V,79968,18068
BMRB,18065,AbpSH3-ArkA12,79968,18068
BMRB,18066,AbpSH3-ArkA_P(-4)A,79968,18068
BMRB,18067,AbpSH3-ArkA_P(2)A,79968,18068
BMRB,18069,AbpSH3-ArkA_P(0)A,79968,18068
BMRB,18070,AbpSH3-ArkA_P(-1)A,79968,18068
BMRB,18071,AbpSH3-Prk17,79968,18068
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79968,18068
BMRB,18073,AbpSH3-PRR,79968,18068
BMRB,18074,AbpSH3-Scp12,79968,18068
BMRB,18075,AbpSH3-Scp17,79968,18068
BMRB,18076,AbpSH3-Sjl17,79968,18068
BMRB,18077,AbpSH3-Srv12,79968,18068
BMRB,18078,AbpSH3-Srv17,79968,18068
BMRB,18054,monomer (free AbpSH3),79983,18069
BMRB,18055,AbpSH3-ArkA,79983,18069
BMRB,18056,AbpSH3-ArkB,79983,18069
BMRB,18057,AbpSH3-ArkA_H(-6)A,79983,18069
BMRB,18058,AbpSH3-ArkA_SI,79983,18069
BMRB,18059,AbpSH3-ArkA_K(-3)A,79983,18069
BMRB,18060,AbpSH3-ArkA_K(-3)R,79983,18069
BMRB,18061,AbpSH3-ArkA_K(-3)V,79983,18069
BMRB,18062,AbpSH3-ArkA_K(3)A,79983,18069
BMRB,18063,AbpSH3-ArkA_L(-7)A,79983,18069
BMRB,18064,AbpSH3-ArkA_L(-7)V,79983,18069
BMRB,18065,AbpSH3-ArkA12,79983,18069
BMRB,18066,AbpSH3-ArkA_P(-4)A,79983,18069
BMRB,18067,AbpSH3-ArkA_P(2)A,79983,18069
BMRB,18068,AbpSH3-ArkA_P(2)V,79983,18069
BMRB,18070,AbpSH3-ArkA_P(-1)A,79983,18069
BMRB,18071,AbpSH3-Prk17,79983,18069
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79983,18069
BMRB,18073,AbpSH3-PRR,79983,18069
BMRB,18074,AbpSH3-Scp12,79983,18069
BMRB,18075,AbpSH3-Scp17,79983,18069
BMRB,18076,AbpSH3-Sjl17,79983,18069
BMRB,18077,AbpSH3-Srv12,79983,18069
BMRB,18078,AbpSH3-Srv17,79983,18069
BMRB,18054,monomer (free AbpSH3),79998,18070
BMRB,18055,AbpSH3-ArkA,79998,18070
BMRB,18056,AbpSH3-ArkB,79998,18070
BMRB,18057,AbpSH3-ArkA_H(-6)A,79998,18070
BMRB,18058,AbpSH3-ArkA_SI,79998,18070
BMRB,18059,AbpSH3-ArkA_K(-3)A,79998,18070
BMRB,18060,AbpSH3-ArkA_K(-3)R,79998,18070
BMRB,18061,AbpSH3-ArkA_K(-3)V,79998,18070
BMRB,18062,AbpSH3-ArkA_K(3)A,79998,18070
BMRB,18063,AbpSH3-ArkA_L(-7)A,79998,18070
BMRB,18064,AbpSH3-ArkA_L(-7)V,79998,18070
BMRB,18065,AbpSH3-ArkA12,79998,18070
BMRB,18066,AbpSH3-ArkA_P(-4)A,79998,18070
BMRB,18067,AbpSH3-ArkA_P(2)A,79998,18070
BMRB,18068,AbpSH3-ArkA_P(2)V,79998,18070
BMRB,18069,AbpSH3-ArkA_P(0)A,79998,18070
BMRB,18071,AbpSH3-Prk17,79998,18070
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,79998,18070
BMRB,18073,AbpSH3-PRR,79998,18070
BMRB,18074,AbpSH3-Scp12,79998,18070
BMRB,18075,AbpSH3-Scp17,79998,18070
BMRB,18076,AbpSH3-Sjl17,79998,18070
BMRB,18077,AbpSH3-Srv12,79998,18070
BMRB,18078,AbpSH3-Srv17,79998,18070
BMRB,18054,monomer (free AbpSH3),80013,18071
BMRB,18055,AbpSH3-ArkA,80013,18071
BMRB,18056,AbpSH3-ArkB,80013,18071
BMRB,18057,AbpSH3-ArkA_H(-6)A,80013,18071
BMRB,18058,AbpSH3-ArkA_SI,80013,18071
BMRB,18059,AbpSH3-ArkA_K(-3)A,80013,18071
BMRB,18060,AbpSH3-ArkA_K(-3)R,80013,18071
BMRB,18061,AbpSH3-ArkA_K(-3)V,80013,18071
BMRB,18062,AbpSH3-ArkA_K(3)A,80013,18071
BMRB,18063,AbpSH3-ArkA_L(-7)A,80013,18071
BMRB,18064,AbpSH3-ArkA_L(-7)V,80013,18071
BMRB,18065,AbpSH3-ArkA12,80013,18071
BMRB,18066,AbpSH3-ArkA_P(-4)A,80013,18071
BMRB,18067,AbpSH3-ArkA_P(2)A,80013,18071
BMRB,18068,AbpSH3-ArkA_P(2)V,80013,18071
BMRB,18069,AbpSH3-ArkA_P(0)A,80013,18071
BMRB,18070,AbpSH3-ArkA_P(-1)A,80013,18071
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80013,18071
BMRB,18073,AbpSH3-PRR,80013,18071
BMRB,18074,AbpSH3-Scp12,80013,18071
BMRB,18075,AbpSH3-Scp17,80013,18071
BMRB,18076,AbpSH3-Sjl17,80013,18071
BMRB,18077,AbpSH3-Srv12,80013,18071
BMRB,18078,AbpSH3-Srv17,80013,18071
BMRB,18054,monomer (free AbpSH3),80028,18072
BMRB,18055,AbpSH3-ArkA,80028,18072
BMRB,18056,AbpSH3-ArkB,80028,18072
BMRB,18057,AbpSH3-ArkA_H(-6)A,80028,18072
BMRB,18058,AbpSH3-ArkA_SI,80028,18072
BMRB,18059,AbpSH3-ArkA_K(-3)A,80028,18072
BMRB,18060,AbpSH3-ArkA_K(-3)R,80028,18072
BMRB,18061,AbpSH3-ArkA_K(-3)V,80028,18072
BMRB,18062,AbpSH3-ArkA_K(3)A,80028,18072
BMRB,18063,AbpSH3-ArkA_L(-7)A,80028,18072
BMRB,18064,AbpSH3-ArkA_L(-7)V,80028,18072
BMRB,18065,AbpSH3-ArkA12,80028,18072
BMRB,18066,AbpSH3-ArkA_P(-4)A,80028,18072
BMRB,18067,AbpSH3-ArkA_P(2)A,80028,18072
BMRB,18068,AbpSH3-ArkA_P(2)V,80028,18072
BMRB,18069,AbpSH3-ArkA_P(0)A,80028,18072
BMRB,18070,AbpSH3-ArkA_P(-1)A,80028,18072
BMRB,18071,AbpSH3-Prk17,80028,18072
BMRB,18073,AbpSH3-PRR,80028,18072
BMRB,18074,AbpSH3-Scp12,80028,18072
BMRB,18075,AbpSH3-Scp17,80028,18072
BMRB,18076,AbpSH3-Sjl17,80028,18072
BMRB,18077,AbpSH3-Srv12,80028,18072
BMRB,18078,AbpSH3-Srv17,80028,18072
BMRB,18054,monomer (free AbpSH3),80043,18073
BMRB,18055,AbpSH3-ArkA,80043,18073
BMRB,18056,AbpSH3-ArkB,80043,18073
BMRB,18057,AbpSH3-ArkA_H(-6)A,80043,18073
BMRB,18058,AbpSH3-ArkA_SI,80043,18073
BMRB,18059,AbpSH3-ArkA_K(-3)A,80043,18073
BMRB,18060,AbpSH3-ArkA_K(-3)R,80043,18073
BMRB,18061,AbpSH3-ArkA_K(-3)V,80043,18073
BMRB,18062,AbpSH3-ArkA_K(3)A,80043,18073
BMRB,18063,AbpSH3-ArkA_L(-7)A,80043,18073
BMRB,18064,AbpSH3-ArkA_L(-7)V,80043,18073
BMRB,18065,AbpSH3-ArkA12,80043,18073
BMRB,18066,AbpSH3-ArkA_P(-4)A,80043,18073
BMRB,18067,AbpSH3-ArkA_P(2)A,80043,18073
BMRB,18068,AbpSH3-ArkA_P(2)V,80043,18073
BMRB,18069,AbpSH3-ArkA_P(0)A,80043,18073
BMRB,18070,AbpSH3-ArkA_P(-1)A,80043,18073
BMRB,18071,AbpSH3-Prk17,80043,18073
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80043,18073
BMRB,18074,AbpSH3-Scp12,80043,18073
BMRB,18075,AbpSH3-Scp17,80043,18073
BMRB,18076,AbpSH3-Sjl17,80043,18073
BMRB,18077,AbpSH3-Srv12,80043,18073
BMRB,18078,AbpSH3-Srv17,80043,18073
BMRB,18054,monomer (free AbpSH3),80058,18074
BMRB,18055,AbpSH3-ArkA,80058,18074
BMRB,18056,AbpSH3-ArkB,80058,18074
BMRB,18057,AbpSH3-ArkA_H(-6)A,80058,18074
BMRB,18058,AbpSH3-ArkA_SI,80058,18074
BMRB,18059,AbpSH3-ArkA_K(-3)A,80058,18074
BMRB,18060,AbpSH3-ArkA_K(-3)R,80058,18074
BMRB,18061,AbpSH3-ArkA_K(-3)V,80058,18074
BMRB,18062,AbpSH3-ArkA_K(3)A,80058,18074
BMRB,18063,AbpSH3-ArkA_L(-7)A,80058,18074
BMRB,18064,AbpSH3-ArkA_L(-7)V,80058,18074
BMRB,18065,AbpSH3-ArkA12,80058,18074
BMRB,18066,AbpSH3-ArkA_P(-4)A,80058,18074
BMRB,18067,AbpSH3-ArkA_P(2)A,80058,18074
BMRB,18068,AbpSH3-ArkA_P(2)V,80058,18074
BMRB,18069,AbpSH3-ArkA_P(0)A,80058,18074
BMRB,18070,AbpSH3-ArkA_P(-1)A,80058,18074
BMRB,18071,AbpSH3-Prk17,80058,18074
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80058,18074
BMRB,18073,AbpSH3-PRR,80058,18074
BMRB,18075,AbpSH3-Scp17,80058,18074
BMRB,18076,AbpSH3-Sjl17,80058,18074
BMRB,18077,AbpSH3-Srv12,80058,18074
BMRB,18078,AbpSH3-Srv17,80058,18074
BMRB,18054,monomer (free AbpSH3),80073,18075
BMRB,18055,AbpSH3-ArkA,80073,18075
BMRB,18056,AbpSH3-ArkB,80073,18075
BMRB,18057,AbpSH3-ArkA_H(-6)A,80073,18075
BMRB,18058,AbpSH3-ArkA_SI,80073,18075
BMRB,18059,AbpSH3-ArkA_K(-3)A,80073,18075
BMRB,18060,AbpSH3-ArkA_K(-3)R,80073,18075
BMRB,18061,AbpSH3-ArkA_K(-3)V,80073,18075
BMRB,18062,AbpSH3-ArkA_K(3)A,80073,18075
BMRB,18063,AbpSH3-ArkA_L(-7)A,80073,18075
BMRB,18064,AbpSH3-ArkA_L(-7)V,80073,18075
BMRB,18065,AbpSH3-ArkA12,80073,18075
BMRB,18066,AbpSH3-ArkA_P(-4)A,80073,18075
BMRB,18067,AbpSH3-ArkA_P(2)A,80073,18075
BMRB,18068,AbpSH3-ArkA_P(2)V,80073,18075
BMRB,18069,AbpSH3-ArkA_P(0)A,80073,18075
BMRB,18070,AbpSH3-ArkA_P(-1)A,80073,18075
BMRB,18071,AbpSH3-Prk17,80073,18075
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80073,18075
BMRB,18073,AbpSH3-PRR,80073,18075
BMRB,18074,AbpSH3-Scp12,80073,18075
BMRB,18076,AbpSH3-Sjl17,80073,18075
BMRB,18077,AbpSH3-Srv12,80073,18075
BMRB,18078,AbpSH3-Srv17,80073,18075
BMRB,18054,monomer (free AbpSH3),80088,18076
BMRB,18055,AbpSH3-ArkA,80088,18076
BMRB,18056,AbpSH3-ArkB,80088,18076
BMRB,18057,AbpSH3-ArkA_H(-6)A,80088,18076
BMRB,18058,AbpSH3-ArkA_SI,80088,18076
BMRB,18059,AbpSH3-ArkA_K(-3)A,80088,18076
BMRB,18060,AbpSH3-ArkA_K(-3)R,80088,18076
BMRB,18061,AbpSH3-ArkA_K(-3)V,80088,18076
BMRB,18062,AbpSH3-ArkA_K(3)A,80088,18076
BMRB,18063,AbpSH3-ArkA_L(-7)A,80088,18076
BMRB,18064,AbpSH3-ArkA_L(-7)V,80088,18076
BMRB,18065,AbpSH3-ArkA12,80088,18076
BMRB,18066,AbpSH3-ArkA_P(-4)A,80088,18076
BMRB,18067,AbpSH3-ArkA_P(2)A,80088,18076
BMRB,18068,AbpSH3-ArkA_P(2)V,80088,18076
BMRB,18069,AbpSH3-ArkA_P(0)A,80088,18076
BMRB,18070,AbpSH3-ArkA_P(-1)A,80088,18076
BMRB,18071,AbpSH3-Prk17,80088,18076
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80088,18076
BMRB,18073,AbpSH3-PRR,80088,18076
BMRB,18074,AbpSH3-Scp12,80088,18076
BMRB,18075,AbpSH3-Scp17,80088,18076
BMRB,18077,AbpSH3-Srv12,80088,18076
BMRB,18078,AbpSH3-Srv17,80088,18076
BMRB,18054,monomer (free AbpSH3),80103,18077
BMRB,18055,AbpSH3-ArkA,80103,18077
BMRB,18056,AbpSH3-ArkB,80103,18077
BMRB,18057,AbpSH3-ArkA_H(-6)A,80103,18077
BMRB,18058,AbpSH3-ArkA_SI,80103,18077
BMRB,18059,AbpSH3-ArkA_K(-3)A,80103,18077
BMRB,18060,AbpSH3-ArkA_K(-3)R,80103,18077
BMRB,18061,AbpSH3-ArkA_K(-3)V,80103,18077
BMRB,18062,AbpSH3-ArkA_K(3)A,80103,18077
BMRB,18063,AbpSH3-ArkA_L(-7)A,80103,18077
BMRB,18064,AbpSH3-ArkA_L(-7)V,80103,18077
BMRB,18065,AbpSH3-ArkA12,80103,18077
BMRB,18066,AbpSH3-ArkA_P(-4)A,80103,18077
BMRB,18067,AbpSH3-ArkA_P(2)A,80103,18077
BMRB,18068,AbpSH3-ArkA_P(2)V,80103,18077
BMRB,18069,AbpSH3-ArkA_P(0)A,80103,18077
BMRB,18070,AbpSH3-ArkA_P(-1)A,80103,18077
BMRB,18071,AbpSH3-Prk17,80103,18077
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80103,18077
BMRB,18073,AbpSH3-PRR,80103,18077
BMRB,18074,AbpSH3-Scp12,80103,18077
BMRB,18075,AbpSH3-Scp17,80103,18077
BMRB,18076,AbpSH3-Sjl17,80103,18077
BMRB,18078,AbpSH3-Srv17,80103,18077
BMRB,18054,monomer (free AbpSH3),80118,18078
BMRB,18055,AbpSH3-ArkA,80118,18078
BMRB,18056,AbpSH3-ArkB,80118,18078
BMRB,18057,AbpSH3-ArkA_H(-6)A,80118,18078
BMRB,18058,AbpSH3-ArkA_SI,80118,18078
BMRB,18059,AbpSH3-ArkA_K(-3)A,80118,18078
BMRB,18060,AbpSH3-ArkA_K(-3)R,80118,18078
BMRB,18061,AbpSH3-ArkA_K(-3)V,80118,18078
BMRB,18062,AbpSH3-ArkA_K(3)A,80118,18078
BMRB,18063,AbpSH3-ArkA_L(-7)A,80118,18078
BMRB,18064,AbpSH3-ArkA_L(-7)V,80118,18078
BMRB,18065,AbpSH3-ArkA12,80118,18078
BMRB,18066,AbpSH3-ArkA_P(-4)A,80118,18078
BMRB,18067,AbpSH3-ArkA_P(2)A,80118,18078
BMRB,18068,AbpSH3-ArkA_P(2)V,80118,18078
BMRB,18069,AbpSH3-ArkA_P(0)A,80118,18078
BMRB,18070,AbpSH3-ArkA_P(-1)A,80118,18078
BMRB,18071,AbpSH3-Prk17,80118,18078
BMRB,18072,AbpSH3-ArkA15_H(-6)A_K(-8)A,80118,18078
BMRB,18073,AbpSH3-PRR,80118,18078
BMRB,18074,AbpSH3-Scp12,80118,18078
BMRB,18075,AbpSH3-Scp17,80118,18078
BMRB,18076,AbpSH3-Sjl17,80118,18078
BMRB,18077,AbpSH3-Srv12,80118,18078
PDB,4A4R,BMRB Entry Tracking System,80133,18079
PDB,2LLM,BMRB Entry Tracking System,80164,18080
PDB,2LOH,BMRB Entry Tracking System,80164,18080
PDB,2LLN,BMRB Entry Tracking System,80184,18081
BMRB,18084,Calmodulin C-lobe,80208,18082
PDB,2LLO,BMRB Entry Tracking System,80208,18082
PDB,2LLP,BMRB Entry Tracking System,80226,18083
BMRB,18082,Calmodulin N-lobe,80242,18084
PDB,2LLQ,BMRB Entry Tracking System,80242,18084
PDB,2LLR,BMRB Entry Tracking System,80260,18085
PDB,2LLZ,BMRB Entry Tracking System,80276,18086
PDB,2LLS,BMRB Entry Tracking System,80294,18087
BMRB,18089,S100A1 protein without Post-translational S-nitrosylation,80329,18088
PDB,2LLT,BMRB Entry Tracking System,80329,18088
BMRB,18088,S100A1 protein with Post-translational S-nitrosylation,80347,18089
PDB,2LLU,BMRB Entry Tracking System,80347,18089
BMRB,18091,yeast Sti1 DP2 domain,80364,18090
PDB,2LLV,BMRB Entry Tracking System,80364,18090
BMRB,18090,yeast Sti1 DP2 domain,80386,18091
PDB,2LLW,BMRB Entry Tracking System,80386,18091
BMRB,15366,"NMR assignments of the C-terminal domain of human
polypeptide release factor eRF1",80408,18092
BMRB,6116,"Backbone (H,CA,CB and N) resonance assignment of the N-terminal domain of human eRF1",80408,18092
BMRB,6763,NMR assignments of the middle domain of human polypeptide release factor eRF1,80408,18092
PDB,1DT9,Crystal structure of human eukaryotic release factor eRF1,80408,18092
PDB,2HST,NMR structure and dynamics of the middle domain of human eRF1,80408,18092
PDB,2KTU,NMR solution structure of the closed conformer of the C-domain of human eRF1,80408,18092
PDB,2KTV,NMR solution structure of the open conformer of the C-domain of human eRF1,80408,18092
PDB,3E1Y,Crystal structure of human eRF1/eRF3 complex,80408,18092
PDB,2LLY,BMRB Entry Tracking System,80442,18093
PDB,2LM0,BMRB Entry Tracking System,80459,18094
PDB,2LM1,BMRB Entry Tracking System,80482,18095
PDB,2LM2,BMRB Entry Tracking System,80505,18096
PDB,2LM3,BMRB Entry Tracking System,80522,18097
TargetDB,YT682A,,80542,18098
PDB,1XO5,Crystal structure of calcium bound CIB1,80575,18099
PDB,2L4H,The Solution Structure of Calcium Bound CIB1,80575,18099
PDB,2L4I,The Solution Structure of Magnesium bound CIB1,80575,18099
PDB,2LM5,BMRB Entry Tracking System,80575,18099
PDB,2LM8,BMRB Entry Tracking System,80632,18102
PDB,2IHB,Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3,80648,18103
PDB,2V4Z,THE CRYSTAL STRUCTURE OF THE HUMAN G-PROTEIN SUBUNIT ALPHA (GNAI3) IN COMPLEX WITH AN ENGINEERED REGULATOR OF G-PROTEIN SIGNALING TYPE 2 DOMAIN (RGS2),80648,18103
BMRB,18105,S25p (phosphorylated),80672,18104
BMRB,18106,S25p complex with 3C3,80672,18104
BMRB,18104,S25p (un-phosphorylated),80692,18105
BMRB,18106,S25p complex with 3C3,80692,18105
BMRB,18104,S25p (un-phosphorylated),80714,18106
BMRB,18105,S25p (phosphorylated),80714,18106
PDB,2LM9,BMRB Entry Tracking System,80738,18107
PDB,2LME,BMRB Entry Tracking System,80752,18108
PDB,2LMB,BMRB Entry Tracking System,80796,18110
PDB,2LMC,BMRB Entry Tracking System,80810,18111
PDB,2LMD,BMRB Entry Tracking System,80826,18112
PDB,2MBX,BMRB Entry Tracking System,80857,18113
PDB,2K6O,LL-37,80873,18114
PDB,2LMF,BMRB Entry Tracking System,80873,18114
PDB,2LMG,BMRB Entry Tracking System,80888,18115
PDB,2LMI,BMRB Entry Tracking System,80938,18118
PDB,2LMJ,BMRB Entry Tracking System,80956,18119
BMRB,15977,CdnL C-terminal domain 55-164 residues,80993,18121
BMRB,18151,CdnL 1-164 residues,80993,18121
PDB,2LT4,BMRB Entry Tracking System,80993,18121
BMRB,6321,PYP delta25,81015,18122
BMRB,6322,PYP delta25,81015,18122
BMRB,18125,"56 kDa chimeric avidin, holo form",81034,18123
BMRB,18123,56 kDa chimeric avidin,81065,18125
PDB,2MF6,BMRB Entry Tracking System,81065,18125
PDB,2LR2,BMRB Entry Tracking System,81084,18126
BMRB,18128,"40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger",81099,18127
BMRB,18129,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger",81099,18127
BMRB,18131,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger",81099,18127
PDB,2LMN,BMRB Entry Tracking System,81099,18127
BMRB,18127,40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry,81114,18128
BMRB,18129,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger",81114,18128
BMRB,18131,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger",81114,18128
PDB,2LMO,BMRB Entry Tracking System,81114,18128
BMRB,18127,40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry,81129,18129
BMRB,18128,"40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger",81129,18129
BMRB,18131,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger",81129,18129
PDB,2LMP,BMRB Entry Tracking System,81129,18129
PDB,2LRC,BMRB Entry Tracking System,81157,18130
BMRB,18127,40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry,81172,18131
BMRB,18128,"40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger",81172,18131
BMRB,18129,"40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger",81172,18131
PDB,2LMQ,BMRB Entry Tracking System,81172,18131
PDB,4AAI,BMRB Entry Tracking System,81187,18132
PDB,2LMR,BMRB Entry Tracking System,81219,18134
PDB,2LMS,BMRB Entry Tracking System,81236,18135
PDB,2LMZ,BMRB Entry Tracking System,81303,18141
PDB,2LN0,BMRB Entry Tracking System,81322,18142
PDB,2LN3,BMRB Entry Tracking System,81341,18145
PDB,2LN4,BMRB Entry Tracking System,81381,18146
BMRB,15977,CdnL C-terminal domain 55-164 residues,81438,18151
BMRB,18121,CdnL N-terminal domain 1-68 residues,81438,18151
PDB,2LWJ,BMRB Entry Tracking System,81438,18151
PDB,2LN7,BMRB Entry Tracking System,81460,18152
PDB,2LN8,BMRB Entry Tracking System,81478,18153
PDB,2LNB,BMRB Entry Tracking System,81586,18158
PDB,2YOM,BMRB Entry Tracking System,81631,18159
PDB,2YON,BMRB Entry Tracking System,81662,18160
BMRB,18145,OR135,81680,18161
BMRB,18166,HR4403E,81680,18161
PDB,2LND,BMRB Entry Tracking System,81680,18161
BMRB,18163,Neurotensin in DMPC:CHAPS bicelle,81710,18162
BMRB,18164,Neurotensin in DMPC:CHAPS:GM1 bicelle,81710,18162
PDB,2LNE,BMRB Entry Tracking System,81710,18162
BMRB,18162,Neurotensin in H2O,81725,18163
BMRB,18164,Neurotensin in DMPC:CHAPS:GM1 bicelle,81725,18163
PDB,2LNF,BMRB Entry Tracking System,81725,18163
BMRB,18162,Neurotensin in H2O,81740,18164
BMRB,18163,Neurotensin in DMPC:CHAPS bicelle,81740,18164
PDB,2LNG,BMRB Entry Tracking System,81740,18164
PDB,2LNH,BMRB Entry Tracking System,81755,18165
BMRB,18145,OR135,81776,18166
BMRB,18161,OR134,81776,18166
PDB,2LNI,BMRB Entry Tracking System,81776,18166
PDB,2LNJ,BMRB Entry Tracking System,81805,18167
PDB,2LNK,BMRB Entry Tracking System,81825,18169
PDB,2LNL,BMRB Entry Tracking System,81861,18170
PDB,2LNM,BMRB Entry Tracking System,81877,18171
PDB,2LNQ,BMRB Entry Tracking System,81894,18175
BMRB,18177,cytosolic region of human VIMP (reduced),81908,18176
PDB,2Q2F,Entry containing crystal structure of residues 52-122 in human VIMP,81908,18176
BMRB,18176,cytosolic region of human VIMP (oxidized),81925,18177
PDB,2Q2F,Entry containing crystal structure of residues 52-122 in human VIMP,81925,18177
BMRB,18179,E60A mutant AGR2,81942,18178
PDB,2LNS,BMRB Entry Tracking System,81942,18178
PDB,2LNT,BMRB Entry Tracking System,81962,18179
PDB,2LNU,BMRB Entry Tracking System,81981,18180
PDB,2LNV,BMRB Entry Tracking System,82018,18181
BMRB,18183,free aS,82039,18182
PDB,2LNW,BMRB Entry Tracking System,82039,18182
BMRB,18182,free as,82059,18183
PDB,2LNX,BMRB Entry Tracking System,82059,18183
PDB,2LNY,BMRB Entry Tracking System,82076,18184
BMRB,18187,Get5 carboxyl domain from A. fumigatus,82108,18186
PDB,2LNZ,BMRB Entry Tracking System,82108,18186
PDB,3VEJ,Crystal structure of a truncated version of this protein,82108,18186
BMRB,18186,Get5 carboxyl domain from S. cerevisiae,82132,18187
PDB,2lnz,Solution structure of the S. cerevisiae homolog,82132,18187
PDB,2LO0,BMRB Entry Tracking System,82132,18187
PDB,3VEJ,Crystal structure of the S. cerevisiae homolog,82132,18187
PDB,2LO1,BMRB Entry Tracking System,82202,18190
BMRB,18192,SGF73,82219,18191
PDB,2LO2,BMRB Entry Tracking System,82219,18191
BMRB,18191,SGF11,82245,18192
PDB,2LO3,BMRB Entry Tracking System,82245,18192
BMRB,18121,"CdnL N-terminal domain from Myxococcus xanthus      
1-68 residues",82275,18193
BMRB,18151,CdnL from Myxococcus xanthus,82275,18193
BMRB,18194,CarD1-72,82275,18193
PDB,2LQK,BMRB Entry Tracking System,82275,18193
BMRB,18121,"CdnL N-terminal domain from Myxococcus xanthus          
residues 1-68",82298,18194
BMRB,18151,CdnL from Myxococcus xanthus,82298,18194
BMRB,18193,"TtCdnL N-terminal domain from Thermus thermophilus         
residues 1-67",82298,18194
PDB,2JVX,,82317,18195
PDB,2LO4,BMRB Entry Tracking System,82317,18195
PDB,2LO5,BMRB Entry Tracking System,82386,18199
PDB,2LO8,BMRB Entry Tracking System,82386,18199
PDB,2LOA,BMRB Entry Tracking System,82386,18199
PDB,2M5J,BMRB Entry Tracking System,82446,18201
PDB,2OB0,Human MAK3 homolog in complex with Acetyl-CoA,82461,18202
PDB,2PSW,Human MAK3 homolog in complex with CoA,82461,18202
PDB,3TFY,Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA,82461,18202
PDB,2LO9,BMRB Entry Tracking System,82479,18203
BMRB,16992,NMR complete assignment of the same protein in different condition: sodium acetate pH4,82498,18204
PDB,2qyq,XR 3D structure,82498,18204
PDB,2LOB,BMRB Entry Tracking System,82512,18205
PDB,2LOC,BMRB Entry Tracking System,82527,18206
BMRB,18208,E46K alpha-synuclein,82545,18207
BMRB,18207,A53T alpha-synuclein fibrils,82560,18208
PDB,2LOD,BMRB Entry Tracking System,82575,18209
PDB,2LOE,BMRB Entry Tracking System,82606,18210
PDB,2LY2,BMRB Entry Tracking System,82625,18211
PDB,2LOK,BMRB Entry Tracking System,82668,18215
PDB,2LOL,BMRB Entry Tracking System,82705,18216
TargetDB,RiprA.10532.a,,82705,18216
BMRB,18218,HIGD1B,82723,18217
BMRB,18219,TMEM14A(NOE),82723,18217
BMRB,18220,TMEM14A(PRE),82723,18217
BMRB,18221,FAM14B,82723,18217
BMRB,18222,TMEM141,82723,18217
BMRB,18223,TMEM14C,82723,18217
PDB,2LOM,BMRB Entry Tracking System,82723,18217
BMRB,18217,HIGD1A,82745,18218
BMRB,18219,TMEM14A(NOE),82745,18218
BMRB,18220,TMEM14A(PRE),82745,18218
BMRB,18221,FAM14B,82745,18218
BMRB,18222,TMEM141,82745,18218
BMRB,18223,TMEM14C,82745,18218
PDB,2LON,BMRB Entry Tracking System,82745,18218
BMRB,18217,HIGD1A,82772,18219
BMRB,18218,HIGD1B,82772,18219
BMRB,18220,TMEM14A(PRE),82772,18219
BMRB,18221,FAM14B,82772,18219
BMRB,18222,TMEM141,82772,18219
BMRB,18223,TMEM14C,82772,18219
PDB,2LOO,BMRB Entry Tracking System,82772,18219
BMRB,18217,HIGD1A,82805,18220
BMRB,18218,HIGD1B,82805,18220
BMRB,18219,TMEM14A(NOE),82805,18220
BMRB,18221,FAM14B,82805,18220
BMRB,18222,TMEM141,82805,18220
BMRB,18223,TMEM14C,82805,18220
PDB,2LOP,BMRB Entry Tracking System,82805,18220
BMRB,18217,HIGD1A,82829,18221
BMRB,18218,HIGD1B,82829,18221
BMRB,18219,TMEM14A(NOE),82829,18221
BMRB,18220,TMEM14A(PRE),82829,18221
BMRB,18222,TMEM141,82829,18221
BMRB,18223,TMEM14C,82829,18221
PDB,2LOQ,BMRB Entry Tracking System,82829,18221
BMRB,18217,HIGD1A,82853,18222
BMRB,18218,HIGD1B,82853,18222
BMRB,18219,TMEM14A(NOE),82853,18222
BMRB,18220,TMEM14A(PRE),82853,18222
BMRB,18221,FAM14B,82853,18222
BMRB,18223,TMEM14C,82853,18222
PDB,2LOR,BMRB Entry Tracking System,82853,18222
BMRB,18217,HIGD1A,82876,18223
BMRB,18218,HIGD1B,82876,18223
BMRB,18219,TMEM14A(NOE),82876,18223
BMRB,18220,TMEM14A(PRE),82876,18223
BMRB,18221,FAM14B,82876,18223
BMRB,18222,TMEM141,82876,18223
PDB,2LOS,BMRB Entry Tracking System,82876,18223
BMRB,18225,MS1 (AR55 in DPC micelles),82900,18224
BMRB,18226,MS1 (AR55 in LPPG micelles),82900,18224
BMRB,18227,MS1 (AR55 in 50% HFIP),82900,18224
BMRB,18224,MS1 (AR55 in SDS micelles),82929,18225
BMRB,18226,MS1 (AR55 in LPPG micelles),82929,18225
BMRB,18227,MS1 (AR55 in 50% HFIP),82929,18225
BMRB,18224,MS1 (AR55 in SDS micelles),82965,18226
BMRB,18225,MS1 (AR55 in DPC micelles),82965,18226
BMRB,18227,MS1 (AR55 in 50% HFIP),82965,18226
BMRB,18224,MS1 (AR55 in SDS micelles),83000,18227
BMRB,18225,MS1 (AR55 in DPC micelles),83000,18227
BMRB,18226,MS1 (AR55 in LPPG micelles),83000,18227
PDB,2M3V,BMRB Entry Tracking System,83030,18228
BMRB,6225,,83048,18229
PDB,1Y5O,,83048,18229
PDB,2GS0,,83048,18229
PDB,2K2U,,83048,18229
PDB,2L2I,,83048,18229
PDB,2LOX,BMRB Entry Tracking System,83048,18229
BMRB,16360,NMR parameters of the same protein without modification and in apo form,83077,18230
BMRB,18231,S100A1 Ca2+,83077,18230
PDB,2L0P,Structure of the same protein without modification and in apo form,83077,18230
BMRB,18230,human S100A1 protein modified at cysteine 85 with homocysteine disulfide bond formation in calcium saturated form,83112,18231
PDB,2LP3,BMRB Entry Tracking System,83112,18231
PDB,1EAY,Entry was use for calculation in this molecular system.,83167,18234
PDB,1I5N,Entry was use for calculation in this molecular system.,83167,18234
PDB,2LP4,BMRB Entry Tracking System,83167,18234
PDB,2KM1,Solution Structure Of The N-Terminal Domain Of The Yeast Protein Dre2,83182,18235
PDB,2OZ2,Related to x-ray crystal structure of cruzain-K777 complex; monomeric solution state.,83197,18236
PDB,2LP7,BMRB Entry Tracking System,83215,18237
BMRB,18250,Bcl-XL,83231,18238
PDB,2LP8,BMRB Entry Tracking System,83231,18238
BMRB,18240,Mutant of the sub-genomic promoter from Brome Mosaic Virus,83255,18239
PDB,2LP9,BMRB Entry Tracking System,83255,18239
BMRB,18239,Pseudo-triloop from the sub-genomic promoter of Brome Mosaic Virus,83269,18240
PDB,2LPA,BMRB Entry Tracking System,83269,18240
PDB,2M5V,BMRB Entry Tracking System,83283,18242
PDB,2LPB,BMRB Entry Tracking System,83316,18244
BMRB,18246,Pepsin backbone assignment with pepstatin,83343,18245
BMRB,18247,Pepsin backbone assignment without pepstatin,83343,18245
BMRB,18245,Pepsin backbone assignment without pepstatin,83359,18246
BMRB,18247,Backbone assignment of porcine pepsinogen,83359,18246
BMRB,18238,,83421,18250
PDB,2LP8,,83421,18250
PDB,2LPC,BMRB Entry Tracking System,83421,18250
BMRB,18252,Cdc42Hs,83437,18251
BMRB,18251,Cdc42Hs,83461,18252
BMRB,17656,"1H, 13C and 15N NMR assignments of inactive form of P1 endolysin Lyz",83487,18253
PDB,2LPD,BMRB Entry Tracking System,83517,18255
TargetDB,BupsA.13472.b,,83517,18255
PDB,1N7L,Solution NMR structure of AFA-PLN in detergent micelle,83538,18256
PDB,2KB7,Hybrid solution and solid-state NMR structure of the T state of AFA-PLN monomer structure in lipid bilayer,83538,18256
PDB,2KYV,Hybrid solution and solid-state NMR structure of the T state of PLN pentamer structure in lipid bilayer,83538,18256
PDB,2LPF,BMRB Entry Tracking System,83538,18256
PDB,1CUN,chicken brain alpha spectrin repeats 16 and 17,83595,18260
PDB,1U4Q,"chicken brain alpha spectrin repeats 15, 16 and 17",83595,18260
BMRB,18262,mutant (A72R),83613,18261
PDB,2LPI,BMRB Entry Tracking System,83613,18261
PDB,3lr2,wild type NT dimer,83613,18261
BMRB,18261,ampullate spidroin 1 N-terminal domain,83632,18262
PDB,2LPJ,BMRB Entry Tracking System,83632,18262
PDB,3lr2,wild type NT dimer,83632,18262
BMRB,4326,N-Terminal Domain of DNA Polymerase B,83724,18267
BMRB,5208,Palm-Thumb Domain of DNA Polymerase B,83724,18267
BMRB,7319,Polymerase Beta and Double gap double hairpin DNA,83724,18267
BMRB,16590,EF-hand domain of polycystin-2,83740,18268
PDB,2LPN,BMRB Entry Tracking System,83756,18269
PDB,2w50,"Structure solved by X-ray crystallography.  
Recombinant protein produced in Spodoptera frugiperda.",83756,18269
PDB,2LPU,BMRB Entry Tracking System,83789,18277
PDB,2LPV,BMRB Entry Tracking System,83808,18278
PDB,2KYO,,83829,18279
PDB,2LPW,BMRB Entry Tracking System,83829,18279
PDB,1G8Q,First X-ray structure,83846,18280
PDB,1IV5,second X-ray structure,83846,18280
PDB,2LPX,BMRB Entry Tracking System,83862,18281
PDB,2LPY,BMRB Entry Tracking System,83878,18282
PDB,2LRV,BMRB Entry Tracking System,83898,18283
BMRB,18286,antifreeze peptide,83913,18284
PDB,2LQ0,BMRB Entry Tracking System,83913,18284
BMRB,18308,HLA-DR1 CLIP106-120flipped,83928,18285
BMRB,18284,antifreeze peptide,83947,18286
PDB,2LQ1,BMRB Entry Tracking System,83947,18286
BMRB,17193,PAP248-286 in SDS,83962,18287
BMRB,17346,PAP248-286 in 50% TFE,83962,18287
PDB,2L3H,PAP248-286 in SDS,83962,18287
PDB,2L77,PAP248-286 in 50% TFE,83962,18287
PDB,2L79,PAP248-286 in 30% TFE,83962,18287
PDB,2LQ2,BMRB Entry Tracking System,83995,18289
PDB,2LQ3,BMRB Entry Tracking System,84010,18290
BMRB,18293,Granulocyte colony-stimulating factor A29G,84037,18291
BMRB,18294,Granulocyte colony-stimulating factor A30G,84037,18291
BMRB,18295,Granulocyte colony-stimulating factor A37G,84037,18291
PDB,2LQ5,BMRB Entry Tracking System,84053,18292
BMRB,18291,Granulocyte colony-stimulating factor,84072,18293
BMRB,18294,Granulocyte colony-stimulating factor A30G,84072,18293
BMRB,18295,Granulocyte colony-stimulating factor A37G,84072,18293
BMRB,18291,Granulocyte colony-stimulating factor,84088,18294
BMRB,18293,Granulocyte colony-stimulating factor A29G,84088,18294
BMRB,18295,Granulocyte colony-stimulating factor A37G,84088,18294
BMRB,18291,Granulocyte colony-stimulating factor,84104,18295
BMRB,18293,Granulocyte colony-stimulating factor A29G,84104,18295
BMRB,18294,Granulocyte colony-stimulating factor A30G,84104,18295
PDB,2LQ6,BMRB Entry Tracking System,84120,18296
PDB,2LQ7,BMRB Entry Tracking System,84140,18297
PDB,2LQ8,BMRB Entry Tracking System,84157,18298
PDB,2LQ9,BMRB Entry Tracking System,84174,18299
PDB,2LQA,BMRB Entry Tracking System,84207,18300
PDB,3Q8J,Crystal structure of asteropusin A  from marine sponge Asteropus sp.,84207,18300
PDB,2LQB,BMRB Entry Tracking System,84224,18301
PDB,2LQC,BMRB Entry Tracking System,84241,18302
BMRB,18305,HEWL-chitotriose,84282,18304
BMRB,18304,HEWL,84299,18305
BMRB,18307,A2POBEC2 1-224,84318,18306
BMRB,18306,A2POBEC2 41-224,84338,18307
BMRB,18285,HLA-DR1 CLIP102-120canonical,84353,18308
BMRB,18310,FliGn-FliFc,84372,18309
BMRB,18309,FliGn homodimer,84387,18310
PDB,2LQG,BMRB Entry Tracking System,84419,18313
BMRB,18315,FOXO3a transactivation domains (CR2C-CR3),84438,18314
BMRB,18314,FOXO3a transactivation domains (CR2C-CR3),84458,18315
PDB,2LQI,BMRB Entry Tracking System,84458,18315
PDB,2LQJ,BMRB Entry Tracking System,84478,18316
BMRB,17258,pineapple phytocystatin,84493,18317
PDB,1EQK,rice phytocystatin,84493,18317
PDB,2L4V,pineapple phytocystatin,84493,18317
PDB,2LQL,BMRB Entry Tracking System,84512,18318
PDB,2LQM,BMRB Entry Tracking System,84556,18320
PDB,2LQN,BMRB Entry Tracking System,84578,18321
BMRB,18325,Mrx1 oxidized form,84595,18322
PDB,2LQO,BMRB Entry Tracking System,84595,18322
PDB,2LQP,BMRB Entry Tracking System,84614,18323
PDB,2CPN,,84633,18324
PDB,3ADL,,84633,18324
PDB,3LLH,,84633,18324
BMRB,18322,Mrx1 reduced form,84650,18325
PDB,2LQQ,BMRB Entry Tracking System,84650,18325
BMRB,18003,apo form,84669,18326
PDB,2LQL,This PDBID is reported in the same manuscript,84711,18328
PDB,2LQT,BMRB Entry Tracking System,84711,18328
PDB,2LQU,BMRB Entry Tracking System,84740,18329
PDB,2LQV,BMRB Entry Tracking System,84779,18332
PDB,2LQW,BMRB Entry Tracking System,84799,18333
PDB,2LQX,BMRB Entry Tracking System,84817,18334
PDB,2LQY,BMRB Entry Tracking System,84835,18335
PDB,2LQZ,BMRB Entry Tracking System,84853,18336
PDB,2lr0,,84869,18337
PDB,2LUW,BMRB Entry Tracking System,84911,18338
PDB,4A2A,,84927,18339
PDB,4A2B,,84927,18339
PDB,1F16,,84941,18340
PDB,2LR1,BMRB Entry Tracking System,84941,18340
BMRB,18342,Get5_UBL domain,84957,18341
PDB,4ASV,BMRB Entry Tracking System,84957,18341
BMRB,18341,Sgt2_NT homodimer,84977,18342
PDB,4ASW,BMRB Entry Tracking System,84977,18342
BMRB,18135,"Interferon Alpha-2A, with GalNac at Thr106.",84993,18344
PDB,2LMS,"Interferon Alpha-2A, with GalNac at Thr106.",84993,18344
PDB,2LR3,BMRB Entry Tracking System,85009,18345
PDB,2LR4,BMRB Entry Tracking System,85030,18346
PDB,2LR5,BMRB Entry Tracking System,85049,18347
PDB,2LR6,BMRB Entry Tracking System,85081,18349
PDB,2LR7,BMRB Entry Tracking System,85100,18350
PDB,2LR8,BMRB Entry Tracking System,85182,18352
PDB,1IEN,"Solution structure of TIA, which was refined during this study.",85225,18354
PDB,2LR9,BMRB Entry Tracking System,85225,18354
BMRB,18356,ADF like UNC-60A Protein,85242,18355
PDB,2LRA,BMRB Entry Tracking System,85242,18355
BMRB,18355,(SSD) Rv0603 Protein,85259,18356
PDB,2LRB,BMRB Entry Tracking System,85259,18356
BMRB,18358,dimeric Acanthaporin,85280,18357
PDB,2LRD,BMRB Entry Tracking System,85280,18357
BMRB,18357,Acanthaporin,85298,18358
PDB,2LRE,BMRB Entry Tracking System,85298,18358
BMRB,18360,IscU(E111A),85317,18359
BMRB,18361,IscU(N90A),85317,18359
BMRB,18362,IscU(S107A),85317,18359
BMRB,18359,IscU(D39V),85336,18360
BMRB,18361,IscU(N90A),85336,18360
BMRB,18362,IscU(S107A),85336,18360
PDB,2KQK,NMR solution structure of apo-IscU(D39A),85336,18360
PDB,2L4X,NMR solution structure of apo-IscU(WT),85336,18360
BMRB,18359,IscU(D39V),85355,18361
BMRB,18360,IscU(E111A),85355,18361
BMRB,18362,IscU(S107A),85355,18361
PDB,2KQK,NMR solution structure of apo-IscU(D39A),85355,18361
PDB,2L4X,NMR solution structure of apo-IscU(WT),85355,18361
BMRB,18359,IscU(D39V),85374,18362
BMRB,18360,IscU(E111A),85374,18362
BMRB,18361,IscU(N90A),85374,18362
PDB,2KQK,NMR solution structure of apo-IscU(D39A),85374,18362
PDB,2L4X,NMR solution structure of apo-IscU(WT),85374,18362
PDB,2MDL,BMRB Entry Tracking System,85393,18363
PDB,2LRG,BMRB Entry Tracking System,85411,18364
BMRB,18366,W28G,85430,18365
BMRB,18367,W62G,85430,18365
BMRB,18368,W108G,85430,18365
BMRB,18369,W111G,85430,18365
BMRB,18370,W123G,85430,18365
BMRB,18365,WT-ALA,85446,18366
BMRB,18367,W62G,85446,18366
BMRB,18368,W108G,85446,18366
BMRB,18369,W111G,85446,18366
BMRB,18370,W123G,85446,18366
BMRB,18365,WT-ALA,85461,18367
BMRB,18366,W28G,85461,18367
BMRB,18368,W108G,85461,18367
BMRB,18369,W111G,85461,18367
BMRB,18370,W123G,85461,18367
BMRB,18365,WT-ALA,85476,18368
BMRB,18366,W28G,85476,18368
BMRB,18367,W62G,85476,18368
BMRB,18369,W111G,85476,18368
BMRB,18370,W123G,85476,18368
BMRB,18365,WT-ALA,85491,18369
BMRB,18366,W28G,85491,18369
BMRB,18367,W62G,85491,18369
BMRB,18368,W108G,85491,18369
BMRB,18370,W123G,85491,18369
BMRB,18365,WT-ALA,85506,18370
BMRB,18366,W28G,85506,18370
BMRB,18367,W62G,85506,18370
BMRB,18368,W108G,85506,18370
BMRB,18369,W111G,85506,18370
BMRB,18348,EB1 CH domain,85521,18371
PDB,2LRH,BMRB Entry Tracking System,85535,18372
PDB,3LEZ,X-Ray structure,85576,18373
PDB,2LRI,BMRB Entry Tracking System,85590,18374
PDB,2LRJ,BMRB Entry Tracking System,85611,18375
BMRB,18377,MTIP(61-204)(61-204)/MyoA(799-818),85627,18376
BMRB,18376,free MTIP(61-204),85642,18377
PDB,4APD,BMRB Entry Tracking System,85658,18378
PDB,2LRK,BMRB Entry Tracking System,85678,18379
PDB,2LRL,BMRB Entry Tracking System,85678,18379
BMRB,16096,dvCcmE'(44-128),85700,18380
BMRB,17836,The chemical shifts of apo-IscU in the disordered conformation,85735,18381
BMRB,17837,The chemical shifts of apo-IscU in the structured conformation,85735,18381
BMRB,18359,IscU(D39V),85735,18381
BMRB,18360,IscU(E111A),85735,18381
BMRB,18361,IscU(N90A),85735,18381
BMRB,18362,IscU(S107A),85735,18381
PDB,2KQK,NMR solution structure of apo-IscU(D39A),85735,18381
PDB,2L4X,NMR solution structure of apo-IscU(WT),85735,18381
BMRB,18386,HP1 CSDalpha(109-185),85753,18385
BMRB,18385,H3(1-59),85768,18386
PDB,2LRN,BMRB Entry Tracking System,85783,18387
TargetDB,NYSGRC-011666,,85783,18387
BMRB,18389,at 50 C,85806,18388
PDB,2LRO,BMRB Entry Tracking System,85806,18388
BMRB,18388,at 25 C,85828,18389
PDB,2LRP,BMRB Entry Tracking System,85828,18389
PDB,2LRQ,BMRB Entry Tracking System,85864,18390
PDB,1msz,Structure of ligand free form,85886,18391
PDB,2LRR,BMRB Entry Tracking System,85886,18391
PDB,2LRS,BMRB Entry Tracking System,85925,18393
TargetDB,011327,,85946,18394
BMRB,15546,Chemical shift assignments for DsbB,85968,18395
BMRB,15966,Integral membrane protein DsbB in solution,85968,18395
BMRB,17710,Membrane protein complex DsbB-DsbA,85968,18395
PDB,2LRU,BMRB Entry Tracking System,86015,18398
PDB,2LRW,BMRB Entry Tracking System,86032,18399
PDB,2LRX,BMRB Entry Tracking System,86046,18400
PDB,2LS0,BMRB Entry Tracking System,86082,18404
PDB,2LS1,BMRB Entry Tracking System,86110,18405
BMRB,15379,solution Sup35 NM,86124,18406
BMRB,17473,chimeric sup35 prion,86124,18406
BMRB,18407,solid state Sup35p,86124,18406
BMRB,15379,solution Sup35 NM,86141,18407
BMRB,17473,chimeric sup35 prion,86141,18407
BMRB,18406,solid state Sup35NM,86141,18407
BMRB,18409,second transmembrane domain from human copper transport 1,86158,18408
BMRB,18410,third transmembrane domain from the human copper transport 1,86158,18408
PDB,2LS2,BMRB Entry Tracking System,86158,18408
BMRB,18408,first transmembrane domain from human copper transport 1,86172,18409
BMRB,18410,third transmembrane domain from the human copper transport 1,86172,18409
PDB,2LS3,BMRB Entry Tracking System,86172,18409
BMRB,18408,first transmembrane domain from human copper transport 1,86199,18410
BMRB,18409,second transmembrane domain from human copper transport 1,86199,18410
PDB,2LS4,BMRB Entry Tracking System,86199,18410
PDB,2LS5,BMRB Entry Tracking System,86213,18411
TargetDB,NYSGRC-011533,,86213,18411
PDB,1N3K,Re-refined with RDCs and explicit solvent for DED only,86237,18412
PDB,2LS7,BMRB Entry Tracking System,86237,18412
BMRB,18414,AdcR [Zn(II)-form],86251,18413
BMRB,18413,Assignments of the Apo-form of AdcR,86267,18414
PDB,2LS8,BMRB Entry Tracking System,86285,18415
TargetDB,NYSGRC-020344,,86285,18415
PDB,2LWP,BMRB Entry Tracking System,86308,18416
PDB,2M8S,BMRB Entry Tracking System,86308,18416
BMRB,18420,Magainin,86338,18418
PDB,2LS9,BMRB Entry Tracking System,86338,18418
BMRB,18418,Pleurocidin,86379,18420
PDB,2LSA,BMRB Entry Tracking System,86379,18420
BMRB,16306,ferric protein with PTM,86413,18422
BMRB,16307,ferric protein without PTM,86413,18422
BMRB,17947,ferrous protein with PTM,86413,18422
BMRB,18423,holoprotein (ligand with HEB and CN),86413,18422
BMRB,18424,holoprotein (ligand with HEM and CN),86413,18422
PDB,2ksc,ferric protein with PTM,86413,18422
BMRB,16306,ferric protein with PTM,86441,18423
BMRB,16307,ferric protein without PTM,86441,18423
BMRB,17947,ferrous protein with PTM,86441,18423
BMRB,18422,holoprotein (ligand with HEB and CO),86441,18423
BMRB,18424,holoprotein (ligand with HEM and CN),86441,18423
PDB,2ksc,ferric protein with PTM,86441,18423
BMRB,16306,ferric protein with PTM,86469,18424
BMRB,16307,ferric protein without PTM,86469,18424
BMRB,17947,ferrous protein with PTM,86469,18424
BMRB,18422,holoprotein (ligand with HEB and CO),86469,18424
BMRB,18423,holoprotein (ligand with HEB and CN),86469,18424
PDB,2ksc,ferric protein with PTM,86469,18424
PDB,2LUC,BMRB Entry Tracking System,86493,18425
PDB,2LSB,BMRB Entry Tracking System,86510,18426
PDB,2LSC,BMRB Entry Tracking System,86529,18427
BMRB,18438,HR7057A,86567,18429
PDB,2LSE,BMRB Entry Tracking System,86567,18429
PDB,2LSF,BMRB Entry Tracking System,86607,18430
BMRB,18433,mouse Rev1 CTD in complex with the RIR of Pol Kappa,86633,18431
PDB,2LSG,BMRB Entry Tracking System,86633,18431
PDB,2LSI,BMRB Entry Tracking System,86653,18432
BMRB,18431,mouse Rev1 C-terminal domain,86668,18433
PDB,2LSJ,BMRB Entry Tracking System,86668,18433
BMRB,18455,C-terminal domain of human REV1 (free form),86688,18434
PDB,2LSK,BMRB Entry Tracking System,86688,18434
PDB,2LSY,C-terminal domain of human REV1 (free form),86688,18434
PDB,2LSL,BMRB Entry Tracking System,86708,18435
PDB,4ERD,Crystal structure of p65 C-terminal xRRM2 domain in complex with stem IV of teloemarse RNA,86708,18435
PDB,4EYT,Crystal structure of p65 C-terminal xRRM2 domain,86708,18435
PDB,2LSM,BMRB Entry Tracking System,86728,18437
BMRB,18429,OR188,86746,18438
TargetDB,HR7057A,,86746,18438
PDB,2LSP,BMRB Entry Tracking System,86777,18439
PDB,2LSQ,BMRB Entry Tracking System,86819,18440
PDB,2KBQ,,86836,18441
PDB,2KBR,,86836,18441
PDB,2LSR,BMRB Entry Tracking System,86836,18441
PDB,2LSS,BMRB Entry Tracking System,86853,18442
PDB,2LST,BMRB Entry Tracking System,86872,18443
TargetDB,NYSGRC-011484,,86872,18443
PDB,2LSU,BMRB Entry Tracking System,86896,18445
PDB,2LSU,,86929,18447
PDB,2LSV,BMRB Entry Tracking System,86929,18447
PDB,2JPE,,86950,18448
PDB,2LSW,BMRB Entry Tracking System,86966,18449
PDB,2LSX,BMRB Entry Tracking System,86995,18452
BMRB,18454,duplex DNA containing the -OH-PdG dA base pair,87012,18453
PDB,2LSZ,BMRB Entry Tracking System,87012,18453
BMRB,18453,duplex DNA containing the -OH-PdG dA base pair,87031,18454
PDB,2LT0,BMRB Entry Tracking System,87031,18454
BMRB,18434,C-terminal domain of human REV1 in complex with DNA-polymerase H (eta),87050,18455
PDB,2LSK,C-terminal domain of human REV1 in complex with DNA-polymerase H (eta),87050,18455
PDB,2LSY,BMRB Entry Tracking System,87050,18455
PDB,2L1I,Solution Structure of HIRAN domain of HLTF,87070,18458
PDB,4AR0,BMRB Entry Tracking System,87087,18459
PDB,2LCF,GppNHp-bound H-RasT35S mutant protein,87122,18461
BMRB,17610,GppNHp-bound H-RasT35S mutant protein,87122,18461
PDB,2LT7,BMRB Entry Tracking System,87149,18462
PDB,2LT8,BMRB Entry Tracking System,87177,18463
BMRB,7008,Entry containing resonance assignments of CBD2 of NCX isoform 1,87195,18464
BMRB,7009,Entry containing assignments of CBD1 of NCX isoform 1,87195,18464
PDB,2LT9,BMRB Entry Tracking System,87195,18464
PDB,2LTA,BMRB Entry Tracking System,87216,18465
BMRB,18467,"FAS1-4, R555W",87255,18466
PDB,2LTB,BMRB Entry Tracking System,87255,18466
BMRB,18466,Wild-type FAS1-4,87277,18467
PDB,2LTC,BMRB Entry Tracking System,87277,18467
PDB,2LTE,BMRB Entry Tracking System,87298,18468
BMRB,18496,YdbC:dT19G1 complex. NESG Target KR150,87325,18469
PDB,2LTD,BMRB Entry Tracking System,87325,18469
PDB,2LTT,,87325,18469
BMRB,18472,Apo form gt CsoR,87368,18470
BMRB,18470,Cu(I)-bound form gt CsoR,87398,18472
PDB,2KTD,,87412,18473
PDB,2M1H,BMRB Entry Tracking System,87428,18474
PDB,2LTF,BMRB Entry Tracking System,87442,18475
PDB,2M16,BMRB Entry Tracking System,87485,18478
PDB,2LTI,BMRB Entry Tracking System,87538,18481
PDB,2LTJ,BMRB Entry Tracking System,87554,18484
PDB,2LTK,BMRB Entry Tracking System,87571,18485
BMRB,18488,oxidized sulfiredoxin,87592,18486
BMRB,18489,HR2876B,87611,18487
BMRB,18486,reduced sulfiredoxin,87645,18488
BMRB,18487,YR313A,87662,18489
PDB,2LTM,BMRB Entry Tracking System,87662,18489
PDB,2LTO,BMRB Entry Tracking System,87696,18490
BMRB,18495,Th205-316 dimer,87712,18491
PDB,1TRL,,87712,18491
PDB,2LEG,Similar refinement method,87752,18493
PDB,2ZUQ,The source of X-ray data,87752,18493
BMRB,18491,Th255-316 dimer,87792,18495
PDB,1TRL,,87792,18495
BMRB,18469,"apo YdbC from Lactococcus lactis, NESG Target KR150",87809,18496
PDB,2LTT,BMRB Entry Tracking System,87809,18496
PDB,2ltd,,87809,18496
PDB,2LTU,BMRB Entry Tracking System,87841,18497
PDB,2LTV,BMRB Entry Tracking System,87862,18498
PDB,2LTW,BMRB Entry Tracking System,87881,18499
PDB,2LTX,BMRB Entry Tracking System,87913,18500
PDB,2LTY,BMRB Entry Tracking System,87932,18501
PDB,2LTZ,BMRB Entry Tracking System,87952,18502
PDB,2LU0,BMRB Entry Tracking System,87972,18503
PDB,2LU1,BMRB Entry Tracking System,87998,18504
PDB,3HD4,Crystal structure of the protein assigned in this entry.,88012,18505
PDB,2LU2,BMRB Entry Tracking System,88029,18506
BMRB,18508,apo-form of the beta2 carbohydrate module of AMP-activated protein kinase,88051,18507
PDB,2LU3,BMRB Entry Tracking System,88051,18507
BMRB,18507,beta2 carbohydrate module of AMP-activated protein kinase bound to glucosyl-cyclodextrin,88073,18508
PDB,2LU4,BMRB Entry Tracking System,88073,18508
PDB,2LU5,BMRB Entry Tracking System,88094,18509
PDB,2LU6,BMRB Entry Tracking System,88124,18510
BMRB,18512,"GS-TAMAPIN DELETION 4N,5L",88163,18513
PDB,2LUA,BMRB Entry Tracking System,88177,18514
PDB,2LUB,BMRB Entry Tracking System,88199,18515
PDB,2JO7,Entry containing solution structure of the wild type of this molecular system,88235,18517
PDB,2LUD,BMRB Entry Tracking System,88235,18517
PDB,2LUE,BMRB Entry Tracking System,88254,18518
PDB,3VTU,Free LC3B crystall structure,88254,18518
PDB,3VTV,OPTN LIR-LC3B crystall structure,88254,18518
PDB,3VTW,T7 OPTN LIR-LC3B crystall structure,88254,18518
PDB,2LUF,BMRB Entry Tracking System,88278,18519
BMRB,15131,intrinsically disordered protein under physiological conditions,88296,18520
BMRB,6100,murine myelin basic protein (MBP) apo form,88296,18520
BMRB,6857,immunodominant epitope of myelin basic protein (MBP),88296,18520
BMRB,7358,golli myelin basic protein (MBP) isoform BG21,88296,18520
PDB,2LUG,BMRB Entry Tracking System,88296,18520
PDB,2LUH,BMRB Entry Tracking System,88315,18521
PDB,2LUI,BMRB Entry Tracking System,88339,18522
PDB,4AXP,BMRB Entry Tracking System,88361,18523
PDB,2LUJ,BMRB Entry Tracking System,88382,18524
PDB,2LUL,BMRB Entry Tracking System,88403,18526
BMRB,18528,alpha tubulin 404-451,88437,18527
BMRB,18527,beta tubulin 394-445,88451,18528
PDB,1IGD,,88501,18531
PDB,1P7E,,88501,18531
PDB,1P7F,,88501,18531
PDB,2LUM,BMRB Entry Tracking System,88501,18531
PDB,2OED,,88501,18531
PDB,1U2P,X-ray structure of MPtpA,88535,18533
PDB,1U2Q,X-ray structure of MPtpA with glycerol in the active site,88535,18533
PDB,2LUO,BMRB Entry Tracking System,88535,18533
BMRB,18535,Double Stranded RNA binding domain of Ribonuclease III (Rnt1p) apo form,88558,18534
PDB,2LUP,BMRB Entry Tracking System,88558,18534
BMRB,18534,Double Stranded RNA binding domain of Ribonuclease III(Rnt1p) in complex with RNA,88580,18535
PDB,2LUQ,BMRB Entry Tracking System,88580,18535
PDB,2LUR,BMRB Entry Tracking System,88601,18536
BMRB,18538,1H and 13C NMR of GPVI mimetic,88617,18537
BMRB,18537,Collagelin 1H and 13C NMR data,88632,18538
PDB,2LUS,BMRB Entry Tracking System,88647,18539
BMRB,18541,midkine-b,88679,18540
PDB,1MKC,C-half domain,88679,18540
PDB,1MKN,N-half domain,88679,18540
PDB,2LUT,BMRB Entry Tracking System,88679,18540
BMRB,18540,midkine-a,88699,18541
PDB,1MKC,C-half domain,88699,18541
PDB,1MKN,N-half domain,88699,18541
PDB,2LUU,BMRB Entry Tracking System,88699,18541
PDB,2LKE,Myristoylated alphaM in Dodecylphospholine micelles,88716,18542
PDB,2LKJ,Myristoylated alphaM SER phosphorylated in Dodecylphospholine micelles,88716,18542
PDB,2LUV,BMRB Entry Tracking System,88716,18542
BMRB,16327,"DsbA, wild type oxidized",88733,18543
BMRB,18544,DsbA(C33S)/DsbB complex,88733,18543
BMRB,16327,"DsbA, wild type oxidized",88750,18544
BMRB,18543,DsbA(C33S) apo form,88750,18544
PDB,2JPT,bovine apo-S100A1-bMe,88768,18545
PDB,2L0P,human apo-S100A1,88768,18545
PDB,2LHL,human apo-S100A1-E32Q,88768,18545
PDB,2LLS,human apo-S100A1-C85M,88768,18545
PDB,2LP2,human holo-S100A1-Hcy,88768,18545
PDB,2LP3,human holo-S100A1,88768,18545
PDB,2LUX,BMRB Entry Tracking System,88768,18545
PDB,2LUY,BMRB Entry Tracking System,88801,18546
PDB,2LUZ,BMRB Entry Tracking System,88823,18547
PDB,2M5H,BMRB Entry Tracking System,88853,18548
PDB,2LV0,BMRB Entry Tracking System,88869,18549
PDB,2lej,,88903,18550
PDB,2LV4,BMRB Entry Tracking System,88970,18553
PDB,2LV5,BMRB Entry Tracking System,88990,18555
PDB,1BBM,"skMLCK peptide coordinates and distance restraints from this entry were used
during rigid-body optimization of the geometry of the CaM/MLCK complex.",89010,18556
PDB,1MXE,"Backbone coordinates of the N- and C-terminal domains from this entry (residues
5-75 and 82-146, respectively) were used during rigid-body optimization of the
geometry of the CaM/MLCK complex.",89010,18556
PDB,2LV6,BMRB Entry Tracking System,89010,18556
PDB,2LV7,BMRB Entry Tracking System,89033,18557
BMRB,16562,NMR data excluded RDC,89055,18558
PDB,2KPO,NMR structure refined without RDC data,89055,18558
BMRB,18560,hs356_22_132,89087,18559
PDB,2LV9,BMRB Entry Tracking System,89087,18559
BMRB,18559,zinc-finger,89123,18560
PDB,2LVA,BMRB Entry Tracking System,89123,18560
PDB,2LVB,BMRB Entry Tracking System,89147,18561
BMRB,18562,VvMARTX,89220,18565
PDB,2M5S,BMRB Entry Tracking System,89235,18566
PDB,2XYY,a cryo-EM model of the full-length coat protein in a procapsid,89235,18566
PDB,2XYZ,a cryo-EM model of the full-length coat protein in a mature virion,89235,18566
PDB,3IYH,a cryo-EM model of the full-length coat protein in a procapsid,89235,18566
BMRB,16864,"Sequence Specific 1H, 13C and 15N backbone resonance assignments of uvi31+ from Chlamydomonas reinhardtii",89255,18567
PDB,2jxf,"Identification of a novel determinant for membrane association in hepatitis C virus nonstructural protein 4B.   
Gouttenoire et al, J Virol. 2009 Jun;83(12):6257-68.",89269,18568
PDB,2LVG,BMRB Entry Tracking System,89269,18568
PDB,1EGX,NMR structure,89286,18569
BMRB,18572,hemi-Mg-bound Phl p 7,89349,18571
BMRB,18573,Ca-bound Phl p 7,89349,18571
PDB,2LVI,BMRB Entry Tracking System,89349,18571
BMRB,18571,apo-Phl p 7,89367,18572
BMRB,18573,Ca-bound Phl p 7,89367,18572
PDB,2LVJ,BMRB Entry Tracking System,89367,18572
BMRB,18571,apo-Phl p 7,89387,18573
BMRB,18772,SCIN-A,93196,18773
BMRB,18572,hemi-Mg-bound Phl p 7,89387,18573
PDB,2LVK,BMRB Entry Tracking System,89387,18573
BMRB,18575,variant XI LipA,89407,18574
BMRB,18574,wild-type Lipase A,89424,18575
BMRB,18578,"Connexin45 Carboxyl Terminal Domain, monomer",89454,18577
BMRB,18577,"Connexin45 Carboxyl Terminal Domain, dimer",89469,18578
PDB,2LVM,BMRB Entry Tracking System,89484,18579
BMRB,18582,gp78CUE bound to ubiquitin,89538,18581
BMRB,18583,gp78CUE/K48-Ub2 complex,89538,18581
BMRB,18584,gp78CUE/K48-Ub2 complex,89538,18581
PDB,2LVN,BMRB Entry Tracking System,89538,18581
BMRB,18581,gp78 CUE domain,89557,18582
BMRB,18583,gp78CUE/K48-Ub2 complex,89557,18582
BMRB,18584,gp78CUE/K48-Ub2 complex,89557,18582
PDB,2LVO,BMRB Entry Tracking System,89557,18582
BMRB,18581,gp78 CUE domain,89577,18583
BMRB,18582,gp78CUE bound to ubiquitin,89577,18583
BMRB,18584,gp78CUE/K48-Ub2 complex,89577,18583
PDB,2LVP,BMRB Entry Tracking System,89577,18583
PDB,2LVR,BMRB Entry Tracking System,89632,18586
PDB,2LVT,BMRB Entry Tracking System,89632,18586
PDB,2LVU,BMRB Entry Tracking System,89632,18586
PDB,2M0A,BMRB Entry Tracking System,89653,18587
PDB,2LVS,BMRB Entry Tracking System,89687,18589
BMRB,16687,dimeric regulatory subunit (ilvN) of E.coli AHAS I,89738,18591
PDB,2LVX,BMRB Entry Tracking System,89763,18592
PDB,2LVY,BMRB Entry Tracking System,89782,18593
BMRB,17064,incomplete assignments of the same protein,89802,18595
PDB,2M3G,BMRB Entry Tracking System,89802,18595
PDB,2LVZ,BMRB Entry Tracking System,89821,18596
PDB,4B2S,BMRB Entry Tracking System,89858,18599
BMRB,18597,Ecoli RBP sugar free backbone assignment,89968,18601
BMRB,18601,Ecoli GGBP sugar free backbone assignment,89968,18601
BMRB,18609,Ecoli GGBP sugar backbone assignment,89968,18601
PDB,1URP,X-ray structure of open unliganded E.coli Ribose Binding Protein,89968,18601
PDB,2DRI,X-ray structure of closed ligand bound E.coli Ribose Binding Protein,89968,18601
PDB,2FW0,Open X-ray structure of ligand free Ecoli GGBP,89968,18601
PDB,2HPH,Closed X-ray structure of ligand bound Ecoli GGBP,89968,18601
PDB,2lw0,Ecoli RBP sugar free solution structure,89968,18601
PDB,2lw2,Ecoli GGBP sugar free solution structure,89968,18601
PDB,2LW3,BMRB Entry Tracking System,89988,18602
BMRB,18597,Ecoli RBP sugar free backbone assignment,90011,18603
BMRB,18601,Ecoli GGBP sugar free backbone assignment,90011,18603
BMRB,18609,Ecoli GGBP sugar backbone assignment,90011,18603
PDB,1URP,X-ray structure of open unliganded E.coli Ribose Binding Protein,90011,18603
PDB,2DRI,X-ray structure of closed ligand bound E.coli Ribose Binding Protein,90011,18603
PDB,2lw0,Ecoli RBP sugar free solution structure,90011,18603
PDB,2lw2,Ecoli GGBP sugar free solution structure,90011,18603
TargetDB,HR8682B,,90057,18605
PDB,2LW5,BMRB Entry Tracking System,90084,18606
PDB,2LW6,BMRB Entry Tracking System,90101,18607
BMRB,18597,Ecoli RBP sugar free backbone assignment,90137,18609
BMRB,18601,Ecoli GGBP sugar free backbone assignment,90137,18609
BMRB,18603,Ecoli RBP sugar backbone assignment,90137,18609
PDB,1URP,X-ray structure of open unliganded E.coli Ribose Binding Protein,90137,18609
PDB,2DRI,X-ray structure of closed ligand bound E.coli Ribose Binding Protein,90137,18609
PDB,2lw0,Ecoli RBP sugar free solution structure,90137,18609
PDB,2lw2,Ecoli GGBP sugar free solution structure,90137,18609
BMRB,18611,Pressure & methanol-induced A-state of Ubiquitin,90156,18610
BMRB,18610,"1H, 13C and 15N assignments of Ubiquitin for both folded and denatured states",90174,18611
PDB,2LW7,BMRB Entry Tracking System,90189,18612
PDB,2LW8,BMRB Entry Tracking System,90203,18613
PDB,2LW9,BMRB Entry Tracking System,90218,18614
BMRB,4768,parvulin 14 assignment,90236,18615
PDB,1EQ3,parvulin 14 solution structure,90236,18615
PDB,1FJD,parvulin 14 solution structure,90236,18615
PDB,3UI4,parvulin 14 X-ray structure,90236,18615
BMRB,16907,The hemagglutinin fusion peptide (H1 subtype) at pH 7.4,90285,18617
PDB,2KXA,,90285,18617
PDB,2LWA,BMRB Entry Tracking System,90285,18617
PDB,2LWB,BMRB Entry Tracking System,90311,18618
PDB,2LWC,BMRB Entry Tracking System,90327,18619
BMRB,18621,La-type RNA-binding domain,90340,18620
PDB,1S79,Solution structure of the central RRM of human La protein,90340,18620
PDB,2VON,Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein.,90340,18620
BMRB,18620,RRM domain,90356,18621
PDB,1S29,La autoantigen N-terminal domain,90356,18621
PDB,1S7A,NMR structure of the La motif of human La protein,90356,18621
PDB,2VON,CRYSTAL STRUCTURE OF N-TERMINAL DOMAINS OF HUMAN LA PROTEIN COMPLEXED WITH RNA OLIGOMER AUAAUUU,90356,18621
BMRB,18623,Solution structure of mutant (T170E) second CARD of human RIG-I,90372,18622
PDB,2LWD,BMRB Entry Tracking System,90372,18622
BMRB,18622,Solution structure of second CARD of human RIG-I.,90393,18623
PDB,2LWE,BMRB Entry Tracking System,90393,18623
PDB,2LWF,BMRB Entry Tracking System,90413,18624
BMRB,18626,Self-Complementary 10 mer DNA Duplex 5'-GGATATATCC-3' in Complex with Netropsin,90430,18625
PDB,2LWG,BMRB Entry Tracking System,90430,18625
BMRB,18626,The free DNA without netropsin.,90448,18626
PDB,2LWG,The free DNA without netropsin.,90448,18626
PDB,2LWH,BMRB Entry Tracking System,90448,18626
PDB,2LWI,BMRB Entry Tracking System,90517,18629
BMRB,18631,N-80 ALR reduced,90544,18630
BMRB,18630,N-80 ALR,90560,18631
PDB,2LWK,BMRB Entry Tracking System,90613,18633
BMRB,18635,Backbone resonance assignments of human beta-defensin 1,90631,18634
PDB,2LWL,BMRB Entry Tracking System,90631,18634
BMRB,18634,Backbone resonance assignments of human beta-defensin 6,90646,18635
PDB,4UET,PDBe entry based on NMR data,90683,18637
BMRB,18638,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90715,18638
BMRB,18639,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90715,18638
PDB,2LWM,BMRB Entry Tracking System,90715,18638
BMRB,18638,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90736,18639
BMRB,18640,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90736,18639
PDB,2LWN,BMRB Entry Tracking System,90736,18639
BMRB,18638,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90757,18640
BMRB,18639,Duplex DNA Containing a b-Carba-Fapy-dG Lesion,90757,18640
PDB,2LWO,BMRB Entry Tracking System,90757,18640
BMRB,18643,PawS Derived Peptide 4 (PDP-4),90778,18641
BMRB,18644,PawS Derived Peptide 5 (PDP-5),90778,18641
BMRB,18645,PawS Derived Peptide 7 (PDP-7),90778,18641
PDB,2LWQ,BMRB Entry Tracking System,90778,18641
BMRB,15074,Parkin in-between RING domain,90796,18642
PDB,2JMO,Parkin in-between RING domain,90796,18642
PDB,2LWR,BMRB Entry Tracking System,90796,18642
BMRB,18641,PawS derived peptide 11 (PDP-11),90821,18643
BMRB,18644,PawS Derived Peptide 5 (PDP-5),90821,18643
BMRB,18645,PawS Derived Peptide 7 (PDP-7),90821,18643
PDB,2LWS,BMRB Entry Tracking System,90821,18643
BMRB,18641,PawS derived peptide 11 (PDP-11),90839,18644
BMRB,18643,PawS Derived Peptide 4 (PDP-4),90839,18644
BMRB,18645,PawS Derived Peptide 7 (PDP-7),90839,18644
PDB,2LWT,BMRB Entry Tracking System,90839,18644
BMRB,18641,PawS derived peptide 11 (PDP-11),90857,18645
BMRB,18643,PawS Derived Peptide 4 (PDP-4),90857,18645
BMRB,18644,PawS Derived Peptide 5 (PDP-5),90857,18645
PDB,2LWU,BMRB Entry Tracking System,90857,18645
BMRB,18649,Transmembrane domain of Amyloid precursor protein WT,90894,18648
PDB,2LZ4,BMRB Entry Tracking System,90894,18648
BMRB,18648,Transmembrane domain of Amyloid precursor protein V44M,90908,18649
PDB,2LZ3,BMRB Entry Tracking System,90908,18649
PDB,2LWW,BMRB Entry Tracking System,90933,18650
PDB,2LWY,BMRB Entry Tracking System,90988,18653
PDB,2LWZ,BMRB Entry Tracking System,91008,18654
PDB,2LX0,BMRB Entry Tracking System,91029,18655
PDB,2LX1,BMRB Entry Tracking System,91049,18656
PDB,2LX2,BMRB Entry Tracking System,91067,18657
PDB,2LX3,BMRB Entry Tracking System,91067,18657
PDB,2LX4,BMRB Entry Tracking System,91081,18658
PDB,2LX5,BMRB Entry Tracking System,91099,18659
PDB,2RQ6,Solution structure of the epsilon subunit of the F1-atpase from thermosynechococcus elongatus BP-1,91099,18659
PDB,2LX7,BMRB Entry Tracking System,91145,18662
BMRB,18666,dUTPase homotrimer (complex form),91211,18665
BMRB,18665,dUTPase homotrimer (apo form),91229,18666
PDB,4B6U,PDBe entry,91249,18667
PDB,2LX9,BMRB Entry Tracking System,91266,18668
BMRB,18670,Sgt2 homodimerization domain,91284,18669
BMRB,18671,complex between the Sgt2 homodimerization domain and the Get5 UBL domain,91284,18669
PDB,2LXA,BMRB Entry Tracking System,91284,18669
PDB,4GOC,Crystal structure of the same protein,91284,18669
PDB,4GOD,"Crystal structure of SGTA dimerization domain, the human homolog of the Get5 binding partner, Sgt2",91284,18669
PDB,4GOE,"Crystal structure of SGTA dimerization domain, the human homolog of Get5 binding partner, Sgt2",91284,18669
PDB,4GOF,"Crystal structure of SGTA dimerization domain, the human homolog of Get5 binding partner, Sgt2",91284,18669
BMRB,18669,Get5 ubiquitin-like domain,91315,18670
BMRB,18671,complex between the Sgt2 homodimerization domain and the Get5 UBL domain,91315,18670
PDB,2lxa,"Solution structure of Get5, the Sgt2 binding partner",91315,18670
PDB,2LXB,BMRB Entry Tracking System,91315,18670
PDB,4GOC,"Crystal structure of Get5, the Sgt2 binding partner",91315,18670
PDB,4GOD,Crystal structure of the human homolog,91315,18670
PDB,4GOE,Crystal structure of the human homolog,91315,18670
PDB,4GOF,Crystal structure of the human homolog,91315,18670
BMRB,18669,Get5 ubiquitin-like domain,91338,18671
BMRB,18670,Sgt2 homodimerization domain,91338,18671
PDB,2lxa,Solution structure of Get5 ubiquitin like domain,91338,18671
PDB,2lxb,Solution structure of Sgt2 homodimerization domain,91338,18671
PDB,2LXC,BMRB Entry Tracking System,91338,18671
PDB,4GOC,Crystal structure of Get5 ubiquitin like domain,91338,18671
PDB,4GOD,"Crystal structure of SGTA homodimerization domain, the human homolog",91338,18671
PDB,4GOE,"Crystal structure of SGTA homodimerization domain, the human homolog",91338,18671
PDB,4GOF,"Crystal structure of SGTA homodimerization domain, the human homolog",91338,18671
PDB,2LXF,BMRB Entry Tracking System,91389,18673
TargetDB,GilaA.01396.a,,91389,18673
PDB,2LXH,BMRB Entry Tracking System,91435,18677
PDB,2LXI,BMRB Entry Tracking System,91454,18678
BMRB,18680,"cold shock protein, LmCsp",91469,18679
PDB,2LXJ,BMRB Entry Tracking System,91469,18679
BMRB,18679,"cold shock protein, LmCsp with dT7",91484,18680
PDB,2LXK,BMRB Entry Tracking System,91484,18680
BMRB,18682,LIP5-CHMP5,91499,18681
PDB,2LXL,BMRB Entry Tracking System,91499,18681
BMRB,18681,LIP5(MIT)2,91514,18682
PDB,2LXM,BMRB Entry Tracking System,91514,18682
BMRB,18686,E170A,91530,18683
BMRB,18687,wild type with 0.35 M TMAO,91530,18683
PDB,2LXO,BMRB Entry Tracking System,91547,18684
BMRB,18683,wild type,91579,18686
BMRB,18687,wild type with 0.35 M TMAO,91579,18686
BMRB,18683,wild type,91596,18687
BMRB,18686,E170A,91596,18687
PDB,2LXP,BMRB Entry Tracking System,91613,18688
BMRB,17691,tpr1 domain,91635,18689
PDB,2LXQ,BMRB Entry Tracking System,91662,18690
BMRB,17689,tpr1 domain,91679,18691
PDB,2LXR,BMRB Entry Tracking System,91695,18692
BMRB,18695,KIX domain complex(3),91728,18694
PDB,2LXS,BMRB Entry Tracking System,91728,18694
BMRB,18694,KIX domain complex(2),91745,18695
PDB,2LXT,BMRB Entry Tracking System,91745,18695
BMRB,18697,rmodN-ACSL complex,91764,18696
BMRB,18696,rmodN,91780,18697
TargetDB,HR8614A,,91797,18698
PDB,2LXV,BMRB Entry Tracking System,91828,18699
PDB,2LXW,BMRB Entry Tracking System,91870,18700
PDB,2l72,,91886,18701
PDB,2lrb,,91886,18701
PDB,4B8T,BMRB Entry Tracking System,91907,18702
BMRB,5356,,91931,18703
PDB,1LQ7,,91931,18703
PDB,2LXY,BMRB Entry Tracking System,91931,18703
PDB,2LXZ,BMRB Entry Tracking System,91977,18705
PDB,2LY0,BMRB Entry Tracking System,91991,18706
PDB,2LY4,BMRB Entry Tracking System,92053,18709
PDB,2LY6,BMRB Entry Tracking System,92085,18710
PDB,4BA8,BMRB Entry Tracking System,92103,18711
PDB,2LY8,BMRB Entry Tracking System,92141,18713
PDB,2LY9,BMRB Entry Tracking System,92164,18714
TargetDB,HR7907F,,92164,18714
BMRB,18716,"HIV-1 myr(-) matrix protein in complex with 1,2-dioctanoyl-sn-phosphatidyl-L-serine",92190,18715
PDB,2LYA,BMRB Entry Tracking System,92190,18715
BMRB,18715,"HIV-1 myr(-) matrix protein in complex with 1,2-dioctanoyl-sn-phosphatidylcholine",92210,18716
PDB,2LYB,BMRB Entry Tracking System,92210,18716
PDB,2LYC,BMRB Entry Tracking System,92230,18717
BMRB,18719,beta 2 integrin tail,92252,18718
BMRB,18718,alpha 4 integrin tail,92267,18719
PDB,2LYD,BMRB Entry Tracking System,92295,18720
BMRB,17909,Resonance assignments of human Steroidogenic acute regulatory-related lipid transfer domain protein 5,92311,18721
BMRB,18723,theta-defensin RTD-1,92335,18722
PDB,1HVZ,"Three-dimensional structure of RTD-1, a cyclic antimicrobial defensins from Rhesus macaque leukocytes.",92335,18722
PDB,2ATG,Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin.,92335,18722
PDB,2LYE,BMRB Entry Tracking System,92335,18722
BMRB,18722,"symmetrical theta-defensin, BTD-2",92355,18723
PDB,1HVZ,"Three-dimensional structure of RTD-1, a cyclic antimicrobial defensins from Rhesus macaque leukocytes.",92355,18723
PDB,2ATG,Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin.,92355,18723
PDB,2LYF,BMRB Entry Tracking System,92355,18723
PDB,2LYG,BMRB Entry Tracking System,92375,18724
PDB,2LYH,BMRB Entry Tracking System,92394,18725
PDB,2LYI,BMRB Entry Tracking System,92415,18726
PDB,1ha1,X-ray crystal structure at 1.75 A resolution,92432,18728
PDB,1l3k,X-ray crystal structure at 1.10 A resolution,92432,18728
PDB,1up1,X-ray crystal structure at 1.90 A resolution,92432,18728
PDB,2LYV,BMRB Entry Tracking System,92432,18728
PDB,4B2V,BMRB Entry Tracking System,92459,18729
BMRB,18733,NB7890A,92536,18732
PDB,2LYX,BMRB Entry Tracking System,92536,18732
BMRB,18732,NP_390345.1,92555,18733
PDB,2LYY,BMRB Entry Tracking System,92555,18733
PDB,2LZ0,BMRB Entry Tracking System,92570,18734
PDB,2lz1,,92590,18735
TargetDB,HR3520O,,92590,18735
PDB,2LZ5,BMRB Entry Tracking System,92616,18736
BMRB,18739,complex of SH3A and Ubiquitin,92633,18737
PDB,2LZ6,BMRB Entry Tracking System,92633,18737
BMRB,17045,KSR1 CA1 monomer,92688,18740
BMRB,17724,KSR1 CA1-CA1a domain (bound to SDS micelles),92688,18740
BMRB,17725,KSR1 CA1-CA1a domain,92688,18740
BMRB,5693,Backbone chemical shift assignments of full-length protein complexed with ligand peptides,92731,18748
PDB,2LZE,BMRB Entry Tracking System,92749,18749
BMRB,18754,IscU Prolyl residues in D-states,92781,18750
PDB,2LZF,BMRB Entry Tracking System,92799,18753
BMRB,18750,IscU Prolyl residues in S-states,92819,18754
PDB,2LZG,BMRB Entry Tracking System,92836,18755
BMRB,18759,C186P/A220P IkappaBalpha (67-287),92854,18756
BMRB,18760,Y254L/T257A IkappaBalpha (67-287),92854,18756
PDB,1HVZ,"Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes",92875,18757
PDB,2ATG,Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin,92875,18757
PDB,2LZI,BMRB Entry Tracking System,92875,18757
PDB,1Z7L,Crystal structure of fragment of mouse ubiquitin-activating enzyme,92895,18758
PDB,2LZJ,BMRB Entry Tracking System,92895,18758
PDB,3CMM,Crystal Structure of the Uba1-Ubiquitin Complex,92895,18758
BMRB,18756,WT IkappaBalpha (67-287),92920,18759
BMRB,18760,Y254L/T257A IkappaBalpha (67-287),92920,18759
BMRB,18756,WT IkappaBalpha (67-287),92949,18760
BMRB,18759,C186P/A220P IkappaBalpha (67-287),92949,18760
PDB,3DXC,CRYSTAL STRUCTURE OF THE INTRACELLULAR DOMAIN OF HUMAN APP IN COMPLEX WITH FE65-PTB2,92965,18761
PDB,2LZK,BMRB Entry Tracking System,92984,18762
PDB,4BD3,BMRB Entry Tracking System,93020,18764
PDB,2LZO,BMRB Entry Tracking System,93057,18766
BMRB,18769,NS2(32-57) GBVB protein,93088,18768
BMRB,18768,NS2(2-32) GBVB protein,93105,18769
BMRB,18771,TatA oligomer,93135,18770
PDB,2LZR,BMRB Entry Tracking System,93135,18770
BMRB,18770,TatA T22P,93155,18771
PDB,2LZS,BMRB Entry Tracking System,93155,18771
BMRB,18773,SCIN-B,93179,18772
BMRB,18775,yeast OMP synthase in complex with orotidine 5 -monophosphate,93213,18774
BMRB,18774,yeast OMP synthase (apo form),93234,18775
BMRB,18781,DNA duplex containing mispair-aligned O6G-heptylene-O6G interstrand cross-link,93348,18780
PDB,1N4B,,93348,18780
PDB,1S37,,93348,18780
PDB,1XCI,,93348,18780
PDB,1N4B,,93371,18781
PDB,1S37,,93371,18781
PDB,1XCI,,93371,18781
PDB,2LZV,,93371,18781
PDB,2YMJ,PDBe entry,93394,18782
BMRB,18786,Erbin PDZ S47,93443,18785
BMRB,18785,Erbin PDZ WT,93459,18786
PDB,2LZZ,BMRB Entry Tracking System,93475,18787
PDB,2M00,BMRB Entry Tracking System,93497,18788
BMRB,18793,BCL-xL in complex with PUMA BH3 peptide,93553,18792
PDB,2M03,BMRB Entry Tracking System,93553,18792
PDB,2M04,Solution structure of BCL-xL in complex with PUMA BH3 peptide,93553,18792
BMRB,18792,"BCL-xL, apo form",93571,18793
PDB,2M03,"Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains",93571,18793
PDB,2M04,BMRB Entry Tracking System,93571,18793
BMRB,18797,OmpX in DPC micelles,93624,18796
BMRB,4936,chemical shifts in DHPC detergent micelles,93624,18796
PDB,1q9f,NMR structure of OmpX in DHPC micelles,93624,18796
PDB,1qj8,Crystal Structure of OmpX,93624,18796
PDB,2M06,BMRB Entry Tracking System,93624,18796
BMRB,18796,NMR resonance assignment of OmpX in phospholipid nanodiscs,93642,18797
BMRB,4936,NMR resonance assignment of OmpX in DHPC micelles,93642,18797
PDB,1q9f,NMR structure of OmpX in DHPC micelles,93642,18797
PDB,1qj8,Crystal structure of OmpX,93642,18797
PDB,2m06,NMR structure of OmpX in phospholipid nanodiscs,93642,18797
PDB,2M07,BMRB Entry Tracking System,93642,18797
BMRB,18799,HO-1 (F79A mutant),93659,18798
BMRB,18800,HO-1 (in complex with zinc protoporphyrin IX),93659,18798
PDB,1IRM,crystal structure of HO-1 (apo form),93659,18798
BMRB,18798,"HO-1 (wild type, apo form)",93677,18799
BMRB,18800,"HO-1 (wild type, in complex with zinc protoporphyrin IX)",93677,18799
PDB,1DVE,crystal structure of HO-1 in complex with heme,93677,18799
PDB,1IRM,crystal structure of HO1 (wild type),93677,18799
PDB,3VYZ,crystal structure of this protein,93677,18799
BMRB,18798,"HO-1 (wild type, apo form)",93707,18800
BMRB,18799,"HO-1 (F79A mutant, apo form)",93707,18800
PDB,1DVE,crystal structure of HO-1 in complex with heme,93707,18800
PDB,1IRM,crystal structure of HO1 (wild type),93707,18800
PDB,3VYZ,crystal structure of this protein,93707,18800
PDB,2M09,BMRB Entry Tracking System,93745,18802
PDB,2M0B,BMRB Entry Tracking System,93782,18804
PDB,2M0C,BMRB Entry Tracking System,93800,18805
TargetDB,HR4490C,,93800,18805
PDB,2LVR,Miz-1 Zinc Finger domain 8,93825,18806
PDB,2LVT,Miz-1 Zinc Finger domain 9,93825,18806
PDB,2LVU,Miz-1 Zinc Finger domain 10,93825,18806
PDB,2M0D,BMRB Entry Tracking System,93825,18806
PDB,2M0E,BMRB Entry Tracking System,93825,18806
PDB,2M0F,BMRB Entry Tracking System,93825,18806
PDB,3PYI,Structure of the N-terminal domain of C. elegans SAS-6,93845,18807
PDB,2M0G,BMRB Entry Tracking System,93865,18808
PDB,1rg3,,93887,18809
PDB,1rg4,,93887,18809
PDB,2M0M,BMRB Entry Tracking System,93914,18811
PDB,2M0N,BMRB Entry Tracking System,93934,18812
PDB,2M0O,BMRB Entry Tracking System,93956,18813
BMRB,18421,eiavCAmonomer,93992,18815
PDB,2FYJ,NMR Solution structure of calcium-loaded LRP double module,94008,18816
PDB,2i1p,Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin,94008,18816
PDB,2M0P,BMRB Entry Tracking System,94008,18816
PDB,2M0R,BMRB Entry Tracking System,94048,18818
BMRB,18820,ApoAcpP-1,94068,18819
BMRB,18821,ApoAcpP,94068,18819
BMRB,18819,ApoAcpP-3,94098,18820
BMRB,18821,ApoAcpP,94098,18820
BMRB,18819,ApoAcpP-3,94115,18821
BMRB,18820,ApoAcpP-1,94115,18821
PDB,2M0S,BMRB Entry Tracking System,94132,18822
BMRB,18825,C-terminal CFTR peptide and extended PDZ1 domain from NHERF1,94164,18824
BMRB,18826,C-terminal CFTR peptide and extended PDZ2 domain from NHERF1,94164,18824
PDB,2M0T,BMRB Entry Tracking System,94164,18824
BMRB,18824,extended PDZ1 domain from NHERF1,94186,18825
BMRB,18826,C-terminal CFTR peptide and extended PDZ2 domain from NHERF1,94186,18825
PDB,2M0U,BMRB Entry Tracking System,94186,18825
BMRB,18824,extended PDZ1 domain from NHERF1,94208,18826
BMRB,18825,C-terminal CFTR peptide and extended PDZ1 domain from NHERF1,94208,18826
PDB,2M0V,BMRB Entry Tracking System,94208,18826
BMRB,18829,TIA-1 protein,94254,18828
BMRB,18828,holocytochrome c,94272,18829
PDB,2M0X,BMRB Entry Tracking System,94313,18831
PDB,2M0Y,BMRB Entry Tracking System,94328,18832
PDB,2M0Z,BMRB Entry Tracking System,94349,18833
PDB,2M10,BMRB Entry Tracking System,94376,18834
PDB,2M11,BMRB Entry Tracking System,94403,18835
BMRB,18317,canecystatin-1 from Saccharum officinarum,94489,18839
PDB,2M13,BMRB Entry Tracking System,94521,18840
PDB,1Y5O,,94580,18842
PDB,2GS0,,94580,18842
PDB,2K2U,,94580,18842
PDB,2L2I,,94580,18842
PDB,2LOX,,94580,18842
PDB,2M14,BMRB Entry Tracking System,94580,18842
PDB,2M74,BMRB Entry Tracking System,94609,18843
BMRB,18846,Sup12-RNA,94652,18845
PDB,4CH0,Sup12,94652,18845
BMRB,18845,SUP-12,94673,18846
PDB,2M18,BMRB Entry Tracking System,94693,18847
PDB,2M19,BMRB Entry Tracking System,94758,18850
PDB,4HRO,,94758,18850
PDB,4HRS,,94758,18850
BMRB,18852,HIV-1 Rev ARM peptide (residues T34-R50),94779,18851
PDB,1ETG,,94779,18851
PDB,1RPV,,94779,18851
BMRB,18851,HIV-1 Rev ARM single polypeptide chain,94798,18852
PDB,1ETG,,94798,18852
PDB,1RPV,,94798,18852
PDB,2M1A,BMRB Entry Tracking System,94798,18852
PDB,1MXI,,94849,18855
PDB,2M1C,BMRB Entry Tracking System,94866,18856
BMRB,16300,intrinsically unfolded alpha-synuclein,94881,18857
BMRB,16342,"Backbone 1H, 13C, 15N and 13C-beta Chemical Shift Assignments for alpha-synuclein at pH 3",94881,18857
BMRB,16543,Backbone 1H and 15N Chemical Shifts for Disordered alpha-Synuclein,94881,18857
BMRB,6968,Heteronuclear assignment of backbone and Cb of naturally unfolded alpha-synuclein,94881,18857
BMRB,18859,Biosynthetic engineered B28K-B29P human insulin monomer structure in in water solutions,94959,18858
PDB,2M1D,BMRB Entry Tracking System,94959,18858
BMRB,18858,Biosynthetic engineered B28K-B29P human insulin monomer structure in in water solutions,94979,18859
PDB,2M1E,BMRB Entry Tracking System,94979,18859
BMRB,16939,NMR Data Upload,95013,18860
BMRB,17498,Solid-state NMR assignment of alpha-synuclein amyloid fibrils,95013,18860
BMRB,18232,Solid-state NMR assignments for mouse alpha-synuclein fibrils,95013,18860
PDB,2RQS,,95122,18864
PDB,1SKH,NMR Solution Structure and Membrane Interaction of the N-Terminal Sequence (1-30) of the Bovine Prion Protein,95155,18865
PDB,1Z65,"NMR Solution Structure of the Peptide Fragment 1-30, Derived from Unprocessed Mouse Doppel Protein, in DHPC Micelles",95155,18865
PDB,2M1K,BMRB Entry Tracking System,95193,18868
PDB,2M1N,BMRB Entry Tracking System,95277,18871
PDB,2M1O,BMRB Entry Tracking System,95292,18872
PDB,1PNX,Structure of the WT PHD domain of ING4 bound to Histone H3 peptide with K4me3,95333,18874
PDB,2k1J,Structure of the WT PHD domain of ING4,95333,18874
PDB,2VNF,Structure of the WT PHD domain of ING4 bound to Histone H3 peptide with K4me3,95333,18874
PDB,4AFL,Structure of the N-terminal dimerization domain of ING4,95333,18874
BMRB,18722,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",95355,18875
PDB,2lye,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",95355,18875
PDB,2M1P,BMRB Entry Tracking System,95355,18875
PDB,3ZEH,BMRB Entry Tracking System,95414,18878
PDB,2K65,,95474,18881
PDB,2K66,,95474,18881
PDB,2M23,,95474,18881
PDB,2M24,,95474,18881
BMRB,18883,TICAM-1 TIR domain,95505,18882
PDB,2M1W,BMRB Entry Tracking System,95505,18882
BMRB,18882,TICAM-2 TIR domain,95524,18883
PDB,2M1X,BMRB Entry Tracking System,95524,18883
PDB,2M1Z,BMRB Entry Tracking System,95578,18887
PDB,2M20,BMRB Entry Tracking System,95596,18888
BMRB,18890,CD3g in native state,95623,18889
BMRB,18889,CD3e cytosolyc domain in disordered and disordered state,95660,18890
BMRB,18892,Solution structure of the helix II template boundary element from Tetrahymena telomerase RNA,95681,18891
PDB,2M21,BMRB Entry Tracking System,95681,18891
BMRB,18891,Solution structure of the Tetrahymena telomerase RNA stem IV terminal loop,95701,18892
PDB,2M22,BMRB Entry Tracking System,95701,18892
BMRB,18894,d3'-hairpin including the exon binding site 1 (EBS1) of the group II intron Sc.ai5gamma,95721,18893
PDB,2K65,,95721,18893
PDB,2K66,,95721,18893
PDB,2M1V,,95721,18893
PDB,2M24,,95721,18893
BMRB,18893,d3'-hairpin of the group II intron Sc.ai5gamma including EBS1 bound to IBS1,95750,18894
PDB,2K65,,95750,18894
PDB,2K66,,95750,18894
PDB,2M1V,,95750,18894
PDB,2M23,,95750,18894
PDB,4B1Q,BMRB Entry Tracking System,95819,18897
BMRB,18911,protein in complex with ligand 1RG,95891,18900
PDB,3ZG4,BMRB Entry Tracking System,95891,18900
PDB,2M26,BMRB Entry Tracking System,95913,18901
PDB,2M27,BMRB Entry Tracking System,95929,18902
PDB,2M2B,BMRB Entry Tracking System,95984,18905
PDB,2M2C,BMRB Entry Tracking System,96015,18907
PDB,2M2D,BMRB Entry Tracking System,96032,18908
PDB,2M2E,BMRB Entry Tracking System,96052,18909
BMRB,18900,protein in apo form,96111,18911
PDB,3ZGP,BMRB Entry Tracking System,96111,18911
PDB,2M2F,BMRB Entry Tracking System,96135,18912
BMRB,18722,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",96150,18913
BMRB,18914,"[Aba3,7,12,16]BTD-2 cyclic peptide",96150,18913
BMRB,18931,"[Aba5,7,12,14]BTD-2 cyclic peptide",96150,18913
BMRB,18937,"[Aba3,5,7,12,14,16]BTD-2 cyclic peptide",96150,18913
BMRB,18938,"BTD-2[3,4] Acyclic analogue",96150,18913
PDB,2lye,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",96150,18913
PDB,2M2G,BMRB Entry Tracking System,96150,18913
BMRB,18913,"[Aba3,16]BTD-2 cyclic peptide",96170,18914
BMRB,18931,"[Aba5,7,12,14]BTD-2 cyclic peptide",96170,18914
BMRB,18937,"[Aba3,5,7,12,14,16]BTD-2 cyclic peptide",96170,18914
BMRB,18938,"BTD-2[3,4] Acyclic analogue",96170,18914
PDB,2M2H,BMRB Entry Tracking System,96170,18914
PDB,2M2I,BMRB Entry Tracking System,96206,18916
PDB,2M2J,BMRB Entry Tracking System,96227,18917
PDB,2M33,BMRB Entry Tracking System,96267,18919
BMRB,18923,[L-HisB24] insulin analogue at pH 8.0,96319,18921
BMRB,18924,[D-HisB24] insulin analogue at pH 1.9,96319,18921
BMRB,18925,[D-HisB24] insulin analogue at pH 8.0,96319,18921
PDB,2M2M,BMRB Entry Tracking System,96319,18921
BMRB,18921,[L-HisB24] insulin analogue at pH 1.9,96353,18923
BMRB,18924,[D-HisB24] insulin analogue at pH 1.9,96353,18923
BMRB,18925,[D-HisB24] insulin analogue at pH 8.0,96353,18923
PDB,2M2N,BMRB Entry Tracking System,96353,18923
BMRB,18921,[L-HisB24] insulin analogue at pH 1.9,96371,18924
BMRB,18923,[L-HisB24] insulin analogue at pH 8.0,96371,18924
BMRB,18925,[D-HisB24] insulin analogue at pH 8.0,96371,18924
PDB,2M2O,BMRB Entry Tracking System,96371,18924
BMRB,18921,[L-HisB24] insulin analogue at pH 1.9,96389,18925
BMRB,18923,[L-HisB24] insulin analogue at pH 8.0,96389,18925
BMRB,18924,[D-HisB24] insulin analogue at pH 1.9,96389,18925
PDB,2M2P,BMRB Entry Tracking System,96389,18925
BMRB,18928,T638E/S657E V5 domain of Protein Kinase C alpha,96421,18927
BMRB,18929,"V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96421,18927
BMRB,18930,"T638E/S657E V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96421,18927
PDB,3IW4,Crystal structure of PKC alpha in complex with NVP-AEB071,96421,18927
BMRB,18927,V5 domain of Protein Kinase C alpha,96436,18928
BMRB,18929,"V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96436,18928
BMRB,18930,"T638E/S657E V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96436,18928
PDB,3IW4,Crystal structure of PKC alpha in complex with NVP-AEB071,96436,18928
BMRB,18927,V5 domain of Protein Kinase C alpha,96451,18929
BMRB,18928,T638E/S657E V5 domain of Protein Kinase C alpha,96451,18929
BMRB,18930,"T638E/S657E V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96451,18929
PDB,3IW4,Crystal structure of PKC alpha in complex with NVP-AEB071,96451,18929
BMRB,18927,V5 domain of Protein Kinase C alpha,96482,18930
BMRB,18928,T638E/S657E V5 domain of Protein Kinase C alpha,96482,18930
BMRB,18929,"V5 domain of Protein Kinase C alpha, in complex with DPC micelles",96482,18930
PDB,3IW4,Crystal structure of PKC alpha in complex with NVP-AEB071,96482,18930
BMRB,18722,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",96499,18931
BMRB,18914,"[Aba3,7,12,16]BTD-2 cyclic peptide",96499,18931
BMRB,18937,"[Aba3,5,7,12,14,16]BTD-2 cyclic peptide",96499,18931
BMRB,18938,"BTD-2[3,4] Acyclic analogue",96499,18931
PDB,2lye,"High resolution NMR solution structure of a symmetrical theta-defensin, BTD-2",96499,18931
PDB,2M2S,BMRB Entry Tracking System,96499,18931
BMRB,18934,Binary complex of African Swine Fever Virus Pol X with MgdGTP,96519,18933
BMRB,18935,Ternary complex of African Swine Fever Virus Pol X with MgdGTP and DNA,96519,18933
PDB,2M2T,African Swine Fever Virus Pol X (free form),96519,18933
PDB,2M2U,Binary complex of African Swine Fever Virus Pol X with MgdGTP,96519,18933
PDB,2M2V,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; substrates-bound protein-only structure,96519,18933
PDB,2M2W,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; coordinates of substrates and protein,96519,18933
BMRB,18933,African Swine Fever Virus Pol X (free form),96536,18934
BMRB,18935,Ternary complex of African Swine Fever Virus Pol X with MgdGTP and DNA,96536,18934
PDB,2M2T,African Swine Fever Virus Pol X (free form),96536,18934
PDB,2M2U,Binary complex of African Swine Fever Virus Pol X with MgdGTP,96536,18934
PDB,2M2V,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; substrates-bound protein-only structure,96536,18934
PDB,2M2W,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; coordinates of substrates and protein,96536,18934
BMRB,18933,African Swine Fever Virus Pol X (free form),96558,18935
BMRB,18934,Binary complex of African Swine Fever Virus Pol X with MgdGTP,96558,18935
PDB,2M2T,African Swine Fever Virus Pol X (free form),96558,18935
PDB,2M2U,Binary complex of African Swine Fever Virus Pol X with MgdGTP,96558,18935
PDB,2M2V,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; substrates-bound protein-only structure,96558,18935
PDB,2M2W,Ternary complex of African Swine Fever Virus Pol X with DNA and MgdGTP; coordinates of substrates and protein,96558,18935
BMRB,18913,"[Aba3,16]BTD-2 cyclic peptide",96580,18937
BMRB,18914,"[Aba3,7,12,16]BTD-2 cyclic peptide",96580,18937
BMRB,18931,"[Aba5,7,12,14]BTD-2 cyclic peptide",96580,18937
BMRB,18938,"BTD-2[3,4] Acyclic analogue",96580,18937
PDB,2lye,"High resolution NMR structure of a symmetrical theta-defensin, BTD-2",96580,18937
PDB,2M2X,BMRB Entry Tracking System,96580,18937
BMRB,18722,High resolution NMR solution structure of a symmetrical theta-defensin BTD-2,96601,18938
BMRB,18913,"[Aba3,16]BTD-2 cyclic peptide",96601,18938
BMRB,18914,"[Aba3,7,12,16]BTD-2 cyclic peptide",96601,18938
BMRB,18931,"[Aba5,7,12,14]BTD-2 cyclic peptide",96601,18938
BMRB,18937,"[Aba3,5,7,12,14,16]BTD-2 cyclic peptide",96601,18938
PDB,2lye,High resolution NMR solution structure of a symmetrical theta-defensin BTD-2,96601,18938
PDB,2M2Y,BMRB Entry Tracking System,96601,18938
PDB,2M2Z,BMRB Entry Tracking System,96620,18939
BMRB,18020,Entry contains the chemical shifts of the apo state of integrin alpha1I-domain,96672,18942
BMRB,18021,Entry contains the chemical shifts of the Mg2+-bound state of integrin alpha1I-domain (no collagen ligand),96672,18942
PDB,2M32,BMRB Entry Tracking System,96672,18942
PDB,2M34,BMRB Entry Tracking System,96716,18944
PDB,2M36,BMRB Entry Tracking System,96753,18946
PDB,2M39,BMRB Entry Tracking System,96829,18950
PDB,2M3C,BMRB Entry Tracking System,96897,18953
PDB,2M3D,BMRB Entry Tracking System,96918,18954
BMRB,18956,Structure of NAB2P tandem Zinc finger 34,96937,18955
PDB,3ZJ1,BMRB Entry Tracking System,96937,18955
PDB,3zj2,Structure of NAB2P tandem Zinc finger 34,96937,18955
BMRB,18955,Structure of NAB2P tandem Zinc finger 12,96961,18956
PDB,3zj1,Structure of NAB2P tandem Zinc finger 12,96961,18956
PDB,3ZJ2,BMRB Entry Tracking System,96961,18956
PDB,2M3K,BMRB Entry Tracking System,97102,18966
PDB,2M3L,BMRB Entry Tracking System,97117,18967
PDB,1GM2,,97169,18970
PDB,1JBL,,97169,18970
PDB,1I5H,,97189,18971
PDB,2EZ5,,97189,18971
PDB,2M3O,BMRB Entry Tracking System,97189,18971
PDB,3ZKT,PDBe entry,97225,18972
PDB,2KZ2,,97300,18976
BMRB,18228,"TpbA, Ligand-free",97327,18977
PDB,2JV2,solution structure of the Ph1500 N-domain,97346,18978
PDB,2M3X,BMRB Entry Tracking System,97346,18978
BMRB,18981,DNA duplex containing a cluster of mutagenic 8-oxo-guanine and abasic site lesion,97373,18979
BMRB,18984,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : alpha anomer (AP6, 8OG 14)",97373,18979
BMRB,18985,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer (6AP, 8OG14)",97373,18979
PDB,1A1T,HIV-1 NC complex with RNA stem loop,97390,18980
PDB,1F6U,HIV-1 NC complex with RNA stem loop,97390,18980
PDB,2M3Z,BMRB Entry Tracking System,97390,18980
BMRB,18979,DNA duplex containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer,97409,18981
BMRB,18984,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : alpha anomer (AP6, 8OG 14)",97409,18981
BMRB,18985,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer (6AP, 8OG14)",97409,18981
PDB,1OA8,X-Ray structure of free ataxin-1 AXH domain,97426,18982
PDB,1V06,Solution structure of the homologous AXH domain from transcription factor HBP1,97426,18982
BMRB,18979,DNA duplex containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer,97449,18984
BMRB,18981,DNA duplex containing a cluster of mutagenic 8-oxo-guanine and abasic site lesion,97449,18984
BMRB,18985,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer (6AP, 8OG14)",97449,18984
BMRB,18979,DNA duplex containing a cluster of 8-oxo-guanine and abasic site lesion : beta anomer,97466,18985
BMRB,18981,DNA duplex containing a cluster of mutagenic 8-oxo-guanine and abasic site lesion,97466,18985
BMRB,18984,"DNA containing a cluster of 8-oxo-guanine and abasic site lesion : alpha anomer (AP6, 8OG 14)",97466,18985
PDB,2M45,BMRB Entry Tracking System,97483,18986
PDB,2M47,BMRB Entry Tracking System,97547,18989
PDB,1WD2,,97574,18990
PDB,2JMO,,97574,18990
PDB,2M48,BMRB Entry Tracking System,97574,18990
BMRB,18992,"[2Fe-2S]-ferredoxin, reduced state",97599,18991
PDB,1I7H,,97599,18991
BMRB,18991,"[2Fe-2S]-ferredoxin, oxidized state",97618,18992
PDB,1I7H,,97618,18992
PDB,3V0R,,97637,18993
BMRB,18999,Allatide O4 Conformation 1,97689,18998
BMRB,18998,Allatide O4 Conformation 2,97703,18999
PDB,2M4E,BMRB Entry Tracking System,97745,19000
PDB,2M4F,BMRB Entry Tracking System,97773,19001
BMRB,19003,Core Domain (10-76) of the Feline Calicivirus VPg protein,97793,19002
PDB,2M4G,BMRB Entry Tracking System,97793,19002
BMRB,19002,Core Domain (11-85) of the Murine Norovirus VPg protein,97814,19003
PDB,2M4H,BMRB Entry Tracking System,97814,19003
BMRB,19005,(His)6CcPCN,97838,19004
BMRB,19004,CcP(His)6CN,97858,19005
PDB,1HF2,,97896,19007
PDB,3GHF,,97896,19007
PDB,2M4J,BMRB Entry Tracking System,97940,19009
BMRB,17410,"1H, 15N and 13C backbone chemical shift assignment of the titin A67-A68 domain tandem",97956,19010
BMRB,19011,"1H, 15N and 13C backbone chemical shift assignment of the titin A60 domain",97956,19010
PDB,1BPV,TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE,97956,19010
BMRB,17410,"1H, 15N and 13C backbone chemical shift assignment of the titin A67-A68 domain tandem",97976,19011
BMRB,19010,"1H, 15N and 13C backbone chemical shift assignment of the titin A59-A60 domain tandem",97976,19011
PDB,1BPV,"TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES",97976,19011
BMRB,19033,SH3 domain of human RAS GAP 1,97996,19012
BMRB,19034,third RNA Recognition Motif (RRM) of U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) 2,97996,19012
PDB,2M4L,BMRB Entry Tracking System,97996,19012
PDB,2M4M,BMRB Entry Tracking System,98015,19013
TargetDB,NYSGRC-019428,,98015,19013
PDB,2M4N,BMRB Entry Tracking System,98037,19014
TargetDB,NYSGRC-010744,,98037,19014
PDB,2IHB,Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3,98063,19015
PDB,2V4Z,THE CRYSTAL STRUCTURE OF THE HUMAN G-PROTEIN SUBUNIT ALPHA (GNAI3) IN COMPLEX WITH AN ENGINEERED REGULATOR OF G-PROTEIN SIGNALING TYPE 2 DOMAIN (RGS2),98063,19015
PDB,4G5R,Structure of LGN GL4/Galphai3 complex,98063,19015
PDB,4G5S,Structure of LGN GL3/Galphai3 complex,98063,19015
PDB,2M4P,BMRB Entry Tracking System,98084,19017
PDB,2M4Q,BMRB Entry Tracking System,98098,19018
PDB,2M4V,BMRB Entry Tracking System,98116,19023
BMRB,17937,"This current entry contains the chemical shift assignments determined by using a different instrument and references, for the same CAP-Gly domain. 
The NMR experiments and assignment process are completely independent from the former deposition.",98154,19025
BMRB,19030,Huwentoxin-IV,98170,19026
BMRB,19032,Huwentoxin-IV,98170,19026
PDB,2M4X,BMRB Entry Tracking System,98170,19026
PDB,2M4Y,BMRB Entry Tracking System,98184,19027
BMRB,19026,HWTX-IV,98232,19030
BMRB,19032,Huwentoxin-IV,98232,19030
PDB,2M4Z,BMRB Entry Tracking System,98232,19030
BMRB,19025,"Using the same NMR experiment conditions, instrument and reference. From the chemical shift difference between the current entry and 19025, we can know the chemical shift perturbations of CAP-Gly upon binding to EB1",98246,19031
BMRB,19026,HWTX-IV,98262,19032
BMRB,19030,Huwentoxin-IV,98262,19032
PDB,2M50,BMRB Entry Tracking System,98262,19032
BMRB,19012,hypothetical protein BT_0846 from Bacteroides thetaiotaomicron VPI-5482 (NP_809759.1),98276,19033
BMRB,19034,third RNA Recognition Motif (RRM) of U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) 2,98276,19033
PDB,2GQI,,98276,19033
PDB,2J05,,98276,19033
PDB,2J06,,98276,19033
PDB,4FSS,,98276,19033
BMRB,19012,hypothetical protein BT_0846 from Bacteroides thetaiotaomicron VPI-5482 (NP_809759.1),98295,19034
BMRB,19033,SH3 domain of human RAS GAP 1,98295,19034
PDB,1O0P,,98295,19034
PDB,1OPI,,98295,19034
PDB,2M0G,,98295,19034
PDB,3V4M,,98295,19034
PDB,4FXW,,98295,19034
PDB,2M53,BMRB Entry Tracking System,98314,19035
PDB,2M55,BMRB Entry Tracking System,98337,19036
NDB,1dz4,,98376,19038
NDB,1xlp,,98376,19038
PDB,2M56,BMRB Entry Tracking System,98376,19038
PDB,2M58,BMRB Entry Tracking System,98435,19040
PDB,1H0T,,98497,19043
PDB,2M5A,BMRB Entry Tracking System,98497,19043
PDB,1pcm,,98518,19044
PDB,2BID,NMR strucuture of apo human BID,98533,19045
PDB,2IMT,X-ray structure of human apo BAK,98533,19045
PDB,2M5B,BMRB Entry Tracking System,98533,19045
BMRB,19048,Metallo-Beta-Lactamase BcII,98575,19047
PDB,2M5C,BMRB Entry Tracking System,98575,19047
BMRB,19047,Metallo-Beta-Lactamase BcII,98606,19048
PDB,2M5D,BMRB Entry Tracking System,98606,19048
PDB,3ZOB,BMRB Entry Tracking System,98637,19049
PDB,1EXR,The 1.0 Angstrom crystal structure of Ca2+-bound calmodulin,98657,19050
PDB,2KXW,Structure of the C-domain fragment of apo-calmodulin bound to the IQ motif of NaV1.2,98657,19050
BMRB,19060,Triplet cross-beta amyloid fibril,98799,19058
PDB,2m5k,BMRB Entry Tracking System,98799,19058
BMRB,19058,doublet cross-beta amyloid fibril,98833,19060
PDB,2M5M,BMRB Entry Tracking System,98833,19060
PDB,2M5N,BMRB Entry Tracking System,98864,19062
BMRB,19064,TIAR RRM2 chemical shifts in bound to RNA 5'-UUAUUU-3',98880,19063
PDB,2DH7,Solution structure of the second RNA binding domain in Nucleolysin TIAR,98880,19063
BMRB,19063,TIAR RRM2 chemical shifts in the apo state,98896,19064
PDB,2DH7,Solution structure of the second RNA binding domain in Nucleolysin TIAR,98896,19064
BMRB,19254,FimH Y48A mutant - Heptyl-mannose complex,98929,19066
BMRB,19255,FimH Y48A mutant,98929,19066
BMRB,19256,FimH -heptyl-mannose complex,98929,19066
PDB,3ZPM,BMRB Entry Tracking System,98957,19067
PDB,2M5O,BMRB Entry Tracking System,98978,19068
BMRB,15826,five mutations,99012,19069
BMRB,5514,eight mutations,99012,19069
BMRB,5666,six mutations,99012,19069
PDB,2Y0G,X-ray structure of EFGP protein (identical sequence),99012,19069
BMRB,19071,"GLUCAGON AIB2,16 LYS13-GAMMAGLU-GAMMAGLU-C16 AMIDE (IN D-TFE)",99030,19070
PDB,2M5P,BMRB Entry Tracking System,99030,19070
BMRB,19070,"GLUCAGON AIB2,16 LYS13-GAMMAGLU-GAMMAGLU-C16 AMIDE (IN WATER)",99051,19071
PDB,2M5Q,BMRB Entry Tracking System,99051,19071
BMRB,17964,"Backbone 1H, 13C, and 15N Chemical Shift Assignment for inactive HIV-1 protease CRF01_AE",99072,19072
BMRB,17994,"Backbone 1H, 13C, and 15N Chemical Shift Assignment for inactive HIV-1 protease Bmut5",99072,19072
BMRB,18963,Free Dido PHD domain,99089,19074
PDB,2M3H,NMR solution structure of free Dido PHD domain,99089,19074
BMRB,19076,"1H, 13C, and 15N backbone chemical shift assignments of the iron-free protoporphyrin IX yeast cytochrome c peroxidase with the C-terminal His-tag",99106,19075
BMRB,19075,"1H, 13C, and 15N backbone chemical shift assignments of the resting-state yeast cytochrome c peroxidase with the N-terminal His-tag",99122,19076
PDB,1TSN,,99229,19082
BMRB,19885,"Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain",99251,19083
PDB,2MMH,BMRB Entry Tracking System,99265,19084
PDB,2M7Y,PDB entry,99265,19084
PDB,4hgu,X-ray structure,99279,19085
PDB,4beh,Solution structure of human ribosomal protein P1.P2 heterodimer,99293,19086
PDB,4BEF,Crystal structure of Rv2140c,99326,19088
BMRB,19090,EADK_CPMG_CaADP (25C),99342,19089
BMRB,19091,EADK_CPMG_MgADP (25C),99342,19089
BMRB,19092,EADK_R156K_CPMG_ADP_2 (20C),99342,19089
BMRB,19093,EADK_R156K_CPMG_MgADP (20C),99342,19089
BMRB,19089,"EADK_CPMG_ADP (20, 25, 30, 40C)",99362,19090
BMRB,19091,EADK_CPMG_MgADP (25C),99362,19090
BMRB,19092,EADK_R156K_CPMG_ADP_2 (20C),99362,19090
BMRB,19093,EADK_R156K_CPMG_MgADP (20C),99362,19090
BMRB,19089,"EADK_CPMG_ADP (20, 25, 30, 40C)",99381,19091
BMRB,19090,EADK_CPMG_CAADP (25C),99381,19091
BMRB,19092,EADK_R156K_CPMG_ADP_2 (20C),99381,19091
BMRB,19093,EADK_R156K_CPMG_MgADP (20C),99381,19091
BMRB,19089,"EADK_CPMG_ADP (20, 25, 30, 40C)",99400,19092
BMRB,19090,EADK_CPMG_CaADP (25C),99400,19092
BMRB,19091,EADK_CPMG_MgADP (25C),99400,19092
BMRB,19093,EADK_R156K_CPMG_MgADP (20C),99400,19092
BMRB,19089,"EADK_CPMG_ADP (20, 25, 30, 40C)",99417,19093
BMRB,19090,EADK_CPMG_CaADP (25C),99417,19093
BMRB,19091,EADK_CPMG_MgADP (25C),99417,19093
BMRB,19092,EADK_R156K_CPMG_ADP (20C),99417,19093
BMRB,19101,Enterocin 7B,99436,19094
PDB,2M5Z,BMRB Entry Tracking System,99436,19094
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99483,19099
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99483,19099
BMRB,19227,Pdx1 (apo form),101870,19228
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99483,19099
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99483,19099
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99483,19099
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99483,19099
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99483,19099
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99483,19099
BMRB,19094,Enterocin 7A,99511,19101
PDB,2M60,BMRB Entry Tracking System,99511,19101
BMRB,19105,MS1 (unfolded),99558,19104
BMRB,19104,MS1 (folded),99576,19105
PDB,2M65,BMRB Entry Tracking System,99627,19108
BMRB,19099,"human beta-2 microglobulin, free protein",99732,19113
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99732,19113
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99732,19113
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99732,19113
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99732,19113
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99732,19113
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99732,19113
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99732,19113
BMRB,19905,Phosphorylated 4E-BP2,99751,19114
PDB,1WAZ,Truncated core domain of the same protein in detergent micelle,99766,19115
PDB,2H3O,Truncated core domain of the same protein in magnetically aligned bicelle,99766,19115
PDB,2LJ2,Truncated core domain of the same protein in proteoliposome,99766,19115
PDB,2M67,BMRB Entry Tracking System,99766,19115
BMRB,19099,"human beta-2 microglobulin, free protein",99780,19116
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99780,19116
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99780,19116
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99780,19116
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99780,19116
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99780,19116
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99780,19116
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99780,19116
PDB,2CNJ,,99798,19117
PDB,2L29,,99798,19117
PDB,2L2A,,99798,19117
BMRB,19099,"human beta-2 microglobulin, free protein",99821,19118
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99821,19118
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99821,19118
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99821,19118
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99821,19118
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99821,19118
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99821,19118
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99821,19118
BMRB,19099,"human beta-2 microglobulin, free protein",99839,19119
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99839,19119
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99839,19119
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99839,19119
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99839,19119
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99839,19119
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99839,19119
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99839,19119
BMRB,19099,"human beta-2 microglobulin, free protein",99857,19120
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99857,19120
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99857,19120
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99857,19120
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99857,19120
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99857,19120
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99857,19120
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99857,19120
BMRB,19099,"human beta-2 microglobulin, free protein",99875,19121
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99875,19121
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99875,19121
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99875,19121
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99875,19121
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99875,19121
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99875,19121
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99875,19121
BMRB,19099,"human beta-2 microglobulin, free protein",99893,19122
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99893,19122
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99893,19122
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99893,19122
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99893,19122
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99893,19122
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99893,19122
BMRB,19123,"bound to the HLA-B2705, complex with Peptide 4 (pGR)",99893,19122
BMRB,19099,"human beta-2 microglobulin, free protein",99911,19123
BMRB,19113,"bound to the HLA-B2709, complex with Peptide 1 (pVIPR)",99911,19123
BMRB,19116,"bound to the HLA-B2709, complex with Peptide 2 (TIS)",99911,19123
BMRB,19118,"bound to the HLA-B2709, complex with Peptide 3 (pLMP2)",99911,19123
BMRB,19119,"bound to the HLA-B2709, complex with Peptide 4 (pGR)",99911,19123
BMRB,19120,"bound to the HLA-B2705, complex with Peptide 1 (pVIPR)",99911,19123
BMRB,19121,"bound to the HLA-B2705, complex with Peptide 2 (TIS)",99911,19123
BMRB,19122,"bound to the HLA-B2705, complex with Peptide 3 (pLMP2)",99911,19123
PDB,2M6A,BMRB Entry Tracking System,99929,19124
PDB,2D9E,solution structure of the bromodomain of Peregrin,99944,19125
PDB,2M6B,monomer structure of the GlyR receptor,99958,19126
PDB,2M6I,pentamer structure of the GlyR receptor,99958,19126
BMRB,16664,"Backbone 1H, 13C, 15N resonance assignments for lysozyme from bacteriophage lambda",99981,19127
BMRB,19129,trans (MAJOR) FORM OF In936,100002,19128
BMRB,19130,cis (MINOR) FORM OF In936 in Methanol,100002,19128
BMRB,19131,trans (MAJOR) FORM OF In937 in Methanol,100002,19128
BMRB,19132,cis(C2-P3) trans (D5-P6) FORM OF lO959 IN WATER,100002,19128
BMRB,19133,trans(C2-P3) trans (D5-P6) of LO959 IN METHANOL,100002,19128
BMRB,19128,cis In936 from C.inscriptus,100016,19129
BMRB,19130,cis (MINOR) FORM OF In936 in Methanol,100016,19129
BMRB,19131,trans (MAJOR) FORM OF In937 in Methanol,100016,19129
BMRB,19132,cis(C2-P3) trans (D5-P6) FORM OF lO959 IN WATER,100016,19129
BMRB,19133,trans(C2-P3) trans (D5-P6) of LO959 IN METHANOL,100016,19129
BMRB,19128,cis In936 from C.inscriptus,100030,19130
BMRB,19129,trans (MAJOR) FORM OF In936,100030,19130
BMRB,19131,trans (MAJOR) FORM OF In937 in Methanol,100030,19130
BMRB,19132,cis(C2-P3) trans (D5-P6) FORM OF lO959 IN WATER,100030,19130
BMRB,19133,trans(C2-P3) trans (D5-P6) of LO959 IN METHANOL,100030,19130
BMRB,19128,cis In936 from C.inscriptus,100044,19131
BMRB,19129,trans (MAJOR) FORM OF In936,100044,19131
BMRB,19130,cis (MINOR) FORM OF In936 in Methanol,100044,19131
BMRB,19132,cis(C2-P3) trans (D5-P6) FORM OF lO959 IN WATER,100044,19131
BMRB,19133,trans(C2-P3) trans (D5-P6) of LO959 IN METHANOL,100044,19131
BMRB,19128,cis In936 from C.inscriptus,100058,19132
BMRB,19129,trans (MAJOR) FORM OF In936,100058,19132
BMRB,19130,cis (MINOR) FORM OF In936 in Methanol,100058,19132
BMRB,19131,trans (MAJOR) FORM OF In937 in Methanol,100058,19132
BMRB,19133,trans(C2-P3) trans (D5-P6) of LO959 IN METHANOL,100058,19132
BMRB,19128,cis In936 from C.inscriptus,100072,19133
BMRB,19129,trans (MAJOR) FORM OF In936,100072,19133
BMRB,19130,cis (MINOR) FORM OF In936 in Methanol,100072,19133
BMRB,19131,trans (MAJOR) FORM OF In937 in Methanol,100072,19133
BMRB,19132,cis(C2-P3) trans (D5-P6) FORM OF lO959 IN WATER,100072,19133
PDB,1ns5,,100086,19134
BMRB,19137,ERGi Backbone Chemical Shifts,100115,19136
BMRB,19138,ERG DNA Complex,100115,19136
BMRB,19136,ERG Ets Domain Backbone Chemical Shifts,100130,19137
BMRB,19138,ERG DNA Complex,100130,19137
BMRB,19136,ERG Ets Domain Backbone Chemical Shifts,100145,19138
BMRB,19137,ERGi Backbone Chemical Shifts,100145,19138
PDB,2X0C,X-Ray structure of the R7-R8 double domain,100162,19139
BMRB,19141,"Dynorphin A, L5S",100176,19140
BMRB,19140,"Dynorphin A, R6W",100193,19141
BMRB,19145,CAP mutant (T127L and S128I) in cGMP-bound state,100243,19144
PDB,4BH9,BMRB Entry Tracking System,100243,19144
PDB,4bhp,CAP mutant (T127L and S128I) in cGMP-bound state,100243,19144
BMRB,19144,CAP mutant (T127L and S128I) in the apo state,100262,19145
PDB,4bh9,CAP mutant (T127L and S128I) in the apo state,100262,19145
PDB,4bhp,CAP mutant (T127L and S128I) in cGMP-bound state,100262,19145
PDB,2CT7,,100302,19147
PDB,2JMO,,100302,19147
PDB,2M6N,BMRB Entry Tracking System,100302,19147
BMRB,19149,actinobacterial transcription factor RbpA,100319,19148
PDB,2M6O,BMRB Entry Tracking System,100319,19148
BMRB,19148,actinobacterial transcription factor RbpA,100335,19149
PDB,2M6P,BMRB Entry Tracking System,100335,19149
BMRB,19152,"1H, 13C and 15N resonance assignments of the apo and holo states of flavodoxin protein YqcA from Escherichia coli",100369,19151
PDB,2M6R,BMRB Entry Tracking System,100369,19151
BMRB,19151,apo YqcA,100386,19152
PDB,2M6S,BMRB Entry Tracking System,100386,19152
PDB,2CNJ,,100405,19153
PDB,2M68,,100405,19153
PDB,3ZPK,ATOMIC-RESOLUTION STRUCTURE OF A CROSS-BETA QUADRUPLET AMYLOID FIBRIL,100489,19157
PDB,2M6X,BMRB Entry Tracking System,100586,19162
PDB,2M6Y,BMRB Entry Tracking System,100608,19163
PDB,4BIT,solution structure of cerebral dopamine neurotrophic factor (CDNF),100627,19164
PDB,2M71,BMRB Entry Tracking System,100687,19168
TargetDB,NYSGRC-011447,,100687,19168
PDB,2M72,BMRB Entry Tracking System,100713,19169
TargetDB,NYSGRC-011441,,100713,19169
BMRB,19173,PTPN11 C-SH2 bound,100784,19172
PDB,2SHP,,100784,19172
PDB,4DGP,,100784,19172
BMRB,19172,PTPN11 C-SH2 free,100800,19173
PDB,2SHP,,100800,19173
PDB,4DGP,,100800,19173
PDB,2M76,BMRB Entry Tracking System,100817,19174
BMRB,18723,High resolution NMR solution structure of the theta-defensin RTD-1,100831,19175
BMRB,19176,[Asp11]RTD-1,100831,19175
BMRB,19177,"[Asp2,11]RTD-1",100831,19175
PDB,2LYF,High resolution NMR solution structure of the theta-defensin RTD-1,100831,19175
PDB,2M77,BMRB Entry Tracking System,100831,19175
BMRB,19175,[Asp2]RTD-1,100850,19176
BMRB,19177,"[Asp2,11]RTD-1",100850,19176
PDB,2M78,BMRB Entry Tracking System,100850,19176
BMRB,19175,[Asp2]RTD-1,100869,19177
BMRB,19176,[Asp11]RTD-1,100869,19177
PDB,2M79,BMRB Entry Tracking System,100869,19177
BMRB,19179,MS1 (ORF PP_3909 from Pseudomonas putida KT2440 encoding a protein similar to bacteriophage lambda ea8.5),100888,19178
PDB,2M7A,BMRB Entry Tracking System,100888,19178
BMRB,19178,MS1 (Enteropathogenic Escherichia coli 0111:H- str. 11128 ORF EC0111_1119 similar to bacteriophage lambda ea8.5),100907,19179
PDB,2M7B,BMRB Entry Tracking System,100907,19179
PDB,1L2Y,,100939,19180
PDB,2JOF,,100939,19180
PDB,2LDJ,,100939,19180
PDB,2LL5,Cyclo-TC1 Trp-cage,100939,19180
PDB,3UC7,,100939,19180
PDB,3UC8,,100939,19180
PDB,1l2y,"original, non-optimized Trp-cage",100987,19183
PDB,1rij,Trp-cage with modified salt-bridge,100987,19183
PDB,2jof,partly optimized Trp-cage,100987,19183
PDB,2ldj,Trp-cage containing D-amino acid,100987,19183
PDB,2ll5,cyclic Trp-cage,100987,19183
PDB,2m7c,circular permutation of the Trp-cage,100987,19183
PDB,2M7G,BMRB Entry Tracking System,101018,19185
BMRB,15131,NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein,101038,19186
BMRB,18520,Entry containing chemical shift assignments for this molecular system in the presence of dodecylphosphocholine micelles,101038,19186
BMRB,6100,"Backbone 1H, 13C and 15N chemical shift assignents of the 18.5kDa isoform of murine myelin basic protein (MBP)",101038,19186
BMRB,6857,Solution structure of an immunodominant epitope of myelin basic protein (MBP) - Conformational dependence on environment of an intrinsically unstructured protein,101038,19186
PDB,2LUG,,101038,19186
PDB,2MA3,BMRB Entry Tracking System,101055,19187
BMRB,19160,hL-FABP in complex with glycocholate,101073,19188
BMRB,19189,hL-FABP in apo form,101073,19188
BMRB,19160,hL-FABP in complex with glycocholate,101093,19189
BMRB,19188,hL-FABP in complex with oleate,101093,19189
PDB,2M7I,BMRB Entry Tracking System,101124,19190
BMRB,19190,Beta-Hairpin Peptidomimetic antibiotic that target LptD in Pseudomonas sp.,101161,19192
PDB,2m7i,,101161,19192
PDB,2M7J,BMRB Entry Tracking System,101161,19192
BMRB,19196,N-terminal domain of (Y81F)-EhCaBP1,101180,19193
BMRB,19197,C-terminal structure of (Y81F)-EhCaBP1,101180,19193
PDB,2M7K,BMRB Entry Tracking System,101180,19193
PDB,1YA7,X-ray structure of the proteasome from Thermoplasma acidophilum in complex with the 11S-activator (PA26) from Trypanosoma brucei,101200,19194
BMRB,19193,N-terminal domain of (Y81F)-EhCaBP1,101236,19196
BMRB,19197,C-terminal structure of (Y81F)-EhCaBP1,101236,19196
PDB,2M7M,BMRB Entry Tracking System,101236,19196
BMRB,19193,N-terminal domain of (Y81F)-EhCaBP1,101256,19197
BMRB,19196,N-terminal domain of (Y81F)-EhCaBP1,101256,19197
PDB,2M7N,BMRB Entry Tracking System,101256,19197
PDB,2M7O,BMRB Entry Tracking System,101277,19198
PDB,2I5O,,101343,19201
PDB,2M7R,BMRB Entry Tracking System,101363,19202
PDB,1X4A,,101380,19203
PDB,2O3D,,101380,19203
PDB,1W7Z,,101414,19205
PDB,2IT7,,101414,19205
BMRB,19209,HDHD4 (complex form),101450,19207
BMRB,6542,,101464,19208
BMRB,19207,HDHD4 (apo form),101488,19209
BMRB,19211,rhodostomin 48ARGDWN-67NGLYG mutant,101517,19210
BMRB,19212,rhodostomin 48ARGDWN-67NPWNG mutant,101517,19210
BMRB,5117,rhodostomin wild type,101517,19210
PDB,2M75,BMRB Entry Tracking System,101517,19210
PDB,2M7F,rhodostomin 48ARGDWN-67NGLYG mutant,101517,19210
PDB,2M7H,rhodostomin 48ARGDWN-67NPWNG mutant,101517,19210
PDB,2PJF,rhodostomin wild type,101517,19210
BMRB,19210,rhodostomin P48A/M52W/P53N mutant,101537,19211
BMRB,19212,rhodostomin 48ARGDWN-67NPWNG mutant,101537,19211
BMRB,5117,rhodostomin wild type,101537,19211
PDB,2M75,rhodostomin P48A/M52W/P53N mutant,101537,19211
PDB,2M7F,BMRB Entry Tracking System,101537,19211
PDB,2M7H,rhodostomin 48ARGDWN-67NPWNG mutant,101537,19211
PDB,2PJF,rhodostomin wild type,101537,19211
BMRB,19210,rhodostomin P48A/M52W/P53N mutant,101557,19212
BMRB,19211,rhodostomin 48ARGDWN-67NGLYG mutant,101557,19212
BMRB,5117,rhodostomin wild type,101557,19212
PDB,2M75,rhodostomin P48A/M52W/P53N mutant,101557,19212
PDB,2M7F,rhodostomin 48ARGDWN-67NGLYG mutant,101557,19212
PDB,2M7H,BMRB Entry Tracking System,101557,19212
PDB,2PJF,rhodostomin wild type,101557,19212
BMRB,19214,"Green Light-Absorbing State of TePixJ, an Active Cyanobacteriochrome Domain",101577,19213
PDB,4FOF,Pb state of TePixJ(GAF) solved to 2.45 A resolution,101577,19213
PDB,4GLQ,Pb state of TePixJ(GAF) solved to 1.77 A resolution,101577,19213
PDB,4FOF,"Pb state of TePixJ(GAF)      
solved to 2.45 A resolution",101598,19214
PDB,4GLQ,"Pb state of TePixJ(GAF)      
solved to 1.77 A resolution",101598,19214
PDB,2LP7,parallel validation of structure using independent methodology,101619,19215
PDB,2M7W,BMRB Entry Tracking System,101619,19215
PDB,2M7X,BMRB Entry Tracking System,101636,19216
BMRB,19221,proteasome related subunit C terminal domain,101703,19220
BMRB,19220,proteasome related subunit N terminal domain,101719,19221
BMRB,19224,PTP1B (residues 1-393),101765,19223
BMRB,19225,carbohydrate binding module of the muscle glycogen-targeting subunit of Protein Phosphatase-1,101765,19223
BMRB,19223,PTP1B (residues 1-301),101786,19224
BMRB,19225,carbohydrate binding module of the muscle glycogen-targeting subunit of Protein Phosphatase-1,101786,19224
BMRB,19223,PTP1B (residues 1-301),101805,19225
BMRB,19224,PTP1B (residues 1-393),101805,19225
BMRB,19228,Pdx1 (DNA complex),101853,19227
PDB,1WEP,,101887,19229
PDB,1X4I,,101887,19229
PDB,1XWH,,101887,19229
PDB,2FUI,,101887,19229
PDB,2JMI,,101887,19229
PDB,2K16,,101887,19229
PDB,2K1J,,101887,19229
PDB,2KKG,,101887,19229
PDB,2M85,BMRB Entry Tracking System,101887,19229
PDB,2RSD,,101887,19229
PDB,2VPD,,101887,19229
PDB,2M86,BMRB Entry Tracking System,101910,19230
BMRB,19234,msp1 E28K variant,101975,19233
BMRB,19233,msp1,101995,19234
PDB,2M89,BMRB Entry Tracking System,102015,19235
BMRB,19247,Populus nigra Plastocyanin (Zn),102039,19236
BMRB,16931,Partial list of chemical shifts for Human FKBP12,102107,19240
BMRB,19241,Analyzing the visible conformational substates of the FK506-binding protein FKBP12,102107,19240
BMRB,19323,Human FKBP12.6-major form,102107,19240
BMRB,19324,Human FKBP12.6-Minor Form,102107,19240
BMRB,16931,Partial list of chemical shifts for Human FKBP12,102125,19241
BMRB,19240,"Analyzing the visible conformational substates of the FK506-binding protein FKBP12, major form",102125,19241
BMRB,19323,Human FKBP12.6-major form,102125,19241
BMRB,19324,Human FKBP12.6-Minor Form,102125,19241
BMRB,19243,Backbone chemical shifts of isolated Domain 1 from E. coli HisJ,102143,19242
BMRB,19244,Backbone chemical shifts of isolated Domain 2 from E. coli HisJ,102143,19242
BMRB,19245,Backbone chemical shifts from E. coli HisJ complexed with Histidine,102143,19242
PDB,2M8C,BMRB Entry Tracking System,102143,19242
BMRB,19242,E. coli apo-HisJ,102162,19243
BMRB,19244,Backbone chemical shifts of isolated Domain 2 from E. coli HisJ,102162,19243
BMRB,19245,Backbone chemical shifts from E. coli HisJ complexed with Histidine,102162,19243
BMRB,19242,E. coli apo-HisJ,102179,19244
BMRB,19243,Backbone chemical shifts of isolated Domain 1 from E. coli HisJ,102179,19244
BMRB,19245,Backbone chemical shifts from E. coli HisJ complexed with Histidine,102179,19244
BMRB,19242,E. coli apo-HisJ,102196,19245
BMRB,19243,Backbone chemical shifts of isolated Domain 1 from E. coli HisJ,102196,19245
BMRB,19244,Backbone chemical shifts of isolated Domain 2 from E. coli HisJ,102196,19245
BMRB,19236,D. crassirhizoma Plastocyanin (Zn),102230,19247
PDB,2M8D,BMRB Entry Tracking System,102247,19248
PDB,2M8F,BMRB Entry Tracking System,102280,19250
PDB,2M8G,BMRB Entry Tracking System,102297,19251
PDB,2M8H,BMRB Entry Tracking System,102317,19252
BMRB,19066,FimH adhesin carbohydrate-binding domain,102352,19254
BMRB,19255,FimH Y48A mutant,102352,19254
BMRB,19256,FimH -heptyl-mannose complex,102352,19254
BMRB,19066,FimH adhesin carbohydrate-binding domain,102373,19255
BMRB,19254,FimH Y48A mutant - Heptyl-mannose complex,102373,19255
BMRB,19256,FimH -heptyl-mannose complex,102373,19255
BMRB,19066,FimH adhesin carbohydrate-binding domain,102392,19256
BMRB,19254,FimH Y48A mutant - Heptyl-mannose complex,102392,19256
BMRB,19255,FimH Y48A mutant,102392,19256
PDB,2M8I,BMRB Entry Tracking System,102434,19258
PDB,2M8K,BMRB Entry Tracking System,102472,19260
PDB,2m8l,BMRB Entry Tracking System,102501,19261
BMRB,19263,peptide derived from the membrane proximal external region of HIV-1 gp41 in DPC,102518,19262
BMRB,19262,Entry for the same peptide in the presence of hexafluoroisoprpanol,102535,19263
PDB,2m8m,Entry for the same peptide in the presence of hexafluoroisoprpanol,102535,19263
PDB,2m8l,,102552,19264
PDB,2m8n,,102552,19264
BMRB,19277,d[GGTTGGCGCGAAGCATTCGCGGGTTGG] duplex-quadruplex hybrid,102760,19276
BMRB,19278,d[GCGCGAAGCATTCGCGGGGAGGTGGGGAAGGG] duplex-quadruplex hybrid,102760,19276
BMRB,19279,d[GGGAAGGGCGCGAAGCATTCGCGAGGTAGG] duplex-quadruplex hybrid,102760,19276
BMRB,19280,d[AGGGTGGGTGCTGGGGCGCGAAGCATTCGCGAGG] duplex-quadruplex hybrid,102760,19276
BMRB,19281,d[TTGGGTGGGCGCGAAGCATTCGCGGGGTGGGT] duplex-quadruplex hybrid,102760,19276
BMRB,19276,d[CGCGAAGCATTCGCG] hairpin,102782,19277
BMRB,19278,d[GCGCGAAGCATTCGCGGGGAGGTGGGGAAGGG] duplex-quadruplex hybrid,102782,19277
BMRB,19279,d[GGGAAGGGCGCGAAGCATTCGCGAGGTAGG] duplex-quadruplex hybrid,102782,19277
BMRB,19280,d[AGGGTGGGTGCTGGGGCGCGAAGCATTCGCGAGG] duplex-quadruplex hybrid,102782,19277
BMRB,19281,d[TTGGGTGGGCGCGAAGCATTCGCGGGGTGGGT] duplex-quadruplex hybrid,102782,19277
BMRB,19276,d[CGCGAAGCATTCGCG] hairpin,102804,19278
BMRB,19277,d[GGTTGGCGCGAAGCATTCGCGGGTTGG] duplex-quadruplex hybrid,102804,19278
BMRB,19279,d[GGGAAGGGCGCGAAGCATTCGCGAGGTAGG] duplex-quadruplex hybrid,102804,19278
BMRB,19280,d[AGGGTGGGTGCTGGGGCGCGAAGCATTCGCGAGG] duplex-quadruplex hybrid,102804,19278
BMRB,19281,d[TTGGGTGGGCGCGAAGCATTCGCGGGGTGGGT] duplex-quadruplex hybrid,102804,19278
BMRB,19276,d[CGCGAAGCATTCGCG] hairpin,102826,19279
BMRB,19277,d[GGTTGGCGCGAAGCATTCGCGGGTTGG] duplex-quadruplex hybrid,102826,19279
BMRB,19278,d[GCGCGAAGCATTCGCGGGGAGGTGGGGAAGGG] duplex-quadruplex hybrid,102826,19279
BMRB,19280,d[AGGGTGGGTGCTGGGGCGCGAAGCATTCGCGAGG] duplex-quadruplex hybrid,102826,19279
BMRB,19281,d[TTGGGTGGGCGCGAAGCATTCGCGGGGTGGGT] duplex-quadruplex hybrid,102826,19279
PDB,2M91,BMRB Entry Tracking System,102826,19279
BMRB,19276,d[CGCGAAGCATTCGCG] hairpin,102848,19280
BMRB,19277,d[GGTTGGCGCGAAGCATTCGCGGGTTGG] duplex-quadruplex hybrid,102848,19280
BMRB,19278,d[GCGCGAAGCATTCGCGGGGAGGTGGGGAAGGG] duplex-quadruplex hybrid,102848,19280
BMRB,19279,d[GGGAAGGGCGCGAAGCATTCGCGAGGTAGG] duplex-quadruplex hybrid,102848,19280
BMRB,19281,d[TTGGGTGGGCGCGAAGCATTCGCGGGGTGGGT] duplex-quadruplex hybrid,102848,19280
PDB,2M92,BMRB Entry Tracking System,102848,19280
BMRB,19276,d[CGCGAAGCATTCGCG] hairpin,102870,19281
BMRB,19277,d[GGTTGGCGCGAAGCATTCGCGGGTTGG] duplex-quadruplex hybrid,102870,19281
BMRB,19278,d[GCGCGAAGCATTCGCGGGGAGGTGGGGAAGGG] duplex-quadruplex hybrid,102870,19281
BMRB,19279,d[GGGAAGGGCGCGAAGCATTCGCGAGGTAGG] duplex-quadruplex hybrid,102870,19281
BMRB,19280,d[AGGGTGGGTGCTGGGGCGCGAAGCATTCGCGAGG] duplex-quadruplex hybrid,102870,19281
PDB,2M93,BMRB Entry Tracking System,102870,19281
BMRB,16912,Delta subunit of RNA polymerase from Bacillus subtilis,102932,19284
PDB,2M4K,,102932,19284
BMRB,16905,Sma0114,102964,19286
PDB,2M98,BMRB Entry Tracking System,102964,19286
PDB,2M9A,BMRB Entry Tracking System,103002,19288
PDB,4bs2,NMR structure of human TDP-43 tandem RRMs in complex with UG-rich RNA,103026,19290
BMRB,19292,Pin1 WW domain mutant 5-1g,103044,19291
BMRB,19295,Pin1 WW domain variant 6-1,103044,19291
BMRB,19296,Pin1 WW domain mutant 6-1g,103044,19291
PDB,2M9E,BMRB Entry Tracking System,103044,19291
BMRB,19291,Pin1 WW domain mutant 5-1,103059,19292
BMRB,19295,Pin1 WW domain variant 6-1,103059,19292
BMRB,19296,Pin1 WW domain mutant 6-1g,103059,19292
PDB,2M9F,BMRB Entry Tracking System,103059,19292
PDB,2m9h,BMRB Entry Tracking System,103092,19294
PDB,19291,Pin1 WW domain mutant 5-1,103107,19295
PDB,19292,Pin1 WW domain mutant 5-1g,103107,19295
PDB,19296,Pin1 WW domain mutant 6-1g,103107,19295
PDB,2M9I,BMRB Entry Tracking System,103107,19295
PDB,19291,Pin1 WW domain mutant 5-1,103123,19296
PDB,19292,Pin1 WW domain mutant 5-1g,103123,19296
PDB,19295,Pin1 WW domain mutant 6-1,103123,19296
PDB,2M9J,BMRB Entry Tracking System,103123,19296
PDB,1K9J,Crystal structure of DC-SIGNR carbohydrate recognition domain in complex with GlcNAc2Man3.,103141,19297
PDB,1SL6,Crystal Structure of a fragment of DC-SIGNR (containg the carbohydrate recognition domain and two repeats of the neck) complexed with Lewis-x.,103141,19297
PDB,1XAR,Crystal Structure of a fragment of DC-SIGNR (containing the carbohydrate recognition domain and two repeats of the neck).,103141,19297
PDB,2m9k,BMRB Entry Tracking System,103159,19298
BMRB,19303,(HhH)2 domain of human FAAP24,103257,19302
BMRB,19302,ERCC4 domain of human FAAP24,103277,19303
BMRB,19306,an inhibitor bound dengue NS3 protease,103314,19305
PDB,2m9q,an inhibitor bound dengue NS3 protease,103314,19305
PDB,2m9p,BMRB Entry Tracking System,103314,19305
BMRB,19305,an inhibitor bound dengue NS3 protease,103334,19306
PDB,2m9p,an inhibitor bound dengue NS3 protease,103334,19306
PDB,2m9q,BMRB Entry Tracking System,103334,19306
BMRB,19308,Biochemical effect of S-67 phosphorylation on UVI31+ from C. reinhardtii,103356,19307
BMRB,19307,Magnesium bound form of UVI31+ from C. reinhardtii,103373,19308
PDB,2M9W,BMRB Entry Tracking System,103429,19312
PDB,2M9X,BMRB Entry Tracking System,103459,19314
TargetDB,HR9151A,,103459,19314
PDB,2MA1,BMRB Entry Tracking System,103511,19317
PDB,4LD3,Complex of this STIL peptide to the CPAP G-box domain,103525,19318
PDB,2MA2,BMRB Entry Tracking System,103542,19319
PDB,4L9M,,103542,19319
BMRB,19316,ETR-3 RRM3 unfolded,103566,19320
NDB,EF017219,,103581,19321
BMRB,16931,Partial list of chemical shifts for Human FKBP12,103617,19323
BMRB,19240,List of chemical shifts for Human FKBP12-major form,103617,19323
BMRB,19241,List of chemical shifts for Human FKBP12-minor form,103617,19323
BMRB,19324,Human FKBP12.6-Minor Form,103617,19323
BMRB,16931,Partial list of chemical shifts for Human FKBP12,103635,19324
BMRB,19240,list of chemical shifts for Human FKBP12-major form,103635,19324
BMRB,19241,list of chemical shifts for Human FKBP12-minor form,103635,19324
BMRB,19323,List of backbone chemical shifts for Human FKBP12.6-major form,103635,19324
PDB,2MA4,BMRB Entry Tracking System,103670,19327
TargetDB,StR106,,103670,19327
PDB,2MA7,BMRB Entry Tracking System,103781,19331
PDB,2MAA,BMRB Entry Tracking System,103845,19334
BMRB,19336,5P12-RANTES-E66S in the presence of dodecylphosphocholine,103860,19335
BMRB,19335,NMR assignments of 5P12-RANTES-E66S,103880,19336
BMRB,19338,aSyn A53T monomer,103895,19337
BMRB,19344,aSyn S87N monomer,103895,19337
BMRB,19345,aSyn A53T&S87N monomer,103895,19337
BMRB,19346,aSyn mouse monomer,103895,19337
BMRB,19347,aSyn mouse_T53A monomer,103895,19337
BMRB,19348,aSyn mouse_N87S monomer,103895,19337
BMRB,19349,aSyn mouse_N87S monomer,103895,19337
BMRB,19350,acetylated aSyn monomer,103895,19337
BMRB,19351,acetylated aSyn A53T monomer,103895,19337
BMRB,19337,aSyn monomer,103910,19338
BMRB,19344,aSyn S87N monomer,103910,19338
BMRB,19345,aSyn A53T&S87N monomer,103910,19338
BMRB,19346,aSyn mouse monomer,103910,19338
BMRB,19347,aSyn mouse_T53A monomer,103910,19338
BMRB,19348,aSyn mouse_N87S monomer,103910,19338
BMRB,19349,aSyn mouse_N87S monomer,103910,19338
BMRB,19350,acetylated aSyn monomer,103910,19338
BMRB,19351,acetylated aSyn A53T monomer,103910,19338
BMRB,19139,Backbone assignments of the R7 domain.,103925,19339
PDB,2X0C,Crystal structure of the R7R8 double domain.,103925,19339
BMRB,19341,Transmembrane-cytosolic part of Trop2 (by chemical sythesis),103959,19342
BMRB,19337,aSyn monomer,103975,19344
BMRB,19338,aSyn A53T monomer,103975,19344
BMRB,19345,aSyn A53T&S87N monomer,103975,19344
BMRB,19346,aSyn mouse monomer,103975,19344
BMRB,19347,aSyn mouse_T53A monomer,103975,19344
BMRB,19348,aSyn mouse_N87S monomer,103975,19344
BMRB,19349,aSyn mouse_N87S monomer,103975,19344
BMRB,19350,acetylated aSyn monomer,103975,19344
BMRB,19351,acetylated aSyn A53T monomer,103975,19344
BMRB,19337,aSyn monomer,103990,19345
BMRB,19338,aSyn A53T monomer,103990,19345
BMRB,19344,aSyn S87N monomer,103990,19345
BMRB,19346,aSyn mouse monomer,103990,19345
BMRB,19347,aSyn mouse_T53A monomer,103990,19345
BMRB,19348,aSyn mouse_N87S monomer,103990,19345
BMRB,19349,aSyn mouse_N87S monomer,103990,19345
BMRB,19350,acetylated aSyn monomer,103990,19345
BMRB,19351,acetylated aSyn A53T monomer,103990,19345
BMRB,19337,aSyn monomer,104005,19346
BMRB,19338,aSyn A53T monomer,104005,19346
BMRB,19344,aSyn S87N monomer,104005,19346
BMRB,19345,aSyn A53T&S97N monomer,104005,19346
BMRB,19347,aSyn mouse_T53A monomer,104005,19346
BMRB,19348,aSyn mouse_N87S monomer,104005,19346
BMRB,19349,aSyn mouse_N87S monomer,104005,19346
BMRB,19350,acetylated aSyn monomer,104005,19346
BMRB,19351,acetylated aSyn A53T monomer,104005,19346
BMRB,19337,aSyn monomer,104020,19347
BMRB,19338,aSyn A53T monomer,104020,19347
BMRB,19344,aSyn S87N monomer,104020,19347
BMRB,19345,aSyn A53T&S97N monomer,104020,19347
BMRB,19346,aSyn mouse monomer,104020,19347
BMRB,19348,aSyn mouse_N87S monomer,104020,19347
BMRB,19349,aSyn mouse_N87S monomer,104020,19347
BMRB,19350,acetylated aSyn monomer,104020,19347
BMRB,19351,acetylated aSyn A53T monomer,104020,19347
BMRB,19337,aSyn monomer,104035,19348
BMRB,19338,aSyn A53T monomer,104035,19348
BMRB,19344,aSyn S87N monomer,104035,19348
BMRB,19345,aSyn A53T&S87N monomer,104035,19348
BMRB,19346,aSyn mouse monomer,104035,19348
BMRB,19347,aSyn mouse_T53A monomer,104035,19348
BMRB,19349,aSyn mouse_T53A&N87S monomer,104035,19348
BMRB,19350,acetylated aSyn monomer,104035,19348
BMRB,19351,acetylated aSyn A53T monomer,104035,19348
BMRB,19337,aSyn monomer,104049,19349
BMRB,19338,aSyn A53T monomer,104049,19349
BMRB,19344,aSyn S87N monomer,104049,19349
BMRB,19345,aSyn A53T&S87N monomer,104049,19349
BMRB,19346,aSyn mouse monomer,104049,19349
BMRB,19347,aSyn mouse_T53A monomer,104049,19349
BMRB,19348,aSyn mouse_N87S monomer,104049,19349
BMRB,19350,acetylated aSyn monomer,104049,19349
BMRB,19351,acetylated aSyn A53T monomer,104049,19349
BMRB,19337,aSyn monomer,104063,19350
BMRB,19338,aSyn A53T monomer,104063,19350
BMRB,19344,aSyn S87N monomer,104063,19350
BMRB,19345,aSyn A53T&S87N monomer,104063,19350
BMRB,19346,aSyn mouse monomer,104063,19350
BMRB,19347,aSyn mouse_T53A monomer,104063,19350
BMRB,19348,aSyn mouse_N87S monomer,104063,19350
BMRB,19349,aSyn mouse_T53A&N87S monomer,104063,19350
BMRB,19351,acetylated aSyn A53T monomer,104063,19350
BMRB,19337,aSyn monomer,104077,19351
BMRB,19338,aSyn A53T monomer,104077,19351
BMRB,19344,aSyn S87N monomer,104077,19351
BMRB,19345,aSyn A53T&S87N monomer,104077,19351
BMRB,19346,aSyn mouse monomer,104077,19351
BMRB,19347,aSyn mouse_T53A monomer,104077,19351
BMRB,19348,aSyn mouse_N87S monomer,104077,19351
BMRB,19349,aSyn mouse_T53A&N87S monomer,104077,19351
BMRB,19350,acetylated aSyn monomer,104077,19351
PDB,4bwh,solution structure of the protein,104149,19356
BMRB,19358,Val66 prodomain region of BDNF,104180,19357
BMRB,19357,Met66 prodomain region of BDNF,104196,19358
BMRB,19363,-CC2 homodimer in complex with two Orai1 C-terminal domains,104238,19362
BMRB,19362,This NMR data was used to calculate the STIM1 CC1-CC2 homodimer in the absence of Orai1 (i.e. the apo state).,104261,19363
PDB,2maj,This PDB represents the STIM1 CC1-CC2 homodimer in the absence of Orai1 (i.e. the apo state).,104261,19363
PDB,1AFH,,104303,19365
PDB,1BV2,,104303,19365
PDB,1BWO,,104303,19365
PDB,1CZ2,,104303,19365
PDB,1GH1,,104303,19365
PDB,1LIP,,104303,19365
PDB,1RZL,,104303,19365
PDB,1SIY,,104303,19365
PDB,1T12,,104303,19365
PDB,1UVA,,104303,19365
PDB,1UVB,,104303,19365
PDB,1UVC,,104303,19365
BMRB,19367,Complex formed by the region 2 of E. coli sigmaE and its cognate -10 non template element TGTCAAA,104322,19366
BMRB,19366,NMR structure of region 2 of E. coli sigmaE,104338,19367
PDB,4bxu,Structure of Pex14 in complex with Pex5 LVxEF motif,104359,19368
BMRB,19370,calbindin D9k calcium bound-form,104377,19369
BMRB,19371,calbindin D9k magnesium bound-form,104377,19369
BMRB,19369,calbindin D9k Apo-form,104395,19370
BMRB,19371,calbindin D9k magnesium bound-form,104395,19370
BMRB,19369,calbindin D9k Apo-form,104413,19371
BMRB,19370,calbindin D9k calcium bound-form,104413,19371
PDB,2MAV,BMRB Entry Tracking System,104467,19375
PDB,4bya,"Calmodulin, C-terminal domain, M144H mutant",104489,19376
BMRB,19386,Parallel-stranded G-quadruplex in DNA poly-G stretches,104569,19381
BMRB,19389,Stacked dimeric G-quadruplex,104569,19381
BMRB,19385,Conotoxin muPIIIA-2,104624,19384
BMRB,19384,conotoxin muPIIIA-1,104645,19385
BMRB,19381,Locked nucleic acid into G-quadruplexes,104666,19386
BMRB,19389,Stacked dimeric G-quadruplex,104666,19386
BMRB,19504,baa38,106864,19505
BMRB,19381,Locked nucleic acid into G-quadruplexes,104736,19389
BMRB,19386,Parallel-stranded G-quadruplex in DNA poly-G stretches,104736,19389
PDB,1R6H,,104849,19395
PDB,1V3A,,104849,19395
PDB,2MBF,BMRB Entry Tracking System,104904,19398
PDB,4BY9,structure of the Box CD enzyme reveals regulation of rRNA methylation,104955,19400
PDB,143D,HUMAN TELOMERE DNA SOLUTION STRUCTURE IN THE PRESENCE OF NA,104977,19402
PDB,1KF1,STRUCTURE AND PACKING OF HUMAN TELOMERIC DNA,104977,19402
PDB,2JSL,HUMAN TELOMERE DNA SOLUTION STRUCTURE IN THE PRESENCE OF K CATIONS NATURAL FORM 2,104977,19402
PDB,2JSM,HUMAN TELOMERE DNA SOLUTION STRUCTURE IN THE PRESENCE OF K CATIONS NATURAL FORM 1,104977,19402
PDB,2KF8,STRUCTURE OF A TWO-G-TETRAD BASKET-TYPE INTRAMOLECULAR G-QUADRUPLEX FORMED BY HUMAN TELOMERIC REPEATS IN K+ SOLUTION,104977,19402
PDB,2MBL,"BMRB Entry Tracking System, CNS Refined",105017,19404
PDB,2MBM,"OR33_ros, structure, restraint Rosetta Refined",105017,19404
BMRB,19412,"K11-linked Diubiquitin average solution structure at pH 6.8, 150 mM NaCl",105052,19406
BMRB,19408,Trimeric Skp with bound OmpX,105068,19407
BMRB,19409,Trimeric Skp with bound tOmpA,105068,19407
BMRB,19410,tOmpA within the trimeric chaperone Skp,105068,19407
BMRB,19411,OmpX within the trimeric chaperone Skp,105068,19407
BMRB,19407,Trimeric Skp,105083,19408
BMRB,19409,Trimeric Skp with bound tOmpA,105083,19408
BMRB,19410,tOmpA within the trimeric chaperone Skp,105083,19408
BMRB,19411,OmpX within the trimeric chaperone Skp,105083,19408
BMRB,19407,Corresponding chemical shifts of Skp when bound to its substrate OmpX,105099,19409
BMRB,19408,Corresponding chemical shifts of apo-SKP,105099,19409
BMRB,19410,tOmpA within the trimeric chaperone Skp,105099,19409
BMRB,19411,OmpX within the trimeric chaperone Skp,105099,19409
BMRB,19407,Corresponding chemical shifts of Skp when bound to its substrate OmpX,105115,19410
BMRB,19408,Corresponding chemical shifts of apo-SKP,105115,19410
BMRB,19409,Trimeric Skp bound with bound tOmpA,105115,19410
BMRB,19411,OmpX within the trimeric chaperone Skp,105115,19410
BMRB,19407,Corresponding chemical shifts of Skp when bound to its substrate OmpX,105131,19411
BMRB,19408,Corresponding chemical shifts of apo-SKP,105131,19411
BMRB,19409,Trimeric Skp with bound tOmpA,105131,19411
BMRB,19410,tOmpA within the trimeric chaperone Skp,105131,19411
BMRB,19406,K11-linked Ub2 average solution structure in the absence of NaCl,105147,19412
BMRB,19414,PaDsbA complex form,105165,19413
BMRB,19417,PaDsbA apo form,105165,19413
BMRB,19413,KpDsbA,105183,19414
BMRB,19417,PaDsbA apo form,105183,19414
PDB,3H93,crystal structure of PaDsbA,105183,19414
PDB,1RUT,LMO4 LIM1+LIM2 in complex with LDB1,105203,19415
PDB,2L4Z,LMO4 LIM1 in complex with CtIP,105203,19415
PDB,4M5D,Crystal Structure of Rrp7 N-terminal Domain,105221,19416
BMRB,19413,KpDsbA,105239,19417
BMRB,19414,PaDsbA in complex form,105239,19417
PDB,2MBT,solution structure of PaDsbA,105239,19417
PDB,3H93,crystal structure of PaDsbA,105239,19417
BMRB,19422,Nosiheptide in Complex with TipAS,105293,19421
PDB,1NY9,,105293,19421
PDB,2mbz,BMRB Entry Tracking System,105293,19421
BMRB,19421,chemical shifts of TipAS in complex with the antibiotic promothiocin A,105328,19422
PDB,1NY9,apo TipAS,105328,19422
PDB,2mbz,TipAS in complex with the antibiotic promothiocin A,105328,19422
PDB,3IM5,RyR2A crystal structure,105384,19424
PDB,3QR5,delta exon 3 RyR2A crystal structure,105384,19424
PDB,4KEI,P164S RyR2A crystal structure,105384,19424
PDB,4KEJ,R169Q RyR2A crystal structure,105384,19424
PDB,4KEK,R176Q RyR2A crystal structure,105384,19424
BMRB,19424,delta exon 3 RyR2A backbone chemical shift assignments,105399,19425
PDB,3IM5,RyR2A crystal structure,105399,19425
PDB,3QR5,delta exon 3 RyR2A crystal structure,105399,19425
PDB,4KEI,P164S RyR2A crystal structure,105399,19425
PDB,4KEJ,R169Q RyR2A crystal structure,105399,19425
PDB,4KEK,R176Q RyR2A crystal structure,105399,19425
BMRB,5236,Entry containing 1H and 15N shifts of an elongated sequence solved at different pH,105417,19426
BMRB,19429,A bacteriophage transcription regulator complex with p7 peptide,105453,19428
BMRB,19428,A bacteriophage transcription regulator,105468,19429
PDB,4HYZ,Crystal structure of the protein at 2.25 A resolution,105502,19431
PDB,2MCA,BMRB Entry Tracking System,105541,19433
PDB,2mcd,BMRB Entry Tracking System,105579,19436
PDB,2mch,murine norovirus NS1/2 CW3 WT,105579,19436
BMRB,19439,murine norovirus NS1/2 CW3 WT,105579,19436
PDB,2mck,murine norovirus CR6 NS1/2 protein,105579,19436
BMRB,19444,murine norovirus CR6 NS1/2 protein,105579,19436
BMRB,19436,murine norovirus NS1/2 D94E mutant,105634,19439
BMRB,19444,murine norovirus CR6 NS1/2 protein,105634,19439
PDB,2mcd,murine norovirus NS1/2 D94E mutant,105634,19439
PDB,2mch,BMRB Entry Tracking System,105634,19439
PDB,2mck,murine norovirus CR6 NS1/2 protein,105634,19439
BMRB,19441,spermine modified DNA duplex,105657,19440
PDB,2MCI,BMRB Entry Tracking System,105657,19440
PDB,2MCJ,spermine modified DNA duplex,105657,19440
PDB,2mcj,BMRB Entry Tracking System,105677,19441
BMRB,19436,murine norovirus NS1/2 D94E mutant,105734,19444
BMRB,19439,murine norovirus NS1/2 CW3 WT,105734,19444
PDB,2mcd,murine norovirus NS1/2 D94E mutant,105734,19444
PDB,2mch,murine norovirus NS1/2 CW3 WT,105734,19444
PDB,2mck,BMRB Entry Tracking System,105734,19444
PDB,2MCN,BMRB Entry Tracking System,105772,19447
BMRB,19435,Opposite enantiomer bound to other end of same quadruplex,105797,19448
PDB,2mcc,Opposite enantiomer bound to other end of same quadruplex,105797,19448
BMRB,19460,ShK-like immunomodulatory peptide from Ancylostoma caninum,105834,19450
PDB,1ROO,,105834,19450
PDB,2K72,,105834,19450
BMRB,19455,piscidin 1 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105907,19454
BMRB,19456,piscidin 3 in aligned 3:1 phosphatidylcholine/phosphoglycerol lipid bilayers,105907,19454
BMRB,19457,piscidin 3 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105907,19454
PDB,2JOS,Piscidin 1 in DPC micelles,105907,19454
PDB,2OJM,Piscidin 1 in SDS micelles,105907,19454
BMRB,19454,piscidin 1 in aligned 3:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105940,19455
BMRB,19456,piscidin 3 in aligned 3:1 phosphatidylcholine/phosphoglycerol lipid bilayers,105940,19455
BMRB,19457,piscidin 3 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105940,19455
PDB,2JOS,Piscidin 1 in DPC micelles,105940,19455
PDB,2OJM,Piscidin 1 in SDS micelles,105940,19455
BMRB,19454,piscidin 1 in aligned 3:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105970,19456
BMRB,19455,piscidin 1 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105970,19456
BMRB,19457,piscidin 3 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105970,19456
PDB,2JOS,Piscidin 1 in DPC micelles,105970,19456
PDB,2OJM,Piscidin 1 in SDS micelles,105970,19456
BMRB,19454,piscidin 1 in aligned 3:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105998,19457
BMRB,19455,piscidin 1 in aligned 1:1 phosphatidylethanolamine/phosphoglycerol lipid bilayers,105998,19457
BMRB,19456,piscidin 3 in aligned 3:1 phosphatidylcholine/phosphoglycerol lipid bilayers,105998,19457
PDB,2JOS,Piscidin 1 in DPC micelles,105998,19457
PDB,2OJM,Piscidin 1 in SDS micelles,105998,19457
BMRB,19459,"Recombinant CR1 fragment, domains 1-2",106027,19458
BMRB,19458,"Recombinant CR1 fragment, domains 2-3",106047,19459
BMRB,19450,ShK-like immunomodulatory peptide from Brugia malayi,106067,19460
BMRB,19462,HlyII-C minor trans form,106087,19461
BMRB,19463,HlyII-C mutant p87m,106087,19461
BMRB,19461,HlyII-C major trans form,106107,19462
BMRB,19463,HlyII-C mutant p87m,106107,19462
BMRB,19461,HlyII-C major trans form,106127,19463
BMRB,19462,HlyII-C minor trans form,106127,19463
BMRB,19467,PKCalpha C-term,106173,19466
BMRB,19466,PICK1 PDZ ASIC1a C-term,106192,19467
BMRB,19469,WK10_LPS,106208,19468
BMRB,19470,KR8_LPS,106208,19468
BMRB,19471,WG12_LPS,106208,19468
PDB,2MD1,BMRB Entry Tracking System,106208,19468
BMRB,19468,WR17_LPS,106223,19469
BMRB,19470,KR8_LPS,106223,19469
BMRB,19471,WG12_LPS,106223,19469
BMRB,19468,WR17_LPS,106238,19470
BMRB,19469,WK10_LPS,106238,19470
BMRB,19471,WG12_LPS,106238,19470
PDB,2MD3,BMRB Entry Tracking System,106238,19470
BMRB,19468,WR17_LPS,106253,19471
BMRB,19469,WK10_LPS,106253,19471
BMRB,19470,KR8_LPS,106253,19471
PDB,2MD4,BMRB Entry Tracking System,106253,19471
BMRB,19473,Sp140 PHD finger cis conformer,106268,19472
PDB,2MD7,BMRB Entry Tracking System,106268,19472
BMRB,19472,Sp140 PHD finger trans conformer,106291,19473
PDB,2MD8,BMRB Entry Tracking System,106291,19473
PDB,2LF7,,106314,19474
PDB,2LF8,,106314,19474
PDB,1DNY,"Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide snthetases",106379,19479
PDB,2GDW,Solution structure of the B. brevis TycC3-PCP in A/H-state,106379,19479
PDB,2GDX,Solution structure of the B. brevis TycC3-PCP in H-state,106379,19479
PDB,2GDY,Solution structure of the B. brevis TycC3-PCP in A-state,106379,19479
PDB,2GE1,Protein complex of A-state TycC3-apo-PCP with the PPtase Sfp (model),106379,19479
BMRB,19481,Ser40 phosphorylated RDTH,106398,19480
BMRB,19480,RDTH dimer,106415,19481
BMRB,19487,PP2WW mutant (KPP2WW) of HYPB,106460,19483
PDB,2MDG,BMRB Entry Tracking System,106513,19486
BMRB,19483,WW domain of HYPB,106540,19487
PDB,2MDJ,BMRB Entry Tracking System,106559,19488
BMRB,4909,"Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectin-3 with lactose bound",106609,19491
PDB,3ZSJ,High resolution X-ray structure (0.86 A) of Gal-3 CRD domain in complex with lactose,106609,19491
PDB,3ZSL,High resolution X-ray structure (1.08 A) of apo Gal-3 CRD domain at cryogenic temperature,106609,19491
PDB,3ZSM,High resolution X-ray structure (1.23 A) of apo Gal-3 CRD domain at room temperature,106609,19491
PDB,2KGU,,106632,19493
PDB,2MDN,BMRB Entry Tracking System,106632,19493
BMRB,19499,HuR RRM3 W261E mutant,106651,19494
BMRB,19500,HuR RRM3 S318D mutant,106651,19494
BMRB,19496,FLNa3-5,106668,19495
BMRB,19495,FLNc4-5,106683,19496
BMRB,19494,HuR RRM3 WT,106737,19499
BMRB,19500,HuR RRM3 S318D mutant,106737,19499
BMRB,19494,HuR RRM3 WT,106767,19500
BMRB,19499,HuR RRM3 W261E mutant,106767,19500
BMRB,19504,baa38,106831,19503
BMRB,19505,WW Domain Strand-Swapped Dimer,106831,19503
PDB,1pin,,106831,19503
PDB,2kcf,,106831,19503
BMRB,19503,WW Domain with Loop 1 Excised,106847,19504
BMRB,19505,WW Domain Strand-Swapped Dimer,106847,19504
BMRB,19503,WW Domain with Loop 1 Excised,106864,19505
PDB,2mdv,,106864,19505
BMRB,15366,"1H, 15N, and 13C chemical shifts of the C-terminal domain of human eRF1",106881,19506
BMRB,18092,"1H, 15N, and 13C chemical shifts of the N-terminal domain of human eRF1",106881,19506
BMRB,6763,"1H, 15N, and 13C chemical shifts of the middle (M) domain of human eRF1",106881,19506
PDB,2KCJ,,106912,19508
PDB,3RCP,,106912,19508
PDB,2MDX,Chemical shifts checked and updated,106912,19508
BMRB,15605,MPER,106966,19512
BMRB,19513,MPER-Con089,106966,19512
BMRB,19514,MPER-Du151,106966,19512
BMRB,19515,MPER-PB7,106966,19512
PDB,2PV6,,106966,19512
BMRB,15605,MPER,106990,19513
BMRB,19512,MPER-HxB2-AA,106990,19513
BMRB,19514,MPER-Du151,106990,19513
BMRB,19515,MPER-PB7,106990,19513
BMRB,15605,MPER,107014,19514
BMRB,19512,MPER-HxB2-AA,107014,19514
BMRB,19513,MPER-Con089,107014,19514
BMRB,19515,MPER-PB7,107014,19514
BMRB,15605,MPER,107038,19515
BMRB,19512,MPER-HxB2-AA,107038,19515
BMRB,19513,MPER-Con089,107038,19515
BMRB,19514,MPER-Du151,107038,19515
PDB,2LM0,Solution NMR structure of the AF4-AF9 complex,107062,19516
PDB,2me5,BMRB Entry Tracking System,107062,19516
BMRB,19524,GS-TAMAPIN MUTATION R7A,107126,19519
BMRB,19527,GS-TAMAPIN MUTATION R13A,107126,19519
BMRB,19528,DOUBLE GS-TAMAPIN MUTATION R6A R7A,107126,19519
PDB,2ky3,GS-Tamapin,107126,19519
PDB,2lu9,r-Tamapin,107126,19519
BMRB,19521,BCL-xL containing the alpha1-alpha2 disordered loop,107141,19520
BMRB,19522,BCL-xL and the p53 Core Domain,107141,19520
BMRB,19520,BCL-xL in its p53-bound conformation,107159,19521
BMRB,19522,BCL-xL and the p53 Core Domain,107159,19521
BMRB,19520,BCL-xL in its p53-bound conformation,107177,19522
BMRB,19521,BCL-xL containing the alpha1-alpha2 disordered loop,107177,19522
PDB,2mek,BMRB Entry Tracking System,107206,19523
BMRB,19519,GS-TAMAPIN MUTATION R6A,107225,19524
BMRB,19527,GS-TAMAPIN MUTATION R13A,107225,19524
BMRB,19528,DOUBLE GS-TAMAPIN MUTATION R6A R7A,107225,19524
PDB,4C7Q,Solution structure of the Nt. GR-RBP1 RRM domain,107242,19525
PDB,1OI1,MBT domains of Scml2,107260,19526
PDB,2BIV,MBT domains of Scml2,107260,19526
PDB,2VYT,MBT domains of Scml2,107260,19526
PDB,4EDU,MBT domains of Scml2,107260,19526
BMRB,19519,GS-TAMAPIN MUTATION R6A,107279,19527
BMRB,19524,GS-TAMAPIN MUTATION R7A,107279,19527
BMRB,19528,DOUBLE GS-TAMAPIN MUTATION R6A R7A,107279,19527
PDB,19519,GS-TAMAPIN MUTATION R6A,107296,19528
PDB,19524,GS-TAMAPIN MUTATION R7A,107296,19528
PDB,19527,GS-TAMAPIN MUTATION R13A,107296,19528
PDB,2MH9,Resonance assignment of RQC domain of human Bloom syndrome protein,107313,19530
PDB,2MF0,"BMRB Entry Tracking System, conformer L",107377,19534
PDB,2MF1,"structure of the same system, conformer R",107377,19534
ArachnoServer,AS000116,,107404,19535
InterPro,IPR012633,,107404,19535
NCBI_Taxon,31925,,107404,19535
Pfam,PF08115,,107404,19535
UniProt,P61095,,107404,19535
BMRB,19539,NMR assignments of streptomyces virginiae VirA acp5b,107423,19536
PDB,2mf4,BMRB Entry Tracking System,107423,19536
PDB,2CIU,Crystal structure of the same protein.,107440,19538
PDB,2mf7,BMRB Entry Tracking System,107440,19538
PDB,4ca3,,107458,19539
PDB,4ca9,BMRB Entry Tracking System,107495,19541
PDB,2mfa,BMRB Entry Tracking System,107526,19542
BMRB,19546,RsmZ(SL2)/RsmE(dimer) 2:1 complex,107546,19544
BMRB,19547,RsmZ(SL3)/RsmE(dimer) 2:1 complex,107546,19544
BMRB,19548,RsmZ(SL4)/RsmE(dimer) 2:1 complex,107546,19544
BMRB,19549,RsmZ(36-44)/RsmE(dimer) 2:1 complex,107546,19544
PDB,2MFC,BMRB Entry Tracking System,107546,19544
PDB,2mfd,BMRB Entry Tracking System,107575,19545
BMRB,19544,RsmZ(SL1)/RsmE(dimer) 2:1 complex,107596,19546
BMRB,19547,RsmZ(SL3)/RsmE(dimer) 2:1 complex,107596,19546
BMRB,19548,RsmZ(SL4)/RsmE(dimer) 2:1 complex,107596,19546
BMRB,19549,RsmZ(36-44)/RsmE(dimer) 2:1 complex,107596,19546
PDB,2MFE,BMRB Entry Tracking System,107596,19546
BMRB,19544,RsmZ(SL1)/RsmE(dimer) 2:1 complex,107625,19547
BMRB,19546,RsmZ(SL2)/RsmE(dimer) 2:1 complex,107625,19547
BMRB,19548,RsmZ(SL4)/RsmE(dimer) 2:1 complex,107625,19547
BMRB,19549,RsmZ(36-44)/RsmE(dimer) 2:1 complex,107625,19547
PDB,2MFF,BMRB Entry Tracking System,107625,19547
BMRB,19544,RsmZ(SL1)/RsmE(dimer) 2:1 complex,107654,19548
BMRB,19546,RsmZ(SL2)/RsmE(dimer) 2:1 complex,107654,19548
BMRB,19547,RsmZ(SL3)/RsmE(dimer) 2:1 complex,107654,19548
BMRB,19549,RsmZ(36-44)/RsmE(dimer) 2:1 complex,107654,19548
PDB,2MFG,BMRB Entry Tracking System,107654,19548
BMRB,19544,RsmZ(SL1)/RsmE(dimer) 2:1 complex,107683,19549
BMRB,19546,RsmZ(SL2)/RsmE(dimer) 2:1 complex,107683,19549
BMRB,19547,RsmZ(SL3)/RsmE(dimer) 2:1 complex,107683,19549
BMRB,19548,RsmZ(SL4)/RsmE(dimer) 2:1 complex,107683,19549
PDB,2MFH,BMRB Entry Tracking System,107683,19549
BMRB,19554,Domain 2 of E. coli ribosomal protein S1,107710,19550
PDB,2KHI,NMR structure of the domain 4 of the E. coli ribosomal protein S1,107710,19550
PDB,2KHJ,NMR structure of the domain 6 of the E. coli ribosomal protein S1,107710,19550
BMRB,19553,Blo 1 12 CBD domain,107753,19552
PDB,2mfj,BMRB Entry Tracking System,107753,19552
BMRB,19552,"Blo t 19, a minor dust mite allergen from Blomia tropicalis",107778,19553
PDB,2mfk,BMRB Entry Tracking System,107778,19553
BMRB,19550,Domain 1 of E. coli ribosomal protein S1,107799,19554
PDB,2KHI,NMR structure of the domain 4 of the E. coli ribosomal protein S1,107799,19554
PDB,2KHJ,NMR structure of the domain 6 of the E. coli ribosomal protein S1,107799,19554
BMRB,19556,C-terminally encoded peptide of the model plant host Medicago truncatula - CEP1,107823,19555
PDB,2mfm,BMRB Entry Tracking System,107823,19555
BMRB,19555,C-terminally encoded peptide of the plant parasitic nematode Meloidogyne hapla - CEP11,107841,19556
PDB,2mfo,BMRB Entry Tracking System,107841,19556
PDB,2L61,NMR solution structure of Cd-form of the linear analog g-Ec-1 domain,107859,19557
PDB,2L62,NMR solution structure of Zn-form of the linear analog g-Ec-1 domain,107859,19557
PDB,2MFP,BMRB Entry Tracking System,107859,19557
PDB,2MFQ,BMRB Entry Tracking System,107961,19562
BMRB,19564,DHFR bound to THF,107992,19563
BMRB,19565,DHFR bound to NADP+ and THF,107992,19563
BMRB,19566,DHFR bound to NADPH,107992,19563
BMRB,19567,DHFR bound to NADP+ and folate,107992,19563
BMRB,19563,DHFR bound to folate,108011,19564
BMRB,19565,DHFR bound to NADP+ and THF,108011,19564
BMRB,19566,DHFR bound to NADPH,108011,19564
BMRB,19567,DHFR bound to NADP+ and folate,108011,19564
BMRB,19563,DHFR bound to folate,108032,19565
BMRB,19564,DHFR bound to THF,108032,19565
BMRB,19566,DHFR bound to NADPH,108032,19565
BMRB,19567,DHFR bound to NADP+ and folate,108032,19565
PDB,4M6L,"crystal structure of human dihdyrofolate reductase (DHFR) bound to NADP+ and 5,10-dideazatetrahydrofolic acid",108032,19565
BMRB,19563,DHFR bound to folate,108055,19566
BMRB,19564,DHFR bound to THF,108055,19566
BMRB,19565,DHFR bound to NADP+ and THF,108055,19566
BMRB,19567,DHFR bound to NADP+ and folate,108055,19566
PDB,4M6J,Crystal structure of human dihydrofolate reductase (DHFR) bound to NADPH,108055,19566
BMRB,19563,DHFR bound to folate,108076,19567
BMRB,19564,DHFR bound to THF,108076,19567
BMRB,19565,DHFR bound to NADP+ and THF,108076,19567
BMRB,19566,DHFR bound to NADPH,108076,19567
PDB,4M6K,Crystal structure of human dihydrofolate reductase (DHFR) bound to NADP+ and folate,108076,19567
PDB,2MFR,BMRB Entry Tracking System,108099,19568
PDB,2MFS,BMRB Entry Tracking System,108135,19570
BMRB,19572,quadruplex d(TGGGTTTGGGTTGGGTTTGGG) in sodium conditions,108154,19571
PDB,2MFT,BMRB Tracking System,108154,19571
BMRB,19571,d(GGGTTTTGGGTGGGTTTTGGG) quadruplex in sodium conditions,108175,19572
PDB,2MFU,quadruplex d(TGGGTTTGGGTTGGGTTTGGG) in sodium conditions,108175,19572
PDB,2MFU,BMRB Tracking System,108175,19572
PDB,2mfv,BMRB Entry Tracking System,108195,19573
PDB,2mfx,BMRB Entry Tracking System,108249,19577
PDB,2MFY,BMRB Entry Tracking System,108268,19578
PDB,2mfz,BMRB Entry Tracking System,108287,19579
PDB,2mg0,BMRB Entry Tracking System,108308,19580
PDB,2mg1,BMRB Entry Tracking System,108326,19581
BMRB,19583,peptide derived from the membrane proximal external region of HIV-1 gp41 in the presence of dodecylphosphocholine micelles,108343,19582
PDB,2MG2,BMRB Entry Tracking System,108343,19582
BMRB,19582,peptide derived from the membrane proximal external region of HIV-1 gp41 in the presence of hexafluoroisopropanol,108361,19583
PDB,2MG3,BMRB Entry Tracking System,108361,19583
PDB,2mg4,BMRB Entry Tracking System,108395,19585
PDB,2MG5,BMRB Entry Tracking System,108410,19586
PDB,2MG6,BMRB Entry Tracking System,108426,19587
BMRB,19591,FF domain L24A mutant,108463,19590
BMRB,19590,Fyn_SH3_G48A,108478,19591
PDB,2mg8,BMRB Entry Tracking System,108493,19592
PDB,2MG9,BMRB Entry Tracking System,108512,19593
PDB,2MGN,BMRB Entry Tracking System,108534,19594
PDB,2MGO,BMRB Entry Tracking System,108557,19595
BMRB,19603,ctr in DPC,108592,19597
BMRB,19599,hman EPRS R12 repeats,108607,19598
BMRB,19598,WHEP repeats,108621,19599
PDB,2MGQ,BMRB Entry Tracking System,108648,19600
PDB,2mgt,BMRB Entry Tracking System,108681,19602
BMRB,19597,ctr in SDS,108713,19603
PDB,2MGU,BMRB Entry Tracking System,108728,19604
PDB,2MGV,BMRB Entry Tracking System,108748,19605
PDB,2mgw,BMRB Entry Tracking System,108770,19606
PDB,2mgx,BMRB Entry Tracking System,108790,19607
PDB,2mgy,BMRB Entry Tracking System,108807,19608
BMRB,11541,Protein-RNA Complex,108834,19609
PDB,2mh0,BMRB Entry Tracking System,108853,19610
PDB,2mh1,BMRB Entry Tracking System,108875,19611
PDB,2MH2,BMRB Entry Tracking System,108895,19613
PDB,2mh3,BMRB Entry Tracking System,108915,19614
BMRB,19616,Dimethylarginine Dimethylaminohydrolase,108935,19615
BMRB,19615,PaDDAH_TM,108955,19616
PDB,2MH4,BMRB Entry Tracking System,108970,19617
PDB,2MH5,BMRB Entry Tracking System,109002,19619
PDB,2MH6,BMRB Entry Tracking System,109028,19620
PDB,2mh7,BMRB Entry Tracking System,109072,19622
PDB,2mh8,BMRB Entry Tracking System,109093,19623
PDB,2MHC,BMRB Entry Tracking System,109130,19625
PDB,2MHD,BMRB Entry Tracking System,109165,19627
PDB,2MHE,BMRB Entry Tracking System,109184,19628
PDB,2MHG,BMRB Entry Tracking System,109220,19632
PDB,2MHH,BMRB Entry Tracking System,109239,19633
BMRB,21047,AIP-IV,118717,21046
PDB,2MHI,BMRB Entry Tracking System,109258,19634
PDB,2MHJ,BMRB Entry Tracking System,109287,19635
PDB,2MHL,BMRB Entry Tracking System,109305,19637
PDB,2MHM,BMRB Entry Tracking System,109321,19638
BMRB,19671,"3rC34Y, variant of Imunoglobulin light-chain of lambda 3",109339,19641
PDB,2MHN,BMRB Entry Tracking System,109355,19642
PDB,2MHO,BMRB Entry Tracking System,109372,19643
BMRB,19645,CD79b cytosolic domain denatured,109393,19644
BMRB,19648,CD79b cytosolic domain,109393,19644
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109393,19644
BMRB,19650,CD79a cytosolic domain phosphorylated,109393,19644
BMRB,19651,CD79a cytosolic domain (denatured),109393,19644
BMRB,19644,CD79a cytosolic domain (native),109414,19645
BMRB,19648,CD79a cytosolic domain phosphorylated,109414,19645
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109414,19645
BMRB,19650,CD79b cytosolic domain,109414,19645
BMRB,19651,CD79b cytosolic domain denatured,109414,19645
BMRB,19655,CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109414,19645
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109414,19645
PDB,2MHP,BMRB Entry Tracking System,109435,19646
BMRB,19644,CD79a cytosolic domain (native),109462,19648
BMRB,19645,CD79b cytosolic domain denatured,109462,19648
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109462,19648
BMRB,19650,CD79b cytosolic domain,109462,19648
BMRB,19651,CD79a cytosolic domain (denatured),109462,19648
BMRB,19655,CCD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109462,19648
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109462,19648
BMRB,19644,CD79a cytosolic domain (native),109481,19649
BMRB,19645,CD79b cytosolic domain denatured,109481,19649
BMRB,19648,CD79a cytosolic domain phosphorylated,109481,19649
BMRB,19650,CD79b cytosolic domain,109481,19649
BMRB,19651,CD79a cytosolic domain (denatured),109481,19649
BMRB,19655,CCD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109481,19649
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109481,19649
BMRB,19644,CD79a cytosolic domain (native),109500,19650
BMRB,19645,CD79b cytosolic domain denatured,109500,19650
BMRB,19648,CD79b cytosolic domain phosphorylated,109500,19650
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109500,19650
BMRB,19651,CD79a cytosolic domain (denatured),109500,19650
BMRB,19655,CCD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109500,19650
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109500,19650
BMRB,19644,CD79a cytosolic domain (native),109519,19651
BMRB,19645,CD79b cytosolic domain denatured,109519,19651
BMRB,19648,CD79b cytosolic domain phosphorylated,109519,19651
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109519,19651
BMRB,19650,CD79b cytosolic domain,109519,19651
BMRB,19655,CCD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109519,19651
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109519,19651
BMRB,18845,SUP-12,109538,19653
BMRB,18846,SUP-12 + GGUGUGC,109538,19653
PDB,4ch1,PDBe structure entry,109538,19653
PDB,2MHS,BMRB Entry Tracking System,109561,19654
BMRB,19644,CD79a cytosolic domain (native),109585,19655
BMRB,19645,CD79b cytosolic domain denatured,109585,19655
BMRB,19648,CD79b cytosolic domain phosphorylated,109585,19655
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109585,19655
BMRB,19650,CD79b cytosolic domain,109585,19655
BMRB,19651,CD79a cytosolic domain (denatured),109585,19655
BMRB,19656,"CD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207, denatured state)",109585,19655
BMRB,19644,CD79a cytosolic domain (native),109604,19656
BMRB,19645,CD79b cytosolic domain denatured,109604,19656
BMRB,19648,CD79b cytosolic domain phosphorylated,109604,19656
BMRB,19649,CD79a cytosolic domain phosphorylated (denatured),109604,19656
BMRB,19650,CD79b cytosolic domain,109604,19656
BMRB,19651,CD79a cytosolic domain (denatured),109604,19656
BMRB,19655,CCD79b cytosolic domain phosphorylated (on the two ITAM tyrosines Tyr196 and Tyr207),109604,19656
PDB,2MHV,BMRB Entry Tracking System,109623,19657
PDB,2MHW,BMRB Entry Tracking System,109640,19658
BMRB,19661,SHB modified duplex,109656,19659
PDB,2mhx,BMRB Entry Tracking System,109656,19659
PDB,2MHY,BMRB Entry Tracking System,109682,19660
BMRB,19659,RHB modified duplex,109700,19661
PDB,2mhz,BMRB Entry Tracking System,109700,19661
PDB,2MI0,BMRB Entry Tracking System,109725,19662
PDB,2MI1,BMRB Entry Tracking System,109757,19663
BMRB,19665,VcDsbA-benzimidazole complex,109772,19664
PDB,2MI3,BMRB Entry Tracking System,109772,19664
PDB,2MI5,BMRB Entry Tracking System,109792,19666
PDB,2MI6,BMRB Entry Tracking System,109813,19667
BMRB,18703,Chemical shift assignments of 2-mercaptophenol-a3C,109828,19668
BMRB,5356,Chemical shift assignments for a3W,109828,19668
PDB,1LQ7,Solution NMR structure of a3W,109828,19668
PDB,2LXY,Solution NMR structure of 2-mercaptophenol-a3C,109828,19668
PDB,2mi7,BMRB Entry Tracking System,109828,19668
PDB,2MI8,BMRB Entry Tracking System,109872,19670
BMRB,19641,"3rCWP7D, variant of Imunoglobulin light-chain of lambda 3",109888,19671
BMRB,19741,p75 transmembrane domain C257A mutant,109921,19673
PDB,2MIC,BMRB Entry Tracking System,109921,19673
PDB,2MJO,p75 transmembrane domain C257A mutant,109921,19673
BMRB,19675,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109939,19674
BMRB,19677,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109939,19674
BMRB,19678,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109939,19674
BMRB,19679,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109939,19674
NCBI,AT1G69320,CLAVATA encoded peptide of Arabidopsis thaliana,109939,19674
PDB,2MID,BMRB Entry Tracking System,109939,19674
PDB,2MIE,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109939,19674
PDB,2MIF,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109939,19674
PDB,2MIG,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109939,19674
PDB,2MIH,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109939,19674
BMRB,19674,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109955,19675
BMRB,19677,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109955,19675
BMRB,19678,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109955,19675
BMRB,19679,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109955,19675
NCBI,AT4G13195,CLAVATA encoded peptide of Arabidopsis thaliana,109955,19675
PDB,2MID,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109955,19675
PDB,2MIE,BMRB Entry Tracking System,109955,19675
PDB,2MIF,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109955,19675
PDB,2MIG,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109955,19675
PDB,2MIH,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109955,19675
BMRB,19674,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109971,19677
BMRB,19675,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109971,19677
BMRB,19678,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109971,19677
BMRB,19679,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109971,19677
PDB,2MID,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109971,19677
PDB,2MIE,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109971,19677
PDB,2MIF,BMRB Entry Tracking System,109971,19677
PDB,2MIG,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,109971,19677
PDB,2MIH,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109971,19677
BMRB,19674,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109987,19678
BMRB,19675,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109987,19678
BMRB,19677,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109987,19678
BMRB,19679,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109987,19678
PDB,2MID,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,109987,19678
PDB,2MIE,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,109987,19678
PDB,2MIF,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,109987,19678
PDB,2MIG,BMRB Entry Tracking System,109987,19678
PDB,2MIH,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE6/7,109987,19678
BMRB,19674,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,110003,19679
BMRB,19675,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,110003,19679
BMRB,19677,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,110003,19679
BMRB,19678,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,110003,19679
PDB,2MID,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10,110003,19679
PDB,2MIE,CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE44,110003,19679
PDB,2MIF,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE4,110003,19679
PDB,2MIH,CLAVATA-like encoded peptide of Meloidogyne hapla - MhCLE5,110003,19679
PDB,2MIH,BMRB Entry Tracking System,110003,19679
PDB,2MII,BMRB Entry Tracking System,110051,19681
PDB,2MIQ,BMRB Entry Tracking System,110073,19682
PDB,2MIJ,BMRB Entry Tracking System,110102,19683
PDB,2MIO,BMRB Entry Tracking System,110123,19684
PDB,2mik,BMRB Entry Tracking System,110150,19685
BMRB,19680,ASD-1,110169,19686
PDB,2MIM,BMRB Entry Tracking System,110186,19687
BMRB,17292,A730 loop of the Neurospora VS ribozyme,110235,19692
PDB,2L5Z,,110235,19692
PDB,2MIS,BMRB Entry Tracking System,110235,19692
BMRB,18705,Antimicrobial Peptide Human Defensin 5,110261,19693
PDB,1ZMP,,110261,19693
PDB,2LXZ,,110261,19693
PDB,2mit,BMRB Entry Tracking System,110261,19693
PDB,2MIU,BMRB Entry Tracking System,110281,19694
BMRB,19696,"N2-guanine adducts derived from the tumorigen dibenzo[a,l]pyrene in DNA (2)",110302,19695
PDB,2miv,BMRB Entry Tracking System,110302,19695
BMRB,19695,"N2-guanine adducts derived from the tumorigen dibenzo[a,l]pyrene in DNA (1)",110322,19696
PDB,2miw,BMRB Entry Tracking System,110322,19696
PDB,2MIX,BMRB Entry Tracking System,110342,19697
PDB,2MIY,BMRB Entry Tracking System,110360,19698
PDB,2MIZ,BMRB Entry Tracking System,110391,19699
PDB,2MJ0,BMRB Entry Tracking System,110417,19700
PDB,1lfm,,110432,19701
PDB,2MJ1,BMRB Entry Tracking System,110432,19701
PDB,2MJ2,BMRB Entry Tracking System,110446,19702
PDB,2MJ3,BMRB Entry Tracking System,110467,19703
BMRB,5052,Old 1H chemical shifts at pH=3.0,110486,19704
BMRB,5690,Current data is the refinement of the old one,110486,19704
PDB,1NOR,Old structure at pH=3.0,110486,19704
PDB,2MJ4,BMRB Entry Tracking System,110486,19704
PDB,2MJ6,BMRB Entry Tracking System,110529,19707
PDB,2MJ7,BMRB Entry Tracking System,110560,19709
TargetDB,HR8998C,,110560,19709
PDB,2MJ8,BMRB Entry Tracking System,110598,19710
BMRB,16009,One fragment Npu DnaE Intein,110618,19711
PDB,2MJ9,BMRB Entry Tracking System,110637,19712
BMRB,17720,Monomer (Solution Structure),110651,19713
PDB,2LEP,Monomer (Solution Structure),110651,19713
PDB,2MJA,BMRB Entry Tracking System,110651,19713
PDB,2MJC,BMRB Entry Tracking System,110704,19716
BMRB,19718,Yah1 Reduced,110723,19717
PDB,2mjd,BMRB Entry Tracking System,110723,19717
BMRB,19717,Yah1 oxidized,110745,19718
PDB,2mje,BMRB Entry Tracking System,110745,19718
PDB,4JLE,Crystal structure of the same domain,110767,19719
BMRB,19721,NMR backbone assignment of Y75A apo-HasAp from Pseudomonas aeruginosa,110783,19720
BMRB,19722,NMR backbone assignment of H83A apo-HasAp from Pseudomonas aeruginosa,110783,19720
BMRB,19720,NMR backbone assignment of WT apo-HasAp from Pseudomonas aeruginosa,110798,19721
BMRB,19722,NMR backbone assignment of H83A apo-HasAp from Pseudomonas aeruginosa,110798,19721
BMRB,19720,NMR backbone assignment of WT apo-HasAp from Pseudomonas aeruginosa,110813,19722
BMRB,19721,NMR backbone assignment of Y75A apo-HasAp from Pseudomonas aeruginosa,110813,19722
BMRB,19724,Ig-alpha Ig-beta construct,110828,19723
BMRB,19725,Ig-alpha YE variant Ig-beta construct,110828,19723
EMBL,S46706.1,Entry containing the amino acid sequence of full-length Ig-alpha (CD79a),110828,19723
BMRB,19723,Ig-alpha Ig-beta construct,110848,19724
BMRB,19725,Ig-alpha YE variant Ig-beta construct,110848,19724
EMBL,M80461.1,Entry containing the amino acid sequence of full-length Ig-beta (CD79b),110848,19724
BMRB,19723,Ig-alpha Ig-beta construct,110870,19725
BMRB,19724,Ig-alpha Ig-beta construct,110870,19725
EMBL,S46706.1,Entry containing the amino acid sequence of WT full-length Ig-alpha (CD79a),110870,19725
PDB,2MJH,BMRB Entry Tracking System,110889,19726
PDB,2MJI,BMRB Entry Tracking System,110922,19727
PDB,2mjj,BMRB Entry Tracking System,110947,19728
PDB,2MJK,BMRB Entry Tracking System,110963,19729
BMRB,19407,Trimeric Skp,110980,19730
BMRB,19409,Trimeric Skp with bound tOmpA,110980,19730
BMRB,19410,tOmpA within the trimeric chaperone Skp,110980,19730
PDB,2MJL,BMRB Entry Tracking System,110997,19731
PDB,2MJM,BMRB Entry Tracking System,111017,19732
BMRB,19407,Trimeric Skp,111036,19733
BMRB,19409,Trimeric Skp with bound tOmpA,111036,19733
BMRB,19410,tOmpA within the trimeric chaperone Skp,111036,19733
BMRB,19730,Trimeric Skp with bound tOmpA,111036,19733
BMRB,17728,13C and 15N Chemical Shift Assignments for the fd Bacteriophage,111052,19734
PDB,2MJN,BMRB Entry Tracking System,111069,19735
PDB,2MJU,BMRB Entry Tracking System,111111,19737
PDB,2mjv,BMRB Entry Tracking System,111130,19738
PDB,2mjw,BMRB Entry Tracking System,111154,19739
PDB,2MJO,,111193,19741
BMRB,19743,Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase,111213,19742
BMRB,19744,Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase,111213,19742
BMRB,19742,Dimethylarginine Dimethylaminohydrolase,111228,19743
BMRB,19744,Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase,111228,19743
BMRB,19742,Dimethylarginine Dimethylaminohydrolase,111242,19744
BMRB,19743,Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase,111242,19744
PDB,2MJX,BMRB Entry Tracking System,111258,19745
PDB,2MJY,BMRB Entry Tracking System,111273,19746
BMRB,17728,13C and 15N Chemical Shift Assignments for the fd Bacteriophage,111297,19747
PDB,2CPB,"SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURES",111297,19747
PDB,2CPS,"SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN SODIUM DODECYL SULPHATE MICELLES, 25 LOWEST ENERGY STRUCTURES",111297,19747
PDB,2MJZ,BMRB Entry Tracking System,111297,19747
BMRB,21031,described in same manuscript,111315,19748
BMRB,21032,described in same manuscript,111315,19748
BMRB,21034,described in same manuscript,111315,19748
BMRB,21053,described in same manuscript,111315,19748
BMRB,21054,described in same manuscript,111315,19748
PDB,2MK1,corresponding coordinates for current entry,111315,19748
PDB,2MK2,BMRB Entry Tracking System,111335,19749
PDB,2MK3,BMRB Entry Tracking System,111378,19750
PDB,2MK4,BMRB Entry Tracking System,111396,19751
PDB,2MK5,BMRB Entry Tracking System,111413,19752
NCBI,5339,gene,111431,19753
UniProt,Q15149,,111431,19753
PDB,2MK6,BMRB Entry Tracking System,111468,19755
PDB,2MK7,BMRB Entry Tracking System,111519,19759
PDB,2MK9,BMRB Entry Tracking System,111562,19764
BMRB,18768,structural study of NS2(2-32) GBVB,111581,19765
BMRB,18769,structural study of NS2(32-57) GBVB,111581,19765
PDB,2lzp,structural study of NS2(2-32) GBVB,111581,19765
PDB,2lzq,structural study of NS2(32-57) GBVB,111581,19765
PDB,2MKB,BMRB Entry Tracking System,111581,19765
PDB,2mkc,BMRB Entry Tracking System,111599,19766
BMRB,19775,CPEB1RRM12,111692,19771
BMRB,19776,CPEB4RRM12 in complex with RNA,111692,19771
BMRB,19777,CPEB4RRM12 in free state,111692,19771
BMRB,19778,CPEB1RRM12 in complex with RNA,111692,19771
PDB,2MKE,BMRB Entry Tracking System,111692,19771
BMRB,19774,tandem UIMs of wild-type RAP80,111712,19773
PDB,2MKF,BMRB Entry Tracking System,111712,19773
PDB,3A1Q,Structure of RAP80 tandem UIMs bound to diubiquitin.,111712,19773
BMRB,19773,E81 deletion mutant from RAP80 tandem UIMs,111731,19774
PDB,2MKg,BMRB Entry Tracking System,111731,19774
PDB,3A1Q,Structure of RAP80 tandem UIMs bound to diubiquitin.,111731,19774
BMRB,19771,CPEB1ZZ,111750,19775
BMRB,19776,CPEB4RRM12 in complex with RNA,111750,19775
BMRB,19777,CPEB4RRM12 in free state,111750,19775
BMRB,19778,CPEB1RRM12 in complex with RNA,111750,19775
PDB,2mkh,BMRB Entry Tracking System,111750,19775
BMRB,19771,CPEB1ZZ,111769,19776
BMRB,19775,CPEB1RRM12,111769,19776
BMRB,19777,CPEB4RRM12 in free state,111769,19776
BMRB,19778,CPEB1RRM12 in complex with RNA,111769,19776
PDB,2MKI,BMRB Entry Tracking System,111769,19776
BMRB,19771,CPEB1ZZ,111791,19777
BMRB,19775,CPEB1RRM12,111791,19777
BMRB,19776,CPEB4RRM12 in complex with RNA,111791,19777
BMRB,19778,CPEB1RRM12 in complex with RNA,111791,19777
PDB,2MKJ,BMRB Entry Tracking System,111791,19777
BMRB,19771,CPEB1ZZ,111814,19778
BMRB,19775,CPEB1RRM12,111814,19778
BMRB,19776,CPEB4RRM12 in complex with RNA,111814,19778
BMRB,19777,CPEB4RRM12 in free state,111814,19778
PDB,2MKK,BMRB Entry Tracking System,111814,19778
PDB,4cpg,Solution structure of the SGTA dimerisation domain,111841,19779
PDB,2mkl,BMRB Entry Tracking System,111881,19783
PDB,2mkm,BMRB Entry Tracking System,111903,19784
BMRB,19788,FKBP52,111925,19787
PDB,3O5P,X-ray structure of FKBP51-FK506 binding domain 1,111925,19787
BMRB,19787,FKBP51,111944,19788
PDB,4LAW,X-ray structure of FKBP52-FK506 binding domain 1 and domain 2,111944,19788
PDB,2MKP,BMRB Entry Tracking System,111963,19789
PDB,2MKR,BMRB Entry Tracking System,111987,19791
PDB,2MKS,BMRB Entry Tracking System,112013,19792
PDB,2JO1,FXYD1,112046,19797
PDB,2JP3,FXYD4,112046,19797
PDB,2MKV,BMRB Entry Tracking System,112046,19797
BMRB,15276,"1H, 13C and 15N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lamdaVI light chain variable domain.",112060,19798
BMRB,19870,Solution Structure of 6aJL2 Amyloidogenic Light Chain Protein,112060,19798
PDB,2W0K,CRYSTAL STRUCTURE OF THE RECOMBINANT VARIABLE DOMAIN 6JAL2,112060,19798
PDB,2MKW,BMRB Entry Tracking System,112060,19798
PDB,2MMX,BMRB Entry Tracking System,112060,19798
PDB,2MKX,BMRB Entry Tracking System,112076,19799
PDB,2mky,BMRB Entry Tracking System,112092,19800
PDB,2mkz,BMRB Entry Tracking System,112107,19801
BMRB,16735,NMR resonance assignment of the apo C-terminal polypeptide of the Anthrax Lethal Factor catalytic domain,112126,19803
EMBL,CAC93932,Lef protein [Bacillus anthracis],112126,19803
EMBL,CAC93933,Lef protein [Bacillus anthracis],112126,19803
PDB,1J7N,Anthrax Toxin Lethal Factor,112126,19803
PDB,2L0R,Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center,112126,19803
PDB,2ML5,BMRB Entry Tracking System,112157,19806
PDB,2ml6,BMRB Entry Tracking System,112178,19807
PDB,2ml7,BMRB Entry Tracking System,112198,19808
PDB,2ML9,BMRB Entry Tracking System,112218,19809
PDB,2JLI,Crystal structure of Yersinia pestis YscUC,112218,19809
PDB,2V5G,Crystal structure of Yersinia enterocolitica YscUC(N263A),112218,19809
PDB,3BZL,Crystal structure of Escherichia coli EscUC,112218,19809
PDB,3BZV,Crystal structure of Escherichia coli EscUC(T264A),112218,19809
PDB,3C01,Crystal structure of Salmonella typhimurium SpaSC,112218,19809
PDB,2MLA,BMRB Entry Tracking System,112236,19810
PDB,2mlb,BMRB Entry Tracking System,112253,19811
PDB,2MLD,BMRB Entry Tracking System,112268,19813
BMRB,19817,mutation G159D in troponin C bound to the anchoring region of troponin I,112313,19816
PDB,2MLE,BMRB Entry Tracking System,112313,19816
BMRB,19816,C-domain of troponin C bound to the anchoring region of troponin I,112339,19817
PDB,2MLF,BMRB Entry Tracking System,112339,19817
BMRB,19819,cyanometNgb,112365,19818
BMRB,19818,metNgb,112383,19819
PDB,2MLG,BMRB Entry Tracking System,112403,19821
PDB,2mli,BMRB Entry Tracking System,112419,19822
PDB,2MLJ,BMRB Entry Tracking System,112441,19823
PDB,4crp,Solution structure of a TrkAIg2 domain construct,112455,19824
PDB,2MLM,BMRB Entry Tracking System,112485,19826
BMRB,19829,HUMAN CCR2 MEMBRANE-PROXIMAL C-TERMINAL REGION (PRO-C) IN A FROUNT BOUND FORM,112506,19828
PDB,2MLO,BMRB Entry Tracking System,112506,19828
BMRB,19828,HUMAN CCR2 MEMBRANE-PROXIMAL C-TERMINAL REGION (PRO-C) IN A MEMBRANE BOUND FORM,112523,19829
PDB,2MLQ,BMRB Entry Tracking System,112523,19829
BMRB,19833,antimicrobial peptide LsbB in TFE,112570,19832
PDB,2MLU,BMRB Entry Tracking System,112570,19832
BMRB,19832,antimicrobial peptide LsbB in DPC micelles,112588,19833
PDB,2MLV,BMRB Entry Tracking System,112588,19833
PDB,2MLW,BMRB Entry Tracking System,112606,19834
BMRB,19836,E. coli Trigger Factor in complex with unfolded PhoA1-150,112623,19835
BMRB,19837,E. coli Trigger Factor in complex with unfolded PhoA365-471,112623,19835
PDB,2MLX,BMRB Entry Tracking System,112623,19835
BMRB,19835,E. coli Trigger Factor in complex with unfolded PhoA220-310,112651,19836
BMRB,19837,E. coli Trigger Factor in complex with unfolded PhoA365-471,112651,19836
PDB,2mlx,,112651,19836
PDB,2MLY,BMRB Entry Tracking System,112651,19836
BMRB,19835,E. coli Trigger Factor in complex with unfolded PhoA220-310,112679,19837
BMRB,19836,E. coli Trigger Factor in complex with unfolded PhoA1-150,112679,19837
PDB,2mlx,,112679,19837
PDB,2mly,,112679,19837
PDB,2MLZ,BMRB Entry Tracking System,112679,19837
BMRB,19839,EcDsbA reduced,112706,19838
BMRB,19838,EcDsbA oxidized,112722,19839
PDB,2MM0,BMRB Entry Tracking System,112738,19840
BMRB,19840,ToxB,112753,19841
PDB,2MM2,BMRB Entry Tracking System,112753,19841
DBJ,BAE06095,,112768,19842
PDB,1UG3,Crystal structure of HEAT2 and HEAT3 domains of human eIF4GI,112768,19842
PDB,2MM3,BMRB Entry Tracking System,112797,19843
PDB,2MM4,BMRB Entry Tracking System,112839,19845
BMRB,19847,alpha amylase inhibitor peptide aS1,112855,19846
PDB,2MM5,BMRB Entry Tracking System,112855,19846
PDB,2MM6,alpha amylase inhibitor peptide aS1,112855,19846
BMRB,19846,alpha amylase inhibitor peptide aS4,112875,19847
PDB,2MM5,alpha amylase inhibitor peptide aS4,112875,19847
PDB,2MM6,BMRB Entry Tracking System,112875,19847
PDB,4csq,NMR solution structure of PA3793 from Pseudomonas aeruginosa,112895,19848
BMRB,19850,GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana,112914,19849
PDB,2mm9,BMRB Entry Tracking System,112914,19849
BMRB,19849,Reduced BolA2 from Arabidopsis thaliana,112932,19850
PDB,2mma,BMRB Entry Tracking System,112932,19850
PDB,2MMB,BMRB Entry Tracking System,112955,19851
PDB,3GJ0,GDP-BOUND HUMAN RAN GTPASE,112975,19852
PDB,2MMC,BMRB Entry Tracking System,112975,19852
PDB,2MMF,BMRB Entry Tracking System,112996,19853
BMRB,19855,Mengovirus Leader Protein Bound to Ran GTPase,113013,19854
BMRB,19857,Phosphorylated Mengovirus Leader Protein,113013,19854
BMRB,19858,Phosphorylated Mengovirus Leader Protein,113013,19854
PDB,2MMG,BMRB Entry Tracking System,113013,19854
BMRB,19854,Mengovirus Leader Protein Bound to Ran GTPase,113034,19855
BMRB,19857,Phosphorylated Mengovirus Leader Protein,113034,19855
BMRB,19858,Phosphorylated Mengovirus Leader Protein,113034,19855
PDB,2MMI,BMRB Entry Tracking System,113034,19855
PDB,2MMJ,BMRB Entry Tracking System,113057,19856
PDB,2MN8,"identical peptide sequence, but with cis-peptide bond at the peptoid residue",113057,19856
PDB,2MN9,peptoid analogue of maculatin G15 - peptoid trans-Nleu at position 13,113057,19856
BMRB,19882,"identical peptide sequence, but with cis-peptide bond at the peptoid residue",113057,19856
BMRB,19883,peptoid analogue of maculatin G15 - peptoid trans-Nleu at position 13,113057,19856
BMRB,19854,Mengovirus Leader Protein Bound to Ran GTPase,113080,19857
BMRB,19855,Mengovirus Leader Protein Bound to Ran GTPase,113080,19857
BMRB,19858,Phosphorylated Mengovirus Leader Protein,113080,19857
PDB,2MMK,BMRB Entry Tracking System,113080,19857
BMRB,19854,Mengovirus Leader Protein Bound to Ran GTPase,113105,19858
BMRB,19855,Mengovirus Leader Protein Bound to Ran GTPase,113105,19858
BMRB,19857,Phosphorylated Mengovirus Leader Protein,113105,19858
PDB,2MML,BMRB Entry Tracking System,113105,19858
PDB,2MMM,BMRB Entry Tracking System,113129,19859
PDB,2MMP,BMRB Entry Tracking System,113148,19860
PDB,2MMQ,BMRB Entry Tracking System,113167,19861
PDB,2MMR,BMRB Entry Tracking System,113186,19862
PDB,2MMS,BMRB Entry Tracking System,113205,19863
PDB,2MMT,BMRB Entry Tracking System,113241,19865
PDB,2mmu,BMRB Entry Tracking System,113270,19867
PDB,2MMV,BMRB Entry Tracking System,113292,19869
PDB,2W0K,6aJL2 determined by X-ray crystallography,113311,19870
PDB,2MKW,BMRB Entry Tracking System,113311,19870
PDB,2MMX,BMRB Entry Tracking System,113311,19870
BMRB,19798,Solution Structure of 6aJL2-R24G Amyloidogenic Light Chain Protein,113311,19870
PDB,2MMZ,BMRB Entry Tracking System,113330,19872
PDB,2MN0,BMRB Entry Tracking System,113358,19873
PDB,2MN1,BMRB Entry Tracking System,113374,19874
PDB,2MN2,BMRB Entry Tracking System,113404,19876
PDB,1b8w,DLP-1 (defensin-like peptide 1) from platypus venom,113437,19878
PDB,1zue,DLP-2 (defensin-like peptide 2) from platypus venom,113437,19878
PDB,1bnb,bovine beta-defensin-12,113437,19878
PDB,2MN3,BMRB Entry Tracking System,113437,19878
PDB,2MN4,BMRB Entry Tracking System,113453,19879
PDB,2MN5,BMRB Entry Tracking System,113468,19880
PDB,2MN7,BMRB Entry Tracking System,113496,19881
BMRB,19883,peptoid analogue of maculatin G15 - peptoid trans-Nleu at position 13,113515,19882
BMRB,19856,peptoid analogue of maculatin G15 (trans-Nleu at position 11),113515,19882
PDB,2MMJ,peptoid analogue of maculatin G15 (trans-Nleu at position 11),113515,19882
PDB,2MN8,BMRB Entry Tracking System,113515,19882
BMRB,19856,maculatin G15 with peptoid residue at position 11,113535,19883
BMRB,19882,"identical peptide sequence, but with cis-peptide bond at the peptoid residue",113535,19883
PDB,2MMJ,maculatin G15 with peptoid residue at position 11,113535,19883
PDB,2MN8,"identical peptide sequence, but with cis-peptide bond at the peptoid residue",113535,19883
PDB,2MN9,BMRB Entry Tracking System,113535,19883
BMRB,19083,"Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for Mutant SENP1 C603S Catalytic Domain",113571,19885
PDB,2MNB,BMRB Entry Tracking System,113587,19886
PDB,2MNC,BMRB Entry Tracking System,113601,19887
BMRB,19889,CGACTAGTCG with AIK-18/51-1,113616,19888
BMRB,19890,CGACTAGTCG dimer,113616,19888
PDB,2MND,BMRB Entry Tracking System,113616,19888
BMRB,19888,"CGACGCGTCG with 5,6,7,8-TETRAHYDROBIOPTERIN",113636,19889
BMRB,19890,CGACTAGTCG dimer,113636,19889
PDB,2MND,BMRB Entry Tracking System,113636,19889
BMRB,19888,"CGACGCGTCG with 5,6,7,8-TETRAHYDROBIOPTERIN",113656,19890
BMRB,19889,CGACTAGTCG with AIK-18/51-1,113656,19890
PDB,2MNF,BMRB Entry Tracking System,113656,19890
PDB,2MNG,BMRB Entry Tracking System,113674,19891
PDB,2mnh,BMRB Entry Tracking System,113691,19892
PDB,2MNI,BMRB Entry Tracking System,113708,19893
PDB,2MNQ,BMRB Entry Tracking System,113741,19901
PDB,2MNS,BMRB Entry Tracking System,113755,19902
PDB,2mnt,BMRB Entry Tracking System,113775,19904
BMRB,19114,4E-BP2,113799,19905
PDB,2MNU,BMRB Entry Tracking System,113816,19906
BMRB,19908,NMR resonance assignment of the archaeal ribosomal protein L7Ae bound to a 25 nt RNA,113831,19907
PDB,1RA4,This is the same protein L7Ae. Structure is derived from x-ray christallography,113831,19907
BMRB,19907,NMR resonance assignment of the archaeal ribosomal protein L7Ae,113848,19908
PDB,1RA4,L7Ae apo,113848,19908
PDB,1SDS,L7Ae bound to H/ACA box RNA,113848,19908
PDB,4PBD,Crystal structure of the N-terminal CS domain of human Shq1,113879,19910
PDB,4PCK,Crystal structure of the P22S mutant of N-terminal CS domain of human Shq1,113879,19910
PDB,2mnw,BMRB Entry Tracking System,113879,19910
PDB,4cz3,PDBe entry 4cz3,113902,19911
PDB,2mnx,BMRB Entry Tracking System,113920,19912
BMRB,19914,KDM5B PHD1 finger in complex with H3K4me0(1-10aa),113946,19913
PDB,2MNY,BMRB Entry Tracking System,113946,19913
BMRB,19913,KDM5B PHD1 finger,113964,19914
PDB,2MNZ,BMRB Entry Tracking System,113964,19914
BMRB,19916,"cold shock protein, TaCsp with dT7",113981,19915
PDB,2MO0,BMRB Entry Tracking System,113981,19915
BMRB,19915,"cold shock protein, TaCsp",113996,19916
PDB,2MO1,BMRB Entry Tracking System,113996,19916
BMRB,19925,DNA dodecamer with A:C mismatch,114013,19917
PDB,2MO2,BMRB Entry Tracking System,114013,19917
PDB,2MO5,BMRB Entry Tracking System,114030,19921
BMRB,19290,human TDP-43 tandem RRMs in complex with UG-rich RNA,114051,19922
PDB,1WF0,,114051,19922
PDB,3D2W,,114051,19922
PDB,4BS2,,114051,19922
BMRB,19917,DNA dodecamer containing the 5-hydroxycytosine,114081,19925
PDB,2MO7,BMRB Entry Tracking System,114081,19925
PDB,3GPG,Crystal structure of macro domain of Chikungunya virus,114112,19927
PDB,3GPQ,Crystal structure of macro domain of Venezuelan Equine ENcephalitis virus,114112,19927
PDB,4cz4,Structure of HP24stab,114147,19929
BMRB,19934,Dual-phosphorylated human p38 alpha apo,114166,19930
BMRB,19935,Dual-phosphorylated human p38 alpha ADP-bound,114166,19930
BMRB,19936,Dual-phosphorylated human p38 alpha MK2 334/D peptide bound,114166,19930
BMRB,19937,Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound,114166,19930
PDB,1CNL,,114201,19932
PDB,1E74,,114201,19932
PDB,1G2G,,114201,19932
PDB,1IM1,,114201,19932
PDB,1IMI,,114201,19932
PDB,2BC7,,114201,19932
PDB,2C9T,,114201,19932
PDB,2MOA,BMRB Entry Tracking System,114201,19932
PDB,4OS1,,114201,19932
PDB,4OS2,,114201,19932
PDB,4OS4,,114201,19932
PDB,4OS5,,114201,19932
PDB,4OS6,,114201,19932
PDB,4OS7,,114201,19932
PDB,2MOC,BMRB Entry Tracking System,114221,19933
BMRB,19930,non-phosphorylated (apo),114236,19934
BMRB,19935,Dual-phosphorylated human p38 alpha ADP-bound,114236,19934
BMRB,19936,Dual-phosphorylated human p38 alpha MK2 334/D peptide bound,114236,19934
BMRB,19937,Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound,114236,19934
BMRB,19930,non-phosphorylated (apo),114256,19935
BMRB,19934,Dual-phosphorylated human p38 alpha apo,114256,19935
BMRB,19936,Dual-phosphorylated human p38 alpha MK2 334/D peptide bound,114256,19935
BMRB,19937,Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound,114256,19935
BMRB,19930,non-phosphorylated (apo),114278,19936
BMRB,19934,Dual-phosphorylated human p38 alpha apo,114278,19936
BMRB,19935,Dual-phosphorylated human p38 alpha ADP-bound,114278,19936
BMRB,19937,Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound,114278,19936
BMRB,19930,non-phosphorylated (apo),114299,19937
BMRB,19934,Dual-phosphorylated human p38 alpha apo,114299,19937
BMRB,19935,Dual-phosphorylated human p38 alpha ADP-bound,114299,19937
BMRB,19936,Dual-phosphorylated human p38 alpha MK2 334/D peptide bound,114299,19937
PDB,2MCS,Structure in the reduced state.,114322,19938
PDB,2MOD,BMRB Entry Tracking System,114322,19938
PDB,2MOE,BMRB Entry Tracking System,114343,19939
PDB,1G90,,114365,19940
PDB,2GE4,,114365,19940
PDB,2MOF,BMRB Entry Tracking System,114382,19941
PDB,2MOG,BMRB Entry Tracking System,114403,19942
PDB,2MOI,BMRB Entry Tracking System,114418,19943
BMRB,19944,Transmembrane domain of the full-length inner membrane protein YgaP from Escherichia coli,114418,19943
BMRB,19946,Cytoplasmic rhodanese domain of the full-length inner membrane protein YgaP from Escherichia coli,114418,19943
PDB,2MOK,BMRB Entry Tracking System,114432,19945
PDB,2MOI,,114451,19946
PDB,2MOJ,,114451,19946
PDB,2MOL,BMRB Entry Tracking System,114451,19946
BMRB,19943,Cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli,114451,19946
BMRB,19944,Transmembrane domain of the full-length inner membrane protein YgaP from Escherichia coli,114451,19946
BMRB,19963,Bitistatin_B,114467,19947
PDB,2MOP,BMRB Entry Tracking System,114467,19947
BMRB,15131,18.5 kDa isoform of murine myelin basic protein,114485,19948
BMRB,18520,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles,114485,19948
BMRB,19186,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP),114485,19948
BMRB,19949,MBP S38-S107 peptide in the presence of Fyn-SH3,114485,19948
BMRB,6100,18.5kDa isoform of murine myelin basic protein (MBP),114485,19948
BMRB,6857,FF2 immunodominant peptide,114485,19948
PDB,2LUG,,114485,19948
BMRB,15131,18.5 kDa isoform of murine myelin basic protein,114504,19949
BMRB,18520,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles,114504,19949
BMRB,19186,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP),114504,19949
BMRB,19948,MBP S38-S107 peptide of 18.5 kDa,114504,19949
BMRB,6100,18.5kDa isoform of murine myelin basic protein (MBP),114504,19949
BMRB,6857,FF2 immunodominant peptide,114504,19949
PDB,2LUG,,114504,19949
PDB,2MOV,BMRB Entry Tracking System,114585,19953
PDB,2MOW,BMRB Entry Tracking System,114602,19954
PDB,2MOX,BMRB Entry Tracking System,114618,19955
PDB,2MP0,BMRB Entry Tracking System,114660,19958
PDB,4cyk,Structure of PAB-DEPENDENT POLY(A)-SPECIFIC RIBONUCLEASE SUBUN,114682,19959
PDB,2MP1,BMRB Entry Tracking System,114713,19960
PDB,2MP2,BMRB Entry Tracking System,114733,19961
PDB,2MP3,BMRB Entry Tracking System,114756,19962
BMRB,19947,Bitistatin_A,114770,19963
PDB,2MP5,BMRB Entry Tracking System,114770,19963
PDB,2MP6,BMRB Entry Tracking System,114788,19966
BMRB,18620,NMR Chemical Shift Assignments of N terminal RRM domain of La protein,114811,19967
BMRB,5235,Resonance assignment and secondary structure determination of a C-terminal fragment of the Lupus Autoantigen (La) protein containing a putative RNA recognition motif (RRM),114811,19967
PDB,1OWX,Solution structure of the C-terminal RRM of human La (La225-334),114811,19967
PDB,2MP8,BMRB Entry Tracking System,114860,19970
BMRB,15131,18.5 kDa isoform of murine myelin basic protein,114900,19972
BMRB,18520,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles,114900,19972
BMRB,19186,S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP),114900,19972
BMRB,19948,MBP S38-S107 peptide of 18.5 kDa,114900,19972
BMRB,19949,MBP S38-S107 peptide in the presence of Fyn-SH3,114900,19972
BMRB,6100,18.5kDa isoform of murine myelin basic protein (MBP),114900,19972
BMRB,6857,FF2 immunodominant peptide,114900,19972
PDB,2LUG,,114900,19972
PDB,2MP9,BMRB Entry Tracking System,114917,19973
PDB,2MPB,BMRB Entry Tracking System,114935,19974
EMBL,BLAC_BACLI,,114951,19976
PDB,1L2S,,114951,19976
PDB,2BLM,,114951,19976
PDB,3LY3,,114951,19976
PDB,3LY4,,114951,19976
PDB,3M2J,,114951,19976
PDB,3M2K,,114951,19976
PDB,4BLM,,114951,19976
PDB,2MPF,BMRB Entry Tracking System,114967,19977
PDB,2MPG,BMRB Entry Tracking System,114991,19978
PDB,2MPI,BMRB Entry Tracking System,115010,19979
BMRB,19981,CnA-VIVIT,115042,19980
BMRB,19980,CnA free,115061,19981
PDB,2P1B,,115081,19982
PDB,1XB9,,115081,19982
PDB,4N8M,,115081,19982
PDB,2MPJ,BMRB Entry Tracking System,115134,19986
PDB,2MPK,BMRB Entry Tracking System,115154,19987
PDB,2MPL,BMRB Entry Tracking System,115173,19988
PDB,1EOT,"Solution Structure of Eotaxin, An Ensemble of 32 NMR Solution Structures",115192,19989
PDB,2EOT,"Solution NMR Structure of Eotaxin, Minimized Average Structre",115192,19989
PDB,2MPM,BMRB Entry Tracking System,115192,19989
BMRB,17068,,115246,19991
BMRB,17641,,115246,19991
BMRB,6356,,115246,19991
PDB,2fql,,115246,19991
PDB,2ga5,,115246,19991
PDB,3oeq,,115246,19991
PDB,3oer,,115246,19991
PDB,4ec2,,115246,19991
BMRB,19995,LysRS Anticodon Binding Domain 72-207,115276,19993
PDB,2moi,,115294,19994
PDB,2mol,,115294,19994
PDB,2MPN,BMRB Entry Tracking System,115294,19994
BMRB,19993,Lysyl t-RNA synthetase 1-72,115311,19995
BMRB,25021,"Backbone chemical shifts of murine Roquin-1 ROQ domain (147-326), apo form",115325,19996
PDB,4QI2,Crystal structure of ROQ domain in complex with Tnf CDE RNA,115325,19996
PDB,4QI0,Crystal structure of ROQ domain,115325,19996
PDB,2MPQ,BMRB Entry Tracking System,115341,19998
BMRB,20004,NMR Structure of Leucine-Enkephalin in DMPC/CHAPS bicelle,115440,20003
BMRB,20005,NMR Structure of Leucine-Enkephalin in DMPC/CHAPS/GM1,115440,20003
BMRB,20003,NMR solution structure of Leucine-enkephalin in,115458,20004
BMRB,20005,NMR solution structure of Leucine-enkephalin in isotropic DMPC+CHAPS+GM1 (1:4:0.3) bicelles,115458,20004
PDB,20003,NMR solution structure of Leucine-enkephalin in water,115476,20005
PDB,20004,NMR solution structure of Leucine-enkephalin in isotropic DMPC+CHAPS (1:4) bicelles,115476,20005
BMRB,20008,"L7P mutant, (CYIQNCPRV)",115494,20007
BMRB,20007,"Con-T, (CYIQNCLRV)",115513,20008
PDB,1UAO,Solution structure of chignolin,115532,20009
BMRB,15639,NMR data for the peptide,115564,20010
BMRB,11021,NMR data for CLN025,115580,20011
PDB,1UAO,Solution structure of chignolin,115580,20011
BMRB,20013,PFR peptide in DPC micelle,115599,20012
BMRB,20012,PFR peptide in SDS micelle,115616,20013
BMRB,20015,BI-32169,115633,20014
BMRB,20017,"antimicrobial peptide, FLPIVTNLLSGLL",115677,20016
BMRB,20018,"antimicrobial peptide, FLSHIAGFLSNLF",115677,20016
BMRB,20016,"antimicrobial peptide, FLSGIVGMLGKLF",115695,20017
BMRB,20018,"antimicrobial peptide, FLSHIAGFLSNLF",115695,20017
BMRB,20016,"antimicrobial peptide, FLSGIVGMLGKLF",115713,20018
BMRB,20017,"antimicrobial peptide, FLPIVTNLLSGLL",115713,20018
PDB,1Q2J,,115808,20023
BMRB,5881,proton chemical shifts SmIIIA,115808,20023
PDB,1q2j,,115834,20024
PDB,1r9i,,115834,20024
PDB,1q2j,,115852,20025
PDB,1r9i,,115852,20025
BMRB,20030,"Apelin 17 (at 5 C, major conformer)",115933,20029
BMRB,20031,"Apelin 17 (at 5 C, major conformer)",115933,20029
BMRB,20029,Apelin 17 (at 35 C),115970,20030
BMRB,20031,"Apelin 17 (at 5 C, major conformer)",115970,20030
BMRB,20029,Apelin 17 (at 35 C),115994,20031
BMRB,20030,"Apelin 17 (at 5 C, major conformer)",115994,20031
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116084,20036
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116084,20036
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116084,20036
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116084,20036
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116084,20036
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116084,20036
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116084,20036
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116100,20037
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116100,20037
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116100,20037
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116100,20037
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116100,20037
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116100,20037
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116100,20037
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116117,20038
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116117,20038
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116117,20038
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116117,20038
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116117,20038
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116117,20038
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116117,20038
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116134,20039
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116134,20039
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116134,20039
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116134,20039
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116134,20039
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116134,20039
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116134,20039
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116151,20040
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116151,20040
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116151,20040
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116151,20040
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116151,20040
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116151,20040
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116151,20040
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116170,20041
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116170,20041
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116170,20041
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116170,20041
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116170,20041
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116170,20041
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116170,20041
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116188,20042
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116188,20042
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116188,20042
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116188,20042
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116188,20042
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116188,20042
BMRB,20043,Cyclic Pseudotetrapeptide (7h),116188,20042
BMRB,20036,Cyclic Pseudotetrapeptide (7a),116206,20043
BMRB,20037,Cyclic Pseudotetrapeptide (7b),116206,20043
BMRB,20038,Cyclic Pseudotetrapeptide (7c),116206,20043
BMRB,20039,Cyclic Pseudotetrapeptide (7d),116206,20043
BMRB,20040,Cyclic Pseudotetrapeptide (7e),116206,20043
BMRB,20041,Cyclic Pseudotetrapeptide (7f),116206,20043
BMRB,20042,Cyclic Pseudotetrapeptide (7g),116206,20043
BMRB,20049,"Mu-KIIIA[C1A,C9A]",116307,20048
PDB,2LXG,BMRB Entry Tracking System,116307,20048
BMRB,20048,Native toxin,116334,20049
BMRB,15391,KIA7 peptide tetramer,116439,20054
BMRB,15392,KIA7F peptide tetramer,116439,20054
BMRB,16023,KIA7H tetramer,116439,20054
BMRB,20055,KIA7H tetramer,116439,20054
PDB,2jo4,,116439,20054
BMRB,15391,KIA7 peptide tetramer,116462,20055
BMRB,15392,KIA7F peptide tetramer,116462,20055
BMRB,16022,KIA7W tetramer,116462,20055
BMRB,20054,KIA7W tetramer,116462,20055
PDB,2jo4,,116462,20055
BMRB,20058,YI12WW,116501,20057
BMRB,20059,YI12WY,116501,20057
BMRB,20060,YI12FF,116501,20057
BMRB,20057,YI12WF,116517,20058
BMRB,20059,YI12WY,116517,20058
BMRB,20060,YI12FF,116517,20058
BMRB,20057,YI12WF,116533,20059
BMRB,20058,YI12WW,116533,20059
BMRB,20060,YI12FF,116533,20059
BMRB,20057,YI12WF,116562,20060
BMRB,20058,YI12WW,116562,20060
BMRB,20059,YI12WY,116562,20060
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116628,20064
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116644,20065
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116644,20065
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116644,20065
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116644,20065
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116644,20065
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116644,20065
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116661,20066
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116661,20066
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116661,20066
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116661,20066
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116661,20066
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116661,20066
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116678,20067
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116678,20067
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116678,20067
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116678,20067
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116678,20067
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116678,20067
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116694,20068
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116694,20068
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116694,20068
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116694,20068
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116694,20068
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116694,20068
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116710,20069
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116710,20069
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116710,20069
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116710,20069
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116710,20069
BMRB,20070,cyclo[BTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116710,20069
BMRB,20064,cyclo[Ala-Aod-BTrp-Leu] alpha/beta-tetrapeptide,116728,20070
BMRB,20065,cyclo[Trp-Leu-BAla-Aod] alpha/beta-tetrapeptide,116728,20070
BMRB,20066,cyclo[Trp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116728,20070
BMRB,20067,cyclo[NMeTrp-BLeu-Ala-Aod] alpha/beta-tetrapeptide,116728,20070
BMRB,20068,cyclo[Trp-BLeu-Pro-Aod] alpha/beta-tetrapeptide,116728,20070
BMRB,20069,cyclo[Trp-BLeu-BAla-Aod] alpha/beta-tetrapeptide,116728,20070
BMRB,20072,"cyclo[Trp-Leu-1,5-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116746,20071
BMRB,20073,"cyclo[Trp-D-Leu-1,5-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116746,20071
BMRB,20071,"cyclo[Trp-Ile-1,4-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116763,20072
BMRB,20073,"cyclo[Trp-D-Leu-1,5-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116763,20072
BMRB,20071,"cyclo[Trp-Ile-1,4-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116780,20073
BMRB,20072,"cyclo[Trp-Leu-1,5-sub-(1,2,3)-triazole-D-Ala-Aod] Tetrapeptides",116780,20073
PDB,2g48,,116797,20074
PDB,2KIB,BMRB Entry Tracking System,116797,20074
PDB,3dgj,,116797,20074
PDB,1l2y,NMR Structure of Trp-Cage Miniprotein Construct TC5b,116831,20076
PDB,1JJQ,previous structure entry,116912,20081
BMRB,20029,Apelin17-35C,116930,20082
BMRB,20030,Apelin17_5C confA,116930,20082
BMRB,20031,Apelin17_5C confB,116930,20082
BMRB,20087,nociceptin analogue,116998,20086
BMRB,20088,nociceptin analogue,116998,20086
BMRB,20089,nociceptin analogue,116998,20086
BMRB,20086,nociceptin Antagonist,117015,20087
BMRB,20088,nociceptin analogue,117015,20087
BMRB,20089,nociceptin analogue,117015,20087
BMRB,20086,nociceptin Antagonist,117034,20088
BMRB,20087,nociceptin analogue,117034,20088
BMRB,20089,nociceptin analogue,117034,20088
BMRB,20086,nociceptin Antagonist,117053,20089
BMRB,20087,nociceptin analogue,117053,20089
BMRB,20088,nociceptin analogue,117053,20089
BMRB,20095,cis Pis-1[NkG],117142,20094
BMRB,20098,Pis-1[PG],117142,20094
BMRB,20094,trans Pis-1[NkG],117159,20095
BMRB,20098,Pis-1[PG],117159,20095
BMRB,20094,trans Pis-1[NkG],117176,20098
BMRB,20095,cis Pis-1[NkG],117176,20098
PDB,1SU4,,117210,20102
PDB,2AGV,,117210,20102
PDB,2ZBD,,117210,20102
PDB,3P9B,,117210,20102
BMRB,20104,XT-7,117228,20103
BMRB,20103,[Lysine4]XT-7,117248,20104
BMRB,20105,BI-32169,117248,20104
BMRB,20014,Capistruin,117268,20105
PDB,1CNL,conotoxin ImI,117285,20107
PDB,1IM1,conotoxin ImI,117285,20107
BMRB,20111,SecA[788-804]Y794A,117304,20108
PDB,2BBL,NMR structure of PV1-VPg,117338,20110
PDB,2F8E,FMDV-VPg1 (fragment) in complex with polymerase,117338,20110
PDB,3CDW,Coxsackie virus VPg (fragment) in complex with polymerase,117338,20110
BMRB,20108,SecA fragment,117359,20111
BMRB,16660,SUBSTANCE P IN WATER COMPLEXED WITH NK1R,117435,20115
BMRB,20116,Substance P in DMPC:CHAPS q=0.25 bicelles,117435,20115
BMRB,20117,Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles,117435,20115
PDB,2KS9,BMRB Entry Tracking System,117435,20115
BMRB,16660,SUBSTANCE P IN WATER COMPLEXED WITH NK1R,117451,20116
BMRB,20115,Substance P 40 structures in water pH 5.5 298 K,117451,20116
BMRB,20117,Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles,117451,20116
PDB,2KSA,BMRB Entry Tracking System,117451,20116
BMRB,16660,Substance P in water complexed with NK1R,117468,20117
BMRB,20115,Substance P 40 structures in water pH 5.5 298 K,117468,20117
BMRB,20116,Substance P in DMPC:CHAPS q=0.25 bicelles,117468,20117
PDB,2KSB,BMRB Entry Tracking System,117468,20117
BMRB,15582,NS3(10-24),117568,20123
BMRB,20100,VK22 in LPS micelle,117601,20125
BMRB,15145,"Assigned chemical shifts of Neurotensin in Membrane-Mimetic Environments:
Molecular Basis for Neurotensin Receptor Recognition",118150,21001
BMRB,21007,"""alpha-conotoxin ImI cystathionine 1-3",118185,21006
BMRB,21006,alpha-conotoxin ImI Cystathionine 2-4,118205,21007
BMRB,21005,related peptides,118225,21008
BMRB,21010,extended upain,118241,21009
BMRB,21009,upain-1,118261,21010
BMRB,21012,DPC micelle bound structure of Cysteine deleted analog of TachyplesinI,118280,21011
PDB,1MA2,TachyplesinI wildtype in solution,118280,21011
PDB,1MA4,Tyrosine mutant of TachyplesinI,118280,21011
PDB,2RSW,BMRB Entry Tracking System,118362,21019
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118376,21022
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118376,21022
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118376,21022
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118376,21022
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118376,21022
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118376,21022
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118390,21023
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118390,21023
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118390,21023
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118390,21023
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118390,21023
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118390,21023
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118404,21024
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118404,21024
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118404,21024
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118404,21024
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118404,21024
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118404,21024
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118420,21025
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118420,21025
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118420,21025
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118420,21025
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118420,21025
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118420,21025
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118434,21026
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118434,21026
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118434,21026
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118434,21026
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118434,21026
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118434,21026
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118448,21027
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118448,21027
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118448,21027
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118448,21027
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118448,21027
BMRB,21028,MDCSGCSRPG-Zn-water complex from acidic conditions,118448,21027
BMRB,21022,MDCSGCSRPG cyclic + copper(I) from acidic,118466,21028
BMRB,21023,MDCSGCSRPG head-to-tail cyclic peptide + Cu(I) no metal constraint - high energy ensemble (B),118466,21028
BMRB,21024,MDCSGCSRPG cyclic peptide bound to Cu(I) from acidic conditions,118466,21028
BMRB,21025,MDCSGCSRPG+Zn from acidic conditions,118466,21028
BMRB,21026,MDCSGCSRPG + Zn from basic conditions,118466,21028
BMRB,21027,MDCSGCSRPG + Zn from basic conditions - tridentate binding,118466,21028
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118484,21031
BMRB,21032,"Solution structure of 1,3-Fucosylated chitobiose",118484,21031
BMRB,21033,"Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein",118484,21031
BMRB,21034,"Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K",118484,21031
BMRB,21053,Solution structure of fucosylated LacDiNAc (LDNF),118484,21031
BMRB,21054,Solution structure of the amphibian egg glycan Bv9 from Bombina variegata,118484,21031
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118506,21032
BMRB,21031,Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me],118506,21032
BMRB,21033,"Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein",118506,21032
BMRB,21034,"Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K",118506,21032
BMRB,21035,AIP-III,118732,21047
BMRB,21053,Solution structure of fucosylated LacDiNAc (LDNF),118506,21032
BMRB,21054,Solution structure of the amphibian egg glycan Bv9 from Bombina variegata,118506,21032
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118530,21033
BMRB,21031,Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me],118530,21033
BMRB,21032,"Solution structure of 1,3-Fucosylated chitobiose",118530,21033
BMRB,21034,"Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K",118530,21033
BMRB,21053,Solution structure of fucosylated LacDiNAc (LDNF),118530,21033
BMRB,21054,Solution structure of the amphibian egg glycan Bv9 from Bombina variegata,118530,21033
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118553,21034
BMRB,21031,Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me],118553,21034
BMRB,21032,"Solution structure of 1,3-Fucosylated chitobiose",118553,21034
BMRB,21033,"Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein",118553,21034
BMRB,21053,Solution structure of fucosylated LacDiNAc (LDNF),118553,21034
BMRB,21054,Solution structure of the amphibian egg glycan Bv9 from Bombina variegata,118553,21034
BMRB,21036,AIP-III_D4A,118578,21035
BMRB,21037,AIP-III_DF5,118578,21035
BMRB,21038,AIP-III_DL7,118578,21035
BMRB,21039,AIP-III_F5A cyclic peptide,118578,21035
BMRB,21040,AIP-III_L7A,118578,21035
BMRB,21041,tAIP-III,118578,21035
BMRB,21042,tAIP-III_D2A,118578,21035
BMRB,21045,AIP-I,118578,21035
BMRB,21046,AIP-II,118578,21035
BMRB,21047,AIP-IV,118578,21035
BMRB,21035,AIP-III,118593,21036
BMRB,21037,AIP-III_DF5,118593,21036
BMRB,21038,AIP-III_DL7,118593,21036
BMRB,21039,AIP-III_F5A cyclic peptide,118593,21036
BMRB,21040,AIP-III_L7A,118593,21036
BMRB,21041,tAIP-III,118593,21036
BMRB,21042,tAIP-III_D2A,118593,21036
BMRB,21035,AIP-III,118608,21037
BMRB,21036,AIP-III_D4A,118608,21037
BMRB,21038,AIP-III_DL7,118608,21037
BMRB,21039,AIP-III_F5A cyclic peptide,118608,21037
BMRB,21040,AIP-III_L7A,118608,21037
BMRB,21041,tAIP-III,118608,21037
BMRB,21042,tAIP-III_D2A,118608,21037
BMRB,21045,AIP-I,118608,21037
BMRB,21046,AIP-II,118608,21037
BMRB,21047,AIP-IV,118608,21037
BMRB,21035,AIP-III,118624,21038
BMRB,21036,AIP-III_D4A,118624,21038
BMRB,21037,AIP-III_DF5,118624,21038
BMRB,21039,AIP-III_F5A cyclic peptide,118624,21038
BMRB,21040,AIP-III_L7A,118624,21038
BMRB,21041,tAIP-III,118624,21038
BMRB,21042,tAIP-III_D2A,118624,21038
BMRB,21045,AIP-I,118624,21038
BMRB,21046,AIP-II,118624,21038
BMRB,21047,AIP-IV,118624,21038
BMRB,21035,AIP-III,118640,21039
BMRB,21036,AIP-III_D4A,118640,21039
BMRB,21037,AIP-III_DF5,118640,21039
BMRB,21038,AIP-III_DL7,118640,21039
BMRB,21040,AIP-III_L7A,118640,21039
BMRB,21041,tAIP-III,118640,21039
BMRB,21042,tAIP-III_D2A,118640,21039
BMRB,21045,AIP-I,118640,21039
BMRB,21046,AIP-II,118640,21039
BMRB,21047,AIP-IV,118640,21039
BMRB,21035,AIP-III,118655,21040
BMRB,21036,AIP-III_D4A,118655,21040
BMRB,21037,AIP-III_DF5,118655,21040
BMRB,21038,AIP-III_DL7,118655,21040
BMRB,21039,AIP-III_F5A cyclic peptide,118655,21040
BMRB,21041,tAIP-III,118655,21040
BMRB,21042,tAIP-III_D2A,118655,21040
BMRB,21045,AIP-I,118655,21040
BMRB,21046,AIP-II,118655,21040
BMRB,21047,AIP-IV,118655,21040
BMRB,21035,AIP-III,118670,21041
BMRB,21036,AIP-III_D4A,118670,21041
BMRB,21037,AIP-III_DF5,118670,21041
BMRB,21038,AIP-III_DL7,118670,21041
BMRB,21039,AIP-III_F5A cyclic peptide,118670,21041
BMRB,21040,AIP-III_L7A,118670,21041
BMRB,21042,tAIP-III_D2A,118670,21041
BMRB,21045,AIP-I,118670,21041
BMRB,21046,AIP-II,118670,21041
BMRB,21047,AIP-IV,118670,21041
BMRB,21035,AIP-III,118686,21042
BMRB,21036,AIP-III_D4A,118686,21042
BMRB,21037,AIP-III_DF5,118686,21042
BMRB,21038,AIP-III_DL7,118686,21042
BMRB,21039,AIP-III_F5A cyclic peptide,118686,21042
BMRB,21040,AIP-III_L7A,118686,21042
BMRB,21041,tAIP-III,118686,21042
BMRB,21045,AIP-I,118686,21042
BMRB,21046,AIP-II,118686,21042
BMRB,21047,AIP-IV,118686,21042
BMRB,21035,AIP-III,118702,21045
BMRB,21036,AIP-III_D4A,118702,21045
BMRB,21037,AIP-III_DF5,118702,21045
BMRB,21038,AIP-III_DL7,118702,21045
BMRB,21039,AIP-III_F5A cyclic peptide,118702,21045
BMRB,21040,AIP-III_L7A,118702,21045
BMRB,21041,tAIP-III,118702,21045
BMRB,21042,tAIP-III_D2A,118702,21045
BMRB,21046,AIP-II,118702,21045
BMRB,21047,AIP-IV,118702,21045
BMRB,21035,AIP-III,118717,21046
BMRB,21036,AIP-III_D4A,118717,21046
BMRB,21037,AIP-III_DF5,118717,21046
BMRB,21038,AIP-III_DL7,118717,21046
BMRB,21039,AIP-III_F5A cyclic peptide,118717,21046
BMRB,21040,AIP-III_L7A,118717,21046
BMRB,21041,tAIP-III,118717,21046
BMRB,21042,tAIP-III_D2A,118717,21046
BMRB,21045,AIP-I,118717,21046
BMRB,21036,AIP-III_D4A,118732,21047
BMRB,21037,AIP-III_DF5,118732,21047
BMRB,21038,AIP-III_DL7,118732,21047
BMRB,21039,AIP-III_F5A cyclic peptide,118732,21047
BMRB,21040,AIP-III_L7A,118732,21047
BMRB,21041,tAIP-III,118732,21047
BMRB,21042,tAIP-III_D2A,118732,21047
BMRB,21045,AIP-I,118732,21047
BMRB,21046,AIP-II,118732,21047
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118747,21053
BMRB,21031,Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me],118747,21053
BMRB,21032,"Solution structure of 1,3-Fucosylated chitobiose",118747,21053
BMRB,21033,"Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein",118747,21053
BMRB,21034,"Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K",118747,21053
BMRB,21054,Solution structure of the amphibian egg glycan Bv9 from Bombina variegata,118747,21053
BMRB,19748,Solution structure of Lactodifucotetraose (LDFT) beta anomer,118768,21054
BMRB,21031,Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me],118768,21054
BMRB,21032,"Solution structure of 1,3-Fucosylated chitobiose",118768,21054
BMRB,21033,"Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein",118768,21054
BMRB,21034,"Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K",118768,21054
BMRB,21053,Solution structure of fucosylated LacDiNAc (LDNF),118768,21054
BMRB,21057,SFTI-TCTR N12 N14,118789,21056
BMRB,21056,N-methylated version of SFTI-TCTR N12 N14,118807,21057
BMRB,21059,Trans-PapMA-k,118823,21058
BMRB,21058,PapMA,118838,21059
BMRB,21060,conotoxin Eb1.6,118853,21062
BMRB,21065,Beta-Pro ZZZ,118870,21064
BMRB,21066,Beta-Pro ZEZ,118870,21064
BMRB,21067,Beta-Pro ZZE,118870,21064
BMRB,21068,Beta-Pro ZZEZ,118870,21064
BMRB,21069,Beta-Pro ZEZZ,118870,21064
BMRB,21064,Beta-Pro EZZ,118888,21065
BMRB,21066,Beta-Pro ZEZ,118888,21065
BMRB,21067,Beta-Pro ZZE,118888,21065
BMRB,21068,Beta-Pro ZZEZ,118888,21065
BMRB,21069,Beta-Pro ZEZZ,118888,21065
BMRB,21064,Beta-Pro EZZ,118906,21066
BMRB,21065,Beta-Pro ZZZ,118906,21066
BMRB,21067,Beta-Pro ZZE,118906,21066
BMRB,21068,Beta-Pro ZZEZ,118906,21066
BMRB,21069,Beta-Pro ZEZZ,118906,21066
BMRB,21064,Beta-Pro EZZ,118924,21067
BMRB,21065,Beta-Pro ZZZ,118924,21067
BMRB,21066,Beta-Pro ZEZ,118924,21067
BMRB,21068,Beta-Pro ZZEZ,118924,21067
BMRB,21069,Beta-Pro ZEZZ,118924,21067
BMRB,21064,Beta-Pro EZZ,118942,21068
BMRB,21065,Beta-Pro ZZZ,118942,21068
BMRB,21066,Beta-Pro ZEZ,118942,21068
BMRB,21067,Beta-Pro ZZE,118942,21068
BMRB,21069,Beta-Pro ZEZZ,118942,21068
BMRB,21064,Beta-Pro EZZ,118960,21069
BMRB,21065,Beta-Pro ZZZ,118960,21069
BMRB,21066,Beta-Pro ZEZ,118960,21069
BMRB,21067,Beta-Pro ZZE,118960,21069
BMRB,21068,Beta-Pro ZZEZ,118960,21069
BMRB,21064,Beta-Pro EZZ,118978,21070
BMRB,21065,Beta-Pro ZZZ,118978,21070
BMRB,21066,Beta-Pro ZEZ,118978,21070
BMRB,21067,Beta-Pro ZZE,118978,21070
BMRB,21068,Beta-Pro ZZEZ,118978,21070
BMRB,21069,Beta-Pro ZEZZ,118978,21070
BMRB,21071,"Beta-Pro homodimer, Z conformation",118978,21070
BMRB,21072,"Beta-Pro heterodimer, E conformation",118978,21070
BMRB,21073,"Beta-Pro heterodimer, Z conformation",118978,21070
BMRB,21064,Beta-Pro EZZ,118997,21071
BMRB,21065,Beta-Pro ZZZ,118997,21071
BMRB,21066,Beta-Pro ZEZ,118997,21071
BMRB,21067,Beta-Pro ZZE,118997,21071
BMRB,21068,Beta-Pro ZZEZ,118997,21071
BMRB,21069,Beta-Pro ZEZZ,118997,21071
BMRB,21070,Beta-Pro homodimer,118997,21071
BMRB,21072,"Beta-Pro heterodimer, E conformation",118997,21071
BMRB,21073,"Beta-Pro heterodimer, Z conformation",118997,21071
BMRB,21064,Beta-Pro EZZ,119016,21072
BMRB,21065,Beta-Pro ZZZ,119016,21072
BMRB,21066,Beta-Pro ZEZ,119016,21072
BMRB,21067,Beta-Pro ZZE,119016,21072
BMRB,21068,Beta-Pro ZZEZ,119016,21072
BMRB,21069,Beta-Pro ZEZZ,119016,21072
BMRB,21070,Beta-Pro homodimer,119016,21072
BMRB,21071,"Beta-Pro homodimer, Z conformation",119016,21072
BMRB,21073,"Beta-Pro heterodimer, Z conformation",119016,21072
BMRB,21064,Beta-Pro EZZ,119035,21073
BMRB,21065,Beta-Pro ZZZ,119035,21073
BMRB,21066,Beta-Pro ZEZ,119035,21073
BMRB,21067,Beta-Pro ZZE,119035,21073
BMRB,21068,Beta-Pro ZZEZ,119035,21073
BMRB,21069,Beta-Pro ZEZZ,119035,21073
BMRB,21070,Beta-Pro homodimer,119035,21073
BMRB,21071,"Beta-Pro homodimer, Z conformation",119035,21073
BMRB,21072,"Beta-Pro heterodimer, E conformation",119035,21073
BMRB,21075,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K724-D728),119054,21074
BMRB,21076,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K725-D729),119054,21074
BMRB,21077,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K728-D732),119054,21074
BMRB,21078,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K729-D733),119054,21074
BMRB,21074,Structure of the membrane proximal region of ITBG3 - residues 722-739,119075,21075
BMRB,21076,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K725-D729),119075,21075
BMRB,21077,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K728-D732),119075,21075
BMRB,21078,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K729-D733),119075,21075
BMRB,21074,Structure of the membrane proximal region of ITBG3 - residues 722-739,119097,21076
BMRB,21075,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K724-D728),119097,21076
BMRB,21077,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K728-D732),119097,21076
BMRB,21078,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K729-D733),119097,21076
BMRB,21074,Structure of the membrane proximal region of ITBG3 - residues 722-739,119119,21077
BMRB,21075,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K724-D728),119119,21077
BMRB,21076,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K725-D729),119119,21077
BMRB,21078,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K729-D733),119119,21077
BMRB,21074,Structure of the membrane proximal region of ITBG3 - residues 722-739,119141,21078
BMRB,21075,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K724-D728),119141,21078
BMRB,21076,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K725-D729),119141,21078
BMRB,21077,NMR Structure of Lactam Constrained beta3-Integrin Cytoplasmic Domain Fragment (K728-D732),119141,21078
BMRB,21064,Beta-Pro EZZ,119197,21084
BMRB,21065,Beta-Pro ZZZ,119197,21084
BMRB,21066,Beta-Pro ZEZ,119197,21084
BMRB,21067,Beta-Pro ZZE,119197,21084
BMRB,21068,Beta-Pro ZZEZ,119197,21084
BMRB,21069,Beta-Pro ZEZZ,119197,21084
BMRB,21070,Beta-Pro homodimer,119197,21084
BMRB,21071,"Beta-Pro homodimer, Z conformation",119197,21084
BMRB,21072,"Beta-Pro heterodimer, E conformation",119197,21084
BMRB,21073,"Beta-Pro heterodimer, Z conformation",119197,21084
BMRB,21084,"Beta-Pro alternating trimer, ZZ confirmation",119197,21084
BMRB,21085,"Beta-Pro heterochiral trimer, ZZ conformation",119197,21084
BMRB,21086,"Beta-Pro heterochiral trimer, ZE conformation",119197,21084
BMRB,21064,Beta-Pro EZZ,119213,21085
BMRB,21065,Beta-Pro ZZZ,119213,21085
BMRB,21066,Beta-Pro ZEZ,119213,21085
BMRB,21067,Beta-Pro ZZE,119213,21085
BMRB,21068,Beta-Pro ZZEZ,119213,21085
BMRB,21069,Beta-Pro ZEZZ,119213,21085
BMRB,21070,Beta-Pro homodimer,119213,21085
BMRB,21071,"Beta-Pro homodimer, Z conformation",119213,21085
BMRB,21072,"Beta-Pro heterodimer, E conformation",119213,21085
BMRB,21073,"Beta-Pro heterodimer, Z conformation",119213,21085
BMRB,21084,"Beta-Pro alternating trimer, ZZ confirmation",119213,21085
BMRB,21085,"Beta-Pro heterochiral trimer, ZZ conformation",119213,21085
BMRB,21086,"Beta-Pro heterochiral trimer, ZE conformation",119213,21085
BMRB,21064,Beta-Pro EZZ,119229,21086
BMRB,21065,Beta-Pro ZZZ,119229,21086
BMRB,21066,Beta-Pro ZEZ,119229,21086
BMRB,21067,Beta-Pro ZZE,119229,21086
BMRB,21068,Beta-Pro ZZEZ,119229,21086
BMRB,21069,Beta-Pro ZEZZ,119229,21086
BMRB,21070,Beta-Pro homodimer,119229,21086
BMRB,21071,"Beta-Pro homodimer, Z conformation",119229,21086
BMRB,21072,"Beta-Pro heterodimer, E conformation",119229,21086
BMRB,21073,"Beta-Pro heterodimer, Z conformation",119229,21086
BMRB,21084,"Beta-Pro alternating trimer, ZZ confirmation",119229,21086
BMRB,21085,"Beta-Pro heterochiral trimer, ZZ conformation",119229,21086
BMRB,4855,"(14-38, 30-51)Ser BPTI folding intermediate",119352,2169
BMRB,4868,BPTI-R52,119352,2169
BMRB,4873,(30-51)Ser BPTI folding intermediate,119352,2169
PDB,2MPT,BMRB Entry Tracking System,121319,25000
PDB,4PHX,AggB,121342,25001
PDB,4PH8,AggA,121342,25001
PDB,4OR1,AafB,121342,25001
PDB,2MPV,BMRB Entry Tracking System,121342,25001
PDB,2mpw,BMRB Entry Tracking System,121357,25002
EMBL,BLAC_BACLI,,121376,25003
PDB,1L2S,,121376,25003
PDB,2BLM,,121376,25003
PDB,3LY3,,121376,25003
PDB,3LY4,,121376,25003
PDB,3M2J,,121376,25003
PDB,3M2K,,121376,25003
PDB,4BLM,,121376,25003
BMRB,17937,CAP-Gly Domain of Mammalian Dynactin,121407,25005
BMRB,19025,CAP-Gly Domain of Mammalian at 19.9 T,121407,25005
BMRB,19031,p150Glued CAP-Gly Domain in complex with EB1 at 19.9 T,121407,25005
PDB,1TXQ,,121407,25005
PDB,2HKQ,,121407,25005
PDB,2HQH,,121407,25005
PDB,2MPX,BMRB Entry Tracking System,121407,25005
PDB,2m02,,121407,25005
PDB,3E2U,,121407,25005
PDB,2MQ0,BMRB Entry Tracking System,121432,25007
BMRB,25010,Hypertrophic Cardiomyopathy-Related R502W Mutant,121432,25007
PDB,2MQ1,BMRB Entry Tracking System,121449,25008
PDB,2MQ2,BMRB Entry Tracking System,121465,25009
BMRB,25011,Cysteine Deleted Protegrin-1 (CDP-1): rr1,121465,25009
BMRB,25012,Cysteine Deleted Protegrin-1 (CDP-1): lr10,121465,25009
PDB,2mq0,Structural Characterization of the Wild-type C3 Domain of Cardiac Myosin Binding Protein-C,121479,25010
BMRB,25007,Structural Characterization of the Wild-type C3 Domain of Cardiac Myosin Binding Protein-C,121479,25010
PDB,2MQ3,BMRB Entry Tracking System,121479,25010
PDB,2MQ4,BMRB Entry Tracking System,121496,25011
BMRB,25012,Cysteine Deleted Protegrin-1 (CDP-1): lr10,121496,25011
BMRB,25009,Cysteine Deleted Protegrin-1 (CDP-1): rr14,121496,25011
PDB,2MQ5,BMRB Entry Tracking System,121510,25012
BMRB,25011,Cysteine Deleted Protegrin-1 (CDP-1): rr11,121510,25012
BMRB,25009,Cysteine Deleted Protegrin-1 (CDP-1): rr14,121510,25012
BMRB,25014,holo YqcA,121524,25013
BMRB,25015,holo FldA,121524,25013
BMRB,25013,apo YqcA,121539,25014
BMRB,25015,holo FldA,121539,25014
BMRB,25013,apo YqcA,121554,25015
BMRB,25014,holo YqcA,121554,25015
PDB,2MQ6,BMRB Entry Tracking System,121569,25016
PDB,2MQ8,BMRB Entry Tracking System,121584,25018
PDB,2MQ9,BMRB Entry Tracking System,121631,25020
BMRB,19996,Roquin-1 ROQ domain in complex with Tnf CDE RNA,121646,25021
PDB,4QI2,Crystal structure of ROQ domain in complex with Tnf CDE RNA,121646,25021
PDB,4QI0,Crystal structure of ROQ domain,121646,25021
PDB,2MQA,BMRB Entry Tracking System,121695,25024
PDB,2MQB,BMRB Entry Tracking System,121739,25026
BMRB,25027,NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482,121739,25026
BMRB,25028,NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri,121739,25026
PDB,2MQC,BMRB Entry Tracking System,121754,25027
BMRB,25026,NMR structure of putative beta-lactamase (NP_372339.1) from Staphylococcus aureus Mu50,121754,25027
BMRB,25028,NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri,121754,25027
PDB,2MQD,BMRB Entry Tracking System,121772,25028
BMRB,25026,NMR structure of putative beta-lactamase (NP_372339.1) from Staphylococcus aureus Mu50,121772,25028
BMRB,25027,NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482,121772,25028
BMRB,4689,NMR Studies of the Backbone Flexibility and Structure of Human Growth Hormone,121790,25029
PDB,2MQE,BMRB Entry Tracking System,121804,25030
PDB,2MQF,BMRB Entry Tracking System,121822,25031
PDB,2MQG,BMRB Entry Tracking System,121838,25032
NCBI,AAN77901.2,putative nucleic acid binding protein [Chlamydomonas reinhardtii],121852,25033
PDB,2MQH,BMRB entry-tracking system,121852,25033
BMRB,25035,troponin C-troponin I hybrid proteins cChimeraX,121871,25034
BMRB,25034,troponin C-troponin I hybrid proteins cChimera,121898,25035
PDB,2MQJ,BMRB Entry Tracking System,121925,25036
PDB,2MQK,BMRB Entry Tracking System,121940,25037
BMRB,25056,Cyp33RRM90 MLLPHD3 H3K4me3,121960,25038
PDB,2MQL,BMRB Entry Tracking System,121960,25038
BMRB,25040,most two C-terminal RNA Recognition Motif Domain of hnRNP L,121980,25039
BMRB,25041,First RNA Recognition Motif Domain of hnRNP L bound to CACACA RNA,121980,25039
BMRB,25042,Second RNA Recognition Motif Domain of hnRNP L bound to ACACAC RNA,121980,25039
BMRB,25043,Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA,121980,25039
PDB,2MQM,BMRB Entry Tracking System,121980,25039
BMRB,25039,Second RNA Recognition Motif Domain of hnRNP L,122000,25040
BMRB,25041,First RNA Recognition Motif Domain of hnRNP L bound to CACACA RNA,122000,25040
BMRB,25042,Second RNA Recognition Motif Domain of hnRNP L bound to ACACAC RNA,122000,25040
BMRB,25043,Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA,122000,25040
PDB,2MQN,BMRB Entry Tracking System,122000,25040
BMRB,25039,Second RNA Recognition Motif Domain of hnRNP L,122020,25041
BMRB,25040,most two C-terminal RNA Recognition Motif Domain of hnRNP L,122020,25041
BMRB,25042,Second RNA Recognition Motif Domain of hnRNP L bound to ACACAC RNA,122020,25041
BMRB,25043,Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA,122020,25041
PDB,2MQO,BMRB Entry Tracking System,122020,25041
BMRB,25039,Second RNA Recognition Motif Domain of hnRNP L,122043,25042
BMRB,25040,most two C-terminal RNA Recognition Motif Domain of hnRNP L,122043,25042
BMRB,25041,First RNA Recognition Motif Domain of hnRNP L bound to CACACA RNA,122043,25042
BMRB,25043,Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA,122043,25042
PDB,2MQP,BMRB Entry Tracking System,122043,25042
BMRB,25039,Second RNA Recognition Motif Domain of hnRNP L,122066,25043
BMRB,25040,most two C-terminal RNA Recognition Motif Domain of hnRNP L,122066,25043
BMRB,25041,First RNA Recognition Motif Domain of hnRNP L bound to CACACA RNA,122066,25043
BMRB,25042,Second RNA Recognition Motif Domain of hnRNP L bound to ACACAC RNA,122066,25043
PDB,2MQQ,BMRB Entry Tracking System,122066,25043
BMRB,19297,Assignment of DC-SIGNR carbohydrate recognition domain in holo (calcium bound) state.,122105,25046
PDB,1K9J,Crystal structure of DC-SIGNR CRD in complex with small glycan fragment GlcNAc2Man3.,122105,25046
PDB,4uqt,RRM-PEPTIDE and RES COMPLEX,122121,25047
PDB,2MQS,BMRB Entry Tracking System,122140,25048
BMRB,25052,RNA (68-MER) and Nucleocapsid protein p10,122161,25049
BMRB,25100,pf tRNApro:MLV-Nucleocapsid (1:2) Complex,122161,25049
BMRB,25101,tRNApro:MLV Nucleocapsid Protein (1:1) Complex,122161,25049
PDB,2MQT,BMRB Entry Tracking System,122161,25049
PDB,2MQU,BMRB Entry Tracking System,122177,25050
BMRB,25049,RNA (68-MER),122194,25052
BMRB,25100,pf tRNApro:MLV-Nucleocapsid (1:2) Complex,122194,25052
BMRB,25101,tRNApro:MLV Nucleocapsid Protein (1:1) Complex,122194,25052
PDB,2MQV,BMRB Entry Tracking System,122194,25052
BMRB,25060,dCDS1-RNA,122213,25059
BMRB,25059,dCSD1,122244,25060
BMRB,25062,OR462,122262,25061
PDB,2MR5,BMRB Entry Tracking System,122262,25061
PDB,2MR6,BMRB Entry Tracking System,122287,25062
BMRB,25080,The chemical shift assignments of [FeZn]-IMP-1 metallo-beta-lactamase.,122316,25063
BMRB,25065,PCP7T holo form,122337,25064
PDB,2MQM,BMRB Entry Tracking System,122337,25064
PDB,2MR8,BMRB Entry Tracking System,122362,25065
BMRB,25064,PCP7T apo form,122362,25065
PDB,2MR7,PCP7T apo form,122362,25065
PDB,2MR9,BMRB Entry Tracking System,122389,25066
BMRB,25088,Ddi1UBL,122389,25066
PDB,2MRP,Ddi1UBL,122389,25066
PDB,2MRA,BMRB Entry Tracking System,122407,25067
PDB,2MRC,BMRB Entry Tracking System,122432,25068
PDB,2MRD,BMRB Entry Tracking System,122450,25069
BMRB,25071,ubiquitin-binding zinc finger (UBZ) domain from human Rad18,122466,25070
PDB,2MRE,BMRB Entry Tracking System,122466,25070
PDB,2MRF,BMRB Entry Tracking System,122489,25071
BMRB,25078,CSD1-UNR bound to msl2 mRNA and Sex-lethal,122512,25072
BMRB,4028,Sex-lethal bound to RNA,122512,25072
BMRB,4029,Sex-lethal in the free state,122512,25072
PDB,1B7F,Crystal structure of Sex-lethal bound to transformer mRNA,122512,25072
PDB,4QQB,Crystal structure of Sex-lethal bound to CSD1-UNR and msl2 mRNA,122512,25072
EMBL,P29074,,122542,25077
BMRB,25059,CSD1 in the free state,122563,25078
BMRB,25060,CSD1 bound to RNA,122563,25078
BMRB,25072,SXL-UNR-msl2-mRNA,122563,25078
PDB,4QQB,crystal structure of CSD1 in complex with SXL and msl2 mRNA,122563,25078
PDB,2MRH,BMRB Entry Tracking System,122577,25079
BMRB,25063,The chemical shift assignments of [ZnZn]-IMP-1 metallo-beta-lactamase.,122596,25080
PDB,4UAM,1.8 Angstrom crystal structure of IMP-1 metallo-beta-lactamase with a mixed iron-zinc center in the active site,122596,25080
BMRB,17368,Fyn SH2 free state,122618,25081
BMRB,17369,Fyn SH2 in complex with the high affinity phosphorilated peptide,122618,25081
BMRB,25082,Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide,122618,25081
PDB,2MRJ,BMRB Entry Tracking System,122618,25081
PDB,2mqi,Fyn SH2 free state,122618,25081
BMRB,17368,Fyn SH2 free state,122637,25082
BMRB,17369,Fyn SH2 in complex with the high affinity inhibitory peptide,122637,25082
BMRB,25081,Fyn SH2 domain bound to the natural inhibitory peptide,122637,25082
PDB,2MRK,BMRB Entry Tracking System,122637,25082
PDB,2mqi,Fyn SH2 free state,122637,25082
PDB,2mrj,Fyn SH2 domain bound to the natural inhibitory peptide,122637,25082
PDB,2MRL,BMRB Entry Tracking System,122657,25083
PDB,2MRM,BMRB Entry Tracking System,122689,25085
PDB,1mvf,MazE addiction antidote,122706,25086
PDB,2MRN,BMRB Entry Tracking System,122706,25086
PDB,2MRP,BMRB Entry Tracking System,122744,25088
BMRB,25066,UBA domain of DNA-damage-inducible 1 protein (Ddi1),122744,25088
PDB,2MR9,UBA domain of DNA-damage-inducible 1 protein (Ddi1),122744,25088
PDB,2mrn,truncated EcMazE,122764,25092
BMRB,25086,truncated EcMazE,122764,25092
PDB,1mvf,X-ray full-length EcMazE,122764,25092
PDB,2mru,BMRB Entry Tracking System,122764,25092
PDB,1mvf,X-ray structure full-length EcMazE,122781,25093
PDB,1mrn,truncated EcMazE,122781,25093
BMRB,25086,truncated EcMazE,122781,25093
BMRB,25094,EcMazE homodimer (full-length EcMazE-DNA complex),122781,25093
BMRB,25092,truncated EcMazE-DNA complex,122798,25094
BMRB,25093,free full-length EcMazE,122798,25094
PDB,2mru,Structure truncated EcMazE-DNA complex,122798,25094
PDB,2MRW,BMRB Entry Tracking System,122813,25096
PDB,2MRY,BMRB Entry Tracking System,122831,25098
PDB,2MRZ,BMRB Entry Tracking System,122852,25099
BMRB,25049,RNA (68-MER),122866,25100
BMRB,25052,RNA (68-MER) and Nucleocapsid protein p10,122866,25100
BMRB,25101,tRNApro:MLV Nucleocapsid Protein (1:1) Complex,122866,25100
PDB,2MS0,BMRB Entry Tracking System,122866,25100
BMRB,25049,RNA (68-MER),122890,25101
BMRB,25052,RNA (68-MER) and Nucleocapsid protein p10,122890,25101
BMRB,25100,pf tRNApro:MLV-Nucleocapsid (1:2) Complex,122890,25101
PDB,2MS1,BMRB Entry Tracking System,122890,25101
PDB,2MS3,BMRB Entry Tracking System,122915,25102
PDB,2MS4,BMRB Entry Tracking System,122933,25104
PDB,3NJ6,0.95 A resolution X-ray structure of (GGCAGCAGCC)2,122948,25106
PDB,3NJ7,1.9 A resolution X-ray structure of (GGCAGCAGCC)2,122948,25106
PDB,4J50,Crystal Structure of an Expanded RNA CAG Repeat,122948,25106
PDB,2MS5,BMRB Entry Tracking System,122948,25106
BMRB,25107,DNA-quercetin,122948,25106
PDB,2MS6,DNA-quercetin,122948,25106
PDB,2MS6,BMRB Entry Tracking System,122963,25107
BMRB,25106,CAG RNA,122963,25107
BMRB,2MS5,CAG RNA,122963,25107
PDB,2MS8,BMRB Entry Tracking System,122997,25109
PDB,2MS9,BMRB Entry Tracking System,123019,25110
PDB,2MSA,BMRB Entry Tracking System,123039,25112
BMRB,25115,GTPase KRas-GNP tethered to a lipid-bilayer nanodisc,123054,25114
BMRB,25116,GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc,123054,25114
PDB,2M4A,,123054,25114
PDB,2M4B,,123054,25114
PDB,2MSC,BMRB Entry Tracking System,123054,25114
BMRB,25114,GTPase KRas-GDP tethered to a lipid-bilayer nanodisc,123076,25115
BMRB,25116,GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc,123076,25115
PDB,2M4A,,123076,25115
PDB,2M4B,,123076,25115
PDB,2MSD,BMRB Entry Tracking System,123076,25115
BMRB,25114,GTPase KRas-GDP tethered to a lipid-bilayer nanodisc,123098,25116
BMRB,25115,GTPase KRas-GNP tethered to a lipid-bilayer nanodisc,123098,25116
PDB,2M4A,,123098,25116
PDB,2M4B,,123098,25116
PDB,2MSE,BMRB Entry Tracking System,123098,25116
BMRB,25119,cTnI[1-73]-cTnC,123123,25118
BMRB,25120,cTnC-cTnI[1-73]-cTnI[144-163],123123,25118
BMRB,25118,cTnI[1-73],123137,25119
BMRB,25120,cTnC-cTnI[1-73]-cTnI[144-163],123137,25119
BMRB,25118,cTnI[1-73],123165,25120
BMRB,25119,cTnI[1-73]-cTnC,123165,25120
PDB,2MSF,BMRB Entry Tracking System,123205,25122
PDB,1D3Z,,123220,25123
PDB,2MSG,BMRB Entry Tracking System,123220,25123
PDB,3ONS,,123220,25123
BMRB,25125,Apo form of the Receiver Domain of Nitrogen Regulatory Protein C ( NTRC ) at 35C,123238,25124
PDB,2MSK,BMRB Entry Tracking System,123238,25124
PDB,2MSN,BMRB Entry Tracking System,123275,25127
BMRB,25129,P-superfamily conotoxin Bru9a cyclised with a Gly-Leu-Pro linker,123296,25128
BMRB,2MSQ,P-superfamily conotoxin Bru9a cyclised with a Gly-Leu-Pro linker,123296,25128
PDB,2MSO,BMRB Entry Tracking System,123296,25128
BMRB,25128,P-superfamily conotoxin Gm9a cycled with a Gly-Leu-Pro linker,123310,25129
BMRB,2MSO,P-superfamily conotoxin Gm9a cycled with a Gly-Leu-Pro linker,123310,25129
PDB,2MSQ,BMRB Entry Tracking System,123310,25129
PDB,2MSR,BMRB Entry Tracking System,123338,25130
PDB,2MSU,BMRB Entry Tracking System,123356,25131
PDB,3GQE,Crystal structure of macro domain of Venezuelan Equine Encephalitis virus,123370,25132
PDB,3GQO,Crystal structure of macro domain of Venezuelan Equine Encephalitis virus in complex with ADP-ribose,123370,25132
BMRB,19864,R1 peptide,123390,25134
PDB,2MSV,BMRB Entry Tracking System,123406,25135
PDB,2MSW,BMRB Entry Tracking System,123441,25137
PDB,2MSX,BMRB Entry Tracking System,123482,25139
BMRB,24141,El_LovR (Mg complex),123504,25140
BMRB,25140,apo EL_LovR,123521,25141
PDB,2MSY,BMRB Entry Tracking System,123539,25142
BMRB,25145,B1 box dimer of the tripartite 19,123554,25143
PDB,2MSZ,BMRB Entry Tracking System,123554,25143
BMRB,25143,RING finger of the tripartite 19,123576,25145
PDB,2MT1,BMRB Entry Tracking System,123576,25145
PDB,2MT3,BMRB Entry Tracking System,123621,25147
PDB,2MT4,BMRB Entry Tracking System,123636,25148
PDB,2MT5,BMRB Entry Tracking System,123654,25149
PDB,2MT6,BMRB Entry Tracking System,123671,25150
PDB,2MT7,BMRB Entry Tracking System,123686,25151
PDB,2MT8,BMRB Entry Tracking System,123704,25152
BMRB,25155,apo FldB,123719,25153
PDB,2MT9,BMRB Entry Tracking System,123719,25153
PDB,4KC0,Crystal structure of mouse Sting,123738,25154
PDB,4LOL,Crystal structure of mSting in complex with DMXAA,123738,25154
BMRB,25153,holo FldB,123755,25155
PDB,2MTB,BMRB Entry Tracking System,123755,25155
BMRB,25157,Decorin Binding Protein A,123772,25156
PDB,2MTC,BMRB Entry Tracking System,123772,25156
BMRB,25156,Decorin Binding Protein A,123790,25157
PDB,2MTD,BMRB Entry Tracking System,123790,25157
PDB,2MTE,BMRB Entry Tracking System,123808,25158
BMRB,25160,RRM1 of human LARP6,123827,25159
PDB,2MTG,BMRB entry-tracking system,123827,25159
BMRB,25159,LARP6-LaM,123847,25160
PDB,2MTF,BMRB entry-tracking system,123847,25160
BMRB,25162,CrnA2,123866,25161
BMRB,25161,CrnA1,123884,25162
PDB,2MTJ,BMRB Entry Tracking System,123902,25163
BMRB,25164,three-way junction from the VS ribozyme,123902,25163
PDB,2MTK,BMRB Entry Tracking System,123923,25164
BMRB,25163,three-way junction from the VS ribozyme,123923,25164
PDB,2MTL,BMRB Entry Tracking System,123948,25165
BMRB,19910,Solution structure of the P22S mutant of N-terminal CS domain of human Shq1,124000,25167
PDB,2MNW,Solution structure of the P22S mutant of N-terminal CS domain of human Shq1,124000,25167
PDB,4PBD,Crystal structure of the N-terminal CS domain of human Shq1,124000,25167
PDB,4PCK,Crystal structure of the P22S mutant of N-terminal CS domain of human Shq1,124000,25167
PDB,2MTM,BMRB Entry Tracking System,124046,25169
PDB,2MTN,BMRB Entry Tracking System,124061,25171
PDB,2JUT,,124122,25174
PDB,2MTO,BMRB Entry Tracking System,124122,25174
BMRB,25193,NisI,124138,25175
BMRB,25194,C-terminal domain of the lantibiotic immunity protein NisI,124138,25175
PDB,2MTP,BMRB Entry Tracking System,124159,25176
PDB,2A3D,,124177,25177
PDB,2MTQ,BMRB Entry Tracking System,124177,25177
PDB,2MTR,BMRB Entry Tracking System,124196,25178
BMRB,25180,mutant NS4A N-terminal domain of DENV (L6E;M10E),124213,25179
BMRB,25179,wt NS4A N-terminal domain of DENV,124234,25180
PDB,2MTS,BMRB Entry Tracking System,124255,25181
BMRB,25183,FSFG-K-6His,124273,25182
BMRB,25184,FG-N,124273,25182
BMRB,25185,FG-N-6His,124273,25182
BMRB,25182,FSFG-K,124290,25183
BMRB,25184,FG-N,124290,25183
BMRB,25185,FG-N-6His,124290,25183
BMRB,25182,FSFG-K,124307,25184
BMRB,25183,FSFG-K-6His,124307,25184
BMRB,25185,FG-N-6His,124307,25184
BMRB,25182,FSFG-K,124324,25185
BMRB,25183,FSFG-K-6His,124324,25185
BMRB,25184,FG-N,124324,25185
PDB,2MTT,BMRB Entry Tracking System,124341,25186
PDB,2MTU,BMRB Entry Tracking System,124357,25187
PDB,2MTV,BMRB Entry Tracking System,124374,25188
BMRB,25190,malaria short AMA-1 peptide analogue,124400,25189
PDB,2MTW,BMRB Entry Tracking System,124400,25189
BMRB,25189,malaria peptide 1815,124414,25190
PDB,2MTX,BMRB Entry Tracking System,124414,25190
PDB,2MTY,BMRB Entry Tracking System,124429,25191
BMRB,25200,STARP peptide 20570,124429,25191
BMRB,18037,"NMR STRUCTURE OF THE IMIPENEM-ACYLATED L,D-TRANSPEPTIDASE FROM BACILLUS SUBTILIS",124443,25192
PDB,2MTZ,BMRB Entry Tracking System,124443,25192
BMRB,25175,N-terminal domain of the lantibiotic immunity protein NisI,124467,25193
BMRB,25194,C-terminal domain of the lantibiotic immunity protein NisI,124467,25193
BMRB,25175,N-terminal domain of the lantibiotic immunity protein NisI,124494,25194
BMRB,25193,NisI,124494,25194
PDB,2MU0,BMRB Entry Tracking System,124515,25195
BMRB,4492,Unmyristoylated GCAP-2 with three calcium ions bound,124570,25199
PDB,2MU6,BMRB Entry Tracking System,124599,25200
BMRB,25191,STARP peptide 20546,124599,25200
BMRB,25204,Malarial Peptide 6673,124613,25201
PDB,2MU7,BMRB Entry Tracking System,124613,25201
PDB,2MU8,BMRB Entry Tracking System,124627,25202
PDB,2MU9,BMRB Entry Tracking System,124641,25203
BMRB,25202,,124641,25203
BMRB,25201,1513 MSP-1 peptide,124655,25204
PDB,2MUA,BMRB Entry Tracking System,124655,25204
BMRB,6467,Solution structure of APETx2,124669,25205
PDB,1WXN,Solution structure of APETx2,124669,25205
PDB,2MUB,BMRB Entry Tracking System,124669,25205
PDB,2MUD,BMRB Entry Tracking System,124688,25206
PDB,2MUE,BMRB Entry Tracking System,124702,25207
PDB,2MUF,BMRB Entry Tracking System,124736,25209
BMRB,25211,peptide 6762,124736,25209
PDB,4uzm,PDBe entry,124750,25210
PDB,2MUG,BMRB Entry Tracking System,124768,25211
BMRB,25209,synthetic peptide 36075,124768,25211
PDB,2MUH,BMRB Entry Tracking System,124782,25212
PDB,4uzw,PDBe entry,124800,25213
PDB,4uzx,PDBe entry,124818,25214
PDB,2MUK,BMRB Entry Tracking System,124850,25217
PDB,2MUL,BMRB Entry Tracking System,124879,25219
PDB,2MUM,BMRB Entry Tracking System,124917,25221
BMRB,18256,"R state structure of monomeric phospholamban (C36A, C41F, C46A)",124939,25222
BMRB,18952,"Serine 16 phosphorylated phospholamban pentamer, Hybrid solution and solid-state NMR structural ensemble",124939,25222
PDB,2MUN,BMRB Entry Tracking System,124955,25223
BMRB,25226,cis-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1),124992,25225
PDB,2MUO,BMRB Entry Tracking System,124992,25225
BMRB,25225,trans-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1),125011,25226
PDB,2MUP,BMRB Entry Tracking System,125011,25226
BMRB,25228,aSyn H50Q monomer,125030,25227
BMRB,25227,aSyn WT monomer,125050,25228
BMRB,25229,Human FAAP20 UBZ-Ubiquitin Complex,125070,25229
PDB,2MUQ,BMRB Entry Tracking System,125070,25229
BMRB,25229,Human FAAP20 UBZ,125094,25230
PDB,2MUR,BMRB Entry Tracking System,125094,25230
PDB,2MUT,BMRB Entry Tracking System,125137,25232
BMRB,25234,M2 19-49,125161,25233
PDB,2MUV,BMRB Entry Tracking System,125161,25233
BMRB,25233,S31N 19-49,125178,25234
PDB,2MUW,BMRB Entry Tracking System,125178,25234
PDB,2MUY,BMRB Entry Tracking System,125196,25235
PDB,2MUZ,BMRB Entry Tracking System,125216,25236
PDB,2MV0,BMRB Entry Tracking System,125232,25237
PDB,2FHW,Solution NMR structure of human relaxin-3,125259,25238
PDB,2MV1,BMRB entry-tracking system,125259,25238
PDB,6RLX,Crystal structure of human relaxin-2,125259,25238
BMRB,18620,NMR Chemical Shift Assignments of N terminal RRM domain of La protein,125279,25239
BMRB,18621,NMR Chemical Shift Assignments of N terminal La motif domain of La protein,125279,25239
PDB,2MV2,BMRB Entry Tracking System,125294,25240
PDB,2MV3,BMRB Entry Tracking System,125314,25241
PDB,4v10,PDBe entry,125333,25242
PDB,2MV5,BMRB Entry Tracking System,125354,25243
BMRB,15948,"1H, 13C, and 15N Chemical Shift Assignments for the RING finger of the E3 ubiquitin ligase Arkadia (RNF111)",125403,25248
BMRB,25249,RING Finger monomer (W972A mutant),125403,25248
PDB,2KIZ,NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase.,125403,25248
PDB,5LG0,Solution NMR structure of Tryptophan to Alanine mutant of Arkadia RING domain,125403,25248
BMRB,15948,"1H, 13C, and 15N Chemical Shift Assignments for the RING finger of the E3 ubiquitin ligase Arkadia (RNF111)",125423,25249
BMRB,25248,RING Finger monomer (W972R mutant),125423,25249
PDB,2KIZ,NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase.,125423,25249
PDB,5LG0,W972A mutant of Arkadia (RNF111) E3 RING domain,125423,25249
BMRB,25251,PrPdelta193-196,125443,25250
GB,AJ000738.1,,125443,25250
GB,CAA04276.1,,125443,25250
PDB,2MV8,BMRB Entry Tracking System,125443,25250
BMRB,25250,PrPdelta190-197,125465,25251
GB,AJ000738.1,,125465,25251
GB,CAA04276.1,,125465,25251
PDB,2MV9,BMRB entry-tracking system,125465,25251
BMRB,18027,CaM bound to iNOS peptides,125486,25253
PDB,2MVA,BMRB Entry Tracking System,125501,25254
BMRB,18028,CaM bound to eNOS peptides,125518,25257
BMRB,25253,"Y99E,N111D CAM-iNOS",125518,25257
PDB,2MVB,BMRB Entry Tracking System,125533,25259
BMRB,25261,[GlnB22]-insulin mutant at pH 1.9,125551,25260
PDB,2MVC,BMRB Entry Tracking System,125551,25260
PDB,2hiu,,125551,25260
BMRB,25260,human insulin at pH 1.9,125569,25261
PDB,2MVD,BMRB Entry Tracking System,125569,25261
PDB,2mvc,human insulin at pH 1.9,125569,25261
PDB,2MVF,BMRB Entry Tracking System,125622,25265
PDB,2MVG,BMRB Entry Tracking System,125638,25266
BMRB,25270,SpoVM P9A mutant,125670,25268
PDB,2MVH,BMRB Entry Tracking System,125670,25268
PDB,2MVI,BMRB Entry Tracking System,125688,25269
BMRB,25268,SpoVM,125721,25270
PDB,2MVJ,BMRB Entry Tracking System,125721,25270
BMRB,15813,E. coli Trigger Factor (TF) Ribosome Binding Domain (RBD),125739,25271
BMRB,19835,E. coli Trigger Factor in complex with unfolded PhoA220-310,125739,25271
BMRB,19836,E. coli Trigger Factor in complex with unfolded PhoA1-150,125739,25271
BMRB,5298,PPIase,125739,25271
PDB,1l1p,,125739,25271
PDB,1w26,,125739,25271
PDB,2vrh,,125739,25271
BMRB,4417,,125756,25272
PDB,2MVK,BMRB Entry Tracking System,125770,25273
PDB,2MVL,BMRB Entry Tracking System,125785,25274
BMRB,25276,eEF1Bdelta CAR domain,125799,25275
PDB,2MVN,BMRB Entry Tracking System,125799,25275
BMRB,25275,eEF1Bdelta CAR domain,125818,25276
PDB,2MVN,BMRB Entry Tracking System,125818,25276
PDB,2MVO,BMRB Entry Tracking System,125837,25277
PDB,2MVQ,BMRB Entry Tracking System,125885,25280
NCBI,NP_668646.1,attachment invasion locus protein [Yersinia pestis KIM10+],125906,25281
PDB,2MVR,BMRB Entry Tracking System,125906,25281
PDB,2MVT,BMRB Entry Tracking System,125945,25283
BMRB,25287,5-phenyl-3-oxo-pentyl Actinorhodin Acyl Carrier Protein,125961,25284
PDB,2MVU,BMRB Entry Tracking System,125961,25284
BMRB,25286,HbI homodymer (in the unliganded state),125982,25285
BMRB,25285,HbI homodimer (bound to CO),126001,25286
BMRB,25284,"3,7-dioxo-octyl Actinorhodin Acyl Carrier Protein",126018,25287
PDB,2MVV,BMRB Entry Tracking System,126018,25287
PDB,2MVW,BMRB Entry Tracking System,126039,25288
PDB,2MVX,BMRB Entry Tracking System,126063,25289
BMRB,17064,,126098,25290
BMRB,18595,,126098,25290
DBJ,BAB74864,,126098,25290
PDB,1xio,,126098,25290
PDB,2m3g,,126098,25290
PDB,4tl3,,126098,25290
REF,NP_487205,,126098,25290
REF,WP_010997316,,126098,25290
PDB,2MVY,BMRB Entry Tracking System,126115,25291
PDB,2MW0,BMRB Entry Tracking System,126149,25293
PDB,2MW1,BMRB Entry Tracking System,126165,25294
BMRB,25323,13C6-15N5-ARG,126186,25295
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126186,25295
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126186,25295
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126186,25295
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126186,25295
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126186,25295
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126186,25295
BMRB,25316,ACE-ALA,126186,25295
BMRB,5166,Assigned Chemical shifts of unbound Hha,126204,25296
PDB,1NI8,Structure of unbound HNS46,126204,25296
PDB,1jw2,Structure of unbound Hha,126204,25296
PDB,2MW2,BMRB Entry Tracking System,126204,25296
PDB,2MW3,BMRB Entry Tracking System,126230,25297
PDB,2MW4,BMRB Entry Tracking System,126248,25298
PDB,1A5R,,126272,25299
PDB,2ASQ,,126272,25299
PDB,2MW5,BMRB Entry Tracking System,126272,25299
BMRB,2MW6,BMRB entry-tracking system,126299,25300
PDB,2MLT,native melittin in crystall,126299,25300
BMRB,25303,titin M10-obscurin-Ig1,126315,25301
BMRB,25304,obscurin Ig1 bound to titin M10,126315,25301
BMRB,25305,titin M10,126315,25301
BMRB,25308,obscurin Ig58,126315,25301
BMRB,25406,H56P mutant,126315,25301
PDB,2MW7,BMRB Entry Tracking System,126329,25302
BMRB,25301,OBSC-Ig1,126353,25303
BMRB,25304,obscurin Ig1 bound to titin M10,126353,25303
BMRB,25305,titin M10,126353,25303
BMRB,25308,obscurin Ig58,126353,25303
BMRB,25406,H56P mutant,126353,25303
BMRB,25301,OBSC-Ig1,126367,25304
BMRB,25303,titin M10-obscurin-Ig1,126367,25304
BMRB,25305,titin M10,126367,25304
BMRB,25308,obscurin Ig58,126367,25304
BMRB,25406,H56P mutant,126367,25304
BMRB,25301,OBSC-Ig1,126381,25305
BMRB,25303,titin M10-obscurin-Ig1,126381,25305
BMRB,25304,obscurin Ig1 bound to titin M10,126381,25305
BMRB,25308,obscurin Ig58,126381,25305
BMRB,25406,H56P mutant,126381,25305
PDB,2MW8,BMRB Entry Tracking System,126416,25307
BMRB,25301,OBSC-Ig1,126436,25308
BMRB,25303,titin M10-obscurin-Ig1,126436,25308
BMRB,25304,obscurin Ig1 bound to titin M10,126436,25308
BMRB,25305,titin M10,126436,25308
PDB,2MWC,BMRB Entry Tracking System,126436,25308
BMRB,25310,FBP28 WW2 mutant W457F,126450,25309
BMRB,25311,FBP28 WW2 mutant Y446L,126450,25309
BMRB,25313,FBP28 WW2 mutant Y438R DNDC,126450,25309
BMRB,25314,FBP28 WW2 mutant Y238R L453A DNDC,126450,25309
BMRB,25315,FBP28 WW2 mutant Y438R DN,126450,25309
PDB,2MW9,BMRB Entry Tracking System,126450,25309
BMRB,25309,"FBP28 WW2 , mutation Y438R",126467,25310
BMRB,25311,FBP28 WW2 mutant W457F,126467,25310
BMRB,25313,FBP28 WW2 mutant Y438R DNDC,126467,25310
BMRB,25314,FBP28 WW2 mutant Y238R L453A DNDC,126467,25310
BMRB,25315,FBP28 WW2 mutant Y438R DN,126467,25310
PDB,2MWA,BMRB Entry Tracking System,126467,25310
BMRB,25309,FBP28 WW2 mutant Y438R,126484,25311
BMRB,25310,FBP28 WW2 mutant Y446L,126484,25311
BMRB,25313,FBP28 WW2 mutant Y438R DNDC,126484,25311
BMRB,25314,FBP28 WW2 mutant Y238R L453A DNDC,126484,25311
BMRB,25315,FBP28 WW2 mutant Y438R DN,126484,25311
PDB,2MWB,BMRB Entry Tracking System,126484,25311
PDB,4d4w,SOLUTION STRUCTURE OF HUMAN MBD1 CXXC1 DOMAIN,126501,25312
BMRB,25309,FBP28 WW2 mutant Y438R,126539,25313
BMRB,25310,FBP28 WW2 mutant Y446L,126539,25313
BMRB,25311,FBP28 WW2 mutant W457F,126539,25313
BMRB,25314,FBP28 WW2 mutant Y238R L453A DNDC,126539,25313
BMRB,25315,FBP28 WW2 mutant Y438R DN,126539,25313
PDB,2MWD,BMRB Entry Tracking System,126539,25313
BMRB,25309,FBP28 WW2 mutant Y438R,126556,25314
BMRB,25310,FBP28 WW2 mutant Y446L,126556,25314
BMRB,25311,FBP28 WW2 mutant W457F,126556,25314
BMRB,25313,FBP28 WW2 mutant Y438R DNDC,126556,25314
BMRB,25315,FBP28 WW2 mutant Y438R DN,126556,25314
PDB,2MWE,BMRB Entry Tracking System,126556,25314
BMRB,25309,FBP28 WW2 mutant Y438R,126573,25315
BMRB,25310,FBP28 WW2 mutant Y446L,126573,25315
BMRB,25311,FBP28 WW2 mutant W457F,126573,25315
BMRB,25313,FBP28 WW2 mutant Y438R DNDC,126573,25315
BMRB,25314,FBP28 WW2 mutant Y238R L453A DNDC,126573,25315
PDB,2MWF,BMRB Entry Tracking System,126573,25315
BMRB,25323,13C6-15N5-ARG,126591,25316
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126591,25316
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126591,25316
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126591,25316
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126591,25316
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126591,25316
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126591,25316
BMRB,25295,ALA-NH2,126591,25316
BMRB,25323,13C6-15N5-ARG,126610,25317
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126610,25317
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126610,25317
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126610,25317
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126610,25317
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126610,25317
BMRB,25316,ACE-ALA,126610,25317
BMRB,25295,ALA-NH2,126610,25317
BMRB,25323,13C6-15N5-ARG,126629,25318
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126629,25318
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126629,25318
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126629,25318
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126629,25318
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126629,25318
BMRB,25316,ACE-ALA,126629,25318
BMRB,25295,ALA-NH2,126629,25318
BMRB,25323,13C6-15N5-ARG,126648,25319
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126648,25319
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126648,25319
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126648,25319
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126648,25319
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126648,25319
BMRB,25316,ACE-ALA,126648,25319
BMRB,25295,ALA-NH2,126648,25319
BMRB,25323,13C6-15N5-ARG,126667,25320
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126667,25320
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126667,25320
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126667,25320
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126667,25320
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126667,25320
BMRB,25316,ACE-ALA,126667,25320
BMRB,25295,ALA-NH2,126667,25320
BMRB,25323,13C6-15N5-ARG,126686,25321
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126686,25321
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126686,25321
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126686,25321
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126686,25321
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126686,25321
BMRB,25316,ACE-ALA,126686,25321
BMRB,25295,ALA-NH2,126686,25321
BMRB,25323,13C6-15N5-ARG,126705,25322
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126705,25322
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126705,25322
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126705,25322
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126705,25322
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126705,25322
BMRB,25316,ACE-ALA,126705,25322
BMRB,25295,ALA-NH2,126705,25322
BMRB,25322,ACE-GLY-LYS-GLY-NH2,126724,25323
BMRB,25321,ACE-GLY-TYR-GLY-NH2,126724,25323
BMRB,25320,ACE-GLY-CYS-GLY-NH2,126724,25323
BMRB,25319,ACE-GLY-HIS-GLY-NH2,126724,25323
BMRB,25318,ACE-GLY-GLU-GLY-NH2,126724,25323
BMRB,25317,ACE-GLY-ASP-GLY-NH2,126724,25323
BMRB,25316,ACE-ALA,126724,25323
BMRB,25295,ALA-NH2,126724,25323
PDB,2MWH,BMRB Entry Tracking System,126742,25324
PDB,2MWI,BMRB Entry Tracking System,126777,25326
BMRB,25329,HUB2,126816,25328
BMRB,25330,HUAB,126816,25328
BMRB,25328,HUA2,126832,25329
BMRB,25330,HUAB,126832,25329
BMRB,25328,HUA2,126847,25330
BMRB,25329,HUB2,126847,25330
BMRB,25332,"Family 1 Carbohydrate-Binding Module from Trichoderma reesei Cel7A with O-mannose residues at Thr1, Ser3, and Ser14",126865,25331
PDB,1CBH,C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I,126865,25331
PDB,2MWJ,BMRB Entry Tracking System,126865,25331
BMRB,25331,Family 1 Carbohydrate-Binding Module from Trichoderma reesei Cel7A with O-mannose residues at Thr1 and Ser3,126885,25332
PDB,1CBH,C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I,126885,25332
PDB,2MWK,BMRB Entry Tracking System,126885,25332
PDB,2MWL,BMRB Entry Tracking System,126935,25335
BMRB,25337,CypA+peptide,126949,25336
BMRB,25338,CypB+peptide,126949,25336
BMRB,25339,CypC+peptide,126949,25336
BMRB,25340,CypD+peptide,126949,25336
BMRB,25341,CypC,126949,25336
BMRB,25336,GeoCyp+peptide,126970,25337
BMRB,25338,CypB+peptide,126970,25337
BMRB,25339,CypC+peptide,126970,25337
BMRB,25340,CypD+peptide,126970,25337
BMRB,25341,CypC,126970,25337
BMRB,25336,GeoCyp+peptide,126991,25338
BMRB,25337,CypA+peptide,126991,25338
BMRB,25339,CypC+peptide,126991,25338
BMRB,25340,CypD+peptide,126991,25338
BMRB,25341,CypC,126991,25338
BMRB,25336,GeoCyp+peptide,127010,25339
BMRB,25337,CypA+peptide,127010,25339
BMRB,25338,CypB+peptide,127010,25339
BMRB,25340,CypD+peptide,127010,25339
BMRB,25341,CypC,127010,25339
BMRB,25336,GeoCyp peptide,127028,25340
BMRB,25337,CypA peptide,127028,25340
BMRB,25338,CypB peptide,127028,25340
BMRB,25339,CypC peptide,127028,25340
BMRB,25341,CypC,127028,25340
BMRB,25336,GeoCyp+peptide,127047,25341
BMRB,25337,CypA+peptide,127047,25341
BMRB,25338,CypB+peptide,127047,25341
BMRB,25339,CypC+peptide,127047,25341
BMRB,25340,CypD+peptide,127047,25341
PDB,3edo,,127067,25342
PDB,2MWM,BMRB Entry Tracking System,127067,25342
PDB,2MWN,BMRB Entry Tracking System,127089,25343
BMRB,25345,PfCDPK3 CLD(B),127110,25344
BMRB,25344,"CaM Tr2C, monomer",127127,25345
BMRB,25348,53BP1 tandem Tudor domains in complex with a p53K382me2 peptide,127158,25347
PDB,2MWO,BMRB Entry Tracking System,127158,25347
BMRB,25347,53BP1 tandem Tudor domains in complex with a p53K370me2 peptide,127186,25348
PDB,2MWP,BMRB Entry Tracking System,127186,25348
BMRB,17357,PsbQ protein,127232,25350
PDB,1VYK,X-Ray structure,127232,25350
PDB,2MWQ,BMRB Entry Tracking System,127232,25350
BMRB,15948,"1H, 13C and 15N Chemical Shift Assignments for the RING finger of the E3 ubiquitin ligase Arkadia (RNF111)",127251,25351
PDB,2KIZ,NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase,127251,25351
PDB,2MWR,BMRB Entry Tracking System,127269,25352
BMRB,25357,Y171W mutant of Adenylate Kinase,127283,25353
BMRB,25360,P177A mutant of Adenylate Kinase in complex with Ap5a,127283,25353
BMRB,25361,Y171W mutant of Adenylate Kinase in complex with Ap5a for state a,127283,25353
BMRB,25362,Y171W mutant of Adenylate Kinase in complex with Ap5a for state b,127283,25353
BMRB,25355,EphB2 kinase domain,127297,25354
BMRB,25356,TPMT *1 16-245,127297,25354
BMRB,25353,P177A mutant of Adenylate Kinase,127339,25357
BMRB,25360,P177A mutant of Adenylate Kinase in complex with Ap5a,127339,25357
BMRB,25361,Y171W mutant of Adenylate Kinase in complex with Ap5a for state a,127339,25357
BMRB,25362,Y171W mutant of Adenylate Kinase in complex with Ap5a for state b,127339,25357
BMRB,25353,P177A mutant of Adenylate Kinase,127385,25360
BMRB,25357,Y171W mutant of Adenylate Kinase,127385,25360
BMRB,25361,Y171W mutant of Adenylate Kinase in complex with Ap5a for state a,127385,25360
BMRB,25362,Y171W mutant of Adenylate Kinase in complex with Ap5a for state b,127385,25360
BMRB,25353,P177A mutant of Adenylate Kinase,127401,25361
BMRB,25357,Y171W mutant of Adenylate Kinase,127401,25361
BMRB,25360,P177A mutant of Adenylate Kinase in complex with Ap5a,127401,25361
BMRB,25362,Y171W mutant of Adenylate Kinase in complex with Ap5a for state b,127401,25361
BMRB,25353,P177A mutant of Adenylate Kinase,127417,25362
BMRB,25357,Y171W mutant of Adenylate Kinase,127417,25362
BMRB,25360,P177A mutant of Adenylate Kinase in complex with Ap5a,127417,25362
BMRB,25361,Y171W mutant of Adenylate Kinase in complex with Ap5a for state a,127417,25362
BMRB,25366,crotalicidin Nt,127433,25363
BMRB,25370,Crotalicidin Ct,127433,25363
PDB,2MWT,BMRB Entry Tracking System,127433,25363
BMRB,25365,drosophila histone mRNA stem-loop-binding protein,127453,25364
BMRB,25364,drosophila stem-loop binding protein complexed with histone mRNA stem-loop,127468,25365
BMRB,25363,1H and 13C chemical shift assignments for wild type crotalicidin in DPC micelles,127482,25366
BMRB,25370,1H and 13C chemical shift assignments for crotalicidin-Ct in DPC micelles,127482,25366
PDB,2MWT,NMR structure of wild type crotalicidin in DPC micelles,127482,25366
PDB,2XEX,Structure of Staphylococcus aureus EF-G.,127517,25368
PDB,2MWU,BMRB Entry Tracking System,127532,25369
BMRB,25363,1H and 13C chemical shift assignments for wild type crotalicidin in DPC micelles,127552,25370
BMRB,25366,1H and 13C chemical shift assignments for Crotalicidin-Nt in DPC micelles,127552,25370
PDB,2MWT,NMR structure of wild type crotalicidin in DPC micelles,127552,25370
PDB,4d7x,PDBe Entry of CG KIX,127570,25372
BMRB,19223,PTP1B (residues 1-301),127609,25375
BMRB,19224,PTP1B (residues 1-393),127609,25375
PDB,2MWX,BMRB Entry Tracking System,127626,25376
PDB,2MWY,BMRB Entry Tracking System,127647,25377
PDB,2GKU,unmodified G-quadruplex reference,127663,25378
PDB,2MWZ,BMRB Entry Tracking System,127663,25378
PDB,2MX0,BMRB Entry Tracking System,127699,25380
PDB,2MX1,BMRB Entry Tracking System,127713,25381
PDB,2MX2,BMRB Entry Tracking System,127733,25382
REF,YP_108067,,127823,25387
BMRB,25390,holo-axxa_cytc,127839,25389
BMRB,25389,holo-wt-cytc,127873,25390
PDB,25457,Cullin3 - BTB interface (two MK8 residues at 9 and 13),128983,25456
PDB,2MYL,BMRB Entry Tracking System,128983,25456
BMRB,6033,"Assignments for 1H and 15N have been deposited. The chemical shift file being uploaded now has revised 1HN and 15N assignments for residues 3, 4, 36, 51 and 59.",127873,25390
PDB,2MX6,BMRB Entry Tracking System,127923,25394
PDB,2MX7,BMRB Entry Tracking System,127939,25395
BMRB,25398,N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 5.5,127972,25397
PDB,2MX8,BMRB Entry Tracking System,127972,25397
BMRB,25397,N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2,127991,25398
PDB,2MX9,BMRB Entry Tracking System,127991,25398
BMRB,26576,"1H, 15N, resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions",128012,25399
PDB,2MXC,BMRB Entry Tracking System,128075,25402
PDB,2MXD,BMRB Entry Tracking System,128106,25404
PDB,2MXE,BMRB Entry Tracking System,128120,25405
BMRB,25301,OBSC-Ig1,128135,25406
BMRB,25303,titin M10-obscurin-Ig1,128135,25406
BMRB,25304,obscurin Ig1 bound to titin M10,128135,25406
BMRB,25305,titin M10,128135,25406
BMRB,25308,obscurin Ig58,128135,25406
BMRB,25405,C-terminal domain of MvaT,128149,25407
PDB,2MXF,BMRB Entry Tracking System,128149,25407
PDB,2MXG,BMRB Entry Tracking System,128165,25408
PDB,2MXH,"VG16KRKP, an antimicrobial peptide in SDS",128165,25408
BMRB,25409,"VG16KRKP, an antimicrobial peptide in SDS",128165,25408
PDB,2MXH,BMRB Entry Tracking System,128179,25409
PDB,2MXG,"VG16KRKP, an antimicrobial peptide in D8PG micelles",128179,25409
BMRB,25408,"VG16KRKP, an antimicrobial peptide in D8PG micelles",128179,25409
PDB,2MXI,BMRB Entry Tracking System,128209,25411
BMRB,25415,3 splice site influenza A: 19-nt duplex,128242,25414
BMRB,25416,3' splice site in influenza A: 39-nt hairpin,128242,25414
PDB,2MXJ,BMRB Entry Tracking System,128242,25414
BMRB,25414,3 splice site influenza A: 11-nt hairpin,128264,25415
BMRB,25416,3' splice site in influenza A: 39-nt hairpin,128264,25415
PDB,2MXK,BMRB Entry Tracking System,128264,25415
BMRB,25414,3 splice site influenza A: 11-nt hairpin,128285,25416
BMRB,25415,3 splice site influenza A: 19-nt duplex,128285,25416
PDB,2MXL,BMRB Entry Tracking System,128285,25416
PDB,4S16,Crystal structure,128303,25417
BMRB,25420,Human Cytochrome c G41S mutant (ferrous),128318,25418
BMRB,25422,Human Cytochrome c G41S mutant (ferric),128318,25418
BMRB,5406,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for ferrous Human Cytochrome c",128318,25418
PDB,3ZCF,Structure for ferric human Cyt c,128318,25418
PDB,2MXM,BMRB Entry Tracking System,128338,25419
BMRB,25422,human Cyt c G41S mutant (ferric),128368,25420
BMRB,25031,Wild type Hhn2b,128389,25421
PDB,2MQF,Wild type Hhn2b,128389,25421
PDB,2MXO,BMRB Entry Tracking System,128389,25421
BMRB,25420,human Cyt c G41S mutant (ferrous),128408,25422
PDB,2MXP,BMRB Entry Tracking System,128430,25423
PDB,4XKL,Crystal structure of NDP52 ZF2 in complex with mono-ubiquitin,128430,25423
PDB,2MXQ,BMRB Entry Tracking System,128452,25424
PDB,2KXM,Solution NMR Structure of the 27 nucleotide engineered neomycin sensing riboswitch RNA-ribostmycin complex,128507,25427
PDB,2MXS,BMRB Entry Tracking System,128507,25427
PDB,2MXT,BMRB Entry Tracking System,128538,25428
PDB,2MXU,BMRB Entry Tracking System,128552,25429
EMBL,AJ249115.1,,128583,25432
PDB,2MXV,BMRB Entry Tracking System,128600,25433
PDB,2MXW,BMRB Entry Tracking System,128620,25434
PDB,2MXX,BMRB Entry Tracking System,128637,25435
PDB,2MXY,BMRB Entry Tracking System,128656,25436
NCBI,AAS19387.1,,128679,25437
PDB,2MXZ,BMRB Entry Tracking System,128679,25437
BMRB,25440,Bud31p protein (Cd3),128695,25439
PDB,2MY1,BMRB Entry Tracking System,128695,25439
PDB,25439,Bud31p protein,128717,25440
PDB,2MY1,Bud31p protein,128717,25440
BMRB,19766,Heterotrimeric pre-mRNA Retention and Splicing Complex,128753,25442
BMRB,25443,Snu17p-Pml1p structure intermediate during RES complex assembly,128753,25442
PDB,2MKC,,128753,25442
BMRB,19766,Heterotrimeric pre-mRNA Retention and Splicing Complex,128777,25443
BMRB,25442,Heterodimeric complex composed of Snu17p/Ist3p(25-138) and Bud13p(215 255),128777,25443
BMRB,2MY2,Heterodimeric complex composed of Snu17p/Ist3p(25-138) and Bud13p(215 255),128777,25443
PDB,2MKC,,128777,25443
PDB,2MY3,BMRB Entry Tracking System,128777,25443
PDB,2MY5,BMRB Entry Tracking System,128815,25446
PDB,2MY6,BMRB Entry Tracking System,128831,25447
PDB,2my0,Entry containing the same protein in two state,128831,25447
PDB,2MY9,BMRB Entry Tracking System,128845,25448
PDB,2lkt,Solution structure of N-terminal domain of human TIG3 in 2 M UREA,128845,25448
NCBI,XP_002809024.1,RRM containing cyclophilin [Plasmodium falciparum 3D7],128870,25449
PDB,2MYF,BMRB Entry Tracking System,128870,25449
PDB,2MYG,BMRB Entry Tracking System,128889,25451
GB,KP308197,Sequence of the gene of precursor protein of the polypeptide toxin omega-Tbo-IT1,128910,25452
PDB,2MYH,BMRB Entry Tracking System,128910,25452
PDB,2YRO,Solution structure of the C-terminal Gal-bind lectin protein from Human Galectin-8,128930,25453
PDB,3OJB,Crystal structure of C-terminal domain of human galectin-8,128930,25453
PDB,3VKL,Protease-resistant mutant form of human Galectin-8 in complex with two lactose molecules,128930,25453
PDB,4GXL,The crystal structure of Galectin-8 C-CRD in complex with NDP52,128930,25453
PDB,2MYJ,BMRB Entry Tracking System,128947,25454
PDB,2MYM,Cullin3 - BTB interface (two MK8 residues at 9 and 13),128983,25456
PDB,25456,Cullin3 - BTB interface (two MK8 residues at 8 and 12),128998,25457
PDB,2MYL,Cullin3 - BTB interface (two MK8 residues at 8 and 12),128998,25457
PDB,2MYM,BMRB Entry Tracking System,128998,25457
PDB,2MYQ,BMRB Entry Tracking System,129013,25458
BMRB,25460,Fungus protein B9WZW9_MAGOR,129031,25459
PDB,2MYV,BMRB Entry Tracking System,129031,25459
BMRB,25459,Fungus protein Q8J180_MAGGR,129066,25460
PDB,2MYW,BMRB Entry Tracking System,129066,25460
PDB,2MYX,BMRB entry-tracking system,129087,25461
SGD,S000004877,Endoplasmic reticulum membrane protein that recruits the ubiquitin-conjugating enzyme Ubc7 to the ER where it functions in protein degradation; contains a CUE domain that binds ubiquitin to facilitate intramolecular monoubiquitination.,129087,25461
BMRB,25463,NS1B ED wild-type,129108,25462
BMRB,25462,NS1B ED mutant monomer,129127,25463
PDB,2MYY,BMRB Entry Tracking System,129146,25464
PDB,2MYZ,BMRB Entry Tracking System,129166,25465
PDB,2MZ0,BMRB Entry Tracking System,129216,25468
PDB,2MZ1,BMRB Entry Tracking System,129235,25469
PDB,25471,IL4pSER415,129269,25470
PDB,25478,IL4pSER411,129269,25470
PDB,2B0Y,Solution Structure of a peptide mimetic of the fourth cytoplasmic loop of the G-protein coupled CB1 cannabinoid receptor,129269,25470
PDB,2MZ2,BMRB Entry tracking System,129269,25470
BMRB,25470,IL4pSER402,129284,25471
BMRB,25478,IL4pSER411,129284,25471
PDB,2B0Y,Solution Structure of a peptide mimetic of the fourth cytoplasmic loop of the G-protein coupled CB1 cannabinoid receptor,129284,25471
PDB,2MZ3,BMRB Entry tracking System,129284,25471
PDB,2MZ4,BMRB Entry Tracking System,129298,25472
SGD,PCF11,Protein 1 of Cleavage and polyadenylation Factor I,129312,25473
SP,P39081,PCF11 YEAST,129312,25473
PDB,2MZ6,BMRB Entry Tracking System,129334,25474
PDB,2MNK,Structure of Tau(162-188) bound to Microtubules,129350,25475
PDB,2MNL,Structure of Tau(211-242) bound to Microtubules,129350,25475
PDB,2MNM,"Structure of     
Tau(239-267) bound to Microtubules",129350,25475
PDB,2MNN,"Structure of Tau(265-290)     
bound to Microtubules",129350,25475
PDB,2MNO,"Structure of Tau(296-321) bound to     
Microtubules",129350,25475
PDB,2MNP,Structure of Tau(368-402) bound to Microtubules,129350,25475
PDB,2MZ7,BMRB entry-tracking system,129350,25475
NCBI,99287,taxonomic identifier,129369,25476
PDB,2MZ8,BMRB Entry Tracking System,129369,25476
SP,Q7CR52,uniprot description,129369,25476
PDB,2MZ9,BMRB Entry Tracking System,129391,25477
BMRB,25470,IL4pSER402,129410,25478
BMRB,25471,IL4pSER415,129410,25478
PDB,2B0Y,Solution Structure of a peptide mimetic of the fourth cytoplasmic loop of the G-protein coupled CB1 cannabinoid receptor,129410,25478
PDB,2MZA,BMRB Entry Tracking System,129410,25478
PDB,2mz2,"Phosphorylation of CB1Cannabinoid Receptor Fourth Intracellular Loop Peptides:                 
Effects on Structure and Function",129410,25478
PDB,2mz3,"Phosphorylation of CB1Cannabinoid Receptor Fourth Intracellular Loop Pepducins:                
Effects on Structure and Function",129410,25478
PDB,4R62,,129424,25479
PDB,2MZB,BMRB Entry Tracking System,129455,25482
PDB,2MZC,BMRB Entry Tracking System,129480,25483
PDB,2K8F,Structural Basis for p300 Taz2-p53 TAD1 Binding and Modulation by Phosphorylation.,129499,25484
PDB,2MZD,BMRB Entry Tracking System,129499,25484
PDB,1mmp,"Active, inhibitor-bound crystal structure, 2.3A",129524,25485
PDB,1mmq,"Active, inhibitor-bound crystal structure, 1.9A",129524,25485
PDB,1mmr,"Active, inhibitor-bound crystal structure, 2.4A",129524,25485
PDB,2MZE,BMRM Entry Tracking System,129524,25485
PDB,2y6c,"Active, inhibitor-bound crystal structure, 1.7A",129524,25485
PDB,2y6d,"Active, inhibitor-bound crystal structure, 1.6A",129524,25485
BMRB,25487,Purotoxin-2 in DPC micelles,129548,25486
PDB,2MZF,BMRB Entry Tracking System,129548,25486
PDB,2MZG,Purotoxin-2 in DPC micelles,129548,25486
BMRB,25486,Purotoxin-2 in water,129565,25487
PDB,2MZF,Purotoxin-2 in water,129565,25487
PDB,2MZG,BMRB Entry Tracking System,129565,25487
BMRB,25485,Solution structure of uncomplexed form,129582,25488
BMRB,25489,PRO Form of Human Matrilysin (proMMP-7) in Complex with Anionic Membrane,129582,25488
BMRB,2MZH,BMRB entry-tracking system,129582,25488
PDB,2MZE,Solution structure of uncomplexed form,129582,25488
BMRB,25485,Solution structure of uncomplexed form.,129606,25489
BMRB,25488,Solution structure of complexed form to zwitterionic membrane.,129606,25489
BMRB,2MZI,BMRB entry-tracking system,129606,25489
PDB,2mze,Solution structure of uncomplexed form.,129606,25489
PDB,2mzh,Solution structure of complexed form to zwitterionic membrane.,129606,25489
PDB,2MZK,BMRB Entry Tracking System,129632,25490
PDB,2MZL,BMRB Entry Tracking System,129652,25491
PDB,2MZN,BMRB Entry Tracking System,129672,25492
PDB,5ODD,OneDep system,129691,25493
PDB,2MZP,BMRB Entry Tracking System,129729,25495
BMRB,25497,RRM1 domain of Hrb1,129756,25496
BMRB,25498,RRM2 domain of Hrb1,129756,25496
BMRB,25499,RRM3 domain of Hrb1,129756,25496
PDB,2MZQ,BMRB Entry Tracking System,129756,25496
BMRB,25496,RRM3 domain of Gbp2,129775,25497
BMRB,25498,RRM2 domain of Hrb1,129775,25497
BMRB,25499,RRM3 domain of Hrb1,129775,25497
PDB,2MZR,BMRB Entry Tracking System,129775,25497
BMRB,25496,RRM3 domain of Gbp2,129794,25498
BMRB,25497,RRM1 domain of Hrb1,129794,25498
BMRB,25499,RRM3 domain of Hrb1,129794,25498
PDB,2MZS,BMRB Entry Tracking System,129794,25498
BMRB,25496,RRM3 domain of Gbp2,129813,25499
BMRB,25497,RRM1 domain of Hrb1,129813,25499
BMRB,25498,RRM2 domain of Hrb1,129813,25499
PDB,2MZT,BMRB Entry Tracking System,129813,25499
BMRB,25501,SH2-SH3 adapter protein drk,129845,25500
PDB,25500,SH2-SH3 adapter protein drk (in the presence of DnaK chaperone),129863,25501
PDB,2MZU,BMRB Entry Tracking System,129879,25502
BMRB,17503,S. aureus FusB assigned chemical shifts in the apo state.,129895,25504
BMRB,25368,S. aureus EF-GC3 assigned chemical shifts in the apo state.,129895,25504
PDB,2MZW,BMRB Entry Tracking System,129895,25504
PDB,2XEX,Crystal structure of S. aureus EF-G.,129895,25504
PDB,4ADN,Crystal structure of S. aureus FusB.,129895,25504
PDB,2MZX,BMRB Entry Tracking System,129931,25505
BMRB,25507,Linear SDPhe-TATE,129945,25506
BMRB,25738,Re-SDPhe-TATE isomer 2,129945,25506
BMRB,25739,Re-SDPhe-TATE isomer 4,129945,25506
BMRB,25506,Re-SDPhe-TATE isomer 1,129965,25507
BMRB,25738,Re-SDPhe-TATE isomer 2,129965,25507
BMRB,25739,Re-SDPhe-TATE isomer 4,129965,25507
PDB,2MZY,BMRB Entry Tracking System,129982,25508
PDB,2MZZ,BMRB Entry Tracking System,130001,25509
PDB,2N00,BMRB Entry Tracking System,130049,25510
BMRB,25034,cChimera Ca2+ bound,130063,25511
BMRB,25035,cChimeraX Ca2+ bound,130063,25511
BMRB,25495,"cNTnC-cTnIA162H, chemical shifts",130063,25511
PDB,2MZP,cNTnC-cTnIA162H structure,130063,25511
BMRB,17257,NMR structure of VirB7 from Xanthomonas citri,130087,25512
PDB,2L4W,NMR structure of VirB7 from Xanthomonas citri,130087,25512
PDB,2N01,BMRB Entry Tracking System,130087,25512
PDB,2MGY,,130109,25513
PDB,2N02,BMRB Entry Tracking System,130109,25513
BMRB,25515,,130132,25514
PDB,2N04,BMRB Entry Tracking System,130132,25514
PDB,2N05,BMRB Entry Tracking System,130150,25515
PDB,2N07,BMRB Entry Tracking System,130167,25516
BMRB,26536,"Short hydrophobic peptide, 11mer, H(AIB)EGTFTSDFF",130184,25517
BMRB,26537,"Short hydrophobic peptide, 11mer, H(AIB)EGKFTSEF(PH8)",130184,25517
BMRB,26538,"Short hydrophobic peptide, 11mer, H(KCY)EG(HCS)FTSDF(PH8)",130184,25517
PDB,2N08,BMRB Entry Tracking System,130184,25517
PDB,2N0A,BMRB Entry Tracking System,130199,25518
BMRB,25520,Neuromedin C in 10% TFE,130222,25519
BMRB,25521,Neuromedin C in 25% TFE,130222,25519
BMRB,25522,Neuromedin C in 40% TFE,130222,25519
BMRB,25523,Neuromedin C in 60% TFE,130222,25519
BMRB,25524,Neuromedin C in 90% TFE,130222,25519
BMRB,25525,Neuromedin C in presence of SDS micelles,130222,25519
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130222,25519
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130222,25519
PDB,2N0B,BMRB Entry Tracking System,130222,25519
BMRB,25519,Neuromedin C in aqueous solution,130242,25520
BMRB,25521,Neuromedin C in 25% TFE,130242,25520
BMRB,25522,Neuromedin C in 40% TFE,130242,25520
BMRB,25523,Neuromedin C in 60% TFE,130242,25520
BMRB,25524,Neuromedin C in 90% TFE,130242,25520
BMRB,25525,Neuromedin C in presence of SDS micelles,130242,25520
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130242,25520
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130242,25520
PDB,2N0C,BMRB Entry Tracking System,130242,25520
BMRB,25519,Neuromedin C in aqueous solution,130259,25521
BMRB,25520,Neuromedin C in 10% TRE,130259,25521
BMRB,25522,Neuromedin C in 40% TRE,130259,25521
BMRB,25523,Neuromedin C in 60% TRE,130259,25521
BMRB,25524,Neuromedin C in 90% TRE,130259,25521
BMRB,25525,Neuromedin C in presence of SDS micelles,130259,25521
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130259,25521
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130259,25521
PDB,2N0D,BMRB Entry Tracking System,130259,25521
BMRB,25519,Neuromedin C in aqueous solutions,130276,25522
BMRB,25520,Neuromedin C in 10% TFE,130276,25522
BMRB,25521,Neuromedin C in 25% TFE,130276,25522
BMRB,25523,Neuromedin C in 60% TFE,130276,25522
BMRB,25524,Neuromedin C in 90% TFE,130276,25522
BMRB,25525,Neuromedin C in presence of SDS micelles,130276,25522
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130276,25522
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130276,25522
PDB,2N0E,BMRB Entry Tracking System,130276,25522
BMRB,25519,Neuromedin C in aqueous solution,130293,25523
BMRB,25520,Neuromedin C in 10% TFE,130293,25523
BMRB,25521,Neuromedin C in 25% TFE,130293,25523
BMRB,25522,Neuromedin C in 40% TFE,130293,25523
BMRB,25524,Neuromedin C in 90% TFE,130293,25523
BMRB,25525,Neuromedin C in presence of SDS micelles,130293,25523
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130293,25523
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130293,25523
PDB,2N0F,BMRB entry-tracking system,130293,25523
BMRB,25519,Neuromedin C in aqueous solution,130313,25524
BMRB,25520,Neuromedin C in 10% TFE,130313,25524
BMRB,25521,Neuromedin C in 25% TFE,130313,25524
BMRB,25522,Neuromedin C in 40% TFE,130313,25524
BMRB,25523,Neuromedin C in 60% TFE,130313,25524
BMRB,25525,Neuromedin C in presence of SDS micelles,130313,25524
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130313,25524
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130313,25524
PDB,2N0G,BMRB Entry Tracking System,130313,25524
BMRB,25519,Neuromedin C in aqueous solution,130330,25525
BMRB,25520,Neuromedin C in 10% TFE,130330,25525
BMRB,25521,Neuromedin C in 25% TFE,130330,25525
BMRB,25522,Neuromedin C in 40% TFE,130330,25525
BMRB,25523,Neuromedin C in 60% TFE,130330,25525
BMRB,25524,Neuromedin C in 90% TFE,130330,25525
PDB,1C98,SOLUTION STRUCTURE OF NEUROMEDIN B,130330,25525
PDB,1C9A,SOLUTION STRUCTURE OF NEUROMEDIN B,130330,25525
PDB,2N0H,BMRB Entry Tracking System,130330,25525
BMRB,16609,"1H, 13C, 15N, 31P chemical shift deposition",130352,25526
PDB,2N0J,BMRB entry-tracking system,130352,25526
PDB,2N0K,BMRB Entry Tracking System,130383,25527
BMRB,25369,,130414,25528
PDB,2MWU,BMRB Entry Tracking System,130414,25528
PDB,2N0O,BMRB Entry Tracking System,130435,25529
PDB,2N0Q,BMRB Entry Tracking System,130471,25531
PDB,2N0R,BMRB Entry Tracking System,130525,25534
BMRB,25546,MDMX-295,130554,25536
PDB,2N0U,BMRB Entry Tracking System,130554,25536
PDB,2N14,MDMX-295,130554,25536
PDB,2N0V,BMRB Entry Tracking System,130573,25537
PDB,2N0W,BMRB Entry Tracking System,130590,25538
PDB,2N0X,BMRB Entry Tracking System,130609,25539
BMRB,18229,,130625,25540
BMRB,18842,,130625,25540
BMRB,6225,,130625,25540
PDB,1y5o,,130625,25540
PDB,2N0Y,BMRB Entry Tracking System,130625,25540
PDB,2lox,,130625,25540
PDB,2m14,,130625,25540
REF,NP_010597,,130625,25540
REF,YP_003848706,,130625,25540
SP,P21698,,130625,25540
SP,P32776,,130625,25540
BMRB,25542,MyUb (1080-1131) of human Myosin VI,130648,25541
BMRB,25543,human Myosin VI isoform3 (998-1071),130648,25541
BMRB,25544,human Myosin VI isoform3 (1050-1131),130648,25541
BMRB,25545,MyUb (1080-1122) of human Myosin VI with K63-diUb,130648,25541
PDB,2N0Z,BMRB Entry Tracking System,130648,25541
BMRB,25541,MyUb (1080-1122) of human Myosin VI,130665,25542
BMRB,25543,human Myosin VI isoform3 (998-1071),130665,25542
BMRB,25544,human Myosin VI isoform3 (1050-1131),130665,25542
BMRB,25545,MyUb (1080-1122) of human Myosin VI with K63-diUb,130665,25542
PDB,2N10,BMRB Entry Tracking System,130665,25542
BMRB,25541,MyUb (1080-1122) of human Myosin VI,130682,25543
BMRB,25542,MyUb (1080-1131) of human Myosin VI,130682,25543
BMRB,25544,human Myosin VI isoform3 (1050-1131),130682,25543
BMRB,25545,MyUb (1080-1122) of human Myosin VI with K63-diUb,130682,25543
PDB,2N11,BMRB Entry Tracking System,130682,25543
BMRB,25541,MyUb (1080-1122) of human Myosin VI,130700,25544
BMRB,25542,MyUb (1080-1131) of human Myosin VI,130700,25544
BMRB,25543,human Myosin VI isoform3 (998-1071),130700,25544
BMRB,25545,MyUb (1080-1122) of human Myosin VI with K63-diUb,130700,25544
PDB,2N12,BMRB Entry Tracking System,130700,25544
BMRB,25541,MyUb (1080-1122) of human Myosin VI,130717,25545
BMRB,25542,MyUb (1080-1131) of human Myosin VI,130717,25545
BMRB,25543,human Myosin VI isoform3 (998-1071),130717,25545
BMRB,25544,human Myosin VI isoform3 (1050-1131),130717,25545
PDB,2N13,BMRB Entry Tracking System,130717,25545
BMRB,25536,MDMX-057,130736,25546
PDB,2N0U,MDMX-057,130736,25546
PDB,2N14,BMRB Entry Tracking System,130736,25546
PDB,2N16,BMRB Entry Tracking System,130755,25548
PDB,2N18,BMRB Entry Tracking System,130785,25551
BMRB,26547,STIL binding to the Polo-box 3 of PLK4 regulates centriole duplication - Backbone assignment of human Polo-box 3 bound to STIL,130808,25552
PDB,2N19,BMRB Entry Tracking System,130808,25552
PDB,4YYP,Crystal structure of human PLK4-PB3 in complex with STIL-CC,130808,25552
PDB,2N1A,BMRB Entry Tracking System,130828,25553
PDB,2N1B,BMRB Entry Tracking System,130846,25554
PDB,2N1C,BMRB Entry Tracking System,130860,25555
PDB,2LKM,Same MRG domain in complex with another protein,130877,25556
PDB,2N1D,BMRB Entry Tracking System,130877,25556
BMRB,25566,Same protein but in the reduced state.,130898,25557
PDB,2N1E,BMRB Entry Tracking System,130915,25558
PDB,2N1G,BMRB Entry Tracking System,130942,25559
PDB,2N1H,BMRB Entry Tracking System,130962,25560
BMRB,25564,Third Type III domain from Human Fibronectin,130990,25562
PDB,2N1I,BMRB Entry Tracking System,130990,25562
BMRB,25562,PR domain from PRDM16,131014,25564
PDB,2N1K,BMRB Entry Tracking System,131014,25564
PDB,2N1L,BMRB Entry Tracking System,131039,25565
PDB,4HPM,,131039,25565
BMRB,25557,Same protein but in the oxidized state.,131057,25566
PDB,2N1M,BMRB Entry Tracking System,131074,25567
PDB,1S6X,Solution structure of VSTx1,131092,25568
PDB,2N1N,BMRB Entry Tracking System,131092,25568
PDB,2N1O,BMRB Entry Tracking System,131110,25569
PDB,2N1P,BMRB Entry Tracking System,131129,25570
PDB,2N1Q,BMRB Entry Tracking System,131147,25571
PDB,2N1R,BMRB Entry Tracking System,131199,25573
GB,CBJ21249,AMP-2 precursor,131223,25574
PDB,2N1S,BMRB Entry Tracking System,131223,25574
PDB,2N1U,BMRB Entry Tracking System,131247,25575
BMRB,6304,Amide chemical shifts of mature human SUMO-1,131266,25576
PDB,1A5R,,131266,25576
PDB,2N1V,BMRB Entry Tracking System,131266,25576
BMRB,25576,human SUMO1,131289,25577
BMRB,6801,human SUMO-2,131289,25577
PDB,1WM3,,131289,25577
PDB,2N1W,BMRB Entry Tracking System,131289,25577
PDB,2N21,BMRB Entry Tracking System,131312,25582
BMRB,25583,complex between the PH domain of the Tfb1 subunit from TFIIH and the transactivation domain of p65,131328,25584
BMRB,6225,Chemical shifts of free Tfb1,131328,25584
PDB,1y5o,NMR structure of free Tfb1,131328,25584
PDB,2N23,BMRB Entry Tracking System,131328,25584
PDB,2l2i,NMR structure of Tfb1 in complex with activation domain of EKLF (TAD2),131328,25584
PDB,2N24,BMRB Entry Tracking System,131347,25585
BMRB,25676,mutant NS4A N-terminal domain,131365,25586
PDB,2N27,BMRB Entry Tracking System,131414,25588
BMRB,25592,Vpu cytoplasmic domain,131454,25591
PDB,2N28,BMRB Entry Tracking System,131454,25591
BMRB,25591,Vpu from HIV-1,131470,25592
PDB,2N29,BMRB Entry Tracking System,131470,25592
PDB,2N2A,BMRB Entry Tracking System,131487,25593
PDB,2N2C,BMRB Entry Tracking System,131506,25595
PDB,2N2D,BMRB Entry Tracking System,131521,25596
PDB,2N2F,BMRB Entry Tracking System,131542,25597
PDB,2N2G,BMRB Entry Tracking System,131561,25598
PDB,2N2H,BMRB Entry Tracking System,131577,25599
PDB,2N2I,BMRB Entry Tracking System,131607,25600
PDB,1UBQ,Starting structure for each subunit in the ensemble refinement,131621,25601
PDB,2N2K,BMRB Entry Tracking System,131621,25601
PDB,3H7P,Lys63-linked diubiquitin in the open state,131621,25601
BMRB,26574,GAT apo state,131649,25602
PDB,2N2N,BMRB Entry Tracking System,131649,25602
BMRB,25604,double base-pair inversion mutant of murine tumour necrosis factor alpha CDE-23 RNA,131664,25603
PDB,2N2O,BMRB Entry Tracking System,131664,25603
PDB,2N2P,double base-pair inversion mutant of murine tumour necrosis factor alpha CDE-23 RNA,131664,25603
BMRB,25603,murine tumour necrosis factor alpha CDE RNA,131685,25604
PDB,2N2O,murine tumour necrosis factor alpha CDE RNA,131685,25604
PDB,2N2P,BMRB Entry Tracking System,131685,25604
BMRB,25609,NMR solution structure of RsAFP2,131706,25605
PDB,2N2Q,BMRB Entry Tracking System,131706,25605
BMRB,25607,human Androgen Receptor-25Q,131724,25606
BMRB,25608,"human Androgen Receptor-4Q, at 308K",131724,25606
BMRB,25606,"human Androgen Receptor-4Q, at 278K",131740,25607
BMRB,25608,"human Androgen Receptor-4Q, at 308K",131740,25607
BMRB,25605,NMR solution structure of HsAFP1,131756,25609
PDB,2N2R,BMRB Entry Tracking System,131756,25609
PDB,2N2S,BMRB Entry Tracking System,131773,25610
BMRB,25612,,131791,25611
PDB,2N2T,BMRB Entry Tracking System,131791,25611
PDB,2N2U,BMRB Entry Tracking System,131818,25612
PDB,2N2V,BMRB Entry Tracking System,131851,25613
PDB,2N2W,BMRB Entry Tracking System,131868,25614
BMRB,25613,Solution structure of [B26-B29 triazole cross-linked]-insulin analogue at pH 1.9,131885,25615
BMRB,25614,Solution structure of [B26-B29 triazole cross-linked]-insulin analogue at pH 8.0,131885,25615
PDB,2N2X,BMRB Entry Tracking System,131885,25615
BMRB,25617,dimeric KaiB bound to CI,131902,25616
BMRB,25618,N-SasA,131902,25616
BMRB,25619,N-SasA bound to CI,131902,25616
BMRB,25620,G89A single mutant of dimeric KaiB,131902,25616
BMRB,25621,D91R single mutant of dimeric KaiB,131902,25616
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131902,25616
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131902,25616
BMRB,25624,"G89A,D91R double mutant of KaiB",131902,25616
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131902,25616
BMRB,25626,"G88A,D90R double mutant of KaiB",131902,25616
BMRB,25616,KaiB dimer,131918,25617
BMRB,25618,N-SasA,131918,25617
BMRB,25619,N-SasA bound to CI,131918,25617
BMRB,25620,G89A single mutant of dimeric KaiB,131918,25617
BMRB,25621,D91R single mutant of dimeric KaiB,131918,25617
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131918,25617
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131918,25617
BMRB,25624,"G89A,D91R double mutant of KaiB",131918,25617
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131918,25617
BMRB,25626,"G88A,D90R double mutant of KaiB",131918,25617
BMRB,25616,KaiB dimer,131935,25618
BMRB,25617,dimeric KaiB bound to CI,131935,25618
BMRB,25619,N-SasA bound to CI,131935,25618
BMRB,25620,G89A single mutant of dimeric KaiB,131935,25618
BMRB,25621,D91R single mutant of dimeric KaiB,131935,25618
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131935,25618
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131935,25618
BMRB,25624,"G89A,D91R double mutant of KaiB",131935,25618
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131935,25618
BMRB,25626,"G88A,D90R double mutant of KaiB",131935,25618
BMRB,25616,KaiB dimer,131951,25619
BMRB,25617,dimeric KaiB bound to CI,131951,25619
BMRB,25618,N-SasA,131951,25619
BMRB,25620,G89A single mutant of dimeric KaiB,131951,25619
BMRB,25621,D91R single mutant of dimeric KaiB,131951,25619
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131951,25619
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131951,25619
BMRB,25624,"G89A,D91R double mutant of KaiB",131951,25619
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131951,25619
BMRB,25626,"G88A,D90R double mutant of KaiB",131951,25619
BMRB,25616,KaiB dimer,131968,25620
BMRB,25617,dimeric KaiB bound to CI,131968,25620
BMRB,25618,N-SasA,131968,25620
BMRB,25619,N-SasA bound to CI,131968,25620
BMRB,25621,D91R single mutant of dimeric KaiB,131968,25620
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131968,25620
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131968,25620
BMRB,25624,"G89A,D91R double mutant of KaiB",131968,25620
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131968,25620
BMRB,25626,"G88A,D90R double mutant of KaiB",131968,25620
BMRB,25616,KaiB dimer,131984,25621
BMRB,25617,dimeric KaiB bound to CI,131984,25621
BMRB,25618,N-SasA,131984,25621
BMRB,25619,N-SasA bound to CI,131984,25621
BMRB,25620,G89A single mutant of dimeric KaiB,131984,25621
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),131984,25621
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",131984,25621
BMRB,25624,"G89A,D91R double mutant of KaiB",131984,25621
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",131984,25621
BMRB,25626,"G88A,D90R double mutant of KaiB",131984,25621
BMRB,25616,KaiB dimer,132000,25622
BMRB,25617,dimeric KaiB bound to CI,132000,25622
BMRB,25618,N-SasA,132000,25622
BMRB,25619,N-SasA bound to CI,132000,25622
BMRB,25620,G89A single mutant of dimeric KaiB,132000,25622
BMRB,25621,D91R single mutant of dimeric KaiB,132000,25622
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",132000,25622
BMRB,25624,"G89A,D91R double mutant of KaiB",132000,25622
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",132000,25622
BMRB,25626,"G88A,D90R double mutant of KaiB",132000,25622
BMRB,25616,KaiB dimer,132016,25623
BMRB,25617,dimeric KaiB bound to CI,132016,25623
BMRB,25618,N-SasA,132016,25623
BMRB,25619,N-SasA bound to CI,132016,25623
BMRB,25620,G89A single mutant of dimeric KaiB,132016,25623
BMRB,25621,D91R single mutant of dimeric KaiB,132016,25623
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),132016,25623
BMRB,25624,"G89A,D91R double mutant of KaiB",132016,25623
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",132016,25623
BMRB,25626,"G88A,D90R double mutant of KaiB",132016,25623
BMRB,25616,KaiB dimer,132032,25624
BMRB,25617,dimeric KaiB bound to CI,132032,25624
BMRB,25618,N-SasA,132032,25624
BMRB,25619,N-SasA bound to CI,132032,25624
BMRB,25620,G89A single mutant of dimeric KaiB,132032,25624
BMRB,25621,D91R single mutant of dimeric KaiB,132032,25624
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),132032,25624
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",132032,25624
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",132032,25624
BMRB,25626,"G88A,D90R double mutant of KaiB",132032,25624
BMRB,25616,KaiB dimer,132048,25625
BMRB,25617,dimeric KaiB bound to CI,132048,25625
BMRB,25618,N-SasA,132048,25625
BMRB,25619,N-SasA bound to CI,132048,25625
BMRB,25620,G89A single mutant of dimeric KaiB,132048,25625
BMRB,25621,D91R single mutant of dimeric KaiB,132048,25625
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),132048,25625
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",132048,25625
BMRB,25624,"G89A,D91R double mutant of KaiB",132048,25625
BMRB,25626,"G88A,D90R double mutant of KaiB",132048,25625
BMRB,25616,KaiB dimer,132065,25626
BMRB,25617,dimeric KaiB bound to CI,132065,25626
BMRB,25618,N-SasA,132065,25626
BMRB,25619,N-SasA bound to CI,132065,25626
BMRB,25620,G89A single mutant of dimeric KaiB,132065,25626
BMRB,25621,D91R single mutant of dimeric KaiB,132065,25626
BMRB,25622,D91R single mutant of dimeric KaiB (thioredoxin-like fold),132065,25626
BMRB,25623,"G89A,D91R double mutant of dimeric KaiB",132065,25626
BMRB,25624,"G89A,D91R double mutant of KaiB",132065,25626
BMRB,25625,"G89A,D91R double mutant of KaiB bound to CI",132065,25626
PDB,2N2Y,BMRB Entry Tracking System,132081,25627
BMRB,25629,"Backbone 1H, 13C and 15N Chemical Shift Assignments for G56C_T163C mutant of Adenylate Kinase at reduced condition",132099,25628
BMRB,25628,"Backbone 1H, 13C and 15N Chemical Shift Assignments for G56C_T163C mutant of Adenylate Kinase at oxidized condition",132113,25629
PDB,2N2Z,BMRB Entry Tracking System,132127,25630
PDB,2N30,BMRB Entry Tracking System,132144,25631
PDB,2N31,BMRB Entry Tracking System,132163,25632
PDB,1GAB,,132178,25634
PDB,2FS1,PSD-1,132178,25634
PDB,2N35,BMRB Entry Tracking System,132178,25634
PDB,2N37,BMRB Entry Tracking System,132197,25636
PDB,2N39,BMRB Entry Tracking System,132216,25638
PDB,2N3A,BMRB Entry Tracking System,132234,25639
PDB,1OCD,Entry for the same protein system encapsulated within reverse micelles incorporating pseudocontact shifts,132252,25640
PDB,2N3B,BMRB Entry Tracking System,132252,25640
PDB,2N3D,BMRB Entry Tracking System,132276,25642
PDB,2N3E,BMRB Entry Tracking System,132300,25643
PDB,2N3J,BMRB Entry Tracking System,132316,25645
BMRB,19673,Assignment of p75 NTR transmembrane domain in DPC micelles,132342,25646
BMRB,25647,p75-TMDCD/DPC,132342,25646
BMRB,25648,p75-TMDCD/LPN,132342,25646
BMRB,19673,Assignment of p75 NTR transmembrane domain in DPC micelles,132356,25647
BMRB,25646,p75-TMICD/LPN,132356,25647
BMRB,25648,p75-TMDCD/LPN,132356,25647
BMRB,26693,DHFR-apo,136315,25861
BMRB,19673,Assignment of p75 NTR transmembrane domain in DPC micelles,132370,25648
BMRB,25646,Backbone chemical shift assignment of rat p75NTR transmembrane and intracellular domains in lipid/protein nanodiscs,132370,25648
BMRB,25647,Backbone chemical shift assignment of rat p75NTR transmembrane and juxtamembrane intracellular domains in DPC micelles,132370,25648
PDB,2N3K,BMRB Entry Tracking System,132384,25649
NCBI,XP_001351730.2,,132412,25650
PDB,2N3L,BMRB Entry Tracking System,132412,25650
PDB,2N3M,BMRB Entry Tracking System,132431,25651
PDB,1SJQ,NMR structure of PTB RRM1 (54-147) in the free state.,132452,25652
PDB,2AD9,NMR structure of PTB RRM1(49-146) bound to single-stranded CUCUCU RNA,132452,25652
PDB,2N3O,BMRB Entry Tracking System,132452,25652
PDB,2N3P,BMRB Entry Tracking System,132494,25653
BMRB,25655,II-III-VI three-way junction from the VS ribozyme in complex with MAGNESIUM,132511,25654
PDB,2N3Q,BMRB Entry Tracking System,132511,25654
BMRB,25654,II-III-VI three-way junction from the VS ribozyme,132534,25655
PDB,2N3R,BMRB Entry Tracking System,132534,25655
PDB,2N3S,BMRB Entry Tracking System,132561,25656
PDB,2N3T,BMRB Entry Tracking System,132578,25657
PDB,5a4g,PDBe entry,132602,25658
PDB,2N3X,BMRB Entry Tracking System,132635,25659
BMRB,18828,NMR assignment of Arabidopsis thaliana reduced cytochrome c.,132653,25660
BMRB,26578,NMR assignment of Homo sapiens oxidized cytochrome c.,132653,25660
PDB,2N3Y,BMRB Entry Tracking System,132653,25660
BMRB,25666,or34,132720,25662
BMRB,25794,"OR446, RDC data",132720,25662
PDB,2N3Z,BMRB Entry Tracking System,132720,25662
PDB,2N75,Refined structure with RDC,132720,25662
PDB,2N40,BMRB Entry Tracking System,132753,25663
BMRB,25662,"DE NOVO DESIGNED PROTEIN, Rossmann2x2 Fold, Northeast Structural Genomics Consortium (NESG) Target OR446",132774,25664
BMRB,25666,OR34,132774,25664
PDB,2N41,BMRB Entry Tracking System,132774,25664
PDB,2WN4,ADP-RIBOSYLTRANSFERASE TOXIN CDTA,132800,25665
BMRB,25662,NESG Target OR34,132827,25666
BMRB,25664,"DE NOVO DESIGNED PROTEIN, Rossmann2x2 Fold, Northeast Structural Genomics Consortium (NESG) Target OR446",132827,25666
PDB,2N4E,BMRB Entry Tracking System,132827,25666
BMRB,25668,Q343R Mutant of TDP-43 Amyloidogenic Core Region,132854,25667
PDB,2N4G,BMRB Entry Tracking System,132854,25667
BMRB,25667,G335D Mutant of TDP-43 Amyloidogenic Core Region,132872,25668
PDB,2N4H,BMRB Entry Tracking System,132872,25668
PDB,2N4J,BMRB Entry Tracking System,132890,25669
PDB,2N4K,BMRB Entry Tracking System,132912,25670
PDB,2N4L,BMRB Entry Tracking System,132926,25671
PDB,2N4M,BMRB Entry Tracking System,132948,25672
BMRB,25764,"Complex with 2-METHYLPROPANE-1,2-DIAMINE",132970,25673
BMRB,25765,Complex with CHOLIC ACID,132970,25673
PDB,2N4N,BMRB Entry Tracking System,132970,25673
PDB,2N4P,BMRB Entry Tracking System,133007,25675
BMRB,25586,wt NS4A N-terminal domain of DENV,133022,25676
PDB,2LM0,NMR Solution Structure of AF4-AF9,133036,25677
PDB,2MV7,NMR Solution Structure of DOT1L-AF9,133036,25677
PDB,2N4Q,BMRB Entry Tracking System,133036,25677
BMRB,25679,L453E,133054,25678
BMRB,25680,L453W,133054,25678
BMRB,25681,E454Y,133054,25678
BMRB,25682,T456D,133054,25678
BMRB,25683,T456Y,133054,25678
PDB,1e0l,Original sequence of the FBP28 WW domain,133054,25678
PDB,2N4R,BMRB Entry Tracking System,133054,25678
BMRB,25678,L453D,133071,25679
BMRB,25680,L453W,133071,25679
BMRB,25681,E454Y,133071,25679
BMRB,25682,T456D,133071,25679
BMRB,25683,T456Y,133071,25679
PDB,2N4S,BMRB Entry Tracking System,133071,25679
BMRB,25678,L453D,133088,25680
BMRB,25679,L453E,133088,25680
BMRB,25681,E454Y,133088,25680
BMRB,25682,T456D,133088,25680
BMRB,25683,T456Y,133088,25680
PDB,2N4T,BMRB Entry Tracking System,133088,25680
BMRB,25678,L453D,133105,25681
BMRB,25679,L453E,133105,25681
BMRB,25680,L453W,133105,25681
BMRB,25682,T456D,133105,25681
BMRB,25683,T456Y,133105,25681
PDB,2N4U,BMRB Entry Tracking System,133105,25681
BMRB,25678,L453D,133122,25682
BMRB,25679,L453E,133122,25682
BMRB,25680,L453W,133122,25682
BMRB,25681,E454Y,133122,25682
BMRB,25683,T456Y,133122,25682
PDB,2N4V,BMRB Entry Tracking System,133122,25682
BMRB,25678,L453D,133139,25683
BMRB,25679,L453E,133139,25683
BMRB,25680,L453W,133139,25683
BMRB,25681,E454Y,133139,25683
BMRB,25682,T456D,133139,25683
PDB,2N4W,BMRB Entry Tracking System,133139,25683
PDB,5a4h,PDBe entry,133156,25684
PDB,2N4X,BMRB Entry Tracking System,133196,25685
PDB,2N4Y,BMRB Entry Tracking System,133216,25686
BMRB,25687,Acyl Carrier Protein,133234,25688
PDB,2N50,BMRB Entry Tracking System,133234,25688
PDB,2N51,BMRB Entry Tracking System,133264,25690
PDB,2N52,BMRB Entry Tracking System,133284,25691
BMRB,25250,Solution structure of ovis Aries PrP with mutation delta190-197,133298,25692
BMRB,25251,Solution structure of ovis Aries PrP with mutation delta193-196,133298,25692
PDB,2MV8,Solution structure of ovis Aries PrP with mutation delta190-197,133298,25692
PDB,2MV9,Solution structure of ovis Aries PrP with mutation delta193-196,133298,25692
PDB,2N53,BMRB Tracking System,133298,25692
PDB,2N54,BMRB Entry Tracking System,133316,25693
PDB,2N55,BMRB Entry Tracking System,133336,25694
BMRB,25697,hCFTR NBD1 deltaRI I539T,133358,25696
BMRB,25698,hCFTR NBD1 deltaRI F508del,133358,25696
BMRB,25696,hCFTR NBD1 deltaRI,133372,25697
BMRB,25698,hCFTR NBD1 deltaRI F508del,133372,25697
BMRB,25696,hCFTR NBD1 deltaRI,133386,25698
BMRB,25697,hCFTR NBD1 deltaRI I539T,133386,25698
PDB,2IW1,NMR structure of residues 103-132.,133401,25699
PDB,2N58,BMRB Entrying Tracking System,133401,25699
PDB,2N59,BMRB Entry Tracking System,133428,25700
BMRB,25752,Complex with Lu3+,133449,25701
BMRB,25703,oxidized form of thioredoxin 1 from Sacharomyces cerevisiae,133471,25702
PDB,2N5A,BMRB Entry Tracking System,133471,25702
BMRB,25702,reduced form of thioredoxin 1 from Sacharomyces cerevisiae,133486,25703
PDB,2N5B,BMRB Entry Tracking System,133486,25703
PDB,2N5C,BMRB Entry Tracking System,133500,25704
PDB,2WJI,Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus,133516,25705
PDB,2YHM,Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus,133516,25705
PDB,4BKK,Electron microscopy structure of respiratory syncytial virus nucleocapsid,133516,25705
SP,P03418,Human respiratory syncytial virus A (strain A2),133516,25705
NCBI,134287118,,133533,25706
PDB,2N5D,,133533,25706
BMRB,25708,Ub S65E,133552,25707
BMRB,25709,Ub S65E in complex with parkin R0RBR,133552,25707
BMRB,4769,"Backbone 1H, 13C and 15N assignments for yeast ubiquitin at pH 7.5",133552,25707
PDB,5C1Z,,133552,25707
PDB,5C23,,133552,25707
BMRB,25707,Ub in complex with parkin R0RBR,133571,25708
BMRB,25709,Ub S65E in complex with parkin R0RBR,133571,25708
BMRB,4769,"Backbone 1H, 13C and 15N assignments for yeast ubiquitin at pH 7.5",133571,25708
PDB,5C1Z,,133571,25708
PDB,5C23,,133571,25708
BMRB,25707,Ub in complex with parkin R0RBR,133588,25709
BMRB,25708,Ub S65E,133588,25709
BMRB,4769,"Backbone 1H, 13C and 15N assignments for yeast ubiquitin at pH 7.5",133588,25709
PDB,5C1Z,,133588,25709
PDB,5C23,,133588,25709
PDB,2N5E,BMRB Entry Tracking System,133607,25710
BMRB,25713,HLA-B2709_pVIPR,133624,25711
BMRB,25714,HLA-B2705_pVIPR,133624,25711
BMRB,25715,HLA-B2709_TIS,133624,25711
PDB,2N5F,BMRB Tracking System,133644,25712
BMRB,25711,HLA-B2705_TIS,133661,25713
BMRB,25714,HLA-B2705_pVIPR,133661,25713
BMRB,25715,HLA-B2709_TIS,133661,25713
BMRB,25711,HLA-B2705_TIS,133681,25714
BMRB,25713,HLA-B2709_pVIPR,133681,25714
BMRB,25715,HLA-B2709_TIS,133681,25714
BMRB,25711,HLA-B2705_TIS,133701,25715
BMRB,25713,HLA-B2709_pVIPR,133701,25715
BMRB,25714,HLA-B2705_pVIPR,133701,25715
BMRB,25717,,133721,25716
PDB,2N5H,BMRB Entry Tracking System,133721,25716
BMRB,25716,In complex with PNS,133740,25717
PDB,2N5I,BMRB Entry Tracking System,133740,25717
BMRB,25719,Regnase-1 Zinc finger domain,133759,25718
BMRB,25720,Regnase-1 C-terminal domain,133759,25718
PDB,2N5J,BMRB Entry Tracking System,133759,25718
BMRB,25718,Regnase-1 N-terminal domain,133780,25719
BMRB,25720,Regnase-1 C-terminal domain,133780,25719
PDB,2N5K,BMRB Entry Tracking System,133780,25719
BMRB,25718,Regnase-1 N-terminal domain,133801,25720
BMRB,25719,Regnase-1 Zinc finger domain,133801,25720
PDB,2N5K,BMRB Entry Tracking System,133801,25720
PDB,2N5M,BMRB Entry Tracking System,133835,25722
PDB,2N5O,BMRB Entry Tracking System,133849,25723
PDB,2N5P,BMRB Entry Tracking System,133872,25724
PDB,2N5Q,BMRB Entry Tracking System,133894,25725
PDB,2N5R,BMRB Entry Tracking System,133913,25726
BMRB,25728,HBPd24r (apo form),133927,25727
PDB,3G7X,"Entry containing 1H, 15N and 13C assignment for this molecule",133927,25727
BMRB,25727,HBPd24r (bound to histamine),133949,25728
PDB,3GAQ,"Entry containing 1H, 15N and 13C assignment for this molecule",133949,25728
PDB,2N5S,BMRB Entry Tracking System,133969,25729
PDB,2N5T,BMRB Entry Tracking System,134013,25731
PDB,2N5U,BMRB Entry Tracking System,134030,25732
BMRB,25735,The selective autophagy receptor TAX1BP1 is required for autophagy-dependent capture of cytosolic Salmonella typhimurium,134049,25734
PDB,5aaq,PDBe entry,134049,25734
BMRB,25374,TBK1 recruitment to cytosol-invading Salmonella induces anti-bacterial autophagy,134067,25735
PDB,5aas,PDBe entry,134067,25735
PDB,5aay,PDBe entry,134085,25736
BMRB,25741,octyl-tridecaptin A1 in DPC micelles containing Gram-negative lipid II,134103,25737
PDB,2N5W,BMRB Entry Tracking System,134103,25737
BMRB,25506,Re-SDPhe-TATE isomer 1,134123,25738
BMRB,25507,Linear SDPhe-TATE,134123,25738
BMRB,25739,Re-SDPhe-TATE isomer 4,134123,25738
BMRB,25506,Re-SDPhe-TATE isomer 1,134141,25739
BMRB,25507,Linear SDPhe-TATE,134141,25739
BMRB,25738,Re-SDPhe-TATE isomer 2,134141,25739
PDB,1US7,crystal structure of MC-Cdc37 two-domain fragment,134172,25740
PDB,2N5X,C-terminal domain of Cdc37 cochaperone,134172,25740
PDB,2W0G,crystal structure of M-Cdc37,134172,25740
BMRB,25737,octyl-tridecaptin A1 in DPC micelles,134191,25741
PDB,2N5Y,BMRB Entry Tracking System,134191,25741
BMRB,25893,F3 free,136922,25894
BMRB,25736,TBK1 recruitment to cytosol-invading Salmonella induces anti-bacterial autophagy,134211,25742
PDB,5aaz,PDBe entry,134211,25742
PDB,2N5Z,BMRB Entry Tracking System,134243,25744
PDB,5abk,PDBe entry,134260,25745
PDB,2N60,BMRB Entry Tracking System,134277,25746
PDB,2N62,BMRB Entry Tracking System,134299,25748
BMRB,25751,VG16KRKP dimer,134314,25749
PDB,2N63,BMRB Entry Tracking System,134314,25749
PDB,2N64,BMRB Entry Tracking System,134342,25750
PDB,5abs,Entry containing X-ray crystal structure of the same domain.,134342,25750
BMRB,25749,VG16KRKP monomer,134358,25751
PDB,2N65,BMRB Entry Tracking System,134358,25751
BMRB,25701,Complex without Lu3+,134372,25752
BMRB,25755,non-sweet mutant (ins18RI19) of sweet protein Brazzein,134396,25753
PDB,2N66,BMRB Entry Tracking System,134396,25753
PDB,2N68,BMRB Entry Tracking System,134418,25754
BMRB,25753,sweeter mutant (D40K) of sweet protein Brazzein,134434,25755
PDB,2N69,BMRB Entry Tracking System,134434,25755
BMRB,17384,Backbone Assignment of the Tyrosine Kinase Src Catalytic Domain in Complex with Imatinib.,134456,25756
PDB,2N6A,BMRB Entry Tracking System,134473,25757
PDB,3EWT,calmodulin complex,134473,25757
PDB,4DJC,calmodulin complex,134473,25757
PDB,2N6B,BMRB Entry Tracking System,134490,25758
PDB,2N6C,BMRB Entry Tracking System,134505,25759
BMRB,25761,PC07372D,134522,25760
PDB,2N6D,BMRB Entry Tracking System,134522,25760
BMRB,25760,GNPTAB,134537,25761
PDB,2N6E,BMRB Entry Tracking System,134537,25761
PDB,2N6F,BMRB Entry Tracking System,134552,25762
PDB,2N6G,BMRB Entry Tracking System,134570,25763
BMRB,25765,Complex with CHOLIC ACID,134591,25764
PDB,2N6H,BMRB Entry Tracking System,134591,25764
BMRB,25764,"Complex with 2-METHYLPROPANE-1,2-DIAMINE",134608,25765
PDB,2N6I,BMRB Entry Tracking System,134608,25765
PDB,2N6J,BMRB Entry Tracking System,134624,25766
PDB,2N6K,BMRB Entry Tracking System,134649,25767
PDB,2N6L,BMRB Entry Tracking System,134665,25768
PDB,2N6M,BMRB Entry Tracking System,134684,25769
BMRB,25772,Elafin,134721,25771
BMRB,25773,Trappin-2,134721,25771
BMRB,25771,Cementoin,134736,25772
BMRB,25773,Trappin-2,134736,25772
BMRB,25771,Cementoin,134751,25773
BMRB,25772,Elafin,134751,25773
PDB,2N6N,BMRB Entry Tracking System,134766,25774
Arachno,AS000224,ArachnoServer (www.arachnoserver.org),134784,25775
PDB,2N60,BMRB Entry Tracking System,134784,25775
SP,P60992,,134784,25775
PDB,2N6P,BMRB Entry Tracking System,134802,25776
PDB,2n6l,,134802,25776
PDB,2N6Q,BMRB Entry Tracking System,134826,25777
PDB,2N6R,BMRB Entry Tracking System,134848,25778
NCBI,XP_001351730.2,Full length protein sequence of PfSR1,134866,25779
BMRB,25781,CssA3 (top stem) of CssA thermometer,134882,25780
BMRB,25784,CssA Thermometer from Neisseria meningitidis,134882,25780
BMRB,25785,CssA5 (middle region) of CssA thermometer,134882,25780
PDB,2N6S,BMRB Entry Tracking System,134882,25780
BMRB,25780,CssA4 (bottom stem) of CssA thermometer,134902,25781
BMRB,25784,CssA Thermometer from Neisseria meningitidis,134902,25781
BMRB,25785,CssA5 (middle region) of CssA thermometer,134902,25781
PDB,2N6T,BMRB Entry Tracking System,134902,25781
BMRB,25783,Astexin3,134921,25782
PDB,2N6U,BMRB Entry Tracking System,134921,25782
PDB,2N6V,BMRB Entry Tracking System,134938,25783
BMRB,25780,CssA4 (bottom stem) of CssA thermometer,134954,25784
BMRB,25781,CssA3 (top stem) of CssA thermometer,134954,25784
BMRB,25785,CssA5 (middle region) of CssA thermometer,134954,25784
PDB,2N6W,BMRB Entry Tracking System,134954,25784
BMRB,25780,CssA4 (bottom stem) of CssA thermometer,134973,25785
BMRB,25781,CssA3 (top stem) of CssA thermometer,134973,25785
BMRB,25784,CssA Thermometer from Neisseria meningitidis,134973,25785
PDB,2N6X,BMRB Entry Tracking System,134973,25785
BMRB,25787,salicylate-loaded ArCP from yersiniabactin synthetase,134990,25786
PDB,2N6Y,BMRB Entry Tracking System,134990,25786
BMRB,25786,holo ArCP from yersiniabactin synthetase,135009,25787
PDB,2N6Z,BMRB Entry Tracking System,135009,25787
PDB,2N70,BMRB Entry Tracking System,135029,25788
PDB,2N71,BMRB Entry Tracking System,135053,25789
BMRB,25791,kinase in complex with its regulatory protein,135075,25790
PDB,2N72,BMRB Entry Tracking System,135075,25790
BMRB,25790,polyQ regulatory protein,135091,25791
PDB,2N73,BMRB Entry Tracking System,135091,25791
BMRB,26647,p65 DBD,135108,25792
PDB,1NFI,,135108,25792
PDB,2N74,BMRB Entry Tracking System,135125,25793
BMRB,25662,assigned chemical shifts,135145,25794
PDB,2n3z,the new entry has RDC/Talosn restraints for the loop region residues.,135145,25794
PDB,2N74,BMRB Entry Tracking System,135174,25796
PDB,1AP4,,135195,25797
PDB,1R2U,,135195,25797
PDB,2CTN,,135195,25797
PDB,2MLF,,135195,25797
PDB,2N79,BMRB Entry Tracking System,135195,25797
BMRB,25799,Structural basis of human Siglec-8-carbohydrate recognition,135212,25798
PDB,2N7A,BMRB Entry Tracking System,135212,25798
BMRB,25798,NMR structure of human I-type lectin domain,135240,25799
BMRB,25895,WGR free,136922,25894
PDB,2N7B,BMRB Entry Tracking System,135240,25799
BMRB,25779,"1H, 13C and 15N resonance assignments of unbound PfSR1-RRM1",135302,25800
NCBI,XP_001351730.2,Polypeptide sequence of PfSR1,135302,25800
PDB,2N3L,Solution structure of unbound PfSR1-RRM1,135302,25800
PDB,2N7C,BMRB Entry Tracking System,135302,25800
BMRB,25803,UBL domain of the yeast DNA damage-inducible protein homolog 1,135323,25801
PDB,2N7D,BMRB Entry Tracking System,135323,25801
BMRB,25801,UBL domain of the human DNA damage-inducible protein homolog 2,135355,25803
PDB,2N7E,BMRB Entry Tracking System,135355,25803
PDB,2N7F,BMRB Entry Tracking System,135370,25804
PDB,2N7G,BMRB Entry Tracking System,135388,25805
PDB,2N7I,BMRB Entry Tracking System,135403,25806
PDB,2N7J,BMRB Entry Tracking System,135421,25807
PDB,2OED,Static model calculated from a subset of the currently used experimental restraints,135421,25807
PDB,2N7K,BMRB Entry Tracking System,135454,25808
BMRB,15480,1H chemical shifts of W60G beta2-microglobulin,135469,25809
BMRB,17165,"1H, 13C, 15N chemical shifts of wt beta2-microglobulin",135469,25809
BMRB,5169,1H chemical shifts of wt beta2-microglobulin,135469,25809
PDB,2N7L,BMRB Entry Tracking System,135484,25810
PDB,2N7M,BMRB Entry Tracking System,135509,25811
BMRB,25814,Peptide PG-990 in DPC micelles,135533,25813
BMRB,25820,Peptide PG-992 in DPC micelles,135533,25813
PDB,2N7N,BMRB Entry Tracking System,135533,25813
BMRB,25813,Peptide PG-989 in DPC micelles,135550,25814
BMRB,25820,Peptide PG-992 in DPC micelles,135550,25814
PDB,2N7O,BMRB Entry Tracking System,135550,25814
PDB,2N7P,BMRB Entry Tracking System,135569,25816
BMRB,25818,transmembrane domain of human nicastrin in DPC micelles,135583,25817
PDB,2N7Q,BMRB Entry Tracking System,135583,25817
BMRB,25817,transmembrane domain of human nicastrin in SDS micelles,135597,25818
PDB,2N7R,BMRB Entry Tracking System,135597,25818
PDB,2N7S,BMRB Entry Tracking System,135611,25819
BMRB,25813,Peptide PG-989 in DPC micelles,135625,25820
BMRB,25814,Peptide PG-990 in DPC micelles,135625,25820
PDB,2N7T,BMRB Entry Tracking System,135625,25820
EMBL,BLAC_BACLI,,135644,25821
PDB,1L2S,,135644,25821
PDB,2BLM,,135644,25821
PDB,3LY3,,135644,25821
PDB,3LY4,,135644,25821
PDB,3M2J,,135644,25821
PDB,3M2K,,135644,25821
PDB,4BLM,,135644,25821
BMRB,25831,complex of microRNA 20b pre-element with Rbfox RRM,135678,25826
PDB,2N7X,BMRB Entry Tracking System,135678,25826
PDB,2N7Y,BMRB Entry Tracking System,135704,25827
PDB,2N7Z,BMRB Entry Tracking System,135720,25828
BMRB,25828,RIP2 CARD,135737,25829
BMRB,25833,p75NTR DD:RIP2 CARD,135737,25829
PDB,2N80,BMRB Entry Tracking System,135737,25829
GB,KJ569141,,135757,25830
PDB,2N81,BMRB Entry Tracking System,135757,25830
BMRB,25826,microRNA 20b pre-element,135773,25831
PDB,2N82,BMRB Entry Tracking System,135773,25831
BMRB,25828,RIP2 CARD,135814,25833
BMRB,25829,p75NTR DD:RhoGDI,135814,25833
PDB,2N83,BMRB Entry Tracking System,135814,25833
PDB,2N84,BMRB Entry Tracking System,135834,25834
BMRB,25836,OtTx1a - ICK,135854,25835
PDB,2N85,BMRB Entry Tracking System,135854,25835
BMRB,25835,OtTx1a - AMP in DPC micelles,135872,25836
PDB,2N86,BRMB Entry Tracking System,135872,25836
PDB,2N88,BMRB Entry Tracking System,135889,25837
PDB,5fim,BMRB Entry Tracking System,135926,25839
PDB,2N89,BMRB Entry Tracking System,135966,25840
BMRB,25845,,135987,25844
PDB,1HA9,,135987,25844
PDB,2N8B,BMRB Entry Tracking System,135987,25844
PDB,1HA9,,136005,25845
PDB,2N8C,BMRB Entry Tracking System,136005,25845
PDB,2N8D,BMRB Entry Tracking System,136024,25846
PDB,2N8E,BMRB Entry Tracking System,136042,25847
PDB,2N8F,BMRB Entry Tracking System,136061,25848
PDB,2N8G,BMRB Entry Tracking System,136080,25849
PDB,2N8I,BMRB Entry Tracking System,136095,25850
BMRB,26681,CaM1234 (apo form),136140,25852
BMRB,26682,CaM12 (apo form),136140,25852
BMRB,26683,CaM34 (apo form),136140,25852
BMRB,26685,CaM12 (complex with Ca),136140,25852
BMRB,26686,CaM34 (complex with Ca),136140,25852
BMRB,26687,CaM34 (complex with iNOS,136140,25852
PDB,2N8J,BMRB Entry Tracking System,136140,25852
PDB,2N8K,BMRB Entry Tracking System,136159,25853
BMRB,25855,Zipcode-binding-protein-1 KH3(DD)KH4 domains in complex with the RNA target UCGGACU,136177,25854
PDB,2N8L,BMRB Entry Tracking System,136177,25854
BMRB,25854,Zipcode-binding-protein-1 KH3KH4(DD) domains in complex with the RNA target CACACCC,136198,25855
PDB,2N8L,BMRB Entry Tracking System,136198,25855
PDB,2N8N,BMRB Entry Tracking System,136219,25856
BMRB,25858,Lacticin Q,136237,25857
BMRB,25857,Aureocin A53,136251,25858
PDB,2N8P,BMRB Entry Tracking System,136251,25858
BMRB,7089,Uncomplexed form.,136266,25859
PDB,2N8R,BMRB Entry Tracking System,136266,25859
PDB,2poj,Uncomplexed form.,136266,25859
BMRB,25861,DHFR-NADPH,136294,25860
BMRB,26693,DHFR-apo,136294,25860
BMRB,26694,S1-DHFR-NADPH-Trimethoprim,136294,25860
BMRB,26695,S1-DHFR-NADPH,136294,25860
BMRB,25860,DHFR-NADPH-Trimethoprim,136315,25861
BMRB,26694,S1-DHFR-NADPH-Trimethoprim,136315,25861
BMRB,26695,S1-DHFR-NADPH,136315,25861
BMRB,25865,rNedd4 WW2 Domain-Cx43CT Peptide Complex,136352,25864
BMRB,25866,rNedd4 WW2 Domain,136352,25864
BMRB,26698,rNedd4 WW3 Domain,136352,25864
PDB,2N8S,BMRB Entry Tracking System,136352,25864
BMRB,25864,rNedd4 WW1,136369,25865
BMRB,25866,rNedd4 WW2 Domain,136369,25865
BMRB,26698,rNedd4 WW3 Domain,136369,25865
PDB,2N8T,BMRB Entry Tracking System,136369,25865
BMRB,25864,rNedd4 WW1,136388,25866
BMRB,25865,rNedd4 WW2 Domain-Cx43CT Peptide Complex,136388,25866
BMRB,26698,rNedd4 WW3 Domain,136388,25866
PDB,2N8U,BMRB Entry Tracking System,136388,25866
PDB,2N8V,BMRB Entry Tracking System,136405,25867
PDB,2N8W,BMRB Entry Tracking System,136424,25868
PDB,2JXP,Lpte from Nitrosomonas europaea,136452,25869
PDB,2R76,Lpte from Shewanella (S.) oneidensis,136452,25869
PDB,3BF2,LptE from Neisseria meningitides,136452,25869
PDB,4N4R,Lpte from S. typhimurium,136452,25869
PDB,4NHR,LptE from E. coli,136452,25869
PDB,4Q35,LptE from S. flexneri,136452,25869
PDB,2N8Y,BMRB Entry Tracking System,136472,25870
PDB,2N8Z,BMRB Entry Tracking System,136491,25871
PDB,2N90,BMRB Entry Tracking System,136508,25872
PDB,2LDO,,136540,25874
PDB,2N91,BMRB Entry Tracking System,136540,25874
BMRB,25878,Holo N-terminal TnC F2 backbone assignment,136562,25875
BMRB,25879,Backbone assignment of Apo C-terminal F2-TnC,136562,25875
BMRB,25880,Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus,136562,25875
BMRB,25896,Backbone Assignment of Apo Troponin C from Lethocerus Indicus,136562,25875
BMRB,25897,Holo F2 TnC,136562,25875
PDB,2N92,BMRB Entry Tracking System,136579,25877
BMRB,25875,Backbone assignment of Calcium loaded C-terminus of Troponin C isoform 2,136595,25878
BMRB,25879,Backbone assignment of Apo C-terminal F2-TnC,136595,25878
BMRB,25880,Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus,136595,25878
BMRB,25896,Backbone Assignment of Apo Troponin C from Lethocerus Indicus,136595,25878
BMRB,25897,Holo F2 TnC,136595,25878
BMRB,25875,Backbone assignment of Calcium loaded C-terminus of Troponin C isoform 2,136611,25879
BMRB,25878,Holo N-terminal TnC F2 backbone assignment,136611,25879
BMRB,25880,Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus,136611,25879
BMRB,25896,Backbone Assignment of Apo Troponin C from Lethocerus Indicus,136611,25879
BMRB,25897,Holo F2 TnC,136611,25879
BMRB,25875,Backbone assignment of Calcium loaded C-terminus of Troponin C isoform 2,136627,25880
BMRB,25878,Holo N-terminal TnC F2 backbone assignment,136627,25880
BMRB,25879,Backbone assignment of Apo C-terminal F2-TnC,136627,25880
BMRB,25896,Backbone Assignment of Apo Troponin C from Lethocerus Indicus,136627,25880
BMRB,25897,Holo F2 TnC,136627,25880
PDB,2N95,BMRB Entry Tracking System,136643,25881
PDB,2N96,BMRB Entry Tracking System,136662,25882
PDB,2N97,BMRB Entry Tracking System,136679,25883
PDB,2N98,BMRB Entry Tracking System,136714,25886
PDB,2N99,BMRB Entry Tracking System,136739,25887
BMRB,25889,F1F2 free,136757,25888
BMRB,25890,DNA free,136757,25888
BMRB,25891,F1F2F3-DNA complex,136757,25888
BMRB,25892,F1F2F3 free,136757,25888
BMRB,25893,F3 free,136757,25888
BMRB,25894,F1F2F3-WGR-DNA complex,136757,25888
BMRB,25895,WGR free,136757,25888
PDB,2N8A,BMRB Entry Tracking System,136757,25888
BMRB,25888,F1F2-DNA complex,136799,25889
BMRB,25890,DNA free,136799,25889
BMRB,25891,F1F2F3-DNA complex,136799,25889
BMRB,25892,F1F2F3 free,136799,25889
BMRB,25893,F3 free,136799,25889
BMRB,25894,F1F2F3-WGR-DNA complex,136799,25889
BMRB,25895,WGR free,136799,25889
BMRB,25888,F1F2-DNA complex,136823,25890
BMRB,25889,F1F2 free,136823,25890
BMRB,25891,F1F2F3-DNA complex,136823,25890
BMRB,25892,F1F2F3 free,136823,25890
BMRB,25893,F3 free,136823,25890
BMRB,25894,F1F2F3-WGR-DNA complex,136823,25890
BMRB,25895,WGR free,136823,25890
BMRB,25888,F1F2-DNA complex,136848,25891
BMRB,25889,F1F2 free,136848,25891
BMRB,25890,DNA free,136848,25891
BMRB,25892,F1F2F3 free,136848,25891
BMRB,25893,F3 free,136848,25891
BMRB,25894,F1F2F3-WGR-DNA complex,136848,25891
BMRB,25895,WGR free,136848,25891
BMRB,25888,F1F2-DNA complex,136874,25892
BMRB,25889,F1F2 free,136874,25892
BMRB,25890,DNA free,136874,25892
BMRB,25891,F1F2F3-DNA complex,136874,25892
BMRB,25893,F3 free,136874,25892
BMRB,25894,F1F2F3-WGR-DNA complex,136874,25892
BMRB,25895,WGR free,136874,25892
BMRB,25888,F1F2-DNA complex,136899,25893
BMRB,25889,F1F2 free,136899,25893
BMRB,25890,DNA free,136899,25893
BMRB,25891,F1F2F3-DNA complex,136899,25893
BMRB,25892,F1F2F3 free,136899,25893
BMRB,25894,F1F2F3-WGR-DNA complex,136899,25893
BMRB,25895,WGR free,136899,25893
BMRB,25888,F1F2-DNA complex,136922,25894
BMRB,25889,F1F2 free,136922,25894
BMRB,25890,DNA free,136922,25894
BMRB,25891,F1F2F3-DNA complex,136922,25894
BMRB,25892,F1F2F3 free,136922,25894
BMRB,25888,F1F2-DNA complex,136950,25895
BMRB,25889,F1F2 free,136950,25895
BMRB,25890,DNA free,136950,25895
BMRB,25891,F1F2F3-DNA complex,136950,25895
BMRB,25892,F1F2F3 free,136950,25895
BMRB,25893,F3 free,136950,25895
BMRB,25894,F1F2F3-WGR-DNA complex,136950,25895
BMRB,25875,Backbone assignment of Calcium loaded C-terminus of Troponin C isoform 2,136971,25896
BMRB,25878,Holo N-terminal TnC F2 backbone assignment,136971,25896
BMRB,25879,Backbone assignment of Apo C-terminal F2-TnC,136971,25896
BMRB,25880,Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus,136971,25896
BMRB,25897,Holo F2 TnC,136971,25896
BMRB,25875,Backbone assignment of Calcium loaded C-terminus of Troponin C isoform 2,136987,25897
BMRB,25878,Holo N-terminal TnC F2 backbone assignment,136987,25897
BMRB,25879,Backbone assignment of Apo C-terminal F2-TnC,136987,25897
BMRB,25880,Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus,136987,25897
BMRB,25896,Backbone Assignment of Apo Troponin C from Lethocerus Indicus,136987,25897
PDB,2N9A,BMRB Entry Tracking System,137003,25898
PDB,2N9B,BMRB Entry Tracking System,137018,25899
PDB,2ZTA,X-ray structure of the GCN4 leucine zipper,137018,25899
PDB,2lw9,Homo sapiens myosin-10 wild-type coiled-coil,137018,25899
PDB,2N9C,BMRB Entry Tracking System,137065,25900
PDB,2N9E,BMRB Entry Tracking System,137080,25901
BMRB,25906,"Glucose as a nuclease mimic in DNA, at residue 6",137121,25903
PDB,2N9F,BMRB Entry Tracking System,137121,25903
PDB,2N9G,BMRB Entry Tracking System,137155,25905
BMRB,25903,"Glucose as a nuclease mimic in DNA, at residue 7",137169,25906
PDB,2N9H,BMRB Entry Tracking System,137169,25906
BMRB,25908,oxidized human cytochrome c,137186,25907
PDB,2N9I,BMRB Entry Tracking System,137186,25907
BMRB,25907,reduced human cytochrome c,137209,25908
PDB,2N9J,BMRB Entry Tracking System,137209,25908
BMRB,25910,in-cell GB1,137231,25909
PDB,2N9K,BMRB Entry Tracking System,137231,25909
BMRB,25909,in vitro GB1,137265,25910
PDB,2N9K,,137265,25910
PDB,2N9L,BMRB Entry Tracking System,137265,25910
PDB,2N9M,BMRB Entry Tracking System,137284,25911
BMRB,25914,RNF126 N-terminal zinc finger domain in complex with BAG6 Ubiquitin-like domain,137313,25913
PDB,2N90,BMRB Entry Tracking System,137313,25913
BMRB,25913,RNF126 N-terminal zinc finger domain,137335,25914
PDB,2N9P,BMRB Entry Tracking System,137335,25914
PDB,2N9Q,BMRB Entry Tracking System,137361,25915
PDB,2N9T,BMRB Entry Tracking System,137403,25917
PDB,2N9U,BMRB Entry Tracking System,137422,25918
PDB,2N9X,BMRB Entry Tracking System,137440,25919
PDB,2K9J,wild-type structure,137470,25920
PDB,2N9Y,BMRB Entry Tracking System,137470,25920
PDB,2N9Z,BMRB Entry Tracking System,137504,25922
PDB,2NA1,BMRB Entry Tracking System,137521,25923
PDB,2NA2,BMRB Entry Tracking System,137541,25924
PDB,2K6O,Human LL-37 Structure,137574,25926
PDB,2NA3,BMRB Entry Tracking System,137574,25926
GB,ECK1025,,137590,25927
NCBI,945711,"Gene ID of csgE,curli secretion specificity factor",137590,25927
PDB,2NA4,BMRB Entry Tracking System,137590,25927
PDB,2NA5,BMRB Entry Tracking System,137610,25928
BMRB,25930,Transmembrane domain of human Fas/CD95 death receptor,137625,25929
PDB,2NA6,BMRB Entry Tracking System,137625,25929
BMRB,25929,Transmembrane domain of mouse Fas/CD95 death receptor,137644,25930
PDB,2NA7,BMRB Entry Tracking System,137644,25930
BMRB,25932,P441A Mutant of Cytokine Receptor Common Subunit beta,137663,25931
PDB,2NA8,BMRB Entry Tracking System,137663,25931
BMRB,25931,Cytokine Receptor Common Subunit beta,137677,25932
PDB,2NA9,BMRB Entry Tracking System,137677,25932
PDB,2na8,wild-type structure,137677,25932
BMRB,25934,Nizp1-C2HR zinc finger,137691,25933
PDB,2NAA,BMRB Entry Tracking System,137691,25933
BMRB,25933,NSD1-PHD_5-C5HCH tandem domain,137712,25934
PDB,2NAB,BMRB Entry Tracking System,137712,25934
PDB,2NAE,BMRB Entry Tracking System,137731,25935
PDB,2NAJ,BMRB Entry tracking System,137749,25939
BMRB,25926,KR-12,137766,25941
PDB,2K6O,Human LL-37 Structure,137766,25941
PDB,2NA3,KR-12 structure,137766,25941
PDB,2NAL,BMRB Entry Tracking System,137766,25941
PDB,2NAM,BMRB Entry Tracking System,137782,25942
PDB,2NAQ,BMRB Entry Tracking System,137797,25943
PDB,2NAR,BMRB Entry Tracking System,137819,25944
PDB,5frg,PDBe entry,137836,25945
BMRB,25947,KYE28A in lipopolysachharide,137870,25946
PDB,2NAT,BMRB Entry Tracking System,137870,25946
BMRB,25946,KYE28 and lipopolysachharide,137884,25947
PDB,2NAU,BMRB Entry Tracking System,137884,25947
PDB,2NAV,BMRB Entry Tracking System,137898,25948
PDB,2NAW,BMRB Entry Tracking System,137917,25949
BMRB,25951,RSLfuc,137935,25950
BMRB,25952,RSL (free form),137935,25950
BMRB,25950,RSLman,137953,25951
BMRB,25952,RSL (free form),137953,25951
BMRB,25950,RSLman,137972,25952
BMRB,25951,RSLfuc,137972,25952
PDB,2NAX,BMRB Entry Tracking System,137988,25953
PDB,2NAY,BMRB Entry Tracking System,138014,25954
BMRB,25956,oxidised RsrA and without zinc ion,138029,25955
PDB,5frf,BMRB Entry Tracking System,138029,25955
PDB,5frh,oxidised RsrA and without zinc ion,138029,25955
BMRB,25955,reduced and zinc-bound RsrA,138046,25956
PDB,5frf,reduced and zinc-bound RsrA,138046,25956
PDB,5frh,BMRB Entry Tracking System,138046,25956
BMRB,19657,Chemical shift list of 15N-13C labelled PAF with the native sequence,138061,25957
PDB,2MHV,Structure of Penicillium antifungal protein (PAF) with the native sequence,138061,25957
PDB,2NB0,BMRB Entry Tracking System,138061,25957
PDB,2KBY,Structure of the tetramerization domain of p73,138080,25958
PDB,2NB1,BMRB Entry Tracking System,138080,25958
PDB,4A9Z,Structure of the tetramerization domain of p63,138080,25958
PDB,2NB2,BMRB Entry Tracking System,138109,25959
PDB,2NB4,BMRB Entry Tracking System,138131,25961
BMRB,18641,NMR solution structure of PawS derived peptide 11 (PDP-11),138145,25962
BMRB,18643,NMR solution structure of PawS Derived Peptide 4 (PDP-4),138145,25962
BMRB,18644,NMR solution structure of PawS Derived Peptide 5 (PDP-5),138145,25962
BMRB,18645,NMR solution structure of PawS Derived Peptide 7 (PDP-7),138145,25962
BMRB,18646,NMR solution structure of PawS Derived Peptide 6 (PDP-6),138145,25962
BMRB,25963,NMR solution structure of PawS Derived Peptide 10 (PDP-10),138145,25962
GB,JX262732,,138145,25962
PDB,2NB5,BMRB Entry Tracking System,138145,25962
BMRB,18641,NMR solution structure of PawS derived peptide 11 (PDP-11),138164,25963
BMRB,18643,NMR solution structure of PawS Derived Peptide 4 (PDP-4),138164,25963
BMRB,18644,NMR solution structure of PawS Derived Peptide 5 (PDP-5),138164,25963
BMRB,18645,NMR solution structure of PawS Derived Peptide 7 (PDP-7),138164,25963
BMRB,18646,NMR solution structure of PawS Derived Peptide 6 (PDP-6),138164,25963
BMRB,25962,NMR solution structure of PawS Derived Peptide 9 (PDP-9),138164,25963
GB,JX262736,,138164,25963
PDB,2NB6,BMRB Entry Tracking System,138164,25963
PDB,5fsf,PDBe entry,138182,25964
BMRB,25966,Solution structure of C-terminal extramembrane domain of SH protein,138202,25965
PDB,2NB7,BMRB Entry Tracking System,138202,25965
BMRB,25965,Solution structure of N-terminal extramembrane domain of SH protein,138216,25966
PDB,2NB8,BMRB Entry Tracking System,138216,25966
PDB,2NB9,BMRB Entry Tracking System,138230,25967
PDB,2NBA,BMRB Entry Tracking System,138265,25969
PDB,5HZ7,,138265,25969
PDB,2NBB,BMRB Entry Tracking System,138279,25970
PDB,2NBC,BMRB Entry Tracking System,138294,25971
BMRB,25973,V26A mutant of Ubiquitin at pH 2.0,138313,25972
PDB,2NBD,BMRB Entry Tracking System,138313,25972
BMRB,25972,V26A mutant of Ubiquitin at pH 6.0,138327,25973
PDB,2NBE,BMRB Entry Tracking System,138327,25973
PDB,2NBF,BMRB Entry Tracking System,138341,25974
PDB,2NBG,BMRB Entry Tracking System,138361,25975
PDB,2NBH,BMRB Entry Tracking System,138380,25976
PDB,2NBK,BMRB Entry Tracking System,138397,25979
PDB,2NBL,BMRB Entry Tracking System,138422,25982
BMRB,25984,Solution NMR structure of palmitated SCP2L2 from Aedes aegypti,138442,25983
PDB,2NBM,BMRB Entry Tracking System,138442,25983
BMRB,25983,Solution NMR structure of ligand free sterol carrier protein 2 like 2 from Aedes aegypti,138464,25984
PDB,2NBN,BMRB Entry Tracking System,138464,25984
BMRB,25987,Solution structure of the T119M variant of transthyretin in its monomeric state,138507,25986
PDB,2NBO,BMRB Entry Tracking System,138507,25986
BMRB,25986,Solution structure of the F87M/L110M variant of transthyretin in the monomeric state,138526,25987
PDB,2NBP,BMRB Entry Tracking System,138526,25987
BMRB,25990,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A289 (E1A-13S)",138563,25989
BMRB,25991,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1ACR3 (E1A CR3)",138563,25989
BMRB,25989,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A243 (E1A 12S)",138581,25990
BMRB,25991,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1ACR3 (E1A CR3)",138581,25990
BMRB,25989,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A243 (E1A 12S)",138598,25991
BMRB,25990,"1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A289 (E1A-13S)",138598,25991
PDB,2NBR,BMRB Entry Tracking System,138634,25993
PDB,2NBS,BMRB Entry Tracking System,138665,25994
PDB,2NBV,BMRB Entry Tracking System,138679,25995
BMRB,25999,Solution structure of the St domain of EMCV IRES,138700,25996
BMRB,26000,Solution structure of the delta-J-delta-K domain of EMCV IRES,138700,25996
BMRB,26997,Solution structure of the J domain of EMCV IRES,138700,25996
BMRB,26998,Solution structure of the K domain of EMCV IRES,138700,25996
PDB,2NBX,BMRB Entry Tracking System,138700,25996
BMRB,25999,Solution structure of the St domain of EMCV IRES,138718,25997
BMRB,26000,Solution structure of the delta-J-delta-K domain of EMCV IRES,138718,25997
BMRB,26996,Solution structure of the J-K region of EMCV IRES,138718,25997
BMRB,26998,Solution structure of the K domain of EMCV IRES,138718,25997
PDB,2NBY,BMRB Entry Tracking System,138718,25997
BMRB,25996,Solution structure of the J-K region of EMCV IRES,138742,25998
BMRB,25999,Solution structure of the St domain of EMCV IRES,138742,25998
BMRB,26000,Solution structure of the delta-J-delta-K domain of EMCV IRES,138742,25998
BMRB,26997,Solution structure of the J domain of EMCV IRES,138742,25998
PDB,2NBZ,BMRB Entry Tracking System,138742,25998
BMRB,25996,Solution structure of the J-K region of EMCV IRES,138766,25999
BMRB,25998,Solution structure of the K domain of EMCV IRES,138766,25999
BMRB,26013,CP12 oxydised,144606,26770
BMRB,26000,Solution structure of the delta-J-delta-K domain of EMCV IRES,138766,25999
BMRB,26997,Solution structure of the J domain of EMCV IRES,138766,25999
PDB,2NC0,BMRB Entry Tracking System,138766,25999
BMRB,25996,Solution structure of the J-K region of EMCV IRES,138816,26000
BMRB,25998,Solution structure of the K domain of EMCV IRES,138816,26000
BMRB,25999,Solution structure of the St domain of EMCV IRES,138816,26000
BMRB,26997,Solution structure of the J domain of EMCV IRES,138816,26000
PDB,2NC1,BMRB Entry Tracking System,138816,26000
PDB,2NC2,BMRB Entry Tracking System,138840,26001
BMRB,26003,peptide U3-scytotoxin-Sth1h,138861,26002
BMRB,26004,peptide U5-scytotoxin-Sth1a,138861,26002
PDB,5fzv,peptide U3-scytotoxin-Sth1a,138861,26002
PDB,5fzw,peptide U3-scytotoxin-Sth1h,138861,26002
PDB,5fzx,peptide U5-scytotoxin-Sth1a,138861,26002
BMRB,26002,peptide U3-scytotoxin-Sth1a,138900,26003
BMRB,26004,peptide U5-scytotoxin-Sth1a,138900,26003
PDB,5fzv,peptide U3-scytotoxin-Sth1a,138900,26003
PDB,5fzw,peptide U3-scytotoxin-Sth1h,138900,26003
PDB,5fzx,peptide U5-scytotoxin-Sth1a,138900,26003
BMRB,26002,peptide U3-scytotoxin-Sth1a,138943,26004
BMRB,26003,peptide U3-scytotoxin-Sth1h,138943,26004
PDB,5fzv,peptide U3-scytotoxin-Sth1a,138943,26004
PDB,5fzw,peptide U3-scytotoxin-Sth1h,138943,26004
PDB,5fzx,peptide U5-scytotoxin-Sth1a,138943,26004
BMRB,26006,Solution Structure of N-Galactosylated Pin1 WW Domain,138983,26005
BMRB,26007,Solution Structure of N-Xylosylated Pin1 WW Domain,138983,26005
BMRB,26008,Solution Structure of N-L-idosylated Pin1 WW Domain,138983,26005
PDB,2NC3,BMRB Entry Tracking System,138983,26005
BMRB,26005,Solution Structure of N-Allosylated Pin1 WW Domain,138999,26006
BMRB,26007,Solution Structure of N-Xylosylated Pin1 WW Domain,138999,26006
BMRB,26008,Solution Structure of N-L-idosylated Pin1 WW Domain,138999,26006
PDB,2NC4,BMRB Entry Tracking System,138999,26006
BMRB,26005,Solution Structure of N-Allosylated Pin1 WW Domain,139015,26007
BMRB,26006,Solution Structure of N-Galactosylated Pin1 WW Domain,139015,26007
BMRB,26008,Solution Structure of N-L-idosylated Pin1 WW Domain,139015,26007
PDB,2NC5,BMRB Entry Tracking System,139015,26007
BMRB,26005,Solution Structure of N-Allosylated Pin1 WW Domain,139031,26008
BMRB,26006,Solution Structure of N-Galactosylated Pin1 WW Domain,139031,26008
BMRB,26007,Solution Structure of N-Xylosylated Pin1 WW Domain,139031,26008
PDB,2NC6,BMRB Entry Tracking System,139031,26008
PDB,2NC7,BMRB Entry Tracking System,139047,26009
PDB,2NC8,BMRB Entry Tracking System,139063,26010
PDB,2NC9,BMRB Entry Tracking System,139083,26011
PDB,1US7,Two-domain fragment of Cdc37,139105,26012
PDB,2K5B,Human Cdc37-Hsp90 docking model,139105,26012
PDB,2N5X,C-terminal Domain of Cdc37,139105,26012
PDB,2NCA,BMRB Entry Tracking System,139105,26012
PDB,2NCE,BMRB Entry Tracking System,139125,26016
PDB,2NCG,BMRB Entry Tracking System,139149,26021
UniProt,S5DUP7,UniProt database,139149,26021
PDB,2NCH,BMRB Entry Tracking System,139167,26022
PDB,2NCI,BMRB Entry Tracking System,139186,26024
PDB,2NCJ,BMRB Entry Tracking System,139242,26026
BMRB,26028,"Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain",139265,26027
BMRB,26029,"Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139265,26027
BMRB,26030,"Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139265,26027
BMRB,26027,"Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG)",139282,26028
BMRB,26029,"Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139282,26028
BMRB,26030,"Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139282,26028
BMRB,26027,"Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG)",139301,26029
BMRB,26028,"Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain",139301,26029
BMRB,26030,"Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139301,26029
BMRB,26027,"Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG)",139319,26030
BMRB,26028,"Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain",139319,26030
BMRB,26029,"Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)",139319,26030
PDB,2NCL,BMRB Entry Tracking System,139338,26031
BMRB,26033,Structural insight for dynamics of r(CGG) motif RNA found in Fragile X syndrome/ Fragile X tremor ataxia at 25 degree C,139362,26032
PDB,2NCQ,BMRB Entry Tracking System,139362,26032
BMRB,26032,Structural insights of r(CGG) motif found in Fragile X Syndrome and Fragile-X associated tremor/ataxia syndrome (FXTAS) at 45 degree C,139378,26033
PDB,2NCR,BMRB Entry Tracking System,139378,26033
BMRB,26035,Chemical shifts for the same peptide in hexafluoroisopropanol,139394,26034
PDB,2NCS,BMRB Entry Tracking System,139394,26034
PDB,2NCT,Structure for the same peptide in hexafluoroisopropanol,139394,26034
BMRB,26034,Chemical shifts for the same peptide in DPC micelles,139413,26035
PDB,2NCS,Structure for the same peptide in DPC micelles,139413,26035
PDB,2NCT,BMRB Entry Tracking System,139413,26035
BMRB,26037,RWS21 structure in LPS,139434,26036
BMRB,26038,WWWKYE21 structure in LPS,139434,26036
PDB,2NCU,BMRB Entry Tracking System,139434,26036
BMRB,26036,KYE21 structure in LPS micelles,139448,26037
BMRB,26038,WWWKYE21 structure in LPS,139448,26037
PDB,2NCV,BMRB Entry Tracking System,139448,26037
BMRB,26036,KYE21 structure in LPS micelles,139462,26038
BMRB,26037,RWS21 structure in LPS,139462,26038
PDB,2NCW,BMRB Entry Tracking System,139462,26038
PDB,2NCY,BMRB Entry Tracking System,139476,26040
BMRB,26042,Solution NMR structures of BRD4 ET domain with LANA peptide,139490,26041
BMRB,26043,Solution NMR structures of BRD4 ET domain in complex with NSD3_3 peptide,139490,26041
PDB,2NCZ,BMRB Entry Tracking System,139490,26041
BMRB,26041,Solution NMR structures of BRD4 ET domain in complex with NSD3_1 peptide,139516,26042
BMRB,26043,Solution NMR structures of BRD4 ET domain in complex with NSD3_3 peptide,139516,26042
PDB,2ND0,BMRB Entry Tracking System,139516,26042
BMRB,26041,Solution NMR structures of BRD4 ET domain in complex with NSD3_1 peptide,139542,26043
BMRB,26042,Solution NMR structures of BRD4 ET domain with LANA peptide,139542,26043
PDB,2ND1,BMRB Entry Tracking System,139542,26043
BMRB,25665,"CDTa, residues 216-420",139566,26044
BMRB,26046,de novo mini protein EEH_04,139591,26045
PDB,2ND2,BMRB Entry Tracking System,139591,26045
BMRB,26045,de novo mini protein HHH_06,139615,26046
PDB,2ND3,BMRB Entry Tracking System,139615,26046
PDB,2ND5,BMRB Entry Tracking System,139639,26047
BMRB,26050,DK17 IN POPC:POPG:CHOLESTEROL:GM1 LUVS,139680,26049
BMRB,26051,STRUCTURES OF DK17 IN TBLE LUVS,139680,26049
PDB,2ND6,BMRB Entry Tracking System,139680,26049
BMRB,26049,STRUCTURE OF DK17 IN GM1 LUVS,139694,26050
BMRB,26051,STRUCTURES OF DK17 IN TBLE LUVS,139694,26050
PDB,2ND7,BMRB Entry Tracking System,139694,26050
BMRB,26049,STRUCTURE OF DK17 IN GM1 LUVS,139708,26051
BMRB,26050,DK17 IN POPC:POPG:CHOLESTEROL:GM1 LUVS,139708,26051
PDB,2ND8,BMRB Entry Tracking System,139708,26051
BMRB,26053,MapZ_SY,139722,26052
PDB,2ND9,BMRB Entry Tracking System,139722,26052
BMRB,26052,MapZ_QG,139744,26053
PDB,2NDA,BMRB Entry Tracking System,139744,26053
PDB,2NDB,BMRB Entry Tracking System,139765,26054
BMRB,26057,Solution Structure of Mutant of BMAP-28(1-18),139779,26055
PDB,2NDC,BMRB Entry Tracking System,139779,26055
PDB,2NDD,BMRB Entry Tracking System,139798,26056
BMRB,26055,Solution Structure of BMAP-28(1-18),139812,26057
PDB,2NDE,BMRB Entry Tracking System,139812,26057
BMRB,26060,AF9 domain with histone crontonylation,139845,26059
PDB,2NDF,BMRB Entry Tracking System,139845,26059
PDB,2NDG,BMRB Entry Tracking System,139883,26060
PDB,2NDH,BMRB Entry Tracking System,139908,26061
PDB,2YP2,crystal structure,139908,26061
PDB,3UB2,crystal structure,139908,26061
PDB,4FZ5,crystal structure,139908,26061
PDB,4LQD,crystal structure,139908,26061
PDB,2NDI,BMRB Entry Tracking System,139926,26062
BMRB,26065,PawS Derived Peptide 21 (PDP-21),139954,26064
BMRB,26066,PawS Derived Peptide 20 (PDP-20),139954,26064
PDB,2NDL,BMRB Entry Tracking System,139954,26064
BMRB,26064,PawS Derived Peptide 22 (PDP-22),139971,26065
BMRB,26066,PawS Derived Peptide 20 (PDP-20),139971,26065
PDB,2NDM,BMRB Entry Tracking System,139971,26065
BMRB,26064,PawS Derived Peptide 22 (PDP-22),139988,26066
BMRB,26065,PawS Derived Peptide 21 (PDP-21),139988,26066
PDB,2NDN,BMRB Entry Tracking System,139988,26066
BMRB,26516,amyloid B peptide and Congo Red,140632,26508
BMRB,26533,E. coli-purified sf-ALR,140809,26515
BMRB,26508,amyloid B peptide and lacmoid,140826,26516
PDB,5agq,PDBe entry,140842,26517
PDB,5aiw,PDBe entry,140862,26518
BMRB,26520,A39G FF domain,140881,26519
BMRB,26519,Abp1p-Ark1p system,140913,26520
BMRB,26527,WHB,140964,26526
BMRB,26528,UBCH10 in complex with WHB,140964,26526
BMRB,26529,WHB in complex with UBCH10,140964,26526
BMRB,26526,UBCH10,140979,26527
BMRB,26528,UBCH10 in complex with WHB,140979,26527
BMRB,26529,WHB in complex with UBCH10,140979,26527
BMRB,26526,UBCH10,140994,26528
BMRB,26527,WHB,140994,26528
BMRB,26529,WHB in complex with UBCH10,140994,26528
BMRB,26526,UBCH10,141010,26529
BMRB,26527,WHB,141010,26529
BMRB,26528,UBCH10 in complex with WHB,141010,26529
BMRB,26515,FAD-free sf-ALR,141076,26533
BMRB,25517,"Short hydrophobic peptide, 11mer, HAEGTFTSDFF",141131,26536
BMRB,26537,"Short hydrophobic peptide, 11mer, H(AIB)EGKFTSEF(PH8)",141131,26536
BMRB,26538,"Short hydrophobic peptide, 11mer, H(KCY)EG(HCS)FTSDF(PH8)",141131,26536
PDB,2N09,BMRB Entry Tracking System,141131,26536
BMRB,25517,"Short hydrophobic peptide, 11mer, HAEGTFTSDFF",141146,26537
BMRB,26536,"Short hydrophobic peptide, 11mer, H(AIB)EGTFTSDFF",141146,26537
BMRB,26538,"Short hydrophobic peptide, 11mer, H(KCY)EG(HCS)FTSDF(PH8)",141146,26537
BMRB,26831,M337P mutant,145607,26827
PDB,2N0N,BMRB Entry Tracking System,141146,26537
BMRB,25517,"Short hydrophobic peptide, 11mer, HAEGTFTSDFF",141163,26538
BMRB,26536,"Short hydrophobic peptide, 11mer, H(AIB)EGTFTSDFF",141163,26538
BMRB,26537,"Short hydrophobic peptide, 11mer, H(AIB)EGKFTSEF(PH8)",141163,26538
PDB,2N0I,BMRB Entry Tracking System,141163,26538
PDB,4X50,Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside,141181,26541
PDB,4X5P,Crystal structure of FimH in complex with a benzoyl-amidophenyl alpha-D-mannopyranoside,141181,26541
PDB,4X5Q,Crystal structure of FimH in complex with 5-nitro-indolinylphenyl alpha-D-mannopyranoside,141181,26541
PDB,4X5R,Crystal structure of FimH in complex with a squaryl-phenyl alpha-D-mannopyranoside derivative,141181,26541
BMRB,26546,SpaO-OrgB,141197,26543
BMRB,26545,Prostate associated gene 4 phosphorylated,141214,26544
BMRB,26544,Prostate associated gene 4,141228,26545
BMRB,26543,SpaO,141243,26546
BMRB,25552,human Polo-box 3,141262,26547
PDB,2N19,BMRB Entry Tracking System,141262,26547
PDB,4YYP,Crystal structure of human PLK4-PB3 in complex with STIL-CC,141262,26547
BMRB,5700,25.8 kDa DNA binding domain of the human p63 protein,141324,26551
PDB,5AJ1,PDBe entry,141355,26553
PDB,1K1S,"Dbh polymerase from Sulfolobus acidocaldarius, apo form crystal structure",141438,26564
PDB,5a17,SOLE element of oskar mRNA,141484,26568
PDB,5a18,"SOLE element of oskar mRNA, after water refinement",141484,26568
BMRB,25399,"1H, 15N, 13C resonance assignment of the aortic medial amyloid protein medin in denaturing conditions.",141595,26576
BMRB,26582,Dark-state Cyanobacteriochrome (NpR6012g4),141610,26577
PDB,5a3g,PDBe entry,141660,26580
BMRB,26577,Light-adapted Cyanobacteriochrome NpR6012g4,141693,26582
BMRB,26584,"Backbone 1H, 13C and 15N chemical shift assignments for the ternary L28F ecDHFR:FOLATE:NADP+ complex",141711,26583
BMRB,26585,"Backbone 1H, 13C and 15N chemical shift assignments for the binary L28F ecDHFR:NADPH complex",141711,26583
BMRB,26583,"Backbone 1H, 13C and 15N chemical shift assignments for the ternary L28F ecDHFR:TETRAHYDROFOLATE:NADP+ complex",141730,26584
BMRB,26585,"Backbone 1H, 13C and 15N chemical shift assignments for the binary L28F ecDHFR:NADPH complex",141730,26584
BMRB,26583,"Backbone 1H, 13C and 15N chemical shift assignments for the ternary L28F ecDHFR:TETRAHYDROFOLATE:NADP+ complex",141749,26585
BMRB,26584,"Backbone 1H, 13C and 15N chemical shift assignments for the ternary L28F ecDHFR:FOLATE:NADP+ complex",141749,26585
PDB,4mez,,141766,26586
BMRB,26588,ROQ-SELEX consensus hexa-loop RNA,141780,26587
BMRB,26587,ROQ-Ox40hexa-loop RNA,141796,26588
BMRB,16598,Chimera cTEM-17m,141826,26590
BMRB,6024,Parent TEM-1,141826,26590
PDB,4ID4,Chimera cTEM-17m,141826,26590
PDB,4R4R,Chimera cTEM-19m,141826,26590
PDB,4R4S,Chimera cTEM-19m,141826,26590
BMRB,26592,LcrG,141840,26591
BMRB,26591,PcrG9-76,141854,26592
BMRB,26595,hTRF1 bound to ADP-DnaK,141889,26594
BMRB,26594,hTRF1 monomer,141903,26595
BMRB,26598,DNA gyrase B subunit,141918,26597
BMRB,26597,DNA gyrase B,141932,26598
PDB,5AJS,X-ray structure of coiled-coil motif of THAP11,141948,26599
BMRB,26601,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N30 beta subunit",141964,26600
BMRB,26602,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor D10 beta subunit",141964,26600
BMRB,26600,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit",141980,26601
BMRB,26602,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor D10 beta subunit",141980,26601
BMRB,26600,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit",141996,26602
BMRB,26601,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N30 beta subunit",141996,26602
SP,Q9BXW4,,142012,26603
BMRB,5500,parkin ubiquitin-like domain,142047,26605
PDB,5C1Z,,142047,26605
PDB,5C23,,142047,26605
BMRB,26609,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142078,26608
BMRB,26610,active domains of the type II topoisomerases (step free form),142078,26608
BMRB,26611,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142078,26608
BMRB,26608,active domains of the type II topoisomerases (free form),142092,26609
BMRB,26610,active domains of the type II topoisomerases (step free form),142092,26609
BMRB,26611,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142092,26609
BMRB,26608,active domains of the type II topoisomerases (free form),142108,26610
BMRB,26609,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142108,26610
BMRB,26611,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142108,26610
BMRB,26608,active domains of the type II topoisomerases (free form),142122,26611
BMRB,26609,active domains of the type II topoisomerases (with a bis-pyridylurea inhibitor),142122,26611
BMRB,26610,active domains of the type II topoisomerases (step free form),142122,26611
BMRB,26613,Skp,142138,26612
BMRB,26612,tOmpA,142152,26613
BMRB,26620,Barnase dCGAC,142253,26619
BMRB,26619,Barnase monomer,142270,26620
BMRB,26624,integrin beta1 TM/CT,142288,26623
BMRB,26623,integrin beta1 TM/CT,142302,26624
BMRB,26627,CaM+Fas47-83,142332,26626
BMRB,26626,CaM+Fas,142352,26627
BMRB,26631,MATH-PUC,142389,26629
PDB,2CR2,,142389,26629
BMRB,26632,Protein G Domain Beta-1 Sequence H,142405,26630
BMRB,26629,MATH,142421,26631
PDB,2CR2,,142421,26631
BMRB,26630,Protein G Domain Beta-1 Wild-Type,142436,26632
BMRB,26823,wild type,145625,26828
BMRB,16876,Entry containing full assignment for the same protein using MES buffer and one specific condition of T/pH. It is the basis of the present assignments.,142484,26636
BMRB,16391,PEG-precipitated human alpha B crystallin assigned by conventional 13C-detected solid-state MAS NMR,142560,26640
BMRB,25527,Solution-state NMR assignment of the excised alpha crystallin domain of human alpha B crystallin.,142560,26640
PDB,2KLR,Solid-state NMR structure of the alpha-crystallin domain in alphaB-crystallin oligomers,142560,26640
PDB,2N0K,"Structure of the alpha-crystallin domain from human, HSPB5",142560,26640
PDB,2YGD,Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach,142560,26640
PDB,3L1G,Crystal structures of truncated alphaA and alphaB crystallins,142560,26640
PDB,4M5S,Human alphaB crystallin core domain in complex with C-terminal peptide,142560,26640
PDB,4QMD,X-Ray crystal structure of envoplakin plakin repeat domain.,142603,26642
BMRB,25792,p65dd/p50dd,142682,26647
PDB,2N78,BMRB Entry Tracking System,142712,26649
BMRB,26652,Akt_PHD (CaM_Complex),142742,26651
BMRB,26651,Akt_PHD,142759,26652
BMRB,26655,emerin 67-170 (8M urea),142790,26654
BMRB,26654,emerin 67-170 (0 Mc),142804,26655
PDB,3KKC,"entry containing crystal structure of nickel-bound form of SczA, deposited by another group",142851,26658
BMRB,26660,src-lactose,142869,26659
BMRB,26661,src-6'-sialyllactose,142869,26659
BMRB,26659,src,142887,26660
BMRB,26661,src-6'-sialyllactose,142887,26660
BMRB,26659,src,142907,26661
BMRB,26660,src-lactose,142907,26661
BMRB,26663,c-Myc,142925,26662
BMRB,26662,"Backbone 1H, 13C and 15N Chemical Shift Assignments for c-Myc-1-88",142941,26663
BMRB,26665,Calmodulin (D58N),142971,26667
BMRB,26666,Calmodulin (D95N),142971,26667
BMRB,26668,Calmodulin (D58N):smMLCK(p),142971,26667
BMRB,26669,Calmodulin (D95N):smMLCK(p),142971,26667
BMRB,26670,Calmodulin (E84K):nNOS(p),142971,26667
BMRB,26665,Calmodulin (D58N),142987,26670
BMRB,26666,Calmodulin (D95N),142987,26670
BMRB,26667,Calmodulin (E84K),142987,26670
BMRB,26668,Calmodulin (D58N):smMLCK(p),142987,26670
BMRB,26669,Calmodulin (D95N):smMLCK(p),142987,26670
BMRB,26675,GVIIJ_SSEA,143022,26674
BMRB,26674,GVIIJ[C24S],143038,26675
BMRB,26677,CP2,143054,26676
BMRB,26676,CP1,143070,26677
BMRB,26679,pEAbeta(3-42),143087,26678
BMRB,26680,pEAbeta(3-42),143087,26678
BMRB,26678,Amyloid-beta(1-42),143102,26679
BMRB,26680,pEAbeta(3-42),143102,26679
BMRB,26678,Amyloid-beta(1-42),143118,26680
BMRB,26679,pEAbeta(3-42),143118,26680
BMRB,26682,CaM12 (apo form),143136,26681
BMRB,26683,CaM34 (apo form),143136,26681
BMRB,26685,CaM12 (complex with Ca),143136,26681
BMRB,26686,CaM34 (complex with Ca),143136,26681
BMRB,26687,CaM34 (complex with iNOS,143136,26681
BMRB,26681,CaM1234 (apo form),143150,26682
BMRB,26683,CaM34 (apo form),143150,26682
BMRB,26685,CaM12 (complex with Ca),143150,26682
BMRB,26686,CaM34 (complex with Ca),143150,26682
BMRB,26687,CaM34 (complex with iNOS,143150,26682
BMRB,26681,CaM1234 (apo form),143164,26683
BMRB,26682,CaM12 (apo form),143164,26683
BMRB,26685,CaM12 (complex with Ca),143164,26683
BMRB,26686,CaM34 (complex with Ca),143164,26683
BMRB,26687,CaM34 (complex with iNOS,143164,26683
BMRB,26681,CaM1234 (apo form),143194,26685
BMRB,26682,CaM12 (apo form),143194,26685
BMRB,26683,CaM34 (apo form),143194,26685
BMRB,26686,CaM34 (complex with Ca),143194,26685
BMRB,26687,CaM34 (complex with iNOS,143194,26685
BMRB,26681,CaM1234 (apo form),143210,26686
BMRB,26682,CaM12 (apo form),143210,26686
BMRB,26683,CaM34 (apo form),143210,26686
BMRB,26685,CaM12 (complex with Ca),143210,26686
BMRB,26687,CaM34 (complex with iNOS,143210,26686
BMRB,26681,CaM1234 (apo form),143226,26687
BMRB,26682,CaM12 (apo form),143226,26687
BMRB,26683,CaM34 (apo form),143226,26687
BMRB,26685,CaM12 (complex with Ca),143226,26687
BMRB,26686,CaM34 (complex with Ca),143226,26687
BMRB,26696,Complex of PqqD + PqqA + PqqE,143262,26690
BMRB,25860,DHFR-NADPH-Trimethoprim,143313,26693
BMRB,25861,DHFR-NADPH,143313,26693
BMRB,26694,S1-DHFR-NADPH-Trimethoprim,143313,26693
BMRB,26695,S1-DHFR-NADPH,143313,26693
BMRB,25860,DHFR-NADPH-Trimethoprim,143330,26694
BMRB,25861,DHFR-NADPH,143330,26694
BMRB,26693,DHFR-apo,143330,26694
BMRB,26695,S1-DHFR-NADPH,143330,26694
BMRB,25860,DHFR-NADPH-Trimethoprim,143351,26695
BMRB,25861,DHFR-NADPH,143351,26695
BMRB,26693,DHFR-apo,143351,26695
BMRB,26694,S1-DHFR-NADPH-Trimethoprim,143351,26695
BMRB,16969,"Structural basis for homodimerization of the Src-associated during mitosis, 68 kD protein (Sam68) Qua1 domain",143400,26700
BMRB,26701,T-STAR KH,143400,26700
BMRB,26700,Sam68 STAR,143415,26701
BMRB,16166,"1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1)",143430,26702
BMRB,16800,"1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) in presence of 50%TFE",143430,26702
BMRB,19055,"1H, 15N and 13C backbone resonance assignments of domain 2 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1)",143430,26702
GB,AJ238799.1,"Hepatitis C virus type 1b complete genome, isolate Con1",143430,26702
PDB,2M5L,"A Proline-Tryptophan Turn in the Intrinsically Disordered    
Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus    
RNA Replication",143430,26702
PDB,4IS7,this is the wild type X-ray structure,143469,26705
BMRB,19120,Chemical shifts for the beta-2 Microglobulin subunit of HLA-B*27:05/pVIPR,143531,26710
BMRB,25714,Chemical shifts for the heavy chain of of HLA-B*27:05/pVIPR,143531,26710
BMRB,19121,Chemical shifts for the beta-2 Microglobulin subunit of HLA-B*27:05/TIS,143572,26711
BMRB,25711,Chemical shifts for the heavy chain of of HLA-B*27:05/TIS,143572,26711
BMRB,26710,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR,143572,26711
BMRB,26712,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*B*27:09 in complex with the peptide pVIPR,143572,26711
BMRB,26713,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*B*27:09 in complex with the peptide TIS,143572,26711
BMRB,26714,Relaxation and model-free data from human beta-2-microglobulin,143572,26711
BMRB,19123,Chemical shifts for the beta-2 Microglobulin subunit of HLA-B*27:09/pVIPR,143617,26712
BMRB,25713,Chemical shifts for the heavy chain of of HLA-B*27:09/pVIPR,143617,26712
BMRB,26710,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR,143617,26712
BMRB,26711,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide TIS,143617,26712
BMRB,26713,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:09 in complex with the peptide TIS,143617,26712
BMRB,26714,Relaxation and model-free data from human beta-2-microglobulin,143617,26712
BMRB,19116,Chemical shifts for the beta-2 Microglobulin subunit of HLA-B*27:09/TIS,143662,26713
BMRB,25715,Chemical shifts for the heavy chain of of HLA-B*27:09/TIS,143662,26713
BMRB,26710,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR,143662,26713
BMRB,26711,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide TIS,143662,26713
BMRB,26712,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:09 in complex with the peptide pVIPR,143662,26713
BMRB,26714,Relaxation and model-free data from human beta-2-microglobulin,143662,26713
BMRB,19099,"1H, 13C and 15N chemical shifts of human beta-2-microglobulin in solution",143707,26714
BMRB,26710,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR,143707,26714
BMRB,26711,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide TIS,143707,26714
BMRB,26712,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*B*27:09 in complex with the peptide pVIPR,143707,26714
BMRB,26713,Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*B*27:09 in complex with the peptide TIS,143707,26714
BMRB,18397,"nanocrystalline GB1 1H, 13C, 15N assignments",143744,26716
BMRB,26720,Phosphorylated Ash1 420-500,143799,26719
BMRB,26719,Non-phosphorylated Ash1 420-500,143813,26720
BMRB,26724,C-terminal domain of Tetrahymena Tcb2 in the presence of calcium,143865,26723
NCBI,P09226.2,25 kDa calcium-binding protein TCBP-25,143865,26723
NCBI,XP_001007754.3,25 kDa calcium-binding protein [Tetrahymena thermophilia SB210],143865,26723
BMRB,26723,C-terminal domain of Tetrahymena Tcb2 in the absence of calcium,143888,26724
NCBI,P09226.2,25 kDa calcium-binding protein TCBP-25,143888,26724
NCBI,XP_001007754.3,25 kDa calcium-binding protein [Tetrahymena thermophilia SB210],143888,26724
BMRB,26731,Paired domain of Pax5 in complex with DNA,143975,26730
BMRB,26730,Paired domain of Pax5,143989,26731
BMRB,26733,Backbone Assignments for MAPK p38g,144005,26732
BMRB,26732,Methyl Assignments for MAPK p38g,144024,26733
BMRB,16087,Chemical shift list of 15N-labelled PAF,144041,26734
BMRB,19657,Chemical shift list of 15N-13C labelled PAF,144041,26734
BMRB,26742,PHD2 Zn(II) 2OG CODD,144117,26741
PDB,2G19,X-Ray crystal structure,144117,26741
PDB,3HQR,X-Ray crystal structure,144117,26741
PDB,3OUJ,X-Ray crystal structure,144117,26741
BMRB,26741,PHD2 Zn(II) 2OG,144142,26742
PDB,2G19,X-Ray crystal structure,144142,26742
PDB,3HQR,X-Ray crystal structure,144142,26742
PDB,3OUJ,X-Ray crystal structure,144142,26742
PDB,1AWZ,"3D SOLUTION STRUCTURE OF HUMAN ANGIOGENIN DETERMINED BY 1H, 15N NMR SPECTROSCOPY, 30 STRUCTURES",144236,26748
PDB,2ANG,CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN OF THE MET(-1) FORM,144236,26748
BMRB,25132,"NMR study of non-structural proteins - 1H, 13C, 15N resonance assignment of macro doamin of Venezuelan equine encephalitis virus (VEEV)",144311,26753
PDB,3GQE,Crystal structure of macro domain of Venezuelan Equine Encephalitis virus,144311,26753
PDB,3GQO,Crystal structure of macro domain of Venezuelan Equine Encephalitis virus in complex with ADP-ribose,144311,26753
BMRB,26757,human F602S Glucocorticoid receptor Ligand Binding Domain,144361,26756
BMRB,26756,human wildtype Glucocorticoid receptor Ligand Binding Domain,144383,26757
BMRB,26571,"1H, 13C and 15N NMR assignments in Ca2+ bound form",144441,26760
BMRB,26786,Elk1 C-terminus aa309-429 - 8 phosphorylated sites (pS337-pT354-pT364-pT369-pS384-pS390-pT418-pS423),144471,26762
BMRB,18777,,144486,26763
PDB,2mou,,144486,26763
PDB,3OOI,Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine,144558,26767
BMRB,26776,response regulator CheY3 at pH 7.25 with BeF3-,144588,26769
BMRB,26777,response regulator CheY3 at pH 4.5 with BeF3-,144588,26769
BMRB,26778,response regulator CheY3 at pH 4.5 in the absence of BeF3-,144588,26769
PDB,4GEW,"This PDB entry contains crystal structure of the C. elegans TDP2 full-length protein, including the N-terminal Ubiquitin Association domain",144622,26771
BMRB,26773,a17,144639,26772
BMRB,26772,Assembly-1,144655,26773
NCBI,XP_001351616.1,Plasmodium falciparum SUMO protein sequence ID.,144685,26775
BMRB,26769,response regulator CheY3 at pH 7.4 in the absence of BeF3-,144706,26776
BMRB,26777,response regulator CheY3 at pH 4.5 with BeF3-,144706,26776
BMRB,26778,response regulator CheY3 at pH 4.5 in the absence of BeF3-,144706,26776
BMRB,26769,response regulator CheY3 at pH 7.4 in the absence of BeF3-,144728,26777
BMRB,26776,response regulator CheY3 at pH 7.25 with BeF3-,144728,26777
BMRB,26778,response regulator CheY3 at pH 4.5 in the absence of BeF3-,144728,26777
BMRB,26769,response regulator CheY3 at pH 7.4 in the absence of BeF3-,144750,26778
BMRB,26776,response regulator CheY3 at pH 7.25 with BeF3-,144750,26778
BMRB,26777,response regulator CheY3 at pH 4.5 with BeF3-,144750,26778
PDB,1QB0,crystal structure,144769,26779
BMRB,26784,UBv-APC11,144828,26783
BMRB,26785,APC11-UBv,144828,26783
BMRB,26783,UBv,144843,26784
BMRB,26785,APC11-UBv,144843,26784
BMRB,26783,UBv,144858,26785
BMRB,26784,UBv-APC11,144858,26785
BMRB,26762,Elk1 C-terminus aa309-429 non-phosphorylated,144873,26786
BMRB,26769,CheY3 at pH 7.4,144932,26789
BMRB,26776,CheY3 at pH 7.25 with BeF3-,144932,26789
BMRB,26777,CheY3 at pH 4.5 with BeF3-,144932,26789
BMRB,26778,CheY3 at pH 4.5,144932,26789
BMRB,26793,Backbone assignment of p24 GOLD domain,145004,26792
BMRB,26792,Backbone assignment of p23 GOLD domain,145018,26793
BMRB,26795,"NMR Assignment of L-Dfp7,D-Trp8-SRIF",145032,26794
BMRB,26796,"NMR Assignment of L-Dfp11,D-Trp8-SRIF",145032,26794
BMRB,26797,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8-SRIF",145032,26794
BMRB,26798,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145032,26794
BMRB,26799,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8, L-Dfp11-SRIF",145032,26794
BMRB,26794,"NMR Assignment of L-Dfp6,D-Trp8-SRIF",145051,26795
BMRB,26796,"NMR Assignment of L-Dfp11,D-Trp8-SRIF",145051,26795
BMRB,26797,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8-SRIF",145051,26795
BMRB,26798,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145051,26795
BMRB,26799,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8, L-Dfp11-SRIF",145051,26795
BMRB,26794,"NMR Assignment of L-Dfp6,D-Trp8-SRIF",145070,26796
BMRB,26795,"NMR Assignment of L-Dfp7,D-Trp8-SRIF",145070,26796
BMRB,26797,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8-SRIF",145070,26796
BMRB,26798,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145070,26796
BMRB,26799,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8, L-Dfp11-SRIF",145070,26796
BMRB,26794,"NMR Assignment of L-Dfp6,D-Trp8-SRIF",145089,26797
BMRB,26795,"NMR Assignment of L-Dfp7,D-Trp8-SRIF",145089,26797
BMRB,26796,"NMR Assignment of L-Dfp11,D-Trp8-SRIF",145089,26797
BMRB,26798,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145089,26797
BMRB,26799,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8, L-Dfp11-SRIF",145089,26797
BMRB,26794,"NMR Assignment of L-Dfp6,D-Trp8-SRIF",145108,26798
BMRB,26795,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145108,26798
BMRB,26796,"NMR Assignment of L-Dfp11,D-Trp8-SRIF",145108,26798
BMRB,26797,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8-SRIF",145108,26798
BMRB,26799,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8, L-Dfp11-SRIF",145108,26798
BMRB,26794,"NMR Assignment of L-Dfp6,D-Trp8-SRIF",145127,26799
BMRB,26795,"NMR Assignment of L-Dfp7,D-Trp8-SRIF",145127,26799
BMRB,26796,"NMR Assignment of L-Dfp11,D-Trp8-SRIF",145127,26799
BMRB,26797,"NMR Assignment of L-Dfp6,L-Msa7,D-Trp8-SRIF",145127,26799
BMRB,26798,"NMR Assignment of L-Dfp11,L-Msa7,D-Trp8-SRIF",145127,26799
PDB,1ELK,Crystal Structure of Tom1 VHS Domain,145252,26806
BMRB,26808,DNA-binding domain of the human Egr-1 - DNA complex,145269,26807
BMRB,26807,DNA-binding domain of the human Egr-1 in the free state,145288,26808
BMRB,26812,Complex I of Retinal and rhodopsin,145343,26811
BMRB,26813,Complex II of Retinal and Metarhodopsin II,145343,26811
BMRB,26811,rhodopsin,145359,26812
BMRB,26813,Complex II of Retinal and Metarhodopsin II,145359,26812
BMRB,26811,rhodopsin,145375,26813
BMRB,26812,Complex I of Retinal and rhodopsin,145375,26813
BMRB,19224,PTP1B (residues 1-393),145391,26814
PDB,5KA0,,145391,26814
BMRB,26819,CHIP-TPR/Hsp70p1,145448,26818
BMRB,26818,CHIP-TPR,145465,26819
BMRB,26824,Lunasin monomer (reduced form),145482,26820
BMRB,26825,Lunasin monomer (oxidized form),145482,26820
BMRB,26826,A321G mutant,145530,26823
BMRB,26827,A321V mutant,145530,26823
BMRB,26828,A326P mutant,145530,26823
BMRB,26829,Q331K mutant,145530,26823
BMRB,26830,M337V mutant,145530,26823
BMRB,26831,M337P mutant,145530,26823
BMRB,26820,Lunasin monomer (16-43),145557,26824
BMRB,26825,Lunasin monomer (oxidized form),145557,26824
BMRB,26820,Lunasin monomer (16-43),145573,26825
BMRB,26824,Lunasin monomer (reduced form),145573,26825
BMRB,26823,wild type,145589,26826
BMRB,26827,A321V mutant,145589,26826
BMRB,26828,A326P mutant,145589,26826
BMRB,26829,Q331K mutant,145589,26826
BMRB,26830,M337V mutant,145589,26826
BMRB,26831,M337P mutant,145589,26826
BMRB,26823,wild type,145607,26827
BMRB,26827,A321V mutant,145607,26827
BMRB,26828,A326P mutant,145607,26827
BMRB,26829,Q331K mutant,145607,26827
BMRB,26830,M337V mutant,145607,26827
BMRB,26826,A321G mutant,145625,26828
BMRB,26827,A321V mutant,145625,26828
BMRB,26829,Q331K mutant,145625,26828
BMRB,26830,M337V mutant,145625,26828
BMRB,26831,M337P mutant,145625,26828
BMRB,26823,wild type,145643,26829
BMRB,26826,A321G mutant,145643,26829
BMRB,26827,A321V mutant,145643,26829
BMRB,26828,A326P mutant,145643,26829
BMRB,26830,M337V mutant,145643,26829
BMRB,26831,M337P mutant,145643,26829
BMRB,26823,wild type,145661,26830
BMRB,26826,A321G mutant,145661,26830
BMRB,26827,A321V mutant,145661,26830
BMRB,26828,A326P mutant,145661,26830
BMRB,26829,Q331K mutant,145661,26830
BMRB,26831,M337P mutant,145661,26830
BMRB,26823,wild type,145679,26831
BMRB,26826,A321G mutant,145679,26831
BMRB,26827,A321V mutant,145679,26831
BMRB,26828,A326P mutant,145679,26831
BMRB,26829,Q331K mutant,145679,26831
BMRB,26830,M337V mutant,145679,26831
BMRB,19224,PTP1B (residues 1-393),145697,26832
PDB,5KA2,,145697,26832
PDB,4K1O,,145714,26833
BMRB,19224,,145743,26835
BMRB,26836,Protein Tyrosine Phosphatase 1B L192A variant,145743,26835
BMRB,26837,Protein Tyrosine Phosphatase 1B N193A variant,145743,26835
BMRB,26838,Protein Tyrosine Phosphatase 1B (1-301) in complex with TCS401,145743,26835
PDB,5KA4,,145743,26835
BMRB,19224,,145760,26836
BMRB,26835,Protein Phosphatase 1B T178A variant,145760,26836
BMRB,26837,Protein Tyrosine Phosphatase 1B N193A variant,145760,26836
BMRB,26838,Protein Tyrosine Phosphatase 1B (1-301) in complex with TCS401,145760,26836
PDB,5KA8,,145760,26836
BMRB,19224,,145777,26837
BMRB,26835,Protein Phosphatase 1B T178A variant,145777,26837
BMRB,26836,Protein Tyrosine Phosphatase 1B L192A variant,145777,26837
BMRB,26838,Protein Tyrosine Phosphatase 1B (1-301) in complex with TCS401,145777,26837
BMRB,19224,,145794,26838
BMRB,26835,Protein Phosphatase 1B T178A variant,145794,26838
BMRB,26836,Protein Tyrosine Phosphatase 1B L192A variant,145794,26838
BMRB,26837,Protein Tyrosine Phosphatase 1B N193A variant,145794,26838
PDB,5K9W,,145794,26838
BMRB,15283,B3 Immunoglobulin-Binding Domain of Streptococcal Protein G (GB3) by MAS-NMR,145923,26845
BMRB,18531,Three-State Ensemble obtained from eNOEs of the Third Immunoglobulin Binding Domain of Protein G (GB3),145923,26845
BMRB,2575,Sequence-Specific 1H NMR Assignments and Secondary Structure of the Streptococcal Protein G B2-Domain,145923,26845
BMRB,25807,Sidechain chi1 distribution in B3 domain of protein G,145923,26845
BMRB,5569,15N relaxation rates for backbone of GB1,145923,26845
BMRB,5839,Differentiating Between Conformational Exchange and Anisotropic Diffusion in the B3 Domain of Protein G,145923,26845
GB,AAA26921,,145923,26845
GB,AAB27024,,145923,26845
GB,ABL60854,,145923,26845
GB,ABL60859,,145923,26845
GB,ABO76907,,145923,26845
PDB,1IGC,,145923,26845
PDB,1IGD,,145923,26845
PDB,1P7E,,145923,26845
PDB,1PGX,,145923,26845
PDB,2IGD,,145923,26845
PDB,2IGH,,145923,26845
PDB,2LUM,,145923,26845
PDB,2N7J,,145923,26845
PDB,2NMQ,,145923,26845
PDB,2OED,,145923,26845
BMRB,19224,protein phosphatase 1B (PTP1B) residues 1-393,145962,26847
PDB,5KAD,,145962,26847
BMRB,26851,"COMT monomer, Sinefungin, DNC, Mg",145981,26848
PDB,3BWM,BMRB Entry Tracking System,145981,26848
PDB,3BWY,BMRB Entry Tracking System,145981,26848
BMRB,26850,Spy,146003,26849
BMRB,26849,Spy,146018,26850
BMRB,26848,"COMT monomer, SAM, DNC, Mg",146035,26851
PDB,3BWM,BMRB Entry Tracking System,146035,26851
PDB,3BWY,BMRB Entry Tracking System,146035,26851
PDB,2BHM,X-ray crystal structure for preiplasmic fragment of VirB8,146057,26852
BMRB,26861,Tunicate_crystallin_Ca2+form,146151,26860
BMRB,26860,Tunicate_EDTA_noCa2+,146173,26861
BMRB,26864,ScribPDZ4withp22phoxC10,146207,26863
BMRB,26863,ScribPDZ4apo,146224,26864
PDB,5EMB,SNX27 DZ domain crystal structure in complex with phosphorylated PDZ peptide binding motif.,146240,26866
BMRB,26876,VcPth-N14D mutant,146340,26875
BMRB,26877,VcPth-N72D mutant,146340,26875
BMRB,26878,VcPth-N118D mutant,146340,26875
BMRB,26875,VcPth-H24N mutant,146357,26876
BMRB,26877,VcPth-N72D mutant,146357,26876
BMRB,26878,VcPth-N118D mutant,146357,26876
BMRB,26875,VcPth-H24N mutant,146374,26877
BMRB,26876,VcPth-N14D mutant,146374,26877
BMRB,26878,VcPth-N118D mutant,146374,26877
BMRB,26875,VcPth-H24N mutant,146390,26878
BMRB,26876,VcPth-N14D mutant,146390,26878
BMRB,26877,VcPth-N72D mutant,146390,26878
PDB,2Q1E,X-ray diffraction structure of the soluble dimer form of the amyloidogenic light chain protein AL-09,146407,26879
PDB,2Q20,"X-ray diffraction structure of the soluble dimer form of the germline counterpart variable light chain protein to AL-09, kI O18/O8",146407,26879
BMRB,17332,Solution structure of the talin Vbs2b domain,146424,26880
PDB,2L7A,Solution structure of the talin Vbs2b domain,146424,26880
BMRB,26886,Ferrous THB1,146499,26885
PDB,4XDI,BMRB Entry Tracking System,146499,26885
BMRB,26885,Ferric THB1,146515,26886
PDB,4xdi,3D structure of the ferric state,146515,26886
BMRB,26888,HBHA and Heparin,146531,26887
BMRB,26887,HBHA apo form,146546,26888
BMRB,26894,monomeric SOD1 (with lysozyme),146618,26893
BMRB,26893,monomeric SOD1 (without lysozyme),146633,26894
BMRB,26903,P_delta[122-160],146663,26902
BMRB,26904,P1-163_tetramer,146663,26902
BMRB,26905,P-S23C_tetramer,146663,26902
BMRB,26906,P-CTD,146663,26902
EMBL,M22644,Genomic RNA sequence,146663,26902
SP,P12579,Protein sequence,146663,26902
BMRB,26902,P1-126,146678,26903
BMRB,26904,P1-163_tetramer,146678,26903
BMRB,26905,P-S23C_tetramer,146678,26903
BMRB,26906,P-CTD,146678,26903
EMBL,M22644,Genomic RNA sequence,146678,26903
SP,P12579,Protein sequence,146678,26903
BMRB,26902,P1-126,146693,26904
BMRB,26903,P_delta[122-160],146693,26904
BMRB,26905,P-S23C_tetramer,146693,26904
BMRB,26906,P-CTD,146693,26904
EMBL,M22644,Genomic RNA sequence,146693,26904
SP,P12579,Protein sequence,146693,26904
BMRB,26902,P1-126,146708,26905
BMRB,26903,P_delta[122-160],146708,26905
BMRB,26904,P1-163_tetramer,146708,26905
BMRB,26906,P-CTD,146708,26905
EMBL,M22644,Genomic RNA sequence,146708,26905
SP,P12579,Protein sequence,146708,26905
BMRB,26902,P1-126,146724,26906
BMRB,26903,P_delta[122-160],146724,26906
BMRB,26904,P1-163_tetramer,146724,26906
BMRB,26905,P-S23C_tetramer,146724,26906
EMBL,M22644,Genomic RNA sequence,146724,26906
SP,P12579,Protein sequence,146724,26906
BMRB,18309,FliGn homodimer,146755,26908
BMRB,18310,Labeled FliGn bound to unlabeled FliFc peptide,146755,26908
BMRB,11028,rigid core of the HET-s(218-289) prion protein in its amyloid conformation,146820,26913
BMRB,11064,rigid core of the HET-s(218-289) prion protein in its amyloid conformation,146820,26913
PDB,5LM1,BMRB Entry Tracking System,146841,26914
PDB,5LM2,BMRB Entry Tracking System,146841,26914
BMRB,18689,"Backbone 1H, 13C, and 15N backbone resonance assignments of the TPR2A domain of mouse STI1",146914,26920
BMRB,18691,"Backbone 1H, 13C, and 15N backbone resonance assignments of the TPR1 domain of mouse STI1",146914,26920
SP,G5ECJ4,C. elegans MEC-8,146944,26922
BMRB,26925,huPrP23-144 amyloid fibrils,146979,26924
BMRB,26926,ShaPrP23-144 amyloid fibrils,146979,26924
BMRB,26924,mouse PrP23-144 amyloid fibril,146997,26925
BMRB,26926,ShaPrP23-144 amyloid fibrils,146997,26925
BMRB,26924,mouse PrP23-144 amyloid fibril,147015,26926
BMRB,26925,huPrP23-144 amyloid fibrils,147015,26926
BMRB,26873,linked NS2B-NS3 Protease of Zika Virus after self-cleavage,147033,26927
BMRB,26928,unlinked NS2B-NS3 Protease of Zika Virus in complex without acetyl-lysine-arginine,147033,26927
BMRB,26933,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde,147033,26927
BMRB,26873,linked NS2B-NS3 Protease of Zika Virus after self-cleavage,147052,26928
BMRB,26927,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine,147052,26928
BMRB,26933,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde,147052,26928
PDB,1o6d,crystal structure of MTTTm,147087,26932
BMRB,26873,linked NS2B-NS3 Protease of Zika Virus after self-cleavage,147101,26933
BMRB,26927,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine,147101,26933
BMRB,26928,unlinked NS2B-NS3 Protease of Zika Virus in complex without acetyl-lysine-arginine,147101,26933
PDB,5H6V,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde,147101,26933
BMRB,26937,nanobody 39,147158,26936
BMRB,26936,nanobody 33,147174,26937
BMRB,26939,ASH1-mRNA,147190,26938
PDB,5MOH,BMRB Entry Tracking System,147190,26938
PDB,5MOI,BMRB Entry Tracking System,147190,26938
PDB,5MOJ,BMRB Entry Tracking System,147190,26938
BMRB,26938,ASH1-mRNA,147204,26939
PDB,5MOH,BMRB Entry Tracking System,147204,26939
PDB,5MOI,BMRB Entry Tracking System,147204,26939
PDB,5MOJ,BMRB Entry Tracking System,147204,26939
BMRB,26944,mini monomeric TGF-b2-7m,147254,26943
BMRB,26943,engineered TGF-b2 monomer,147271,26944
PDB,5MEY,,147288,26945
PDB,5MEZ,,147288,26945
PDB,5MF0,,147288,26945
BMRB,25136,Chemical Shift Assignments for S100A4dC,147304,26946
BMRB,26956,C-terminal truncated S100A4 in complex with C-ERMAD fragment of ezrin,147304,26946
BMRB,26955,Fyn SH3 WT delta57,147405,26954
BMRB,26954,Fyn SH3 V39V/N53P/V55L delta56,147420,26955
BMRB,26946,"C-terminal truncated S100A4, apo form",147435,26956
PDB,5MHK,Crystal structure of ICP4 DNA-binding domain in complex with 19mer DNA duplex,147453,26957
BMRB,15177,Resonance assignments of CzrA in apo form,147482,26959
BMRB,27028,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for Zn(II) CzrA",147482,26959
BMRB,7376,Resonance assignments of CzrA in complex with Zinc ion,147482,26959
BMRB,7377,Resonance assignments of CzrA in complex with DNA,147482,26959
PDB,1R1U,crystal structure of CzrA in apo form,147482,26959
PDB,1R1V,crystal structure of CzrA in Zn(II) form,147482,26959
PDB,2KJB,Solution structure of CzrA in the DNA bound state,147482,26959
PDB,2KJC,Soluction structure of CzrA in the Zn(II) state,147482,26959
BMRB,26965,Assignments at at pH = 7.1 and T = 4 C,147591,26964
BMRB,26964,Assignments at pH = 1.66 in a 10% formic acid environment,147605,26965
BMRB,26968,Dictyostelium Skp1,147636,26967
BMRB,26967,Dictyostelium GlcNAc-Skp1,147653,26968
BMRB,26971,Lc-LTP2 in complex with DHPC,147687,26970
BMRB,34036,Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid LPPG,147687,26970
BMRB,26970,Lc-LTP2 in complex with DMPG,147701,26971
BMRB,34036,Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid LPPG,147701,26971
BMRB,18103,Backbone resonance assignments for G protein alpha i3 subunit in the GTP-bound state,147766,26975
BMRB,19015,Backbone resonance assignments for G protein alpha i3 subunit in the GDP-bound state,147766,26975
BMRB,26976,G alpha i3 bound to GoLoco14,147766,26975
PDB,2IHB,Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3,147766,26975
PDB,2V4Z,THE CRYSTAL STRUCTURE OF THE HUMAN G-PROTEIN SUBUNIT ALPHA (GNAI3) IN COMPLEX WITH AN ENGINEERED REGULATOR OF G-PROTEIN SIGNALING TYPE 2 DOMAIN (RGS2),147766,26975
PDB,4G5R,Structure of LGN GL4/Galphai3 complex,147766,26975
PDB,4G5S,Structure of LGN GL3/Galphai3 complex,147766,26975
BMRB,18103,Backbone resonance assignments for G protein alpha i3 subunit in the GTP-bound state,147783,26976
BMRB,19015,Backbone resonance assignments for G protein alpha i3 subunit in the GDP-bound state,147783,26976
BMRB,26975,G protein alpha i3 subunit in the GDP-bound state,147783,26976
PDB,1KJY,Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14,147783,26976
PDB,2IHB,Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3,147783,26976
PDB,2V4Z,THE CRYSTAL STRUCTURE OF THE HUMAN G-PROTEIN SUBUNIT ALPHA (GNAI3) IN COMPLEX WITH AN ENGINEERED REGULATOR OF G-PROTEIN SIGNALING TYPE 2 DOMAIN (RGS2),147783,26976
PDB,4G5R,Structure of LGN GL4/Galphai3 complex,147783,26976
PDB,4G5S,Structure of LGN GL3/Galphai3 complex,147783,26976
BMRB,26980,Wild type fused Npu DnaE from Nostoc punctiforme with Gly +2 Extein,147839,26979
BMRB,26981,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147839,26979
BMRB,26984,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147839,26979
BMRB,26979,Wild type fused Npu DnaE from Nostoc punctiforme with Phe +2 Extein,147856,26980
BMRB,26981,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147856,26980
BMRB,26984,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147856,26980
BMRB,26979,Wild type fused Npu DnaE from Nostoc punctiforme with Phe +2 Extein,147873,26981
BMRB,26980,Wild type fused Npu DnaE from Nostoc punctiforme with Gly +2 Extein,147873,26981
BMRB,26984,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147873,26981
BMRB,25727,HBP(D24R) : Histamine,147907,26983
BMRB,25728,HBPd24r (apo form),147907,26983
BMRB,26979,Wild type fused Npu DnaE from Nostoc punctiforme with Phe +2 Extein,147929,26984
BMRB,26980,Wild type fused Npu DnaE from Nostoc punctiforme with Gly +2 Extein,147929,26984
BMRB,26981,Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein,147929,26984
PDB,2I9H,,147961,26986
PDB,3F3Q,,147961,26986
BMRB,26993,Nav1.4 with N-terminal formyl group,148010,26992
BMRB,26992,Nav1.4,148030,26993
BMRB,27003,human 4E-BP1 (fragment 44 to 87) (apo form),148099,26997
PDB,5BXV,,148099,26997
BMRB,27047,Hamster PrP 90-231,148114,26998
BMRB,27000,Adenylate kinase R119A mutant Apo form,148131,26999
BMRB,27001,Adenylate kinase R119K mutant Apo form,148131,26999
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148131,26999
BMRB,27005,Adenylate kinase wild type bound to ATP,148131,26999
BMRB,27006,Adenylate kinase wild type bound to AMP,148131,26999
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148131,26999
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148131,26999
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148131,26999
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148131,26999
BMRB,26999,Adenylate kinase wild type Apo form,148161,27000
BMRB,27001,Adenylate kinase R119K mutant Apo form,148161,27000
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148161,27000
BMRB,27005,Adenylate kinase wild type bound to ATP,148161,27000
BMRB,27006,Adenylate kinase wild type bound to AMP,148161,27000
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148161,27000
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148161,27000
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148161,27000
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148161,27000
BMRB,26999,Adenylate kinase wild type Apo form,148177,27001
BMRB,27000,Adenylate kinase R119A mutant Apo form,148177,27001
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148177,27001
BMRB,27005,Adenylate kinase wild type bound to ATP,148177,27001
BMRB,27006,Adenylate kinase wild type bound to AMP,148177,27001
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148177,27001
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148177,27001
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148177,27001
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148177,27001
BMRB,26997,human 4E-BP1 (fragment 44 to 87) (bound to mouse eIF4E),148209,27003
BMRB,26999,Adenylate kinase wild type Apo form,148224,27004
BMRB,27000,Adenylate kinase R119A mutant Apo form,148224,27004
BMRB,27001,Adenylate kinase R119K mutant Apo form,148224,27004
BMRB,27005,Adenylate kinase wild type bound to ATP,148224,27004
BMRB,27006,Adenylate kinase wild type bound to AMP,148224,27004
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148224,27004
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148224,27004
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148224,27004
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148224,27004
BMRB,26999,Adenylate kinase wild type Apo form,148242,27005
BMRB,27000,Adenylate kinase R119A mutant Apo form,148242,27005
BMRB,27001,Adenylate kinase R119K mutant Apo form,148242,27005
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148242,27005
BMRB,27006,Adenylate kinase wild type bound to AMP,148242,27005
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148242,27005
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148242,27005
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148242,27005
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148242,27005
BMRB,26999,Adenylate kinase wild type Apo form,148260,27007
BMRB,27000,Adenylate kinase R119A mutant Apo form,148260,27007
BMRB,27001,Adenylate kinase R119K mutant Apo form,148260,27007
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148260,27007
BMRB,27005,Adenylate kinase wild type bound to ATP,148260,27007
BMRB,27006,Adenylate kinase wild type bound to AMP,148260,27007
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148260,27007
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148260,27007
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148260,27007
BMRB,26999,Adenylate kinase wild type Apo form,148278,27008
BMRB,27000,Adenylate kinase R119A mutant Apo form,148278,27008
BMRB,27001,Adenylate kinase R119K mutant Apo form,148278,27008
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148278,27008
BMRB,27005,Adenylate kinase wild type bound to ATP,148278,27008
BMRB,27006,Adenylate kinase wild type bound to AMP,148278,27008
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148278,27008
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148278,27008
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,148278,27008
BMRB,26999,Adenylate kinase wild type Apo form,148296,27010
BMRB,27000,Adenylate kinase R119A mutant Apo form,148296,27010
BMRB,27001,Adenylate kinase R119K mutant Apo form,148296,27010
BMRB,27004,Adenylate kinase wild type bound to Ap5A,148296,27010
BMRB,27005,Adenylate kinase wild type bound to ATP,148296,27010
BMRB,27006,Adenylate kinase wild type bound to AMP,148296,27010
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,148296,27010
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,148296,27010
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,148296,27010
BMRB,34089,Assignment of Sigma1.1 domain of sigmaA,148314,27011
PDB,5MWW,Structure of Sigma1.1 domain of sigmaA,148314,27011
BMRB,27013,reduced n-NmDsbD,148342,27012
BMRB,27014,oxidised c-NmDsbD,148342,27012
BMRB,27015,reduced c-NmDsbD,148342,27012
BMRB,27012,oxidised n-NmDsbD,148358,27013
BMRB,27014,oxidised c-NmDsbD,148358,27013
BMRB,27015,reduced c-NmDsbD,148358,27013
BMRB,27012,oxidised n-NmDsbD,148374,27014
BMRB,27013,reduced n-NmDsbD,148374,27014
BMRB,27015,reduced c-NmDsbD,148374,27014
BMRB,27012,oxidised n-NmDsbD,148390,27015
BMRB,27013,reduced n-NmDsbD,148390,27015
BMRB,27014,oxidised c-NmDsbD,148390,27015
NCBI,5532,Entrez gene entry for beta calcineurin,148421,27017
NCBI,AAB20487.1,GenBank entry for calmodulin,148421,27017
PDB,1CLM,Structure of Paramecium tetraurelia calmodulin at 1.8 Angstroms resolution,148421,27017
PDB,1EXR,The 1.0 Angstrom crystal structure of Ca+2 bound calmodulin,148421,27017
UniProt,P07463,UniProt entry for calmodulin,148421,27017
UniProt,P16298,UniProt entry for beta calcineurin,148421,27017
PDB,2WZB,"THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP, 3PG AND MAGNESIUM TRIFLUORIDE",148479,27022
BMRB,27024,Ascl1 fragment B,148502,27023
BMRB,27025,Ascl1 fragment C,148502,27023
BMRB,27026,Ascl1 fragment D,148502,27023
BMRB,27023,Ascl1 fragment A,148519,27024
BMRB,27025,Ascl1 fragment C,148519,27024
BMRB,27026,Ascl1 fragment D,148519,27024
BMRB,27023,Ascl1 fragment A,148536,27025
BMRB,27024,Ascl1 fragment B,148536,27025
BMRB,27026,Ascl1 fragment D,148536,27025
BMRB,27023,Ascl1 fragment A,148553,27026
BMRB,27024,Ascl1 fragment B,148553,27026
BMRB,27025,Ascl1 fragment C,148553,27026
BMRB,15177,Resonance assignments of CzrA in apo form,148584,27028
BMRB,26959,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for apo CzrA",148584,27028
BMRB,7376,Resonance assignments of CzrA in complex with Zinc ion,148584,27028
BMRB,7377,Resonance assignments of CzrA in complex with DNA,148584,27028
PDB,1R1U,crystal structure of CzrA in apo form,148584,27028
PDB,1R1V,crystal structure of CzrA in Zn(II) form,148584,27028
PDB,2KJB,Solution structure of CzrA in the DNA bound state,148584,27028
PDB,2KJC,Soluction structure of CzrA in the Zn(II) state,148584,27028
BMRB,27031,DANCER-1,148613,27030
BMRB,27032,DANCER-3,148613,27030
BMRB,27030,DANCER-0,148629,27031
BMRB,27032,DANCER-3,148629,27031
BMRB,27030,DANCER-0,148644,27032
BMRB,27031,DANCER-1,148644,27032
BMRB,27038,C-terminal dimerization domain (residues 511-624) of HtpG,148723,27037
BMRB,27037,N-terminal domain (residues 1-215) of HtpG,148745,27038
BMRB,16173,Solution NMR chemical shifts of cataract-causing P23T mutant of HgD crystallin in solution.,148766,27039
PDB,2KFB,Solution NMR structure of cataract-causing P23T mutant of HgD crystallin in solution.,148766,27039
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150333,27142
PDB,4JGF,Crystal structure of cataract-causing P23T mutant of HgD crystallin obtained by X-ray crystallography.,148766,27039
BMRB,25146,Solid-state NMR chemical shifts of amyloid-like fibrils formed by huntingtin N-terminal fragments (httNTQ30P10K2),148848,27045
BMRB,25645,Chemical Shift Assignments and Structure of HSPB1_ACD,148867,27046
PDB,2n3j,"Solution Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1",148867,27046
PDB,4mjh,Human Hsp27 core domain in complex with C-terminal peptide,148867,27046
BMRB,26998,Rabbit Prp 90-231,148881,27047
BMRB,27050,Trypanosoma brucei brucei Tryparedoxin oxidized,148916,27049
BMRB,27049,Trypanosoma brucei brucei Tryparedoxin reduced,148938,27050
BMRB,27071,BTHB domain from human FKBP25,149238,27070
SP,Q00688,Peptidyl-prolyl cis-trans isomerase FKBP3,149238,27070
BMRB,27070,human FKBP25,149254,27071
SP,Q00688,Peptidyl-prolyl cis-trans isomerase FKBP3,149254,27071
PDB,2XXD,,149286,27073
BMRB,27075,phosphorylated S129 alpha-synuclein,149315,27074
BMRB,27076,Y133F/Y136F mutant alpha-synuclein,149315,27074
BMRB,27077,phosphorylated Y125 Y133F/Y136F mutant alpha-synuclein,149315,27074
BMRB,27074,wild-type alpha-synuclein,149330,27075
BMRB,27076,Y133F/Y136F mutant alpha-synuclein,149330,27075
BMRB,27077,phosphorylated Y125 Y133F/Y136F mutant alpha-synuclein,149330,27075
BMRB,27074,wild-type alpha-synuclein,149346,27076
BMRB,27075,phosphorylated S129 alpha-synuclein,149346,27076
BMRB,27077,phosphorylated Y125 Y133F/Y136F mutant alpha-synuclein,149346,27076
BMRB,27074,wild-type alpha-synuclein,149361,27077
BMRB,27075,phosphorylated S129 alpha-synuclein,149361,27077
BMRB,27076,Y133F/Y136F mutant alpha-synuclein,149361,27077
PDB,4CP3,Crystal Strucutre,149405,27079
BMRB,27083,Tyrosine Kinase domain of human fibroblast receptor 3 in complex with inhibitor PD173074,149469,27082
BMRB,27082,Tyrosine Kinase domain of human fibroblast receptor 3 in apo state,149486,27083
PDB,5NPN,refined structure of native cytotoxin-1 from N. oxiana,149547,27086
PDB,5T8A,recombinant cytotoxin-1,149547,27086
BMRB,27089,ISCU (D39V),149581,27088
BMRB,27088,ISCU (M108I),149597,27089
NCBI,AAD45181.1,GenBank entry for calmodulin,149698,27094
NCBI,NP_001035232.1,NCBI reference sequence for NaV1.2,149698,27094
PDB,1CFC,Solution Structure of apo Calmodulin,149698,27094
PDB,2KXW,Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2,149698,27094
PDB,2L53,Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel NaV1.5,149698,27094
PDB,2M5E,Structure of the C-domain of Calcium-saturated Calmodulin bound to the IQ motif of NaV1.2,149698,27094
NCBI,AAD45181.1,GenBank entry for calmodulin,149716,27095
NCBI,NP_001035232.1,NCBI reference sequence for NaV1.2,149716,27095
PDB,1CFC,Solution Structure of apo Calmodulin,149716,27095
PDB,2KXW,Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2,149716,27095
PDB,2L53,Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel NaV1.5,149716,27095
PDB,2M5E,Structure of the C-domain of Calcium-saturated Calmodulin bound to the IQ motif of NaV1.2,149716,27095
PIR,P04117,Entry does not contain Methionine 1.,149736,27096
BMRB,27098,assignments of Mth10bTQQA,149752,27097
BMRB,27097,assignments of Mvo10b,149771,27098
BMRB,27113,apo-form dFABP,149927,27112
BMRB,27112,complex of dFABP with oleic acid,149943,27113
BMRB,27126,SH2B1/JAK2-pep complex,149957,27119
BMRB,15680,34kDa catalytic domain of human PTPN7,150000,27121
BMRB,27122,catalytic domain of HePTP (residues 44-339) in presence of vanadate (inhibitor) at pH 7.8,150000,27121
BMRB,15680,34kDa catalytic domain of human PTPN7,150015,27122
BMRB,27121,catalytic domain of HePTP (residues 44-339) at pH 7.8,150015,27122
BMRB,27124,hnRNPA2 D290V low complexity domain,150032,27123
BMRB,27123,hnRNPA2 WT low complexity domain,150047,27124
BMRB,27119,SH2B1 SH2 Domain,150077,27126
BMRB,27136,"T94T variant of human liver FABP, in complex with glycocholic acid",150123,27129
PDB,4KKP,Crystal structure of RbmA (crystal form 2),150140,27130
PDB,4KKQ,Crystal structure of RbmA (crystal form 1),150140,27130
PDB,4KKR,Crystal structure of RbmA (crystal form 3),150140,27130
PDB,1UGH,Entry contains crystal structure of human uracil-DNA glycosylase,150174,27133
PDB,4SKN,Entry contains crystal structure of human uracil-DNA glycosylase bound to DNA,150174,27133
PDB,4F91,"Structure of Brr2, contains the C-terminal Sec63 unit",150217,27135
BMRB,27129,"T94T variant of human liver FABP, apo form",150239,27136
BMRB,27138,HypF-N backbone assignment in non-toxic oligomer solution conditions,150255,27137
BMRB,27139,HypF-N native backbone assignment,150255,27137
BMRB,27137,HypF-N backbone assignment in toxic oligomer solution condition,150270,27138
BMRB,27139,HypF-N native backbone assignment,150270,27138
BMRB,27137,HypF-N backbone assignment in toxic oligomer solution condition,150285,27139
BMRB,27138,HypF-N backbone assignment in non-toxic oligomer solution conditions,150285,27139
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150300,27140
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150300,27140
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150300,27140
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150300,27140
BMRB,27155,CUGBP2 RRM3 Y428A,150300,27140
BMRB,27156,CUGBP2 RRM3 H429A,150300,27140
BMRB,27157,CUGBP2 RRM3 F455A,150300,27140
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150333,27142
BMRB,18324,,152181,27262
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150333,27142
BMRB,27155,CUGBP2 RRM3 Y428A,150333,27142
BMRB,27156,CUGBP2 RRM3 H429A,150333,27142
BMRB,27157,CUGBP2 RRM3 F455A,150333,27142
BMRB,27148,wild-type PACT-D3,150350,27143
PDB,1E0B,S. pombe Swi6 chromoshadow domain,150407,27145
PDB,1S4Z,HP1 chromoshadow with CAF-1 peptide,150407,27145
PDB,3I3C,CBX5 chromoshadow,150407,27145
PDB,3KUP,CBX3 chromoshadow,150407,27145
PDB,3P7J,Drosophila HP1a chromoshadow,150407,27145
PDB,3Q6S,HP1 beta with Shugoshin Peptide,150407,27145
PDB,5T1G,CBX1 with histone peptide,150407,27145
PDB,5T1I,CBX3 chromoshadow with histone H3 peptide,150407,27145
BMRB,27143,PACT-D3 L273R mutant,150465,27148
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150504,27152
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150504,27152
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150504,27152
BMRB,27155,CUGBP2 RRM3 Y428A,150504,27152
BMRB,27156,CUGBP2 RRM3 H429A,150504,27152
BMRB,27157,CUGBP2 RRM3 F455A,150504,27152
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150521,27153
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150521,27153
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150521,27153
BMRB,27155,CUGBP2 RRM3 Y428A,150521,27153
BMRB,27156,CUGBP2 RRM3 H429A,150521,27153
BMRB,27157,CUGBP2 RRM3 F455A,150521,27153
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150538,27154
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150538,27154
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150538,27154
BMRB,27155,CUGBP2 RRM3 Y428A,150538,27154
BMRB,27156,CUGBP2 RRM3 H429A,150538,27154
BMRB,27157,CUGBP2 RRM3 F455A,150538,27154
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150555,27155
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150555,27155
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150555,27155
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150555,27155
BMRB,27156,CUGBP2 RRM3 H429A,150555,27155
BMRB,27157,CUGBP2 RRM3 F455A,150555,27155
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150571,27156
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150571,27156
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150571,27156
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150571,27156
BMRB,27155,CUGBP2 RRM3 Y428A,150571,27156
BMRB,27157,CUGBP2 RRM3 F455A,150571,27156
BMRB,27142,CUGBP2 RRM3 Y428A in complex with UUUAA RNA,150587,27157
BMRB,27152,CUGBP2 RRM3 H429A in complex with UUUAA RNA,150587,27157
BMRB,27153,CUGBP2 RRM3 F455A in complex with UUUAA RNA,150587,27157
BMRB,27154,CUGBP2 RRM3 wild type in complex with UGUGU RNA,150587,27157
BMRB,27155,CUGBP2 RRM3 Y428A,150587,27157
BMRB,27156,CUGBP2 RRM3 H429A,150587,27157
PDB,3GPG,Crystal structure of macro domain of Chikungunya virus,150603,27158
PDB,3GPO,Crystal structure of macro domain of Chikungunya virus in complex with ADP-ribose,150603,27158
PDB,3Q8K,"Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap DNA, SM3+, and K+",150636,27160
BMRB,27168,"1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)",150717,27167
BMRB,27167,"1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human protein kinase ataxia-telangiectasia mutated (ATM) fused to the B1 domain of streptococcal protein G (GB1)",150740,27168
BMRB,27176,truncated forms of the coronavirus nsp1 protein; nsp1(13-25),150759,27169
BMRB,27177,truncated forms of the coronavirus nsp1 protein; nsp1(13-50),150759,27169
BMRB,4342,"Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Involved in Friedreich Ataxia.",150787,27171
BMRB,27175,"1H, 15N, 13C backbone resonance assignments of the D10N variant of beta-phosphoglucomutase in a MgII-free complex with beta-glucose 1,6-bisphosphate",150845,27174
BMRB,27174,"1H, 15N, 13C backbone resonance assignments of the D10N variant of beta-phosphoglucomutase in a MgII-bound complex with beta-glucose 1,6-bisphosphate",150864,27175
BMRB,27169,solubility domain GB1,150881,27176
BMRB,27177,truncated forms of the coronavirus nsp1 protein; nsp1(13-50),150881,27176
BMRB,27169,solubility domain GB1,150895,27177
BMRB,27176,truncated forms of the coronavirus nsp1 protein; nsp1(13-25),150895,27177
BMRB,18392,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal Domain of E. coli Enzyme I",150963,27183
BMRB,27191,ProXp-ala bound to microhelixPro,150992,27185
PDB,1CFC,Apo calmodulin,151079,27190
PDB,2KXW,Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2,151079,27190
PDB,2L53,Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel NaV1.5,151079,27190
PDB,2M5E,Structure of the C-domain of Calcium-saturated Calmodulin bound to the IQ motif of NaV1.2,151079,27190
BMRB,27185,ProXp-ala free form,151097,27191
BMRB,16401,Separation of Inhibitor and Substrate Binding Locations in the Globin Dehaloperoxidase,151146,27194
PDB,2QFK,,151146,27194
BMRB,27198,Chemical Shift Assignments for Dm. Par3 PDZ3 domain,151193,27197
BMRB,27203,Chemical Shift Assignments for Dm. Par3 PDZ2 domain,151193,27197
BMRB,27204,Chemical Shift Assignments for Hs. Par3 PDZ2 domain,151193,27197
BMRB,27205,Chemical Shift Assignments for Hs. Par3 PDZ3 domain,151193,27197
BMRB,27197,Chemical Shift Assignments for Dm. Par3 PDZ1 domain,151208,27198
PDB,3LLH,,152181,27262
BMRB,27203,Chemical Shift Assignments for Dm. Par3 PDZ2 domain,151208,27198
BMRB,27204,Chemical Shift Assignments for Hs. Par3 PDZ2 domain,151208,27198
BMRB,27205,Chemical Shift Assignments for Hs. Par3 PDZ3 domain,151208,27198
BMRB,27197,Chemical Shift Assignments for Dm. Par3 PDZ1 domain,151272,27203
BMRB,27198,Chemical Shift Assignments for Dm. Par3 PDZ3 domain,151272,27203
BMRB,27204,Chemical Shift Assignments for Hs. Par3 PDZ2 domain,151272,27203
BMRB,27205,Chemical Shift Assignments for Hs. Par3 PDZ3 domain,151272,27203
BMRB,27197,Chemical Shift Assignments for Dm. Par3 PDZ1 domain,151286,27204
BMRB,27198,Chemical Shift Assignments for Dm. Par3 PDZ3 domain,151286,27204
BMRB,27203,Chemical Shift Assignments for Dm. Par3 PDZ2 domain,151286,27204
BMRB,27205,Chemical Shift Assignments for Hs. Par3 PDZ3 domain,151286,27204
BMRB,27197,Chemical Shift Assignments for Dm. Par3 PDZ1 domain,151300,27205
BMRB,27198,Chemical Shift Assignments for Dm. Par3 PDZ3 domain,151300,27205
BMRB,27203,Chemical Shift Assignments for Dm. Par3 PDZ2 domain,151300,27205
BMRB,27204,Chemical Shift Assignments for Hs. Par3 PDZ2 domain,151300,27205
PDB,3L2P,,151364,27209
EMDB,EMD-3851,Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM,151414,27212
PDB,5OQV,Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM,151414,27212
BMRB,27214,RSK1 phosphorylated C-terminal peptide (696-735),151430,27213
BMRB,27213,RSK1 C-terminal peptide (696-735),151444,27214
BMRB,27216,prothymosin alpha,151459,27215
BMRB,27215,prothymosin alpha,151476,27216
BMRB,27218,S99T/C115S/I97V Mutant of Human Cyclophilin A,151494,27217
BMRB,27217,S99T/C115S Mutant of Human Cyclophilin A,151512,27218
BMRB,27220,membrane embedded NaK channel (ion-favored conformer),151530,27219
BMRB,27219,membrane embedded NaK channel (ion-free conformer),151545,27220
PDB,3P62,WILD-TYPE PENTAERYTHRITOL TETRANITRATE REDUCTASE CONTAINING A C-TERMINAL 8-HISTIDINE TAG FROM ENTEROBACTER CLOACAE,151577,27224
PDB,5LGX,STRUCTURE OF OXIDISED PENTAERYTHRITOL TETRANITRATE REDUCTASE FROM ENTEROBACTER CLOACAE,151577,27224
BMRB,27226,hsa-miR-34a-mSIRT1 bulge,151594,27225
BMRB,27229,hsa-miR-34a-mSIRT1 bulge U5C9mut,151594,27225
BMRB,27225,mature hsa-miR-34a-5p (22-mer),151609,27226
BMRB,27229,hsa-miR-34a-mSIRT1 bulge U5C9mut,151609,27226
BMRB,27225,mature hsa-miR-34a-5p (22-mer),151654,27229
BMRB,27226,hsa-miR-34a-mSIRT1 bulge,151654,27229
BMRB,11550,Chemical shifts of SAIL signals of subunit c-ring of thermophilic FoF1 ATP synthase,151699,27232
SP,Q14008,CKAP5_HUMAN,151731,27235
BMRB,27238,Chemical Shift Assignments for S-nitrosylated mouse galectin-2,151765,27237
BMRB,27237,Chemical Shift Assignments for mouse galectin-2,151780,27238
BMRB,27298,C8 bound E.coli GcvH backbone chemical shift assignments,151838,27241
BMRB,27239,Trigger factor: RBD; SBD; PPD; RBD-SBD; SBD-PPD,151852,27242
BMRB,16635,chemical shifts for N-terminal of delta subunit of RNA polymerase from Bacillus subtilis,151901,27245
BMRB,16912,chemical shifts for delta subunit of RNA polymerase from Bacillus subtilis,151901,27245
BMRB,18903,15N NMR relaxation data for delta subunit of RNA polymerase from Bacillus subtilis,151901,27245
BMRB,19284,15N NMR relaxation data for delta subunit of RNA polymerase from Bacillus subtilis,151901,27245
EMBL,CAA89869,,151901,27245
EMBL,CAB15744,,151901,27245
EMBL,CCU60814,,151901,27245
EMBL,CEI59524,,151901,27245
EMBL,CEJ79381,,151901,27245
GB,AAA22710,,151901,27245
GB,ADM39706,,151901,27245
GB,ADV94526,,151901,27245
GB,AEP92774,,151901,27245
GB,AFI30331,,151901,27245
PDB,2KRC,Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase,151901,27245
PDB,4NC7,N-terminal domain of delta-subunit of RNA polymerase complexed with I3C and nickel ion,151901,27245
PDB,4NC8,N-terminal domain of delta-subunit of RNA polymerase complexed with nickel ions,151901,27245
REF,NP_391597,,151901,27245
REF,WP_003221959,,151901,27245
REF,WP_003227609,,151901,27245
REF,WP_003235832,,151901,27245
REF,WP_003243661,,151901,27245
SP,P12464,,151901,27245
BMRB,27247,Backbone assignments of domain swapped dimer of engineered hairpin loop3  mutant of single chain Monellin,151920,27246
BMRB,27246,Backbone assignments of domain swapped dimer of engineered hairpin loop3 mutant of single chain Monellin,151936,27247
BMRB,27249,"methyl chemical shift assignments for H2-Dd, a murine class I major histocompatibility molecule heavy chain",151952,27248
BMRB,27248,"methyl chemical shift assignments for Beta2-microglobulin, a human class I major histocompatibility molecule light chain",151971,27249
BMRB,27251,CW42 bound to H3K4me1,151991,27250
BMRB,27250,CW domain of ASHH2 methyltransferase,152007,27251
BMRB,27256,Galactin-7 in apo form,152058,27255
BMRB,27257,Galactin-8 NTD in apo form,152058,27255
BMRB,27258,Galactin-8 CTD in apo form,152058,27255
BMRB,27255,Galactin-1 in apo form,152076,27256
BMRB,27257,Galactin-8 NTD in apo form,152076,27256
BMRB,27258,Galactin-8 CTD in apo form,152076,27256
BMRB,27255,Galactin-1 in apo form,152094,27257
BMRB,27256,Galactin-7 in apo form,152094,27257
BMRB,27258,Galactin-8 CTD in apo form,152094,27257
BMRB,27255,Galactin-1 in apo form,152112,27258
BMRB,27256,Galactin-7 in apo form,152112,27258
BMRB,27257,Galactin-8 NTD in apo form,152112,27258
BMRB,27264,"1H, 15N, 13C resonance assignments for Human prion protein (91-231): wild type (scilicet HuPrPM129)",152130,27259
SP,P29274,,152162,27261
BMRB,27259,"1H, 15N, 13C resonance assignments for Human prion protein (91-231): mutant V127M129 (scilicet HuPrPG127V)",152212,27264
PDB,1TNF,Entry contains the X-ray structure of Tumor Necrosis Factor alpha at 2.6 Angstrom Resolution.,152241,27266
GB,AB047639,"GENBANK Hepatitis C virus (isolate JFH-1) genomic RNA, complete genome.",152309,27270
SP,Q99IB,SWISS-PROT POLG_HCVJF,152309,27270
BMRB,18094,AF4-AF9 complex,152325,27271
BMRB,19516,Dot1L in complex with AF9 (Dot1L-AF9),152325,27271
BMRB,25677,CBX8 in complex with AF9 (CBX8-AF9),152325,27271
BMRB,27275,SGTA TPR_C-terminal(deltaQ) domains,152349,27272
BMRB,27276,SGTA N-terminal domain including linker residues,152349,27272
BMRB,17471,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for non-phosphorylated p38 alpha MAPK",152365,27273
BMRB,19934,Dual-phospholyrated apo Human p38 alpha ILVM methyl resonance assignments,152365,27273
BMRB,27274,phosphorylated (T183 and Y185) p38 alpha in complex with an MKK3bKIM peptide,152365,27273
BMRB,17471,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for non-phosphorylated p38 alpha MAPK",152382,27274
BMRB,19934,Dual-phospholyrated apo Human p38 alpha ILVM methyl resonance assignments,152382,27274
BMRB,27273,phosphorylated (T183 and Y185) p38 alpha,152382,27274
BMRB,27272,SGTA C-terminal domain,152400,27275
BMRB,27276,SGTA N-terminal domain including linker residues,152400,27275
BMRB,27272,SGTA C-terminal domain,152416,27276
BMRB,27275,SGTA TPR_C-terminal(deltaQ) domains,152416,27276
BMRB,26600,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit",152453,27278
BMRB,27279,T cell receptor N30 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152453,27278
BMRB,27280,T cell receptor N15 beta subunit C domain mutant m22 (Y50A/E51A/F128R/V144Q/L146Q),152453,27278
BMRB,27281,T cell receptor N15 beta subunit C domain mutant m23 (Q48A/Y50A/E51A/F128R/V144Q/L146Q),152453,27278
BMRB,26601,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N30 beta subunit",152470,27279
BMRB,27278,T cell receptor N15 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152470,27279
BMRB,27280,T cell receptor N15 beta subunit C domain mutant m22 (Y50A/E51A/F128R/V144Q/L146Q),152470,27279
BMRB,27281,T cell receptor N15 beta subunit C domain mutant m23 (Q48A/Y50A/E51A/F128R/V144Q/L146Q),152470,27279
BMRB,26600,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit",152488,27280
BMRB,27278,T cell receptor N15 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152488,27280
BMRB,27279,T cell receptor N30 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152488,27280
BMRB,27281,T cell receptor N15 beta subunit C domain mutant m23 (Q48A/Y50A/E51A/F128R/V144Q/L146Q),152488,27280
BMRB,26600,"Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit",152506,27281
BMRB,27278,T cell receptor N15 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152506,27281
BMRB,27279,T cell receptor N30 beta subunit C domain mutant c1 (F128R/V144Q/L146Q),152506,27281
BMRB,27280,T cell receptor N15 beta subunit C domain mutant m22 (Y50A/E51A/F128R/V144Q/L146Q),152506,27281
BMRB,26927,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine,152524,27282
BMRB,26928,unlinked NS2B-NS3 Protease of Zika Virus,152524,27282
BMRB,26933,unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine aldehyde,152524,27282
BMRB,27286,VSV8 peptide bound to a truncated MHC H-2Kb (VSV8/Kb-t),152560,27285
PDB,1KPU,X-ray crystal structure of VSV8/Kb/b2m heterotrimeric complex.,152560,27285
BMRB,27285,VSV8 peptide bound to MHC H-2Kb (VSV8/Kb),152582,27286
EMDB,EMD-7079,,152633,27289
EMDB,EMD-7080,,152633,27289
BMRB,27293,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Isoprenaline-bound form",152669,27292
BMRB,27294,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Apo form",152669,27292
BMRB,27295,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Isoprenaline-bound form",152669,27292
BMRB,27296,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9, without orthosteric ligand",152669,27292
BMRB,27297,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9 and full agonist isoprenaline",152669,27292
BMRB,27292,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Apo form",152684,27293
BMRB,27294,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Apo form",152684,27293
BMRB,27295,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Isoprenaline-bound form",152684,27293
BMRB,27296,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9, without orthosteric ligand",152684,27293
BMRB,27297,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9 and full agonist isoprenaline",152684,27293
BMRB,27292,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Apo form",152701,27294
BMRB,27293,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Isoprenaline-bound form",152701,27294
BMRB,27295,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Isoprenaline-bound form",152701,27294
BMRB,27296,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9, without orthosteric ligand",152701,27294
BMRB,27297,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9 and full agonist isoprenaline",152701,27294
BMRB,27292,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Apo form",152716,27295
BMRB,27293,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Isoprenaline-bound form",152716,27295
BMRB,27294,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Apo form",152716,27295
BMRB,27296,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9, without orthosteric ligand",152716,27295
BMRB,27297,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9 and full agonist isoprenaline",152716,27295
BMRB,27292,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Apo form",152733,27296
BMRB,27293,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Isoprenaline-bound form",152733,27296
BMRB,27294,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Apo form",152733,27296
BMRB,27295,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Isoprenaline-bound form",152733,27296
BMRB,27297,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9 and full agonist isoprenaline",152733,27296
BMRB,27292,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Apo form",152749,27297
BMRB,27293,"Turkey beta-1 adrenergic receptor, Delta5 mutant, Isoprenaline-bound form",152749,27297
BMRB,27294,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Apo form",152749,27297
BMRB,27295,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, Isoprenaline-bound form",152749,27297
BMRB,27296,"Turkey beta-1 adrenergic receptor, Delta5-L190M mutant, bound to nanobody Nb6B9, without orthosteric ligand",152749,27297
BMRB,27241,E.coli GcvH backbone chemical shift assignments,152767,27298
BMRB,34151,BMRB entry of of RCD1 499-572 in complex with DREB2A,152828,27302
PDB,5OAO,Structure of RCD1 499-572 in complex with DREB2A,152828,27302
BMRB,34152,Chemical shift assignments of DREB2A in complex with RCD1,152845,27303
PDB,5OAP,NMR structure of DREB2A in complex with RCD1,152845,27303
BMRB,34085,Apo BAMB5917 assignments list,152864,27304
PDB,5MTI,Apo BAMB5917 PDB,152864,27304
GB,AAQ67167.1,hypothetical protein PG_2227,152947,27313
NCBI,PG_RS09910,Hypothetical protein,152947,27313
PDB,1ECE,"E1 catalytic domain, wild type (not containing Y245G mutation)",152971,27314
BMRB,15201,Sequence-specific resonance assignments for OmpX in 8 M urea aqueous solution,152987,27315
BMRB,18796,OmpX in phopspholipid nanodiscs,152987,27315
BMRB,15969,Solution NMR assignment on HBV core protein dimer,153017,27317
BMRB,27336,N-terminal domain of FOXO1,153031,27320
BMRB,27337,N-terminal FOXO1 pThr24,153031,27320
BMRB,25740,C-terminal domain of Cdc37 cochaperone,153069,27322
BMRB,27323,C-terminal domain of Cdc37 (Y298F mutant),153069,27322
BMRB,27324,C-terminal domain of Cdc37 (unfolded),153069,27322
BMRB,25740,C-terminal domain of Cdc37 cochaperone,153085,27323
BMRB,27322,C-terminal domain of Cdc37 (Y298E mutant),153085,27323
BMRB,27324,C-terminal domain of Cdc37 (unfolded),153085,27323
BMRB,25740,C-terminal domain of Cdc37 cochaperone,153100,27324
BMRB,27322,C-terminal domain of Cdc37 (Y298E mutant),153100,27324
BMRB,27323,C-terminal domain of Cdc37 (Y298F mutant),153100,27324
BMRB,27326,Yes1-SH2 (Yes1 SH2 domain in complex with Cdc37-derived phosphopeptide),153115,27325
BMRB,27327,Yes1-SH3 (Yes1 kinase SH3 domain),153115,27325
BMRB,27325,Yes1-SH2 (SH2 domain of Yes1 kinase),153130,27326
BMRB,27327,Yes1-SH3 (Yes1 kinase SH3 domain),153130,27326
BMRB,27325,Yes1-SH2 (SH2 domain of Yes1 kinase),153144,27327
BMRB,27326,Yes1 SH2 9domain in complex with Cdc37-derived phosphopeptide),153144,27327
BMRB,27334,Ataxin7N10QT3N9 (Residues:1-62),153190,27333
BMRB,27335,Ataxin7N22QT3N9 (Residues:1-62),153190,27333
BMRB,27333,Ataxin7N10Q (Residues:1-62),153204,27334
BMRB,27335,Ataxin7N22QT3N9 (Residues:1-62),153204,27334
BMRB,27320,transcription factor FOXO1,153218,27336
BMRB,27337,N-terminal FOXO1 pThr24,153218,27336
BMRB,27320,transcription factor FOXO1,153232,27337
BMRB,27336,N-terminal domain of FOXO1,153232,27337
BMRB,16696,Assignment of shorter peptide construct from the same protein,153276,27341
BMRB,27344,GA Seq5 monomer,153310,27343
BMRB,27345,SH3 Seq3 monomer,153310,27343
BMRB,27343,GB1 Seq2 monomer,153327,27344
BMRB,27345,SH3 Seq3 monomer,153327,27344
BMRB,27343,GB1 Seq2 monomer,153344,27345
BMRB,27344,GA Seq5 monomer,153344,27345
BMRB,6968,intrinsically disordered alpha-synuclein,153377,27348
PDB,6FGM,AC12 peptide from Hypsiboas raniceps,153541,27357
BMRB,27362,Abl1 SH3 pY89pY134 monomer,153573,27359
BMRB,27361,STIM1 CC1 R304W monomer,153591,27360
BMRB,27360,STIM1 CC1 monomer,153606,27361
BMRB,27359,Abl1 SH3 monomer,153621,27362
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153658,27364
BMRB,27366,KaisoE535Q-MeCG2 complex,153658,27364
BMRB,27367,KaisoE535A-MeCG2 complex,153658,27364
BMRB,27368,Kaiso-MeKBS complex,153658,27364
BMRB,27369,KaisoE535Q-MeKBS complex,153658,27364
BMRB,27370,KaisoE535A-MeKBS complex,153658,27364
BMRB,27371,Kaiso-MeKBSsemi complex,153658,27364
BMRB,27372,Kaiso-MeKBShemi complex,153658,27364
PDB,2LT7,,153658,27364
PDB,4F6M,,153658,27364
PDB,4F6N,,153658,27364
PDB,5VMU,,153658,27364
PDB,5VMV,,153658,27364
PDB,5VMW,,153658,27364
PDB,5VMX,,153658,27364
PDB,5VMY,,153658,27364
PDB,5VMZ,,153658,27364
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153693,27366
BMRB,27364,Kaiso-MeCG2 complex,153693,27366
BMRB,27367,KaisoE535A-MeCG2 complex,153693,27366
BMRB,27368,Kaiso-MeKBS complex,153693,27366
BMRB,27369,KaisoE535Q-MeKBS complex,153693,27366
BMRB,27370,KaisoE535A-MeKBS complex,153693,27366
BMRB,27371,Kaiso-MeKBSsemi complex,153693,27366
BMRB,27372,Kaiso-MeKBShemi complex,153693,27366
PDB,2LT7,,153693,27366
PDB,4F6M,,153693,27366
PDB,4F6N,,153693,27366
PDB,5VMU,,153693,27366
PDB,5VMV,,153693,27366
PDB,5VMW,,153693,27366
PDB,5VMX,,153693,27366
PDB,5VMY,,153693,27366
PDB,5VMZ,,153693,27366
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153713,27367
BMRB,27364,Kaiso-MeCG2 complex,153713,27367
BMRB,27366,KaisoE535Q-MeCG2 complex,153713,27367
BMRB,27368,Kaiso-MeKBS complex,153713,27367
BMRB,27369,KaisoE535Q-MeKBS complex,153713,27367
BMRB,27370,KaisoE535A-MeKBS complex,153713,27367
BMRB,27371,Kaiso-MeKBSsemi complex,153713,27367
BMRB,27372,Kaiso-MeKBShemi complex,153713,27367
PDB,2LT7,,153713,27367
PDB,4F6M,,153713,27367
PDB,4F6N,,153713,27367
PDB,5VMU,,153713,27367
PDB,5VMV,,153713,27367
PDB,5VMW,,153713,27367
PDB,5VMX,,153713,27367
PDB,5VMY,,153713,27367
PDB,5VMZ,,153713,27367
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153733,27368
BMRB,27364,Kaiso-MeCG2 complex,153733,27368
BMRB,27366,KaisoE535Q-MeCG2 complex,153733,27368
BMRB,27367,KaisoE535A-MeCG2 complex,153733,27368
BMRB,27369,KaisoE535Q-MeKBS complex,153733,27368
BMRB,27370,KaisoE535A-MeKBS complex,153733,27368
BMRB,27371,Kaiso-MeKBSsemi complex,153733,27368
BMRB,27372,Kaiso-MeKBShemi complex,153733,27368
PDB,2LT7,,153733,27368
PDB,4F6M,,153733,27368
PDB,4F6N,,153733,27368
PDB,5VMU,,153733,27368
PDB,5VMV,,153733,27368
PDB,5VMW,,153733,27368
PDB,5VMX,,153733,27368
PDB,5VMY,,153733,27368
PDB,5VMZ,,153733,27368
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153753,27369
BMRB,27364,Kaiso-MeCG2 complex,153753,27369
BMRB,27366,KaisoE535Q-MeCG2 complex,153753,27369
BMRB,27367,KaisoE535A-MeCG2 complex,153753,27369
BMRB,27368,Kaiso-MeKBS complex,153753,27369
BMRB,27370,KaisoE535A-MeKBS complex,153753,27369
BMRB,27371,Kaiso-MeKBSsemi complex,153753,27369
BMRB,27372,Kaiso-MeKBShemi complex,153753,27369
PDB,2LT7,,153753,27369
PDB,4F6M,,153753,27369
PDB,4F6N,,153753,27369
PDB,5VMU,,153753,27369
PDB,5VMV,,153753,27369
PDB,5VMW,,153753,27369
PDB,5VMX,,153753,27369
PDB,5VMY,,153753,27369
PDB,5VMZ,,153753,27369
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153774,27370
BMRB,27364,Kaiso-MeCG2 complex,153774,27370
BMRB,27366,KaisoE535Q-MeCG2 complex,153774,27370
BMRB,27367,KaisoE535A-MeCG2 complex,153774,27370
BMRB,27368,Kaiso-MeKBS complex,153774,27370
BMRB,27369,KaisoE535Q-MeKBS complex,153774,27370
BMRB,27371,Kaiso-MeKBSsemi complex,153774,27370
BMRB,27372,Kaiso-MeKBShemi complex,153774,27370
PDB,2LT7,,153774,27370
PDB,4F6M,,153774,27370
PDB,4F6N,,153774,27370
PDB,5VMU,,153774,27370
PDB,5VMV,,153774,27370
PDB,5VMW,,153774,27370
PDB,5VMX,,153774,27370
PDB,5VMY,,153774,27370
PDB,5VMZ,,153774,27370
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153795,27371
BMRB,27364,Kaiso-MeCG2 complex,153795,27371
BMRB,27366,KaisoE535Q-MeCG2 complex,153795,27371
BMRB,27367,KaisoE535A-MeCG2 complex,153795,27371
BMRB,27368,Kaiso-MeKBS complex,153795,27371
BMRB,27369,KaisoE535Q-MeKBS complex,153795,27371
BMRB,27370,KaisoE535A-MeKBS complex,153795,27371
BMRB,27372,Kaiso-MeKBShemi complex,153795,27371
PDB,2LT7,,153795,27371
PDB,4F6M,,153795,27371
PDB,4F6N,,153795,27371
PDB,5VMU,,153795,27371
PDB,5VMV,,153795,27371
PDB,5VMW,,153795,27371
PDB,5VMX,,153795,27371
PDB,5VMY,,153795,27371
PDB,5VMZ,,153795,27371
BMRB,18462,Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA,153816,27372
BMRB,27364,Kaiso-MeCG2 complex,153816,27372
BMRB,27366,KaisoE535Q-MeCG2 complex,153816,27372
BMRB,27367,KaisoE535A-MeCG2 complex,153816,27372
BMRB,27368,Kaiso-MeKBS complex,153816,27372
BMRB,27369,KaisoE535Q-MeKBS complex,153816,27372
BMRB,27370,KaisoE535A-MeKBS complex,153816,27372
BMRB,27371,Kaiso-MeKBSsemi complex,153816,27372
PDB,2LT7,,153816,27372
PDB,4F6M,,153816,27372
PDB,4F6N,,153816,27372
PDB,5VMU,,153816,27372
PDB,5VMV,,153816,27372
PDB,5VMW,,153816,27372
PDB,5VMX,,153816,27372
PDB,5VMY,,153816,27372
PDB,5VMZ,,153816,27372
BMRB,27375,prelamin A C-terminal region,153861,27374
BMRB,27376,Progerin C-terminal region,153861,27374
BMRB,27374,Progerin C-ter,153875,27375
BMRB,27376,prelamin A C-terminal region,153875,27375
BMRB,27374,Progerin C-ter,153889,27376
BMRB,27375,Progerin C-terminal region,153889,27376
BMRB,27378,HIV-1 Protease Homodimer (WT bound to Darunavir),153903,27377
BMRB,27377,HIV-1 Protease Homodimer [(Flap + mutant) bound to Darunavir],153922,27378
BMRB,27382,conotoxin_muPIIIA-4,153941,27379
BMRB,27383,conotoxin_muPIIIA-5,153941,27379
BMRB,27384,conotoxin_muPIIIA-6,153941,27379
BMRB,27385,conotoxin_muPIIIA-9,153941,27379
BMRB,27386,conotoxin_muPIIIA-11,153941,27379
BMRB,27389,conotoxin_muPIIIA-10,153941,27379
BMRB,27390,conotoxin_muPIIIA-15,153941,27379
BMRB,27391,conotoxin_muPIIIA-14,153941,27379
BMRB,27379,conotoxin_muPIIIA-3,153994,27382
BMRB,27383,conotoxin_muPIIIA-5,153994,27382
BMRB,27384,conotoxin_muPIIIA-6,153994,27382
BMRB,27385,conotoxin_muPIIIA-9,153994,27382
BMRB,27386,conotoxin_muPIIIA-11,153994,27382
BMRB,27388,conotoxin_muPIIIA-8,153994,27382
BMRB,27389,conotoxin_muPIIIA-10,153994,27382
BMRB,27390,conotoxin_muPIIIA-15,153994,27382
BMRB,27391,conotoxin_muPIIIA-14,153994,27382
BMRB,27379,conotoxin_muPIIIA-3,154013,27383
BMRB,27382,conotoxin_muPIIIA-4,154013,27383
BMRB,27384,conotoxin_muPIIIA-6,154013,27383
BMRB,27385,conotoxin_muPIIIA-9,154013,27383
BMRB,27386,conotoxin_muPIIIA-11,154013,27383
BMRB,27388,conotoxin_muPIIIA-8,154013,27383
BMRB,27389,conotoxin_muPIIIA-10,154013,27383
BMRB,27390,conotoxin_muPIIIA-15,154013,27383
BMRB,27391,conotoxin_muPIIIA-14,154013,27383
BMRB,27379,conotoxin_muPIIIA-3,154033,27384
BMRB,27382,conotoxin_muPIIIA-4,154033,27384
BMRB,27383,conotoxin_muPIIIA-5,154033,27384
BMRB,27385,conotoxin_muPIIIA-9,154033,27384
BMRB,27386,conotoxin_muPIIIA-11,154033,27384
BMRB,27388,conotoxin_muPIIIA-8,154033,27384
BMRB,27389,conotoxin_muPIIIA-10,154033,27384
BMRB,27390,conotoxin_muPIIIA-15,154033,27384
BMRB,27391,conotoxin_muPIIIA-14,154033,27384
BMRB,27379,conotoxin_muPIIIA-3,154052,27385
BMRB,27382,conotoxin_muPIIIA-4,154052,27385
BMRB,27383,conotoxin_muPIIIA-5,154052,27385
BMRB,27384,conotoxin_muPIIIA-6,154052,27385
BMRB,27386,conotoxin_muPIIIA-11,154052,27385
BMRB,27388,conotoxin_muPIIIA-8,154052,27385
BMRB,27389,conotoxin_muPIIIA-10,154052,27385
BMRB,27390,conotoxin_muPIIIA-15,154052,27385
BMRB,27391,conotoxin_muPIIIA-14,154052,27385
BMRB,27379,conotoxin_muPIIIA-3,154071,27386
BMRB,27382,conotoxin_muPIIIA-4,154071,27386
BMRB,27383,conotoxin_muPIIIA-5,154071,27386
BMRB,27384,conotoxin_muPIIIA-6,154071,27386
BMRB,27385,conotoxin_muPIIIA-9,154071,27386
BMRB,27388,conotoxin_muPIIIA-8,154071,27386
BMRB,27389,conotoxin_muPIIIA-10,154071,27386
BMRB,27390,conotoxin_muPIIIA-15,154071,27386
BMRB,27391,conotoxin_muPIIIA-14,154071,27386
BMRB,27379,conotoxin_muPIIIA-3,154106,27388
BMRB,27382,conotoxin_muPIIIA-4,154106,27388
BMRB,27383,conotoxin_muPIIIA-5,154106,27388
BMRB,27384,conotoxin_muPIIIA-6,154106,27388
BMRB,27385,conotoxin_muPIIIA-9,154106,27388
BMRB,27386,conotoxin_muPIIIA-11,154106,27388
BMRB,27389,conotoxin_muPIIIA-10,154106,27388
BMRB,27390,conotoxin_muPIIIA-15,154106,27388
BMRB,27391,conotoxin_muPIIIA-14,154106,27388
BMRB,27379,conotoxin_muPIIIA-3,154125,27389
BMRB,27382,conotoxin_muPIIIA-4,154125,27389
BMRB,27383,conotoxin_muPIIIA-5,154125,27389
BMRB,27384,conotoxin_muPIIIA-6,154125,27389
BMRB,27385,conotoxin_muPIIIA-9,154125,27389
BMRB,27386,conotoxin_muPIIIA-11,154125,27389
BMRB,27388,conotoxin_muPIIIA-8,154125,27389
BMRB,27390,conotoxin_muPIIIA-15,154125,27389
BMRB,27391,conotoxin_muPIIIA-14,154125,27389
BMRB,27379,conotoxin_muPIIIA-3,154144,27390
BMRB,27382,conotoxin_muPIIIA-4,154144,27390
BMRB,27383,conotoxin_muPIIIA-5,154144,27390
BMRB,27384,conotoxin_muPIIIA-6,154144,27390
BMRB,27385,conotoxin_muPIIIA-9,154144,27390
BMRB,27386,conotoxin_muPIIIA-11,154144,27390
BMRB,27388,conotoxin_muPIIIA-8,154144,27390
BMRB,27389,conotoxin_muPIIIA-10,154144,27390
BMRB,27391,conotoxin_muPIIIA-14,154144,27390
BMRB,27379,conotoxin_muPIIIA-3,154163,27391
BMRB,27382,conotoxin_muPIIIA-4,154163,27391
BMRB,27383,conotoxin_muPIIIA-5,154163,27391
BMRB,27384,conotoxin_muPIIIA-6,154163,27391
BMRB,27385,conotoxin_muPIIIA-9,154163,27391
BMRB,27386,conotoxin_muPIIIA-11,154163,27391
BMRB,27388,conotoxin_muPIIIA-8,154163,27391
BMRB,27389,conotoxin_muPIIIA-10,154163,27391
BMRB,27390,conotoxin_muPIIIA-15,154163,27391
PDB,7HSC,High resolution solution structure of human Hsc70 substrate binding domain,154228,27395
BMRB,27399,USR+YTH domain (RNA complex),154290,27398
BMRB,27398,USR+YTH domain (APO),154307,27399
BMRB,27160,"1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of wild-type human flap endonuclease-1",154386,27403
BMRB,27404,"1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of K93A human flap endonuclease-1 in complex with dual-hairpin DNA substrate",154386,27403
PDB,3Q8K,"Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap DNA, SM3+, and K+",154386,27403
BMRB,27160,"1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of wild-type human flap endonuclease-1.",154402,27404
BMRB,27403,"1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of P188A human flap endonuclease-1",154402,27404
PDB,3Q8K,"Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap DNA, SM3+, and K+",154402,27404
BMRB,27409,Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta and 1-nucleotide gapped double hairpin DNA binary complex,154449,27407
BMRB,27410,"Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta, 1-nucleotide gapped double hairpin DNA and  dAMPCPP ternary complex",154449,27407
BMRB,27407,Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta,154481,27409
BMRB,27449,AV Rop,155146,27450
BMRB,27451,IVVA Rop,155146,27450
BMRB,27410,"Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta, 1-nucleotide gapped double hairpin DNA and  dAMPCPP ternary complex",154481,27409
BMRB,27407,Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta,154505,27410
BMRB,27409,Ile and Met methyl 1H and 13C chemical shifts of DNA polymerase beta and 1-nucleotide gapped double hairpin DNA binary complex,154505,27410
PDB,3ZUD,X-ray crystal structure of TaLPMO9A,154530,27411
BMRB,27416,"Human Myc S373D/T400D, N353 to A399",154578,27414
BMRB,27418,"Human Myc S373D, N353 to A399",154578,27414
BMRB,27419,"Human Myc S373E/T400E, N353 to A399",154578,27414
BMRB,27421,"Human Myc T400D, N353 to A399",154578,27414
BMRB,27422,"Human Myc, N353 to A399, phosphorylated by PAK2",154578,27414
BMRB,27414,Human Myc N353 to A399,154609,27416
BMRB,27418,"Human Myc S373D, N353 to A399",154609,27416
BMRB,27419,"Human Myc S373E/T400E, N353 to A399",154609,27416
BMRB,27421,"Human Myc T400D, N353 to A399",154609,27416
BMRB,27422,"Human Myc, N353 to A399, phosphorylated by PAK2",154609,27416
BMRB,27414,Human Myc N353 to A399,154648,27418
BMRB,27416,"Human Myc S373D/T400D, N353 to A399",154648,27418
BMRB,27419,"Human Myc S373E/T400E, N353 to A399",154648,27418
BMRB,27421,"Human Myc T400D, N353 to A399",154648,27418
BMRB,27422,"Human Myc, N353 to A399, phosphorylated by PAK2",154648,27418
BMRB,27414,Human Myc N353 to A399,154662,27419
BMRB,27416,"Human Myc S373D/T400D, N353 to A399",154662,27419
BMRB,27418,"Human Myc S373D, N353 to A399",154662,27419
BMRB,27421,"Human Myc T400D, N353 to A399",154662,27419
BMRB,27422,"Human Myc, N353 to A399, phosphorylated by PAK2",154662,27419
BMRB,27414,Human Myc N353 to A399,154692,27421
BMRB,27416,"Human Myc S373D/T400D, N353 to A399",154692,27421
BMRB,27418,"Human Myc S373D, N353 to A399",154692,27421
BMRB,27419,"Human Myc S373E/T400E, N353 to A399",154692,27421
BMRB,27422,"Human Myc, N353 to A399, phosphorylated by PAK2",154692,27421
BMRB,27414,Human Myc N353 to A399,154706,27422
BMRB,27416,"Human Myc S373D/T400D, N353 to A399",154706,27422
BMRB,27418,"Human Myc S373D, N353 to A399",154706,27422
BMRB,27419,"Human Myc S373E/T400E, N353 to A399",154706,27422
BMRB,27421,"Human Myc T400D, N353 to A399",154706,27422
BMRB,25426,Wild-type MBD2 intrinsically disordered region,154752,27426
BMRB,27430,KIBRA C2 domain: variant C771A,154767,27429
PDB,6FB4,KIBRA C2(C771A) crystal structure,154767,27429
PDB,6FD0,KIBRA variant C2 crystal structure,154767,27429
PDB,6FJC,"KIBRA C2(C771A)-PI(3,4,5)P3 complex crystal structure",154767,27429
PDB,6FJD,"KIBRA C2(C771A)-PI(3,4,5)P3 complex crystal structure",154767,27429
BMRB,27429,KIBRA C2 domain: C771A,154784,27430
PDB,6FB4,KIBRA C2(C771A) crystal structure,154784,27430
PDB,6FD0,KIBRA variant C2 crystal structure,154784,27430
PDB,6FJC,"KIBRA C2(C771A)-PI(3,4,5)P3 complex crystal structure",154784,27430
PDB,6FJD,"KIBRA C2(C771A)-PI(3,4,5)P3 complex crystal structure",154784,27430
PDB,6FSU,Crystal structure of E.coli C-ter extended BamA barrel,154801,27431
BMRB,27441,a6tcr beta,154973,27440
BMRB,27440,a6tcr alpha,154989,27441
BMRB,15519,Backbone chemical shift assigment of chicken osteopontin,155021,27443
BMRB,18413,Backbone and methyl side chain assignments of apo AdcR at pH 6.0,155068,27447
BMRB,18414,Backbone and methyl side chain assignments of Zn(II) AdcR at pH 6.0,155068,27447
BMRB,27448,"Backbone and side-chain methyl relaxation rates, methyl order parameters, stereospecific resonance assignments, and relaxation rates for apo-AdcR",155068,27447
PDB,3TGN,Crystal Structure of the zinc-dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-bound State,155068,27447
PDB,5JLS,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes (C-terminally His tagged),155068,27447
PDB,5JLU,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes,155068,27447
PDB,5YHX,"Structure of Lactococcus lactis ZitR, wild type",155068,27447
PDB,5YHY,"Structure of Lactococcus lactis ZitR, C30S mutant",155068,27447
PDB,5YHZ,"Structure of Lactococcus lactis ZitR, E41A mutant",155068,27447
PDB,5YI0,"Structure of Lactococcus lactis ZitR, C30AH42A mutant",155068,27447
PDB,5YI1,"Structure of Lactococcus lactis ZitR, C30AH42A mutant in apo form",155068,27447
PDB,5YI2,"Structure of Lactococcus lactis ZitR, wild type in complex with DNA",155068,27447
PDB,5YI3,"Structure of Lactococcus lactis ZitR, C30S mutant in complex with DNA",155068,27447
BMRB,18413,Backbone and methyl side chain assignments of apo AdcR at pH 6.0,155100,27448
BMRB,18414,Backbone and methyl side chain assignments of Zn(II) AdcR at pH 6.0,155100,27448
BMRB,27447,"Backbone and side-chain methyl relaxation rates, methyl order parameters, stereospecific resonance assignments, and relaxation rates for Zn(II) AdcR",155100,27448
PDB,3TGN,Crystal Structure of the zinc-dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-bound State,155100,27448
PDB,5JLS,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes (C-terminally His tagged),155100,27448
PDB,5JLU,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes,155100,27448
PDB,5YHX,"Structure of Lactococcus lactis ZitR, wild type",155100,27448
PDB,5YHY,"Structure of Lactococcus lactis ZitR, C30S mutant",155100,27448
PDB,5YHZ,"Structure of Lactococcus lactis ZitR, E41A mutant",155100,27448
PDB,5YI0,"Structure of Lactococcus lactis ZitR, C30AH42A mutant",155100,27448
PDB,5YI1,"Structure of Lactococcus lactis ZitR, C30AH42A mutant in apo form",155100,27448
PDB,5YI2,"Structure of Lactococcus lactis ZitR, wild type in complex with DNA",155100,27448
PDB,5YI3,"Structure of Lactococcus lactis ZitR, C30S mutant in complex with DNA",155100,27448
BMRB,27450,WT Rop,155130,27449
BMRB,27451,IVVA Rop,155130,27449
BMRB,27449,AV Rop,155162,27451
BMRB,27450,WT Rop,155162,27451
BMRB,15177,Resonance assignments of CzrA in apo form,155232,27455
BMRB,26959,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for apo CzrA",155232,27455
BMRB,27028,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for Zn(II) CzrA",155232,27455
BMRB,27459,side-chain methyl order parameters for Zn(II)-bound CzrA L34A mutant at 25C-40C,155232,27455
BMRB,7376,Resonance assignments of CzrA in complex with Zinc ion,155232,27455
BMRB,7377,Resonance assignments of CzrA in complex with DNA,155232,27455
PDB,1R1U,crystal structure of CzrA in apo form,155232,27455
PDB,1R1V,crystal structure of CzrA in Zn(II) form,155232,27455
PDB,2KJB,Solution structure of CzrA in the DNA bound state,155232,27455
PDB,2KJC,Soluction structure of CzrA in the Zn(II) state,155232,27455
BMRB,15177,Resonance assignments of CzrA in apo form,155293,27459
BMRB,26959,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for apo CzrA",155293,27459
BMRB,27028,"side-chain methyl order parameters, stereospecific resonance assignments, and relaxation rates for Zn(II) CzrA",155293,27459
BMRB,27455,side-chain methyl order parameters for apo CzrA L34A mutant at 25C-40C,155293,27459
BMRB,7376,Resonance assignments of CzrA in complex with Zinc ion,155293,27459
BMRB,7377,Resonance assignments of CzrA in complex with DNA,155293,27459
PDB,1R1U,crystal structure of CzrA in apo form,155293,27459
PDB,1R1V,crystal structure of CzrA in Zn(II) form,155293,27459
PDB,2KJB,Solution structure of CzrA in the DNA bound state,155293,27459
PDB,2KJC,Soluction structure of CzrA in the Zn(II) state,155293,27459
BMRB,27463,Holo form of Biliverdin reductase B,155357,27462
BMRB,27462,Apo form of Biliverdin reductase B,155373,27463
BMRB,27099,Entry containing backbone resonances for this molecular system,155449,27468
BMRB,27224,"1H, 15N, 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2 in complex with oxidised flavin mononucleotide",155470,27469
BMRB,27470,"1H, 15N, 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2 in complex with 1,4,5,6-tetrahydro-NAD",155470,27469
PDB,3P62,WILD-TYPE PENTAERYTHRITOL TETRANITRATE REDUCTASE CONTAINING A C-TERMINAL 8-HISTIDINE TAG FROM ENTEROBACTER CLOACAE,155470,27469
PDB,5LGX,STRUCTURE OF OXIDISED PENTAERYTHRITOL TETRANITRATE REDUCTASE FROM ENTEROBACTER CLOACAE,155470,27469
BMRB,27224,"1H, 15N, 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2 in complex with oxidised flavin mononucleotide",155487,27470
BMRB,27469,"1H, 15N, 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2 in complex with 1,4,5,6-tetrahydro-NADP",155487,27470
PDB,3P62,WILD-TYPE PENTAERYTHRITOL TETRANITRATE REDUCTASE CONTAINING A C-TERMINAL 8-HISTIDINE TAG FROM ENTEROBACTER CLOACAE,155487,27470
PDB,5LGX,STRUCTURE OF OXIDISED PENTAERYTHRITOL TETRANITRATE REDUCTASE FROM ENTEROBACTER CLOACAE,155487,27470
BMRB,27479,teixobactin in solution,155608,27478
BMRB,27480,teixobactin:lipid II complex in DPC micelles,155608,27478
BMRB,27478,teixobactin in DPC micelles,155626,27479
BMRB,27480,teixobactin:lipid II complex in DPC micelles,155626,27479
BMRB,27478,teixobactin in DPC micelles,155644,27480
BMRB,27479,teixobactin in solution,155644,27480
BMRB,27490,"1H, 15N Assignment of rS1-D345",155754,27489
BMRB,27489,"1H, 15N, 13C Assignment of rS1-D5",155772,27490
BMRB,27492,SGPI-2 variant,155788,27491
BMRB,27491,SGPI-2 variant,155803,27492
BMRB,16942,"Solution NMR Structure () from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518",155818,27493
PDB,2KY9,"Solution NMR Structure of ydhK C-terminal Domain from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518",155818,27493
BMRB,27495,deubiquitinase A phosphorylated at Ser177,155843,27494
BMRB,27494,deubiquitinase A,155858,27495
BMRB,27501,SP6 variant of SPINK1,155959,27500
BMRB,27500,SP5 variant of SPINK1,155977,27501
BMRB,27511,HECT domain C-lobe,156042,27508
BMRB,27512,C-lobe,156042,27508
PDB,6FX4,,156042,27508
BMRB,27510,"hFABP1 K57A, E77A, K96A mutant",156056,27509
BMRB,27509,"hFABP1 K57A, E77A, K96A mutant",156072,27510
BMRB,27508,C-lobe,156088,27511
BMRB,27512,C-lobe,156088,27511
PDB,6FX4,,156088,27511
BMRB,27514,wild-type transthyretin,156116,27513
BMRB,27515,V30M,156116,27513
BMRB,27516,V122I Transthyretin,156116,27513
BMRB,27513,transthyretin,156130,27514
BMRB,27515,V30M,156130,27514
BMRB,27516,V122I Transthyretin,156130,27514
BMRB,27513,transthyretin,156144,27515
BMRB,27514,wild-type transthyretin,156144,27515
BMRB,27516,V122I Transthyretin,156144,27515
BMRB,27513,transthyretin,156158,27516
BMRB,27514,wild-type transthyretin,156158,27516
BMRB,27515,V30M Transthyretin,156158,27516
BMRB,27521,shp2-cd5,156224,27520
BMRB,27522,shp2_shnc_e76k,156224,27520
BMRB,27520,shp2-fl-iso2-dC,156245,27521
BMRB,27522,shp2_shnc_e76k,156245,27521
PIR,PR:Q8TDQ0,,156320,27525
BMRB,26833,wild type,156336,27526
BMRB,27467,FAT10 C-terminal domain,156350,27527
PDB,6GF1,,156350,27527
NCBI,NP_001164226.1,,156443,27533
BMRB,30493,chemical shift assignment,156459,27534
BMRB,27538,Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0,156514,27537
BMRB,27537,Chemical Shift Assignments for the C-terminal domain of histone H1.0,156533,27538
GB,AAB00389,,156890,27561
GB,AAH60998,,156890,27561
BMRB,27541,Influenza A virus (2013 H7N9 strain) non-structural protein 1 effector domain,156554,27539
BMRB,27539,Influenza A virus non-structural protein 1 (NS1) effector domain,156588,27541
BMRB,27544,Pongo pygmaeus ECP,156606,27542
BMRB,27545,Pongo abelii RNase 3,156606,27542
BMRB,27546,Aotus trivirgatus EDN,156606,27542
EMBL,U24098.1,,156606,27542
BMRB,27542,Macaca fascicularis ECP,156635,27544
BMRB,27545,Pongo abelii RNase 3,156635,27544
BMRB,27546,Aotus trivirgatus EDN,156635,27544
EMBL,AAC50147.1,,156635,27544
BMRB,27542,Macaca fascicularis ECP,156649,27545
BMRB,27544,Pongo pygmaeus ECP,156649,27545
BMRB,27546,Aotus trivirgatus EDN,156649,27545
EMBL,PNJ36109.1,Pongo abelii (Sumatran orangutan) RNASE3 isoform 1,156649,27545
BMRB,27542,Macaca fascicularis ECP,156663,27546
BMRB,27544,Pongo pygmaeus ECP,156663,27546
BMRB,27545,Pongo abelii RNase 3,156663,27546
EMBL,AAB71338.1,Aotus trivirgatus (douroucouli) ribonuclease precursor,156663,27546
BMRB,27187,assignments of H2B in H2A/H2B dimer,156677,27547
BMRB,27346,assignments of H2A in the nucleosome,156677,27547
BMRB,27554,intrinsically disordered SH4 and Unique domains of p61Hck,156759,27553
BMRB,27553,intrinsically disordered SH4 and Unique domains of p59Hck,156777,27554
BMRB,26942,"Backbone and Side-Chain (1)H, (13)C, and (15)N Chemical Shift Assignments for the homodimeric Histone-like DNA binding protein (Hup) of Helicobacter pylori",156827,27557
BMRB,18267,Substrate-dependent millisecond domain motions in DNA polymerase beta,156857,27559
BMRB,27560,protein-gapped DNA complex,156857,27559
BMRB,27561,protein-gapped DNA-nucelotide complex,156857,27559
BMRB,5208,Perdeuterated 22 kD Palm-thumb Domain of DNA Polymerase Beta,156857,27559
DBJ,BAC36630,,156857,27559
DBJ,BAE27405,,156857,27559
DBJ,BAE30399,,156857,27559
GB,AAA41900,,156857,27559
GB,AAA41901,,156857,27559
GB,AAB00389,,156857,27559
GB,AAH60998,,156857,27559
GB,AAH98668,,156857,27559
PDB,1BPB,,156857,27559
PDB,1BPD,,156857,27559
PDB,1BPE,,156857,27559
PDB,1HUO,,156857,27559
PDB,1HUZ,,156857,27559
PDB,1JN3,,156857,27559
PDB,1NOM,,156857,27559
PDB,1RPL,,156857,27559
PDB,1ZQU,,156857,27559
PDB,1ZQV,,156857,27559
PDB,1ZQW,,156857,27559
PDB,1ZQX,,156857,27559
PDB,1ZQY,,156857,27559
PDB,1ZQZ,,156857,27559
PDB,2BPC,,156857,27559
PDB,2BPF,,156857,27559
PDB,2BPG,,156857,27559
PDB,2VAN,,156857,27559
PDB,3K75,,156857,27559
PDB,3LQC,,156857,27559
PDB,3UXN,,156857,27559
PDB,3UXO,,156857,27559
PDB,3UXP,,156857,27559
PDB,3V72,,156857,27559
PDB,3V7J,,156857,27559
PDB,3V7K,,156857,27559
PDB,3V7L,,156857,27559
PDB,6BTE,,156857,27559
PDB,6BTF,,156857,27559
REF,NP_035260,,156857,27559
REF,NP_058837,,156857,27559
REF,XP_005066593,,156857,27559
REF,XP_005362476,,156857,27559
BMRB,18267,Substrate-dependent millisecond domain motions in DNA polymerase beta,156872,27560
BMRB,27559,Apo DNA Polymerase beta,156872,27560
BMRB,27561,protein-gapped DNA-nucelotide complex,156872,27560
BMRB,5208,Perdeuterated 22 kD Palm-thumb Domain of DNA Polymerase Beta,156872,27560
DBJ,BAC36630,,156872,27560
DBJ,BAE27405,,156872,27560
DBJ,BAE30399,,156872,27560
GB,AAA41900,,156872,27560
GB,AAA41901,,156872,27560
GB,AAB00389,,156872,27560
GB,AAH60998,,156872,27560
GB,AAH98668,,156872,27560
PDB,1BPB,,156872,27560
PDB,1BPD,,156872,27560
PDB,1BPE,,156872,27560
PDB,1HUO,,156872,27560
PDB,1HUZ,,156872,27560
PDB,1JN3,,156872,27560
PDB,1NOM,,156872,27560
PDB,1RPL,,156872,27560
PDB,1ZQU,,156872,27560
PDB,1ZQV,,156872,27560
PDB,1ZQW,,156872,27560
PDB,1ZQX,,156872,27560
PDB,1ZQY,,156872,27560
PDB,1ZQZ,,156872,27560
PDB,2BPC,,156872,27560
PDB,2BPF,,156872,27560
PDB,2BPG,,156872,27560
PDB,2VAN,,156872,27560
PDB,3K75,,156872,27560
PDB,3LQC,,156872,27560
PDB,3UXN,,156872,27560
PDB,3UXO,,156872,27560
PDB,3UXP,,156872,27560
PDB,3V72,,156872,27560
PDB,3V7J,,156872,27560
PDB,3V7K,,156872,27560
PDB,3V7L,,156872,27560
PDB,6BTE,,156872,27560
PDB,6BTF,,156872,27560
REF,NP_035260,,156872,27560
REF,NP_058837,,156872,27560
REF,XP_005066593,,156872,27560
REF,XP_005362476,,156872,27560
BMRB,18267,Substrate-dependent millisecond domain motions in DNA polymerase beta,156890,27561
BMRB,27559,Apo DNA Polymerase beta,156890,27561
BMRB,27560,protein-gapped DNA complex,156890,27561
BMRB,5208,Perdeuterated 22 kD Palm-thumb Domain of DNA Polymerase Beta,156890,27561
DBJ,BAC36630,,156890,27561
DBJ,BAE27405,,156890,27561
DBJ,BAE30399,,156890,27561
GB,AAA41900,,156890,27561
GB,AAA41901,,156890,27561
GB,AAH98668,,156890,27561
PDB,1BPB,,156890,27561
PDB,1BPD,,156890,27561
PDB,1BPE,,156890,27561
PDB,1HUO,,156890,27561
PDB,1HUZ,,156890,27561
PDB,1JN3,,156890,27561
PDB,1NOM,,156890,27561
PDB,1RPL,,156890,27561
PDB,1ZQU,,156890,27561
PDB,1ZQV,,156890,27561
PDB,1ZQW,,156890,27561
PDB,1ZQX,,156890,27561
PDB,1ZQY,,156890,27561
PDB,1ZQZ,,156890,27561
PDB,2BPC,,156890,27561
PDB,2BPF,,156890,27561
PDB,2BPG,,156890,27561
PDB,2VAN,,156890,27561
PDB,3K75,,156890,27561
PDB,3LQC,,156890,27561
PDB,3UXN,,156890,27561
PDB,3UXO,,156890,27561
PDB,3UXP,,156890,27561
PDB,3V72,,156890,27561
PDB,3V7J,,156890,27561
PDB,3V7K,,156890,27561
PDB,3V7L,,156890,27561
PDB,6BTE,,156890,27561
PDB,6BTF,,156890,27561
REF,NP_035260,,156890,27561
REF,NP_058837,,156890,27561
REF,XP_005066593,,156890,27561
REF,XP_005362476,,156890,27561
PDB,6G6J,2.25A X-ray crystal structure.,157051,27571
PDB,6G6K,1.35A X-ray crystal structure.,157051,27571
PDB,6G6L,2.2 X-ray crystal structure.,157051,27571
PDB,1TFG,,157106,27574
PDB,2TGI,,157106,27574
BMRB,27576,A97S TTR in 5% DMSO,157121,27575
BMRB,27575,wt TTR in 5% DMSO,157137,27576
BMRB,36206,Rac1 in the low-affinity state for Mg2+,157153,27577
BMRB,5511,21 kDa GTPase Rac1 complexed to GDP and Mg2+,157153,27577
PDB,6AGP,,157153,27577
BMRB,27417,Putative methyltransferase WBSCR27 in complex with S-adenosyl-L-methionine,157172,27578
BMRB,27585,MAK33 EV-CH2-SK antibody domain extended variant,157268,27584
BMRB,27584,"MAK33 CH2 antibody domain, wild type",157284,27585
PDB,5LBN,High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6,157317,27587
BMRB,27589,crystalline E.coli asparaginase II (ANSII) by solid-state NMR,157331,27588
BMRB,27590,pegylated E.coli asparaginase II (ANSII) by solid-state NMR,157331,27588
BMRB,27588,E.coli asparaginase (ANSII) by solution NMR,157348,27589
BMRB,27590,pegylated E.coli asparaginase II (ANSII) by solid-state NMR,157348,27589
BMRB,27588,E.coli asparaginase (ANSII) by solution NMR,157366,27590
BMRB,27589,crystalline E.coli asparaginase II (ANSII) by solid-state NMR,157366,27590
BMRB,27592,BM13851 strain of P[8] VP8* rotavirus,157384,27591
BMRB,27591,BM11596 strain of P[6] VP8* rotavirus,157400,27592
PDB,5D6H,Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii,157433,27594
PDB-Dev,PDBDEV_00000024,Ghrelin Binding at its G Protein-Coupled Receptor,157531,27600
BMRB,26721,RXFP1-LDLa-linker,157547,27601
BMRB,27019,RXFP2-LDLa-linker,157547,27601
BMRB,15276,"1H, 13C and 15N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lambda VI light chain variable domain",157561,27602
BMRB,19798,Solution chemical shifts of 6aJL2-R24G mutant Amyloidogenic Light Chain Protein,157561,27602
BMRB,19870,Solution chemical shifts of 6aJL2 Amyloidogenic Light Chain Protein,157561,27602
SP,P51955,Nek2 homo sapiens full length,157594,27605
PDB,3PYI,Crystallographic structure of a dimer formed by this domain,157631,27607
PDB,4G79,Crystallographic structure of this domain,157631,27607
BMRB,27610,FN III 14 module,157662,27609
BMRB,27609,FN III 13 module,157677,27610
BMRB,30043,Mayaro virus macro domain,157706,27612
PDB,5IQ5,,157706,27612
SP,P62937,Peptidyl-prolyl cis-trans isomerase A,157815,27620
BMRB,27624,Klebsiella pneumoniae sigma4 of sigmaS fused to the beta-flap-tip helix,157859,27623
BMRB,27623,Klebsiella pneumoniae sigma4 of sigma70 fused to the beta-flap-tip helix,157873,27624
BMRB,27630,FBP21(326-276) Fragment in Complex with the Brr2-CSec63 domain,157948,27629
BMRB,27629,FBP21(326-276) Fragment,157976,27630
BMRB,27632,NRASQ61K/HLA-A*01:01/human beta2m,157992,27631
BMRB,27682,NIH:H-2Ld:hb2m,157992,27631
BMRB,27631,TAX/HLA-A*02:01/human beta2m,158011,27632
BMRB,27682,NIH:H-2Ld:hb2m,158011,27632
BMRB,27638,oleate bound form,158118,27637
BMRB,27637,apo form,158134,27638
BMRB,27642,Mps1 62-239,158194,27641
BMRB,27641,Mps1 1-239,158208,27642
PDB,4B94,,158208,27642
BMRB,27648,Kinase Inducible Domain of CREB,158279,27647
BMRB,27647,Phosphorylated Kinase Inducible Domain (KID) of CREB,158299,27648
BMRB,18413,Backbone and methyl side chain assignments of apo AdcR at pH 6.0,158393,27655
BMRB,18414,Backbone and methyl side chain assignments of Zn(II) AdcR at pH 6.0,158393,27655
BMRB,27447,"Backbone and side-chain methyl relaxation rates, methyl order parameters, stereospecific resonance assignments, and zn AdcR",158393,27655
BMRB,27448,"Backbone and side-chain methyl relaxation rates, methyl order parameters, stereospecific resonance assignments, and relaxation rates for WT apo-AdcR",158393,27655
BMRB,27656,Backbone assignments and relaxation rates for apo L57M AdcR,158393,27655
PDB,3TGN,Crystal Structure of the zinc-dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-bound State,158393,27655
PDB,5JLS,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes (C-terminally His tagged),158393,27655
PDB,5JLU,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes,158393,27655
PDB,5YHX,"Structure of Lactococcus lactis ZitR, wild type",158393,27655
PDB,5YHY,"Structure of Lactococcus lactis ZitR, C30S mutant",158393,27655
PDB,5YHZ,"Structure of Lactococcus lactis ZitR, E41A mutant",158393,27655
PDB,5YI0,"Structure of Lactococcus lactis ZitR, C30AH42A mutant",158393,27655
PDB,5YI1,"Structure of Lactococcus lactis ZitR, C30AH42A mutant in apo form",158393,27655
PDB,5YI2,"Structure of Lactococcus lactis ZitR, wild type in complex with DNA",158393,27655
PDB,5YI3,"Structure of Lactococcus lactis ZitR, C30S mutant in complex with DNA",158393,27655
BMRB,18413,Backbone and methyl side chain assignments of apo AdcR at pH 6.0,158418,27656
BMRB,18414,Backbone and methyl side chain assignments of Zn(II) AdcR at pH 6.0,158418,27656
BMRB,27447,"Backbone and side-chain methyl relaxation rates, methyl order parameters, stereospecific resonance assignments for Zn(II) AdcR",158418,27656
BMRB,27448,"Backbone and side-chain methyl relaxation rates, methyl order parameters, and stereospecific resonance assignments WT apo AdcR",158418,27656
BMRB,27655,Backbone assignments and relaxation rates for Zn L57M AdcR,158418,27656
PDB,3TGN,Crystal Structure of the zinc-dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-bound State,158418,27656
PDB,5JLS,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes (C-terminally His tagged),158418,27656
PDB,5JLU,Crystal Structure of Adhesin competence repressor (AdcR) from Streptococcus pyogenes,158418,27656
PDB,5YHX,"Structure of Lactococcus lactis ZitR, wild type",158418,27656
PDB,5YHY,"Structure of Lactococcus lactis ZitR, C30S mutant",158418,27656
PDB,5YHZ,"Structure of Lactococcus lactis ZitR, E41A mutant",158418,27656
PDB,5YI0,"Structure of Lactococcus lactis ZitR, C30AH42A mutant",158418,27656
PDB,5YI1,"Structure of Lactococcus lactis ZitR, C30AH42A mutant in apo form",158418,27656
PDB,5YI2,"Structure of Lactococcus lactis ZitR, wild type in complex with DNA",158418,27656
PDB,5YI3,"Structure of Lactococcus lactis ZitR, C30S mutant in complex with DNA",158418,27656
BMRB,15498,UbcH7,158488,27664
BMRB,4769,Yeast ubiquitin,158488,27664
BMRB,10010,bovine beta-lactoglobulin A34C mutant,158541,27668
PDB,1CJ5,BOVINE BETA-LACTOGLOBULIN A,158541,27668
PDB,1DV9,STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER,158541,27668
PDB,6G2K,RRM+U6,158591,27671
PDB,6GD1,RRM3-Trx,158591,27671
PDB,6GD2,RRM3+AU15,158591,27671
PDB,6GD3,RRM3+AU6tnf,158591,27671
BMRB,26746,,158609,27672
BMRB,27678,E71A mutant,158669,27676
BMRB,27679,E71I mutant,158669,27676
BMRB,27680,E71Q mutant,158669,27676
BMRB,27676,Wild Type,158702,27678
BMRB,27679,E71I mutant,158702,27678
BMRB,27680,E71Q mutant,158702,27678
BMRB,27676,Wild Type,158719,27679
BMRB,27678,E71A mutant,158719,27679
BMRB,27680,E71Q mutant,158719,27679
BMRB,27676,Wild Type,158749,27680
BMRB,27678,E71A mutant,158749,27680
BMRB,27679,E71I mutant,158749,27680
BMRB,27631,TAX/HLA-A*02:01/human beta2m,158786,27682
BMRB,27632,NRASQ61K/HLA-A*01:01/human beta2m,158786,27682
BMRB,19165,Backbone and side chain chemical shift assignments of inactive HdeA,158920,27693
PDB,5WYO,solution NMR structure of inactive HdeA,158920,27693
BMRB,27695,FK506 bound FKBP12 C22A,158935,27694
BMRB,27694,apo FKBP12 C22A,158949,27695
BMRB,27698,"P15 mutant K15C, K24C, C54S, and C99S",158963,27696
BMRB,27696,This is the aNMR assignment of the doubly ubiquitinated p15CCSS,158978,27698
BMRB,27700,Human linker histone NGH1x in low ionic strength conditions,158992,27699
BMRB,27699,Human linker histone NGH1x in high ionic strength conditions,159017,27700
BMRB,27702,bHLHZip domain of Myc (in presence of 2.4 M GdmCl),159041,27701
BMRB,27703,bHLHZip domain of Myc (in presence of 1.6 M GdmCl),159041,27701
BMRB,27704,bHLHZip domain of Myc,159041,27701
BMRB,27701,bHLHZip domain of Myc (in presence of 3.2 M GdmCl),159055,27702
BMRB,27703,bHLHZip domain of Myc (in presence of 1.6 M GdmCl),159055,27702
BMRB,27704,bHLHZip domain of Myc,159055,27702
BMRB,27701,bHLHZip domain of Myc (in presence of 3.2 M GdmCl),159069,27703
BMRB,27702,bHLHZip domain of Myc (in presence of 2.4 M GdmCl),159069,27703
BMRB,27704,bHLHZip domain of Myc,159069,27703
BMRB,27701,bHLHZip domain of Myc (in presence of 3.2 M GdmCl),159083,27704
BMRB,27702,bHLHZip domain of Myc (in presence of 2.4 M GdmCl),159083,27704
BMRB,27703,bHLHZip domain of Myc (in precence of 1.6 M GdmCl),159083,27704
BMRB,27543,Backbone assignment of mouse MARCH9 transmembrane domains in LMPG micelles,159162,27709
BMRB,27714,L4Q8,159215,27713
BMRB,27715,L4Q12,159215,27713
BMRB,27716,L4Q16,159215,27713
BMRB,27717,L4Q20,159215,27713
BMRB,27713,L4Q4,159229,27714
BMRB,27715,L4Q12,159229,27714
BMRB,27716,L4Q16,159229,27714
BMRB,27717,L4Q20,159229,27714
BMRB,27713,L4Q4,159245,27715
BMRB,27714,L4Q8,159245,27715
BMRB,27716,L4Q16,159245,27715
BMRB,27717,L4Q20,159245,27715
BMRB,27713,Androgen Receptor (AR) polyQ-derived peptide L4Q4,159261,27716
BMRB,27714,Androgen Receptor (AR) polyQ-derived peptide L4Q8,159261,27716
BMRB,27715,Androgen Receptor (AR) polyQ-derived peptide L4Q12,159261,27716
BMRB,27717,Androgen Receptor (AR) polyQ-derived peptide L4Q20,159261,27716
BMRB,27713,Androgen Receptor (AR) polyQ-derived peptide L4Q4,159277,27717
BMRB,27714,Androgen Receptor (AR) polyQ-derived peptide L4Q8,159277,27717
BMRB,27715,Androgen Receptor (AR) polyQ-derived peptide L4Q12,159277,27717
BMRB,27716,Androgen Receptor (AR) polyQ-derived peptide L4Q16,159277,27717
BMRB,27719,KRas-G12D(1-169)-GDP,159293,27718
BMRB,27720,KRas-wt(1-169)-GDP,159293,27718
BMRB,27718,KRas-G12V(1-169)-GDP,159312,27719
BMRB,27720,KRas-wt(1-169)-GDP,159312,27719
BMRB,27718,KRas-G12V(1-169)-GDP,159331,27720
BMRB,27719,KRas-G12D(1-169)-GDP,159331,27720
BMRB,27722,Galectin-3 bound to R,159350,27721
BMRB,27721,Galectin-3 bound to S,159394,27722
BMRB,30550,NMR assignments of this entity in the complex with arachidonic acid,159438,27724
PDB,6NBN,Structure of OBP22 in the complex with arachidonic acid,159438,27724
BMRB,27730,TMC.BHV,159493,27728
PDB,6NCU,,159512,27729
BMRB,27728,N.BHV,159528,27730
BMRB,27733,FKBP12 protein from Aspergillus fumigatus bound to FK506,159547,27732
BMRB,27734,FKBP12 from the pathogenic fungi Mucor circinelloides,159547,27732
BMRB,27737,FKBP12 protein from the pathogenic fungi Mucor circinelloides bound to FK506,159547,27732
BMRB,27738,Human FKBP12 protein,159547,27732
BMRB,27739,Human FKBP12 protein bound to FK506,159547,27732
NCBI,XP_751096.1,Sequence for FKBP12,159547,27732
BMRB,27732,apo FKBP12 protein from Aspergillus fumigatus,159568,27733
BMRB,27734,FKBP12 from the pathogenic fungi Mucor circinelloides,159568,27733
BMRB,27737,FKBP12 protein from the pathogenic fungi Mucor circinelloides bound to FK506,159568,27733
BMRB,27738,Human FKBP12 protein,159568,27733
BMRB,27739,Human FKBP12 protein bound to FK506,159568,27733
NCBI,XP_751096.1,Sequence for FKBP12,159568,27733
BMRB,27732,apo FKBP12 protein from Aspergillus fumigatus,159591,27734
BMRB,27733,FKBP12 protein from Aspergillus fumigatus bound to FK506,159591,27734
BMRB,27737,FKBP12 protein from the pathogenic fungi Mucor circinelloides bound to FK506,159591,27734
BMRB,27738,Human FKBP12 protein,159591,27734
BMRB,27739,Human FKBP12 protein bound to FK506,159591,27734
NCBI,AGW24132.1,Sequence for FKBP12,159591,27734
BMRB,27732,apo FKBP12 protein from Aspergillus fumigatus,159612,27737
BMRB,27733,FKBP12 protein from Aspergillus fumigatus bound to FK506,159612,27737
BMRB,27734,FKBP12 from the pathogenic fungi Mucor circinelloides,159612,27737
BMRB,27738,Human FKBP12 protein,159612,27737
BMRB,27739,Human FKBP12 protein bound to FK506,159612,27737
NCBI,AGW24132.1,,159612,27737
BMRB,27732,apo FKBP12 protein from Aspergillus fumigatus,159635,27738
BMRB,27733,FKBP12 protein from Aspergillus fumigatus bound to FK506,159635,27738
BMRB,27734,FKBP12 from the pathogenic fungi Mucor circinelloides,159635,27738
BMRB,27737,FKBP12 protein from the pathogenic fungi Mucor circinelloides bound to FK506,159635,27738
BMRB,27739,Human FKBP12 protein bound to FK506,159635,27738
NCBI,AAP36774.1,,159635,27738
BMRB,27732,apo FKBP12 protein from Aspergillus fumigatus,159656,27739
BMRB,27733,FKBP12 protein from Aspergillus fumigatus bound to FK506,159656,27739
BMRB,27734,FKBP12 from the pathogenic fungi Mucor circinelloides,159656,27739
BMRB,27737,FKBP12 protein from the pathogenic fungi Mucor circinelloides bound to FK506,159656,27739
BMRB,27738,Human FKBP12 protein,159656,27739
NCBI,AAP36774.1,,159656,27739
BMRB,16942,"Solution NMR Structure () from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518",159679,27741
BMRB,27493,"1H, and 15N Chemical Shift Titration Study of Copper Binding Lipoprotein (bsCopL) using Cu(II).",159679,27741
PDB,2KY9,"Solution NMR Structure of ydhK C-terminal Domain from B.subtilis, Northeast Structural Genomics Consortium Target SR518",159679,27741
BMRB,27743,hSmad2-beta MH1 domain,159702,27742
BMRB,27742,hSmad2 MH1 domain,159718,27743
BMRB,27751,G335N TDP-43_267-414 Monomer,159784,27750
BMRB,27750,G335A TDP-43_267-414 Monomer,159800,27751
BMRB,27754,CdiA-CT MHI813 Cys21Ser Cys27Ser cytoplasm entry domain monomer,159838,27753
BMRB,27755,CdiA-CT MHI813 Cys49Ser Cys56Ser cytoplasm entry domain monomer,159838,27753
NCBI,WP_001383049.1,CdiA from Escherichia coli MHI813,159838,27753
BMRB,27753,CdiA-CT MHI813 cytoplasm entry domain monomer,159853,27754
BMRB,27755,CdiA-CT MHI813 Cys49Ser Cys56Ser cytoplasm entry domain monomer,159853,27754
NCBI,WP_001383049.1,CdiA from Escherichia coli MHI813,159853,27754
BMRB,27753,CdiA-CT MHI813 cytoplasm entry domain monomer,159868,27755
BMRB,27754,CdiA-CT MHI813 Cys21Ser Cys27Ser cytoplasm entry domain monomer,159868,27755
NCBI,WP_001383049.1,CdiA from Escherichia coli MHI813,159868,27755
PDB,6QB2,Structure of SQT-1N monomer. Release of structure held until publication,159904,27757
BMRB,27183,"1H, 15N, 13C backbone resonance assignment of the C-terminal domain of Enzyme I from Thermoanaerobacter tengcongensis",159952,27762
BMRB,27764,Phosphorylated FoxM1 TAD,159968,27763
BMRB,27763,FoxM1 TAD,159984,27764
BMRB,27882,Different Receiver domain (Rec2) of the same ShkA kinase protein of Caulobacter crescentus,160017,27768
BMRB,27770,GA-branchsite-containing RNA duplex with pseudouridine-modified U2 snRNA site,160031,27769
BMRB,27769,GA-branchsite-containing RNA duplex with unmodified U2 snRNA site,160051,27770
BMRB,27772,Solanum tuberosum Plant Specific Insert at pH 2.0,160071,27771
PDB,3RFI,Crystal structure of the dimeric form of this protein,160071,27771
BMRB,27771,Solanum tuberosum Plant Specific Insert at pH 7.0,160086,27772
PDB,3RFI,Crystal structure of the dimeric form of this protein,160086,27772
PDB,6QEY,,160159,27777
BMRB,27752,"Entry containing NMR data for a congener peptide, cyclosporin B.",160190,27779
BMRB,27785,first and second CUE domains from chromatin remodeler SMARCAD1,160212,27780
BMRB,11055,NMR structure of Grb2 SH2 domain complexed with the inhibitor,160231,27781
PDB,1BM2,Complex With Cyclo-[n-Alpha-Acetyl-L-Thi Alysyl-O-Phosphotyrosyl-Valyl-Asparagyl-Valyl-Prolyl] (Pkf273-791),160231,27781
PDB,1BMB,Complex With KpfyVnvef,160231,27781
PDB,1FHS,The three-dimensional solution structure of the Src homology domain-2 of the growth factor receptor-bound protein-2 in pH 5.3,160231,27781
PDB,1FYR,Crystal structure complex with AC-PYVNV,160231,27781
PDB,1JYQ,Complexed with mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor,160231,27781
PDB,1JYR,Complexed with a Phosphorylated Peptide,160231,27781
PDB,1JYU,Complexed with PSpYVNVQN,160231,27781
PDB,1QG1,complexed with a Shc-derived phosphotyrosine (pTyr)-containing peptide,160231,27781
PDB,1TZE,Complexed with KFPPYVNC-NH2,160231,27781
PDB,1ZFP,Complexed with the inhibitor 2-Abz-EpYINQ-NH2,160231,27781
PDB,2AOA,Complexed with a potent non-phosphorus-containing macrocyclic peptide mimetic,160231,27781
PDB,2H46,Complexed with AcNH-pTyr-Val-Asn-NH(2),160231,27781
PDB,2H5K,Complexed with Ac-NH-pTyr-Val-Asn-NH2,160231,27781
PDB,2HUW,Complexed with cyclopropane-derived ligand,160231,27781
PDB,3C7I,Complexed with FPTVN,160231,27781
PDB,3IMD,Complexed with Ac-pY-Q-N-NH2,160231,27781
PDB,3IMJ,Complexed with Ac-pTyr-Ile-Asn-NH2,160231,27781
PDB,3IN7,Complexed with Ac-pY-Q-N-NH2,160231,27781
PDB,3KFJ,Complexed with Ac-pY-E-N-NH2,160231,27781
PDB,3MXC,Complexed with AICD peptide,160231,27781
PDB,3N7Y,Complexed with 20-Membered Macrocyclic Ligand Having the Sequence pYVNV,160231,27781
PDB,3N84,Complexed with a 23-Membered Macrocyclic Ligand Having the Sequence pYVNVP,160231,27781
PDB,3N8M,Complexed with pYVNVP,160231,27781
PDB,3OV1,Complexed with a pYXN-Derived Tripeptide,160231,27781
PDB,3S8L,Complexed with Ac-pTyr-Xaa-Asn,160231,27781
PDB,3WA4,Complexed with CD28-derived peptide,160231,27781
BMRB,27784,the Pfr state of monomeric PAS-GAF-PHY,160265,27783
BMRB,27783,the Pr state of monomeric PAS-GAF-PHY,160279,27784
BMRB,27780,N-terminal extended region and first CUE domain from chromatin remodeler SMARCAD1,160293,27785
BMRB,27791,Complex between RNF168-RING domain and Dm. histone H2A/H2B dimer (H2A isotope labeled),160311,27786
BMRB,27792,Complex between RNF168-RING domain and Dm. histone H2A/H2B dimer (H2B isotope labeled),160311,27786
BMRB,27789,G335S TDP-43_267-414,160357,27788
BMRB,27790,G335A TDP-43_267-414,160357,27788
BMRB,27788,G335N TDP-43_267-414,160373,27789
BMRB,27790,G335A TDP-43_267-414,160373,27789
BMRB,27788,G335N TDP-43_267-414,160389,27790
BMRB,27789,G335S TDP-43_267-414,160389,27790
BMRB,27786,Complex between RNF168-RING domain and Dm. nucleosome (H2A and H2B isotope labeled),160405,27791
BMRB,27792,Complex between RNF168-RING domain and Dm. histone H2A/H2B dimer (H2B isotope labeled),160405,27791
BMRB,27786,Complex between RNF168-RING domain and Dm. nucleosome (H2A and H2B isotope labeled),160429,27792
BMRB,27791,Complex between RNF168-RING domain and Dm. histone H2A/H2B dimer (H2A isotope labeled),160429,27792
BMRB,27162,NMR resonance assignments of the EVH1-domain of Neurofibromin's recruitment factor Spred1,160447,27793
BMRB,25661,GTP binding aptamers 9-12 and class II derive from same SELEX procedure,160461,27794
PDB,5LWJ,GTP binding aptamers 9-12 and class II derive from same SELEX procedure,160461,27794
BMRB,18857,alpha-synuclein at different pH and temperature,160510,27796
BMRB,27797,alpha-synuclein homogeneously modified with CEL,160510,27796
BMRB,6968,intrinsically disordered alpha-synuclein,160510,27796
PDB,6FLT,Structure of alpha-synuclein fibrils,160510,27796
BMRB,18857,alpha-synuclein at different pH and temperature,160526,27797
BMRB,27796,native alpha-synuclein,160526,27797
BMRB,6968,intrinsically disordered alpha-synuclein,160526,27797
PDB,6FLT,Structure of alpha-synuclein fibrils,160526,27797
BMRB,17437,"1H, 13C and 15N backbone chemical shift assignments of the UBC domain of Ube2S WT",160543,27798
BMRB,27799,"1H, 13C and 15N backbone chemical shift assignments of an Ube2S-ubiquitin -conjugate",160543,27798
PDB,1zdn,Crystall structure of the UBC domain of the Ubiquitin-conjugating enzyme E2S WT,160543,27798
BMRB,17437,"1H, 13C and 15N backbone chemical shift assignments of the UBC domain of Ube2S WT",160557,27799
BMRB,27798,"1H, 13C and 15N backbone chemical shift assignments of a mutated variant of UBE2S",160557,27799
PDB,1zdn,Crystall structure of the UBC domain of the Ubiquitin-conjugating enzyme E2S WT,160557,27799
BMRB,27752,"Spectroscopic data about a congener peptide, cyclosporin B.",160572,27800
BMRB,27779,"Spectroscopic data about a congener peptide, cyclosporin D.",160572,27800
BMRB,27994,RCAN1 residues 89-197,160594,27801
BMRB,27995,phosphorylated RCAN1 residues 89-197,160594,27801
BMRB,27996,calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164,160594,27801
BMRB,27997,RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348,160594,27801
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160610,27802
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160610,27802
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160610,27802
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160610,27802
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160610,27802
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160610,27802
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160610,27802
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160610,27802
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160624,27803
BMRB,6968,NMR assignments of alpha-synuclein,162027,27901
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160624,27803
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160624,27803
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160624,27803
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160624,27803
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160624,27803
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160624,27803
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160624,27803
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160638,27804
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160638,27804
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160638,27804
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160638,27804
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160638,27804
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160638,27804
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160638,27804
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160638,27804
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160652,27805
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160652,27805
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160652,27805
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160652,27805
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160652,27805
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160652,27805
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160652,27805
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160652,27805
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160666,27806
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160666,27806
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160666,27806
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160666,27806
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160666,27806
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160666,27806
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160666,27806
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160666,27806
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160680,27807
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160680,27807
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160680,27807
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160680,27807
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160680,27807
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160680,27807
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160680,27807
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160680,27807
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160694,27808
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160694,27808
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160694,27808
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160694,27808
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160694,27808
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160694,27808
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160694,27808
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160694,27808
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160708,27809
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160708,27809
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160708,27809
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160708,27809
EMBL,CAG33339,,162027,27901
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160708,27809
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160708,27809
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160708,27809
BMRB,27810,Backbone 1H and 15N Chemical Shift Assignments for K63-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160708,27809
BMRB,27802,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin including propargyl acrylate linker,160722,27810
BMRB,27803,Backbone 1H and 15N Chemical Shift Assignments for K11C mutant of ubiquitin,160722,27810
BMRB,27804,Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160722,27810
BMRB,27805,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin including propargyl acrylate linker,160722,27810
BMRB,27806,Backbone 1H and 15N Chemical Shift Assignments for K27C mutant of ubiquitin,160722,27810
BMRB,27807,Backbone 1H and 15N Chemical Shift Assignments for K27-linked ubiquitin dimer artificially conjugated via propargyl acrylate,160722,27810
BMRB,27808,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin including propargyl acrylate linker,160722,27810
BMRB,27809,Backbone 1H and 15N Chemical Shift Assignments for K63C mutant of ubiquitin,160722,27810
BMRB,26755,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for the intrinsically disordered NHE1 distal tail",160750,27812
BMRB,27815,Human IMP3 KH1-2 amide chemical shifts,160768,27813
BMRB,27816,Human IMP3 KH1-2 delta2 amide chemical shifts,160768,27813
BMRB,27827,Human IMP3 KH1-2 delta 1 amide chemical shifts,160768,27813
BMRB,27817,Assignments of ITSN1 SH3AD20,160784,27814
BMRB,27818,Assignments of ITSN1 L-SH3A,160784,27814
BMRB,27819,Assignments of ITSN1 SH3A-L,160784,27814
BMRB,27820,Assignments of ITSN1 L-SH3AD20,160784,27814
BMRB,27821,Assignments of ITSN1 SH3AD20-L,160784,27814
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160784,27814
BMRB,27813,Amide chemical shifts of human IMP3 RRM1-2 (1-156),160800,27815
BMRB,27816,Human IMP3 KH1-2 delta2 amide chemical shifts,160800,27815
BMRB,27827,Human IMP3 KH1-2 delta 1 amide chemical shifts,160800,27815
BMRB,27813,Amide chemical shifts of human IMP3 RRM1-2 (1-156),160817,27816
BMRB,27815,Human IMP3 KH1-2 amide chemical shifts,160817,27816
BMRB,27827,Human IMP3 KH1-2 delta 1 amide chemical shifts,160817,27816
BMRB,27814,Assignments of both isoforms of ITSN1 SH3A,160835,27817
BMRB,27818,Assignments of ITSN1 L-SH3A,160835,27817
BMRB,27819,Assignments of ITSN1 SH3A-L,160835,27817
BMRB,27820,Assignments of ITSN1 L-SH3AD20,160835,27817
BMRB,27821,Assignments of ITSN1 SH3AD20-L,160835,27817
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160835,27817
BMRB,27814,Assignments of both isoforms of ITSN1 SH3A,160850,27818
BMRB,27817,Assignments of ITSN1 SH3AD20,160850,27818
BMRB,27819,Assignments of ITSN1 SH3A-L,160850,27818
BMRB,27820,Assignments of ITSN1 L-SH3AD20,160850,27818
BMRB,27821,Assignments of ITSN1 SH3AD20-L,160850,27818
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160850,27818
BMRB,27814,Assignments of both isoforms of ITSN1 SH3A,160865,27819
BMRB,27817,Assignments of ITSN1 SH3AD20,160865,27819
BMRB,27818,Assignments of ITSN1 L-SH3A,160865,27819
BMRB,27820,Assignments of ITSN1 L-SH3AD20,160865,27819
BMRB,27821,Assignments of ITSN1 SH3AD20-L,160865,27819
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160865,27819
BMRB,27814,Assignments of both isoforms of ITSN1 SH3A,160880,27820
BMRB,27817,Assignments of ITSN1 SH3AD20,160880,27820
BMRB,27818,Assignments of ITSN1 L-SH3A,160880,27820
BMRB,27819,Assignments of ITSN1 SH3A-L,160880,27820
BMRB,27821,Assignments of ITSN1 SH3AD20-L,160880,27820
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160880,27820
BMRB,27814,Assignments of both isoforms of ITSN1 SH3A,160895,27821
BMRB,27817,Assignments of ITSN1 SH3AD20,160895,27821
BMRB,27818,Assignments of ITSN1 L-SH3A,160895,27821
BMRB,27819,Assignments of ITSN1 SH3A-L,160895,27821
BMRB,27820,Assignments of ITSN1 L-SH3AD20,160895,27821
PDB,6H5T,Crystal Structure of the Assigned Domain construct from the same publication,160895,27821
BMRB,27826,Backbone chemical shift assignments of RNase H domain bound to YLC2-155,160910,27825
BMRB,27825,Backbone chemical shift assignments of RNase H domain bound to ZW566,160931,27826
BMRB,27813,Amide chemical shifts of human IMP3 RRM1-2 (1-156),160953,27827
BMRB,27815,Human IMP3 KH1-2 amide chemical shifts,160953,27827
BMRB,27816,Human IMP3 KH1-2 delta2 amide chemical shifts,160953,27827
BMRB,27829,complex between d(CGATATCG)2 and C-1305,160971,27828
BMRB,27828,d(CGATATCG)2; free form,160985,27829
BMRB,27833,tEIN backbone and resonance assignment,161036,27832
BMRB,27832,Methyl Chemical shift Assignment of EIC from the thermophile thermoanaerobacter tengcongenesis,161050,27833
BMRB,27841,human T686A and flip variant form of GluR2-LBD complexed with glutamate,161155,27840
BMRB,27842,human T686S and flip variant form of GluR2-LBD complexed with glutamate,161155,27840
BMRB,27843,human flip variant form of GluR2-LBD complexed with kainate,161155,27840
BMRB,5182,rat flop variant form of GluR2-LBD complexed with glutamate,161155,27840
PDB,1FTJ,rat flop variant form of GluR2-LBD complexed with glutamate,161155,27840
PDB,2UXA,rat flip variant form of GluR2-LBD complexed with glutamate,161155,27840
PDB,3DP6,rat flop variant form of GluR2-LBD complexed with glutamate,161155,27840
BMRB,27840,human flip variant form of GluR2-LBD complexed with glutamate,161173,27841
BMRB,27842,human T686S and flip variant form of GluR2-LBD complexed with glutamate,161173,27841
BMRB,27843,human flip variant form of GluR2-LBD complexed with kainate,161173,27841
PDB,3B6Q,rat T686A and flop variant form of GluR2-LBD complexed with glutamate,161173,27841
BMRB,27840,human flip variant form of GluR2-LBD complexed with glutamate,161191,27842
BMRB,27841,human T686A and flip variant form of GluR2-LBD complexed with glutamate,161191,27842
BMRB,27843,human flip variant form of GluR2-LBD complexed with kainate,161191,27842
PDB,3B6W,rat T686S and flop variant form of GluR2-LBD complexed with glutamate,161191,27842
BMRB,15496,rat flop variant form of GluR2-LBD complexed with kainate,161211,27843
BMRB,27840,human flip variant form of GluR2-LBD complexed with glutamate,161211,27843
BMRB,27841,human T686A and flip variant form of GluR2-LBD complexed with glutamate,161211,27843
BMRB,27842,human T686S and flip variant form of GluR2-LBD complexed with glutamate,161211,27843
PDB,1FTK,rat flop variant form of GluR2-LBD complexed with kainate,161211,27843
PDB,1FW0,rat flop variant form of GluR2-LBD complexed with kainate,161211,27843
PDB,1GR2,rat flop variant form of GluR2-LBD complexed with kainate,161211,27843
PDB,2Z5E,Entry providing structure for this molecular system.,161231,27844
BMRB,27317,Solid-state NMR of HBV core protein at 17.5 kHz MAS,161247,27845
PDB,1QGT,X-ray structure of HBV capsid,161247,27845
BMRB,27853,c-di-GMP bound PilF159-302,161338,27852
BMRB,27852,apo tate PilF159-302,161354,27853
BMRB,27865,"calredoxin, with calcium ions",161454,27860
BMRB,25334,Entry containing chemical shift assignments for this molecular system.,161468,27861
BMRB,27863,peptide EVNPPVP,161484,27862
BMRB,27864,peptide EVNAPVP,161484,27862
BMRB,27862,peptide EVNPAVP,161499,27863
BMRB,27864,peptide EVNAPVP,161499,27863
BMRB,27862,peptide EVNPAVP,161514,27864
BMRB,27863,peptide EVNPPVP,161514,27864
BMRB,27860,"calredoxin, apo form",161529,27865
BMRB,27874,"D38A AcpP, titrated with 0.00, 0.50, 1.00, 1.50, and 2.00 equivalents of FabB",161625,27872
PDB,5KOF,Crystal structure of AcpP crosslinked to FabB,161625,27872
BMRB,27872,"wt AcpP, titrated with 0.00, 0.50, 1.00, 1.50, and 2.00 equivalents of FabB",161675,27874
PDB,5KOF,Crystal structure of AcpP crosslinked to FabB,161675,27874
BMRB,27768,Different Receiver domain (Rec1) of the same ShkA kinase protein of Caulobacter crescentus,161828,27882
BMRB,27884,HMGA1a S64C mutant phosphorylated by Casein Kinase 2,161844,27883
BMRB,27883,HMGA1a S64C mutant,161860,27884
BMRB,26672,Assignments for the low complexity prion-like domain of Fused in Sarcoma (FUS 1-163),161892,27887
BMRB,27125,FUS low complexity domain with 12 phosphomimetic S/T to E mutations,161892,27887
BMRB,27067,Wildtype protein with 6xHis purifiation tag,161909,27888
BMRB,27889,BlaC variant G132N,161909,27888
BMRB,27890,BlaC in bound to clavulanic acid,161909,27888
BMRB,27891,BlaC variant K234R,161909,27888
BMRB,27067,Wildtype protein with 6xHis purifiation tag,161936,27890
BMRB,27888,BlaC in free form,161936,27890
BMRB,27889,BlaC variant G132N,161936,27890
BMRB,27891,BlaC variant K234R,161936,27890
BMRB,5362,Native form of the fragment,161961,27893
PDB,1L1C,Structure of the RNA binding domain,161961,27893
BMRB,16300,Unfolded state of alpha synuclein,162011,27900
BMRB,16342,Alpha synuclein at pH 3,162011,27900
BMRB,16939,WT-alpha synuclein,162011,27900
BMRB,17649,Partially assignment of alpha synuclein,162011,27900
BMRB,17665,Human alpha synuclein,162011,27900
BMRB,17910,alpha synuclein in vesicles,162011,27900
BMRB,18857,NMR assignments of alpha-synuclein at different pHs,162011,27900
BMRB,18860,Solid state assignment of alpha synuclein,162011,27900
BMRB,19257,alpha synuclein assignment in E. Coli cells,162011,27900
BMRB,19337,Alpha synuclein in PBS,162011,27900
BMRB,25227,"assignment of alpha synuclein, monomeric state",162011,27900
BMRB,27901,Human DDP1P2 Alpha-Synuclein,162011,27900
BMRB,6968,NMR assignments of alpha-synuclein,162011,27900
EMBL,CAG33339,,162011,27900
EMBL,CAG46454,,162011,27900
GB,AAA16117,,162011,27900
GB,AAC02114,,162011,27900
GB,AAG30302,,162011,27900
GB,AAH13293,,162011,27900
GB,AAI08276,,162011,27900
PDB,1XQ8,,162011,27900
PDB,2KKW,,162011,27900
REF,NP_000336,,162011,27900
REF,NP_001009158,,162011,27900
REF,NP_001032222,,162011,27900
REF,NP_001129014,,162011,27900
REF,NP_001139526,,162011,27900
SP,P37840,,162011,27900
SP,P61139,,162011,27900
SP,P61140,,162011,27900
SP,P61142,,162011,27900
SP,P61143,,162011,27900
BMRB,16300,Unfolded state of alpha synuclein,162027,27901
BMRB,16342,Alpha synuclein at pH 3,162027,27901
BMRB,16939,WT-alpha synuclein,162027,27901
BMRB,17649,Partially assignment of alpha synuclein,162027,27901
BMRB,17665,Human alpha synuclein,162027,27901
BMRB,17910,alpha synuclein in vesicles,162027,27901
BMRB,18857,NMR assignments of alpha-synuclein at different pHs,162027,27901
BMRB,18860,Solid state assignment of alpha synuclein,162027,27901
BMRB,19257,alpha synuclein assignment in E. Coli cells,162027,27901
BMRB,19337,Alpha synuclein in PBS,162027,27901
BMRB,25227,"assignment of alpha synuclein, monomeric state",162027,27901
BMRB,27900,Human alpha-Synuclein (wt),162027,27901
EMBL,CAG46454,,162027,27901
GB,AAA16117,,162027,27901
GB,AAC02114,,162027,27901
GB,AAG30302,,162027,27901
GB,AAH13293,,162027,27901
GB,AAI08276,,162027,27901
PDB,1XQ8,,162027,27901
PDB,2KKW,,162027,27901
REF,NP_000336,,162027,27901
REF,NP_001009158,,162027,27901
REF,NP_001032222,,162027,27901
REF,NP_001129014,,162027,27901
REF,NP_001139526,,162027,27901
SP,P37840,,162027,27901
SP,P61139,,162027,27901
SP,P61140,,162027,27901
SP,P61142,,162027,27901
SP,P61143,,162027,27901
BMRB,27905,Clr4 1-191 NCP,162043,27903
BMRB,27903,Clr4 1-191 free,162073,27905
BMRB,27912,ARPP19,162087,27911
BMRB,27911,ARPP16,162102,27912
BMRB,27916,p50 heterodimer,162150,27915
BMRB,27915,p50 homodimer,162174,27916
BMRB,7235,Backbone NMR assignments of wild-type beta-phosphoglucomutase,162212,27920
PDB,2WHE,X-ray crystal structure of wild-type beta-phosphoglucomutase,162212,27920
BMRB,27923,scAtg3FR(86-159),162229,27922
BMRB,27924,scAtg8,162229,27922
BMRB,27922,Atg3,162246,27923
BMRB,27924,scAtg8,162246,27923
BMRB,27922,Atg3,162261,27924
BMRB,27923,scAtg3FR(86-159),162261,27924
BMRB,27927,Polypeptide chain (RTNLB13 18-mer),162292,27926
BMRB,27928,Polypeptide chain (R13-APH22 22-mer),162292,27926
BMRB,27926,Polypeptide chain (RTN13 16-mer),162309,27927
BMRB,27928,Polypeptide chain (R13-APH22 22-mer),162309,27927
BMRB,27926,Polypeptide chain (RTNLB13 18-mer),162326,27928
BMRB,27927,Polypeptide chain (R13-APH22 22-mer),162326,27928
BMRB,27067,Wildtype protein with 6xHis purifiation tag,162343,27929
BMRB,27888,BlaC in free form,162343,27929
BMRB,27889,BlaC variant G132N,162343,27929
BMRB,27890,BlaC bound to clavulanic acid,162343,27929
BMRB,27891,BlaC variant K234R,162343,27929
BMRB,27932,FUS (371-526) (Folded),162384,27931
BMRB,27931,FUS (371-526) (Unfolded),162398,27932
PDB,6ROL,Structure of IMP2 KH34 domains,162414,27934
BMRB,27947,oxidized (cysteine sulfinic acid 106) human DJ-1,162449,27943
BMRB,27948,bL12 dimer (with LBT tag),162465,27944
BMRB,27946,RA-bound CRABP2 monomer,162479,27945
BMRB,27945,CRABP2 monomer,162493,27946
BMRB,27943,reduced (cysteine sulfinic acid 106) human DJ-1,162509,27947
BMRB,27944,bL12 dimer,162526,27948
BMRB,27953,PFE0055c,162589,27952
PDB,6RZY,,162589,27952
BMRB,27952,PFA0660w,162605,27953
BMRB,26999,Adenylate kinase wild type Apo form,162621,27954
BMRB,27000,Adenylate kinase R119A mutant Apo form,162621,27954
BMRB,27001,Adenylate kinase R119K mutant Apo form,162621,27954
BMRB,27004,Adenylate kinase wild type bound to Ap5A,162621,27954
BMRB,27005,Adenylate kinase wild type bound to ATP,162621,27954
BMRB,27006,Adenylate kinase wild type bound to AMP,162621,27954
BMRB,27007,Adenylate kinase R119A mutant bound to Ap5A,162621,27954
BMRB,27008,Adenylate kinase R119A mutant bound to ATP,162621,27954
BMRB,27009,Adenylate kinase R119A mutant bound to AMP,162621,27954
BMRB,27010,Adenylate kinase R119K mutant bound to Ap5A,162621,27954
BMRB,27956,MR complex [Rad50 NBD (L828F) with unlabeled Mre11],162639,27955
BMRB,27957,MR complex [Rad50 NBD (D829N) with unlabeled Mre11],162639,27955
BMRB,27955,MR complex [Rad50 NBD (wild type) with unlabeled Mre11],162655,27956
BMRB,27957,MR complex [Rad50 NBD (D829N) with unlabeled Mre11],162655,27956
BMRB,27955,MR complex [Rad50 NBD (L828F) with unlabeled Mre11],162671,27957
BMRB,27956,MR complex [Rad50 NBD (D829N) with unlabeled Mre11],162671,27957
BMRB,27965,Cor a 1.0401,162741,27961
BMRB,27967,Cor a 1.0403,162741,27961
BMRB,28016,Cor a 1.0404,162741,27961
BMRB,16635,N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase,162774,27963
BMRB,16912,Delta subunit of RNA polymerase from Bacillus subtilis,162774,27963
BMRB,18903,Relaxation study of Delta subunit of RNA polymerase from Bacillus subtilis,162774,27963
BMRB,19284,Relaxation data of the delta subunit of RNA polymerase from Bacillus subtilis,162774,27963
BMRB,27245,Backbone 15N relaxation data for c-teminal domain of delta subunit of RNA polymerase from bacillus subtilis,162774,27963
BMRB,27964,Delta subunit of RNA polymerase from Bacillus subtilis with mutated lisine strecht to glutamic acid,162774,27963
BMRB,16635,N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase,162789,27964
BMRB,16912,Delta subunit of RNA polymerase from Bacillus subtilis,162789,27964
BMRB,18903,Relaxation study of Delta subunit of RNA polymerase from Bacillus subtilis,162789,27964
BMRB,19284,Relaxation data of the delta subunit of RNA polymerase from Bacillus subtilis,162789,27964
BMRB,27245,Backbone 15N relaxation data for c-teminal domain of delta subunit of RNA polymerase from bacillus subtilis,162789,27964
BMRB,27963,RDC of Delta subunit of RNA polymerase from Bacillus subtilis,162789,27964
BMRB,27961,Cor a 1.0402,162808,27965
BMRB,27967,Cor a 1.0403,162808,27965
BMRB,28016,Cor a 1.0404,162808,27965
BMRB,27961,Cor a 1.0402,162823,27967
BMRB,27965,Cor a 1.0401,162823,27967
BMRB,28016,Cor a 1.0404,162823,27967
BMRB,17937,Solid-state chemical shift assignments for CAP-Gly domain,162838,27968
BMRB,17938,Solution chemical shift assignments for CAP-Gly domain (p150Glued 19-107),162838,27968
BMRB,19025,Solid-state chemical shift assignments for CAP-Gly Domain at 19.9 T,162838,27968
BMRB,19031,Solid-state NMR assignments of CAP-Gly with EB1,162838,27968
BMRB,25005,MAS Structure of CAP-Gly Domain in complex with microtubules,162838,27968
BMRB,27973,Solid-state NMR Chemical Shift Assignments for p150Glued(1-191) of Dynactin,162838,27968
PDB,2COY,,162838,27968
PDB,2M02,,162838,27968
PDB,2MPX,,162838,27968
BMRB,27970,mIL-2/JES6-1 complex,162853,27969
BMRB,27971,mIL-2/IL-2Ralpha,162853,27969
BMRB,27974,R52A mutant,162853,27969
BMRB,27969,mIL-2 monomeric,162868,27970
BMRB,27971,mIL-2/IL-2Ralpha,162868,27970
BMRB,27974,R52A mutant,162868,27970
BMRB,27969,mIL-2 monomeric,162882,27971
BMRB,27970,mIL-2/JES6-1 complex,162882,27971
BMRB,27974,R52A mutant,162882,27971
BMRB,17937,Solid-state chemical shift assignments for CAP-Gly domain,162910,27973
BMRB,17938,Solution chemical shift assignments for CAP-Gly domain (p150Glued 19-107),162910,27973
BMRB,19025,Solid-state chemical shift assignments for CAP-Gly Domain at 19.9 T,162910,27973
BMRB,25005,MAS Structure of CAP-Gly Domain in complex with microtubules,162910,27973
BMRB,27968,Solution NMR Backbone Resonance Assignments for p150Glued(1-191) of Dynactin,162910,27973
PDB,2COY,Solution structure of the CAP-Gly domain in human Dynactin 1,162910,27973
PDB,2M02,3D structure of cap-gly domain of mammalian dynactin determined by magic angle spinning NMR spectroscopy,162910,27973
PDB,2MPX,Three-dimensional structure of CAP-GLY DOMAIN ASSEMBLED ON MICROTUBULES DETERMINED BY MAS NMR SPECTROSCOPY,162910,27973
BMRB,27969,mIL-2 monomeric,162928,27974
BMRB,27970,mIL-2/JES6-1 complex,162928,27974
BMRB,27971,mIL-2/IL-2Ralpha,162928,27974
BMRB,27976,Mouse Lemur Biliverdin B bound to NADP,162943,27975
BMRB,27975,Mouse Lemur BLVRB monomer,162958,27976
PDB,6SAP,Solution structure of the PUB domain of human UBXD1 protein,162975,27977
BMRB,4757,"1H, 13C, 15N Chemical Shift Assignment for the UBA(2) Domain of HHR23A",162995,27978
BMRB,27982,Ca2+ depleted form 1,163059,27981
BMRB,27983,Ca2+ depleted form 2,163059,27981
PDB,6PW7,X-ray crystal structure of C. elegans STIM EF-SAM domain,163059,27981
BMRB,27981,Ca2+ loaded monomer,163079,27982
BMRB,27983,Ca2+ depleted form 2,163079,27982
PDB,6PW7,X-ray crystal structure of C. elegans STIM EF-SAM domain,163079,27982
BMRB,27981,Ca2+ loaded monomer,163099,27983
BMRB,27982,Ca2+ depleted form 1,163099,27983
PDB,6PW7,X-ray crystal structure of C. elegans STIM EF-SAM domain,163099,27983
NCBI,BC145869.1,Mus musculus chemokine (C-C motif) ligand 2,163134,27986
BMRB,27993,MYB29 residues 118-178,163233,27992
BMRB,27992,MYB28 residues 116-197,163249,27993
BMRB,27995,phosphorylated RCAN1 residues 89-197,163265,27994
BMRB,27996,calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164,163265,27994
BMRB,27997,RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348,163265,27994
BMRB,27994,RCAN1 residues 89-197,163280,27995
BMRB,27996,calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164,163280,27995
BMRB,27997,RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348,163280,27995
BMRB,27994,RCAN1 residues 89-197,163297,27996
BMRB,27995,phosphorylated RCAN1 residues 89-197,163297,27996
BMRB,27997,RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348,163297,27996
BMRB,27994,RCAN1 residues 89-197,163313,27997
BMRB,27995,phosphorylated RCAN1 residues 89-197,163313,27997
BMRB,27996,calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164,163313,27997
BMRB,27999,Sis1 SBD,163332,27998
BMRB,28000,Ydj1 SBD,163332,27998
BMRB,28001,CbpA SBD,163332,27998
BMRB,27998,DnaJB1 SBD,163347,27999
BMRB,28000,Ydj1 SBD,163347,27999
BMRB,28001,CbpA SBD,163347,27999
BMRB,27998,DnaJB1 SBD,163375,28000
BMRB,27999,Sis1 SBD,163375,28000
BMRB,28001,CbpA SBD,163375,28000
BMRB,27998,DnaJB1 SBD,163390,28001
BMRB,27999,Sis1 SBD,163390,28001
BMRB,28000,Ydj1 SBD,163390,28001
BMRB,28003,Human Mitochondrial Ferredoxin FDX2,163405,28002
BMRB,28002,Human Mitochondrial Ferredoxin FDX1,163422,28003
BMRB,28006,MapZcyto-WT monomer,163441,28005
BMRB,28005,MapZcyto-2TE monomer,163456,28006
BMRB,27961,Cor a 1.0402,163528,28016
BMRB,27965,Cor a 1.0401,163528,28016
BMRB,27967,Cor a 1.0403,163528,28016
BMRB,28011,Human Mdm2(aa284-434),163560,28019
BMRB,28011,non-modified human Mdm2(aa284-434),163593,28020
BMRB,28026,human TNPO1 328-381,163648,28025
BMRB,28027,human CIRBP 38-137,163648,28025
BMRB,28025,human CIRBP 138-172,163662,28026
BMRB,28027,human CIRBP 38-137,163662,28026
BMRB,28025,human CIRBP 138-172,163676,28027
BMRB,28026,human TNPO1 328-381,163676,28027
PDB,4X06,Crystal structure corresponding to the protein here assigned,163706,28030
BMRB,25645,HSPB1 ACD,163764,28034
BMRB,26994,Proline isomerization in the C-terminal region of HSP27,163764,28034
BMRB,27046,oxidized alpha-crystallin domain of HSP27 (HSPB1),163764,28034
BMRB,27681,HSPB1 containing residues 1-176,163764,28034
PDB,2N3J,,163764,28034
PDB,4MJH,,163764,28034
PDB,6GJH,,163764,28034
BMRB,28038,FKBP12 protein from the pathogenic fungi Candida auris,163812,28037
BMRB,28037,FKBP12 protein from the pathogenic fungi Candida glabrata,163829,28038
BMRB,28128,Methionine sulfone-containing peptide,164491,28126
BMRB,16342,"Backbone 1H, 13C, 15N and 13C-beta Chemical Shift Assignments for alpha-synuclein at pH 3",163885,28045
BMRB,16939,WT alpha-synuclein fibrils,163885,28045
BMRB,17665,human alpha synuclein construct,163885,28045
BMRB,19257,"1H, 13C, and 15N chemical shift assignments for alpha-synuclein in living E. coli cells",163885,28045
BMRB,19353,Structure of alpha-synuclein in complex with an engineered binding protein,163885,28045
BMRB,25227,"1H, 13C, and 15N chemical shift assignments for alpha-synuclein monomer (WT)",163885,28045
BMRB,25535,Conformational space of alpha-synuclein fibrils. Data from solid-state NMR assignment of a high-pH polymorph,163885,28045
BMRB,27074,1H and 15N Chemical Shift Assignments for wild-type alpha-synuclein,163885,28045
BMRB,27348,"C', CA, N and HN assignment of alpha-synuclein near-phsysiological conditions",163885,28045
BMRB,27900,"HN, N, CA and CB chemical shift assignments for alpha-synuclein monomer (WT). Low pH",163885,28045
BMRB,27901,"HN, N, CA and CB chemical shift assignments for alpha-synuclein monomer (DP1P2). Low pH",163885,28045
PDB,2n0a,Atomic-resolution structure of alpha-synuclein fibrils,163885,28045
BMRB,28047,RalA.GDP,163908,28046
BMRB,28046,RalA.GMPPNP,163927,28047
BMRB,28051,Rad50-Mre11 (L828A mutant),163958,28049
BMRB,28049,Rad50-Mre11 (D829A mutant),163993,28051
BMRB,50125,VDAC E73V assignment in DHPC7 micelles,164027,28053
BMRB,28057,"holo form of the solute binding protein PiuA, with Ga(III) 4-LICAM",164056,28056
PDB,4JCC,Crystal structure of a close homolog,164056,28056
BMRB,28056,apo form of the solute binding protein PiuA,164072,28057
PDB,4JCC,Crystal structure of a close homolog,164072,28057
PDB,6SJW,NMR data for the structure. Should be released in the same time.,164092,28058
BMRB,27779,1H and 13C assignment of cyclosporin D in chloroform,164171,28066
BMRB,28087,dUnr Cterminal Q-rich,164207,28086
BMRB,28088,dUnr CSD456,164207,28086
BMRB,28089,dUnr CSD6,164207,28086
BMRB,28086,Unr CSD789,164223,28088
BMRB,28087,dUnr Cterminal Q-rich,164223,28088
BMRB,28089,dUnr CSD6,164223,28088
PDB,6FRR,"crystal structure of the same protein, same construct",164239,28092
PDB,6W3M,,164256,28094
BMRB,28096,binary complex; bPGM-Mg; with trans K145-P146 peptide bond,164271,28095
BMRB,28097,transition state analogue complex; bPGM-P146A-Mg-MgF3-G6P TSA,164271,28095
BMRB,7235,Backbone NMR assignments of wild-type substrate-free beta-phosphoglucomutase with a cis K145-P146 peptide bond,164271,28095
PDB,2WHE,X-ray crystal structure of wild-type beta-phosphoglucomutase (containing a cis K145-P146 peptide bond),164271,28095
BMRB,28095,binary complex; bPGM-Mg; with cis K145-P146 peptide bond,164288,28096
BMRB,28097,transition state analogue complex; bPGM-P146A-Mg-MgF3-G6P TSA,164288,28096
BMRB,7235,Backbone NMR assignments of wild-type substrate-free beta-phosphoglucomutase with a cis K145-P146 peptide bond,164288,28096
PDB,2WHE,X-ray crystal structure of wild-type beta-phosphoglucomutase (containing cis K145-P146 peptide bond),164288,28096
BMRB,27920,Backbone resonance assignments of the P146A variant of beta-phosphoglucomutase in its substrate-free form,164305,28097
BMRB,28095,binary complex; bPGM-Mg; with cis K145-P146 peptide bond,164305,28097
BMRB,28096,binary complex; bPGM-Mg; with trans K145-P146 peptide bond,164305,28097
BMRB,7234,Backbone resonance assignments of wild-type beta-phosphoglucomutase in a transition state analogue complex with glucose 6-phosphate and trifluoromagnesate,164305,28097
PDB,2WF5,X-ray crystal structure of wild-type beta-phosphoglucomutase in a transition state analogue complex with glucose 6-phosphate and trifluoromagnesate,164305,28097
BMRB,28108,Entry containing the HLA-A*02:01 / human beta-2 microglobulin (in complex with the chaperone TAPBPR),164345,28107
BMRB,28107,Entry containing the TAX9/ ILVproS HLA-A*02:01 / human beta-2 microglobulin (no in complex with the chaperone TAPBPR),164362,28108
BMRB,18696,revmodN,164394,28113
BMRB,28124,5-Hydroxytryptophan-containing peptide,164429,28123
BMRB,28125,Kynurenine-containing peptide,164429,28123
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164429,28123
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164429,28123
BMRB,28128,Methionine sulfone-containing peptide,164429,28123
BMRB,28129,N-formylkynurenine-containing peptide,164429,28123
BMRB,28130,Oxindolylalanine-containing peptide,164429,28123
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164451,28124
BMRB,28125,Kynurenine-containing peptide,164451,28124
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164451,28124
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164451,28124
BMRB,28128,Methionine sulfone-containing peptide,164451,28124
BMRB,28129,N-formylkynurenine-containing peptide,164451,28124
BMRB,28130,Oxindolylalanine-containing peptide,164451,28124
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164471,28125
BMRB,28124,5-Hydroxytryptophan-containing peptide,164471,28125
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164471,28125
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164471,28125
BMRB,28128,Methionine sulfone-containing peptide,164471,28125
BMRB,28129,N-formylkynurenine-containing peptide,164471,28125
BMRB,28130,Oxindolylalanine-containing peptide,164471,28125
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164491,28126
BMRB,28124,5-Hydroxytryptophan-containing peptide,164491,28126
BMRB,28125,Kynurenine-containing peptide,164491,28126
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164491,28126
BMRB,28129,N-formylkynurenine-containing peptide,164491,28126
BMRB,28130,Oxindolylalanine-containing peptide,164491,28126
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164513,28127
BMRB,28124,5-Hydroxytryptophan-containing peptide,164513,28127
BMRB,28125,Kynurenine-containing peptide,164513,28127
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164513,28127
BMRB,28128,Methionine sulfone-containing peptide,164513,28127
BMRB,28129,N-formylkynurenine-containing peptide,164513,28127
BMRB,28130,Oxindolylalanine-containing peptide,164513,28127
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164535,28128
BMRB,28124,5-Hydroxytryptophan-containing peptide,164535,28128
BMRB,28125,Kynurenine-containing peptide,164535,28128
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164535,28128
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164535,28128
BMRB,28129,N-formylkynurenine-containing peptide,164535,28128
BMRB,28130,Oxindolylalanine-containing peptide,164535,28128
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164555,28129
BMRB,28124,5-Hydroxytryptophan-containing peptide,164555,28129
BMRB,28125,Kynurenine-containing peptide,164555,28129
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164555,28129
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164555,28129
BMRB,28128,Methionine sulfone-containing peptide,164555,28129
BMRB,28130,Oxindolylalanine-containing peptide,164555,28129
BMRB,28123,Methionine sulfoxide-containing peptide (with Gly as succeeding residue),164576,28130
BMRB,28124,5-Hydroxytryptophan-containing peptide,164576,28130
BMRB,28125,Kynurenine-containing peptide,164576,28130
BMRB,28126,Methionine sulfoxide-containing peptide (with Ala as succeeding residue),164576,28130
BMRB,28127,Methionine sulfoxide-containing peptide (with Pro as succeeding residue),164576,28130
BMRB,28128,Methionine sulfone-containing peptide,164576,28130
BMRB,28129,N-formylkynurenine-containing peptide,164576,28130
BMRB,28138,Rabies Phosphoprotein RavP C terminus (140-297),164630,28137
BMRB,28137,Rabies Phosphoprotein RavP (1-152),164644,28138
PDB,5GAJ,BMRB Entry Tracking System,165228,30000
BMRB,30003,Solution Structure of TAZ2-p53TAD,165248,30002
BMRB,30004,Solution Structure of TAZ2-p53AD2,165248,30002
PDB,5HOU,BMRB Entry Tracking System,165248,30002
BMRB,30002,Solution Structure of p53TAD-TAZ1,165274,30003
BMRB,30004,Solution Structure of TAZ2-p53TAD,165274,30003
PDB,5HP0,BMRB Entry Tracking System,165274,30003
BMRB,30002,Solution Structure of p53TAD-TAZ1,165299,30004
BMRB,30003,Solution Structure of TAZ2-p53AD2,165299,30004
PDB,5HPD,BMRB Entry Tracking System,165299,30004
PDB,5HUZ,BMRB Entry Tracking System,165327,30005
PDB,5HV8,BMRB Entry Tracking System,165347,30006
PDB,5HVC,BMRB Entry Tracking System,165365,30007
PDB,5I1R,BMRB Entry Tracking System,165381,30008
BMRB,30011,W7A mutant of mu-TRTX-Pre1a,165400,30009
PDB,5I1X,BMRB Entry Tracking System,165400,30009
PDB,5I22,BMRB Entry Tracking System,165420,30010
BMRB,30009,F8A mutant of beta-TRTX-Pre1a,165438,30011
PDB,5I2P,BMRB Entry Tracking System,165438,30011
PDB,5I2V,BMRB Entry Tracking System,165458,30012
BMRB,30022,porcine lactoferricin,165480,30013
PDB,5I4G,BMRB Entry Tracking System,165480,30013
PDB,5HQF,BMRB Entry Tracking System,165497,30015
PDB,5HQQ,BMRB Entry Tracking System,165516,30016
PDB,5I8N,BMRB Entry Tracking System,165534,30017
PDB,5IAY,BMRB Entry Tracking System,165551,30019
PDB,5IAZ,BMRB Entry Tracking System,165572,30020
PDB,5ID3,BMRB Entry Tracking System,165596,30021
BMRB,30013,porcinelactoferricin in TFE,165619,30022
PDB,5ID5,BMRB Entry Tracking System,165619,30022
BMRB,30025,BeF3-activated conformation of SdrG from Pseudomonas melonis Fr1,165636,30023
PDB,5IEB,BMRB Entry Tracking System,165636,30023
PDB,5IEC,BMRB Entry Tracking System,165654,30024
BMRB,30023,SdrG from Sphingomonas melonis Fr1,165671,30025
PDB,5IEJ,BMRB Entry Tracking System,165671,30025
PDB,5IEM,BMRB Entry Tracking System,165689,30026
BMRB,30028,GCN4p pH 4.4,165710,30027
BMRB,30029,GCN4p pH 1.5,165710,30027
PDB,5IEW,BMRB Entry Tracking System,165710,30027
BMRB,30027,GCN4p pH 6.6,165727,30028
BMRB,30029,GCN4p pH 1.5,165727,30028
PDB,5IIR,BMRB Entry Tracking System,165727,30028
BMRB,30027,GCN4p pH 6.6,165746,30029
BMRB,30028,GCN4p pH 4.4,165746,30029
PDB,5IIV,BMRB Entry Tracking System,165746,30029
PDB,5IJ4,BMRB Entry Tracking System,165765,30030
PDB,5IM8,BMRB Entry Tracking System,165787,30031
PDB,5ION,BMRB Entry Tracking System,165802,30032
PDB,5IPO,BMRB Entry Tracking System,165822,30033
PDB,5IRD,BMRB Entry Tracking System,165843,30034
PDB,5IRT,BMRB Entry Tracking System,165868,30035
PDB,6HT4,BMRB Entry Tracking System,165889,30037
BMRB,30044,DNA Dodecamer with 8-oxoguanine at 10th Position,165906,30038
PDB,5IV1,BMRB Entry Tracking System,165906,30038
PDB,5IX5,BMRB Entry Tracking System,165929,30039
PDB,5IX9,BMRB Entry Tracking System,165948,30040
PDB,5IZB,BMRB Entry Tracking System,165966,30042
PDB,5IQ5,BMRB Entry Tracking System,165988,30043
BMRB,30038,DNA Dodecamer with 8-oxoguanine at 4th Position,166020,30044
PDB,5IZP,BMRB Entry Tracking System,166020,30044
BMRB,30055,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTTGG),166045,30045
BMRB,30056,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTGG),166045,30045
BMRB,30058,DIY G-Quadruplexes: d(GGGGTTTGGGGTTTTGGGGAAGGGG),166045,30045
PDB,5J05,BMRB Entry Tracking System,166045,30045
BMRB,30049,Excited state (Bound-like): HIV-1 TAR complexed with cyclic peptide mimetic of Tat,166061,30046
BMRB,30051,Intermediate state lying on the pathway of release of Tat from HIV-1 TAR,166061,30046
PDB,5J0M,BMRB Entry Tracking System,166061,30046
PDB,5J17,BMRB Entry Tracking System,166079,30047
BMRB,30050,Ras Binding Domain (RBD) of B-Raf,166098,30048
PDB,5J18,BMRB Entry Tracking System,166098,30048
BMRB,30046,Ground state: HIV-1 TAR complexed with cyclic peptide mimetic of Tat,166116,30049
BMRB,30051,Intermediate state lying on the pathway of release of Tat from HIV-1 TAR,166116,30049
PDB,5J1O,BMRB Entry Tracking System,166116,30049
BMRB,30048,Ras Binding Domain (RBD) of B-Raf complexed with Rigosertib (Complex I),166133,30050
PDB,5J2R,BMRB Entry Tracking System,166133,30050
BMRB,30046,Ground state: HIV-1 TAR complexed with cyclic peptide mimetic of Tat,166151,30051
BMRB,30049,Excited state (Bound-like): HIV-1 TAR complexed with cyclic peptide mimetic of Tat,166151,30051
PDB,5J2W,BMRB Entry Tracking System,166151,30051
BMRB,30053,PT-free dsDNA from Streptomyces lividans,166168,30052
BMRB,30054,"[Sp, Sp]-PT dsDNA",166168,30052
PDB,5J3F,BMRB Entry Tracking System,166168,30052
BMRB,30052,"[Rp, Rp]-PT dsDNA",166188,30053
BMRB,30054,"[Sp, Sp]-PT dsDNA",166188,30053
PDB,5J3G,BMRB Entry Tracking System,166188,30053
BMRB,30052,"[Rp, Rp]-PT dsDNA",166208,30054
BMRB,30053,PT-free dsDNA from Streptomyces lividans,166208,30054
PDB,5J3I,BMRB Entry Tracking System,166208,30054
BMRB,30045,DIY G-Quadruplexes: d(GGGTTTGGGTTTTGGGAGGG),166228,30055
BMRB,30056,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTGG),166228,30055
BMRB,30058,DIY G-Quadruplexes: d(GGGGTTTGGGGTTTTGGGGAAGGGG),166228,30055
PDB,5J4P,BMRB Entry Tracking System,166228,30055
BMRB,30045,DIY G-Quadruplexes: d(GGGTTTGGGTTTTGGGAGGG),166244,30056
BMRB,30055,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTTGG),166244,30056
BMRB,30058,DIY G-Quadruplexes: d(GGGGTTTGGGGTTTTGGGGAAGGGG),166244,30056
PDB,5J4W,BMRB Entry Tracking System,166244,30056
BMRB,30059,hylin-a1 analogs: Hylin-D,166259,30057
BMRB,30060,hylin-a1 analogs: Hylin-K,166259,30057
PDB,5J6T,BMRB Entry Tracking System,166259,30057
BMRB,30045,DIY G-Quadruplexes: d(GGGTTTGGGTTTTGGGAGGG),166276,30058
BMRB,30055,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTTGG),166276,30058
BMRB,30056,DIY G-Quadruplexes: d(GGTTTGGTTTTGGTTGG),166276,30058
PDB,5J6U,BMRB Entry Tracking System,166276,30058
BMRB,30057,hylin-a1 analogs: Hylin-Ac,166292,30059
BMRB,30060,hylin-a1 analogs: Hylin-K,166292,30059
PDB,5J6V,BMRB Entry Tracking System,166292,30059
BMRB,30057,hylin-a1 analogs: Hylin-Ac,166308,30060
BMRB,30059,hylin-a1 analogs: Hylin-D,166308,30060
PDB,5J6W,BMRB Entry Tracking System,166308,30060
PDB,5J6Z,BMRB Entry Tracking System,166324,30061
PDB,5J7J,BMRB Entry Tracking System,166344,30062
PDB,5J8H,BMRB Entry Tracking System,166364,30063
PDB,5J8T,BMRB Entry Tracking System,166397,30064
PDB,5JDP,BMRB Entry Tracking System,166419,30065
PDB,5JDX,BMRB Entry Tracking System,166443,30066
BMRB,30069,de novo miniprotein EEHE_02,166461,30067
PDB,5JHI,BMRB Entry Tracking System,166461,30067
PDB,5JHJ,BMRB Entry Tracking System,166484,30068
BMRB,30067,de novo miniprotein EHE_06,166500,30069
PDB,5JI4,BMRB Entry Tracking System,166500,30069
PDB,5JN6,BMRB Entry Tracking System,166522,30070
BMRB,30072,Calcium-free EF-hand domain of L-plastin,166537,30071
PDB,5JOJ,BMRB Entry Tracking System,166537,30071
BMRB,30071,Calcium-loaded EF-hand domain of L-plastin,166557,30072
PDB,5JOL,BMRB Entry Tracking System,166557,30072
PDB,5JPL,BMRB Entry Tracking System,166575,30073
PDB,5JPW,BMRB Entry Tracking System,166593,30074
PDB,5JPX,BMRB Entry Tracking System,166612,30075
PDB,5JR0,BMRB Entry Tracking System,166635,30076
BMRB,30078,Structural Model of a Protein alpha subunit in complex with GDP obtained with SAXS and NMR residual couplings,166654,30077
PDB,5JS7,BMRB Entry Tracking System,166654,30077
BMRB,30077,Structural Model of a apo G-protein alpha subunit determined with NMR residual dipolar couplings and SAXS,166674,30078
PDB,5JS8,BMRB Entry Tracking System,166674,30078
PDB,5JTK,BMRB Entry Tracking System,166692,30079
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166713,30080
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166713,30080
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166713,30080
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166713,30080
BMRB,30085,SecB in complex with unstructured MBP binding site d,166713,30080
BMRB,30086,SecB in complex with unstructured MBP binding site e,166713,30080
PDB,5JTL,BMRB Entry Tracking System,166713,30080
BMRB,30080,SecB in complex with unstructured proPhoA,166736,30081
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166736,30081
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166736,30081
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166736,30081
BMRB,30085,SecB in complex with unstructured MBP binding site d,166736,30081
BMRB,30086,SecB in complex with unstructured MBP binding site e,166736,30081
PDB,5JTM,BMRB Entry Tracking System,166736,30081
BMRB,30080,SecB in complex with unstructured proPhoA,166762,30082
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166762,30082
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166762,30082
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166762,30082
BMRB,30085,SecB in complex with unstructured MBP binding site d,166762,30082
BMRB,30086,SecB in complex with unstructured MBP binding site e,166762,30082
PDB,5JTN,BMRB Entry Tracking System,166762,30082
BMRB,30080,SecB in complex with unstructured proPhoA,166786,30083
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166786,30083
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166786,30083
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166786,30083
BMRB,30085,SecB in complex with unstructured MBP binding site d,166786,30083
BMRB,30086,SecB in complex with unstructured MBP binding site e,166786,30083
PDB,5JTO,BMRB Entry Tracking System,166786,30083
BMRB,30080,SecB in complex with unstructured proPhoA,166812,30084
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166812,30084
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166812,30084
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166812,30084
BMRB,30085,SecB in complex with unstructured MBP binding site d,166812,30084
BMRB,30086,SecB in complex with unstructured MBP binding site e,166812,30084
PDB,5JTP,BMRB Entry Tracking System,166812,30084
BMRB,30080,SecB in complex with unstructured proPhoA,166838,30085
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166838,30085
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166838,30085
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166838,30085
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166838,30085
BMRB,30086,SecB in complex with unstructured MBP binding site e,166838,30085
PDB,5JTQ,BMRB Entry Tracking System,166838,30085
BMRB,30080,SecB in complex with unstructured proPhoA,166862,30086
BMRB,30081,SecB in complex with unstructured PhoA binding site a,166862,30086
BMRB,30082,SecB in complex with unstructured proPhoA binding site c,166862,30086
BMRB,30083,SecB in complex with unstructured proPhoA binding site d,166862,30086
BMRB,30084,SecB in complex with unstructured proPhoA binding site e,166862,30086
BMRB,30085,SecB in complex with unstructured MBP binding site d,166862,30086
PDB,5JTR,BMRB Entry Tracking System,166862,30086
PDB,5JWJ,BMRB Entry Tracking System,166888,30087
PDB,5JXV,BMRB Entry Tracking System,166907,30088
PDB,5JYH,BMRB Entry Tracking System,166926,30089
PDB,5JYN,BMRB Entry Tracking System,166944,30090
BMRB,30092,pseudo receiver domain of CikA,166967,30091
BMRB,30093,Circadian clock protein KaiB in complex with pseudo receiver domain of CikA,166967,30091
PDB,5JYT,BMRB Entry Tracking System,166967,30091
BMRB,30091,Circadian clock protein KaiB,166990,30092
BMRB,30093,Circadian clock protein KaiB in complex with pseudo receiver domain of CikA,166990,30092
PDB,5JYU,BMRB Entry Tracking System,166990,30092
BMRB,30091,Circadian clock protein KaiB,167013,30093
BMRB,30092,pseudo receiver domain of CikA,167013,30093
PDB,5JYV,BMRB Entry Tracking System,167013,30093
PDB,5JZR,BMRB Entry Tracking System,167059,30094
PDB,5K57,BMRB Entry Tracking System,167077,30097
PDB,5K5F,BMRB Entry Tracking System,167095,30098
PDB,5K5G,BMRB Entry Tracking System,167117,30099
PDB,5K6P,BMRB Entry Tracking System,167151,30100
PDB,5KBO,BMRB Entry Tracking System,167175,30101
PDB,5KES,BMRB Entry Tracking System,167200,30102
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167221,30105
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167221,30105
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167221,30105
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167221,30105
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167221,30105
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167221,30105
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167221,30105
PDB,5KGV,BMRB Entry Tracking System,167221,30105
BMRB,30107,Phenol-soluble modulin Beta2,167243,30106
PDB,5KGY,BMRB Entry Tracking System,167243,30106
BMRB,30106,Phenol-soluble modulin Alpha 3,167262,30107
PDB,5KGZ,BMRB Entry Tracking System,167262,30107
PDB,5KH8,BMRB Entry Tracking System,167280,30108
PDB,5KHB,BMRB Entry Tracking System,167304,30109
PDB,5KI0,BMRB Entry Tracking System,167323,30110
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167339,30111
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167339,30111
BMRB,30123,Connexin 32 G12R N-Terminal Mutant,167530,30120
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167339,30111
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167339,30111
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167339,30111
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167339,30111
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167339,30111
PDB,5KI4,BMRB Entry Tracking System,167339,30111
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167361,30112
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167361,30112
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167361,30112
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167361,30112
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167361,30112
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167361,30112
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167361,30112
PDB,5KI5,BMRB Entry Tracking System,167361,30112
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167383,30113
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167383,30113
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167383,30113
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167383,30113
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167383,30113
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167383,30113
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167383,30113
PDB,5KI7,BMRB Entry Tracking System,167383,30113
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167405,30114
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167405,30114
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167405,30114
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167405,30114
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167405,30114
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167405,30114
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167405,30114
PDB,5KIB,BMRB Entry Tracking System,167405,30114
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167427,30115
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167427,30115
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167427,30115
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167427,30115
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167427,30115
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167427,30115
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167427,30115
PDB,5KIE,BMRB Entry Tracking System,167427,30115
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167449,30116
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167449,30116
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167449,30116
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167449,30116
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167449,30116
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167449,30116
BMRB,30117,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167449,30116
PDB,5KIF,BMRB Entry Tracking System,167449,30116
BMRB,30105,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167471,30117
BMRB,30111,"DNA (5'-D(*AP*TP*CP*CP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167471,30117
BMRB,30112,"DNA (5'-D(*TP*TP*AP*GP*GP*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167471,30117
BMRB,30113,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167471,30117
BMRB,30114,"DNA/RNA (5'-D(*TP*TP*AP*G)-R(P*G)-D(P*CP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*GP*CP*CP*TP*AP*A)-3')",167471,30117
BMRB,30115,"DNA/RNA (5'-D(*AP*TP*GP*GP*A)-R(P*G)-D(P*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*CP*CP*AP*T)-3')",167471,30117
BMRB,30116,"DNA/RNA (5'-D(*AP*TP*CP*C)-R(P*G)-D(P*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*CP*GP*GP*AP*T)-3')",167471,30117
PDB,5KIH,BMRB Entry Tracking System,167471,30117
PDB,5KIZ,BMRB Entry Tracking System,167493,30118
BMRB,30120,Connexin 26 G12R mutant,167511,30119
BMRB,30123,Connexin 32 G12R N-Terminal Mutant,167511,30119
PDB,5KJ3,BMRB Entry Tracking System,167511,30119
BMRB,30119,Connexin 26 WT peptide,167530,30120
PDB,5KJG,BMRB Entry Tracking System,167530,30120
PDB,5KK3,BMRB Entry Tracking System,167548,30121
BMRB,30119,Connexin 26 WT peptide,167571,30123
BMRB,30120,Connexin 26 G12R mutant,167571,30123
PDB,5KK9,BMRB Entry Tracking System,167571,30123
PDB,5KKM,BMRB Entry Tracking System,167590,30124
PDB,5KNW,BMRB Entry Tracking System,167606,30126
PDB,5KP0,BMRB Entry Tracking System,167629,30127
PDB,5KPE,BMRB Entry Tracking System,167651,30128
PDB,5KPH,BMRB Entry Tracking System,167672,30129
BMRB,30131,Peptidase M23 in complex with two ZN ions,167693,30130
PDB,5KQB,BMRB Entry Tracking System,167693,30130
BMRB,30130,Peptidase M23 in complex with one ZN ion,167712,30131
PDB,5KQC,BMRB Entry Tracking System,167712,30131
PDB,5KQE,BMRB Entry Tracking System,167731,30132
BMRB,30122,Solution Structure of Antibiotic-Resistance Factor ANT(2'')-Ia Reveals Substrate-Regulated Conformation Dynamics,167754,30133
PDB,5KQJ,BMRB Entry Tracking System,167754,30133
PDB,5KRW,BMRB Entry Tracking System,167774,30134
PDB,5KS5,BMRB Entry Tracking System,167800,30135
PDB,5KS6,BMRB Entry Tracking System,167826,30136
PDB,5KTF,BMRB Entry Tracking System,167849,30137
BMRB,30140,Designed Peptide NC_EHE_D1,167868,30138
BMRB,30141,Designed Peptide NC_EEH_D2,167868,30138
BMRB,30142,Designed Peptide NC_EEH_D1,167868,30138
BMRB,30143,Designed Peptide NC_cHH_D1,167868,30138
BMRB,30144,Designed Peptide NC_cHh_DL_D1,167868,30138
BMRB,30145,Designed Peptide NC_cHHH_D1,167868,30138
BMRB,30146,Designed Peptide NC_cEE_D1,167868,30138
PDB,5KVN,BMRB Entry Tracking System,167868,30138
PDB,5KVP,BMRB Entry Tracking System,167887,30139
BMRB,30138,Designed Peptide NC_HEE_D1,167915,30140
BMRB,30141,Designed Peptide NC_EEH_D2,167915,30140
BMRB,30142,Designed Peptide NC_EEH_D1,167915,30140
BMRB,30143,Designed Peptide NC_cHH_D1,167915,30140
BMRB,30144,Designed Peptide NC_cHh_DL_D1,167915,30140
BMRB,30145,Designed Peptide NC_cHHH_D1,167915,30140
BMRB,30146,Designed Peptide NC_cEE_D1,167915,30140
PDB,5KWO,BMRB Entry Tracking System,167915,30140
BMRB,30138,Designed Peptide NC_HEE_D1,167935,30141
BMRB,30140,Designed Peptide NC_EHE_D1,167935,30141
BMRB,30142,Designed Peptide NC_EEH_D1,167935,30141
BMRB,30143,Designed Peptide NC_cHH_D1,167935,30141
BMRB,30144,Designed Peptide NC_cHh_DL_D1,167935,30141
BMRB,30145,Designed Peptide NC_cHHH_D1,167935,30141
BMRB,30146,Designed Peptide NC_cEE_D1,167935,30141
PDB,5KWP,BMRB Entry Tracking System,167935,30141
BMRB,30138,Designed Peptide NC_HEE_D1,167956,30142
BMRB,30140,Designed Peptide NC_EHE_D1,167956,30142
BMRB,30141,Designed Peptide NC_EEH_D2,167956,30142
BMRB,30143,Designed Peptide NC_cHH_D1,167956,30142
BMRB,30144,Designed Peptide NC_cHh_DL_D1,167956,30142
BMRB,30145,Designed Peptide NC_cHHH_D1,167956,30142
BMRB,30146,Designed Peptide NC_cEE_D1,167956,30142
PDB,5KWX,BMRB Entry Tracking System,167956,30142
BMRB,30138,Designed Peptide NC_HEE_D1,167975,30143
BMRB,30140,Designed Peptide NC_EHE_D1,167975,30143
BMRB,30141,Designed Peptide NC_EEH_D2,167975,30143
BMRB,30142,Designed Peptide NC_EEH_D1,167975,30143
BMRB,30144,Designed Peptide NC_cHh_DL_D1,167975,30143
BMRB,30145,Designed Peptide NC_cHHH_D1,167975,30143
BMRB,30146,Designed Peptide NC_cEE_D1,167975,30143
PDB,5KWZ,BMRB Entry Tracking System,167975,30143
BMRB,30138,Designed Peptide NC_HEE_D1,167993,30144
BMRB,30140,Designed Peptide NC_EHE_D1,167993,30144
BMRB,30141,Designed Peptide NC_EEH_D2,167993,30144
BMRB,30142,Designed Peptide NC_EEH_D1,167993,30144
BMRB,30143,Designed Peptide NC_cHH_D1,167993,30144
BMRB,30145,Designed Peptide NC_cHHH_D1,167993,30144
BMRB,30146,Designed Peptide NC_cEE_D1,167993,30144
PDB,5KX0,BMRB Entry Tracking System,167993,30144
BMRB,30138,Designed Peptide NC_HEE_D1,168018,30145
BMRB,30140,Designed Peptide NC_EHE_D1,168018,30145
BMRB,30141,Designed Peptide NC_EEH_D2,168018,30145
BMRB,30142,Designed Peptide NC_EEH_D1,168018,30145
BMRB,30143,Designed Peptide NC_cHH_D1,168018,30145
BMRB,30144,Designed Peptide NC_cHh_DL_D1,168018,30145
BMRB,30146,Designed Peptide NC_cEE_D1,168018,30145
PDB,5KX1,BMRB Entry Tracking System,168018,30145
BMRB,30138,Designed Peptide NC_HEE_D1,168036,30146
BMRB,30140,Designed Peptide NC_EHE_D1,168036,30146
BMRB,30141,Designed Peptide NC_EEH_D2,168036,30146
BMRB,30142,Designed Peptide NC_EEH_D1,168036,30146
BMRB,30143,Designed Peptide NC_cHH_D1,168036,30146
BMRB,30144,Designed Peptide NC_cHh_DL_D1,168036,30146
BMRB,30145,Designed Peptide NC_cHHH_D1,168036,30146
PDB,5KX2,BMRB Entry Tracking System,168036,30146
PDB,5KZO,BMRB Entry Tracking System,168055,30147
BMRB,30151,DNA Dodecamer with 5-methylcytosine at the 9th Position,168074,30148
PDB,5L06,BMRB Entry Tracking System,168074,30148
PDB,5L1C,BMRB Entry Tracking System,168095,30149
PDB,5L1Y,original pdb entry,168116,30150
PDB,6BF2,revised coordinates pdb entry,168116,30150
BMRB,30148,DNA Dodecamer with 5-methylcytosine at the 3rd Position,168140,30151
PDB,5L2G,BMRB Entry Tracking System,168140,30151
PDB,5L34,BMRB Entry Tracking System,168162,30152
PDB,5SXY,BMRB Entry Tracking System,168184,30153
PDB,5SYQ,BMRB Entry Tracking System,168206,30154
PDB,5SZW,BMRB Entry Tracking System,168223,30155
PDB,5T0X,BMRB Entry Tracking System,168243,30156
PDB,5T17,BMRB Entry Tracking System,168263,30157
BMRB,30159,NPr (1-85) in complex with EIN-Ntr (170-424),168281,30158
PDB,5T1N,BMRB Entry Tracking System,168281,30158
BMRB,30158,"NPr (1-85), apo form",168309,30159
PDB,5T1O,BMRB Entry Tracking System,168309,30159
PDB,5T3M,BMRB Entry Tracking System,168342,30160
PDB,5T3Y,BMRB Entry Tracking System,168361,30161
PDB,5T42,BMRB Entry Tracking System,168381,30162
PDB,5T43,BMRB Entry Tracking System,168403,30163
PDB,5T4R,BMRB Entry Tracking System,168419,30164
PDB,5T56,BMRB Entry Tracking System,168437,30165
BMRB,30168,Initial Topology of the globular isomer of PnID,168454,30167
PDB,5T6T,BMRB Entry Tracking System,168454,30167
BMRB,30167,Reverse topology of the globular isoform of PnID,168471,30168
PDB,5T6V,BMRB Entry Tracking System,168471,30168
PDB,5T7Q,BMRB Entry Tracking System,168488,30170
PDB,5T82,BMRB Entry Tracking System,168503,30171
PDB,5T8A,BMRB Entry Tracking System,168518,30172
PDB,5TBG,BMRB Entry Tracking System,168536,30176
PDB,5TBN,BMRB Entry Tracking System,168554,30177
BMRB,30179,Magnesium-bound Conantokin-R1B Mutant,168582,30178
PDB,5TBQ,BMRB Entry Tracking System,168582,30178
BMRB,30178,Magnesium-bound Conantokin-R1B Mutant,168600,30179
PDB,5TBR,BMRB Entry Tracking System,168600,30179
PDB,5TCE,BMRB Entry Tracking System,168619,30180
PDB,5TCZ,BMRB Entry Tracking System,168637,30181
PDB,5TGG,BMRB Entry Tracking System,168655,30184
PDB,5TGW,BMRB Entry Tracking System,168678,30185
PDB,5TGY,BMRB Entry Tracking System,168700,30186
BMRB,30188,"Benenodin-1-dC5, state 2",168723,30188
PDB,5TJ1,BMRB Entry Tracking System,168723,30188
PDB,5TLQ,BMRB Entry Tracking System,168739,30189
PDB,5TLR,BMRB Entry Tracking System,168758,30190
PDB,6ALT,BMRB Entry Tracking System,168782,30191
BMRB,30193,Solution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis,168802,30192
BMRB,30194,Solution Structure of the C-terminal multimerization domain of the master biofilm-regulator SinR from Bacillus subtilis,168802,30192
PDB,5TMX,BMRB Entry Tracking System,168802,30192
BMRB,30192,"Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus subtilis",168821,30193
BMRB,30194,Solution Structure of the C-terminal multimerization domain of the master biofilm-regulator SinR from Bacillus subtilis,168821,30193
PDB,5TN0,BMRB Entry Tracking System,168821,30193
BMRB,30192,"Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus subtilis",168840,30194
BMRB,30193,Solution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis,168840,30194
PDB,5TN2,BMRB Entry Tracking System,168840,30194
BMRB,30196,Solution structure of the CaM34 with the iNOS CaM binding domain peptide,168859,30195
PDB,5TP5,BMRB Entry Tracking System,168859,30195
BMRB,30195,Solution structure of the calcium deficient mutant calmodulin CaM1234,168874,30196
PDB,5TP6,BMRB Entry Tracking System,168874,30196
PDB,5TR5,BMRB Entry Tracking System,168890,30197
PDB,5TRN,BMRB Entry Tracking System,168912,30198
PDB,5TTB,BMRB Entry Tracking System,168935,30199
PDB,5TTT,BMRB Entry Tracking System,168969,30200
PDB,5TVZ,BMRB Entry Tracking System,168988,30201
BMRB,30203,Cyclic peptide AAA(UN1)ARAARAARA(NH2),169011,30202
PDB,5TWI,BMRB Entry Tracking System,169011,30202
BMRB,30202,Cyclic peptide ARA(UN1)(NH2),169029,30203
PDB,5TWW,BMRB Entry Tracking System,169029,30203
PDB,5TX8,BMRB Entry Tracking System,169046,30204
PDB,5U3H,BMRB Entry Tracking System,169069,30205
PDB,5U5S,BMRB Entry Tracking System,169088,30206
BMRB,30208,Solution structure of the zinc fingers 3 and 4 of MBNL1,169114,30207
BMRB,30210,Solution structure of the zinc fingers 1 and 2 of MBNL1 in complex with human cardiac troponin T pre-mRNA,169114,30207
PDB,5U6H,BMRB Entry Tracking System,169114,30207
BMRB,30207,Solution structure of the zinc fingers 1 and 2 of MBNL1,169137,30208
BMRB,30210,Solution structure of the zinc fingers 1 and 2 of MBNL1 in complex with human cardiac troponin T pre-mRNA,169137,30208
PDB,5U6L,BMRB Entry Tracking System,169137,30208
PDB,5U87,BMRB Entry Tracking System,169160,30209
BMRB,30207,Solution structure of the zinc fingers 1 and 2 of MBNL1,169177,30210
BMRB,30208,Solution structure of the zinc fingers 3 and 4 of MBNL1,169177,30210
PDB,5U9B,BMRB Entry Tracking System,169177,30210
PDB,5U9Q,BMRB Entry Tracking System,169201,30211
BMRB,30211,Ocellatin LB1,169221,30212
BMRB,30213,Ocellatin F1,169221,30212
BMRB,30214,Ocellatin LB1,169221,30212
BMRB,30215,Ocellatin-LB2,169221,30212
BMRB,30216,Ocellatin K1 (26),169221,30212
BMRB,30217,Ocellatin LB1,169221,30212
BMRB,30218,Ocellatin LB2,169221,30212
BMRB,30219,Ocellatin F1,169221,30212
PDB,5U9R,BMRB Entry Tracking System,169221,30212
BMRB,30211,Ocellatin LB1,169241,30213
BMRB,30212,Ocellatin LB2,169241,30213
BMRB,30214,Ocellatin LB1,169241,30213
BMRB,30215,Ocellatin-LB2,169241,30213
BMRB,30216,Ocellatin K1 (26),169241,30213
BMRB,30217,Ocellatin LB1,169241,30213
BMRB,30218,Ocellatin LB2,169241,30213
BMRB,30219,Ocellatin F1,169241,30213
PDB,5U9S,BMRB Entry Tracking System,169241,30213
BMRB,30211,Ocellatin LB1,169261,30214
BMRB,30212,Ocellatin LB2,169261,30214
BMRB,30213,Ocellatin F1,169261,30214
BMRB,30215,Ocellatin-LB2,169261,30214
BMRB,30216,Ocellatin K1 (26),169261,30214
BMRB,30217,Ocellatin LB1,169261,30214
BMRB,30218,Ocellatin LB2,169261,30214
BMRB,30219,Ocellatin F1,169261,30214
PDB,5U9V,BMRB Entry Tracking System,169261,30214
BMRB,30211,Ocellatin LB1,169281,30215
BMRB,30212,Ocellatin LB2,169281,30215
BMRB,30213,Ocellatin F1,169281,30215
BMRB,30214,Ocellatin LB1,169281,30215
BMRB,30216,Ocellatin K1 (26),169281,30215
BMRB,30217,Ocellatin LB1,169281,30215
BMRB,30218,Ocellatin LB2,169281,30215
BMRB,30219,Ocellatin F1,169281,30215
PDB,5U9X,BMRB Entry Tracking System,169281,30215
BMRB,30211,Ocellatin LB1,169301,30216
BMRB,30212,Ocellatin LB2,169301,30216
BMRB,30213,Ocellatin F1,169301,30216
BMRB,30214,Ocellatin LB1,169301,30216
BMRB,30215,Ocellatin K1 (24),169301,30216
BMRB,30217,Ocellatin LB1,169301,30216
BMRB,30218,Ocellatin LB2,169301,30216
BMRB,30219,Ocellatin F1,169301,30216
PDB,5U9Y,BMRB Entry Tracking System,169301,30216
BMRB,30211,Ocellatin LB1,169321,30217
BMRB,30212,Ocellatin LB2,169321,30217
BMRB,30213,Ocellatin F1,169321,30217
BMRB,30214,Ocellatin LB1,169321,30217
BMRB,30215,Ocellatin-LB2,169321,30217
BMRB,30216,Ocellatin K1 (26),169321,30217
BMRB,30218,Ocellatin LB2,169321,30217
BMRB,30219,Ocellatin F1,169321,30217
PDB,5UA6,BMRB Entry Tracking System,169321,30217
BMRB,30211,Ocellatin LB1,169341,30218
BMRB,30212,Ocellatin LB2,169341,30218
BMRB,30213,Ocellatin F1,169341,30218
BMRB,30214,Ocellatin LB1,169341,30218
BMRB,30215,Ocellatin-LB2,169341,30218
BMRB,30216,Ocellatin K1 (26),169341,30218
BMRB,30217,Ocellatin LB1,169341,30218
BMRB,30219,Ocellatin F1,169341,30218
PDB,5UA7,BMRB Entry Tracking System,169341,30218
BMRB,30211,Ocellatin LB1,169362,30219
BMRB,30212,Ocellatin LB2,169362,30219
BMRB,30213,Ocellatin F1,169362,30219
BMRB,30214,Ocellatin LB1,169362,30219
BMRB,30215,Ocellatin-LB2,169362,30219
BMRB,30216,Ocellatin K1 (26),169362,30219
BMRB,30217,Ocellatin LB1,169362,30219
BMRB,30218,Ocellatin LB2,169362,30219
PDB,5UA8,BMRB Entry Tracking System,169362,30219
BMRB,30221,NERD-S,169382,30220
BMRB,30222,major species of DANCER-2,169382,30220
BMRB,30223,minor species of DANCER-2,169382,30220
PDB,5UB0,BMRB Entry Tracking System,169382,30220
BMRB,30220,NERD-C,169404,30221
BMRB,30222,major species of DANCER-2,169404,30221
BMRB,30223,minor species of DANCER-2,169404,30221
PDB,5UBS,BMRB Entry Tracking System,169404,30221
BMRB,30220,NERD-C,169428,30222
BMRB,30221,NERD-S,169428,30222
BMRB,30223,minor species of DANCER-2,169428,30222
PDB,5UCE,BMRB Entry Tracking System,169428,30222
BMRB,30220,NERD-C,169450,30223
BMRB,30221,NERD-S,169450,30223
BMRB,30222,major species of DANCER-2,169450,30223
PDB,5UCF,BMRB Entry Tracking System,169450,30223
PDB,5UF3,BMRB Entry Tracking System,169472,30224
BMRB,30226,NMR SOLUTION STRUCTURE OF THE ALPHA-CONOTOXIN GID MUTANT V13Y,169494,30225
PDB,5UG3,BMRB Entry Tracking System,169494,30225
BMRB,30225,NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID MUTANT A10V,169519,30226
PDB,5UG5,BMRB Entry Tracking System,169519,30226
PDB,5UGK,BMRB Entry Tracking System,169545,30227
PDB,5UI6,BMRB Entry Tracking System,169565,30229
PDB,5UI7,BMRB Entry Tracking System,169580,30230
PDB,5UJ5,BMRB Entry Tracking System,169595,30231
BMRB,30233,ov-GRN12-34,169615,30232
PDB,5UJG,BMRB Entry Tracking System,169615,30232
BMRB,30232,ovGRN12-35_3s,169633,30233
PDB,5UJH,BMRB Entry Tracking System,169633,30233
PDB,5UJL,BMRB Entry Tracking System,169651,30234
BMRB,30236,Bacteriocin CbnX,169670,30235
PDB,5UJQ,BMRB Entry Tracking System,169670,30235
BMRB,30235,Bacteriocin CbnY,169686,30236
PDB,5UJR,BMRB Entry Tracking System,169686,30236
PDB,5UKE,BMRB Entry Tracking System,169702,30237
PDB,5UKZ,BMRB Entry Tracking System,169719,30238
PDB,5UNK,BMRB Entry Tracking System,169734,30239
BMRB,30241,de novo mini protein EEHEE_rd3_1049,169753,30240
BMRB,30242,de novo mini protein EHEE_rd1_0284,169753,30240
PDB,5UOI,BMRB Entry Tracking System,169753,30240
BMRB,30240,de novo mini protein HHH_rd1_0142,169770,30241
BMRB,30242,de novo mini protein EHEE_rd1_0284,169770,30241
PDB,5UP1,BMRB Entry Tracking System,169770,30241
BMRB,30240,de novo mini protein HHH_rd1_0142,169788,30242
BMRB,30241,de novo mini protein EEHEE_rd3_1049,169788,30242
PDB,5UP5,BMRB Entry Tracking System,169788,30242
PDB,5URN,BMRB Entry Tracking System,169806,30243
PDB,5US3,BMRB Entry Tracking System,169830,30244
PDB,5US5,BMRB Entry Tracking System,169855,30245
PDB,5UTG,BMRB Entry Tracking System,169876,30246
PDB,5UTV,BMRB Entry Tracking System,169898,30247
PDB,5UY2,BMRB Entry Tracking System,169923,30248
PDB,5UYO,BMRB Entry Tracking System,169941,30249
PDB,5UZ1,BMRB Entry Tracking System,169961,30250
PDB,5UZ2,BMRB Entry Tracking System,169983,30251
PDB,5UZ3,BMRB Entry Tracking System,170005,30252
BMRB,30254,DNA Duplexes containing m1A - A6-DNA structure,170027,30253
BMRB,30255,DNA Duplexes containing m1A - A6-DNAm1A16 structure,170027,30253
PDB,5UZD,BMRB Entry Tracking System,170027,30253
BMRB,30253,DNA Duplexes containing m1A - A2-DNA structure,170050,30254
BMRB,30255,DNA Duplexes containing m1A - A6-DNAm1A16 structure,170050,30254
PDB,5UZF,BMRB Entry Tracking System,170050,30254
BMRB,30253,DNA Duplexes containing m1A - A2-DNA structure,170073,30255
BMRB,30254,DNA Duplexes containing m1A - A6-DNA structure,170073,30255
PDB,5UZI,BMRB Entry Tracking System,170073,30255
PDB,5UZL,BMRB Entry Tracking System,170096,30256
PDB,5UZT,BMRB Entry Tracking System,170112,30257
PDB,5UZZ,BMRB Entry Tracking System,170135,30258
PDB,5V0Y,BMRB Entry Tracking System,170156,30259
PDB,5V11,BMRB Entry Tracking System,170172,30260
PDB,5V16,BMRB Entry Tracking System,170188,30261
PDB,5V17,BMRB Entry Tracking System,170211,30262
PDB,5V1E,BMRB Entry Tracking System,170232,30263
PDB,5V2B,BMRB Entry Tracking System,170254,30265
PDB,5V2G,BMRB Entry Tracking System,170271,30267
PDB,5V2R,BMRB Entry Tracking System,170290,30268
PDB,5V4C,BMRB Entry Tracking System,170312,30270
PDB,5V4U,BMRB Entry Tracking System,170329,30271
PDB,5V7Z,BMRB Entry Tracking System,170347,30273
PDB,5VAV,BMRB Entry Tracking System,170367,30274
PDB,5VEY,BMRB Entry Tracking System,170385,30275
PDB,5VF0,BMRB Entry Tracking System,170408,30276
PDB,5VFW,BMRB Entry Tracking System,170432,30281
PDB,5VH7,BMRB Entry Tracking System,170450,30282
PDB,5VH8,BMRB Entry Tracking System,170475,30283
PDB,5VJ8,BMRB Entry Tracking System,170499,30284
PDB,5VKG,BMRB Entry Tracking System,170516,30285
PDB,5VKV,BMRB Entry Tracking System,170543,30286
PDB,5VL6,BMRB Entry Tracking System,170565,30287
PDB,5VLN,BMRB Entry Tracking System,170582,30288
PDB,5VNT,BMRB Entry Tracking System,170606,30289
PDB,5VO7,BMRB Entry Tracking System,170627,30290
PDB,5VR1,BMRB Entry Tracking System,170645,30291
PDB,5VR5,BMRB Entry Tracking System,170663,30292
PDB,5VSO,BMRB Entry Tracking System,170680,30293
PDB,5VTO,,170710,30295
PDB,5VWE,BMRB Entry Tracking System,170729,30296
PDB,5VWL,BMRB Entry Tracking System,170748,30297
PDB,5VX7,BMRB Entry Tracking System,170767,30298
PDB,5VZM,BMRB Entry Tracking System,170789,30300
PDB,5W0Y,BMRB Entry Tracking System,170814,30301
PDB,5W3G,BMRB Entry Tracking System,170833,30303
PDB,5W3N,BMRB Entry Tracking System,170852,30304
PDB,5W4S,BMRB Entry Tracking System,170876,30305
PDB,5W54,BMRB Entry Tracking System,170906,30306
PDB,5W72,BMRB Entry Tracking System,170923,30307
PDB,5W88,BMRB Entry Tracking System; peptide mode,170943,30308
PDB,5WCL,BMRB Entry Tracking System; solvent exposed mode,170943,30308
PDB,5W8Y,BMRB Entry Tracking System,170966,30309
PDB,5W8Z,BMRB Entry Tracking System,170989,30310
PDB,5W96,BMRB Entry Tracking System,171011,30311
PDB,5W9F,BMRB Entry Tracking System,171027,30312
PDB,5WAH,BMRB Entry Tracking System,171050,30313
PDB,5WBT,BMRB Entry Tracking System,171074,30314
PDB,5WCV,BMRB Entry Tracking System,171090,30315
PDB,5WDZ,BMRB Entry Tracking System,171107,30316
PDB,5WE3,BMRB Entry Tracking System,171126,30317
PDB,5WLX,BMRB Entry Tracking System,171149,30318
PDB,5WOC,BMRB Entry Tracking System,171167,30319
PDB,5WOD,BMRB Entry Tracking System,171199,30320
PDB,5WOE,BMRB Entry Tracking System,171216,30321
PDB,5WOT,BMRB Entry Tracking System,171236,30322
BMRB,30324,Solution NMR structure of cyclotide MCoTI-I,171254,30323
PDB,5WOV,BMRB Entry Tracking System,171254,30323
BMRB,30323,Solution NMR structure of cyclotide MCoTI-I,171273,30324
PDB,5WOW,BMRB Entry Tracking System,171273,30324
PDB,5WOX,BMRB Entry Tracking System,171292,30325
PDB,5WOY,BMRB Entry Tracking System,171308,30326
PDB,5WOZ,BMRB Entry Tracking System,171324,30327
PDB,6ALS,BMRB Entry Tracking System,171342,30328
PDB,6ALU,BMRB Entry Tracking System,171365,30329
PDB,6ALY,BMRB Entry Tracking System,171388,30330
BMRB,30332,Abl1b Regulatory Module 'Activating' conformation,171411,30331
PDB,6AMV,BMRB Entry Tracking System,171411,30331
BMRB,30331,Abl 1b Regulatory Module 'inhibiting state',171430,30332
PDB,6AMW,BMRB Entry Tracking System,171430,30332
PDB,6ANF,BMRB Entry Tracking System,171449,30333
PDB,6AP5,BMRB Entry Tracking System,171471,30334
PDB,6ASF,BMRB Entry Tracking System,171487,30335
PDB,6AST,BMRB Entry Tracking System,171504,30336
BMRB,30344,PawL-Derived Peptide PLP-10 (cis conformer),171523,30337
PDB,6AWK,BMRB Entry Tracking System,171523,30337
PDB,6AWM,BMRB Entry Tracking System,171541,30338
PDB,6CT1,,173485,30441
PDB,6AX2,BMRB Entry Tracking System,171559,30339
PDB,6AXD,BMRB Entry Tracking System,171578,30340
PDB,6AXI,BMRB Entry Tracking System,171596,30341
PDB,6AZA,BMRB Entry Tracking System,171616,30342
PDB,6AZF,BMRB Entry Tracking System,171635,30343
BMRB,30337,PawL-Derived Peptide PLP-12,171654,30344
PDB,6AZG,BMRB Entry Tracking System,171654,30344
PDB,6B1G,BMRB Entry Tracking System,171673,30345
PDB,6B34,BMRB Entry Tracking System,171695,30346
PDB,6B35,BMRB Entry Tracking System,171713,30347
PDB,6B3N,BMRB Entry Tracking System,171731,30348
PDB,6B3U,,171751,30349
PDB,6B9K,BMRB Entry Tracking System,171773,30350
PDB,6B9W,BMRB Entry Tracking System,171794,30351
PDB,6BA3,BMRB Entry Tracking System,171813,30352
PDB,6BA6,BMRB Entry Tracking System,171836,30353
PDB,6BB6,BMRB Entry Tracking System,171862,30354
PDB,6BE7,BMRB Entry Tracking System,171880,30355
PDB,6BE9,BMRB Entry Tracking System,171899,30356
PDB,6BEN,BMRB Entry Tracking System,171918,30357
PDB,6BEO,BMRB Entry Tracking System,171938,30358
PDB,6BEQ,BMRB Entry Tracking System,171957,30359
PDB,6BER,BMRB Entry Tracking System,171990,30360
PDB,6BES,BMRB Entry Tracking System,172012,30361
PDB,6BET,BMRB Entry Tracking System,172035,30362
PDB,6BEU,BMRB Entry Tracking System,172056,30363
PDB,6BEW,BMRB Entry Tracking System,172077,30364
PDB,6BF3,BMRB Entry Tracking System,172099,30365
PDB,6BF5,BMRB Entry Tracking System,172118,30366
PDB,6BGG,BMRB Entry Tracking System,172137,30367
PDB,6BGH,,172160,30368
PDB,6BI6,BMRB Entry Tracking System,172180,30370
PDB,6BJF,,172198,30371
PDB,6BL9,BMRB Entry Tracking System,172216,30372
PDB,6BNH,BMRB Entry Tracking System,172235,30373
PDB,6BP9,BMRB Entry Tracking System,172259,30374
PDB,6BQI,BMRB Entry Tracking System,172285,30375
PDB,6BR0,,172300,30376
PDB,6BTV,BMRB Entry Tracking System,172319,30377
PDB,6BUC,BMRB Entry Tracking System,172338,30378
PDB,6BV7,BMRB Entry Tracking System,172355,30379
PDB,6BVU,BMRB Entry Tracking System,172378,30380
PDB,6BVW,,172397,30381
PDB,6BVX,BMRB Entry Tracking System,172417,30382
PDB,6BVY,,172436,30383
PDB,6BX9,,172455,30385
PDB,6BY4,14-mer UUCG Tetraloop,172477,30386
PDB,6BY5,14-mer UUCG Tetraloop,172477,30386
PDB,6BYV,,172497,30388
PDB,6BZJ,,172521,30389
PDB,6BZK,,172538,30390
PDB,6BZL,,172556,30391
PDB,6C2U,,172574,30394
PDB,6C2V,,172596,30395
PDB,6C41,,172618,30396
PDB,6C44,,172640,30397
PDB,6C8U,,172657,30398
PDB,6CAH,,172678,30399
PDB,6CC9,,172699,30400
PDB,6CCH,,172726,30401
PDB,6CCW,,172755,30402
PDB,6CCX,,172775,30403
PDB,6CE5,,172806,30404
PDB,6CEG,,172824,30405
PDB,6CEI,,172843,30406
PDB,6CEJ,,172863,30407
PDB,6CFA,,172880,30408
PDB,6CFB,,172901,30409
PDB,6CGH,,172920,30410
PDB,6CGW,,172949,30411
PDB,6CGX,,172967,30412
PDB,6CHC,,172984,30413
PDB,6CIV,,173002,30414
PDB,6CIX,,173019,30415
BMRB,30427,CSP1-E1A,173035,30416
BMRB,30428,CSP1-R3A,173035,30416
BMRB,30429,CSP1-K6A,173035,30416
PDB,6CJ8,,173035,30416
PDB,6CJD,,173051,30417
PDB,6CJZ,,173067,30418
PDB,6CKD,,173087,30419
PDB,6CKF,,173104,30420
PDB,6CKQ,,173121,30421
PDB,6CKU,,173141,30422
PDB,6CKV,,173160,30423
PDB,6CL3,,173177,30424
PDB,6CLZ,,173198,30425
PDB,6CM1,,173222,30426
BMRB,30428,CSP1-R3A,173246,30427
BMRB,30429,CSP1-K6A,173246,30427
BMRB,30430,CSP1-F11A,173246,30427
PDB,6COO,,173246,30427
BMRB,30427,CSP1-E1A,173262,30428
BMRB,30429,CSP1-K6A,173262,30428
BMRB,30430,CSP1-F11A,173262,30428
PDB,6COP,,173262,30428
BMRB,30427,CSP1-E1A,173278,30429
BMRB,30428,CSP1-R3A,173278,30429
BMRB,30430,CSP1-F11A,173278,30429
PDB,6COQ,,173278,30429
BMRB,30427,CSP1-E1A,173294,30430
BMRB,30428,CSP1-R3A,173294,30430
BMRB,30429,CSP1-K6A,173294,30430
PDB,6COR,,173294,30430
PDB,6COS,,173310,30431
BMRB,30433,CSP2-E1Ad10,173328,30432
BMRB,30434,CSP2-l14,173328,30432
PDB,6COT,,173328,30432
BMRB,30432,CSP2-d10,173344,30433
BMRB,30434,CSP2-l14,173344,30433
PDB,6COU,,173344,30433
BMRB,30432,CSP2-d10,173360,30434
BMRB,30433,CSP2-E1Ad10,173360,30434
PDB,6COV,,173360,30434
BMRB,30427,CSP1-E1A,173376,30435
BMRB,30428,CSP1-R3A,173376,30435
BMRB,30429,CSP1-K6A,173376,30435
BMRB,30430,CSP1-F11A,173376,30435
PDB,6COW,,173376,30435
PDB,6CPI,,173392,30436
PDB,6CPJ,,173411,30437
PDB,6CPK,,173430,30438
PDB,6CSK,,173449,30439
PDB,6CSZ,,173467,30440
PDB,6CT4,,173503,30442
PDB,6CTG,,173521,30443
PDB,6CUI,,173543,30444
PDB,6CWS,,173561,30445
PDB,6CXN,,173583,30446
PDB,6CXP,,173598,30447
PDB,6CXQ,,173613,30448
PDB,6CXR,,173629,30449
PDB,6CZT,,173647,30450
PDB,6D10,,173647,30450
PDB,6D2H,,173665,30451
PDB,6D2U,,173687,30452
PDB,6D37,,173713,30453
PDB,6D3T,,173732,30454
PDB,6D6S,,173750,30456
PDB,6D6X,,173779,30457
PDB,6D74,,173798,30458
PDB,6D8H,,173817,30459
PDB,6D8Q,,173835,30460
PDB,6D8R,,173853,30461
PDB,6D8S,,173871,30462
PDB,6D8T,,173889,30463
PDB,6D8U,,173907,30464
PDB,6D8Y,,173925,30465
PDB,6D93,,173943,30466
PDB,6D9O,,173961,30467
PDB,6D9P,,173979,30468
PDB,6DG1,,173997,30469
PDB,6DHR,,174017,30470
PDB,6DL4,,174034,30471
PDB,6DLN,,174050,30472
PDB,6DM7,,174072,30473
PDB,6DMP,,174096,30474
PDB,6DMZ,,174115,30475
PDB,6DNY,,174133,30476
PDB,6DO6,,174149,30477
PDB,6DO7,,174169,30478
PDB,6DRG,,174169,30478
PDB,6DRI,,174191,30479
PDB,6DSL,,174210,30480
PDB,6DST,,174228,30481
PDB,6DUL,,174249,30482
PDB,6DUU,,174271,30483
PDB,6DVT,,174293,30484
PDB,6DXM,,174316,30485
PDB,6DZ9,,174339,30486
PDB,6DZA,,174356,30487
PDB,6DZB,,174373,30488
PDB,6DZC,,174390,30489
PDB,6DZE,,174407,30490
PDB,6E25,,174424,30491
PDB,6E26,,174448,30492
BMRB,27534,time-domain data,174469,30493
PDB,6E4H,,174469,30493
PDB,6E4J,,174499,30494
PDB,6NS8,,174499,30494
PDB,6E5C,,174526,30495
PDB,6E5H,,174542,30496
PDB,6E5I,,174560,30497
PDB,6E5J,,174578,30498
PDB,6E5K,,174599,30499
PDB,6E5N,,174618,30500
PDB,6E83,,174640,30501
PDB,6E86,,174663,30502
PDB,6E8W,,174686,30503
PDB,6E98,,174709,30504
PDB,6E9M,,174728,30505
PDB,6ED9,,174747,30506
PDB,6EE9,,174770,30507
PDB,6EFE,,174788,30508
PDB,6MBM,,174803,30509
PDB,6MCE,,174820,30510
PDB,6MCF,,174841,30511
PDB,6MCI,,174865,30512
PDB,6MF8,,174886,30513
PDB,6MG9,,174904,30514
PDB,6MI5,,174922,30515
PDB,6MI9,,174943,30516
PDB,6MIE,,174965,30517
PDB,6MIF,,174995,30518
PDB,6MJD,,175016,30519
PDB,6MJV,,175035,30520
PDB,6MK4,,175052,30521
PDB,6MK5,,175068,30522
PDB,6MK7,,175086,30523
PDB,6MK8,,175117,30524
PDB,6MM4,,175135,30525
PDB,6MSP,,175152,30527
PDB,6MUN,,175172,30528
PDB,6MV3,,175199,30529
PDB,6MW6,,175222,30530
PDB,6MWM,,175239,30531
PDB,6MXP,,175262,30532
PDB,6MXQ,,175284,30533
PDB,6MY1,,175308,30534
PDB,6MY2,,175328,30535
PDB,6MY3,,175348,30536
PDB,6MZA,,175368,30537
PDB,6MZT,,175388,30538
PDB,6N2M,,175409,30543
PDB,6N68,,175439,30544
PDB,6N8C,,175458,30545
BMRB,30547,RNA Duplex containing the internal loop 5'-GCAU/3'-UACG,175483,30546
BMRB,30548,RNA Duplex containing the internal loop 5'-UUCG/3'-GCUU,175483,30546
PDB,6N8F,,175483,30546
BMRB,30546,RNA Duplex containing the internal loop 5'-GCUU/3'-UUCG,175503,30547
BMRB,30548,RNA Duplex containing the internal loop 5'-UUCG/3'-GCUU,175503,30547
PDB,6N8H,,175503,30547
BMRB,30546,RNA Duplex containing the internal loop 5'-GCUU/3'-UUCG,175520,30548
BMRB,30547,RNA Duplex containing the internal loop 5'-GCAU/3'-UACG,175520,30548
PDB,6N8I,,175520,30548
PDB,6NBN,,175538,30550
PDB,6NE8,,175568,30551
PDB,6NEB,,175587,30552
PDB,6NHW,,175606,30553
PDB,6NHY,,175627,30554
PDB,6NK9,,175648,30555
PDB,6NL3,,175668,30556
PDB,6NM2,,175688,30557
PDB,6NM3,,175705,30558
PDB,6NNB,,175722,30559
PDB,6NOA,,175740,30560
PDB,6NOM,,175767,30561
PDB,6NOX,,175786,30562
PDB,6NU4,,175805,30565
PDB,6NUG,,175829,30566
PDB,6NVZ,,175847,30567
PDB,6NW8,,175865,30568
PDB,6NX4,,175883,30569
PDB,6NZ2,,175914,30570
PDB,6NZL,BMRB Entry Tracking System,175935,30571
PDB,6NZN,,175955,30572
PDB,6O0C,,175976,30573
PDB,6O0I,,175993,30574
PDB,6O1Q,,176010,30575
PDB,6O22,,176030,30576
PDB,6O2L,,176059,30577
PDB,6O3Q,,176077,30579
PDB,6O3S,,176098,30580
PDB,6O6I,,176119,30583
PDB,6O6W,,176141,30584
PDB,6O7G,,176169,30585
PDB,6O8J,,176193,30586
PDB,6O8P,,176193,30586
PDB,6O8R,BMRB Entry Tracking System,176207,30587
PDB,6O8S,BMRB Entry Tracking System,176221,30588
PDB,6OB1,,176235,30590
PDB,6OBI,,176257,30591
PDB,6OBK,,176280,30592
PDB,6OBW,,176298,30593
PDB,6OC2,,176314,30594
PDB,6OC4,,176331,30595
PDB,6OC9,,176348,30596
PDB,6OFA,,176368,30597
PDB,6OHX,,176390,30598
PDB,6OKX,,176411,30599
PDB,6OKY,,176442,30600
PDB,6OLD,,176460,30601
PDB,6OQ2,,176477,30602
PDB,6OQ9,,176500,30603
PDB,6OQH,,176518,30604
PDB,6OQJ,,176534,30605
PDB,6OQK,,176556,30606
PDB,6OQP,,176578,30607
PDB,6OSW,,176599,30608
PDB,6OTA,,176629,30609
PDB,6OVC,,176648,30610
PDB,6OWR,,176668,30611
BMRB,30614,CS-Rosetta Model of PEA-15 Death Effector Domain in the Complex with ERK2,176688,30613
PDB,6P6B,,176688,30613
BMRB,30613,CS-Rosetta Model of PEA-15 Death Effector Domain,176704,30614
PDB,6P6C,,176704,30614
PDB,6PEZ,,176720,30615
PDB,6PF0,,176752,30616
PDB,6PI2,,176783,30617
PDB,6PI3,,176802,30618
PDB,6PIN,,176821,30619
PDB,6PIO,,176839,30620
PDB,6PIP,,176857,30621
PDB,6PK9,,176875,30622
PDB,6PMG,,176897,30623
PDB,6POR,,176919,30625
PDB,6PPC,,176937,30626
PDB,6PPT,,176954,30627
PDB,6PQ2,,176974,30628
PDB,6PQE,,176995,30629
PDB,6PQF,,177016,30630
PDB,6PQG,,177035,30631
PDB,6PQM,,177053,30632
PDB,6PQT,,177073,30633
PDB,6PRI,,177089,30634
PDB,6PRJ,,177109,30635
PDB,6PRP,,177130,30636
PDB,6PRQ,,177151,30637
PDB,6PSI,,177173,30638
BMRB,30640,KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B),177195,30639
PDB,6PTS,,177195,30639
BMRB,30639,KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A),177233,30640
PDB,6PTW,,177233,30640
PDB,6PV0,,177271,30641
PDB,6PV1,,177292,30642
PDB,6PV2,,177313,30643
PDB,6PV3,,177334,30644
PDB,6PVR,,177359,30645
PDB,6PVT,,177377,30646
PDB,6PX7,,177396,30647
PDB,6PX8,,177412,30648
PDB,6Q08,,177440,30650
PDB,6Q1X,,177460,30651
BMRB,30653,Human CstF-64 RRM mutant - D50A,177476,30652
PDB,6Q2I,,177476,30652
BMRB,30652,Human CstF-64 RRM,177492,30653
PDB,6TZE,,177492,30653
PDB,6U24,,177508,30654
PDB,6U3R,,177529,30655
PDB,6U3S,,177557,30656
PDB,6U46,,177585,30657
PDB,6U4M,,177604,30658
PDB,6U4N,,177626,30659
PDB,6U6G,,177650,30660
PDB,6U6P,,177674,30661
PDB,6U6Q,,177696,30662
PDB,6U6R,,177718,30663
PDB,6U6S,,177740,30664
PDB,6U79,,177762,30665
PDB,6U7Q,,177778,30666
PDB,6U7R,,177796,30667
PDB,6U7S,,177814,30668
PDB,6U7U,,177833,30669
PDB,6U7W,,177853,30670
PDB,6U7X,,177873,30671
PDB,6UCH,,177893,30672
PDB,6UCO,,177913,30673
PDB,6UCP,,177934,30674
PDB,6UF2,,177954,30676
PDB,6UHW,,177970,30677
PDB,6UJU,,177994,30678
PDB,6UM9,,178020,30679
PDB,6URS,,178039,30680
PDB,6UT2,,178057,30681
PDB,6UY2,,178078,30684
PDB,6UZJ,,178078,30684
PDB,6V0L,,178097,30688
PDB,6V1N,,178119,30690
PDB,6V1W,,178136,30691
PDB,6V5D,,178158,30693
PDB,6V5L,,178176,30694
PDB,6V6T,,178201,30695
PDB,6V88,,178219,30696
PDB,6VA1,,178244,30697
PDB,6VA2,,178265,30698
PDB,6VA3,,178290,30699
PDB,6VA4,,178327,30700
PDB,6VE9,,178350,30702
PDB,6VED,,178373,30703
PDB,6VEE,,178394,30704
PDB,6VFO,BMRB Entry Tracking System,178415,30705
PDB,6VG7,BMRB Entry Tracking System,178435,30706
PDB,6VGA,BMRB Entry Tracking System,178454,30707
PDB,6VGB,BMRB Entry Tracking System,178474,30708
PDB,6VGT,,178494,30710
PDB,6VH8,BMRB Entry Tracking System,178515,30711
PDB,6VHJ,,178534,30712
PDB,7jvf,,178555,30713
PDB,6VJQ,,178578,30714
PDB,6VLJ,,178600,30718
PDB,6VNZ,,178624,30719
PDB,6VPN,,178642,30720
PDB,6VTI,,178660,30722
PDB,6VU1,,178678,30723
PDB,6VVJ,,178697,30724
PDB,6VXW,BMRB Entry Tracking System,178738,30727
PDB,6VY8,BMRB Entry Tracking System,178764,30729
PDB,6VZC,BMRB Entry Tracking System,178784,30730
PDB,6W4E,,178804,30734
PDB,6W4F,,178830,30735
PDB,6WA3,,178856,30738
PDB,6WA4,,178882,30739
PDB,6WA5,,178908,30740
PDB,6WAP,BMRB Entry Tracking System,178934,30741
PDB,6WPB,BMRB Entry Tracking System,178964,30744
PDB,6WPD,BMRB Entry Tracking System,178983,30745
PDB,6WPV,BMRB Entry Tracking System,179002,30747
PDB,6WQJ,BMRB Entry Tracking System,179020,30748
PDB,6WQL,BMRB Entry Tracking System,179041,30749
PDB,6WQR,BMRB Entry Tracking System,179060,30750
PDB,6X4X,BMRB Entry Tracking System,179080,30755
PDB,6X7I,BMRB Entry Tracking System,179101,30757
PDB,6X8R,BMRB Entry Tracking System,179123,30758
PDB,6XEH,BMRB Entry Tracking System,179143,30763
PDB,6XFL,BMRB Entry Tracking System,179167,30765
PDB,6XR6,BMRB Entry Tracking System,179194,30770
PDB,6XR7,BMRB Entry Tracking System,179216,30771
PDB,6XRG,BMRB Entry Tracking System,179238,30772
PDB,7JGI,BMRB Entry Tracking System,179261,30774
PDB,7JN6,BMRB Entry Tracking System,179297,30783
PDB,7JNN,BMRB Entry Tracking System,179315,30784
PDB,7JU1,BMRB Entry Tracking System,179333,30788
PDB,7JU9,BMRB Entry Tracking System,179352,30789
PDB,7K1Z,BMRB Entry Tracking System,179390,30794
PDB,7K3G,BMRB Entry Tracking System,179415,30795
PDB,7K7A,BMRB Entry Tracking System,179435,30799
PDB,1E8P,BMRB Entry Tracking System,179722,3322
PDB,1E8Q,BMRB Entry Tracking System,179722,3322
BMRB,34001,D11 bound [S39_PQ]-IGF-II,179841,34000
BMRB,34002,"D11 bound [N29, S39_PQ]-IGF-II",179841,34000
PDB,5L3L,BMRB Entry Tracking System,179841,34000
BMRB,34000,D11 bound IGF-II,179859,34001
BMRB,34002,"D11 bound [N29, S39_PQ]-IGF-II",179859,34001
PDB,5L3M,BMRB Entry Tracking System,179859,34001
BMRB,34000,D11 bound IGF-II,179877,34002
BMRB,34001,D11 bound [S39_PQ]-IGF-II,179877,34002
PDB,5L3N,BMRB Entry Tracking System,179877,34002
PDB,5L6R,BMRB Entry Tracking System,179895,34003
PDB,5L7B,BMRB Entry Tracking System,179916,34004
PDB,5L7M,BMRB Entry Tracking System,179933,34005
PDB,5L82,BMRB Entry Tracking System,179953,34006
PDB,5L85,BMRB Entry Tracking System,179971,34007
PDB,5LAH,BMRB Entry Tracking System,179989,34008
PDB,5LAM,BMRB Entry Tracking System,180006,34009
PDB,5LAO,BMRB Entry Tracking System,180022,34010
PDB,5LBJ,BMRB Entry Tracking System,180038,34011
EMDB,EMD-4033,,180055,34012
PDB,5LCB,BMRB Entry Tracking System,180055,34012
PDB,5LCI,BMRB Entry Tracking System,180075,34013
PDB,5LCS,BMRB Entry Tracking System,180098,34014
PDB,5LDL,BMRB Entry Tracking System,180117,34015
PDB,5LFF,BMRB Entry Tracking System,180136,34016
PDB,5LFH,BMRB Entry Tracking System,180153,34017
PDB,5LFI,BMRB Entry Tracking System,180172,34018
PDB,5LFY,BMRB Entry Tracking System,180188,34019
PDB,5LG9,BMRB Entry Tracking System,180210,34022
PDB,5LGM,BMRB Entry Tracking System,180229,34024
PDB,5LIG,BMRB Entry Tracking System,180247,34025
PDB,5LKN,BMRB Entry Tracking System,180270,34026
PDB,5LM0,BMRB Entry Tracking System,180293,34027
PDB,5LME,BMRB Entry Tracking System,180309,34028
PDB,5LMY,BMRB Entry Tracking System,180329,34029
PDB,5LNF,BMRB Entry Tracking System,180349,34030
PDB,5LO2,BMRB Entry Tracking System,180370,34031
PDB,5LO3,BMRB Entry Tracking System,180390,34032
PDB,5LO4,BMRB Entry Tracking System,180411,34033
BMRB,34035,A two-quartet G-quadruplex formed by human telomere in KCl solution at pH 5.0,180433,34034
PDB,5LQG,BMRB Entry Tracking System,180433,34034
BMRB,34034,A two-quartet G-quadruplex formed by human telomere in KCl solution at neutral pH,180452,34035
PDB,5LQH,BMRB Entry Tracking System,180452,34035
PDB,5LQV,BMRB Entry Tracking System,180471,34036
PDB,5LSD,BMRB Entry Tracking System,180489,34037
PDB,5LSN,BMRB Entry Tracking System,180511,34038
PDB,5LUE,BMRB Entry Tracking System,180531,34039
PDB,5LV6,BMRB Entry Tracking System,180565,34040
PDB,5LVF,BMRB Entry Tracking System,180580,34041
PDB,5LVY,BMRB Entry Tracking System,180600,34042
PDB,5LW8,BMRB Entry Tracking System,180616,34043
PDB,5LWC,BMRB Entry Tracking System,180633,34044
PDB,5LXJ,BMRB Entry Tracking System,180652,34045
PDB,5LXK,BMRB Entry Tracking System,180672,34046
PDB,5LXL,BMRB Entry Tracking System,180690,34047
PDB,5M0A,BMRB Entry Tracking System,180708,34048
PDB,5M1G,,180727,34049
PDB,5M1H,BMRB Entry Tracking System,180748,34050
PDB,5M1L,BMRB Entry Tracking System,180766,34051
PDB,5M1U,BMRB Entry Tracking System,180784,34052
PDB,5M1W,BMRB Entry Tracking System,180802,34053
PDB,5M2L,BMRB Entry Tracking System,180827,34054
PDB,5M4T,BMRB Entry Tracking System,180847,34055
PDB,5M4W,BMRB Entry Tracking System,180866,34056
PDB,5M8I,BMRB Entry Tracking System,180884,34057
PDB,5M9D,BMRB Entry Tracking System,180912,34058
PDB,5M9U,BMRB Entry Tracking System,180933,34059
PDB,5M9Y,BMRB Entry Tracking System,180950,34060
PDB,5M9Z,BMRB Entry Tracking System,180972,34061
BMRB,34063,Quadruplex with flipped tetrad formed by an artificial sequence,180999,34062
PDB,5MBR,BMRB Entry Tracking System,180999,34062
BMRB,34062,Quadruplex with flipped tetrad formed by a human telomeric sequence,181018,34063
PDB,5MCR,BMRB Entry Tracking System,181018,34063
PDB,5MCS,BMRB Entry Tracking System,181037,34064
BMRB,34066,Harzianin HK-VI in trifluoroethanol,181060,34065
PDB,5MF3,BMRB Entry Tracking System,181060,34065
BMRB,34065,Harzianin HK-VI in SDS micelles,181080,34066
PDB,5MF8,BMRB Entry Tracking System,181080,34066
BMRB,34068,RBM5 OCRE domain,181100,34067
PDB,5MF9,BMRB Entry Tracking System,181100,34067
PDB,5O9B,,182634,34149
BMRB,34067,RBM5 OCRE domain in complex with polyproline SmN peptide,181120,34068
PDB,5MFY,BMRB Entry Tracking System,181120,34068
PDB,5MGQ,BMRB Entry Tracking System,181138,34069
PDB,5MHD,BMRB Entry Tracking System,181158,34070
PDB,5MJX,BMRB Entry Tracking System,181176,34071
BMRB,34076,"NMR structure of the Littorina littorea metallothionein, a snail MT folding into three distinct domains",181194,34072
PDB,5ML1,BMRB Entry Tracking System,181194,34072
PDB,5MMC,BMRB Entry Tracking System,181219,34073
BMRB,34075,HYL-20k peptide,181238,34074
PDB,5MMK,BMRB Entry Tracking System,181238,34074
BMRB,34074,HYL-20 peptide,181256,34075
PDB,5MML,BMRB Entry Tracking System,181256,34075
BMRB,34072,"NMR structure of the Littorina littorea metallothionein, a snail MT folding into three distinct domains",181274,34076
PDB,5MN3,BMRB Entry Tracking System,181274,34076
PDB,5MNW,BMRB Entry Tracking System,181297,34077
PDB,5MOU,BMRB Entry Tracking System,181320,34078
PDB,5MPG,BMRB Entry Tracking System,181336,34079
PDB,5MPL,BMRB Entry Tracking System,181362,34080
PDB,5MRG,BMRB Entry Tracking System,181389,34081
PDB,5MSL,BMRB Entry Tracking System,181403,34082
PDB,5MTA,,181423,34083
PDB,5MTG,,181442,34084
PDB,5MTI,BMRB Entry Tracking System,181461,34085
PDB,5MVB,BMRB Entry Tracking System,181480,34086
PDB,5MWQ,BMRB Entry Tracking System,181504,34087
PDB,5MWV,BMRB Entry Tracking System,181523,34088
BMRB,27011,Relaxation data of Sigma1.1 domain of sigmaA,181566,34089
PDB,5MWW,BMRB Entry Tracking System,181566,34089
BMRB,34091,peptide WYHRLSHLHSRLQD(NH2),181588,34090
BMRB,34092,peptide WYHRLSHIHSRLQD(NH2),181588,34090
PDB,5MXL,BMRB Entry Tracking System,181588,34090
BMRB,34090,peptide GLFDIVKKVVGALG(NH2),181604,34091
BMRB,34092,peptide WYHRLSHIHSRLQD(NH2),181604,34091
PDB,5MXS,BMRB Entry Tracking System,181604,34091
BMRB,34090,peptide GLFDIVKKVVGALG(NH2),181620,34092
BMRB,34091,peptide WYHRLSHLHSRLQD(NH2),181620,34092
PDB,5MXT,BMRB Entry Tracking System,181620,34092
PDB,5MYE,BMRB Entry Tracking System,181636,34093
PDB,5N14,BMRB Entry Tracking System,181657,34094
PDB,5N2O,BMRB Entry Tracking System,181685,34095
PDB,5N5A,BMRB Entry Tracking System,181706,34098
PDB,5N5B,BMRB Entry Tracking System,181726,34099
PDB,5N5C,BMRB Entry Tracking System,181759,34100
PDB,5N6R,BMRB Entry Tracking System,181782,34101
PDB,5N7Y,,181803,34102
PDB,5N8L,,181825,34103
PDB,5N8M,,181851,34104
PDB,5N9U,BMRB Entry Tracking System,181877,34105
PDB,5N9V,,181897,34106
PDB,5NAM,BMRB Entry Tracking System,181915,34108
PDB,5NAO,,181936,34109
PDB,5NB9,BMRB Entry Tracking System,181952,34110
PDB,5NBB,BMRB Entry Tracking System,181971,34111
PDB,5NCA,BMRB Entry Tracking System,181989,34112
PDB,5NCE,BMRB Entry Tracking System,182008,34113
PDB,5NDA,BMRB Entry Tracking System,182026,34114
PDB,5NF8,,182045,34115
PDB,5NHQ,BMRB Entry Tracking System,182072,34116
PDB,5NIP,BMRB Entry Tracking System,182091,34118
PDB,5NIQ,,182108,34119
PDB,5NKO,BMRB Entry Tracking System,182129,34120
PDB,5NMY,BMRB Entry Tracking System,182146,34121
PDB,5NOC,BMRB Entry Tracking System,182167,34122
PDB,5NPA,BMRB Entry Tracking System,182186,34123
PDB,5NPG,BMRB Entry Tracking System,182202,34124
PDB,5NQ4,BMRB Entry Tracking System,182218,34125
BMRB,34127,Dictyostelium discoidans MATB protein,182242,34126
PDB,5NR5,BMRB Entry Tracking System,182242,34126
PDB,5NR6,BMRB Entry Tracking System,182262,34127
PDB,5NVB,,182282,34129
PDB,5NVP,BMRB Entry Tracking System,182302,34130
PDB,5NWM,BMRB Entry Tracking System,182319,34131
PDB,5NWU,BMRB Entry Tracking System,182351,34132
PDB,5NWV,BMRB Entry Tracking System,182368,34133
PDB,5NWW,BMRB Entry Tracking System,182385,34134
BMRB,34136,M2 G-quadruplex 20 wt% ethylene glycol,182402,34135
BMRB,34137,M2 G-quadruplex 10 wt% PEG8000,182402,34135
PDB,5NYS,M2 G-quadruplex dilute solution,182402,34135
BMRB,34135,M2 G-quadruplex dilute solution,182420,34136
BMRB,34137,M2 G-quadruplex 10 wt% PEG8000,182420,34136
PDB,5NYT,M2 G-quadruplex 20 wt% ethylene glycol,182420,34136
BMRB,34135,M2 G-quadruplex dilute solution,182437,34137
BMRB,34136,M2 G-quadruplex 20 wt% ethylene glycol,182437,34137
PDB,5NYU,M2 G-quadruplex 10 wt% PEG8000,182437,34137
PDB,5NZ9,BMRB Entry Tracking System,182453,34138
PDB,5O1Q,BMRB Entry Tracking System,182472,34139
PDB,5O1T,BMRB Entry Tracking System,182490,34140
BMRB,34142,CAS SH3 domain PTP-PEST peptide chimera,182513,34141
BMRB,34143,CAS SH3 domain Vinculin peptide chimera,182513,34141
PDB,5O2M,BMRB Entry Tracking System,182513,34141
BMRB,34141,CAS SH3 domain,182531,34142
BMRB,34143,CAS SH3 domain Vinculin peptide chimera,182531,34142
PDB,5O2P,BMRB Entry Tracking System,182531,34142
BMRB,34141,CAS SH3 domain,182549,34143
BMRB,34142,CAS SH3 domain PTP-PEST peptide chimera,182549,34143
PDB,5O2Q,BMRB Entry Tracking System,182549,34143
PDB,5O2V,BMRB Entry Tracking System,182567,34144
PDB,5O4D,,182590,34145
PDB,5O57,BMRB Entry Tracking System,182611,34146
PDB,5OAO,BMRB Entry Tracking System,182652,34151
PDB,5OAP,BMRB Entry Tracking System,182679,34152
PDB,5OAY,BMRB Entry Tracking System,182704,34153
PDB,5OB4,BMRB Entry Tracking System,182721,34154
PDB,5OBN,,182737,34155
PDB,5ODF,BMRB Entry Tracking System,182760,34157
PDB,5ODM,BMRB Entry Tracking System,182790,34158
PDB,5OE1,BMRB Entry Tracking System,182820,34159
PDB,5OEK,,182850,34160
PDB,5OEO,,182872,34161
PDB,5OGA,BMRB Entry Tracking System,182896,34162
PDB,5OGU,BMRB Entry Tracking System,182915,34163
PDB,5OHD,,182930,34164
PDB,5OJT,BMRB Entry Tracking System,182952,34165
PDB,5OLF,,182974,34166
PDB,5OMZ,BMRB Entry Tracking System,182992,34167
PDB,5OPH,,183013,34168
PDB,5OQK,,183033,34169
PDB,5OQS,,183047,34170
PDB,5OR0,BMRB Entry Tracking System,183067,34171
PDB,5OR5,BMRB Entry Tracking System,183085,34172
PDB,5OUN,BMRB Entry Tracking System,183108,34173
PDB,5OV2,BMRB Entry Tracking System,183125,34174
PDB,5OVM,,183143,34175
PDB,6EHZ,BMRB Entry Tracking System,183163,34176
PDB,6EKA,,183185,34178
PDB,6EMO,,183203,34179
PDB,6EMP,,183219,34180
PDB,6EMQ,,183236,34181
PDB,6EMR,,183253,34182
PDB,6ENA,,183269,34183
PDB,6EQY,,183290,34184
PDB,6ER0,,183307,34185
PDB,6ERL,,183324,34186
PDB,6ES5,,183342,34187
PDB,6ES6,,183363,34188
PDB,6ES7,,183381,34189
PDB,6ESP,,183399,34190
PDB,6EVI,,183417,34191
PDB,6EWS,,183434,34193
PDB,6EWT,,183460,34194
PDB,6EWU,,183484,34195
PDB,6EWV,,183513,34196
PDB,6EY3,BMRB Entry Tracking System,183539,34198
PDB,6EZ0,BMRB Entry Tracking System,183555,34199
PDB,6EZ4,BMRB Entry Tracking System,183587,34200
PDB,6F0Y,BMRB Entry Tracking System,183605,34201
PDB,6F24,BMRB Entry Tracking System,183631,34202
PDB,6F27,BMRB Entry Tracking System,183647,34203
PDB,6F3V,BMRB Entry Tracking System,183665,34206
PDB,6F3W,BMRB Entry Tracking System,183683,34207
PDB,6F3X,BMRB Entry Tracking System,183701,34208
PDB,6F3Y,BMRB Entry Tracking System,183722,34209
PDB,6F4Z,,183749,34210
PDB,6F55,,183767,34211
PDB,6F61,,183799,34212
PDB,6F7M,,183817,34213
PDB,6F7N,BMRB Entry Tracking System,183837,34214
PDB,6F7O,BMRB Entry Tracking System,183857,34215
PDB,6F8E,,183877,34216
PDB,6F98,,183893,34217
PDB,6F99,,183915,34218
PDB,6F9A,,183938,34219
PDB,6FBL,,183960,34220
PDB,6FC9,,183980,34221
PDB,6FCE,BMRB Entry Tracking System,184000,34222
PDB,6FDP,BMRB Entry Tracking System,184020,34223
PDB,6FDT,BMRB Entry Tracking System,184040,34224
PDB,6FE6,,184060,34225
PDB,6FEH,,184083,34226
BMRB,34229,"Solution NMR structure of CBM64 from S.thermophila using 20% 13C, 100% 15N",184110,34227
PDB,6FFQ,,184110,34227
PDB,6FFR,,184130,34228
BMRB,34227,Solution NMR structure of CBM64 from S.thermophila,184149,34229
PDB,6FFU,,184149,34229
PDB,6FGN,,184169,34231
PDB,6FGP,,184190,34232
PDB,6FGS,,184214,34233
PDB,6FI7,,184235,34234
PDB,6FIP,,184252,34235
PDB,6FNV,,184271,34236
PDB,6FS4,,184293,34237
PDB,6FS5,,184309,34238
PDB,6FTK,,184325,34239
PDB,6FVC,,184343,34240
PDB,6FWN,,184361,34243
BMRB,34245,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (minor species),184384,34244
BMRB,34398,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (apo species),184384,34244
PDB,6FY6,,184384,34244
PDB,6FY7,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (minor species),184384,34244
PDB,6RLS,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (apo species),184384,34244
BMRB,34244,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (major species),184407,34245
BMRB,34398,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (apo species),184407,34245
PDB,6FY6,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (major species),184407,34245
PDB,6FY7,,184407,34245
PDB,6RLS,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (apo species),184407,34245
PDB,6FZK,,184426,34246
PDB,6G03,,184449,34247
PDB,6G04,,184468,34248
PDB,6G4A,,184491,34249
BMRB,34251,brevinin-1BYa sodium dodecyl sulphate,184506,34250
BMRB,34252,brevinin-1BYa in dodecylphosphocholine,184506,34250
BMRB,34253,brevinin-1BYa in 33% trifluoroethanol,184506,34250
BMRB,34254,brevinin-1BYa in sodium dodecyl sulphate,184506,34250
PDB,6G4I,,184506,34250
PDB,6G4K,,184522,34251
BMRB,34250,brevinin-1BYa in 33% trifluoroethanol,184539,34252
BMRB,34251,brevinin-1BYa sodium dodecyl sulphate,184539,34252
BMRB,34253,brevinin-1BYa in 33% trifluoroethanol,184539,34252
BMRB,34254,brevinin-1BYa in sodium dodecyl sulphate,184539,34252
PDB,6G4U,,184539,34252
BMRB,34250,brevinin-1BYa in 33% trifluoroethanol,184555,34253
PDB,6QYV,,186915,34373
BMRB,34251,brevinin-1BYa sodium dodecyl sulphate,184555,34253
BMRB,34252,brevinin-1BYa in dodecylphosphocholine,184555,34253
BMRB,34254,brevinin-1BYa in sodium dodecyl sulphate,184555,34253
PDB,6G4V,,184555,34253
BMRB,34250,brevinin-1BYa in 33% trifluoroethanol,184571,34254
BMRB,34251,brevinin-1BYa sodium dodecyl sulphate,184571,34254
BMRB,34252,brevinin-1BYa in dodecylphosphocholine,184571,34254
BMRB,34253,brevinin-1BYa in 33% trifluoroethanol,184571,34254
PDB,6G4X,,184571,34254
PDB,6G5R,,184587,34255
PDB,6G5S,,184611,34256
PDB,6G81,,184633,34257
PDB,6G99,,184659,34258
PDB,6GBM,,184690,34259
PDB,6GC3,,184721,34260
PDB,6GD5,,184741,34261
BMRB,34263,Calmodulin mutant - F141L apo-form Unstructured C-domain,184775,34262
PDB,6GDK,,184775,34262
PDB,6GDL,,184797,34263
PDB,6GDZ,,184813,34264
PDB,6GE1,,184834,34265
PDB,6GE2,,184855,34266
PDB,6GFT,,184876,34267
PDB,6GGZ,,184893,34268
PDB,6GH0,,184910,34269
PDB,6GIF,,184944,34270
PDB,6GIG,,184960,34271
BMRB,34273,NMR structure of temporin B L1FK,184978,34272
BMRB,34274,NMR structure of temporin B,184978,34272
PDB,6GIJ,,184978,34272
BMRB,34272,NMR structure of temporin B KKG6A,184996,34273
BMRB,34274,NMR structure of temporin B,184996,34273
PDB,6GIK,,184996,34273
BMRB,34272,NMR structure of temporin B KKG6A,185014,34274
BMRB,34273,NMR structure of temporin B L1FK,185014,34274
PDB,6GIL,,185014,34274
PDB,6GMY,,185032,34276
PDB,6GN4,,185057,34277
BMRB,34279,Plantaricin S-b,185083,34278
PDB,6GNZ,,185083,34278
BMRB,34278,Plantaricin S-b,185101,34279
PDB,6GO0,,185101,34279
PDB,6GPI,,185119,34280
PDB,6GQ9,,185145,34281
PDB,6GRV,,185162,34282
PDB,6GS5,,185190,34283
PDB,6GS9,,185207,34284
PDB,6GSE,,185225,34285
PDB,6GSF,,185244,34286
PDB,6GT7,,185263,34287
PDB,6GV6,,185283,34288
PDB,6GV7,,185310,34289
PDB,6GVQ,,185338,34290
PDB,6GVT,,185338,34290
PDB,6GVU,,185376,34291
PDB,6GW7,,185402,34292
PDB,6GW8,,185425,34293
PDB,6GWM,,185450,34294
PDB,6GWX,,185466,34295
PDB,6GZ7,,185489,34296
PDB,6GZN,,185509,34297
PDB,6H0I,,185526,34298
BMRB,34301,B1-type ACP domain from module 7 of MLSB,185542,34299
PDB,6H0J,,185542,34299
PDB,6F2X,,185565,34300
BMRB,34299,A1-type ACP domain from module 5 of MLSA1,185588,34301
PDB,6H0Q,,185588,34301
PDB,6H1K,,185611,34302
PDB,6H3E,,185627,34303
PDB,6H5H,,185650,34304
PDB,6H7I,,185669,34305
PDB,6H7Q,,185686,34306
PDB,6H8C,,185703,34307
PDB,6HD2,,185727,34308
PDB,6HH0,,185754,34309
PDB,6HMI,,185769,34311
PDB,6HMO,,185789,34312
PDB,6HN9,,185811,34313
PDB,6HNE,,185828,34314
PDB,6HNG,,185845,34315
PDB,6HNH,,185862,34316
PDB,6HQ1,,185879,34318
PDB,6HVB,,185901,34319
PDB,6HVC,,185901,34319
PDB,6HVK,,185918,34320
PDB,6HYK,,185936,34321
PDB,6HZ2,,185959,34322
PDB,6I1V,,185978,34323
PDB,6I1W,,185999,34324
PDB,6I2O,,186020,34325
PDB,6I3R,,186038,34326
PDB,6I4O,,186058,34328
PDB,6I57,,186079,34329
PDB,6I9H,,186109,34330
PDB,6IA0,,186131,34331
PDB,6IA4,,186148,34332
PDB,6IB6,,186165,34333
PDB,6Q2Z,,186183,34334
PDB,6Q5Z,,186206,34335
PDB,6Q6E,,186224,34336
PDB,6Q8L,,186245,34337
PDB,6QAM,,186263,34338
PDB,6QAN,,186279,34339
BMRB,34342,peptide LGQQQAFPPQQPY,186301,34340
BMRB,34343,peptide LGQQQPAPPQQPY,186301,34340
PDB,6QAX,,186301,34340
PDB,6QAY,,186318,34341
BMRB,34340,peptide LGQQQPFPPQQPY,186338,34342
BMRB,34343,peptide LGQQQPAPPQQPY,186338,34342
PDB,6QB0,,186338,34342
BMRB,34340,peptide LGQQQPFPPQQPY,186354,34343
BMRB,34342,peptide LGQQQAFPPQQPY,186354,34343
PDB,6QB1,,186354,34343
PDB,6QBI,,186370,34344
PDB,6QBK,,186388,34345
PDB,6QBL,,186405,34346
PDB,6QEB,,186423,34347
PDB,6QES,,186443,34348
PDB,6QET,,186459,34349
PDB,6QEU,,186489,34350
PDB,6QF8,,186505,34351
PDB,6QH2,,186525,34352
PDB,6QHI,,186545,34353
PDB,6QJB,,186568,34354
PDB,6QK5,,186584,34355
PDB,6QK6,,186608,34356
PDB,6QKF,,186631,34357
PDB,6QKP,,186648,34358
PDB,6QKQ,,186667,34359
PDB,6QM1,,186699,34360
PDB,6QS0,,186716,34361
PDB,6QTC,,186734,34362
PDB,6QTF,,186756,34363
PDB,6QWR,,186773,34365
PDB,6QXB,,186793,34366
PDB,6QXC,,186812,34367
PDB,6QYR,,186831,34369
PDB,6QYS,,186863,34370
PDB,6QYT,,186880,34371
PDB,6QYU,,186897,34372
PDB,6QYW,,186932,34374
PDB,6R0J,,186951,34376
PDB,6R14,,186968,34378
PDB,6R1V,,186989,34379
PDB,6R28,,187011,34380
PDB,6R2X,,187029,34381
PDB,6R3C,,187047,34383
PDB,6R5G,,187064,34384
PDB,6R8D,BMRB Entry Tracking System,187086,34385
PDB,6R95,,187103,34387
PDB,6R96,,187121,34388
PDB,6R9K,,187140,34389
PDB,6R9L,,187159,34390
PDB,6R9Z,,187178,34391
PDB,6RC7,BMRB Entry Tracking System,187197,34392
PDB,6RFM,BMRB Entry Tracking System,187218,34393
PDB,6RH5,,187235,34394
PDB,6RH6,,187256,34395
PDB,6RHY,,187280,34396
PDB,6RIO,,187303,34397
BMRB,34244,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (major species),187324,34398
BMRB,34245,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (minor species),187324,34398
PDB,6FY6,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (major species),187324,34398
PDB,6FY7,Concerted dynamics of metallo-base pairs in an A/B-form helical transition (minor species),187324,34398
PDB,6RLS,,187324,34398
PDB,6RPV,,187343,34399
PDB,6RQS,,187376,34400
PDB,6RRL,,187397,34401
PDB,6RRO,,187416,34402
PDB,6RS3,,187435,34403
PDB,6RSM,,187471,34406
PDB,6RSS,,187491,34407
PDB,6RVA,,187513,34408
PDB,6RWG,,187532,34409
PDB,6RY9,,187566,34410
PDB,6RYQ,,187585,34411
PDB,6RZ1,BMRB Entry Tracking System,187603,34412
PDB,6RZC,,187621,34413
PDB,6S0N,,187639,34414
PDB,6S2D,,187655,34416
PDB,6SAA,BMRB Entry Tracking System,187673,34417
PDB,6SAB,BMRB Entry Tracking System,187689,34418
PDB,6SAI,,187705,34419
PDB,6SCW,BMRB Entry Tracking System,187735,34420
PDB,6SDW,,187751,34421
PDB,6SDY,,187785,34422
PDB,6SGO,,187815,34423
PDB,6SJX,,187834,34424
PDB,6SLY,,187866,34425
PDB,6SNJ,,187886,34427
BMRB,34429,Mouse RBM20 RRM domain,187914,34428
PDB,6SO9,,187914,34428
PDB,6SOE,Mouse RBM20 RRM domain,187914,34428
BMRB,34428,Mouse RBM20 RRM domain in complex with AUCUUA RNA,187942,34429
PDB,6SO9,Mouse RBM20 RRM domain in complex with AUCUUA RNA,187942,34429
PDB,6SOE,,187942,34429
PDB,6SOW,BMRB Entry Tracking System,187964,34430
BMRB,34441,KRAS32R G25T conformer G-quadruplex within KRAS promoter region,187986,34431
PDB,6SUU,,187986,34431
PDB,6T2G,KRAS32R G25T conformer G-quadruplex within KRAS promoter region,187986,34431
PDB,6SVC,,188008,34432
PDB,6SVE,,188025,34433
PDB,6SVH,,188042,34434
PDB,6SX3,,188059,34435
PDB,6SX6,BMRB Entry Tracking System,188079,34436
PDB,6SY2,,188100,34437
PDB,6SYK,BMRB Entry Tracking System,188119,34438
PDB,6SZC,,188140,34439
PDB,6SZF,,188158,34440
BMRB,34431,KRAS32R G9T conformer G-quadruplex within KRAS promoter region,188174,34441
PDB,6SUU,KRAS32R G9T conformer G-quadruplex within KRAS promoter region,188174,34441
PDB,6T2G,,188174,34441
PDB,6TAZ,BMRB Entry Tracking System,188197,34443
PDB,6TC8,,188214,34444
PDB,6TCG,,188235,34445
PDB,6TDD,,188256,34446
PDB,6TDM,BMRB Entry Tracking System,188273,34447
PDB,6TDN,BMRB Entry Tracking System,188290,34448
PDB,6TG5,,188307,34451
PDB,6TH8,,188330,34452
PDB,6TI5,BMRB Entry Tracking System,188347,34454
PDB,6TI6,BMRB Entry Tracking System,188366,34455
PDB,6TI7,BMRB Entry Tracking System,188389,34456
PDB,6TIQ,refined structure calculation,188412,34457
PDB,6TIR,ligand binding model,188412,34457
PDB,6TJ3,,188430,34459
PDB,6TL0,,188454,34461
PDB,6TO6,,188479,34462
PDB,6TOB,,188498,34463
PDB,6TPH,,188515,34465
PDB,6TR0,BMRB Entry Tracking System,188544,34466
PDB,6TR2,,188561,34467
PDB,6TRM,,188578,34468
PDB,6TRP,,188597,34469
PDB,6TVM,BMRB Entry Tracking System,188624,34475
PDB,6TWG,BMRB Entry Tracking System,188640,34476
PDB,6TXT,,188658,34477
PDB,6XTT,BMRB Entry Tracking System,188677,34480
PDB,6XWI,,188693,34481
PDB,6XWJ,BMRB Entry Tracking System,188713,34482
PDB,6XWW,BMRB Entry Tracking System,188733,34483
PDB,6XXB,BMRB Entry Tracking System,188733,34483
PDB,6XXA,BMRB Entry Tracking System,188752,34484
PDB,6Y06,,188773,34488
PDB,6Y07,,188793,34489
PDB,6Y1H,,188825,34490
PDB,6Y4H,,188843,34492
PDB,6Y6M,BMRB Entry Tracking System,188862,34493
PDB,6Y8V,,188883,34494
PDB,6Y8W,,188900,34495
PDB,6Y94,BMRB Entry Tracking System,188917,34496
PDB,6Y95,BMRB Entry Tracking System,188945,34497
PDB,6Y96,BMRB Entry Tracking System,188971,34498
PDB,6YCV,BMRB Entry Tracking System,188990,34499
PDB,6YDH,BMRB Entry Tracking System,189026,34500
PDB,6YEP,BMRB Entry Tracking System,189052,34502
PDB,6YI3,,189071,34511
PDB,6YTC,BMRB Entry Tracking System,189088,34514
PDB,6ZL2,BMRB Entry Tracking System,189106,34524
BMRB,50322,ABD23ss peptide,214910,50317
PDB,6ZL9,BMRB Entry Tracking System,189124,34525
PDB,6ZTE,BMRB Entry Tracking System,189140,34533
BMRB,25576,SOLUTION STRUCTURE OF HUMAN SUMO1,189434,36000
BMRB,25577,SOLUTION STRUCTURE OF HUMAN SUMO2,189434,36000
BMRB,36006,SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2,189434,36000
BMRB,36007,SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2,189434,36000
BMRB,36008,SOLUTION STRUCTURE OF LYS39 ACETYLATED HUMAN SUMO1,189434,36000
PDB,5B7A,BMRB Entry Tracking System,189434,36000
PDB,5B7J,BMRB Entry Tracking System,189458,36001
PDB,5GGM,BMRB Entry Tracking System,189480,36005
BMRB,25576,SOLUTION STRUCTURE OF HUMAN SUMO1,189503,36006
BMRB,25577,SOLUTION STRUCTURE OF HUMAN SUMO2,189503,36006
BMRB,36000,SOLUTION STRUCTURE OF LYS37 ACETYLATED HUMAN SUMO1,189503,36006
BMRB,36007,SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2,189503,36006
BMRB,36008,SOLUTION STRUCTURE OF LYS39 ACETYLATED HUMAN SUMO1,189503,36006
PDB,5GHB,BMRB Entry Tracking System,189503,36006
BMRB,25576,SOLUTION STRUCTURE OF HUMAN SUMO1,189527,36007
BMRB,25577,SOLUTION STRUCTURE OF HUMAN SUMO2,189527,36007
BMRB,36000,SOLUTION STRUCTURE OF LYS37 ACETYLATED HUMAN SUMO1,189527,36007
BMRB,36006,SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2,189527,36007
BMRB,36008,SOLUTION STRUCTURE OF LYS39 ACETYLATED HUMAN SUMO1,189527,36007
PDB,5GHC,BMRB Entry Tracking System,189527,36007
BMRB,25576,SOLUTION STRUCTURE OF HUMAN SUMO1,189551,36008
BMRB,25577,SOLUTION STRUCTURE OF HUMAN SUMO2,189551,36008
BMRB,36000,SOLUTION STRUCTURE OF LYS37 ACETYLATED HUMAN SUMO1,189551,36008
BMRB,36006,SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2,189551,36008
BMRB,36007,SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2,189551,36008
PDB,5GHD,BMRB Entry Tracking System,189551,36008
PDB,5GIW,BMRB Entry Tracking System,189575,36009
PDB,5GJL,BMRB Entry Tracking System,189593,36011
PDB,5GO0,BMRB Entry Tracking System,189613,36012
PDB,5GOW,BMRB Entry Tracking System,189630,36013
PDB,5GPH,BMRB Entry Tracking System,189654,36014
PDB,5GSF,BMRB Entry Tracking System,189673,36016
PDB,5GVO,BMRB Entry Tracking System,189689,36017
PDB,5GVQ,BMRB Entry Tracking System,189706,36018
PDB,5GWG,BMRB Entry Tracking System,189724,36019
BMRB,36022,Structure of two TTTA repeats,189742,36020
PDB,5GWL,BMRB Entry Tracking System,189742,36020
PDB,5GWM,BMRB Entry Tracking System,189760,36021
BMRB,36020,Structure of two CCTG repeats,189779,36022
PDB,5GWQ,BMRB Entry Tracking System,189779,36022
BMRB,36024,"NMR structure of TIBA, a chimera of SFTI",189797,36023
PDB,5H1H,BMRB Entry Tracking System,189797,36023
BMRB,36023,"NMR structure of SLBA, a chimera of SFTI",189813,36024
PDB,5H1I,BMRB Entry Tracking System,189813,36024
PDB,5H2S,BMRB Entry Tracking System,189829,36025
BMRB,36027,Solution structure of human Gelsolin protein domain 1 at pH 7.3,189846,36026
PDB,5H3M,BMRB Entry Tracking System,189846,36026
BMRB,36026,Solution structure of human Gelsolin protein domain 1 at pH 5.0,189862,36027
PDB,5H3N,BMRB Entry Tracking System,189862,36027
PDB,5H7U,BMRB Entry Tracking System,189878,36034
PDB,5WQZ,BMRB Entry Tracking System,189897,36037
PDB,5WRX,BMRB Entry Tracking System,189911,36038
PDB,5WUZ,BMRB Entry Tracking System,189927,36040
PDB,5WXE,BMRB Entry Tracking System,189944,36041
PDB,5WYE,BMRB Entry Tracking System,189962,36044
PDB,5WYO,BMRB Entry Tracking System,189977,36045
PDB,5X0S,BMRB Entry Tracking System,189995,36047
PDB,5X1X,BMRB Entry Tracking System,190012,36048
PDB,5X29,BMRB Entry Tracking System,190031,36049
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190051,36050
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190051,36050
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190051,36050
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190051,36050
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190051,36050
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190051,36050
PDB,5X34,BMRB Entry Tracking System,190051,36050
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190070,36051
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190070,36051
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190070,36051
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190070,36051
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190070,36051
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190070,36051
PDB,5X35,BMRB Entry Tracking System,190070,36051
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190091,36052
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190091,36052
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190091,36052
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190091,36052
BMRB,36105,Solution structure of arenicin-3 derivative N6,190783,36106
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190091,36052
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190091,36052
PDB,5X36,BMRB Entry Tracking System,190091,36052
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190112,36053
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190112,36053
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190112,36053
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190112,36053
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190112,36053
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190112,36053
PDB,5X37,BMRB Entry Tracking System,190112,36053
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190133,36054
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190133,36054
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190133,36054
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190133,36054
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190133,36054
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190133,36054
PDB,5X38,BMRB Entry Tracking System,190133,36054
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190154,36055
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190154,36055
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190154,36055
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190154,36055
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190154,36055
BMRB,36056,Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3,190154,36055
PDB,5X39,BMRB Entry Tracking System,190154,36055
BMRB,36050,"Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form",190175,36056
BMRB,36051,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1,190175,36056
BMRB,36052,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3,190175,36056
BMRB,36053,Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14,190175,36056
BMRB,36054,Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3,190175,36056
BMRB,36055,Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3,190175,36056
PDB,5X3C,BMRB Entry Tracking System,190175,36056
PDB,5X3L,BMRB Entry Tracking System,190196,36057
BMRB,36059,Solution structure of musashi1 RBD2 in complex with RNA,190212,36058
PDB,5X3Y,BMRB Entry Tracking System,190212,36058
PDB,5X3Z,BMRB Entry Tracking System,190230,36059
PDB,5X4F,BMRB Entry Tracking System,190250,36060
PDB,5X5S,BMRB Entry Tracking System,190269,36061
PDB,5X6T,BMRB Entry Tracking System,190287,36062
PDB,5X9X,BMRB Entry Tracking System,190303,36064
PDB,5XBD,BMRB Entry Tracking System,190322,36066
PDB,5XDI,BMRB Entry Tracking System,190340,36068
PDB,5XDJ,BMRB Entry Tracking System,190357,36069
BMRB,36071,NMR solution structure of the aromatic mutant H43F H67F cytochrome b5,190372,36070
PDB,5XE4,BMRB Entry Tracking System,190372,36070
BMRB,36070,NMR solution structure of the aromatic mutant H43W H67F cytochrome b5,190390,36071
PDB,5XEE,BMRB Entry Tracking System,190390,36071
PDB,5XEK,BMRB Entry Tracking System,190409,36072
BMRB,36074,TK9 NMR structure in SDS micelle,190426,36073
PDB,5XER,BMRB Entry Tracking System,190426,36073
BMRB,36073,TK9 NMR structure in DPC micelle,190442,36074
PDB,5XES,BMRB Entry Tracking System,190442,36074
PDB,5XHT,BMRB Entry Tracking System,190458,36075
BMRB,36078,Solution structure for human HSP70 substrate binding domain L542Y mutant,190476,36077
PDB,5XI9,BMRB Entry Tracking System,190476,36077
BMRB,36077,Solution structure for human HSP70 substrate binding domain,190495,36078
PDB,5XIR,BMRB Entry Tracking System,190495,36078
PDB,5XIV,BMRB Entry Tracking System,190514,36079
PDB,5XJK,BMRB Entry Tracking System,190531,36080
BMRB,36082,Relaxed state of S65-phosphorylated ubiquitin,190546,36081
PDB,5XK4,BMRB Entry Tracking System,190546,36081
BMRB,36081,Retracted state of S65-phosphorylated ubiquitin,190563,36082
PDB,5XK5,BMRB Entry Tracking System,190563,36082
PDB,5XM4,,190580,36083
PDB,5XME,BMRB Entry Tracking System,190597,36084
PDB,5XN4,,190614,36085
PDB,5XND,BMRB Entry Tracking System,190629,36086
PDB,5XNG,BMRB Entry Tracking System,190652,36087
PDB,5XQM,BMRB Entry Tracking System,190667,36096
PDB,5XR1,BMRB Entry Tracking System,190684,36097
PDB,5XRX,BMRB Entry Tracking System,190699,36098
PDB,5XV8,BMRB Entry Tracking System,190727,36101
PDB,5XZK,BMRB Entry Tracking System,190751,36103
BMRB,36106,Solution structure of arenicin-3 derivative N1,190766,36105
BMRB,36107,Solution structure of arenicin-3 derivative N2,190766,36105
PDB,5Y0H,BMRB Entry Tracking System,190766,36105
BMRB,50319,ABD2 peptide,214910,50317
BMRB,36107,Solution structure of arenicin-3 derivative N2,190783,36106
PDB,5Y0I,BMRB Entry Tracking System,190783,36106
BMRB,36105,Solution structure of arenicin-3 derivative N6,190800,36107
BMRB,36106,Solution structure of arenicin-3 derivative N1,190800,36107
PDB,5Y0J,BMRB Entry Tracking System,190800,36107
BMRB,36110,NMR-Based Model of the 22 Amino Acid Peptide in Polysialyltransferase Domain (PSTD) of the Polysialyltransferase ST8Sia IV in the Presence of Polysialic Acid (PolySia),190817,36109
PDB,5Y22,BMRB Entry Tracking System,190817,36109
BMRB,36109,NMR-Based Model of the 22 Amino Acid Peptide in Polysialyltransferase Domain (PSTD) of the Polysialyltransferase ST8Sia IV,190834,36110
PDB,5Y3U,BMRB Entry Tracking System,190834,36110
PDB,5Y4B,BMRB Entry Tracking System,190851,36111
PDB,5Y70,BMRB Entry Tracking System,190870,36112
BMRB,36115,NMR structure of YAP1-2 WW2 domain with LATS1 PPxY motif complex,190886,36114
PDB,5YDX,BMRB Entry Tracking System,190886,36114
BMRB,36114,NMR structure of YAP1-2 WW1 domain with LATS1 PPxY motif complex,190904,36115
PDB,5YDY,BMRB Entry Tracking System,190904,36115
PDB,5YEY,BMRB Entry Tracking System,190922,36116
PDB,5YFG,BMRB Entry Tracking System,190941,36117
PDB,5YI4,BMRB Entry Tracking System,190963,36119
PDB,5YKK,BMRB Entry Tracking System,190982,36124
PDB,5YKL,BMRB Entry Tracking System,190998,36125
PDB,5YKQ,BMRB Entry Tracking System,191014,36126
PDB,5YQ3,,191030,36129
PDB,6IJQ,,191051,36133
PDB,5YXI,,191069,36136
PDB,5YZ6,,191084,36142
PDB,5YZ9,,191106,36143
PDB,5Z17,,191124,36144
PDB,5Z1Y,,191140,36146
BMRB,36148,"solution structure of G2,7,13A SMAP-18 analogue",191157,36147
PDB,5Z26,,191157,36147
BMRB,36147,solution structure of SMAP-18,191174,36148
PDB,5Z2O,,191174,36148
BMRB,36150,LPS bound solution NMR structure of WS2-VR18,191191,36149
PDB,5Z31,,191191,36149
BMRB,36149,LPS bound solution structure of WS2-KG18,191207,36150
PDB,5Z32,,191207,36150
BMRB,36158,Nukacin ISK-1 in inactive state,191223,36157
PDB,5Z5Q,BMRB Entry Tracking System,191223,36157
BMRB,36157,Nukacin ISK-1 in active state,191240,36158
PDB,5Z5R,BMRB Entry Tracking System,191240,36158
BMRB,36160,Solution structure for the unique dimeric 4:2 complex of a platinum(II)-based tripod bound to a hybrid-1 human telomeric G-quadruplex,191257,36159
PDB,5Z80,BMRB Entry Tracking System,191257,36159
BMRB,36159,Solution structure for the 1:1 complex of a platinum(II)-based tripod bound to a hybrid-1 human telomeric G-quadruplex,191280,36160
PDB,5Z8F,,191280,36160
PDB,5Z8I,,191305,36161
PDB,5Z8Q,,191322,36162
PDB,5Z9C,BMRB Entry Tracking System,191339,36163
PDB,5ZAZ,,191359,36165
PDB,5ZC6,,191381,36166
PDB,5ZCN,,191401,36167
PDB,5ZEV,,191419,36168
BMRB,36171,NMR structure of IRD12 from Capsicum annum,191437,36170
PDB,5ZFN,,191437,36170
BMRB,36170,NMR structure of IRD7 from Capsicum annum,191455,36171
PDB,5ZFO,,191455,36171
PDB,5ZGG,,191474,36172
PDB,5ZLD,,191493,36174
PDB,5ZMB,,191513,36175
PDB,5ZMR,,191529,36176
PDB,5ZNU,,191549,36177
PDB,5ZOR,,191566,36179
PDB,5ZPV,,191581,36180
PDB,5ZR0,BMRB Entry Tracking System,191596,36181
PDB,5ZUH,,191614,36185
BMRB,36187,Solution Structure of the DNA-Binding Domain of Rok,191629,36186
PDB,5ZUX,,191629,36186
BMRB,36186,Solution Structure of the DNA complex of the C-terminal Domain of Rok,191654,36187
PDB,5ZUZ,,191654,36187
PDB,6AHZ,,191687,36207
BMRB,36221,Solution structure of the Sigma-anti-sigma factor complex RsgI1N-SigI1C from Clostridium thermocellum,191705,36220
PDB,6IVS,,191705,36220
BMRB,36220,Solution structure of the N-terminal domain of the anti-sigma factor RsgI1 from Clostridium thermocellum,191720,36221
PDB,6IVU,,191720,36221
PDB,6J12,BMRB Entry Stacking System,191737,36228
PDB,6K59,,191754,36258
PDB,6K84,,191771,36263
PDB,6K8Q,,191790,36264
PDB,6KBO,,191808,36265
PDB,6KBV,,191825,36266
PDB,6KLM,,191842,36273
PDB,6KR8,,191858,36284
PDB,6KYN,,191884,36288
PDB,6LAG,,191903,36299
PDB,6LQZ,BMRB Entry Tracking System,191934,36309
PDB,6M3N,BMRB Entry Tracking System,191954,36320
PDB,6M56,BMRB Entry Tracking System,191974,36321
PDB,7BW5,BMRB Entry Tracking System,191997,36343
BMRB,4029,chemical shifts for the free Sex-Lethal protein,192533,4028
BMRB,4028,chemical shifts for the Sex-Lethal protein - RNA complex,192550,4029
BMRB,4096,"Atomic coordinates and additional dynamic and kinetic data for
  GMH4CO",192682,4038
BMRB,4041,chemical shifts for the calcium-bound form of SytI-C2A,192697,4039
BMRB,4039,Chemical shifts for the calcium-free form of SytI-C2A,192726,4041
BMRB,4053,SNS ternary complex form with Ca2+ and Thymidine-3'-5'-bisphosphate.,192904,4052
BMRB,4052,SNS free form.,192923,4053
BMRB,4050,"1H, 13C, and 15N chemical shifts for reduced rubredoxin",193123,4066
BMRB,4051,"1H, 13C, and 15N chemical shifts for oxidized rubredoxin",193123,4066
BMRB,4137,reduced form,193123,4066
BMRB,4073,Chemical Shift of Oxidized Human Ferredoxin,193257,4073
BMRB,5337,"Complete assignments of 1H, 13C and 15N Chemical Shifts for Oxidized Human Adrenodoxin (4-114)",193257,4073
BMRB,50320,ABD3 peptide,214910,50317
BMRB,4073,oxidized human ferredoxin,193281,4074
BMRB,4104,DNA complexed with the Antennapedia Homeodomain protein,193757,4103
BMRB,4103,uncomplexed 14mer DNA duplex,193773,4104
BMRB,4108,chemical shifts for CspA in the acid/urea denatured state,193828,4107
BMRB,4107,chemical shifts for CspA in the acid denatured state,193843,4108
BMRB,4116,homologous Immunity protein Im9,193986,4115
BMRB,4293,DNase domain of non cognate binding partner E9,193986,4115
BMRB,4352,Im9 bound DNase domain of non cognate binding partner E9,193986,4115
BMRB,7323,Colicin immunity protein IM2,193986,4115
BMRB,4115,homologous Immunity protein Im9 bound to DNase domain of colicin E9,194001,4116
BMRB,4293,DNase domain of non cognate binding partner E9,194001,4116
BMRB,4352,Im9 bound DNase domain of non cognate binding partner E9,194001,4116
BMRB,7323,Colicin immunity protein IM2,194001,4116
PDB,1A60,BMRB Entry Tracking System,194042,4120
BMRB,6535,Tag-OBD (131-259) - RPA32C complex,194149,4127
PDB,1Q80,BMRB Entry Tracking System,194177,4129
BMRB,4131,"1H, 13C, and 15N chemical shifts for Rat Ferrocytochrome b5, B conformation",194210,4130
BMRB,4130,"1H, 13C, and 15N chemical shifts for rat ferrocytochrome b5, A conformation",194226,4131
BMRB,7080,Complex of TM1a(1-14)Zip with TM9a(251-284),194257,4133
BMRB,4107,denatured state assignments of a protein belonging to the OB-fold superfamily,194270,4134
BMRB,4108,denatured state assignments of a protein belonging to the OB-fold superfamily,194270,4134
BMRB,4050,"1H, 13C, and 15N chemical shifts for reduced rubredoxin",194324,4137
BMRB,4051,"1H, 13C, and 15N chemical shifts for oxidized rubredoxin",194324,4137
BMRB,4137,reduced form,194324,4137
BMRB,4151,pH 8.0 chemical shift assignments,194480,4146
BMRB,4146,pH5.0 structure,194574,4151
BMRB,4143,Neural Cell Adhesion Molecule module 2,194780,4162
BMRB,4169,free form of Pyoverdin G4R,194811,4164
BMRB,4167,C2A/Ca2+/6PS complex,194855,4166
BMRB,4166,C2A-Ca2+ complex,194874,4167
BMRB,4164,complex form of Pyoverdin G4R with Gallium,194909,4169
PDB,1BN9,BMRB Entry Tracking System,194980,4172
PDB,1BN0,BMRB Entry Tracking System,195044,4175
PDB,1BJD,BMRB Entry Tracking System,195060,4176
BMRB,4180,Loop peptide from the peripheral subunit-binding domain,195100,4179
BMRB,4179,helix1 from the peripheral subunit-binding domain,195129,4180
BMRB,4182,rubredoxin,195145,4181
PDB,1PFD,BMRB Entry Tracking System,195145,4181
BMRB,4181,ferredoxin,195166,4182
PDB,1EH2,BMRB Entry Tracking System,195197,4184
PDB,1SKP,BMRB Entry Tracking System,195266,4187
PDB,1BH1,BMRB Entry Tracking System,195411,4194
PDB,1A3P,BMRB Entry Tracking System,195550,4201
PDB,1BHI,BMRB Entry Tracking System,195866,4216
PDB,1BHU,BMRB Entry Tracking System,195879,4217
BMRB,4260,,195907,4219
BMRB,4261,,195907,4219
PDB,1BKU,BMRB Entry Tracking System,195907,4219
PDB,1TBA,BMRB Entry Tracking System,195992,4223
PDB,1LDZ,BMRB Entry Tracking System,196046,4226
BMRB,4227,the N-terminal fragment (residues 1-78),196086,4228
PDB,1BUQ,BMRB Entry Tracking System,196133,4230
BMRB,5702,"H, C and N chemical shifts by a different group",196193,4233
PDB,1BWT,BMRB Entry Tracking System,196229,4235
PDB,1C11,BMRB Entry Tracking System,196375,4243
BMRB,4235,DNA decamer,196399,4244
PDB,2V1V,BMRB Entry Tracking System,196442,4246
PDB,3PHP,BMRB Entry Tracking System,196544,4250
BMRB,4254,Mbp1 in its free form,196649,4256
BMRB,4219,,196733,4260
BMRB,4261,,196733,4260
PDB,1BYV,BMRB Entry Tracking System,196733,4260
BMRB,4219,,196753,4261
BMRB,4260,,196753,4261
BMRB,2498,,197072,4278
BMRB,4011,,197072,4278
PDB,1K2H,BMRB Entry Tracking System,197255,4285
BMRB,4115,homologous Immunity protein Im9 bound to DNase domain of colicin E9,197408,4293
BMRB,4116,homologous Immunity protein Im9,197408,4293
BMRB,4352,Im9 bound DNase domain of non cognate binding partner E9,197408,4293
BMRB,7323,Colicin immunity protein IM2,197408,4293
BMRB,4075,,197507,4297
PDB,2F63,BMRB Entry Tracking System,197540,4299
BMRB,4299,apo-HPPK,197568,4300
BMRB,7103,H98S mutant,197810,4313
BMRB,4320,dipolar coupling data of the reduced form.,197943,4319
BMRB,4050,chemical shift data of the reduced form.,197943,4319
BMRB,4051,chemical shift data of the oxidized form.,197943,4319
BMRB,4319,dipolar coupling data of the oxidized form.,197982,4320
BMRB,4050,chemical shift data of the reduced form.,197982,4320
BMRB,4051,chemical shift data of the oxidized form.,197982,4320
BMRB,4298,V3 loop peptide of RF HIV-1 gp120 envelope protein,198023,4322
BMRB,4325,dimeric form of B-domain of Staphyococcal Protein A,198054,4324
BMRB,4324,monomer,198071,4325
PDB,1KQQ,BMRB Entry Tracking System,198233,4334
BMRB,4337,,198274,4336
BMRB,4338,,198274,4336
BMRB,4336,,198298,4337
BMRB,4338,,198298,4337
BMRB,4336,,198319,4338
BMRB,4337,,198319,4338
BMRB,4315,Oxidized Fe-superoxide Dismutase,198407,4341
BMRB,4346,,198495,4345
BMRB,4345,,198516,4346
PDB,1QP6,BMRB Entry Tracking System,198533,4347
PDB,1QGM,BMRB Entry Tracking System,198631,4351
BMRB,4115,homologous Immunity protein Im9 bound to DNase domain of colicin E9,198648,4352
BMRB,4116,homologous Immunity protein Im9,198648,4352
BMRB,4293,DNase domain of non cognate binding partner E9,198648,4352
BMRB,7323,Colicin immunity protein IM2,198648,4352
BMRB,4362,zinc-complex,198821,4361
BMRB,4361,cobalt-complex,198845,4362
BMRB,4365,complex with PNU-107859,198893,4364
BMRB,4366,complex with PNU-142372,198893,4364
BMRB,4364,complex with PNU-99533,198912,4365
BMRB,4366,complex with PNU-142372,198912,4365
BMRB,4364,complex with PNU-99533,198933,4366
BMRB,4365,complex with PNU-107859,198933,4366
BMRB,4076,wild-type assignments,198954,4367
PDB,1C32,BMRB Entry Tracking System,199071,4372
PDB,1C34,BMRB Entry Tracking System,199071,4372
BMRB,15047,chemical shifts of denatured ubiquitin,199119,4375
BMRB,1520,"Partially Denatured State of a Protein by Two-Dimensional NMR: 
Reduction of the Hydrophobic Interactions in Ubiquitin",199119,4375
BMRB,2573,Fast Internal Main-Chain Dynamics of Human Ubiquitin,199119,4375
BMRB,2574,Fast Internal Main-Chain Dynamics of Human Ubiquitin,199119,4375
BMRB,68,"Sequential 1H NMR Assignments and Secondary Structure Identification of 
Human Ubiquitin",199119,4375
PDB,1CYZ,,199465,4392
BMRB,5214,Y2 selective analogue-I of neuropeptide Y,199569,4398
BMRB,5215,Y2 selective analogue-II of neuropeptide Y,199569,4398
BMRB,5216,Y2 selective analogue-III of neuropeptide Y,199569,4398
PDB,1QFA,BMRB Entry Tracking System,199569,4398
PDB,1B4Y,BMRB Entry Tracking System,199626,4400
PDB,1KHM,BMRB Entry Tracking System,199745,4405
BMRB,4408,minor form,199758,4406
PDB,1QFB,BMRB Entry Tracking System,199758,4406
PDB,1QL5,,199890,4412
PDB,1COK,BMRB Entry Tracking System,199907,4413
PDB,1COC,BMRB Entry Tracking System,199982,4416
BMRB,4419,,200030,4418
BMRB,4418,,200056,4419
PDB,1CCV,BMRB Entry Tracking System,200124,4422
PDB,1QKY,BMRB Entry Tracking System,200243,4427
BMRB,4433,glycine receptor alpha 1 subunit TM2 segment S267Y mutant,200375,4432
BMRB,5607,Human Neuronal Glycine Receptor alpha-1 Chain TM2,200375,4432
BMRB,4432,glycine receptor alpha 1 subunit TM2 segment native sequence,200397,4433
BMRB,5607,Human Neuronal Glycine Receptor alpha-1 Chain TM2,200397,4433
BMRB,4402,human prion protein hPrP(23-230),200419,4434
BMRB,4459,Oxidized Bacteriophage T4 Glutaredoxin,200993,4458
BMRB,4458,Reduced Bacteriophage T4 Glutaredoxin,201008,4459
BMRB,6534,RPA32C (172-270) -Tag-OBD (131-259),201023,4460
PDB,1DF6,BMRB Entry Tracking System,201062,4461
BMRB,4406,,201133,4464
BMRB,4408,,201133,4464
BMRB,4468,,201133,4464
BMRB,4280,,201192,4467
BMRB,4406,,201229,4468
BMRB,4408,,201229,4468
BMRB,4464,,201229,4468
BMRB,4777,chemical shift assignments for the oxidized cytochrome c552,201293,4471
BMRB,5079,relaxation data of reduced cytochrome c552,201293,4471
BMRB,5080,relaxation data of oxidized cytochrome c552,201293,4471
PDB,1CR8,BMRB Entry Tracking System,201372,4475
BMRB,4477,SER 15 and 21 phosphorylated,201389,4476
PDB,1B4G,BMRB Entry Tracking System,201389,4476
BMRB,4476,SER 8 phosphorylated,201404,4477
PDB,1CE3,BMRB Entry Tracking System,201476,4487
PDB,1QJT,BMRB Entry Tracking System,201538,4491
PDB,1UD7,BMRB Entry Tracking System,201574,4493
PDB,1CL4,BMRB Entry Tracking System,201669,4498
BMRB,5262,The first fibronectin type II module of MMP-2 (col-1),201829,4510
PDB,1CXW,BMRB Entry Tracking System,201829,4510
PDB,1D2L,BMRB Entry Tracking System,201861,4514
PDB,1D5G,BMRB Entry Tracking System,201886,4516
BMRB,4528,phosphorylated form,202021,4527
BMRB,4527,phosphorylated form,202040,4528
PDB,1DGO,BMRB Entry Tracking System,202079,4536
PDB,1NLA,BMRB Entry Tracking System,202115,4540
PDB,1QTG,BMRB Entry Tracking System,202115,4540
PDB,1QUZ,BMRB Entry Tracking System,202128,4541
PDB,1QE7,BMRB Entry Tracking System,202146,4542
PDB,1C2Q,BMRB Entry Tracking System,202168,4547
PDB,1CQO,BMRB Entry Tracking System,202211,4550
BMRB,5938,CP-11in DPC micelles,202247,4552
BMRB,5941,cycloCP-11,202247,4552
BMRB,4379,Entry 4379 is human prion protein fragment 121-230,202534,4563
BMRB,5909,Sso7d monomer,202703,4570
BMRB,5910,Sso7d V30I mutant,202703,4570
PDB,1ED0,BMRB Entry Tracking System,203066,4587
PDB,1EHX,BMRB Entry Tracking System,203112,4589
BMRB,4592,complex state with PIP2,203170,4591
BMRB,4591,free non-complex state,203189,4592
BMRB,4596,P26 in Trifluroethanol,203232,4595
BMRB,4597,P26 in H2O,203232,4595
BMRB,4598,P25 in H2O,203232,4595
BMRB,4595,P25 in Trifluroethanol,203250,4596
BMRB,4597,P26 in H2O,203250,4596
BMRB,4598,P25 in H2O,203250,4596
BMRB,4595,P25 in Trifluroethanol,203268,4597
BMRB,4596,P26 in Trifluroethanol,203268,4597
BMRB,4598,P25 in H2O,203268,4597
BMRB,4595,P25 in Trifluroethanol,203286,4598
BMRB,4596,P26 in Trifluroethanol,203286,4598
BMRB,4597,P26 in H2O,203286,4598
PDB,1EMQ,BMRB Entry Tracking System,203475,4609
PDB,1EVM,BMRB Entry Tracking System,203507,4610
PDB,1EVO,BMRB Entry Tracking System,203526,4612
PDB,1F5G,BMRB Entry Tracking System,203544,4614
PDB,1DXN,BMRB Entry Tracking System,203609,4618
PDB,1E4U,BMRB Entry Tracking System,203669,4621
PDB,1E5C,BMRB Entry Tracking System,203697,4623
PDB,1FYJ,BMRB Entry Tracking System,203809,4634
PDB,1FA3,BMRB Entry Tracking System,203877,4638
BMRB,4939,ninth zinc-finger domain of the u-shaped transcription factor,203993,4644
PDB,1FYI,BMRB Entry Tracking System,204033,4646
BMRB,5405,Same protein in TFE/D2O solution.,204128,4650
PDB,1G04,BMRB Entry Tracking System,204128,4650
PDB,1EDX,BMRB Entry Tracking System,204157,4652
PDB,1G26,BMRB Entry Tracking System,204217,4656
PDB,1C3T,BMRB Entry Tracking System,204265,4663
BMRB,4682,holo CRBP-II,204549,4681
BMRB,4681,apo CRBP-II,204571,4682
BMRB,25029,assignments based on new series of NMR spectra,204696,4689
BMRB,5158,"apomyoglobin N132G,E136G mutant",204776,4695
BMRB,7088,IF2 domain III-IV,204806,4697
PDB,1D1N,BMRB Entry Tracking System,204806,4697
BMRB,2525,,204892,4701
BMRB,4099,second component of the complex,204914,4702
BMRB,4705,2FXb-BCX,204957,4704
PDB,1CX1,BMRB Entry Tracking System,204974,4706
BMRB,4708,WT1-KTS/DNA complex,204998,4707
BMRB,4709,WT1+KTS/free,204998,4707
BMRB,4710,WT1+KTS/DNA complex,204998,4707
BMRB,4707,WT1-KTS/DNA free,205025,4708
BMRB,4709,WT1+KTS/free,205025,4708
BMRB,4710,WT1+KTS/DNA complex,205025,4708
BMRB,4707,WT1-KTS/free,205054,4709
BMRB,4708,WT1-KTS/DNA complex,205054,4709
BMRB,4710,WT1+KTS/DNA complex,205054,4709
BMRB,4707,WT1-KTS/free,205095,4710
BMRB,4708,WT1-KTS/DNA complex,205095,4710
BMRB,4709,WT1+KTS/free,205095,4710
BMRB,15179,Inhibitor-2 residues 9 - 164,205311,4720
BMRB,4724,basic form,205364,4723
BMRB,4723,acidic form,205385,4724
BMRB,4733,bulge DNA,205551,4732
BMRB,4734,HMG-D protein - bulge DNA complex,205551,4732
BMRB,4732,free HMG-D protein,205571,4733
BMRB,4734,HMG-D protein - bulge DNA complex,205571,4733
BMRB,4732,free HMG-D protein,205593,4734
BMRB,4733,free bulge DNA,205593,4734
PDB,1K8S,BMRB Entry Tracking System,205887,4745
BMRB,4753,zinc complex,205903,4746
BMRB,4746,cobalt complex,206126,4753
PDB,1J5L,BMRB Entry Tracking System,206155,4754
BMRB,4527,Chemical shifts of NtrC wild type,206308,4762
BMRB,4528,Chemical shifts of NtrC phosporylated,206308,4762
BMRB,4763,Relaxation data of NtrCr double mutant (D86N/A89T),206308,4762
BMRB,4764,Relaxation data of NtrCr wt phosporylated,206308,4762
BMRB,4527,Chemical shifts of NtrC wild type,206329,4763
BMRB,4528,Chemical shifts of NtrC phosporylated,206329,4763
BMRB,4762,Relaxation data of NtrCr wild type,206329,4763
BMRB,4764,Relaxation data of NtrCr wt phosporylated,206329,4763
BMRB,6258,TolAIII in complex with g3pN1,206477,4771
BMRB,4076,Outer Surface Protein A,206514,4773
BMRB,4471,chemical shift assignments for the reduced cytochrome c552,206580,4777
BMRB,5079,relaxation data of reduced cytochrome c552,206580,4777
BMRB,5080,relaxation data of oxidized cytochrome c552,206580,4777
BMRB,4770,GDP-loaded Cdc42,206617,4778
PDB,1F6U,BMRB Entry Tracking System,206671,4780
BMRB,4786,BRP complexed to Bleomycin,206767,4785
BMRB,4785,BRP,206783,4786
PDB,1JR6,BMRB Entry Tracking System,206929,4791
BMRB,4795,human D187N gelsolin domain 2,207008,4794
BMRB,4794,wild type Gelsolin,207027,4795
BMRB,4801,oxidized form,207156,4800
BMRB,4800,reduced form,207181,4801
BMRB,4804,cyt b5 N17D red,207226,4803
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207226,4803
BMRB,4806,cyt b5 oxid,207226,4803
BMRB,4807,cyt b5 N17D oxid,207226,4803
BMRB,4808,cyt b5 red - cyt c red complex,207226,4803
BMRB,4809,cyt b5 N17D red - cyt c red complex,207226,4803
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207226,4803
BMRB,4803,cyt b5 red,207248,4804
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207248,4804
BMRB,4806,cyt b5 oxid,207248,4804
BMRB,4807,cyt b5 N17D oxid,207248,4804
BMRB,4808,cyt b5 red - cyt c red complex,207248,4804
BMRB,4809,cyt b5 N17D red - cyt c red complex,207248,4804
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207248,4804
BMRB,4803,cyt b5 red,207270,4805
BMRB,4804,cyt b5 N17D red,207270,4805
BMRB,4806,cyt b5 oxid,207270,4805
BMRB,4807,cyt b5 N17D oxid,207270,4805
BMRB,4808,cyt b5 red - cyt c red complex,207270,4805
BMRB,4809,cyt b5 N17D red - cyt c red complex,207270,4805
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207270,4805
BMRB,4803,cyt b5 red,207295,4806
BMRB,4804,cyt b5 N17D red,207295,4806
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207295,4806
BMRB,4807,cyt b5 N17D oxid,207295,4806
BMRB,4808,cyt b5 red - cyt c red complex,207295,4806
BMRB,4809,cyt b5 N17D red - cyt c red complex,207295,4806
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207295,4806
BMRB,4803,cyt b5 red,207317,4807
BMRB,4804,cyt b5 N17D red,207317,4807
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207317,4807
BMRB,4806,cyt b5 oxid,207317,4807
BMRB,4808,cyt b5 red - cyt c red complex,207317,4807
BMRB,4809,cyt b5 N17D red - cyt c red complex,207317,4807
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207317,4807
BMRB,4803,cyt b5 red,207339,4808
BMRB,4804,cyt b5 N17D red,207339,4808
BMRB,4806,cyt b5 oxid,207339,4808
BMRB,4807,cyt b5 N17D oxid,207339,4808
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207339,4808
BMRB,4809,cyt b5 N17D red - cyt c red complex,207339,4808
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207339,4808
BMRB,4803,cyt b5 red,207364,4809
BMRB,4804,cyt b5 N17D red,207364,4809
BMRB,4806,cyt b5 oxid,207364,4809
BMRB,4807,cyt b5 N17D oxid,207364,4809
BMRB,4808,cyt b5 red - cyt c red complex,207364,4809
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207364,4809
BMRB,4810,cyt b5 oxid - cyt c oxid complex,207364,4809
BMRB,4803,cyt b5 red,207402,4810
BMRB,4804,cyt b5 N17D red,207402,4810
BMRB,4806,cyt b5 oxid,207402,4810
BMRB,4807,cyt b5 N17D oxid,207402,4810
BMRB,4808,cyt b5 red - cyt c red complex,207402,4810
BMRB,4809,cyt b5 N17D red - cyt c red complex,207402,4810
BMRB,4805,cyt b5 N17D oxid - cyt c oxid complex,207402,4810
BMRB,4332,,207427,4811
BMRB,4419,,207494,4815
PDB,1JO7,BMRB Entry Tracking System,207514,4816
BMRB,4823,holo form,207640,4822
BMRB,4824,complex with Troponin I peptide,207640,4822
BMRB,4822,apo form,207652,4823
BMRB,4824,complex with Troponin I peptide,207652,4823
BMRB,4822,apo form,207666,4824
BMRB,4823,holo form,207666,4824
BMRB,4828,P25S variant,207705,4827
BMRB,4827,wild type,207723,4828
BMRB,5457,assignment of SID24 in complex with PAH2 domain of mSin3B,208009,4841
BMRB,5808,PAH2 domain of mSin3B with SID24 complex,208009,4841
BMRB,4420,alpha-conotoxin Im1,208086,4845
BMRB,4846,alpha-conotoxin Im1(R7L),208086,4845
BMRB,4847,alpha-conotoxin Im1(D5N),208086,4845
BMRB,4420,alpha-conotoxin Im1,208102,4846
BMRB,4845,alpha-conotoxin Im1(R11E),208102,4846
BMRB,4847,alpha-conotoxin Im1(D5N),208102,4846
PDB,1E75,BMRB Entry Tracking System,208102,4846
BMRB,4420,alpha-conotoxin Im1,208117,4847
BMRB,4845,alpha-conotoxin Im1(R11E),208117,4847
BMRB,4846,alpha-conotoxin Im1(R7L),208117,4847
PDB,1E76,BMRB Entry Tracking System,208117,4847
BMRB,4854,N-terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase,208132,4848
BMRB,5689,Pheromone-binding protein from Antheraea polyphemus,208147,4849
BMRB,6313,Pheromone-binding Protein fragment BmPBP(1-128),208147,4849
BMRB,4848,N-terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase in the presence of substrate,208259,4854
BMRB,2169,,208281,4855
PDB,1F8P,BMRB Entry Tracking System,208421,4862
PDB,1FVN,BMRB Entry Tracking System,208421,4862
BMRB,4865,complex form,208459,4864
BMRB,4864,free form,208472,4865
BMRB,2169,,208531,4868
BMRB,4855,,208531,4868
BMRB,15930,4 sigma70,208578,4870
PDB,1FMH,BMRB Entry Tracking System,208636,4872
BMRB,2169,(5-55)Ser BPTI folding intermediate,208657,4873
BMRB,4855,"(14-38, 30-51)Ser BPTI folding intermediate",208657,4873
BMRB,4868,BPTI-R52,208657,4873
BMRB,4875,"(30-51, 5-14)Ser BPTI folding intermediate",208657,4873
BMRB,4877,"(30-51, 5-38)Ser BPTI folding intermediate",208657,4873
BMRB,2169,(5-55)Ser BPTI folding intermediate,208708,4875
BMRB,4855,"(14-38, 30-51)Ser BPTI folding intermediate",208708,4875
BMRB,4868,BPTI-R52,208708,4875
BMRB,4873,(30-51)Ser BPTI folding intermediate,208708,4875
BMRB,4877,"(30-51, 5-38)Ser BPTI folding intermediate",208708,4875
BMRB,4883,Ca2+-free state of Canine Milk Lysozyme at 20 deg,208730,4876
BMRB,4887,Ca2+-bound state of Canine Milk Lysozyme at 20 deg,208730,4876
BMRB,2169,(5-55)Ser BPTI folding intermediate,208745,4877
BMRB,4855,"(14-38, 30-51)Ser BPTI folding intermediate",208745,4877
BMRB,4868,BPTI-R52,208745,4877
BMRB,4873,(30-51)Ser BPTI folding intermediate,208745,4877
BMRB,4875,"(30-51, 5-14)Ser BPTI folding intermediate",208745,4877
PDB,1IJA,BMRB Entry Tracking System,208788,4879
BMRB,376,Megasphaera elsdenii flavodoxin in the reduced state,208858,4881
BMRB,1379,Megasphaera elsdenii flavodoxin in the oxidized state,208858,4881
BMRB,4886,Azotobacter vinelandii C69A apoflavodoxin,208858,4881
BMRB,4876,Ca2+-bound state of Canine Milk Lysozyme at 30 deg,208902,4883
BMRB,4887,Ca2+-bound state of Canine Milk Lysozyme at 20 deg,208902,4883
BMRB,376,,208966,4886
BMRB,1379,,208966,4886
BMRB,4881,,208966,4886
BMRB,4876,Ca2+-bound state of Canine Milk Lysozyme at 30 deg,208990,4887
BMRB,4883,Ca2+-free state of Canine Milk Lysozyme at 20 deg,208990,4887
BMRB,4889,c-Src SH3 RLP2 peptide complex,209005,4888
BMRB,4888,c-Src SH3 monomer,209019,4889
PDB,1G6M,BMRB Entry Tracking System,209071,4891
PDB,1EKZ,BMRB Entry Tracking System,209127,4894
PDB,1HEH,BMRB Entry Tracking System,209301,4900
PDB,1HEJ,BMRB Entry Tracking System,209301,4900
PDB,1HDL,BMRB Entry Tracking System,209514,4910
BMRB,4912,free form,209533,4911
BMRB,4911,complex with NNOS (fragment peptide),209560,4912
PDB,1G92,BMRB Entry Tracking System,209754,4921
PDB,1G9P,BMRB Entry Tracking System,209809,4923
PDB,1HP2,BMRB Entry Tracking System,209823,4924
PDB,1N02,BMRB Entry Tracking System,209874,4927
BMRB,4233,1H Chemical Shift Assignments for Omega-Atracotoxin-Hv1a,210109,4937
PDB,1JJR,BMRB Entry Tracking System,210196,4941
BMRB,4947,complexed with aromatized chromophore,210312,4946
BMRB,4946,free form,210328,4947
BMRB,4195,Alpha-Bungaratoxin/Library Peptide Complex,210346,4948
BMRB,5988,alpha-bungarotoxin,210346,4948
BMRB,975,Sequential Assignment of the 1H NMR of Barnase,210707,4964
BMRB,7308,L11 - RNA (- Thiostrepton) complex,210736,4965
BMRB,7307,L11 - RNA complex,210736,4965
BMRB,5513,Free L11 of Thermotoga maritima,210736,4965
BMRB,5307,Time domain data of BPTI at pH 5.8,210807,4968
BMRB,5757,Crh dimer,210963,4972
BMRB,4820,Pheromone Er-22 Luginbuhl,211125,4979
PDB,1HA8,BMRB Entry Tracking System,211125,4979
PDB,1KOS,BMRB Entry Tracking System,211273,4984
BMRB,4987,maltose bound form,211320,4986
BMRB,4986,ligand-free state,211340,4987
PDB,1ILO,BMRB Entry Tracking System,211442,4991
BMRB,4601,Solution structure of the channel-former Zervamicin IIB (peptaibol antibiotic),211484,4993
BMRB,4604,NMR Structure of the Peptaibol Chrysospermin C Bound to DPC Micelles,211484,4993
PDB,1IH9,BMRB Entry Tracking System,211484,4993
PDB,1IH0,BMRB Entry Tracking System,211508,4994
BMRB,27990,apo ARR_CleD,211747,50001
BMRB,50011,rsFolder off state,211853,50010
BMRB,50010,rsFolder on state,211869,50011
PDB,5du0,"rsFolder non-fluorescent ""off"" state",211869,50011
BMRB,50013,IMP13 metallo beta-lactamase bound to hydrolysed ertapenem,211884,50012
BMRB,50012,IMP13 metallo beta-lactamase (apo-state),211898,50013
BMRB,17549,chemical shift assignment of the vWFA2 domain,211962,50020
PDB,6S4C,Crystal structure of the vWFA2 domain,211962,50020
EMBL,P9WKD7,,212033,50025
PDB,1USL,,212033,50025
PDB,6T33,RUMC1,212062,50027
BMRB,5005,oxidized form,212090,5003
BMRB,50031,CDC25B; R482A mutant,212095,50030
BMRB,50032,CDC25B; R544A mutant,212095,50030
BMRB,50033,CDC25B; W550A mutant,212095,50030
BMRB,50030,CDC25B; wild type,212108,50031
BMRB,50032,CDC25B; R544A mutant,212108,50031
BMRB,50033,CDC25B; W550A mutant,212108,50031
BMRB,50030,CDC25B; wild type,212121,50032
BMRB,50031,CDC25B; R482A mutant,212121,50032
BMRB,50033,CDC25B; W550A mutant,212121,50032
BMRB,50030,CDC25B; wild type,212134,50033
BMRB,50031,CDC25B; R482A mutant,212134,50033
BMRB,50032,CDC25B; R544A mutant,212134,50033
BMRB,4843,"Chemical shift data for the same molecule reported by Byrd, et. al.",212147,5004
BMRB,5003,reduced form,212161,5005
BMRB,4948,,212184,5006
BMRB,5852,A mimic of the VS Ribozyme Hairpin Substrate,212199,5007
PDB,1HWQ,BMRB Entry Tracking System,212199,5007
PDB,1J6Q,BMRB Entry Tracking System,212199,5007
BMRB,50078,BRCA2 53-131,212258,50077
BMRB,50079,BRCA2 190-284,212258,50077
BMRB,50077,BRCA2 48-218(C4A),212271,50078
BMRB,50079,BRCA2 190-284,212271,50078
BMRB,50077,BRCA2 48-218(C4A),212284,50079
BMRB,50078,BRCA2 53-131,212284,50079
BMRB,5009,PA90 mutant,212297,5008
BMRB,5008,wild type,212359,5009
BMRB,50096,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212416,50095
BMRB,50097,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212416,50095
BMRB,50095,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212432,50096
BMRB,50097,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212432,50096
BMRB,50095,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212448,50097
BMRB,50096,"1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modifications",212448,50097
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212463,50098
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212463,50098
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212463,50098
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212463,50098
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212463,50098
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212463,50098
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212476,50099
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212476,50099
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212476,50099
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212476,50099
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212476,50099
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212476,50099
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212527,50100
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212527,50100
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212527,50100
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212527,50100
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212527,50100
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212527,50100
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212540,50101
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212540,50101
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212540,50101
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212540,50101
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212540,50101
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212540,50101
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212553,50102
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212553,50102
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212553,50102
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212553,50102
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212553,50102
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212553,50102
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212566,50103
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212566,50103
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212566,50103
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212566,50103
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212566,50103
BMRB,50105,Nipah virus phosphoprotein residues 588-650,212566,50103
BMRB,50106,human Grb2 N-terminal SH3 domain conjugated with Sos1-derived modified peptide,212579,50104
PDB,1GBQ,,212579,50104
BMRB,50098,Nipah virus phosphoprotein residues 1-100,212594,50105
BMRB,50099,Nipah virus phosphoprotein residues 91-190,212594,50105
BMRB,50100,Nipah virus phosphoprotein residues 173-240,212594,50105
BMRB,50101,Nipah virus phosphoprotein residues 223-319,212594,50105
BMRB,50102,Nipah virus phosphoprotein residues 299-401,212594,50105
BMRB,50103,Nipah virus phosphoprotein residues 387-479,212594,50105
BMRB,50104,human Grb2 N-terminal SH3 domain in complex with Sos1-derived peptide,212607,50106
PDB,1GBQ,,212607,50106
BMRB,34461,complex of the VPS29 and the VARP,212622,50107
BMRB,50108,free components (VARP 687-747),212622,50107
PDB,6TL0,complex of the VPS29 and the VARP,212622,50107
BMRB,34461,complex of the VPS29 and the VARP,212638,50108
BMRB,50107,free components (VPS29),212638,50108
PDB,6TL0,complex of the VPS29 and the VARP,212638,50108
BMRB,15412,Assignments for Snu13p,212692,50110
PDB,1ZWZ,,212692,50110
PDB,2ALE,,212692,50110
PDB,4NUT,,212692,50110
SP,P39990,,212692,50110
BMRB,50118,human STIM1 CC1 R304W mutant,212723,50114
BMRB,50114,"human STIM1 CC1 fragment, wild-type",212758,50118
BMRB,50120,EB1 linker-4D,212775,50119
PDB,1J7M,BMRB Entry Tracking System,212794,5012
BMRB,50119,EB1 linker-wt,212808,50120
BMRB,5823,RPA70(181-422) ssDNA binding domains,212827,50121
BMRB,28053,VDAC E73V mutant in MSP1D1 nanodiscs,212868,50125
BMRB,50130,Tau fragment (224-325) with P301L mutation,212960,50129
BMRB,50129,"Tau fragment (225-325), wild type",212993,50130
BMRB,12016,Solution SC Sup35NM,213006,50131
BMRB,50132,"Chimeric SC Sup35NM, 5MT-A",213006,50131
BMRB,50133,"Chimeric SC Sup35NM, 5MT-B",213006,50131
BMRB,50134,"Chimeric SC Sup35NM, 4MT-A",213006,50131
BMRB,12016,Solution SC Sup35NM,213019,50132
BMRB,50131,KL Sup35NM,213019,50132
BMRB,50133,"Chimeric SC Sup35NM, 5MT-B",213019,50132
BMRB,50134,"Chimeric SC Sup35NM, 4MT-A",213019,50132
BMRB,12016,Solution SC Sup35NM,213032,50133
BMRB,50131,KL Sup35NM,213032,50133
BMRB,50132,"Chimeric SC Sup35NM, 5MT-A",213032,50133
BMRB,50134,"Chimeric SC Sup35NM, 4MT-A",213032,50133
BMRB,12016,Solution SC Sup35NM,213045,50134
BMRB,50131,KL Sup35NM,213045,50134
BMRB,50132,"Chimeric SC Sup35NM, 5MT-A",213045,50134
BMRB,50133,"Chimeric SC Sup35NM, 5MT-B",213045,50134
BMRB,50123,KirBac1.1 in POPC:POPG micelle,213058,50135
PDB,1p7b,reported crystal structure for assigned protein (KirBac1.1),213058,50135
PDB,6P7A,Crystal Structure of Apo-Fpr,213132,50141
PDB,6P7B,Crystal Structure of Fpr-HJ complex,213132,50141
PDB,6a7f,Cryo-EM structure of filamentous bacteriophage IKe,213158,50152
BMRB,50160,"Point mutant of Oligosaccharyltransferase subunit, Ost4V23D",213208,50159
BMRB,50159,Oligosaccharyltransferase subunit Ost4p,213221,50160
BMRB,50162,hyen L,213236,50161
BMRB,50163,hyen E,213236,50161
BMRB,50164,hyen M,213236,50161
BMRB,50165,hyen C,213236,50161
BMRB,50161,hyen D,213249,50162
BMRB,50163,hyen E,213249,50162
BMRB,50164,hyen M,213249,50162
BMRB,50165,hyen C,213249,50162
BMRB,50161,hyen D,213262,50163
BMRB,50162,hyen L,213262,50163
BMRB,50164,hyen M,213262,50163
BMRB,50165,hyen C,213262,50163
BMRB,50161,hyen D,213275,50164
BMRB,50162,hyen L,213275,50164
BMRB,50163,hyen E,213275,50164
BMRB,50165,hyen C,213275,50164
BMRB,50161,hyen D,213288,50165
BMRB,50162,hyen L,213288,50165
BMRB,50163,hyen E,213288,50165
BMRB,50164,hyen M,213288,50165
BMRB,50173,Rab1b bound to GDP,213334,50172
BMRB,50174,Rab1b bound to GTP (AMPylation at Y77),213334,50172
BMRB,50175,Rab1b bound to GDP (AMPylation at Y77),213334,50172
BMRB,50176,Rab1b bound to GTP (Phosphocholination at S76),213334,50172
BMRB,50177,Rab1b bound to GDP (Phosphocholination at S76),213334,50172
BMRB,50172,Rab1b bound to GTP,213351,50173
BMRB,50174,Rab1b bound to GTP (AMPylation at Y77),213351,50173
BMRB,50175,Rab1b bound to GDP (AMPylation at Y77),213351,50173
BMRB,50176,Rab1b bound to GTP (Phosphocholination at S76),213351,50173
BMRB,50177,Rab1b bound to GDP (Phosphocholination at S76),213351,50173
BMRB,50172,Rab1b bound to GTP,213368,50174
BMRB,50173,Rab1b bound to GDP,213368,50174
BMRB,50175,Rab1b bound to GDP (AMPylation at Y77),213368,50174
BMRB,50176,Rab1b bound to GTP (Phosphocholination at S76),213368,50174
BMRB,50177,Rab1b bound to GDP (Phosphocholination at S76),213368,50174
BMRB,50172,Rab1b bound to GTP,213383,50175
BMRB,50173,Rab1b bound to GDP,213383,50175
BMRB,50174,Rab1b bound to GTP (AMPylation at Y77),213383,50175
BMRB,50176,Rab1b bound to GTP (Phosphocholination at S76),213383,50175
BMRB,50321,ABD2' peptide,214910,50317
BMRB,50177,Rab1b bound to GDP (Phosphocholination at S76),213383,50175
BMRB,50172,Rab1b bound to GTP,213398,50176
BMRB,50173,Rab1b bound to GDP,213398,50176
BMRB,50174,Rab1b bound to GTP (AMPylation at Y77),213398,50176
BMRB,50175,Rab1b bound to GDP (AMPylation at Y77),213398,50176
BMRB,50177,Rab1b bound to GDP (Phosphocholination at S76),213398,50176
BMRB,50172,Rab1b bound to GTP,213413,50177
BMRB,50173,Rab1b bound to GDP,213413,50177
BMRB,50174,Rab1b bound to GTP (AMPylation at Y77),213413,50177
BMRB,50175,Rab1b bound to GDP (AMPylation at Y77),213413,50177
BMRB,50176,Rab1b bound to GTP (Phosphocholination at S76),213413,50177
BMRB,50179,Cdc42 bound to GDP,213428,50178
BMRB,50180,Cdc42 bound to GTP (AMPylation at T35),213428,50178
BMRB,50181,Cdc42 bound to GDP (AMPylation at T35),213428,50178
BMRB,50182,Cdc42 bound to GTP (AMPylation at Y32),213428,50178
BMRB,50183,Cdc42 bound to GDP (AMPylation at Y32),213428,50178
BMRB,50178,Cdc42 bound to GTP,213443,50179
BMRB,50180,Cdc42 bound to GTP (AMPylation at T35),213443,50179
BMRB,50181,Cdc42 bound to GDP (AMPylation at T35),213443,50179
BMRB,50182,Cdc42 bound to GTP (AMPylation at Y32),213443,50179
BMRB,50183,Cdc42 bound to GDP (AMPylation at Y32),213443,50179
BMRB,50179,Cdc42 bound to GDP,213477,50180
BMRB,50180,Cdc42 bound to GTP,213477,50180
BMRB,50181,Cdc42 bound to GDP (AMPylation at T35),213477,50180
BMRB,50182,Cdc42 bound to GTP (AMPylation at Y32),213477,50180
BMRB,50183,Cdc42 bound to GDP (AMPylation at Y32),213477,50180
BMRB,50179,Cdc42 bound to GDP,213492,50181
BMRB,50180,Cdc42 bound to GTP (AMPylation at T35),213492,50181
BMRB,50181,Cdc42 bound to GTP,213492,50181
BMRB,50182,Cdc42 bound to GTP (AMPylation at Y32),213492,50181
BMRB,50183,Cdc42 bound to GDP (AMPylation at Y32),213492,50181
BMRB,50179,Cdc42 bound to GDP,213507,50182
BMRB,50180,Cdc42 bound to GTP (AMPylation at T35),213507,50182
BMRB,50181,Cdc42 bound to GDP (AMPylation at T35),213507,50182
BMRB,50182,Cdc42 bound to GTP,213507,50182
BMRB,50183,Cdc42 bound to GDP (AMPylation at Y32),213507,50182
BMRB,50179,Cdc42 bound to GDP,213522,50183
BMRB,50180,Cdc42 bound to GTP (AMPylation at T35),213522,50183
BMRB,50181,Cdc42 bound to GDP (AMPylation at T35),213522,50183
BMRB,50182,Cdc42 bound to GTP (AMPylation at Y32),213522,50183
BMRB,50183,Cdc42 bound to GTP,213522,50183
BMRB,50191,"RBM5 RRM1-Zf1, C191G mutant",213563,50187
BMRB,50187,"RBM5 RRM1-Zf1, wild type",213602,50191
PDB,5L6Q,,213618,50192
BMRB,4272,VAMP2(1-96) in solution,213645,50198
BMRB,50199,VAMP2(1-96) in HEK-293T Cells,213645,50198
BMRB,4272,VAMP2(1-96) in solution,213659,50199
BMRB,50198,VAMP2(1-96) in SH-SY5Y Cells,213659,50199
BMRB,4177,This entry was used to transfer NMR assignment,213785,50207
BMRB,50208,His6-tagged human chemokine CCL7,213785,50207
BMRB,4177,This entry was used to transfer NMR assignment,213800,50208
BMRB,50207,Native human chemokine CCL7,213800,50208
PDB,1I8E,BMRB Entry Tracking System,213815,5021
BMRB,50192,S3706 VL fibrils,213834,50211
PDB,5L6Q,,213834,50211
PDB,1YAX,CYSTAL STRUCTURE ANALYSIS OF S.TYPHIMURIUM PHOQ SENSOR DOMAIN WITH CALCIUM,213893,50214
BMRB,50228,kinetoplastid kinetochore protein KKT4 145-232,213906,50215
BMRB,50229,kinetoplastid kinetochore protein KKT4 115-343,213906,50215
BMRB,50219,Mfd RID,213939,50218
BMRB,50218,UvrD CTD,213953,50219
BMRB,25504,Backbone assignments for the same protein system,213990,50220
BMRB,50221,EF-GC3 from Staphylococcus aureus in apo form,213990,50220
PDB,2MZW,Structure of Staphylococcus aureus EF-G.,213990,50220
BMRB,25368,Backbone assignments for the same protein system,214008,50221
BMRB,50220,EF-GC3 from Staphylococcus aureus in complex with FusB,214008,50221
PDB,2XEX,Structure of Staphylococcus aureus EF-G.,214008,50221
BMRB,50215,kinetoplastid kinetochore protein KKT4 115-174,214023,50228
BMRB,50229,kinetoplastid kinetochore protein KKT4 115-343,214023,50228
BMRB,50215,kinetoplastid kinetochore protein KKT4 115-174,214041,50229
BMRB,50228,kinetoplastid kinetochore protein KKT4 145-232,214041,50229
PDB,1I4C,BMRB Entry Tracking System,214058,5023
BMRB,50243,protein kinase Inhibitor alpha (PKIa) free state,214089,50238
BMRB,50261,Vitronectin hemopexin-like domain with DHPC,214132,50241
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214149,50242
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214149,50242
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214149,50242
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214149,50242
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214149,50242
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214149,50242
BMRB,50238,protein kinase Inhibitor alpha (PKIa) bound to cAMP-dependent protein kinase A.,214164,50243
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214192,50244
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214192,50244
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214192,50244
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214192,50244
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214192,50244
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214192,50244
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214206,50245
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214206,50245
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214206,50245
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214206,50245
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214206,50245
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214206,50245
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214220,50246
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214220,50246
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214220,50246
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214220,50246
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214220,50246
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214220,50246
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214235,50247
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214235,50247
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214235,50247
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214235,50247
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214235,50247
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214235,50247
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214250,50248
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214250,50248
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214250,50248
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214250,50248
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214250,50248
BMRB,50249,[r(UGGUGGPs)]4 G-quadruplex,214250,50248
BMRB,50242,[r(UGGUGG)d(U)]4 G-quadruplex,214264,50249
BMRB,50244,[r(UGGUGG)(2'OMeU)]4 G-quadruplex,214264,50249
BMRB,50245,[r(UGGUGGC)]4 G-quadruplex,214264,50249
BMRB,50246,[r(UGGUGGT)]4 G-quadruplex,214264,50249
BMRB,50247,[r(UGGUGG)d(T)]4 G-quadruplex,214264,50249
BMRB,50248,[r(UGGUGG)(LNA-T)]4 G-quadruplex,214264,50249
PDB,5WB5,Crystal Structure of Leishmania IF4E-1 bound to Leishmania 4E-IP1,214304,50250
BMRB,50255,hnRNPA2 1-189 310K,214352,50254
BMRB,50257,hnRNPA2 1-189 bound to rA2RE11,214352,50254
BMRB,50254,hnRNPA2 1-189,214366,50255
BMRB,50257,hnRNPA2 1-189 bound to rA2RE11,214366,50255
BMRB,50254,hnRNPA2 1-189,214380,50257
BMRB,50255,hnRNPA2 1-189 310K,214380,50257
BMRB,50241,Vitronectin hemopexin-like domain with CaCl2 and DHPC,214435,50261
PDB,6WTK,X-ray structure,214450,50262
BMRB,50264,TREM2 transmembrane helix K186A variant,214466,50263
BMRB,50265,TREM2 transmembrane helix in complex with the partner protein DAP12,214466,50263
BMRB,50263,transmembrane helix of TREM2,214480,50264
BMRB,50265,TREM2 transmembrane helix in complex with the partner protein DAP12,214480,50264
BMRB,50263,transmembrane helix of TREM2,214494,50265
BMRB,50264,TREM2 transmembrane helix K186A variant,214494,50265
BMRB,50275,"globular CRES, in solid state",214583,50273
PDB,6UIO,X-ray crystal structure of CRES,214583,50273
BMRB,50273,"globular CRES, in solution state",214618,50275
PDB,1IB9,BMRB Entry Tracking System,214682,5028
BMRB,4279,Solution Structure of a beta-Neurotoxin,214700,5029
PDB,1CSM,ScCM R-state T226I variant crystallized with two Trp ligands bound,214714,50297
PDB,2CSM,ScCM Y-state structure crystallized with two Tyr ligands bound,214714,50297
PDB,3CSM,"ScCM ""Super R-state"" structure crystallized with two Trp ligands bound and two TSA ligands bound",214714,50297
PDB,4CSM,"ScCM ""Super R-state"" structure crystallized with two Tyt ligands bound and two TSA ligands bound",214714,50297
PDB,5CSM,"ScCM ""Super R-state"" structure, T226S variant, crystallized with two Trp ligands bound and two TSA ligands bound",214714,50297
PDB,3Q0Y,,214786,50300
BMRB,16587,Chemical shifts of a native-like folding intermediate of beta2-microglobulin,214815,50302
BMRB,19099,Wild type human Beta-2 microglobulin pH 7.5,214815,50302
BMRB,19118,Wild type human Beta-2 microglobulin bound to HLA,214815,50302
BMRB,19119,Wild type human Beta-2 microglobulin bound to HLA,214815,50302
BMRB,19121,Wild type human Beta-2 microglobulin bound to HLA,214815,50302
BMRB,25809,Wild type Beta-2 microglobulin W60G,214815,50302
BMRB,27437,"1H, 13CA, 13CB and 15N chemical shift assignments of b2-microglobulin and a-chain of the neonatal Fc receptor",214815,50302
BMRB,3079,Wild type human Beta-2 microglobulin,214815,50302
BMRB,5169,Wild type Beta-2 microglobulin,214815,50302
BMRB,5783,Wild type Beta-2 microglobulin,214815,50302
PDB,1JNJ,NMR solution structure of the human beta2-microglobulin,214815,50302
PDB,3EKC,structure of W60V beta-2 microglobulin mutant,214815,50302
PDB,3QDA,Crystal structure of W95L beta-2 microglobulin,214815,50302
PDB,4FXL,Crystal structure of the D76N Beta-2 Microglobulin mutant,214815,50302
PDB,4KDT,Structure of an early native-like intermediate of beta2-microglobulin amyloidosis,214815,50302
PDB,4L3C,Structure of HLA-A2 in complex with D76N b2m mutant and NY-ESO1 double mutant,214815,50302
PDB,4RMW,Crystal structure of the D76A Beta-2 Microglobulin mutant,214815,50302
PDB,5CS7,The crystal structure of wt beta2-microglobulin at room temperature,214815,50302
PDB,5CSB,The crystal structure of beta2-microglobulin D76N mutant at room temperature,214815,50302
PDB,6Z4A,"Structure of the human SAS-6 N-terminal domain, F131E mutant",214831,50308
BMRB,50316,ABD12 peptide,214884,50315
BMRB,50317,ABD13 peptide,214884,50315
BMRB,50318,ABD1 peptide,214884,50315
BMRB,50319,ABD2 peptide,214884,50315
BMRB,50320,ABD3 peptide,214884,50315
BMRB,50321,ABD2' peptide,214884,50315
BMRB,50322,ABD23ss peptide,214884,50315
BMRB,50323,ABD23ac peptide,214884,50315
BMRB,50315,ABD peptide,214897,50316
BMRB,50317,ABD13 peptide,214897,50316
BMRB,50318,ABD1 peptide,214897,50316
BMRB,50319,ABD2 peptide,214897,50316
BMRB,50320,ABD3 peptide,214897,50316
BMRB,50321,ABD2' peptide,214897,50316
BMRB,50322,ABD23ss peptide,214897,50316
BMRB,50323,ABD23ac peptide,214897,50316
BMRB,50315,ABD peptide,214910,50317
BMRB,50316,ABD12 peptide,214910,50317
BMRB,50318,ABD1 peptide,214910,50317
BMRB,50323,ABD23ac peptide,214910,50317
BMRB,50315,ABD peptide,214923,50318
BMRB,50316,ABD12 peptide,214923,50318
BMRB,50317,ABD13 peptide,214923,50318
BMRB,50319,ABD2 peptide,214923,50318
BMRB,50320,ABD3 peptide,214923,50318
BMRB,50321,ABD2' peptide,214923,50318
BMRB,50322,ABD23ss peptide,214923,50318
BMRB,50323,ABD23ac peptide,214923,50318
BMRB,50315,ABD peptide,214936,50319
BMRB,50316,ABD12 peptide,214936,50319
BMRB,50317,ABD13 peptide,214936,50319
BMRB,50318,ABD1 peptide,214936,50319
BMRB,50320,ABD3 peptide,214936,50319
BMRB,50321,ABD2' peptide,214936,50319
BMRB,50322,ABD23ss peptide,214936,50319
BMRB,50323,ABD23ac peptide,214936,50319
BMRB,4675,"1H, 13C and 15N resonance assignments of the DNA binding domain of AFX",214949,5032
BMRB,50315,ABD peptide,214970,50320
BMRB,50316,ABD12 peptide,214970,50320
BMRB,50317,ABD13 peptide,214970,50320
BMRB,50318,ABD1 peptide,214970,50320
BMRB,50319,ABD2 peptide,214970,50320
BMRB,50321,ABD2' peptide,214970,50320
BMRB,50322,ABD23ss peptide,214970,50320
BMRB,50323,ABD23ac peptide,214970,50320
BMRB,50315,ABD peptide,214983,50321
BMRB,50316,ABD12 peptide,214983,50321
BMRB,50317,ABD13 peptide,214983,50321
BMRB,50318,ABD1 peptide,214983,50321
BMRB,50319,ABD2 peptide,214983,50321
BMRB,50320,ABD3 peptide,214983,50321
BMRB,50322,ABD23ss peptide,214983,50321
BMRB,50323,ABD23ac peptide,214983,50321
BMRB,50315,ABD peptide,214996,50322
BMRB,50316,ABD12 peptide,214996,50322
BMRB,50317,ABD13 peptide,214996,50322
BMRB,50318,ABD1 peptide,214996,50322
BMRB,50319,ABD2 peptide,214996,50322
BMRB,50320,ABD3 peptide,214996,50322
BMRB,50321,ABD2' peptide,214996,50322
BMRB,50323,ABD23ac peptide,214996,50322
BMRB,50315,ABD peptide,215009,50323
BMRB,50316,ABD12 peptide,215009,50323
BMRB,50317,ABD13 peptide,215009,50323
BMRB,50318,ABD1 peptide,215009,50323
BMRB,50319,ABD2 peptide,215009,50323
BMRB,50320,ABD3 peptide,215009,50323
BMRB,50321,ABD2' peptide,215009,50323
BMRB,50322,ABD23ss peptide,215009,50323
PDB,1I2U,BMRB Entry Tracking System,215038,5033
PDB,1I2V,BMRB Entry Tracking System,215038,5033
BMRB,28056,Backbone assignments of the apo form of the solute binding protein PiuA,215056,50332
BMRB,28057,"Backbone assignments of the holo form of the solute binding protein PiuA, with Ga(III) 4-LICAM",215056,50332
BMRB,50333,Backbone relaxation rates for the solute binding protein PiuA bound to Ga(III) 4-LICAM,215056,50332
PDB,4JCC,Crystal structure of a close homolog,215056,50332
BMRB,28056,Backbone assignments of the apo form of the solute binding protein PiuA,215072,50333
BMRB,28057,Backbone assignments of the solute binding protein PiuA bound to Ga(III) 4-LICAM,215072,50333
BMRB,50332,Backbone relaxation rates for apo form of the solute binding protein PiuA,215072,50333
PDB,4JCC,Crystal structure of a close homolog,215072,50333
NCBI,YP_009725299.1,,215092,50334
BMRB,50340,chemical shifts of the 5_SL5stem,215143,50339
BMRB,50341,chemical shifts of the 3_s2m,215143,50339
BMRB,50342,chemical shifts of the 3_SL1,215143,50339
BMRB,50343,chemical shifts of the 2_SL3,215143,50339
BMRB,50344,chemical shifts of the 5_SL2+3,215143,50339
BMRB,50346,chemical shifts of the 5_SL5a,215143,50339
BMRB,50347,chemical shifts of the 5_SL4,215143,50339
BMRB,50348,chemical shifts of the PK (Pseudoknot),215143,50339
BMRB,50349,chemical shifts of the 5_SL1,215143,50339
BMRB,50350,chemical shifts of the 3_SL3base,215143,50339
BMRB,50351,chemical shifts of the 5_SL6,215143,50339
BMRB,50352,chemical shifts of the 5_SL8,215143,50339
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215143,50339
PDB,1HU6,BMRB Entry Tracking System,215159,5034
PDB,1HU7,BMRB Entry Tracking System,215159,5034
BMRB,50339,chemical shifts of the 5_SL5B+C,215177,50340
BMRB,50341,chemical shifts of the 3_s2m,215177,50340
BMRB,50342,chemical shifts of the 3_SL1,215177,50340
BMRB,50343,chemical shifts of the 2_SL3,215177,50340
BMRB,50344,chemical shifts of the 5_SL2+3,215177,50340
BMRB,50346,chemical shifts of the 5_SL5a,215177,50340
BMRB,50347,chemical shifts of the 5_SL4,215177,50340
BMRB,50348,chemical shifts of the PK (Pseudoknot),215177,50340
BMRB,50349,chemical shifts of the 5_SL1,215177,50340
BMRB,50350,chemical shifts of the 3_SL3base,215177,50340
BMRB,50351,chemical shifts of the 5_SL6,215177,50340
BMRB,50352,chemical shifts of the 5_SL8,215177,50340
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215177,50340
BMRB,50339,chemical shifts of the 5_SL5B+C,215194,50341
BMRB,50340,chemical shifts of the 5_SL5stem,215194,50341
BMRB,50342,chemical shifts of the 3_SL1,215194,50341
BMRB,50343,chemical shifts of the 2_SL3,215194,50341
BMRB,50344,chemical shifts of the 5_SL2+3,215194,50341
BMRB,50346,chemical shifts of the 5_SL5a,215194,50341
BMRB,50347,chemical shifts of the 5_SL4,215194,50341
BMRB,50348,chemical shifts of the PK (Pseudoknot),215194,50341
BMRB,50349,chemical shifts of the 5_SL1,215194,50341
BMRB,50350,chemical shifts of the 3_SL3base,215194,50341
BMRB,50351,chemical shifts of the 5_SL6,215194,50341
BMRB,50352,chemical shifts of the 5_SL8,215194,50341
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215194,50341
BMRB,50339,chemical shifts of the 5_SL5B+C,215209,50342
BMRB,50340,chemical shifts of the 5_SL5stem,215209,50342
BMRB,50341,chemical shifts of the 3_s2m,215209,50342
BMRB,50343,chemical shifts of the 2_SL3,215209,50342
BMRB,50344,chemical shifts of the 5_SL2+3,215209,50342
BMRB,50346,chemical shifts of the 5_SL5a,215209,50342
BMRB,50347,chemical shifts of the 5_SL4,215209,50342
BMRB,50348,chemical shifts of the PK (Pseudoknot),215209,50342
BMRB,50349,chemical shifts of the 5_SL1,215209,50342
BMRB,50350,chemical shifts of the 3_SL3base,215209,50342
BMRB,50351,chemical shifts of the 5_SL6,215209,50342
BMRB,50352,chemical shifts of the 5_SL8,215209,50342
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215209,50342
BMRB,50339,chemical shifts of the 5_SL5B+C,215230,50343
BMRB,50340,chemical shifts of the 5_SL5stem,215230,50343
BMRB,50341,chemical shifts of the 3_s2m,215230,50343
BMRB,50342,chemical shifts of the 3_SL1,215230,50343
BMRB,50344,chemical shifts of the 5_SL2+3,215230,50343
BMRB,50346,chemical shifts of the 5_SL5a,215230,50343
BMRB,50347,chemical shifts of the 5_SL4,215230,50343
BMRB,50348,chemical shifts of the PK (Pseudoknot),215230,50343
BMRB,50349,chemical shifts of the 5_SL1,215230,50343
BMRB,50350,chemical shifts of the 3_SL3base,215230,50343
BMRB,50351,chemical shifts of the 5_SL6,215230,50343
BMRB,50352,chemical shifts of the 5_SL8,215230,50343
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215230,50343
BMRB,50339,chemical shifts of the 5_SL5B+C,215250,50344
BMRB,50340,chemical shifts of the 5_SL5stem,215250,50344
BMRB,50341,chemical shifts of the 3_s2m,215250,50344
BMRB,50342,chemical shifts of the 3_SL1,215250,50344
BMRB,50343,chemical shifts of the 2_SL3,215250,50344
BMRB,50346,chemical shifts of the 5_SL5a,215250,50344
BMRB,50347,chemical shifts of the 5_SL4,215250,50344
BMRB,50348,chemical shifts of the PK (Pseudoknot),215250,50344
BMRB,50349,chemical shifts of the 5_SL1,215250,50344
BMRB,50350,chemical shifts of the 3_SL3base,215250,50344
BMRB,50351,chemical shifts of the 5_SL6,215250,50344
BMRB,50352,chemical shifts of the 5_SL8,215250,50344
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215250,50344
BMRB,50339,chemical shifts of the 5_SL5B+C,215265,50346
BMRB,50340,chemical shifts of the 5_SL5stem,215265,50346
BMRB,50341,chemical shifts of the 3_s2m,215265,50346
BMRB,50342,chemical shifts of the 3_SL1,215265,50346
BMRB,50343,chemical shifts of the 2_SL3,215265,50346
BMRB,50344,chemical shifts of the 5_SL2+3,215265,50346
BMRB,50347,chemical shifts of the 5_SL4,215265,50346
BMRB,50348,chemical shifts of the PK (Pseudoknot),215265,50346
BMRB,50349,chemical shifts of the 5_SL1,215265,50346
BMRB,50350,chemical shifts of the 3_SL3base,215265,50346
BMRB,50351,chemical shifts of the 5_SL6,215265,50346
BMRB,50352,chemical shifts of the 5_SL8,215265,50346
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215265,50346
BMRB,50339,chemical shifts of the 5_SL5B+C,215280,50347
BMRB,50340,chemical shifts of the 5_SL5stem,215280,50347
BMRB,50341,chemical shifts of the 3_s2m,215280,50347
BMRB,50342,chemical shifts of the 3_SL1,215280,50347
BMRB,50343,chemical shifts of the 2_SL3,215280,50347
BMRB,50344,chemical shifts of the 5_SL2+3,215280,50347
BMRB,50346,chemical shifts of the 5_SL5a,215280,50347
BMRB,50348,chemical shifts of the PK (Pseudoknot),215280,50347
BMRB,50349,chemical shifts of the 5_SL1,215280,50347
BMRB,50350,chemical shifts of the 3_SL3base,215280,50347
BMRB,50351,chemical shifts of the 5_SL6,215280,50347
BMRB,50352,chemical shifts of the 5_SL8,215280,50347
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215280,50347
BMRB,50339,chemical shifts of the 5_SL5B+C,215298,50348
BMRB,50340,chemical shifts of the 5_SL5stem,215298,50348
BMRB,50341,chemical shifts of the 3_s2m,215298,50348
BMRB,50342,chemical shifts of the 3_SL1,215298,50348
BMRB,50343,chemical shifts of the 2_SL3,215298,50348
BMRB,50344,chemical shifts of the 5_SL2+3,215298,50348
BMRB,50346,chemical shifts of the 5_SL5a,215298,50348
BMRB,50347,chemical shifts of the 5_SL4,215298,50348
BMRB,50349,chemical shifts of the 5_SL1,215298,50348
BMRB,50350,chemical shifts of the 3_SL3base,215298,50348
BMRB,50351,chemical shifts of the 5_SL6,215298,50348
BMRB,50352,chemical shifts of the 5_SL8,215298,50348
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215298,50348
BMRB,50339,chemical shifts of the 5_SL5B+C,215317,50349
BMRB,50340,chemical shifts of the 5_SL5stem,215317,50349
BMRB,50341,chemical shifts of the 3_s2m,215317,50349
BMRB,50342,chemical shifts of the 3_SL1,215317,50349
BMRB,50343,chemical shifts of the 2_SL3,215317,50349
BMRB,50344,chemical shifts of the 5_SL2+3,215317,50349
BMRB,50346,chemical shifts of the 5_SL5a,215317,50349
BMRB,50347,chemical shifts of the 5_SL4,215317,50349
BMRB,50348,chemical shifts of the PK (Pseudoknot),215317,50349
BMRB,50350,chemical shifts of the 3_SL3base,215317,50349
BMRB,50351,chemical shifts of the 5_SL6,215317,50349
BMRB,50352,chemical shifts of the 5_SL8,215317,50349
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215317,50349
BMRB,50339,chemical shifts of the 5_SL5B+C,215338,50350
BMRB,50340,chemical shifts of the 5_SL5stem,215338,50350
BMRB,50341,chemical shifts of the 3_s2m,215338,50350
BMRB,50342,chemical shifts of the 3_SL1,215338,50350
BMRB,50343,chemical shifts of the 2_SL3,215338,50350
BMRB,50344,chemical shifts of the 5_SL2+3,215338,50350
BMRB,50346,chemical shifts of the 5_SL5a,215338,50350
BMRB,50347,chemical shifts of the 5_SL4,215338,50350
BMRB,50348,chemical shifts of the PK (Pseudoknot),215338,50350
BMRB,50349,chemical shifts of the 5_SL1,215338,50350
BMRB,50351,chemical shifts of the 5_SL6,215338,50350
BMRB,50352,chemical shifts of the 5_SL8,215338,50350
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215338,50350
BMRB,50339,chemical shifts of the 5_SL5B+C,215353,50351
BMRB,50340,chemical shifts of the 5_SL5stem,215353,50351
BMRB,50341,chemical shifts of the 3_s2m,215353,50351
BMRB,50342,chemical shifts of the 3_SL1,215353,50351
BMRB,50343,chemical shifts of the 2_SL3,215353,50351
BMRB,50344,chemical shifts of the 5_SL2+3,215353,50351
BMRB,50346,chemical shifts of the 5_SL5a,215353,50351
BMRB,50347,chemical shifts of the 5_SL4,215353,50351
BMRB,50348,chemical shifts of the PK (Pseudoknot),215353,50351
BMRB,50349,chemical shifts of the 5_SL1,215353,50351
BMRB,50350,chemical shifts of the 3_SL3base,215353,50351
BMRB,50352,chemical shifts of the 5_SL8,215353,50351
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215353,50351
BMRB,50339,chemical shifts of the 5_SL5B+C,215372,50352
BMRB,50340,chemical shifts of the 5_SL5stem,215372,50352
BMRB,50341,chemical shifts of the 3_s2m,215372,50352
BMRB,50342,chemical shifts of the 3_SL1,215372,50352
BMRB,50343,chemical shifts of the 2_SL3,215372,50352
BMRB,50344,chemical shifts of the 5_SL2+3,215372,50352
BMRB,50346,chemical shifts of the 5_SL5a,215372,50352
BMRB,50347,chemical shifts of the 5_SL4,215372,50352
BMRB,50348,chemical shifts of the PK (Pseudoknot),215372,50352
BMRB,50349,chemical shifts of the 5_SL1,215372,50352
BMRB,50350,chemical shifts of the 3_SL3base,215372,50352
BMRB,50351,chemical shifts of the 5_SL6,215372,50352
NCBI,NC_045512.2,"Severe acute respiratory syndrome coronavirus 2 isolate Wuhan-Hu-1, complete genome.",215372,50352
BMRB,17148,N-terminal domain of Nephila clavipes major ampulate spidroin 1,215388,50353
BMRB,18262,NMR structure of major ampullate spidroin 1 N-terminal domain at pH 7.2,215388,50353
PDB,1HU5,BMRB Entry Tracking System,215444,5037
BMRB,27832,Methyl Chemical shift Assignment of EIC from the thermophile thermoanaerobacter tengcongenesis,215506,50386
BMRB,27833,tEIN backbone and I/L/V methyl resonance assignment,215506,50386
BMRB,50388,macrodomain of SARS-CoV-2 non-structural protein 3b bound to ADPr,215525,50387
BMRB,50387,"macrodomain of SARS-CoV-2 non-structural protein 3b, apo form",215540,50388
BMRB,27949,HNH from SpyCas9,215557,50389
BMRB,4707,"WT1-KTSs free; contains only HN, N, CA, CB assignments",215627,50405
BMRB,4708,WT1-KTS/DNA complex,215627,50405
BMRB,4709,WT1+KTS/free,215627,50405
BMRB,4710,WT1+KTS/DNA complex,215627,50405
BMRB,50236,WT1-KTS/RNA complex,215627,50405
BMRB,50408,V98A EcRNHI 15N-1H Backbone Chemical Shifts,215648,50407
BMRB,50409,SoRNHI 15N-1H Backbone Chemical Shifts,215648,50407
BMRB,50407,V98A EcRNHI* (Cys-free) 15N-1H Backbone Chemical Shifts,215663,50408
BMRB,50409,SoRNHI 15N-1H Backbone Chemical Shifts,215663,50408
BMRB,50407,V98A EcRNHI* (Cys-free) 15N-1H Backbone Chemical Shifts,215677,50409
BMRB,50408,V98A EcRNHI 15N-1H Backbone Chemical Shifts,215677,50409
BMRB,6353,chemical shifs of RFC p140 375-480 BRCT domain in complex with DNA,215691,5041
PDB,1IE5,BMRB Entry Tracking System,215783,5044
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215811,50454
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215811,50454
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215811,50454
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215811,50454
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215811,50454
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215811,50454
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215811,50454
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215840,50455
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215840,50455
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215840,50455
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215840,50455
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215840,50455
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215840,50455
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215840,50455
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215862,50456
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215862,50456
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215862,50456
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215862,50456
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215862,50456
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215862,50456
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215862,50456
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215884,50457
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215884,50457
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215884,50457
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215884,50457
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215884,50457
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215884,50457
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215884,50457
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215906,50458
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215906,50458
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215906,50458
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215906,50458
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215906,50458
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215906,50458
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215906,50458
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215928,50459
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215928,50459
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215928,50459
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215928,50459
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215928,50459
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215928,50459
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215928,50459
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215971,50460
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215971,50460
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215971,50460
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215971,50460
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215971,50460
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215971,50460
BMRB,50461,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L713F mutant,215971,50460
BMRB,50454,"human PARP-1 CAT domain HN, N, CA and CB assignments and backbone amide group 15N relaxation data",215991,50461
BMRB,50455,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to veliparib,215991,50461
BMRB,50456,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to olaparib,215991,50461
BMRB,50457,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib,215991,50461
BMRB,50458,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to EB-47,215991,50461
BMRB,50459,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765F mutant,215991,50461
BMRB,50460,Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain L765A mutant,215991,50461
BMRB,5319,chemical shift assignments of the holo protein,216063,5048
BMRB,5330,relaxation data of the apo protein,216063,5048
BMRB,5331,relaxation data of the holo protein,216063,5048
PDB,1JC6,BMRB Entry Tracking System,216115,5050
BMRB,5690,Chemical shifts by different group,216175,5052
PDB,1JE9,BMRB Entry Tracking System,216175,5052
BMRB,4448,Free form,216216,5054
PDB,1IBI,BMRB Entry Tracking System,216472,5065
BMRB,5069,hen egg white lysozyme (CYS mutants),216546,5068
BMRB,5803,Three-disulfide variant of hen lysozyme: C64A/C80A,216546,5068
PDB,2JP2,NMR structure,236000,5939
BMRB,5804,Three-disulfide variant of hen lysozyme: C76A/C94A,216546,5068
BMRB,6415,"hen lysozyme CYS mutants (30 and 115) by Ala, C30A/C115A",216546,5068
BMRB,5068,recombinant hen lysozyme containing the extra N-terminal Met,216566,5069
BMRB,5803,Three-disulfide variant of hen lysozyme: C64A/C80A,216566,5069
BMRB,5804,Three-disulfide variant of hen lysozyme: C76A/C94A,216566,5069
PDB,1JBJ,BMRB Entry Tracking System,216656,5072
BMRB,4147,data for folded protein,216729,5076
BMRB,4471,chemical shift assignments of reduced cytochrome c552,216816,5079
BMRB,4777,chemical shift assignments of oxidized cytochrome c552,216816,5079
BMRB,5080,cytochrome c552 oxidized,216816,5079
BMRB,4471,chemical shift assignments of reduced cytochrome c552,216860,5080
BMRB,4777,chemical shift assignments of oxidized cytochrome c552,216860,5080
BMRB,5079,cytochrome c552 reduced,216860,5080
BMRB,4309,Free form Hemophore HasA.,216890,5081
PDB,1JLZ,BMRB Entry Tracking System,216909,5082
BMRB,4915,non-liganded C-terminal domain of PABP,216942,5084
BMRB,5085,PABC-Paip2 complex,216942,5084
BMRB,4915,non-liganded C-terminal domain of PABP,216969,5085
BMRB,5084,PABC-Paip1 complex,216969,5085
BMRB,5087,oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552,217000,5086
BMRB,5088,reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552,217000,5086
BMRB,5089,oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552,217000,5086
BMRB,5086,reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552,217019,5087
BMRB,5088,reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552,217019,5087
BMRB,5089,oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552,217019,5087
BMRB,5086,reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552,217037,5088
BMRB,5087,oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552,217037,5088
BMRB,5089,oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552,217037,5088
BMRB,5086,reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552,217056,5089
BMRB,5087,oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552,217056,5089
BMRB,5088,reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552,217056,5089
PDB,1JN7,BMRB Entry Tracking System,217197,5096
PDB,1IJC,BMRB Entry Tracking System,217223,5097
PDB,1J2O,BMRB Entry Tracking System,217305,5100
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,217481,5108
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,217481,5108
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,217481,5108
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,217481,5108
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,217481,5108
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,217481,5108
BMRB,5139,DDap (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,217481,5108
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,217481,5108
PDB,1JAA,BMRB Entry Tracking System,217481,5108
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,217500,5109
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,217500,5109
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,217500,5109
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,217500,5109
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,217500,5109
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,217500,5109
BMRB,5139,DDap (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,217500,5109
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,217500,5109
PDB,1J9V,BMRB Entry Tracking System,217500,5109
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,217534,5110
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,217534,5110
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,217534,5110
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,217534,5110
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,217534,5110
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,217534,5110
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,217534,5110
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,217534,5110
PDB,1J8Z,BMRB Entry Tracking System,217534,5110
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,217554,5111
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,217554,5111
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,217554,5111
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,217554,5111
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,217554,5111
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,217554,5111
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,217554,5111
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,217554,5111
PDB,1J8N,BMRB Entry Tracking System,217554,5111
BMRB,5113,psi-conotoxin PIIIE,217574,5112
PDB,1JLP,BMRB Entry Tracking System,217574,5112
BMRB,5112,psi-conotoxin PIIIF,217599,5113
PDB,1JLO,BMRB Entry Tracking System,217599,5113
PDB,1JJZ,BMRB Entry Tracking System,217621,5114
PDB,1K48,BMRB Entry Tracking System,217621,5114
BMRB,5116,reduced form,217637,5115
BMRB,5115,oxidized form,217670,5116
BMRB,19210,rhodostomin P48A/M52W/P53N mutant,217701,5117
BMRB,19211,rhodostomin 48ARGDWN-67NGLYG mutant,217701,5117
BMRB,19212,rhodostomin 48ARGDWN-67NPWNG mutant,217701,5117
PDB,2PJF,rhodostomin  wild type,217701,5117
PDB,2M75,rhodostomin  P48A/M52W/P53N mutant,217701,5117
PDB,2M7F,rhodostomin  48ARGDWN-67NGLYG mutant,217701,5117
PDB,2M7H,rhodostomin 48ARGDWN-67NPWNG mutant,217701,5117
BMRB,4316,The protein was meassured in dodecyl sulfate micelle system.,217724,5119
PDB,1GK5,BMRB Entry Tracking System,217767,5120
BMRB,4297,DnaB(24-136) recorded at different conditions,217782,5121
BMRB,5122,cyclic N-terminal domain of DnaB helicase,217782,5121
BMRB,4297,DnaB(24-136) recorded at different conditions,217802,5122
BMRB,5121,N-terminal domain of DnaB(24-136) helicase,217802,5122
BMRB,5124,human lysozyme I56T,217820,5123
BMRB,5125,human lysozyme D67H,217820,5123
BMRB,5123,human lysozyme,217836,5124
BMRB,5125,human lysozyme D67H,217836,5124
BMRB,5123,human lysozyme,217851,5125
BMRB,5124,human lysozyme I56T,217851,5125
BMRB,5247,chemical shifts of calcium-loaded murine Mts1,217892,5127
BMRB,5142,human lysozyme at 4 C,217970,5130
BMRB,6060,PDZ2 from PTP-BL,217983,5131
BMRB,6091,PDZ2 from PTP-BL (complex with NTR),217983,5131
BMRB,6092,PDZ2 from PTP-BL (complex with RIL),217983,5131
BMRB,5056,full-length ATT,218019,5132
BMRB,5133,mature ATT,218019,5132
BMRB,5056,full-length ATT,218032,5133
BMRB,5132,mature  ATT with N-terminal YVEF cloning artifact,218032,5133
BMRB,5135,dAATAA DNA Bulge: 5'-D(*GP*CP*AP*TP*CP*GP*AP*AP*TP*AP*AP*GP*CP*TP*AP*CP*G)-3',218047,5134
PDB,1JS5,BMRB Entry Tracking System,218047,5134
PDB,1JS7,BMRB Entry Tracking System,218047,5134
BMRB,5134,dAAUAA DNA Bulge: 5'-D(*GP*CP*AP*TP*CP*GP*AP*AP*UP*AP*AP*GP*CP*TP*AP*CP*G)-3',218071,5135
PDB,1JRV,BMRB Entry Tracking System,218071,5135
PDB,1JRW,BMRB Entry Tracking System,218071,5135
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,218095,5136
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,218095,5136
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,218095,5136
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,218095,5136
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,218095,5136
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,218095,5136
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,218095,5136
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,218095,5136
PDB,1JDK,BMRB Entry Tracking System,218095,5136
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,218114,5137
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,218114,5137
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,218114,5137
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,218114,5137
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,218114,5137
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,218114,5137
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,218114,5137
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,218114,5137
PDB,1JD8,BMRB Entry Tracking System,218114,5137
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,218133,5138
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,218133,5138
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,218133,5138
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,218133,5138
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,218133,5138
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,218133,5138
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,218133,5138
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,218133,5138
PDB,1JCP,BMRB Entry Tracking System,218133,5138
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,218152,5139
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,218152,5139
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,218152,5139
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,218152,5139
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,218152,5139
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,218152,5139
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,218152,5139
BMRB,5140,DDab (Ace)IWGDSGKLI(Dab)TTA analogue of HIV GP41,218152,5139
PDB,1JC8,BMRB Entry Tracking System,218152,5139
BMRB,5108,DapE (Ace)IWG(Dap)SGKLIETTA analogue of HIV GP41,218185,5140
BMRB,5109,DabD (Ace)IWG(DAB)SGKLIDTTA analogue of HIV GP41,218185,5140
BMRB,5110,HCYS (ACE)IWG(BCX)SGKLICTTA analogue of HIV GP41,218185,5140
BMRB,5111,HSER (ACE)IWGC(BSE)GKLICTTA analogue of HIV GP41,218185,5140
BMRB,5136,EDap (Ace)IWGESGKLI(DAB)TTA analogue of HIV GP41,218185,5140
BMRB,5137,DapD (Ace)IWG(DAP)SGKLIDTTA analogue of HIV GP41,218185,5140
BMRB,5138,EDap (Ace)IWGESGKLI(DNP)TTA analogue of HIV GP41,218185,5140
BMRB,5139,DapD (Ace)IWGDSGKLI(DNP)TTA analogue of HIV GP41,218185,5140
PDB,1JAR,BMRB Entry Tracking System,218185,5140
BMRB,5130,human lysozyme at 35 C,218228,5142
PDB,1IY3,BMRB Entry Tracking System,218228,5142
BMRB,5144,rhodopsin T3-I2-T4 peptide,218241,5143
BMRB,5149,D130I mutant T3-I2(D130I) peptide,218241,5143
BMRB,5150,T3-I2-T4 peptide,218241,5143
BMRB,5143,wild type T3-I2 peptide,218257,5144
BMRB,5149,D130I mutant T3-I2(D130I) peptide,218257,5144
BMRB,5150,T3-I2-T4 peptide,218257,5144
PDB,1LG4,BMRB Entry Tracking System,218273,5145
BMRB,5143,wild type T3-I2 peptide,218361,5149
BMRB,5144,rhodopsin T3-I2-T4 peptide,218361,5149
BMRB,5150,T3-I2-T4 peptide,218361,5149
BMRB,5143,wild type T3-I2 peptide,218391,5150
BMRB,5144,rhodopsin T3-I2-T4 peptide,218391,5150
BMRB,5149,D130I mutant T3-I2(D130I) peptide,218391,5150
PDB,1FD6,BMRB Entry Tracking System,218407,5151
PDB,1FCL,BMRB Entry Tracking System,218430,5152
BMRB,5154,N-terminal domain of Tissue Inhibitor of Metalloproteinases-1,218454,5153
BMRB,5153,"N-terminal domain of Tissue Inhibitor of
Metalloproteinases-1/MatrixMetalloProteinase-3(E202Q)(deltaC) complex",218480,5154
BMRB,4695,myoglobin H64F mutant,218583,5158
PDB,1JUU,BMRB Entry Tracking System,218718,5164
PDB,1JVE,BMRB Entry Tracking System,218780,5167
BMRB,5782,DN3 beta2-microglobulin (truncated form without the first 3 residues),218802,5169
BMRB,5783,DN3 beta2-microglobulin (R3A mutant),218802,5169
BMRB,5784,DN3 beta2-microglobulin (H31Y mutant),218802,5169
PDB,1JU7,BMRB Entry Tracking System,218836,5170
PDB,1JWC,BMRB Entry Tracking System,218836,5170
PDB,1JV8,BMRB Entry Tracking System,218859,5171
PDB,1JV9,BMRB Entry Tracking System,218859,5171
PDB,1HA9,BMRB Entry Tracking System,218944,5176
PDB,1K85,BMRB Entry Tracking System,218996,5178
PDB,1K1Z,BMRB Entry Tracking System,219011,5179
PDB,1HBW,BMRB Entry Tracking System,219025,5180
BMRB,5186,Assignments for vascular endothelial growth factor in free form,219156,5185
BMRB,5198,Assignments for v107 in complex with vascular endothelial growth factor,219156,5185
BMRB,5185,Assignments for vascular endothelial growth factor in complex with v107,219172,5186
BMRB,5198,Assignments for v107 in complex with vascular endothelial growth factor,219172,5186
PDB,1V4R,BMRB Entry Tracking System,219188,5187
PDB,1K8V,BMRB Entry Tracking System,219287,5192
PDB,1JZC,BMRB Entry Tracking System,219302,5193
BMRB,5185,Assignments for vascular endothelial growth factor in complex with v107,219389,5198
BMRB,5186,Assignments for vascular endothelial growth factor in free form,219389,5198
PDB,1I6Y,BMRB Entry Tracking System,219447,5201
BMRB,7167,CNPase homolog (RICH) protein,219466,5202
BMRB,4878,Calreticulin P-domain,219516,5204
BMRB,5205,Calreticulin P-domain fragment 221-256,219516,5204
BMRB,4878,Calreticulin P-domain,219537,5205
BMRB,5204,Calreticulin P-domain fragment 189-261,219537,5205
PDB,1K91,BMRB Entry Tracking System,219537,5205
BMRB,5377,human S100B in complex with TRTK-12 peptide.,219557,5206
BMRB,4581,calbindin D9K N56A,219583,5207
PDB,1K7B,BMRB Entry Tracking System,219656,5210
BMRB,5212,SAP/SH2D1A bound to peptide n-Py.,219677,5211
BMRB,5211,SAP/SH2D1A bound to peptide n-Y-c.,219698,5212
PDB,1K0V,BMRB Entry Tracking System,219722,5213
BMRB,4398,neuropeptide Y,219744,5214
BMRB,5215,Y2 selective analogue-II of neuropeptide Y,219744,5214
BMRB,5216,Y2 selective analogue-III of neuropeptide Y,219744,5214
BMRB,4398,neuropeptide Y,219770,5215
BMRB,5214,Y2 selective analogue-I of neuropeptide Y,219770,5215
BMRB,5216,Y2 selective analogue-III of neuropeptide Y,219770,5215
BMRB,4398,neuropeptide Y,219791,5216
BMRB,5214,Y2 selective analogue-I of neuropeptide Y,219791,5216
BMRB,5215,Y2 selective analogue-II of neuropeptide Y,219791,5216
BMRB,4768,Structure of parvulin hPar14.,219989,5225
BMRB,4670,Arabidopsis thaliana PIN1At Protein (prolyl cis/trans isomerase).,219989,5225
BMRB,6019,P62A dimer,220024,5226
BMRB,5286,CaM:CaMKIp(299-320) complex,220052,5227
BMRB,5287,CaM:CaMKI(1-320) complex,220052,5227
BMRB,5625,assignments of Ferri-cytochrome c3 by EMBL.,220296,5239
BMRB,5241,Alicyclobacillus acidocaldarius thioredoxin (K18G/R82E mutant),220312,5240
BMRB,5240,Alicyclobacillus acidocaldarius thioredoxin,220340,5241
PDB,1KN6,BMRB Entry Tracking System,220368,5242
PDB,1IR5,BMRB Entry Tracking System,220387,5243
PDB,1K1R,BMRB Entry Tracking System,220433,5245
BMRB,5127,chemical shifts of murine apo-mts1,220484,5247
BMRB,5260,Pseudocontact chemical shifts for [Fe(II)/Fe(II)]Dx,220533,5249
BMRB,5271,Pseudocontact chemical shifts for [Fe(II)/Zn(II)]Dx,220533,5249
BMRB,5253,"d(CCATGCGTGG)2, G-T mismatch structure",220585,5252
PDB,1KKV,BMRB Entry Tracking System,220585,5252
BMRB,5252,"d(CCACGCGTGG)2, parent to G-T mismatch structure",220603,5253
PDB,1KKW,BMRB Entry Tracking System,220603,5253
BMRB,5259,I6A modified anticodon Stem-loop from E. coli tRNA(Phe),220647,5256
PDB,1KKA,BMRB Entry Tracking System,220647,5256
BMRB,5256,Unmodified anticodon Stem-loop from E. coli tRNA(Phe),220683,5259
PDB,1KKA,BMRB Entry Tracking System,220683,5259
BMRB,5249,Backbone chemical shifts for desulforedoxin,220707,5260
BMRB,5271,Pseudocontact chemical shifts for [Fe(II)/Zn(II)]Dx,220707,5260
BMRB,4510,The Second Type II Module From Human Matrix Metalloproteinase 2,220746,5262
BMRB,5758,full assignment of YqgF,220910,5270
BMRB,5249,Backbone chemical shifts for desulforedoxin,220932,5271
BMRB,5260,Pseudocontact chemical shifts for [Fe(II)/Fe(II)]Dx,220932,5271
BMRB,6881,1H and 15N chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor complexed with bovine chymotrypsin,220958,5272
BMRB,6880,1H and 15N chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor at pH=6.0,220958,5272
BMRB,5273,"1H chemical shift assignments for SGCI[L30R, K31M]",220958,5272
BMRB,5274,1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor,220958,5272
BMRB,5272,1H chemical shift assignments for Schistocerca gregaria chymotrypsin inhibitor,220987,5273
BMRB,5274,1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor,220987,5273
PDB,1KIO,BMRB Entry Tracking System,220987,5273
BMRB,5272,1H Chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor,221001,5274
BMRB,5273,"1H chemical shift assignments for SGCI[L30R, K31M]",221001,5274
BMRB,6242,two-domain Thrombin inhibitor Dipetalin,221067,5276
PDB,1KMA,BMRB Entry Tracking System,221067,5276
BMRB,4743,reduced cytochrome c7.,221122,5279
BMRB,15019,DAGK wild type,262731,7340
BMRB,4744,oxidized cytochrome c7.,221122,5279
PDB,1KR8,BMRB Entry Tracking System,221194,5282
PDB,1PQT,BMRB Entry Tracking System,221194,5282
BMRB,5285,Point mutation at position 54 with respect to this entry.,221239,5284
BMRB,5284,"Chemical Shift Assignments for A54 I-FABP, identical to Swiss-Prot entry P12104.",221260,5285
BMRB,5227,smMLCK:CaM complex (Calmodulin with different kinase recognition domain).,221281,5286
BMRB,5287,CaM:CaMKI(1-320) complex.,221281,5286
BMRB,5227,smMLCK:CaM complex (Calmodulin with different kinase recognition domain).,221303,5287
BMRB,5286,CaM:CaMKIp(299-320) complex,221303,5287
BMRB,5290,"Double mutant [W6F,W14F]",221342,5289
BMRB,5291,penetratin 12,221342,5289
PDB,1KZ0,BMRB Entry Tracking System,221342,5289
BMRB,5289,Third helix of Antennapedia homeodomain,221361,5290
BMRB,5291,penetratin 12,221361,5290
PDB,1KZ2,BMRB Entry Tracking System,221361,5290
BMRB,5289,Third helix of Antennapedia homeodomain,221378,5291
BMRB,5290,"Double mutant [W6F,W14F]",221378,5291
PDB,1KZ5,BMRB Entry Tracking System,221378,5291
PDB,1L2Y,BMRB Entry Tracking System,221395,5292
BMRB,5296,Non-Sweet variant of Brazzein [brazzein-ins(R18a-I18b)],221471,5295
BMRB,5295,Brazzein; an intensely sweet protein,221486,5296
BMRB,5341,"longer protein, containing Rep1-136 and N-terminal Histidine tag.",221501,5297
PDB,1KYJ,BMRB Entry Tracking System,221657,5301
PDB,1KUW,BMRB Entry Tracking System,221677,5302
BMRB,4968,chemical shift assignments of BPTI at pH 6.5,221793,5307
PDB,1M7T,BMRB Entry Tracking System,221814,5308
PDB,1M3V,BMRB Entry Tracking System,221831,5309
BMRB,5318,Protein in free form.,221878,5310
BMRB,5960,myristoylated HIV-1 matrix,222025,5316
BMRB,5310,Protein in complex form with a PDGFR-derived phosphopeptide.,222065,5318
PDB,2PLD,BMRB Entry Tracking System,222065,5318
BMRB,5048,chemical shift assignments of the apo protein,222084,5319
BMRB,5330,relaxation data of the apo protein,222084,5319
BMRB,5331,relaxation data of the holo protein,222084,5319
PDB,1L1W,BMRB Entry Tracking System,222145,5321
PDB,1L6T,BMRB Entry Tracking System,222248,5326
BMRB,5048,chemical shift assignments of the apo protein,222342,5330
BMRB,5319,chemical shift assignments of the holo protein,222342,5330
BMRB,5331,relaxation data of the holo protein,222342,5330
BMRB,5048,chemical shift assignments of the apo protein,222367,5331
BMRB,5319,chemical shift assignments of the holo protein,222367,5331
BMRB,5330,relaxation data of the apo protein,222367,5331
BMRB,4566,Chemical Shift of Bovine Adrenodoxin,222485,5337
BMRB,4073,Chemical Shift of Oxidized Human Ferredoxin,222485,5337
PDB,1K2K,BMRB Entry Tracking System,222526,5339
PDB,2BID,BMRB Entry Tracking System,222542,5340
BMRB,5297,"shorter protein, containing Rep4-121.",222557,5341
BMRB,5343,Neocarzinostatin Apo-Protein,222610,5343
BMRB,5344,Apo-Protein Bound to a Synthetic Chromophore,222610,5343
BMRB,6888,Apo-Protein Bound to a Flavone,222610,5343
BMRB,5343,neocarzinostatin apo-protein free form.,222640,5344
BMRB,6888,Neocarzinostatin apo-protein with Flavone.,222640,5344
PDB,1IW4,BMRB Entry Tracking System,222728,5348
BMRB,5359,Free form of BPTI.,222924,5358
BMRB,5358,Complex form of BPTI with trypsin.,222937,5359
PDB,1KMD,BMRB Entry Tracking System,223103,5366
PDB,1LC6,BMRB Entry Tracking System,223206,5371
BMRB,5660,four conformers of ferricyt c.,223219,5372
BMRB,5381,BPTI A16V mutant.,223282,5375
PDB,1LD6,BMRB Entry Tracking System,223282,5375
BMRB,5206,human S100B in the calcium-bound form,223321,5377
BMRB,5548,relaxation data for this peptide,223371,5379
BMRB,5375,BPTI 8A mutant.,223405,5381
PDB,1LD5,BMRB Entry Tracking System,223405,5381
PDB,1N2W,BMRB Entry Tracking System,223465,5385
BMRB,4245,Relaxation data of ubiquitin,223514,5387
BMRB,7111,Solid-state NMR data,223514,5387
BMRB,5395,unmodified U2 snRNA - Intron duplex,223690,5394
PDB,1LPW,BMRB Entry Tracking System,223690,5394
BMRB,5394,U2 snRNA-Intron duplex,223711,5395
PDB,1LMV,BMRB Entry Tracking System,223711,5395
BMRB,5668,3-methyladenine DNA glycosylase I (TAG) complex with zinc,223803,5398
BMRB,6287,assignment and structure calculation for a different construct of the protein GABPa,223879,5401
BMRB,4089,Peptide Deformylase Catalytic Core,223943,5404
BMRB,4834,Backbone Resonance Assignments of a Peptide Deformylase,223943,5404
BMRB,4650,Same protein in H2O/D2O solution.,223974,5405
PDB,1M25,BMRB Entry Tracking System,223974,5405
PDB,1MPZ,BMRB Entry Tracking System,224115,5410
BMRB,4864,Chemical shifts of OMTKY3.,224132,5411
BMRB,5412,pKa value of P2'-Lys OMTKY3,224132,5411
BMRB,5413,pKa value of P2'-His OMTKY3,224132,5411
BMRB,5414,pKa value of P2'-GLU OMTKY3,224132,5411
BMRB,5415,pKa value of P2'-Asp OMTKY3,224132,5411
BMRB,5416,pKa value of P3'-Ala OMTKY3,224132,5411
BMRB,5417,pKa value of P3'-Asp OMTKY3,224132,5411
BMRB,5418,pKa value of P3'-Glu OMTKY3,224132,5411
BMRB,5419,pKa value of P3'-His OMTKY3,224132,5411
BMRB,5420,pKa value of P3'-Lys OMTKY3,224132,5411
BMRB,5421,pKa value of P1'-Asp OMTKY3,224132,5411
BMRB,5422,pKa value of P1'-His OMTKY3,224132,5411
BMRB,5423,pKa value of P1'-Lys OMTKY3,224132,5411
BMRB,5424,pKa value of P1-Asp OMTKY3,224132,5411
BMRB,5425,pKa value of P1-Glu OMTKY3,224132,5411
BMRB,5426,pKa value of P1-Gly OMTKY3,224132,5411
BMRB,5427,pKa value of P1-Ala OMTKY3,224132,5411
BMRB,5428,pKa value of P1-His OMTKY3,224132,5411
BMRB,5429,pKa value of P1-Lys OMTKY3,224132,5411
BMRB,5430,pKa value of P2-Asp OMTKY3,224132,5411
BMRB,5431,pKa value of P2-Glu OMTKY3,224132,5411
BMRB,5432,pKa value of P2-Val OMTKY3,224132,5411
BMRB,5433,pKa value of P2-His OMTKY3,224132,5411
BMRB,5434,pKa value of P2-Lys OMTKY3,224132,5411
BMRB,5435,pKa value of P4-Asp OMTKY3,224132,5411
BMRB,5436,pKa value of P4-Glu OMTKY3,224132,5411
BMRB,5437,pKa value of P4-His OMTKY3,224132,5411
BMRB,5438,pKa value of P4-Lys OMTKY3,224132,5411
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224132,5411
BMRB,5440,pKa value of P5-Asp OMTKY3,224132,5411
BMRB,5441,pKa value of P5-Glu OMTKY3,224132,5411
BMRB,5442,pKa value of P5-His OMTKY3,224132,5411
BMRB,5443,pKa value of P6-Asp OMTKY3,224132,5411
BMRB,5444,pKa value of P6-Glu OMTKY3,224132,5411
BMRB,5445,pKa value of P6-His OMTKY3,224132,5411
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224132,5411
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224132,5411
BMRB,5448,pKa value of OMTKY3 (no salt added),224132,5411
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224132,5411
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224132,5411
BMRB,5451,pKa value of AAPD,224132,5411
BMRB,5452,pKa value of AAPE,224132,5411
BMRB,5453,pKa value of AAPK,224132,5411
BMRB,4864,Chemical shifts of OMTKY3.,224146,5412
BMRB,5411,pKa value of OMTKY3,224146,5412
BMRB,5413,pKa value of P2'-His OMTKY3,224146,5412
BMRB,5414,pKa value of P2'-GLU OMTKY3,224146,5412
BMRB,5415,pKa value of P2'-Asp OMTKY3,224146,5412
BMRB,5416,pKa value of P3'-Ala OMTKY3,224146,5412
BMRB,5417,pKa value of P3'-Asp OMTKY3,224146,5412
BMRB,5418,pKa value of P3'-Glu OMTKY3,224146,5412
BMRB,5419,pKa value of P3'-His OMTKY3,224146,5412
BMRB,5420,pKa value of P3'-Lys OMTKY3,224146,5412
BMRB,5421,pKa value of P1'-Asp OMTKY3,224146,5412
BMRB,5422,pKa value of P1'-His OMTKY3,224146,5412
BMRB,5423,pKa value of P1'-Lys OMTKY3,224146,5412
BMRB,5424,pKa value of P1-Asp OMTKY3,224146,5412
BMRB,5425,pKa value of P1-Glu OMTKY3,224146,5412
BMRB,5426,pKa value of P1-Gly OMTKY3,224146,5412
BMRB,5427,pKa value of P1-Ala OMTKY3,224146,5412
BMRB,5428,pKa value of P1-His OMTKY3,224146,5412
BMRB,5429,pKa value of P1-Lys OMTKY3,224146,5412
BMRB,5430,pKa value of P2-Asp OMTKY3,224146,5412
BMRB,5431,pKa value of P2-Glu OMTKY3,224146,5412
BMRB,5432,pKa value of P2-Val OMTKY3,224146,5412
BMRB,5433,pKa value of P2-His OMTKY3,224146,5412
BMRB,5434,pKa value of P2-Lys OMTKY3,224146,5412
BMRB,5435,pKa value of P4-Asp OMTKY3,224146,5412
BMRB,5436,pKa value of P4-Glu OMTKY3,224146,5412
BMRB,5437,pKa value of P4-His OMTKY3,224146,5412
BMRB,5438,pKa value of P4-Lys OMTKY3,224146,5412
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224146,5412
BMRB,5440,pKa value of P5-Asp OMTKY3,224146,5412
BMRB,5441,pKa value of P5-Glu OMTKY3,224146,5412
BMRB,5442,pKa value of P5-His OMTKY3,224146,5412
BMRB,5443,pKa value of P6-Asp OMTKY3,224146,5412
BMRB,5444,pKa value of P6-Glu OMTKY3,224146,5412
BMRB,5445,pKa value of P6-His OMTKY3,224146,5412
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224146,5412
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224146,5412
BMRB,5448,pKa value of OMTKY3 (no salt added),224146,5412
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224146,5412
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224146,5412
BMRB,5451,pKa value of AAPD,224146,5412
BMRB,5452,pKa value of AAPE,224146,5412
BMRB,5453,pKa value of AAPK,224146,5412
BMRB,4864,Chemical shifts of OMTKY3.,224160,5413
BMRB,5411,pKa value of OMTKY3,224160,5413
BMRB,5412,pKa value of P2'-Lys OMTKY3,224160,5413
BMRB,5414,pKa value of P2'-GLU OMTKY3,224160,5413
BMRB,5415,pKa value of P2'-Asp OMTKY3,224160,5413
BMRB,5416,pKa value of P3'-Ala OMTKY3,224160,5413
BMRB,5417,pKa value of P3'-Asp OMTKY3,224160,5413
BMRB,5418,pKa value of P3'-Glu OMTKY3,224160,5413
BMRB,5419,pKa value of P3'-His OMTKY3,224160,5413
BMRB,5420,pKa value of P3'-Lys OMTKY3,224160,5413
BMRB,5421,pKa value of P1'-Asp OMTKY3,224160,5413
BMRB,5422,pKa value of P1'-His OMTKY3,224160,5413
BMRB,5423,pKa value of P1'-Lys OMTKY3,224160,5413
BMRB,5424,pKa value of P1-Asp OMTKY3,224160,5413
BMRB,5425,pKa value of P1-Glu OMTKY3,224160,5413
BMRB,5426,pKa value of P1-Gly OMTKY3,224160,5413
BMRB,5427,pKa value of P1-Ala OMTKY3,224160,5413
BMRB,5428,pKa value of P1-His OMTKY3,224160,5413
BMRB,5429,pKa value of P1-Lys OMTKY3,224160,5413
BMRB,5430,pKa value of P2-Asp OMTKY3,224160,5413
BMRB,5431,pKa value of P2-Glu OMTKY3,224160,5413
BMRB,5432,pKa value of P2-Val OMTKY3,224160,5413
BMRB,5433,pKa value of P2-His OMTKY3,224160,5413
BMRB,5434,pKa value of P2-Lys OMTKY3,224160,5413
BMRB,5435,pKa value of P4-Asp OMTKY3,224160,5413
BMRB,5436,pKa value of P4-Glu OMTKY3,224160,5413
BMRB,5437,pKa value of P4-His OMTKY3,224160,5413
BMRB,5438,pKa value of P4-Lys OMTKY3,224160,5413
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224160,5413
BMRB,5440,pKa value of P5-Asp OMTKY3,224160,5413
BMRB,5441,pKa value of P5-Glu OMTKY3,224160,5413
BMRB,5442,pKa value of P5-His OMTKY3,224160,5413
BMRB,5443,pKa value of P6-Asp OMTKY3,224160,5413
BMRB,5444,pKa value of P6-Glu OMTKY3,224160,5413
BMRB,5445,pKa value of P6-His OMTKY3,224160,5413
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224160,5413
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224160,5413
BMRB,5448,pKa value of OMTKY3 (no salt added),224160,5413
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224160,5413
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224160,5413
BMRB,5451,pKa value of AAPD,224160,5413
BMRB,5452,pKa value of AAPE,224160,5413
BMRB,5453,pKa value of AAPK,224160,5413
BMRB,4864,Chemical shifts of OMTKY3.,224174,5414
BMRB,5411,pKa value of OMTKY3,224174,5414
BMRB,5412,pKa value of P2'-Lys OMTKY3,224174,5414
BMRB,5413,pKa value of P2'-His OMTKY3,224174,5414
BMRB,5415,pKa value of P2'-Asp OMTKY3,224174,5414
BMRB,5416,pKa value of P3'-Ala OMTKY3,224174,5414
BMRB,5417,pKa value of P3'-Asp OMTKY3,224174,5414
BMRB,5418,pKa value of P3'-Glu OMTKY3,224174,5414
BMRB,5419,pKa value of P3'-His OMTKY3,224174,5414
BMRB,5420,pKa value of P3'-Lys OMTKY3,224174,5414
BMRB,5421,pKa value of P1'-Asp OMTKY3,224174,5414
BMRB,5422,pKa value of P1'-His OMTKY3,224174,5414
BMRB,5423,pKa value of P1'-Lys OMTKY3,224174,5414
BMRB,5424,pKa value of P1-Asp OMTKY3,224174,5414
BMRB,5425,pKa value of P1-Glu OMTKY3,224174,5414
BMRB,5426,pKa value of P1-Gly OMTKY3,224174,5414
BMRB,5427,pKa value of P1-Ala OMTKY3,224174,5414
BMRB,5428,pKa value of P1-His OMTKY3,224174,5414
BMRB,5429,pKa value of P1-Lys OMTKY3,224174,5414
BMRB,5430,pKa value of P2-Asp OMTKY3,224174,5414
BMRB,5431,pKa value of P2-Glu OMTKY3,224174,5414
BMRB,5432,pKa value of P2-Val OMTKY3,224174,5414
BMRB,5433,pKa value of P2-His OMTKY3,224174,5414
BMRB,5434,pKa value of P2-Lys OMTKY3,224174,5414
BMRB,5435,pKa value of P4-Asp OMTKY3,224174,5414
BMRB,5436,pKa value of P4-Glu OMTKY3,224174,5414
BMRB,5437,pKa value of P4-His OMTKY3,224174,5414
BMRB,5438,pKa value of P4-Lys OMTKY3,224174,5414
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224174,5414
BMRB,5440,pKa value of P5-Asp OMTKY3,224174,5414
BMRB,5441,pKa value of P5-Glu OMTKY3,224174,5414
BMRB,5442,pKa value of P5-His OMTKY3,224174,5414
BMRB,5443,pKa value of P6-Asp OMTKY3,224174,5414
BMRB,5444,pKa value of P6-Glu OMTKY3,224174,5414
BMRB,5445,pKa value of P6-His OMTKY3,224174,5414
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224174,5414
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224174,5414
BMRB,5448,pKa value of OMTKY3 (no salt added),224174,5414
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224174,5414
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224174,5414
BMRB,5451,pKa value of AAPD,224174,5414
BMRB,5452,pKa value of AAPE,224174,5414
BMRB,5453,pKa value of AAPK,224174,5414
BMRB,4864,Chemical shifts of OMTKY3.,224188,5415
BMRB,5411,pKa value of OMTKY3,224188,5415
BMRB,5412,pKa value of P2'-Lys OMTKY3,224188,5415
BMRB,5413,pKa value of P2'-His OMTKY3,224188,5415
BMRB,5414,pKa value of P2'-GLU OMTKY3,224188,5415
BMRB,5416,pKa value of P3'-Ala OMTKY3,224188,5415
BMRB,5417,pKa value of P3'-Asp OMTKY3,224188,5415
BMRB,5418,pKa value of P3'-Glu OMTKY3,224188,5415
BMRB,5419,pKa value of P3'-His OMTKY3,224188,5415
BMRB,5420,pKa value of P3'-Lys OMTKY3,224188,5415
BMRB,5421,pKa value of P1'-Asp OMTKY3,224188,5415
BMRB,5422,pKa value of P1'-His OMTKY3,224188,5415
BMRB,5423,pKa value of P1'-Lys OMTKY3,224188,5415
BMRB,5424,pKa value of P1-Asp OMTKY3,224188,5415
BMRB,5425,pKa value of P1-Glu OMTKY3,224188,5415
BMRB,5426,pKa value of P1-Gly OMTKY3,224188,5415
BMRB,5427,pKa value of P1-Ala OMTKY3,224188,5415
BMRB,5428,pKa value of P1-His OMTKY3,224188,5415
BMRB,5429,pKa value of P1-Lys OMTKY3,224188,5415
BMRB,5430,pKa value of P2-Asp OMTKY3,224188,5415
BMRB,5431,pKa value of P2-Glu OMTKY3,224188,5415
BMRB,5432,pKa value of P2-Val OMTKY3,224188,5415
BMRB,5433,pKa value of P2-His OMTKY3,224188,5415
BMRB,5434,pKa value of P2-Lys OMTKY3,224188,5415
BMRB,5435,pKa value of P4-Asp OMTKY3,224188,5415
BMRB,5436,pKa value of P4-Glu OMTKY3,224188,5415
BMRB,5437,pKa value of P4-His OMTKY3,224188,5415
BMRB,5438,pKa value of P4-Lys OMTKY3,224188,5415
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224188,5415
BMRB,5440,pKa value of P5-Asp OMTKY3,224188,5415
BMRB,5441,pKa value of P5-Glu OMTKY3,224188,5415
BMRB,5442,pKa value of P5-His OMTKY3,224188,5415
BMRB,5443,pKa value of P6-Asp OMTKY3,224188,5415
BMRB,5444,pKa value of P6-Glu OMTKY3,224188,5415
BMRB,5445,pKa value of P6-His OMTKY3,224188,5415
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224188,5415
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224188,5415
BMRB,5448,pKa value of OMTKY3 (no salt added),224188,5415
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224188,5415
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224188,5415
BMRB,5451,pKa value of AAPD,224188,5415
BMRB,5452,pKa value of AAPE,224188,5415
BMRB,5453,pKa value of AAPK,224188,5415
BMRB,4864,Chemical shifts of OMTKY3.,224202,5416
BMRB,5411,pKa value of OMTKY3,224202,5416
BMRB,5412,pKa value of P2'-Lys OMTKY3,224202,5416
BMRB,5413,pKa value of P2'-His OMTKY3,224202,5416
BMRB,5414,pKa value of P2'-GLU OMTKY3,224202,5416
BMRB,5415,pKa value of P2'-Asp OMTKY3,224202,5416
BMRB,5417,pKa value of P3'-Asp OMTKY3,224202,5416
BMRB,5418,pKa value of P3'-Glu OMTKY3,224202,5416
BMRB,5419,pKa value of P3'-His OMTKY3,224202,5416
BMRB,5420,pKa value of P3'-Lys OMTKY3,224202,5416
BMRB,5421,pKa value of P1'-Asp OMTKY3,224202,5416
BMRB,5422,pKa value of P1'-His OMTKY3,224202,5416
BMRB,5423,pKa value of P1'-Lys OMTKY3,224202,5416
BMRB,5424,pKa value of P1-Asp OMTKY3,224202,5416
BMRB,5425,pKa value of P1-Glu OMTKY3,224202,5416
BMRB,5426,pKa value of P1-Gly OMTKY3,224202,5416
BMRB,5427,pKa value of P1-Ala OMTKY3,224202,5416
BMRB,5428,pKa value of P1-His OMTKY3,224202,5416
BMRB,5429,pKa value of P1-Lys OMTKY3,224202,5416
BMRB,5430,pKa value of P2-Asp OMTKY3,224202,5416
BMRB,5431,pKa value of P2-Glu OMTKY3,224202,5416
BMRB,5432,pKa value of P2-Val OMTKY3,224202,5416
BMRB,5433,pKa value of P2-His OMTKY3,224202,5416
BMRB,5434,pKa value of P2-Lys OMTKY3,224202,5416
BMRB,5435,pKa value of P4-Asp OMTKY3,224202,5416
BMRB,5436,pKa value of P4-Glu OMTKY3,224202,5416
BMRB,5437,pKa value of P4-His OMTKY3,224202,5416
BMRB,5438,pKa value of P4-Lys OMTKY3,224202,5416
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224202,5416
BMRB,5440,pKa value of P5-Asp OMTKY3,224202,5416
BMRB,5441,pKa value of P5-Glu OMTKY3,224202,5416
BMRB,5442,pKa value of P5-His OMTKY3,224202,5416
BMRB,5443,pKa value of P6-Asp OMTKY3,224202,5416
BMRB,5444,pKa value of P6-Glu OMTKY3,224202,5416
BMRB,5445,pKa value of P6-His OMTKY3,224202,5416
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224202,5416
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224202,5416
BMRB,5448,pKa value of OMTKY3 (no salt added),224202,5416
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224202,5416
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224202,5416
BMRB,5451,pKa value of AAPD,224202,5416
BMRB,5452,pKa value of AAPE,224202,5416
BMRB,5453,pKa value of AAPK,224202,5416
BMRB,4864,Chemical shifts of OMTKY3.,224216,5417
BMRB,5411,pKa value of OMTKY3,224216,5417
BMRB,5412,pKa value of P2'-Lys OMTKY3,224216,5417
BMRB,5413,pKa value of P2'-His OMTKY3,224216,5417
BMRB,5414,pKa value of P2'-GLU OMTKY3,224216,5417
BMRB,5415,pKa value of P2'-Asp OMTKY3,224216,5417
BMRB,5416,pKa value of P3'-Ala OMTKY3,224216,5417
BMRB,5418,pKa value of P3'-Glu OMTKY3,224216,5417
BMRB,5419,pKa value of P3'-His OMTKY3,224216,5417
BMRB,5420,pKa value of P3'-Lys OMTKY3,224216,5417
BMRB,5421,pKa value of P1'-Asp OMTKY3,224216,5417
BMRB,5422,pKa value of P1'-His OMTKY3,224216,5417
BMRB,5423,pKa value of P1'-Lys OMTKY3,224216,5417
BMRB,5424,pKa value of P1-Asp OMTKY3,224216,5417
BMRB,5425,pKa value of P1-Glu OMTKY3,224216,5417
BMRB,5426,pKa value of P1-Gly OMTKY3,224216,5417
BMRB,5427,pKa value of P1-Ala OMTKY3,224216,5417
BMRB,5428,pKa value of P1-His OMTKY3,224216,5417
BMRB,5429,pKa value of P1-Lys OMTKY3,224216,5417
BMRB,5430,pKa value of P2-Asp OMTKY3,224216,5417
BMRB,5431,pKa value of P2-Glu OMTKY3,224216,5417
BMRB,5432,pKa value of P2-Val OMTKY3,224216,5417
BMRB,5433,pKa value of P2-His OMTKY3,224216,5417
BMRB,5434,pKa value of P2-Lys OMTKY3,224216,5417
BMRB,5435,pKa value of P4-Asp OMTKY3,224216,5417
BMRB,5436,pKa value of P4-Glu OMTKY3,224216,5417
BMRB,5437,pKa value of P4-His OMTKY3,224216,5417
BMRB,5438,pKa value of P4-Lys OMTKY3,224216,5417
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224216,5417
BMRB,5440,pKa value of P5-Asp OMTKY3,224216,5417
BMRB,5441,pKa value of P5-Glu OMTKY3,224216,5417
BMRB,5442,pKa value of P5-His OMTKY3,224216,5417
BMRB,5443,pKa value of P6-Asp OMTKY3,224216,5417
BMRB,5444,pKa value of P6-Glu OMTKY3,224216,5417
BMRB,5445,pKa value of P6-His OMTKY3,224216,5417
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224216,5417
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224216,5417
BMRB,5448,pKa value of OMTKY3 (no salt added),224216,5417
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224216,5417
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224216,5417
BMRB,5451,pKa value of AAPD,224216,5417
BMRB,5452,pKa value of AAPE,224216,5417
BMRB,5453,pKa value of AAPK,224216,5417
BMRB,4864,Chemical shifts of OMTKY3.,224230,5418
BMRB,5411,pKa value of OMTKY3,224230,5418
BMRB,5412,pKa value of P2'-Lys OMTKY3,224230,5418
BMRB,5413,pKa value of P2'-His OMTKY3,224230,5418
BMRB,5414,pKa value of P2'-GLU OMTKY3,224230,5418
BMRB,5415,pKa value of P2'-Asp OMTKY3,224230,5418
BMRB,5416,pKa value of P3'-Ala OMTKY3,224230,5418
BMRB,5417,pKa value of P3'-Asp OMTKY3,224230,5418
BMRB,5419,pKa value of P3'-His OMTKY3,224230,5418
BMRB,5420,pKa value of P3'-Lys OMTKY3,224230,5418
BMRB,5421,pKa value of P1'-Asp OMTKY3,224230,5418
BMRB,5422,pKa value of P1'-His OMTKY3,224230,5418
BMRB,5423,pKa value of P1'-Lys OMTKY3,224230,5418
BMRB,5424,pKa value of P1-Asp OMTKY3,224230,5418
BMRB,5425,pKa value of P1-Glu OMTKY3,224230,5418
BMRB,5426,pKa value of P1-Gly OMTKY3,224230,5418
BMRB,5427,pKa value of P1-Ala OMTKY3,224230,5418
BMRB,5428,pKa value of P1-His OMTKY3,224230,5418
BMRB,5429,pKa value of P1-Lys OMTKY3,224230,5418
BMRB,5430,pKa value of P2-Asp OMTKY3,224230,5418
BMRB,5431,pKa value of P2-Glu OMTKY3,224230,5418
BMRB,5432,pKa value of P2-Val OMTKY3,224230,5418
BMRB,5433,pKa value of P2-His OMTKY3,224230,5418
BMRB,5434,pKa value of P2-Lys OMTKY3,224230,5418
BMRB,5435,pKa value of P4-Asp OMTKY3,224230,5418
BMRB,5436,pKa value of P4-Glu OMTKY3,224230,5418
BMRB,5437,pKa value of P4-His OMTKY3,224230,5418
BMRB,5438,pKa value of P4-Lys OMTKY3,224230,5418
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224230,5418
BMRB,5440,pKa value of P5-Asp OMTKY3,224230,5418
BMRB,5441,pKa value of P5-Glu OMTKY3,224230,5418
BMRB,5442,pKa value of P5-His OMTKY3,224230,5418
BMRB,5443,pKa value of P6-Asp OMTKY3,224230,5418
BMRB,5444,pKa value of P6-Glu OMTKY3,224230,5418
BMRB,5445,pKa value of P6-His OMTKY3,224230,5418
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224230,5418
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224230,5418
BMRB,5448,pKa value of OMTKY3 (no salt added),224230,5418
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224230,5418
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224230,5418
BMRB,5451,pKa value of AAPD,224230,5418
BMRB,5452,pKa value of AAPE,224230,5418
BMRB,5453,pKa value of AAPK,224230,5418
BMRB,4864,Chemical shifts of OMTKY3.,224244,5419
BMRB,5411,pKa value of OMTKY3,224244,5419
BMRB,5412,pKa value of P2'-Lys OMTKY3,224244,5419
BMRB,5413,pKa value of P2'-His OMTKY3,224244,5419
BMRB,5414,pKa value of P2'-GLU OMTKY3,224244,5419
BMRB,5415,pKa value of P2'-Asp OMTKY3,224244,5419
BMRB,5416,pKa value of P3'-Ala OMTKY3,224244,5419
BMRB,5417,pKa value of P3'-Asp OMTKY3,224244,5419
BMRB,5418,pKa value of P3'-Glu OMTKY3,224244,5419
BMRB,5420,pKa value of P3'-Lys OMTKY3,224244,5419
BMRB,5421,pKa value of P1'-Asp OMTKY3,224244,5419
BMRB,5422,pKa value of P1'-His OMTKY3,224244,5419
BMRB,5423,pKa value of P1'-Lys OMTKY3,224244,5419
BMRB,5424,pKa value of P1-Asp OMTKY3,224244,5419
BMRB,5425,pKa value of P1-Glu OMTKY3,224244,5419
BMRB,5426,pKa value of P1-Gly OMTKY3,224244,5419
BMRB,5427,pKa value of P1-Ala OMTKY3,224244,5419
BMRB,5428,pKa value of P1-His OMTKY3,224244,5419
BMRB,5429,pKa value of P1-Lys OMTKY3,224244,5419
BMRB,5430,pKa value of P2-Asp OMTKY3,224244,5419
BMRB,5431,pKa value of P2-Glu OMTKY3,224244,5419
BMRB,5432,pKa value of P2-Val OMTKY3,224244,5419
BMRB,5433,pKa value of P2-His OMTKY3,224244,5419
BMRB,5434,pKa value of P2-Lys OMTKY3,224244,5419
BMRB,5435,pKa value of P4-Asp OMTKY3,224244,5419
BMRB,5436,pKa value of P4-Glu OMTKY3,224244,5419
BMRB,5437,pKa value of P4-His OMTKY3,224244,5419
BMRB,5438,pKa value of P4-Lys OMTKY3,224244,5419
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224244,5419
BMRB,5440,pKa value of P5-Asp OMTKY3,224244,5419
BMRB,5441,pKa value of P5-Glu OMTKY3,224244,5419
BMRB,5442,pKa value of P5-His OMTKY3,224244,5419
BMRB,5443,pKa value of P6-Asp OMTKY3,224244,5419
BMRB,5444,pKa value of P6-Glu OMTKY3,224244,5419
BMRB,5445,pKa value of P6-His OMTKY3,224244,5419
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224244,5419
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224244,5419
BMRB,5448,pKa value of OMTKY3 (no salt added),224244,5419
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224244,5419
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224244,5419
BMRB,5451,pKa value of AAPD,224244,5419
BMRB,5452,pKa value of AAPE,224244,5419
BMRB,5453,pKa value of AAPK,224244,5419
BMRB,4864,Chemical shifts of OMTKY3.,224258,5420
BMRB,5411,pKa value of OMTKY3,224258,5420
BMRB,5412,pKa value of P2'-Lys OMTKY3,224258,5420
BMRB,5413,pKa value of P2'-His OMTKY3,224258,5420
BMRB,5414,pKa value of P2'-GLU OMTKY3,224258,5420
BMRB,5415,pKa value of P2'-Asp OMTKY3,224258,5420
BMRB,5416,pKa value of P3'-Ala OMTKY3,224258,5420
BMRB,5417,pKa value of P3'-Asp OMTKY3,224258,5420
BMRB,5418,pKa value of P3'-Glu OMTKY3,224258,5420
BMRB,5419,pKa value of P3'-His OMTKY3,224258,5420
BMRB,5421,pKa value of P1'-Asp OMTKY3,224258,5420
BMRB,5422,pKa value of P1'-His OMTKY3,224258,5420
BMRB,5423,pKa value of P1'-Lys OMTKY3,224258,5420
BMRB,5424,pKa value of P1-Asp OMTKY3,224258,5420
BMRB,5425,pKa value of P1-Glu OMTKY3,224258,5420
BMRB,5426,pKa value of P1-Gly OMTKY3,224258,5420
BMRB,5427,pKa value of P1-Ala OMTKY3,224258,5420
BMRB,5428,pKa value of P1-His OMTKY3,224258,5420
BMRB,5429,pKa value of P1-Lys OMTKY3,224258,5420
BMRB,5430,pKa value of P2-Asp OMTKY3,224258,5420
BMRB,5431,pKa value of P2-Glu OMTKY3,224258,5420
BMRB,5432,pKa value of P2-Val OMTKY3,224258,5420
BMRB,5433,pKa value of P2-His OMTKY3,224258,5420
BMRB,5434,pKa value of P2-Lys OMTKY3,224258,5420
BMRB,5435,pKa value of P4-Asp OMTKY3,224258,5420
BMRB,5436,pKa value of P4-Glu OMTKY3,224258,5420
BMRB,5437,pKa value of P4-His OMTKY3,224258,5420
BMRB,5438,pKa value of P4-Lys OMTKY3,224258,5420
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224258,5420
BMRB,5440,pKa value of P5-Asp OMTKY3,224258,5420
BMRB,5441,pKa value of P5-Glu OMTKY3,224258,5420
BMRB,5442,pKa value of P5-His OMTKY3,224258,5420
BMRB,5443,pKa value of P6-Asp OMTKY3,224258,5420
BMRB,5444,pKa value of P6-Glu OMTKY3,224258,5420
BMRB,5445,pKa value of P6-His OMTKY3,224258,5420
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224258,5420
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224258,5420
BMRB,5448,pKa value of OMTKY3 (no salt added),224258,5420
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224258,5420
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224258,5420
BMRB,5451,pKa value of AAPD,224258,5420
BMRB,5452,pKa value of AAPE,224258,5420
BMRB,5453,pKa value of AAPK,224258,5420
BMRB,4864,Chemical shifts of OMTKY3.,224272,5421
BMRB,5411,pKa value of OMTKY3,224272,5421
BMRB,5412,pKa value of P2'-Lys OMTKY3,224272,5421
BMRB,5413,pKa value of P2'-His OMTKY3,224272,5421
BMRB,5414,pKa value of P2'-GLU OMTKY3,224272,5421
BMRB,5415,pKa value of P2'-Asp OMTKY3,224272,5421
BMRB,5416,pKa value of P3'-Ala OMTKY3,224272,5421
BMRB,5417,pKa value of P3'-Asp OMTKY3,224272,5421
BMRB,5418,pKa value of P3'-Glu OMTKY3,224272,5421
BMRB,5419,pKa value of P3'-His OMTKY3,224272,5421
BMRB,5420,pKa value of P3'-Lys OMTKY3,224272,5421
BMRB,5422,pKa value of P1'-His OMTKY3,224272,5421
BMRB,5423,pKa value of P1'-Lys OMTKY3,224272,5421
BMRB,5424,pKa value of P1-Asp OMTKY3,224272,5421
BMRB,5425,pKa value of P1-Glu OMTKY3,224272,5421
BMRB,5426,pKa value of P1-Gly OMTKY3,224272,5421
BMRB,5427,pKa value of P1-Ala OMTKY3,224272,5421
BMRB,5428,pKa value of P1-His OMTKY3,224272,5421
BMRB,5429,pKa value of P1-Lys OMTKY3,224272,5421
BMRB,5430,pKa value of P2-Asp OMTKY3,224272,5421
BMRB,5431,pKa value of P2-Glu OMTKY3,224272,5421
BMRB,5432,pKa value of P2-Val OMTKY3,224272,5421
BMRB,5433,pKa value of P2-His OMTKY3,224272,5421
BMRB,5434,pKa value of P2-Lys OMTKY3,224272,5421
BMRB,5435,pKa value of P4-Asp OMTKY3,224272,5421
BMRB,5436,pKa value of P4-Glu OMTKY3,224272,5421
BMRB,5437,pKa value of P4-His OMTKY3,224272,5421
BMRB,5438,pKa value of P4-Lys OMTKY3,224272,5421
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224272,5421
BMRB,5440,pKa value of P5-Asp OMTKY3,224272,5421
BMRB,5441,pKa value of P5-Glu OMTKY3,224272,5421
BMRB,5442,pKa value of P5-His OMTKY3,224272,5421
BMRB,5443,pKa value of P6-Asp OMTKY3,224272,5421
BMRB,5444,pKa value of P6-Glu OMTKY3,224272,5421
BMRB,5445,pKa value of P6-His OMTKY3,224272,5421
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224272,5421
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224272,5421
BMRB,5448,pKa value of OMTKY3 (no salt added),224272,5421
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224272,5421
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224272,5421
BMRB,5451,pKa value of AAPD,224272,5421
BMRB,5452,pKa value of AAPE,224272,5421
BMRB,5453,pKa value of AAPK,224272,5421
BMRB,4864,Chemical shifts of OMTKY3.,224286,5422
BMRB,5411,pKa value of OMTKY3,224286,5422
BMRB,5412,pKa value of P2'-Lys OMTKY3,224286,5422
BMRB,5413,pKa value of P2'-His OMTKY3,224286,5422
BMRB,5414,pKa value of P2'-GLU OMTKY3,224286,5422
BMRB,5415,pKa value of P2'-Asp OMTKY3,224286,5422
BMRB,5416,pKa value of P3'-Ala OMTKY3,224286,5422
BMRB,5417,pKa value of P3'-Asp OMTKY3,224286,5422
BMRB,5418,pKa value of P3'-Glu OMTKY3,224286,5422
BMRB,5419,pKa value of P3'-His OMTKY3,224286,5422
BMRB,5420,pKa value of P3'-Lys OMTKY3,224286,5422
BMRB,5421,pKa value of P1'-Asp OMTKY3,224286,5422
BMRB,5423,pKa value of P1'-Lys OMTKY3,224286,5422
BMRB,5424,pKa value of P1-Asp OMTKY3,224286,5422
BMRB,5425,pKa value of P1-Glu OMTKY3,224286,5422
BMRB,5426,pKa value of P1-Gly OMTKY3,224286,5422
BMRB,5427,pKa value of P1-Ala OMTKY3,224286,5422
BMRB,5428,pKa value of P1-His OMTKY3,224286,5422
BMRB,5429,pKa value of P1-Lys OMTKY3,224286,5422
BMRB,5430,pKa value of P2-Asp OMTKY3,224286,5422
BMRB,5431,pKa value of P2-Glu OMTKY3,224286,5422
BMRB,5432,pKa value of P2-Val OMTKY3,224286,5422
BMRB,5433,pKa value of P2-His OMTKY3,224286,5422
BMRB,5434,pKa value of P2-Lys OMTKY3,224286,5422
BMRB,5435,pKa value of P4-Asp OMTKY3,224286,5422
BMRB,5436,pKa value of P4-Glu OMTKY3,224286,5422
BMRB,5437,pKa value of P4-His OMTKY3,224286,5422
BMRB,5438,pKa value of P4-Lys OMTKY3,224286,5422
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224286,5422
BMRB,5440,pKa value of P5-Asp OMTKY3,224286,5422
BMRB,5441,pKa value of P5-Glu OMTKY3,224286,5422
BMRB,5442,pKa value of P5-His OMTKY3,224286,5422
BMRB,5443,pKa value of P6-Asp OMTKY3,224286,5422
BMRB,5444,pKa value of P6-Glu OMTKY3,224286,5422
BMRB,5445,pKa value of P6-His OMTKY3,224286,5422
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224286,5422
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224286,5422
BMRB,5448,pKa value of OMTKY3 (no salt added),224286,5422
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224286,5422
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224286,5422
BMRB,5451,pKa value of AAPD,224286,5422
BMRB,5452,pKa value of AAPE,224286,5422
BMRB,5453,pKa value of AAPK,224286,5422
BMRB,4864,Chemical shifts of OMTKY3.,224300,5423
BMRB,5411,pKa value of OMTKY3,224300,5423
BMRB,5412,pKa value of P2'-Lys OMTKY3,224300,5423
BMRB,5413,pKa value of P2'-His OMTKY3,224300,5423
BMRB,5414,pKa value of P2'-GLU OMTKY3,224300,5423
BMRB,5415,pKa value of P2'-Asp OMTKY3,224300,5423
BMRB,5416,pKa value of P3'-Ala OMTKY3,224300,5423
BMRB,5417,pKa value of P3'-Asp OMTKY3,224300,5423
BMRB,5418,pKa value of P3'-Glu OMTKY3,224300,5423
BMRB,5419,pKa value of P3'-His OMTKY3,224300,5423
BMRB,5420,pKa value of P3'-Lys OMTKY3,224300,5423
BMRB,5421,pKa value of P1'-Asp OMTKY3,224300,5423
BMRB,5422,pKa value of P1'-His OMTKY3,224300,5423
BMRB,5424,pKa value of P1-Asp OMTKY3,224300,5423
BMRB,5425,pKa value of P1-Glu OMTKY3,224300,5423
BMRB,5426,pKa value of P1-Gly OMTKY3,224300,5423
BMRB,5427,pKa value of P1-Ala OMTKY3,224300,5423
BMRB,5428,pKa value of P1-His OMTKY3,224300,5423
BMRB,5429,pKa value of P1-Lys OMTKY3,224300,5423
BMRB,5430,pKa value of P2-Asp OMTKY3,224300,5423
BMRB,5431,pKa value of P2-Glu OMTKY3,224300,5423
BMRB,5432,pKa value of P2-Val OMTKY3,224300,5423
BMRB,5433,pKa value of P2-His OMTKY3,224300,5423
BMRB,5434,pKa value of P2-Lys OMTKY3,224300,5423
BMRB,5435,pKa value of P4-Asp OMTKY3,224300,5423
BMRB,5436,pKa value of P4-Glu OMTKY3,224300,5423
BMRB,5437,pKa value of P4-His OMTKY3,224300,5423
BMRB,5438,pKa value of P4-Lys OMTKY3,224300,5423
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224300,5423
BMRB,5440,pKa value of P5-Asp OMTKY3,224300,5423
BMRB,5441,pKa value of P5-Glu OMTKY3,224300,5423
BMRB,5442,pKa value of P5-His OMTKY3,224300,5423
BMRB,5443,pKa value of P6-Asp OMTKY3,224300,5423
BMRB,5444,pKa value of P6-Glu OMTKY3,224300,5423
BMRB,5445,pKa value of P6-His OMTKY3,224300,5423
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224300,5423
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224300,5423
BMRB,5448,pKa value of OMTKY3 (no salt added),224300,5423
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224300,5423
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224300,5423
BMRB,5451,pKa value of AAPD,224300,5423
BMRB,5452,pKa value of AAPE,224300,5423
BMRB,5453,pKa value of AAPK,224300,5423
BMRB,4864,Chemical shifts of OMTKY3.,224314,5424
BMRB,5411,pKa value of OMTKY3,224314,5424
BMRB,5412,pKa value of P2'-Lys OMTKY3,224314,5424
BMRB,5413,pKa value of P2'-His OMTKY3,224314,5424
BMRB,5414,pKa value of P2'-GLU OMTKY3,224314,5424
BMRB,5415,pKa value of P2'-Asp OMTKY3,224314,5424
BMRB,5416,pKa value of P3'-Ala OMTKY3,224314,5424
BMRB,5417,pKa value of P3'-Asp OMTKY3,224314,5424
BMRB,5418,pKa value of P3'-Glu OMTKY3,224314,5424
BMRB,5419,pKa value of P3'-His OMTKY3,224314,5424
BMRB,5420,pKa value of P3'-Lys OMTKY3,224314,5424
BMRB,5421,pKa value of P1'-Asp OMTKY3,224314,5424
BMRB,5422,pKa value of P1'-His OMTKY3,224314,5424
BMRB,5423,pKa value of P1'-Lys OMTKY3,224314,5424
BMRB,5425,pKa value of P1-Glu OMTKY3,224314,5424
BMRB,5426,pKa value of P1-Gly OMTKY3,224314,5424
BMRB,5427,pKa value of P1-Ala OMTKY3,224314,5424
BMRB,5428,pKa value of P1-His OMTKY3,224314,5424
BMRB,5429,pKa value of P1-Lys OMTKY3,224314,5424
BMRB,5430,pKa value of P2-Asp OMTKY3,224314,5424
BMRB,5431,pKa value of P2-Glu OMTKY3,224314,5424
BMRB,5432,pKa value of P2-Val OMTKY3,224314,5424
BMRB,5433,pKa value of P2-His OMTKY3,224314,5424
BMRB,5434,pKa value of P2-Lys OMTKY3,224314,5424
BMRB,5435,pKa value of P4-Asp OMTKY3,224314,5424
BMRB,5436,pKa value of P4-Glu OMTKY3,224314,5424
BMRB,5437,pKa value of P4-His OMTKY3,224314,5424
BMRB,5438,pKa value of P4-Lys OMTKY3,224314,5424
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224314,5424
BMRB,5440,pKa value of P5-Asp OMTKY3,224314,5424
BMRB,5441,pKa value of P5-Glu OMTKY3,224314,5424
BMRB,5442,pKa value of P5-His OMTKY3,224314,5424
BMRB,5443,pKa value of P6-Asp OMTKY3,224314,5424
BMRB,5444,pKa value of P6-Glu OMTKY3,224314,5424
BMRB,5445,pKa value of P6-His OMTKY3,224314,5424
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224314,5424
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224314,5424
BMRB,5448,pKa value of OMTKY3 (no salt added),224314,5424
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224314,5424
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224314,5424
BMRB,5451,pKa value of AAPD,224314,5424
BMRB,5452,pKa value of AAPE,224314,5424
BMRB,5453,pKa value of AAPK,224314,5424
BMRB,4864,Chemical shifts of OMTKY3.,224328,5425
BMRB,5411,pKa value of OMTKY3,224328,5425
BMRB,5412,pKa value of P2'-Lys OMTKY3,224328,5425
BMRB,5413,pKa value of P2'-His OMTKY3,224328,5425
BMRB,5414,pKa value of P2'-GLU OMTKY3,224328,5425
BMRB,5415,pKa value of P2'-Asp OMTKY3,224328,5425
BMRB,5416,pKa value of P3'-Ala OMTKY3,224328,5425
BMRB,5417,pKa value of P3'-Asp OMTKY3,224328,5425
BMRB,5418,pKa value of P3'-Glu OMTKY3,224328,5425
BMRB,5419,pKa value of P3'-His OMTKY3,224328,5425
BMRB,5420,pKa value of P3'-Lys OMTKY3,224328,5425
BMRB,5421,pKa value of P1'-Asp OMTKY3,224328,5425
BMRB,5422,pKa value of P1'-His OMTKY3,224328,5425
BMRB,5423,pKa value of P1'-Lys OMTKY3,224328,5425
BMRB,5424,pKa value of P1-Asp OMTKY3,224328,5425
BMRB,5426,pKa value of P1-Gly OMTKY3,224328,5425
BMRB,5427,pKa value of P1-Ala OMTKY3,224328,5425
BMRB,5428,pKa value of P1-His OMTKY3,224328,5425
BMRB,5429,pKa value of P1-Lys OMTKY3,224328,5425
BMRB,5430,pKa value of P2-Asp OMTKY3,224328,5425
BMRB,5431,pKa value of P2-Glu OMTKY3,224328,5425
BMRB,5432,pKa value of P2-Val OMTKY3,224328,5425
BMRB,5433,pKa value of P2-His OMTKY3,224328,5425
BMRB,5434,pKa value of P2-Lys OMTKY3,224328,5425
BMRB,5435,pKa value of P4-Asp OMTKY3,224328,5425
BMRB,5436,pKa value of P4-Glu OMTKY3,224328,5425
BMRB,5437,pKa value of P4-His OMTKY3,224328,5425
BMRB,5438,pKa value of P4-Lys OMTKY3,224328,5425
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224328,5425
BMRB,5440,pKa value of P5-Asp OMTKY3,224328,5425
BMRB,5441,pKa value of P5-Glu OMTKY3,224328,5425
BMRB,5442,pKa value of P5-His OMTKY3,224328,5425
BMRB,5443,pKa value of P6-Asp OMTKY3,224328,5425
BMRB,5444,pKa value of P6-Glu OMTKY3,224328,5425
BMRB,5445,pKa value of P6-His OMTKY3,224328,5425
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224328,5425
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224328,5425
BMRB,5448,pKa value of OMTKY3 (no salt added),224328,5425
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224328,5425
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224328,5425
BMRB,5451,pKa value of AAPD,224328,5425
BMRB,5452,pKa value of AAPE,224328,5425
BMRB,5453,pKa value of AAPK,224328,5425
BMRB,4864,Chemical shifts of OMTKY3.,224342,5426
BMRB,5411,pKa value of OMTKY3,224342,5426
BMRB,5412,pKa value of P2'-Lys OMTKY3,224342,5426
BMRB,5413,pKa value of P2'-His OMTKY3,224342,5426
BMRB,5414,pKa value of P2'-GLU OMTKY3,224342,5426
BMRB,5415,pKa value of P2'-Asp OMTKY3,224342,5426
BMRB,5416,pKa value of P3'-Ala OMTKY3,224342,5426
BMRB,5417,pKa value of P3'-Asp OMTKY3,224342,5426
BMRB,5418,pKa value of P3'-Glu OMTKY3,224342,5426
BMRB,5419,pKa value of P3'-His OMTKY3,224342,5426
BMRB,5420,pKa value of P3'-Lys OMTKY3,224342,5426
BMRB,5421,pKa value of P1'-Asp OMTKY3,224342,5426
BMRB,5422,pKa value of P1'-His OMTKY3,224342,5426
BMRB,5423,pKa value of P1'-Lys OMTKY3,224342,5426
BMRB,5424,pKa value of P1-Asp OMTKY3,224342,5426
BMRB,5425,pKa value of P1-Glu OMTKY3,224342,5426
BMRB,5427,pKa value of P1-Ala OMTKY3,224342,5426
BMRB,5428,pKa value of P1-His OMTKY3,224342,5426
BMRB,5429,pKa value of P1-Lys OMTKY3,224342,5426
BMRB,5430,pKa value of P2-Asp OMTKY3,224342,5426
BMRB,5431,pKa value of P2-Glu OMTKY3,224342,5426
BMRB,5432,pKa value of P2-Val OMTKY3,224342,5426
BMRB,5433,pKa value of P2-His OMTKY3,224342,5426
BMRB,5434,pKa value of P2-Lys OMTKY3,224342,5426
BMRB,5435,pKa value of P4-Asp OMTKY3,224342,5426
BMRB,5436,pKa value of P4-Glu OMTKY3,224342,5426
BMRB,5437,pKa value of P4-His OMTKY3,224342,5426
BMRB,5438,pKa value of P4-Lys OMTKY3,224342,5426
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224342,5426
BMRB,5440,pKa value of P5-Asp OMTKY3,224342,5426
BMRB,5441,pKa value of P5-Glu OMTKY3,224342,5426
BMRB,5442,pKa value of P5-His OMTKY3,224342,5426
BMRB,5443,pKa value of P6-Asp OMTKY3,224342,5426
BMRB,5444,pKa value of P6-Glu OMTKY3,224342,5426
BMRB,5445,pKa value of P6-His OMTKY3,224342,5426
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224342,5426
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224342,5426
BMRB,5448,pKa value of OMTKY3 (no salt added),224342,5426
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224342,5426
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224342,5426
BMRB,5451,pKa value of AAPD,224342,5426
BMRB,5452,pKa value of AAPE,224342,5426
BMRB,5453,pKa value of AAPK,224342,5426
BMRB,4864,Chemical shifts of OMTKY3.,224356,5427
BMRB,5411,pKa value of OMTKY3,224356,5427
BMRB,5412,pKa value of P2'-Lys OMTKY3,224356,5427
BMRB,5413,pKa value of P2'-His OMTKY3,224356,5427
BMRB,5414,pKa value of P2'-GLU OMTKY3,224356,5427
BMRB,5415,pKa value of P2'-Asp OMTKY3,224356,5427
BMRB,5416,pKa value of P3'-Ala OMTKY3,224356,5427
BMRB,5417,pKa value of P3'-Asp OMTKY3,224356,5427
BMRB,5418,pKa value of P3'-Glu OMTKY3,224356,5427
BMRB,5419,pKa value of P3'-His OMTKY3,224356,5427
BMRB,5420,pKa value of P3'-Lys OMTKY3,224356,5427
BMRB,5421,pKa value of P1'-Asp OMTKY3,224356,5427
BMRB,5422,pKa value of P1'-His OMTKY3,224356,5427
BMRB,5423,pKa value of P1'-Lys OMTKY3,224356,5427
BMRB,5424,pKa value of P1-Asp OMTKY3,224356,5427
BMRB,5425,pKa value of P1-Glu OMTKY3,224356,5427
BMRB,5426,pKa value of P1-Gly OMTKY3,224356,5427
BMRB,5428,pKa value of P1-His OMTKY3,224356,5427
BMRB,5429,pKa value of P1-Lys OMTKY3,224356,5427
BMRB,5430,pKa value of P2-Asp OMTKY3,224356,5427
BMRB,5431,pKa value of P2-Glu OMTKY3,224356,5427
BMRB,5432,pKa value of P2-Val OMTKY3,224356,5427
BMRB,5433,pKa value of P2-His OMTKY3,224356,5427
BMRB,5434,pKa value of P2-Lys OMTKY3,224356,5427
BMRB,5435,pKa value of P4-Asp OMTKY3,224356,5427
BMRB,5436,pKa value of P4-Glu OMTKY3,224356,5427
BMRB,5437,pKa value of P4-His OMTKY3,224356,5427
BMRB,5438,pKa value of P4-Lys OMTKY3,224356,5427
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224356,5427
BMRB,5440,pKa value of P5-Asp OMTKY3,224356,5427
BMRB,5441,pKa value of P5-Glu OMTKY3,224356,5427
BMRB,5442,pKa value of P5-His OMTKY3,224356,5427
BMRB,5443,pKa value of P6-Asp OMTKY3,224356,5427
BMRB,5444,pKa value of P6-Glu OMTKY3,224356,5427
BMRB,5445,pKa value of P6-His OMTKY3,224356,5427
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224356,5427
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224356,5427
BMRB,5448,pKa value of OMTKY3 (no salt added),224356,5427
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224356,5427
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224356,5427
BMRB,5451,pKa value of AAPD,224356,5427
BMRB,5452,pKa value of AAPE,224356,5427
BMRB,5453,pKa value of AAPK,224356,5427
BMRB,4864,Chemical shifts of OMTKY3.,224370,5428
BMRB,5411,pKa value of OMTKY3,224370,5428
BMRB,5412,pKa value of P2'-Lys OMTKY3,224370,5428
BMRB,5413,pKa value of P2'-His OMTKY3,224370,5428
BMRB,5414,pKa value of P2'-GLU OMTKY3,224370,5428
BMRB,5415,pKa value of P2'-Asp OMTKY3,224370,5428
BMRB,5416,pKa value of P3'-Ala OMTKY3,224370,5428
BMRB,5417,pKa value of P3'-Asp OMTKY3,224370,5428
BMRB,5418,pKa value of P3'-Glu OMTKY3,224370,5428
BMRB,5419,pKa value of P3'-His OMTKY3,224370,5428
BMRB,5420,pKa value of P3'-Lys OMTKY3,224370,5428
BMRB,5421,pKa value of P1'-Asp OMTKY3,224370,5428
BMRB,5422,pKa value of P1'-His OMTKY3,224370,5428
BMRB,5423,pKa value of P1'-Lys OMTKY3,224370,5428
BMRB,5424,pKa value of P1-Asp OMTKY3,224370,5428
BMRB,5425,pKa value of P1-Glu OMTKY3,224370,5428
BMRB,5426,pKa value of P1-Gly OMTKY3,224370,5428
BMRB,5427,pKa value of P1-Ala OMTKY3,224370,5428
BMRB,5429,pKa value of P1-Lys OMTKY3,224370,5428
BMRB,5430,pKa value of P2-Asp OMTKY3,224370,5428
BMRB,5431,pKa value of P2-Glu OMTKY3,224370,5428
BMRB,5432,pKa value of P2-Val OMTKY3,224370,5428
BMRB,5433,pKa value of P2-His OMTKY3,224370,5428
BMRB,5434,pKa value of P2-Lys OMTKY3,224370,5428
BMRB,5435,pKa value of P4-Asp OMTKY3,224370,5428
BMRB,5436,pKa value of P4-Glu OMTKY3,224370,5428
BMRB,5437,pKa value of P4-His OMTKY3,224370,5428
BMRB,5438,pKa value of P4-Lys OMTKY3,224370,5428
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224370,5428
BMRB,5440,pKa value of P5-Asp OMTKY3,224370,5428
BMRB,5441,pKa value of P5-Glu OMTKY3,224370,5428
BMRB,5442,pKa value of P5-His OMTKY3,224370,5428
BMRB,5443,pKa value of P6-Asp OMTKY3,224370,5428
BMRB,5444,pKa value of P6-Glu OMTKY3,224370,5428
BMRB,5445,pKa value of P6-His OMTKY3,224370,5428
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224370,5428
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224370,5428
BMRB,5448,pKa value of OMTKY3 (no salt added),224370,5428
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224370,5428
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224370,5428
BMRB,5451,pKa value of AAPD,224370,5428
BMRB,5452,pKa value of AAPE,224370,5428
BMRB,5453,pKa value of AAPK,224370,5428
BMRB,4864,Chemical shifts of OMTKY3.,224384,5429
BMRB,5411,pKa value of OMTKY3,224384,5429
BMRB,5412,pKa value of P2'-Lys OMTKY3,224384,5429
BMRB,5413,pKa value of P2'-His OMTKY3,224384,5429
BMRB,5414,pKa value of P2'-GLU OMTKY3,224384,5429
BMRB,5415,pKa value of P2'-Asp OMTKY3,224384,5429
BMRB,5416,pKa value of P3'-Ala OMTKY3,224384,5429
BMRB,5417,pKa value of P3'-Asp OMTKY3,224384,5429
BMRB,5418,pKa value of P3'-Glu OMTKY3,224384,5429
BMRB,5419,pKa value of P3'-His OMTKY3,224384,5429
BMRB,5420,pKa value of P3'-Lys OMTKY3,224384,5429
BMRB,5421,pKa value of P1'-Asp OMTKY3,224384,5429
BMRB,5422,pKa value of P1'-His OMTKY3,224384,5429
BMRB,5423,pKa value of P1'-Lys OMTKY3,224384,5429
BMRB,5424,pKa value of P1-Asp OMTKY3,224384,5429
BMRB,5425,pKa value of P1-Glu OMTKY3,224384,5429
BMRB,5426,pKa value of P1-Gly OMTKY3,224384,5429
BMRB,5427,pKa value of P1-Ala OMTKY3,224384,5429
BMRB,5428,pKa value of P1-His OMTKY3,224384,5429
BMRB,5430,pKa value of P2-Asp OMTKY3,224384,5429
BMRB,5431,pKa value of P2-Glu OMTKY3,224384,5429
BMRB,5432,pKa value of P2-Val OMTKY3,224384,5429
BMRB,5433,pKa value of P2-His OMTKY3,224384,5429
BMRB,5434,pKa value of P2-Lys OMTKY3,224384,5429
BMRB,5435,pKa value of P4-Asp OMTKY3,224384,5429
BMRB,5436,pKa value of P4-Glu OMTKY3,224384,5429
BMRB,5437,pKa value of P4-His OMTKY3,224384,5429
BMRB,5438,pKa value of P4-Lys OMTKY3,224384,5429
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224384,5429
BMRB,5440,pKa value of P5-Asp OMTKY3,224384,5429
BMRB,5441,pKa value of P5-Glu OMTKY3,224384,5429
BMRB,5442,pKa value of P5-His OMTKY3,224384,5429
BMRB,5443,pKa value of P6-Asp OMTKY3,224384,5429
BMRB,5444,pKa value of P6-Glu OMTKY3,224384,5429
BMRB,5445,pKa value of P6-His OMTKY3,224384,5429
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224384,5429
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224384,5429
BMRB,5448,pKa value of OMTKY3 (no salt added),224384,5429
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224384,5429
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224384,5429
BMRB,5451,pKa value of AAPD,224384,5429
BMRB,5452,pKa value of AAPE,224384,5429
BMRB,5453,pKa value of AAPK,224384,5429
BMRB,4864,Chemical shifts of OMTKY3.,224414,5430
BMRB,5411,pKa value of OMTKY3,224414,5430
BMRB,5412,pKa value of P2'-Lys OMTKY3,224414,5430
BMRB,5413,pKa value of P2'-His OMTKY3,224414,5430
BMRB,5414,pKa value of P2'-GLU OMTKY3,224414,5430
BMRB,5415,pKa value of P2'-Asp OMTKY3,224414,5430
BMRB,5416,pKa value of P3'-Ala OMTKY3,224414,5430
BMRB,5417,pKa value of P3'-Asp OMTKY3,224414,5430
BMRB,5418,pKa value of P3'-Glu OMTKY3,224414,5430
BMRB,5419,pKa value of P3'-His OMTKY3,224414,5430
BMRB,5420,pKa value of P3'-Lys OMTKY3,224414,5430
BMRB,5421,pKa value of P1'-Asp OMTKY3,224414,5430
BMRB,5422,pKa value of P1'-His OMTKY3,224414,5430
BMRB,5423,pKa value of P1'-Lys OMTKY3,224414,5430
BMRB,5424,pKa value of P1-Asp OMTKY3,224414,5430
BMRB,5425,pKa value of P1-Glu OMTKY3,224414,5430
BMRB,5426,pKa value of P1-Gly OMTKY3,224414,5430
BMRB,5427,pKa value of P1-Ala OMTKY3,224414,5430
BMRB,5428,pKa value of P1-His OMTKY3,224414,5430
BMRB,5429,pKa value of P1-Lys OMTKY3,224414,5430
BMRB,5431,pKa value of P2-Glu OMTKY3,224414,5430
BMRB,5432,pKa value of P2-Val OMTKY3,224414,5430
BMRB,5433,pKa value of P2-His OMTKY3,224414,5430
BMRB,5434,pKa value of P2-Lys OMTKY3,224414,5430
BMRB,5435,pKa value of P4-Asp OMTKY3,224414,5430
BMRB,5436,pKa value of P4-Glu OMTKY3,224414,5430
BMRB,5437,pKa value of P4-His OMTKY3,224414,5430
BMRB,5438,pKa value of P4-Lys OMTKY3,224414,5430
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224414,5430
BMRB,5440,pKa value of P5-Asp OMTKY3,224414,5430
BMRB,5441,pKa value of P5-Glu OMTKY3,224414,5430
BMRB,5442,pKa value of P5-His OMTKY3,224414,5430
BMRB,5443,pKa value of P6-Asp OMTKY3,224414,5430
BMRB,5444,pKa value of P6-Glu OMTKY3,224414,5430
BMRB,5445,pKa value of P6-His OMTKY3,224414,5430
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224414,5430
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224414,5430
BMRB,5448,pKa value of OMTKY3 (no salt added),224414,5430
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224414,5430
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224414,5430
BMRB,5451,pKa value of AAPD,224414,5430
BMRB,5452,pKa value of AAPE,224414,5430
BMRB,5453,pKa value of AAPK,224414,5430
BMRB,4864,Chemical shifts of OMTKY3.,224428,5431
BMRB,5411,pKa value of OMTKY3,224428,5431
BMRB,5412,pKa value of P2'-Lys OMTKY3,224428,5431
BMRB,5413,pKa value of P2'-His OMTKY3,224428,5431
BMRB,5414,pKa value of P2'-GLU OMTKY3,224428,5431
BMRB,5415,pKa value of P2'-Asp OMTKY3,224428,5431
BMRB,5416,pKa value of P3'-Ala OMTKY3,224428,5431
BMRB,5417,pKa value of P3'-Asp OMTKY3,224428,5431
BMRB,5418,pKa value of P3'-Glu OMTKY3,224428,5431
BMRB,5419,pKa value of P3'-His OMTKY3,224428,5431
BMRB,5420,pKa value of P3'-Lys OMTKY3,224428,5431
BMRB,5421,pKa value of P1'-Asp OMTKY3,224428,5431
BMRB,5422,pKa value of P1'-His OMTKY3,224428,5431
BMRB,5423,pKa value of P1'-Lys OMTKY3,224428,5431
BMRB,5424,pKa value of P1-Asp OMTKY3,224428,5431
BMRB,5425,pKa value of P1-Glu OMTKY3,224428,5431
BMRB,5426,pKa value of P1-Gly OMTKY3,224428,5431
BMRB,5427,pKa value of P1-Ala OMTKY3,224428,5431
BMRB,5428,pKa value of P1-His OMTKY3,224428,5431
BMRB,5429,pKa value of P1-Lys OMTKY3,224428,5431
BMRB,5430,pKa value of P2-Asp OMTKY3,224428,5431
BMRB,5432,pKa value of P2-Val OMTKY3,224428,5431
BMRB,5433,pKa value of P2-His OMTKY3,224428,5431
BMRB,5434,pKa value of P2-Lys OMTKY3,224428,5431
BMRB,5435,pKa value of P4-Asp OMTKY3,224428,5431
BMRB,5436,pKa value of P4-Glu OMTKY3,224428,5431
BMRB,5437,pKa value of P4-His OMTKY3,224428,5431
BMRB,5438,pKa value of P4-Lys OMTKY3,224428,5431
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224428,5431
BMRB,5440,pKa value of P5-Asp OMTKY3,224428,5431
BMRB,5441,pKa value of P5-Glu OMTKY3,224428,5431
BMRB,5442,pKa value of P5-His OMTKY3,224428,5431
BMRB,5443,pKa value of P6-Asp OMTKY3,224428,5431
BMRB,5444,pKa value of P6-Glu OMTKY3,224428,5431
BMRB,5445,pKa value of P6-His OMTKY3,224428,5431
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224428,5431
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224428,5431
BMRB,5448,pKa value of OMTKY3 (no salt added),224428,5431
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224428,5431
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224428,5431
BMRB,5451,pKa value of AAPD,224428,5431
BMRB,5452,pKa value of AAPE,224428,5431
BMRB,5453,pKa value of AAPK,224428,5431
BMRB,4864,Chemical shifts of OMTKY3.,224442,5432
BMRB,5411,pKa value of OMTKY3,224442,5432
BMRB,5412,pKa value of P2'-Lys OMTKY3,224442,5432
BMRB,5413,pKa value of P2'-His OMTKY3,224442,5432
BMRB,5414,pKa value of P2'-GLU OMTKY3,224442,5432
BMRB,5415,pKa value of P2'-Asp OMTKY3,224442,5432
BMRB,5416,pKa value of P3'-Ala OMTKY3,224442,5432
BMRB,5417,pKa value of P3'-Asp OMTKY3,224442,5432
BMRB,5418,pKa value of P3'-Glu OMTKY3,224442,5432
BMRB,5419,pKa value of P3'-His OMTKY3,224442,5432
BMRB,5420,pKa value of P3'-Lys OMTKY3,224442,5432
BMRB,5421,pKa value of P1'-Asp OMTKY3,224442,5432
BMRB,5422,pKa value of P1'-His OMTKY3,224442,5432
BMRB,5423,pKa value of P1'-Lys OMTKY3,224442,5432
BMRB,5424,pKa value of P1-Asp OMTKY3,224442,5432
BMRB,5425,pKa value of P1-Glu OMTKY3,224442,5432
BMRB,5426,pKa value of P1-Gly OMTKY3,224442,5432
BMRB,5427,pKa value of P1-Ala OMTKY3,224442,5432
BMRB,5428,pKa value of P1-His OMTKY3,224442,5432
BMRB,5429,pKa value of P1-Lys OMTKY3,224442,5432
BMRB,5430,pKa value of P2-Asp OMTKY3,224442,5432
BMRB,5431,pKa value of P2-Glu OMTKY3,224442,5432
BMRB,5433,pKa value of P2-His OMTKY3,224442,5432
BMRB,5434,pKa value of P2-Lys OMTKY3,224442,5432
BMRB,5435,pKa value of P4-Asp OMTKY3,224442,5432
BMRB,5436,pKa value of P4-Glu OMTKY3,224442,5432
BMRB,5437,pKa value of P4-His OMTKY3,224442,5432
BMRB,5438,pKa value of P4-Lys OMTKY3,224442,5432
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224442,5432
BMRB,5440,pKa value of P5-Asp OMTKY3,224442,5432
BMRB,5441,pKa value of P5-Glu OMTKY3,224442,5432
BMRB,5442,pKa value of P5-His OMTKY3,224442,5432
BMRB,5443,pKa value of P6-Asp OMTKY3,224442,5432
BMRB,5444,pKa value of P6-Glu OMTKY3,224442,5432
BMRB,5445,pKa value of P6-His OMTKY3,224442,5432
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224442,5432
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224442,5432
BMRB,5448,pKa value of OMTKY3 (no salt added),224442,5432
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224442,5432
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224442,5432
BMRB,5451,pKa value of AAPD,224442,5432
BMRB,5452,pKa value of AAPE,224442,5432
BMRB,5453,pKa value of AAPK,224442,5432
BMRB,4864,Chemical shifts of OMTKY3.,224456,5433
BMRB,5411,pKa value of OMTKY3,224456,5433
BMRB,5412,pKa value of P2'-Lys OMTKY3,224456,5433
BMRB,5413,pKa value of P2'-His OMTKY3,224456,5433
BMRB,5414,pKa value of P2'-GLU OMTKY3,224456,5433
BMRB,5415,pKa value of P2'-Asp OMTKY3,224456,5433
BMRB,5416,pKa value of P3'-Ala OMTKY3,224456,5433
BMRB,5417,pKa value of P3'-Asp OMTKY3,224456,5433
BMRB,5418,pKa value of P3'-Glu OMTKY3,224456,5433
BMRB,5419,pKa value of P3'-His OMTKY3,224456,5433
BMRB,5420,pKa value of P3'-Lys OMTKY3,224456,5433
BMRB,5421,pKa value of P1'-Asp OMTKY3,224456,5433
BMRB,5422,pKa value of P1'-His OMTKY3,224456,5433
BMRB,5423,pKa value of P1'-Lys OMTKY3,224456,5433
BMRB,5424,pKa value of P1-Asp OMTKY3,224456,5433
BMRB,5425,pKa value of P1-Glu OMTKY3,224456,5433
BMRB,5426,pKa value of P1-Gly OMTKY3,224456,5433
BMRB,5427,pKa value of P1-Ala OMTKY3,224456,5433
BMRB,5428,pKa value of P1-His OMTKY3,224456,5433
BMRB,5429,pKa value of P1-Lys OMTKY3,224456,5433
BMRB,5430,pKa value of P2-Asp OMTKY3,224456,5433
BMRB,5431,pKa value of P2-Glu OMTKY3,224456,5433
BMRB,5432,pKa value of P2-Val OMTKY3,224456,5433
BMRB,5434,pKa value of P2-Lys OMTKY3,224456,5433
BMRB,5435,pKa value of P4-Asp OMTKY3,224456,5433
BMRB,5436,pKa value of P4-Glu OMTKY3,224456,5433
BMRB,5437,pKa value of P4-His OMTKY3,224456,5433
BMRB,5438,pKa value of P4-Lys OMTKY3,224456,5433
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224456,5433
BMRB,5440,pKa value of P5-Asp OMTKY3,224456,5433
BMRB,5441,pKa value of P5-Glu OMTKY3,224456,5433
BMRB,5442,pKa value of P5-His OMTKY3,224456,5433
BMRB,5443,pKa value of P6-Asp OMTKY3,224456,5433
BMRB,5444,pKa value of P6-Glu OMTKY3,224456,5433
BMRB,5445,pKa value of P6-His OMTKY3,224456,5433
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224456,5433
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224456,5433
BMRB,5448,pKa value of OMTKY3 (no salt added),224456,5433
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224456,5433
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224456,5433
BMRB,5451,pKa value of AAPD,224456,5433
BMRB,5452,pKa value of AAPE,224456,5433
BMRB,5453,pKa value of AAPK,224456,5433
BMRB,4864,Chemical shifts of OMTKY3.,224470,5434
BMRB,5411,pKa value of OMTKY3,224470,5434
BMRB,5412,pKa value of P2'-Lys OMTKY3,224470,5434
BMRB,5413,pKa value of P2'-His OMTKY3,224470,5434
BMRB,5414,pKa value of P2'-GLU OMTKY3,224470,5434
BMRB,5415,pKa value of P2'-Asp OMTKY3,224470,5434
BMRB,5416,pKa value of P3'-Ala OMTKY3,224470,5434
BMRB,5417,pKa value of P3'-Asp OMTKY3,224470,5434
BMRB,5418,pKa value of P3'-Glu OMTKY3,224470,5434
BMRB,5419,pKa value of P3'-His OMTKY3,224470,5434
BMRB,5420,pKa value of P3'-Lys OMTKY3,224470,5434
BMRB,5421,pKa value of P1'-Asp OMTKY3,224470,5434
BMRB,5422,pKa value of P1'-His OMTKY3,224470,5434
BMRB,5423,pKa value of P1'-Lys OMTKY3,224470,5434
BMRB,5424,pKa value of P1-Asp OMTKY3,224470,5434
BMRB,5425,pKa value of P1-Glu OMTKY3,224470,5434
BMRB,5426,pKa value of P1-Gly OMTKY3,224470,5434
BMRB,5427,pKa value of P1-Ala OMTKY3,224470,5434
BMRB,5428,pKa value of P1-His OMTKY3,224470,5434
BMRB,5429,pKa value of P1-Lys OMTKY3,224470,5434
BMRB,5430,pKa value of P2-Asp OMTKY3,224470,5434
BMRB,5431,pKa value of P2-Glu OMTKY3,224470,5434
BMRB,5432,pKa value of P2-Val OMTKY3,224470,5434
BMRB,5433,pKa value of P2-His OMTKY3,224470,5434
BMRB,5435,pKa value of P4-Asp OMTKY3,224470,5434
BMRB,5436,pKa value of P4-Glu OMTKY3,224470,5434
BMRB,5437,pKa value of P4-His OMTKY3,224470,5434
BMRB,5438,pKa value of P4-Lys OMTKY3,224470,5434
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224470,5434
BMRB,5440,pKa value of P5-Asp OMTKY3,224470,5434
BMRB,5441,pKa value of P5-Glu OMTKY3,224470,5434
BMRB,5442,pKa value of P5-His OMTKY3,224470,5434
BMRB,5443,pKa value of P6-Asp OMTKY3,224470,5434
BMRB,5444,pKa value of P6-Glu OMTKY3,224470,5434
BMRB,5445,pKa value of P6-His OMTKY3,224470,5434
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224470,5434
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224470,5434
BMRB,5448,pKa value of OMTKY3 (no salt added),224470,5434
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224470,5434
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224470,5434
BMRB,5451,pKa value of AAPD,224470,5434
BMRB,5452,pKa value of AAPE,224470,5434
BMRB,5453,pKa value of AAPK,224470,5434
BMRB,4864,Chemical shifts of OMTKY3.,224484,5435
BMRB,5411,pKa value of OMTKY3,224484,5435
BMRB,5412,pKa value of P2'-Lys OMTKY3,224484,5435
BMRB,5413,pKa value of P2'-His OMTKY3,224484,5435
BMRB,5414,pKa value of P2'-GLU OMTKY3,224484,5435
BMRB,5415,pKa value of P2'-Asp OMTKY3,224484,5435
BMRB,5416,pKa value of P3'-Ala OMTKY3,224484,5435
BMRB,5417,pKa value of P3'-Asp OMTKY3,224484,5435
BMRB,5418,pKa value of P3'-Glu OMTKY3,224484,5435
BMRB,5419,pKa value of P3'-His OMTKY3,224484,5435
BMRB,5420,pKa value of P3'-Lys OMTKY3,224484,5435
BMRB,5421,pKa value of P1'-Asp OMTKY3,224484,5435
BMRB,5422,pKa value of P1'-His OMTKY3,224484,5435
BMRB,5423,pKa value of P1'-Lys OMTKY3,224484,5435
BMRB,5424,pKa value of P1-Asp OMTKY3,224484,5435
BMRB,5425,pKa value of P1-Glu OMTKY3,224484,5435
BMRB,5426,pKa value of P1-Gly OMTKY3,224484,5435
BMRB,5427,pKa value of P1-Ala OMTKY3,224484,5435
BMRB,5428,pKa value of P1-His OMTKY3,224484,5435
BMRB,5429,pKa value of P1-Lys OMTKY3,224484,5435
BMRB,5430,pKa value of P2-Asp OMTKY3,224484,5435
BMRB,5431,pKa value of P2-Glu OMTKY3,224484,5435
BMRB,5432,pKa value of P2-Val OMTKY3,224484,5435
BMRB,5433,pKa value of P2-His OMTKY3,224484,5435
BMRB,5434,pKa value of P2-Lys OMTKY3,224484,5435
BMRB,5436,pKa value of P4-Glu OMTKY3,224484,5435
BMRB,5437,pKa value of P4-His OMTKY3,224484,5435
BMRB,5438,pKa value of P4-Lys OMTKY3,224484,5435
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224484,5435
BMRB,5440,pKa value of P5-Asp OMTKY3,224484,5435
BMRB,5441,pKa value of P5-Glu OMTKY3,224484,5435
BMRB,5442,pKa value of P5-His OMTKY3,224484,5435
BMRB,5443,pKa value of P6-Asp OMTKY3,224484,5435
BMRB,5444,pKa value of P6-Glu OMTKY3,224484,5435
BMRB,5445,pKa value of P6-His OMTKY3,224484,5435
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224484,5435
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224484,5435
BMRB,5448,pKa value of OMTKY3 (no salt added),224484,5435
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224484,5435
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224484,5435
BMRB,5451,pKa value of AAPD,224484,5435
BMRB,5452,pKa value of AAPE,224484,5435
BMRB,5453,pKa value of AAPK,224484,5435
BMRB,4864,Chemical shifts of OMTKY3.,224498,5436
BMRB,5411,pKa value of OMTKY3,224498,5436
BMRB,5412,pKa value of P2'-Lys OMTKY3,224498,5436
BMRB,5413,pKa value of P2'-His OMTKY3,224498,5436
BMRB,5414,pKa value of P2'-GLU OMTKY3,224498,5436
BMRB,5415,pKa value of P2'-Asp OMTKY3,224498,5436
BMRB,5416,pKa value of P3'-Ala OMTKY3,224498,5436
BMRB,5417,pKa value of P3'-Asp OMTKY3,224498,5436
BMRB,5418,pKa value of P3'-Glu OMTKY3,224498,5436
BMRB,5419,pKa value of P3'-His OMTKY3,224498,5436
BMRB,5420,pKa value of P3'-Lys OMTKY3,224498,5436
BMRB,5421,pKa value of P1'-Asp OMTKY3,224498,5436
BMRB,5422,pKa value of P1'-His OMTKY3,224498,5436
BMRB,5423,pKa value of P1'-Lys OMTKY3,224498,5436
BMRB,5424,pKa value of P1-Asp OMTKY3,224498,5436
BMRB,5425,pKa value of P1-Glu OMTKY3,224498,5436
BMRB,5426,pKa value of P1-Gly OMTKY3,224498,5436
BMRB,5427,pKa value of P1-Ala OMTKY3,224498,5436
BMRB,5428,pKa value of P1-His OMTKY3,224498,5436
BMRB,5429,pKa value of P1-Lys OMTKY3,224498,5436
BMRB,5430,pKa value of P2-Asp OMTKY3,224498,5436
BMRB,5431,pKa value of P2-Glu OMTKY3,224498,5436
BMRB,5432,pKa value of P2-Val OMTKY3,224498,5436
BMRB,5433,pKa value of P2-His OMTKY3,224498,5436
BMRB,5434,pKa value of P2-Lys OMTKY3,224498,5436
BMRB,5435,pKa value of P4-Asp OMTKY3,224498,5436
BMRB,5437,pKa value of P4-His OMTKY3,224498,5436
BMRB,5438,pKa value of P4-Lys OMTKY3,224498,5436
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224498,5436
BMRB,5440,pKa value of P5-Asp OMTKY3,224498,5436
BMRB,5441,pKa value of P5-Glu OMTKY3,224498,5436
BMRB,5442,pKa value of P5-His OMTKY3,224498,5436
BMRB,5443,pKa value of P6-Asp OMTKY3,224498,5436
BMRB,5444,pKa value of P6-Glu OMTKY3,224498,5436
BMRB,5445,pKa value of P6-His OMTKY3,224498,5436
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224498,5436
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224498,5436
BMRB,5448,pKa value of OMTKY3 (no salt added),224498,5436
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224498,5436
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224498,5436
BMRB,5451,pKa value of AAPD,224498,5436
BMRB,5452,pKa value of AAPE,224498,5436
BMRB,5453,pKa value of AAPK,224498,5436
BMRB,4864,Chemical shifts of OMTKY3.,224512,5437
BMRB,5411,pKa value of OMTKY3,224512,5437
BMRB,5412,pKa value of P2'-Lys OMTKY3,224512,5437
BMRB,5413,pKa value of P2'-His OMTKY3,224512,5437
BMRB,5414,pKa value of P2'-GLU OMTKY3,224512,5437
BMRB,5415,pKa value of P2'-Asp OMTKY3,224512,5437
BMRB,5416,pKa value of P3'-Ala OMTKY3,224512,5437
BMRB,5417,pKa value of P3'-Asp OMTKY3,224512,5437
BMRB,5418,pKa value of P3'-Glu OMTKY3,224512,5437
BMRB,5419,pKa value of P3'-His OMTKY3,224512,5437
BMRB,5420,pKa value of P3'-Lys OMTKY3,224512,5437
BMRB,5421,pKa value of P1'-Asp OMTKY3,224512,5437
BMRB,5422,pKa value of P1'-His OMTKY3,224512,5437
BMRB,5423,pKa value of P1'-Lys OMTKY3,224512,5437
BMRB,5424,pKa value of P1-Asp OMTKY3,224512,5437
BMRB,5425,pKa value of P1-Glu OMTKY3,224512,5437
BMRB,5426,pKa value of P1-Gly OMTKY3,224512,5437
BMRB,5427,pKa value of P1-Ala OMTKY3,224512,5437
BMRB,5428,pKa value of P1-His OMTKY3,224512,5437
BMRB,5429,pKa value of P1-Lys OMTKY3,224512,5437
BMRB,5430,pKa value of P2-Asp OMTKY3,224512,5437
BMRB,5431,pKa value of P2-Glu OMTKY3,224512,5437
BMRB,5432,pKa value of P2-Val OMTKY3,224512,5437
BMRB,5433,pKa value of P2-His OMTKY3,224512,5437
BMRB,5434,pKa value of P2-Lys OMTKY3,224512,5437
BMRB,5435,pKa value of P4-Asp OMTKY3,224512,5437
BMRB,5436,pKa value of P4-Glu OMTKY3,224512,5437
BMRB,5438,pKa value of P4-Lys OMTKY3,224512,5437
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224512,5437
BMRB,5440,pKa value of P5-Asp OMTKY3,224512,5437
BMRB,5441,pKa value of P5-Glu OMTKY3,224512,5437
BMRB,5442,pKa value of P5-His OMTKY3,224512,5437
BMRB,5443,pKa value of P6-Asp OMTKY3,224512,5437
BMRB,5444,pKa value of P6-Glu OMTKY3,224512,5437
BMRB,5445,pKa value of P6-His OMTKY3,224512,5437
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224512,5437
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224512,5437
BMRB,5448,pKa value of OMTKY3 (no salt added),224512,5437
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224512,5437
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224512,5437
BMRB,5451,pKa value of AAPD,224512,5437
BMRB,5452,pKa value of AAPE,224512,5437
BMRB,5453,pKa value of AAPK,224512,5437
BMRB,4864,Chemical shifts of OMTKY3.,224526,5438
BMRB,5411,pKa value of OMTKY3,224526,5438
BMRB,5412,pKa value of P2'-Lys OMTKY3,224526,5438
BMRB,5413,pKa value of P2'-His OMTKY3,224526,5438
BMRB,5414,pKa value of P2'-GLU OMTKY3,224526,5438
BMRB,5415,pKa value of P2'-Asp OMTKY3,224526,5438
BMRB,5416,pKa value of P3'-Ala OMTKY3,224526,5438
BMRB,5417,pKa value of P3'-Asp OMTKY3,224526,5438
BMRB,5418,pKa value of P3'-Glu OMTKY3,224526,5438
BMRB,5419,pKa value of P3'-His OMTKY3,224526,5438
BMRB,5420,pKa value of P3'-Lys OMTKY3,224526,5438
BMRB,5421,pKa value of P1'-Asp OMTKY3,224526,5438
BMRB,5422,pKa value of P1'-His OMTKY3,224526,5438
BMRB,5423,pKa value of P1'-Lys OMTKY3,224526,5438
BMRB,5424,pKa value of P1-Asp OMTKY3,224526,5438
BMRB,5425,pKa value of P1-Glu OMTKY3,224526,5438
BMRB,5426,pKa value of P1-Gly OMTKY3,224526,5438
BMRB,5427,pKa value of P1-Ala OMTKY3,224526,5438
BMRB,5428,pKa value of P1-His OMTKY3,224526,5438
BMRB,5429,pKa value of P1-Lys OMTKY3,224526,5438
BMRB,5430,pKa value of P2-Asp OMTKY3,224526,5438
BMRB,5431,pKa value of P2-Glu OMTKY3,224526,5438
BMRB,5432,pKa value of P2-Val OMTKY3,224526,5438
BMRB,5433,pKa value of P2-His OMTKY3,224526,5438
BMRB,5434,pKa value of P2-Lys OMTKY3,224526,5438
BMRB,5435,pKa value of P4-Asp OMTKY3,224526,5438
BMRB,5436,pKa value of P4-Glu OMTKY3,224526,5438
BMRB,5437,pKa value of P4-His OMTKY3,224526,5438
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224526,5438
BMRB,5440,pKa value of P5-Asp OMTKY3,224526,5438
BMRB,5441,pKa value of P5-Glu OMTKY3,224526,5438
BMRB,5442,pKa value of P5-His OMTKY3,224526,5438
BMRB,5443,pKa value of P6-Asp OMTKY3,224526,5438
BMRB,5444,pKa value of P6-Glu OMTKY3,224526,5438
BMRB,5445,pKa value of P6-His OMTKY3,224526,5438
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224526,5438
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224526,5438
BMRB,5448,pKa value of OMTKY3 (no salt added),224526,5438
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224526,5438
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224526,5438
BMRB,5451,pKa value of AAPD,224526,5438
BMRB,5452,pKa value of AAPE,224526,5438
BMRB,5453,pKa value of AAPK,224526,5438
BMRB,4864,Chemical shifts of OMTKY3.,224540,5439
BMRB,5411,pKa value of OMTKY3,224540,5439
BMRB,5412,pKa value of P2'-Lys OMTKY3,224540,5439
BMRB,5413,pKa value of P2'-His OMTKY3,224540,5439
BMRB,5414,pKa value of P2'-GLU OMTKY3,224540,5439
BMRB,5415,pKa value of P2'-Asp OMTKY3,224540,5439
BMRB,5416,pKa value of P3'-Ala OMTKY3,224540,5439
BMRB,5417,pKa value of P3'-Asp OMTKY3,224540,5439
BMRB,5418,pKa value of P3'-Glu OMTKY3,224540,5439
BMRB,5419,pKa value of P3'-His OMTKY3,224540,5439
BMRB,5420,pKa value of P3'-Lys OMTKY3,224540,5439
BMRB,5421,pKa value of P1'-Asp OMTKY3,224540,5439
BMRB,5422,pKa value of P1'-His OMTKY3,224540,5439
BMRB,5423,pKa value of P1'-Lys OMTKY3,224540,5439
BMRB,5424,pKa value of P1-Asp OMTKY3,224540,5439
BMRB,5425,pKa value of P1-Glu OMTKY3,224540,5439
BMRB,5426,pKa value of P1-Gly OMTKY3,224540,5439
BMRB,5427,pKa value of P1-Ala OMTKY3,224540,5439
BMRB,5428,pKa value of P1-His OMTKY3,224540,5439
BMRB,5429,pKa value of P1-Lys OMTKY3,224540,5439
BMRB,5430,pKa value of P2-Asp OMTKY3,224540,5439
BMRB,5431,pKa value of P2-Glu OMTKY3,224540,5439
BMRB,5432,pKa value of P2-Val OMTKY3,224540,5439
BMRB,5433,pKa value of P2-His OMTKY3,224540,5439
BMRB,5434,pKa value of P2-Lys OMTKY3,224540,5439
BMRB,5435,pKa value of P4-Asp OMTKY3,224540,5439
BMRB,5436,pKa value of P4-Glu OMTKY3,224540,5439
BMRB,5437,pKa value of P4-His OMTKY3,224540,5439
BMRB,5438,pKa value of P4-Lys OMTKY3,224540,5439
BMRB,5440,pKa value of P5-Asp OMTKY3,224540,5439
BMRB,5441,pKa value of P5-Glu OMTKY3,224540,5439
BMRB,5442,pKa value of P5-His OMTKY3,224540,5439
BMRB,5443,pKa value of P6-Asp OMTKY3,224540,5439
BMRB,5444,pKa value of P6-Glu OMTKY3,224540,5439
BMRB,5445,pKa value of P6-His OMTKY3,224540,5439
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224540,5439
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224540,5439
BMRB,5448,pKa value of OMTKY3 (no salt added),224540,5439
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224540,5439
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224540,5439
BMRB,5451,pKa value of AAPD,224540,5439
BMRB,5452,pKa value of AAPE,224540,5439
BMRB,5453,pKa value of AAPK,224540,5439
BMRB,4864,Chemical shifts of OMTKY3.,224570,5440
BMRB,5411,pKa value of OMTKY3,224570,5440
BMRB,5412,pKa value of P2'-Lys OMTKY3,224570,5440
BMRB,5413,pKa value of P2'-His OMTKY3,224570,5440
BMRB,5414,pKa value of P2'-GLU OMTKY3,224570,5440
BMRB,5415,pKa value of P2'-Asp OMTKY3,224570,5440
BMRB,5416,pKa value of P3'-Ala OMTKY3,224570,5440
BMRB,5417,pKa value of P3'-Asp OMTKY3,224570,5440
BMRB,5418,pKa value of P3'-Glu OMTKY3,224570,5440
BMRB,5419,pKa value of P3'-His OMTKY3,224570,5440
BMRB,5420,pKa value of P3'-Lys OMTKY3,224570,5440
BMRB,5421,pKa value of P1'-Asp OMTKY3,224570,5440
BMRB,5422,pKa value of P1'-His OMTKY3,224570,5440
BMRB,5423,pKa value of P1'-Lys OMTKY3,224570,5440
BMRB,5424,pKa value of P1-Asp OMTKY3,224570,5440
BMRB,5425,pKa value of P1-Glu OMTKY3,224570,5440
BMRB,5426,pKa value of P1-Gly OMTKY3,224570,5440
BMRB,5427,pKa value of P1-Ala OMTKY3,224570,5440
BMRB,5428,pKa value of P1-His OMTKY3,224570,5440
BMRB,5429,pKa value of P1-Lys OMTKY3,224570,5440
BMRB,5430,pKa value of P2-Asp OMTKY3,224570,5440
BMRB,5431,pKa value of P2-Glu OMTKY3,224570,5440
BMRB,5432,pKa value of P2-Val OMTKY3,224570,5440
BMRB,5433,pKa value of P2-His OMTKY3,224570,5440
BMRB,5434,pKa value of P2-Lys OMTKY3,224570,5440
BMRB,5435,pKa value of P4-Asp OMTKY3,224570,5440
BMRB,5436,pKa value of P4-Glu OMTKY3,224570,5440
BMRB,5437,pKa value of P4-His OMTKY3,224570,5440
BMRB,5438,pKa value of P4-Lys OMTKY3,224570,5440
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224570,5440
BMRB,5441,pKa value of P5-Glu OMTKY3,224570,5440
BMRB,5442,pKa value of P5-His OMTKY3,224570,5440
BMRB,5443,pKa value of P6-Asp OMTKY3,224570,5440
BMRB,5444,pKa value of P6-Glu OMTKY3,224570,5440
BMRB,5445,pKa value of P6-His OMTKY3,224570,5440
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224570,5440
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224570,5440
BMRB,5448,pKa value of OMTKY3 (no salt added),224570,5440
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224570,5440
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224570,5440
BMRB,5451,pKa value of AAPD,224570,5440
BMRB,5452,pKa value of AAPE,224570,5440
BMRB,5453,pKa value of AAPK,224570,5440
BMRB,4864,Chemical shifts of OMTKY3.,224584,5441
BMRB,5411,pKa value of OMTKY3,224584,5441
BMRB,5412,pKa value of P2'-Lys OMTKY3,224584,5441
BMRB,5413,pKa value of P2'-His OMTKY3,224584,5441
BMRB,5414,pKa value of P2'-GLU OMTKY3,224584,5441
BMRB,5415,pKa value of P2'-Asp OMTKY3,224584,5441
BMRB,5416,pKa value of P3'-Ala OMTKY3,224584,5441
BMRB,5417,pKa value of P3'-Asp OMTKY3,224584,5441
BMRB,5418,pKa value of P3'-Glu OMTKY3,224584,5441
BMRB,5419,pKa value of P3'-His OMTKY3,224584,5441
BMRB,5420,pKa value of P3'-Lys OMTKY3,224584,5441
BMRB,5421,pKa value of P1'-Asp OMTKY3,224584,5441
BMRB,5422,pKa value of P1'-His OMTKY3,224584,5441
BMRB,5423,pKa value of P1'-Lys OMTKY3,224584,5441
BMRB,5424,pKa value of P1-Asp OMTKY3,224584,5441
BMRB,5425,pKa value of P1-Glu OMTKY3,224584,5441
BMRB,5426,pKa value of P1-Gly OMTKY3,224584,5441
BMRB,5427,pKa value of P1-Ala OMTKY3,224584,5441
BMRB,5428,pKa value of P1-His OMTKY3,224584,5441
BMRB,5429,pKa value of P1-Lys OMTKY3,224584,5441
BMRB,5430,pKa value of P2-Asp OMTKY3,224584,5441
BMRB,5431,pKa value of P2-Glu OMTKY3,224584,5441
BMRB,5432,pKa value of P2-Val OMTKY3,224584,5441
BMRB,5433,pKa value of P2-His OMTKY3,224584,5441
BMRB,5434,pKa value of P2-Lys OMTKY3,224584,5441
BMRB,5435,pKa value of P4-Asp OMTKY3,224584,5441
BMRB,5436,pKa value of P4-Glu OMTKY3,224584,5441
BMRB,5437,pKa value of P4-His OMTKY3,224584,5441
BMRB,5438,pKa value of P4-Lys OMTKY3,224584,5441
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224584,5441
BMRB,5440,pKa value of P5-Asp OMTKY3,224584,5441
BMRB,5442,pKa value of P5-His OMTKY3,224584,5441
BMRB,5443,pKa value of P6-Asp OMTKY3,224584,5441
BMRB,5444,pKa value of P6-Glu OMTKY3,224584,5441
BMRB,5445,pKa value of P6-His OMTKY3,224584,5441
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224584,5441
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224584,5441
BMRB,5448,pKa value of OMTKY3 (no salt added),224584,5441
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224584,5441
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224584,5441
BMRB,5451,pKa value of AAPD,224584,5441
BMRB,5452,pKa value of AAPE,224584,5441
BMRB,5453,pKa value of AAPK,224584,5441
BMRB,4864,Chemical shifts of OMTKY3.,224598,5442
BMRB,5411,pKa value of OMTKY3,224598,5442
BMRB,5412,pKa value of P2'-Lys OMTKY3,224598,5442
BMRB,5413,pKa value of P2'-His OMTKY3,224598,5442
BMRB,5414,pKa value of P2'-GLU OMTKY3,224598,5442
BMRB,5415,pKa value of P2'-Asp OMTKY3,224598,5442
BMRB,5416,pKa value of P3'-Ala OMTKY3,224598,5442
BMRB,5417,pKa value of P3'-Asp OMTKY3,224598,5442
BMRB,5418,pKa value of P3'-Glu OMTKY3,224598,5442
BMRB,5419,pKa value of P3'-His OMTKY3,224598,5442
BMRB,5420,pKa value of P3'-Lys OMTKY3,224598,5442
BMRB,5421,pKa value of P1'-Asp OMTKY3,224598,5442
BMRB,5422,pKa value of P1'-His OMTKY3,224598,5442
BMRB,5423,pKa value of P1'-Lys OMTKY3,224598,5442
BMRB,5424,pKa value of P1-Asp OMTKY3,224598,5442
BMRB,5425,pKa value of P1-Glu OMTKY3,224598,5442
BMRB,5426,pKa value of P1-Gly OMTKY3,224598,5442
BMRB,5427,pKa value of P1-Ala OMTKY3,224598,5442
BMRB,5428,pKa value of P1-His OMTKY3,224598,5442
BMRB,5429,pKa value of P1-Lys OMTKY3,224598,5442
BMRB,5430,pKa value of P2-Asp OMTKY3,224598,5442
BMRB,5431,pKa value of P2-Glu OMTKY3,224598,5442
BMRB,5432,pKa value of P2-Val OMTKY3,224598,5442
BMRB,5433,pKa value of P2-His OMTKY3,224598,5442
BMRB,5434,pKa value of P2-Lys OMTKY3,224598,5442
BMRB,5435,pKa value of P4-Asp OMTKY3,224598,5442
BMRB,5436,pKa value of P4-Glu OMTKY3,224598,5442
BMRB,5437,pKa value of P4-His OMTKY3,224598,5442
BMRB,5438,pKa value of P4-Lys OMTKY3,224598,5442
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224598,5442
BMRB,5440,pKa value of P5-Asp OMTKY3,224598,5442
BMRB,5441,pKa value of P5-Glu OMTKY3,224598,5442
BMRB,5443,pKa value of P6-Asp OMTKY3,224598,5442
BMRB,5444,pKa value of P6-Glu OMTKY3,224598,5442
BMRB,5445,pKa value of P6-His OMTKY3,224598,5442
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224598,5442
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224598,5442
BMRB,5448,pKa value of OMTKY3 (no salt added),224598,5442
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224598,5442
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224598,5442
BMRB,5451,pKa value of AAPD,224598,5442
BMRB,5452,pKa value of AAPE,224598,5442
BMRB,5453,pKa value of AAPK,224598,5442
BMRB,4864,Chemical shifts of OMTKY3.,224612,5443
BMRB,5411,pKa value of OMTKY3,224612,5443
BMRB,5412,pKa value of P2'-Lys OMTKY3,224612,5443
BMRB,5413,pKa value of P2'-His OMTKY3,224612,5443
BMRB,5414,pKa value of P2'-GLU OMTKY3,224612,5443
BMRB,5415,pKa value of P2'-Asp OMTKY3,224612,5443
BMRB,5416,pKa value of P3'-Ala OMTKY3,224612,5443
BMRB,5417,pKa value of P3'-Asp OMTKY3,224612,5443
BMRB,5418,pKa value of P3'-Glu OMTKY3,224612,5443
BMRB,5419,pKa value of P3'-His OMTKY3,224612,5443
BMRB,5420,pKa value of P3'-Lys OMTKY3,224612,5443
BMRB,5421,pKa value of P1'-Asp OMTKY3,224612,5443
BMRB,5422,pKa value of P1'-His OMTKY3,224612,5443
BMRB,5423,pKa value of P1'-Lys OMTKY3,224612,5443
BMRB,5424,pKa value of P1-Asp OMTKY3,224612,5443
BMRB,5425,pKa value of P1-Glu OMTKY3,224612,5443
BMRB,5426,pKa value of P1-Gly OMTKY3,224612,5443
BMRB,5427,pKa value of P1-Ala OMTKY3,224612,5443
BMRB,5428,pKa value of P1-His OMTKY3,224612,5443
BMRB,5429,pKa value of P1-Lys OMTKY3,224612,5443
BMRB,5430,pKa value of P2-Asp OMTKY3,224612,5443
BMRB,5431,pKa value of P2-Glu OMTKY3,224612,5443
BMRB,5432,pKa value of P2-Val OMTKY3,224612,5443
BMRB,5433,pKa value of P2-His OMTKY3,224612,5443
BMRB,5434,pKa value of P2-Lys OMTKY3,224612,5443
BMRB,5435,pKa value of P4-Asp OMTKY3,224612,5443
BMRB,5436,pKa value of P4-Glu OMTKY3,224612,5443
BMRB,5437,pKa value of P4-His OMTKY3,224612,5443
BMRB,5438,pKa value of P4-Lys OMTKY3,224612,5443
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224612,5443
BMRB,5440,pKa value of P5-Asp OMTKY3,224612,5443
BMRB,5441,pKa value of P5-Glu OMTKY3,224612,5443
BMRB,5442,pKa value of P5-His OMTKY3,224612,5443
BMRB,5444,pKa value of P6-Glu OMTKY3,224612,5443
BMRB,5445,pKa value of P6-His OMTKY3,224612,5443
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224612,5443
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224612,5443
BMRB,5448,pKa value of OMTKY3 (no salt added),224612,5443
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224612,5443
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224612,5443
BMRB,5451,pKa value of AAPD,224612,5443
BMRB,5452,pKa value of AAPE,224612,5443
BMRB,5453,pKa value of AAPK,224612,5443
BMRB,4864,Chemical shifts of OMTKY3.,224626,5444
BMRB,5411,pKa value of OMTKY3,224626,5444
BMRB,5412,pKa value of P2'-Lys OMTKY3,224626,5444
BMRB,5413,pKa value of P2'-His OMTKY3,224626,5444
BMRB,5414,pKa value of P2'-GLU OMTKY3,224626,5444
BMRB,5415,pKa value of P2'-Asp OMTKY3,224626,5444
BMRB,5416,pKa value of P3'-Ala OMTKY3,224626,5444
BMRB,5417,pKa value of P3'-Asp OMTKY3,224626,5444
BMRB,5418,pKa value of P3'-Glu OMTKY3,224626,5444
BMRB,5419,pKa value of P3'-His OMTKY3,224626,5444
BMRB,5420,pKa value of P3'-Lys OMTKY3,224626,5444
BMRB,5421,pKa value of P1'-Asp OMTKY3,224626,5444
BMRB,5422,pKa value of P1'-His OMTKY3,224626,5444
BMRB,5423,pKa value of P1'-Lys OMTKY3,224626,5444
BMRB,5424,pKa value of P1-Asp OMTKY3,224626,5444
BMRB,5425,pKa value of P1-Glu OMTKY3,224626,5444
BMRB,5426,pKa value of P1-Gly OMTKY3,224626,5444
BMRB,5427,pKa value of P1-Ala OMTKY3,224626,5444
BMRB,5428,pKa value of P1-His OMTKY3,224626,5444
BMRB,5429,pKa value of P1-Lys OMTKY3,224626,5444
BMRB,5430,pKa value of P2-Asp OMTKY3,224626,5444
BMRB,5431,pKa value of P2-Glu OMTKY3,224626,5444
BMRB,5432,pKa value of P2-Val OMTKY3,224626,5444
BMRB,5433,pKa value of P2-His OMTKY3,224626,5444
BMRB,5434,pKa value of P2-Lys OMTKY3,224626,5444
BMRB,5435,pKa value of P4-Asp OMTKY3,224626,5444
BMRB,5436,pKa value of P4-Glu OMTKY3,224626,5444
BMRB,5437,pKa value of P4-His OMTKY3,224626,5444
BMRB,5438,pKa value of P4-Lys OMTKY3,224626,5444
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224626,5444
BMRB,5440,pKa value of P5-Asp OMTKY3,224626,5444
BMRB,5441,pKa value of P5-Glu OMTKY3,224626,5444
BMRB,5442,pKa value of P5-His OMTKY3,224626,5444
BMRB,5443,pKa value of P6-Asp OMTKY3,224626,5444
BMRB,5445,pKa value of P6-His OMTKY3,224626,5444
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224626,5444
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224626,5444
BMRB,5448,pKa value of OMTKY3 (no salt added),224626,5444
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224626,5444
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224626,5444
BMRB,5451,pKa value of AAPD,224626,5444
BMRB,5452,pKa value of AAPE,224626,5444
BMRB,5453,pKa value of AAPK,224626,5444
BMRB,4864,Chemical shifts of OMTKY3.,224640,5445
BMRB,5411,pKa value of OMTKY3,224640,5445
BMRB,5412,pKa value of P2'-Lys OMTKY3,224640,5445
BMRB,5413,pKa value of P2'-His OMTKY3,224640,5445
BMRB,5414,pKa value of P2'-GLU OMTKY3,224640,5445
BMRB,5415,pKa value of P2'-Asp OMTKY3,224640,5445
BMRB,5416,pKa value of P3'-Ala OMTKY3,224640,5445
BMRB,5417,pKa value of P3'-Asp OMTKY3,224640,5445
BMRB,5418,pKa value of P3'-Glu OMTKY3,224640,5445
BMRB,5419,pKa value of P3'-His OMTKY3,224640,5445
BMRB,5420,pKa value of P3'-Lys OMTKY3,224640,5445
BMRB,5421,pKa value of P1'-Asp OMTKY3,224640,5445
BMRB,5422,pKa value of P1'-His OMTKY3,224640,5445
BMRB,5423,pKa value of P1'-Lys OMTKY3,224640,5445
BMRB,5424,pKa value of P1-Asp OMTKY3,224640,5445
BMRB,5425,pKa value of P1-Glu OMTKY3,224640,5445
BMRB,5426,pKa value of P1-Gly OMTKY3,224640,5445
BMRB,5427,pKa value of P1-Ala OMTKY3,224640,5445
BMRB,5428,pKa value of P1-His OMTKY3,224640,5445
BMRB,5429,pKa value of P1-Lys OMTKY3,224640,5445
BMRB,5430,pKa value of P2-Asp OMTKY3,224640,5445
BMRB,5431,pKa value of P2-Glu OMTKY3,224640,5445
BMRB,5432,pKa value of P2-Val OMTKY3,224640,5445
BMRB,5433,pKa value of P2-His OMTKY3,224640,5445
BMRB,5434,pKa value of P2-Lys OMTKY3,224640,5445
BMRB,5435,pKa value of P4-Asp OMTKY3,224640,5445
BMRB,5436,pKa value of P4-Glu OMTKY3,224640,5445
BMRB,5437,pKa value of P4-His OMTKY3,224640,5445
BMRB,5438,pKa value of P4-Lys OMTKY3,224640,5445
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224640,5445
BMRB,5440,pKa value of P5-Asp OMTKY3,224640,5445
BMRB,5441,pKa value of P5-Glu OMTKY3,224640,5445
BMRB,5442,pKa value of P5-His OMTKY3,224640,5445
BMRB,5443,pKa value of P6-Asp OMTKY3,224640,5445
BMRB,5444,pKa value of P6-Glu OMTKY3,224640,5445
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224640,5445
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224640,5445
BMRB,5448,pKa value of OMTKY3 (no salt added),224640,5445
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224640,5445
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224640,5445
BMRB,5451,pKa value of AAPD,224640,5445
BMRB,5452,pKa value of AAPE,224640,5445
BMRB,5453,pKa value of AAPK,224640,5445
BMRB,4864,Chemical shifts of OMTKY3.,224654,5446
BMRB,5411,pKa value of OMTKY3,224654,5446
BMRB,5412,pKa value of P2'-Lys OMTKY3,224654,5446
BMRB,5413,pKa value of P2'-His OMTKY3,224654,5446
BMRB,5414,pKa value of P2'-GLU OMTKY3,224654,5446
BMRB,5415,pKa value of P2'-Asp OMTKY3,224654,5446
BMRB,5416,pKa value of P3'-Ala OMTKY3,224654,5446
BMRB,5417,pKa value of P3'-Asp OMTKY3,224654,5446
BMRB,5418,pKa value of P3'-Glu OMTKY3,224654,5446
BMRB,5419,pKa value of P3'-His OMTKY3,224654,5446
BMRB,5420,pKa value of P3'-Lys OMTKY3,224654,5446
BMRB,5421,pKa value of P1'-Asp OMTKY3,224654,5446
BMRB,5422,pKa value of P1'-His OMTKY3,224654,5446
BMRB,5423,pKa value of P1'-Lys OMTKY3,224654,5446
BMRB,5424,pKa value of P1-Asp OMTKY3,224654,5446
BMRB,5425,pKa value of P1-Glu OMTKY3,224654,5446
BMRB,5426,pKa value of P1-Gly OMTKY3,224654,5446
BMRB,5427,pKa value of P1-Ala OMTKY3,224654,5446
BMRB,5428,pKa value of P1-His OMTKY3,224654,5446
BMRB,5429,pKa value of P1-Lys OMTKY3,224654,5446
BMRB,5430,pKa value of P2-Asp OMTKY3,224654,5446
BMRB,5431,pKa value of P2-Glu OMTKY3,224654,5446
BMRB,5432,pKa value of P2-Val OMTKY3,224654,5446
BMRB,5433,pKa value of P2-His OMTKY3,224654,5446
BMRB,5434,pKa value of P2-Lys OMTKY3,224654,5446
BMRB,5435,pKa value of P4-Asp OMTKY3,224654,5446
BMRB,5436,pKa value of P4-Glu OMTKY3,224654,5446
BMRB,5437,pKa value of P4-His OMTKY3,224654,5446
BMRB,5438,pKa value of P4-Lys OMTKY3,224654,5446
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224654,5446
BMRB,5440,pKa value of P5-Asp OMTKY3,224654,5446
BMRB,5441,pKa value of P5-Glu OMTKY3,224654,5446
BMRB,5442,pKa value of P5-His OMTKY3,224654,5446
BMRB,5443,pKa value of P6-Asp OMTKY3,224654,5446
BMRB,5444,pKa value of P6-Glu OMTKY3,224654,5446
BMRB,5445,pKa value of P6-His OMTKY3,224654,5446
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224654,5446
BMRB,5448,pKa value of OMTKY3 (no salt added),224654,5446
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224654,5446
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224654,5446
BMRB,5451,pKa value of AAPD,224654,5446
BMRB,5452,pKa value of AAPE,224654,5446
BMRB,5453,pKa value of AAPK,224654,5446
BMRB,4864,Chemical shifts of OMTKY3.,224668,5447
BMRB,5411,pKa value of OMTKY3,224668,5447
BMRB,5412,pKa value of P2'-Lys OMTKY3,224668,5447
BMRB,5413,pKa value of P2'-His OMTKY3,224668,5447
BMRB,5414,pKa value of P2'-GLU OMTKY3,224668,5447
BMRB,5415,pKa value of P2'-Asp OMTKY3,224668,5447
BMRB,5416,pKa value of P3'-Ala OMTKY3,224668,5447
BMRB,5417,pKa value of P3'-Asp OMTKY3,224668,5447
BMRB,5418,pKa value of P3'-Glu OMTKY3,224668,5447
BMRB,5419,pKa value of P3'-His OMTKY3,224668,5447
BMRB,5420,pKa value of P3'-Lys OMTKY3,224668,5447
BMRB,5421,pKa value of P1'-Asp OMTKY3,224668,5447
BMRB,5422,pKa value of P1'-His OMTKY3,224668,5447
BMRB,5423,pKa value of P1'-Lys OMTKY3,224668,5447
BMRB,5424,pKa value of P1-Asp OMTKY3,224668,5447
BMRB,5425,pKa value of P1-Glu OMTKY3,224668,5447
BMRB,5426,pKa value of P1-Gly OMTKY3,224668,5447
BMRB,5427,pKa value of P1-Ala OMTKY3,224668,5447
BMRB,5428,pKa value of P1-His OMTKY3,224668,5447
BMRB,5429,pKa value of P1-Lys OMTKY3,224668,5447
BMRB,5430,pKa value of P2-Asp OMTKY3,224668,5447
BMRB,5431,pKa value of P2-Glu OMTKY3,224668,5447
BMRB,5432,pKa value of P2-Val OMTKY3,224668,5447
BMRB,5433,pKa value of P2-His OMTKY3,224668,5447
BMRB,5434,pKa value of P2-Lys OMTKY3,224668,5447
BMRB,5435,pKa value of P4-Asp OMTKY3,224668,5447
BMRB,5436,pKa value of P4-Glu OMTKY3,224668,5447
BMRB,5437,pKa value of P4-His OMTKY3,224668,5447
BMRB,5438,pKa value of P4-Lys OMTKY3,224668,5447
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224668,5447
BMRB,5440,pKa value of P5-Asp OMTKY3,224668,5447
BMRB,5441,pKa value of P5-Glu OMTKY3,224668,5447
BMRB,5442,pKa value of P5-His OMTKY3,224668,5447
BMRB,5443,pKa value of P6-Asp OMTKY3,224668,5447
BMRB,5444,pKa value of P6-Glu OMTKY3,224668,5447
BMRB,5445,pKa value of P6-His OMTKY3,224668,5447
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224668,5447
BMRB,5448,pKa value of OMTKY3 (no salt added),224668,5447
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224668,5447
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224668,5447
BMRB,5451,pKa value of AAPD,224668,5447
BMRB,5452,pKa value of AAPE,224668,5447
BMRB,5453,pKa value of AAPK,224668,5447
BMRB,4864,Chemical shifts of OMTKY3.,224682,5448
BMRB,5411,pKa value of OMTKY3,224682,5448
BMRB,5412,pKa value of P2'-Lys OMTKY3,224682,5448
BMRB,5413,pKa value of P2'-His OMTKY3,224682,5448
BMRB,5414,pKa value of P2'-GLU OMTKY3,224682,5448
BMRB,5415,pKa value of P2'-Asp OMTKY3,224682,5448
BMRB,5416,pKa value of P3'-Ala OMTKY3,224682,5448
BMRB,5417,pKa value of P3'-Asp OMTKY3,224682,5448
BMRB,5418,pKa value of P3'-Glu OMTKY3,224682,5448
BMRB,5419,pKa value of P3'-His OMTKY3,224682,5448
BMRB,5420,pKa value of P3'-Lys OMTKY3,224682,5448
BMRB,5421,pKa value of P1'-Asp OMTKY3,224682,5448
BMRB,5422,pKa value of P1'-His OMTKY3,224682,5448
BMRB,5423,pKa value of P1'-Lys OMTKY3,224682,5448
BMRB,5424,pKa value of P1-Asp OMTKY3,224682,5448
BMRB,5425,pKa value of P1-Glu OMTKY3,224682,5448
BMRB,5426,pKa value of P1-Gly OMTKY3,224682,5448
BMRB,5427,pKa value of P1-Ala OMTKY3,224682,5448
BMRB,5428,pKa value of P1-His OMTKY3,224682,5448
BMRB,5429,pKa value of P1-Lys OMTKY3,224682,5448
BMRB,5430,pKa value of P2-Asp OMTKY3,224682,5448
BMRB,5431,pKa value of P2-Glu OMTKY3,224682,5448
BMRB,5432,pKa value of P2-Val OMTKY3,224682,5448
BMRB,5433,pKa value of P2-His OMTKY3,224682,5448
BMRB,5434,pKa value of P2-Lys OMTKY3,224682,5448
BMRB,5435,pKa value of P4-Asp OMTKY3,224682,5448
BMRB,5436,pKa value of P4-Glu OMTKY3,224682,5448
BMRB,5437,pKa value of P4-His OMTKY3,224682,5448
BMRB,5438,pKa value of P4-Lys OMTKY3,224682,5448
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224682,5448
BMRB,5440,pKa value of P5-Asp OMTKY3,224682,5448
BMRB,5441,pKa value of P5-Glu OMTKY3,224682,5448
BMRB,5442,pKa value of P5-His OMTKY3,224682,5448
BMRB,5443,pKa value of P6-Asp OMTKY3,224682,5448
BMRB,5444,pKa value of P6-Glu OMTKY3,224682,5448
BMRB,5445,pKa value of P6-His OMTKY3,224682,5448
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224682,5448
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224682,5448
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224682,5448
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224682,5448
BMRB,5451,pKa value of AAPD,224682,5448
BMRB,5452,pKa value of AAPE,224682,5448
BMRB,5453,pKa value of AAPK,224682,5448
BMRB,4864,Chemical shifts of OMTKY3.,224696,5449
BMRB,5411,pKa value of OMTKY3,224696,5449
BMRB,5412,pKa value of P2'-Lys OMTKY3,224696,5449
BMRB,5413,pKa value of P2'-His OMTKY3,224696,5449
BMRB,5414,pKa value of P2'-GLU OMTKY3,224696,5449
BMRB,5415,pKa value of P2'-Asp OMTKY3,224696,5449
BMRB,5416,pKa value of P3'-Ala OMTKY3,224696,5449
BMRB,5417,pKa value of P3'-Asp OMTKY3,224696,5449
BMRB,5418,pKa value of P3'-Glu OMTKY3,224696,5449
BMRB,5419,pKa value of P3'-His OMTKY3,224696,5449
BMRB,5420,pKa value of P3'-Lys OMTKY3,224696,5449
BMRB,5421,pKa value of P1'-Asp OMTKY3,224696,5449
BMRB,5422,pKa value of P1'-His OMTKY3,224696,5449
BMRB,5423,pKa value of P1'-Lys OMTKY3,224696,5449
BMRB,5424,pKa value of P1-Asp OMTKY3,224696,5449
BMRB,5425,pKa value of P1-Glu OMTKY3,224696,5449
BMRB,5426,pKa value of P1-Gly OMTKY3,224696,5449
BMRB,5427,pKa value of P1-Ala OMTKY3,224696,5449
BMRB,5428,pKa value of P1-His OMTKY3,224696,5449
BMRB,5429,pKa value of P1-Lys OMTKY3,224696,5449
BMRB,5430,pKa value of P2-Asp OMTKY3,224696,5449
BMRB,5431,pKa value of P2-Glu OMTKY3,224696,5449
BMRB,5432,pKa value of P2-Val OMTKY3,224696,5449
BMRB,5433,pKa value of P2-His OMTKY3,224696,5449
BMRB,5434,pKa value of P2-Lys OMTKY3,224696,5449
BMRB,5435,pKa value of P4-Asp OMTKY3,224696,5449
BMRB,5436,pKa value of P4-Glu OMTKY3,224696,5449
BMRB,5437,pKa value of P4-His OMTKY3,224696,5449
BMRB,5438,pKa value of P4-Lys OMTKY3,224696,5449
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224696,5449
BMRB,5440,pKa value of P5-Asp OMTKY3,224696,5449
BMRB,5441,pKa value of P5-Glu OMTKY3,224696,5449
BMRB,5442,pKa value of P5-His OMTKY3,224696,5449
BMRB,5443,pKa value of P6-Asp OMTKY3,224696,5449
BMRB,5444,pKa value of P6-Glu OMTKY3,224696,5449
BMRB,5445,pKa value of P6-His OMTKY3,224696,5449
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224696,5449
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224696,5449
BMRB,5448,pKa value of OMTKY3 (no salt added),224696,5449
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224696,5449
BMRB,5451,pKa value of AAPD,224696,5449
BMRB,5452,pKa value of AAPE,224696,5449
BMRB,5453,pKa value of AAPK,224696,5449
BMRB,4864,Chemical shifts of OMTKY3.,224726,5450
BMRB,5411,pKa value of OMTKY3,224726,5450
BMRB,5412,pKa value of P2'-Lys OMTKY3,224726,5450
BMRB,5413,pKa value of P2'-His OMTKY3,224726,5450
BMRB,5414,pKa value of P2'-GLU OMTKY3,224726,5450
BMRB,5415,pKa value of P2'-Asp OMTKY3,224726,5450
BMRB,5416,pKa value of P3'-Ala OMTKY3,224726,5450
BMRB,5417,pKa value of P3'-Asp OMTKY3,224726,5450
BMRB,5418,pKa value of P3'-Glu OMTKY3,224726,5450
BMRB,5419,pKa value of P3'-His OMTKY3,224726,5450
BMRB,5420,pKa value of P3'-Lys OMTKY3,224726,5450
BMRB,5421,pKa value of P1'-Asp OMTKY3,224726,5450
BMRB,5422,pKa value of P1'-His OMTKY3,224726,5450
BMRB,5423,pKa value of P1'-Lys OMTKY3,224726,5450
BMRB,5424,pKa value of P1-Asp OMTKY3,224726,5450
BMRB,5425,pKa value of P1-Glu OMTKY3,224726,5450
BMRB,5426,pKa value of P1-Gly OMTKY3,224726,5450
BMRB,5427,pKa value of P1-Ala OMTKY3,224726,5450
BMRB,5428,pKa value of P1-His OMTKY3,224726,5450
BMRB,5429,pKa value of P1-Lys OMTKY3,224726,5450
BMRB,5430,pKa value of P2-Asp OMTKY3,224726,5450
BMRB,5431,pKa value of P2-Glu OMTKY3,224726,5450
BMRB,5432,pKa value of P2-Val OMTKY3,224726,5450
BMRB,5433,pKa value of P2-His OMTKY3,224726,5450
BMRB,5434,pKa value of P2-Lys OMTKY3,224726,5450
BMRB,5435,pKa value of P4-Asp OMTKY3,224726,5450
BMRB,5436,pKa value of P4-Glu OMTKY3,224726,5450
BMRB,5437,pKa value of P4-His OMTKY3,224726,5450
BMRB,5438,pKa value of P4-Lys OMTKY3,224726,5450
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224726,5450
BMRB,5440,pKa value of P5-Asp OMTKY3,224726,5450
BMRB,5441,pKa value of P5-Glu OMTKY3,224726,5450
BMRB,5442,pKa value of P5-His OMTKY3,224726,5450
BMRB,5443,pKa value of P6-Asp OMTKY3,224726,5450
BMRB,5444,pKa value of P6-Glu OMTKY3,224726,5450
BMRB,5445,pKa value of P6-His OMTKY3,224726,5450
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224726,5450
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224726,5450
BMRB,5448,pKa value of OMTKY3 (no salt added),224726,5450
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224726,5450
BMRB,5451,pKa value of AAPD,224726,5450
BMRB,5452,pKa value of AAPE,224726,5450
BMRB,5453,pKa value of AAPK,224726,5450
BMRB,4864,Chemical shifts of OMTKY3.,224740,5451
BMRB,5411,pKa value of OMTKY3,224740,5451
BMRB,5412,pKa value of P2'-Lys OMTKY3,224740,5451
BMRB,5413,pKa value of P2'-His OMTKY3,224740,5451
BMRB,5414,pKa value of P2'-GLU OMTKY3,224740,5451
BMRB,5415,pKa value of P2'-Asp OMTKY3,224740,5451
BMRB,5416,pKa value of P3'-Ala OMTKY3,224740,5451
BMRB,5417,pKa value of P3'-Asp OMTKY3,224740,5451
BMRB,5418,pKa value of P3'-Glu OMTKY3,224740,5451
BMRB,5419,pKa value of P3'-His OMTKY3,224740,5451
BMRB,5420,pKa value of P3'-Lys OMTKY3,224740,5451
BMRB,5421,pKa value of P1'-Asp OMTKY3,224740,5451
BMRB,5422,pKa value of P1'-His OMTKY3,224740,5451
BMRB,5423,pKa value of P1'-Lys OMTKY3,224740,5451
BMRB,5424,pKa value of P1-Asp OMTKY3,224740,5451
BMRB,5425,pKa value of P1-Glu OMTKY3,224740,5451
BMRB,5426,pKa value of P1-Gly OMTKY3,224740,5451
BMRB,5427,pKa value of P1-Ala OMTKY3,224740,5451
BMRB,5428,pKa value of P1-His OMTKY3,224740,5451
BMRB,5429,pKa value of P1-Lys OMTKY3,224740,5451
BMRB,5430,pKa value of P2-Asp OMTKY3,224740,5451
BMRB,5431,pKa value of P2-Glu OMTKY3,224740,5451
BMRB,5432,pKa value of P2-Val OMTKY3,224740,5451
BMRB,5433,pKa value of P2-His OMTKY3,224740,5451
BMRB,5434,pKa value of P2-Lys OMTKY3,224740,5451
BMRB,5435,pKa value of P4-Asp OMTKY3,224740,5451
BMRB,5436,pKa value of P4-Glu OMTKY3,224740,5451
BMRB,5437,pKa value of P4-His OMTKY3,224740,5451
BMRB,5438,pKa value of P4-Lys OMTKY3,224740,5451
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224740,5451
BMRB,5440,pKa value of P5-Asp OMTKY3,224740,5451
BMRB,5441,pKa value of P5-Glu OMTKY3,224740,5451
BMRB,5442,pKa value of P5-His OMTKY3,224740,5451
BMRB,5443,pKa value of P6-Asp OMTKY3,224740,5451
BMRB,5444,pKa value of P6-Glu OMTKY3,224740,5451
BMRB,5445,pKa value of P6-His OMTKY3,224740,5451
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224740,5451
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224740,5451
BMRB,5448,pKa value of OMTKY3 (no salt added),224740,5451
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224740,5451
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224740,5451
BMRB,5452,pKa value of AAPE,224740,5451
BMRB,5453,pKa value of AAPK,224740,5451
BMRB,4864,Chemical shifts of OMTKY3.,224755,5452
BMRB,5411,pKa value of OMTKY3,224755,5452
BMRB,5412,pKa value of P2'-Lys OMTKY3,224755,5452
BMRB,5413,pKa value of P2'-His OMTKY3,224755,5452
BMRB,5414,pKa value of P2'-GLU OMTKY3,224755,5452
BMRB,5415,pKa value of P2'-Asp OMTKY3,224755,5452
BMRB,5416,pKa value of P3'-Ala OMTKY3,224755,5452
BMRB,5417,pKa value of P3'-Asp OMTKY3,224755,5452
BMRB,5418,pKa value of P3'-Glu OMTKY3,224755,5452
BMRB,5419,pKa value of P3'-His OMTKY3,224755,5452
BMRB,5420,pKa value of P3'-Lys OMTKY3,224755,5452
BMRB,5421,pKa value of P1'-Asp OMTKY3,224755,5452
BMRB,5422,pKa value of P1'-His OMTKY3,224755,5452
BMRB,5423,pKa value of P1'-Lys OMTKY3,224755,5452
BMRB,5424,pKa value of P1-Asp OMTKY3,224755,5452
BMRB,5425,pKa value of P1-Glu OMTKY3,224755,5452
BMRB,5426,pKa value of P1-Gly OMTKY3,224755,5452
BMRB,5427,pKa value of P1-Ala OMTKY3,224755,5452
BMRB,5428,pKa value of P1-His OMTKY3,224755,5452
BMRB,5429,pKa value of P1-Lys OMTKY3,224755,5452
BMRB,5430,pKa value of P2-Asp OMTKY3,224755,5452
BMRB,5431,pKa value of P2-Glu OMTKY3,224755,5452
BMRB,5432,pKa value of P2-Val OMTKY3,224755,5452
BMRB,5433,pKa value of P2-His OMTKY3,224755,5452
BMRB,5434,pKa value of P2-Lys OMTKY3,224755,5452
BMRB,5435,pKa value of P4-Asp OMTKY3,224755,5452
BMRB,5436,pKa value of P4-Glu OMTKY3,224755,5452
BMRB,5437,pKa value of P4-His OMTKY3,224755,5452
BMRB,5438,pKa value of P4-Lys OMTKY3,224755,5452
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224755,5452
BMRB,5440,pKa value of P5-Asp OMTKY3,224755,5452
BMRB,5441,pKa value of P5-Glu OMTKY3,224755,5452
BMRB,5442,pKa value of P5-His OMTKY3,224755,5452
BMRB,5443,pKa value of P6-Asp OMTKY3,224755,5452
BMRB,5444,pKa value of P6-Glu OMTKY3,224755,5452
BMRB,5445,pKa value of P6-His OMTKY3,224755,5452
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224755,5452
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224755,5452
BMRB,5448,pKa value of OMTKY3 (no salt added),224755,5452
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224755,5452
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224755,5452
BMRB,5451,pKa value of AAPD,224755,5452
BMRB,5453,pKa value of AAPK,224755,5452
BMRB,4864,Chemical shifts of OMTKY3.,224770,5453
BMRB,5411,pKa value of OMTKY3,224770,5453
BMRB,5412,pKa value of P2'-Lys OMTKY3,224770,5453
BMRB,5413,pKa value of P2'-His OMTKY3,224770,5453
BMRB,5414,pKa value of P2'-GLU OMTKY3,224770,5453
BMRB,5415,pKa value of P2'-Asp OMTKY3,224770,5453
BMRB,5416,pKa value of P3'-Ala OMTKY3,224770,5453
BMRB,5417,pKa value of P3'-Asp OMTKY3,224770,5453
BMRB,5418,pKa value of P3'-Glu OMTKY3,224770,5453
BMRB,5419,pKa value of P3'-His OMTKY3,224770,5453
BMRB,5420,pKa value of P3'-Lys OMTKY3,224770,5453
BMRB,5421,pKa value of P1'-Asp OMTKY3,224770,5453
BMRB,5422,pKa value of P1'-His OMTKY3,224770,5453
BMRB,5423,pKa value of P1'-Lys OMTKY3,224770,5453
BMRB,5424,pKa value of P1-Asp OMTKY3,224770,5453
BMRB,5425,pKa value of P1-Glu OMTKY3,224770,5453
BMRB,5426,pKa value of P1-Gly OMTKY3,224770,5453
BMRB,5427,pKa value of P1-Ala OMTKY3,224770,5453
BMRB,5428,pKa value of P1-His OMTKY3,224770,5453
BMRB,5429,pKa value of P1-Lys OMTKY3,224770,5453
BMRB,5430,pKa value of P2-Asp OMTKY3,224770,5453
BMRB,5431,pKa value of P2-Glu OMTKY3,224770,5453
BMRB,5432,pKa value of P2-Val OMTKY3,224770,5453
BMRB,5433,pKa value of P2-His OMTKY3,224770,5453
BMRB,5434,pKa value of P2-Lys OMTKY3,224770,5453
BMRB,5435,pKa value of P4-Asp OMTKY3,224770,5453
BMRB,5436,pKa value of P4-Glu OMTKY3,224770,5453
BMRB,5437,pKa value of P4-His OMTKY3,224770,5453
BMRB,5438,pKa value of P4-Lys OMTKY3,224770,5453
BMRB,5439,pKa value of P4-Asp OMTKY3 (no salt added),224770,5453
BMRB,5440,pKa value of P5-Asp OMTKY3,224770,5453
BMRB,5441,pKa value of P5-Glu OMTKY3,224770,5453
BMRB,5442,pKa value of P5-His OMTKY3,224770,5453
BMRB,5443,pKa value of P6-Asp OMTKY3,224770,5453
BMRB,5444,pKa value of P6-Glu OMTKY3,224770,5453
BMRB,5445,pKa value of P6-His OMTKY3,224770,5453
BMRB,5446,"pKa value of P2-Val,P3'-Ala OMTKY3",224770,5453
BMRB,5447,"pKa value of P8-Phe,P6-Asp OMTKY3",224770,5453
BMRB,5448,pKa value of OMTKY3 (no salt added),224770,5453
BMRB,5449,pKa value of P5-His OMTKY3 (no salt added),224770,5453
BMRB,5450,pKa value of P4-Glu OMTKY3 (no salt added),224770,5453
BMRB,5451,pKa value of AAPD,224770,5453
BMRB,5452,pKa value of AAPE,224770,5453
BMRB,15949,Assignments of the Reduced and Active Form,224802,5455
BMRB,4841,PAH2 domain of mSin3B with Mad1-SID,224839,5457
BMRB,5808,PAH2 domain of mSin3B with SID24 complex,224839,5457
PDB,1IYM,BMRB Entry Tracking System,224887,5459
PDB,1M12,BMRB Entry Tracking System,225010,5465
PDB,1SN6,BMRB Entry Tracking System,225010,5465
PDB,1LMS,BMRB Entry Tracking System,225030,5466
PDB,1RI9,BMRB Entry Tracking System,225051,5467
BMRB,5470,Double mutant p14c/n39c of omsvp3.,225095,5469
BMRB,5469,Wild type of omsvp3.,225124,5470
PDB,1IY6,BMRB Entry Tracking System,225124,5470
BMRB,5473,chemical shifts of trans conformer,225164,5472
BMRB,5472,chemical shifts of cis conformer,225180,5473
BMRB,5477,tF1 peptide,225244,5476
BMRB,5478,F1tbp peptide,225244,5476
BMRB,5479,sF1 peptide,225244,5476
BMRB,5476,F1 peptide,225264,5477
BMRB,5478,F1tbp peptide,225264,5477
BMRB,5479,sF1 peptide,225264,5477
BMRB,5476,F1 peptide,225284,5478
BMRB,5477,tF1 peptide,225284,5478
BMRB,5479,sF1 peptide,225284,5478
BMRB,5476,F1 peptide,225304,5479
BMRB,5477,tF1 peptide,225304,5479
BMRB,5478,F1tbp peptide,225304,5479
BMRB,5487,"Tachyplesin I, tyrosine mutant",225520,5486
BMRB,5488,"Tachyplesin I, phenylalanine mutant",225520,5486
BMRB,5489,"Tachyplesin I, alanine mutant",225520,5486
BMRB,5486,"Tachyplesin I, Wild type",225542,5487
BMRB,5488,"Tachyplesin I, phenylalanine mutant",225542,5487
BMRB,5489,"Tachyplesin I, alanine mutant",225542,5487
BMRB,5486,"Tachyplesin I, Wild type",225563,5488
BMRB,5487,"Tachyplesin I, tyrosine mutant",225563,5488
BMRB,5489,"Tachyplesin I, alanine mutant",225563,5488
BMRB,5486,"Tachyplesin I, Wild type",225581,5489
BMRB,5487,"Tachyplesin I, tyrosine mutant",225581,5489
BMRB,5488,"Tachyplesin I, phenylalanine mutant",225581,5489
BMRB,4671,Pru a 1,225599,5490
BMRB,4259,Ribonuclease Sa,225643,5492
PDB,1LMM,BMRB Entry Tracking System,225701,5495
BMRB,5502,shorter Hepcidin,225831,5501
BMRB,5501,longer Hepcidin,225847,5502
PDB,1M4E,BMRB Entry Tracking System,225847,5502
BMRB,5858,Relaxation data over large pH range,225911,5505
BMRB,5507,wild type transthyretin,225986,5508
BMRB,5509,mutant v30m,225986,5508
BMRB,5510,mutant l55p,225986,5508
BMRB,5507,wild type transthyretin,226003,5509
BMRB,5508,mutant t119m,226003,5509
BMRB,5510,mutant l55p,226003,5509
BMRB,5507,wild type transthyretin,226020,5510
BMRB,5508,mutant t119m,226020,5510
BMRB,5509,mutant v30m,226020,5510
BMRB,7308,L11 - RNA (- Thiostrepton) complex,226079,5513
BMRB,7307,L11 - RNA complex,226079,5513
BMRB,4965,Free L11 of Thermus thermophilus,226079,5513
BMRB,5519,OMIPF3 at pH 6.0 and 298K,226200,5518
BMRB,5520,Reactive site hydrolyzed OMTKY3 at pH 6.0 and pH 3.9 and 298K,226200,5518
BMRB,5521,Reactive site hydrolyzed OMIPF3 at pH 6.0 and pH 3.9 and 298K,226200,5518
BMRB,5518,OMTKY3 at pH 6.0 and 298K,226224,5519
BMRB,5520,Reactive site hydrolyzed OMTKY3 at pH 6.0 and pH 3.9 and 298K,226224,5519
BMRB,5521,Reactive site hydrolyzed OMIPF3 at pH 6.0 and pH 3.9 and 298K,226224,5519
BMRB,5518,OMTKY3 at pH 6.0 and 298K,226248,5520
BMRB,5519,OMIPF3 at pH 6.0 and 298K,226248,5520
BMRB,5521,Reactive site hydrolyzed OMIPF3 at pH 6.0 and pH 3.9 and 298K,226248,5520
BMRB,5518,OMTKY3 at pH 6.0 and 298K,226298,5521
BMRB,5519,OMIPF3 at pH 6.0 and 298K,226298,5521
BMRB,5520,Reactive site hydrolyzed OMTKY3 at pH 6.0 and pH 3.9 and 298K,226298,5521
PDB,1M82,BMRB Entry Tracking System,226471,5528
PDB,1M9G,BMRB Entry Tracking System,226498,5529
BMRB,5531,Nucleotide 37 Guanosine to 1N-Methylguanosine mutation,226521,5530
PDB,1LUX,BMRB Entry Tracking System,226521,5530
BMRB,5530,Nucleotide 37 1N-Methylguanosine to Guanosine mutation,226545,5531
PDB,1LUU,BMRB Entry Tracking System,226545,5531
BMRB,4905,Urea-denatured G88W-110 Fragment of Staphylococcal Nuclease,226649,5536
BMRB,6907,V66W110 fragment of staphylococcal nuclease,226649,5536
BMRB,6908,SNase110 fragment of Staphylococcal Nuclease,226649,5536
BMRB,5571,oxidized form.,226759,5540
BMRB,5543,"Penetratin(W48F,W56F) in phospolipid bicelles and SDS micelles.",226810,5542
BMRB,5542,Penetratin in phospolipid bicelles.,226824,5543
BMRB,5379,chemical shifts and coupling constants of this peptide Bound to DPC Micelles,226920,5548
PDB,1H0Z,BMRB Entry Tracking System,227031,5551
PDB,1MFY,BMRB Entry Tracking System,227067,5553
BMRB,5556,Mi2-beta and transcription factor WSTF,227108,5555
BMRB,5555,Mi2-beta,227132,5556
PDB,1MM3,BMRB Entry Tracking System,227132,5556
BMRB,6198,homologous T. maritima protein TM1816,227241,5560
PDB,1N1K,BMRB Entry Tracking System,227289,5562
BMRB,5841,Relaxation and H-exchange data of the protein,227320,5564
PDB,1N3H,BMRB Entry Tracking System,227362,5566
PDB,1N3J,BMRB Entry Tracking System,227375,5567
BMRB,5540,reduced form.,227570,5571
BMRB,5573,Spruce budworm antifreeze protein (5 C),227594,5572
BMRB,5572,Spruce budworm antifreeze protein (30 C),227607,5573
PDB,1MYU,BMRB Entry Tracking System,227620,5574
BMRB,5577,ATPase alpha-1 free form,227655,5576
BMRB,5576,ATPase alpha-1 complex form with ATP,227677,5577
BMRB,5579,Apo form.,227696,5578
BMRB,5578,Holo form.,227726,5579
BMRB,5581,free form lantibiotics mersacidin in MeOH/H2O.,227767,5580
BMRB,5582,free form lantibiotics mersacidin in DPC micelles.,227767,5580
PDB,1MQZ,BMRB Entry Tracking System,227767,5580
BMRB,5580,free form lantibiotics mersacidin bound to lipid II in DPC micelles.,227789,5581
BMRB,5582,free form lantibiotics mersacidin in DPC micelles.,227789,5581
PDB,1MQX,BMRB Entry Tracking System,227789,5581
BMRB,5580,free form lantibiotics mersacidin bound to lipid II in DPC micelles.,227811,5582
BMRB,5581,free form lantibiotics mersacidin in MeOH/H2O.,227811,5582
PDB,1MQY,BMRB Entry Tracking System,227811,5582
BMRB,5587,related molecule 5'-R(*GP*GP*CP*AP*(P5P)P*GP*CP*CP*U)-3',227899,5586
BMRB,5588,related molecule 5'-R(*GP*GP*CP*(P5P)P*(P5P)P*GP*CP*CP*U)-3',227899,5586
BMRB,5614,related molecule 5'-R(*GP*GP*CP*AP*AP*GP*CP*CP*U)-3',227899,5586
PDB,1MV1,BMRB Entry Tracking System,227899,5586
BMRB,5586,related molecule 5'-R(*GP*GP*CP*(P5P)P*AP*GP*CP*CP*U)-3',227919,5587
BMRB,5588,related molecule 5'-R(*GP*GP*CP*(P5P)P*(P5P)P*GP*CP*CP*U)-3',227919,5587
BMRB,5614,related molecule 5'-R(*GP*GP*CP*AP*AP*GP*CP*CP*U)-3',227919,5587
PDB,1MV2,BMRB Entry Tracking System,227919,5587
BMRB,5586,related molecule 5'-R(*GP*GP*CP*(P5P)P*AP*GP*CP*CP*U)-3',227939,5588
BMRB,5587,related molecule 5'-R(*GP*GP*CP*AP*(P5P)P*GP*CP*CP*U)-3',227939,5588
BMRB,5614,related molecule 5'-R(*GP*GP*CP*AP*AP*GP*CP*CP*U)-3',227939,5588
PDB,1MV1,BMRB Entry Tracking System,227939,5588
BMRB,5172,oxidized cytochrome c553 from Bacillus pasteurii,228245,5597
PDB,1OP1,BMRB Entry Tracking System,228269,5598
PDB,1OV2,BMRB Entry Tracking System,228269,5598
BMRB,4051,"CpRdFe(III) 1H,13C,15N data",228329,5600
BMRB,4050,"CpRdFe(II) 1H,13C,15N data",228329,5600
BMRB,4182,CpRdFe(II) 1H data,228329,5600
BMRB,4137,CpRdFe(II) and CpRdFe(III) 1H/2H isotopic shifts,228329,5600
BMRB,4066,CpRdFe(II) and CpRdFe(III) 15N hyperfine shifts,228329,5600
BMRB,4319,CpRdFe(III) 1H-15N and 1H-13C dipolar shifts,228329,5600
BMRB,4320,CpRdFe(II) 1H-15N and 1H-13C dipolar shifts,228329,5600
BMRB,5601,"PfRdZn(II) 1H,13C,15N data",228329,5600
BMRB,4051,"CpRdFe(III) 1H,13C,15N data",228364,5601
BMRB,4050,"CpRdFe(II) 1H,13C,15N data",228364,5601
BMRB,4182,CpRdFe(II) 1H data,228364,5601
BMRB,4137,CpRdFe(II) and CpRdFe(III) 1H/2H isotopic shifts,228364,5601
BMRB,4066,CpRdFe(II) and CpRdFe(III) 15N hyperfine shifts,228364,5601
BMRB,4319,CpRdFe(III) 1H-15N and 1H-13C dipolar shifts,228364,5601
BMRB,4320,CpRdFe(II) 1H-15N and 1H-13C dipolar shifts,228364,5601
BMRB,5600,"CpRdZn(II) 1H,13C,15N data",228364,5601
BMRB,4432,glycine receptor alpha 1 subunit TM2 segment,228523,5607
BMRB,4433,glycine receptor alpha 1 subunit TM2 segment S267Y,228523,5607
PDB,1NXN,BMRB Entry Tracking System,228549,5608
PDB,1N1U,BMRB Entry Tracking System,228575,5609
BMRB,7080,Complex of TM1a(1-14)Zip with TM9a(251-284),228603,5610
PDB,1N6T,BMRB Entry Tracking System,228625,5611
PDB,1N09,BMRB Entry Tracking System,228659,5613
BMRB,5586,related molecule 5'-R(*GP*GP*CP*(P5P)P*AP*GP*CP*CP*U)-3',228679,5614
BMRB,5587,related molecule 5'-R(*GP*GP*CP*AP*(P5P)P*GP*CP*CP*U)-3',228679,5614
BMRB,5588,related molecule 5'-R(*GP*GP*CP*(P5P)P*(P5P)P*GP*CP*CP*U)-3',228679,5614
PDB,1MUV,BMRB Entry Tracking System,228679,5614
BMRB,5239,assignments of ferri-cytochrome c3 by CNRS.,228954,5625
PDB,1NA2,BMRB Entry Tracking System,229165,5632
BMRB,5635,chemical shifts of SS2.,229206,5634
BMRB,5636,chemical shifts of SS3.,229206,5634
BMRB,5637,chemical shifts of SS4.,229206,5634
BMRB,5638,chemical shifts of SS5.,229206,5634
BMRB,5639,chemical shifts of SS6.,229206,5634
BMRB,5640,chemical shifts of SS7.,229206,5634
BMRB,5641,chemical shifts of SS8.,229206,5634
BMRB,5642,chemical shifts of SS9.,229206,5634
BMRB,5643,chemical shifts of SS10.,229206,5634
BMRB,5644,chemical shifts of SS11.,229206,5634
BMRB,5645,chemical shifts of SS12.,229206,5634
BMRB,5646,chemical shifts of SS13.,229206,5634
BMRB,5647,chemical shifts of SS14.,229206,5634
BMRB,5648,chemical shifts of SS15.,229206,5634
BMRB,5649,chemical shifts of SS16.,229206,5634
BMRB,5634,chemical shifts of SS1.,229220,5635
BMRB,5636,chemical shifts of SS3.,229220,5635
BMRB,5637,chemical shifts of SS4.,229220,5635
BMRB,5638,chemical shifts of SS5.,229220,5635
BMRB,5639,chemical shifts of SS6.,229220,5635
BMRB,5640,chemical shifts of SS7.,229220,5635
BMRB,5641,chemical shifts of SS8.,229220,5635
BMRB,5642,chemical shifts of SS9.,229220,5635
BMRB,5643,chemical shifts of SS10.,229220,5635
BMRB,5644,chemical shifts of SS11.,229220,5635
BMRB,5645,chemical shifts of SS12.,229220,5635
BMRB,5646,chemical shifts of SS13.,229220,5635
BMRB,5647,chemical shifts of SS14.,229220,5635
BMRB,5648,chemical shifts of SS15.,229220,5635
BMRB,5649,chemical shifts of SS16.,229220,5635
BMRB,5634,chemical shifts of SS1.,229234,5636
BMRB,5635,chemical shifts of SS2.,229234,5636
BMRB,5637,chemical shifts of SS4.,229234,5636
BMRB,5638,chemical shifts of SS5.,229234,5636
BMRB,5639,chemical shifts of SS6.,229234,5636
BMRB,5640,chemical shifts of SS7.,229234,5636
BMRB,5641,chemical shifts of SS8.,229234,5636
BMRB,5642,chemical shifts of SS9.,229234,5636
BMRB,5643,chemical shifts of SS10.,229234,5636
BMRB,5644,chemical shifts of SS11.,229234,5636
BMRB,5645,chemical shifts of SS12.,229234,5636
BMRB,5646,chemical shifts of SS13.,229234,5636
BMRB,5647,chemical shifts of SS14.,229234,5636
BMRB,5648,chemical shifts of SS15.,229234,5636
BMRB,5649,chemical shifts of SS16.,229234,5636
BMRB,5634,chemical shifts of SS1.,229248,5637
BMRB,5635,chemical shifts of SS2.,229248,5637
BMRB,5636,chemical shifts of SS3.,229248,5637
BMRB,5638,chemical shifts of SS5.,229248,5637
BMRB,5639,chemical shifts of SS6.,229248,5637
BMRB,5640,chemical shifts of SS7.,229248,5637
BMRB,5641,chemical shifts of SS8.,229248,5637
BMRB,5642,chemical shifts of SS9.,229248,5637
BMRB,5643,chemical shifts of SS10.,229248,5637
BMRB,5644,chemical shifts of SS11.,229248,5637
BMRB,5645,chemical shifts of SS12.,229248,5637
BMRB,5646,chemical shifts of SS13.,229248,5637
BMRB,5647,chemical shifts of SS14.,229248,5637
BMRB,5648,chemical shifts of SS15.,229248,5637
BMRB,5649,chemical shifts of SS16.,229248,5637
BMRB,5634,chemical shifts of SS1.,229262,5638
BMRB,5635,chemical shifts of SS2.,229262,5638
BMRB,5636,chemical shifts of SS3.,229262,5638
BMRB,5637,chemical shifts of SS4.,229262,5638
BMRB,5639,chemical shifts of SS6.,229262,5638
BMRB,5640,chemical shifts of SS7.,229262,5638
BMRB,5641,chemical shifts of SS8.,229262,5638
BMRB,5642,chemical shifts of SS9.,229262,5638
BMRB,5643,chemical shifts of SS10.,229262,5638
BMRB,5644,chemical shifts of SS11.,229262,5638
BMRB,5645,chemical shifts of SS12.,229262,5638
BMRB,5646,chemical shifts of SS13.,229262,5638
BMRB,5647,chemical shifts of SS14.,229262,5638
BMRB,5648,chemical shifts of SS15.,229262,5638
BMRB,5649,chemical shifts of SS16.,229262,5638
BMRB,5634,chemical shifts of SS1.,229276,5639
BMRB,5635,chemical shifts of SS2.,229276,5639
BMRB,5636,chemical shifts of SS3.,229276,5639
BMRB,5637,chemical shifts of SS4.,229276,5639
BMRB,5638,chemical shifts of SS5.,229276,5639
BMRB,5640,chemical shifts of SS7.,229276,5639
BMRB,5641,chemical shifts of SS8.,229276,5639
BMRB,5642,chemical shifts of SS9.,229276,5639
BMRB,5643,chemical shifts of SS10.,229276,5639
BMRB,5644,chemical shifts of SS11.,229276,5639
BMRB,5645,chemical shifts of SS12.,229276,5639
BMRB,5646,chemical shifts of SS13.,229276,5639
BMRB,5647,chemical shifts of SS14.,229276,5639
BMRB,5648,chemical shifts of SS15.,229276,5639
BMRB,5649,chemical shifts of SS16.,229276,5639
BMRB,5634,chemical shifts of SS1.,229290,5640
BMRB,5635,chemical shifts of SS2.,229290,5640
BMRB,5636,chemical shifts of SS3.,229290,5640
BMRB,5637,chemical shifts of SS4.,229290,5640
BMRB,5638,chemical shifts of SS5.,229290,5640
BMRB,5639,chemical shifts of SS6.,229290,5640
BMRB,5641,chemical shifts of SS8.,229290,5640
BMRB,5642,chemical shifts of SS9.,229290,5640
BMRB,5643,chemical shifts of SS10.,229290,5640
BMRB,5644,chemical shifts of SS11.,229290,5640
BMRB,5645,chemical shifts of SS12.,229290,5640
BMRB,5646,chemical shifts of SS13.,229290,5640
BMRB,5647,chemical shifts of SS14.,229290,5640
BMRB,5648,chemical shifts of SS15.,229290,5640
BMRB,5649,chemical shifts of SS16.,229290,5640
BMRB,5634,chemical shifts of SS1.,229304,5641
BMRB,5635,chemical shifts of SS2.,229304,5641
BMRB,5636,chemical shifts of SS3.,229304,5641
BMRB,5637,chemical shifts of SS4.,229304,5641
BMRB,5638,chemical shifts of SS5.,229304,5641
BMRB,5639,chemical shifts of SS6.,229304,5641
BMRB,5640,chemical shifts of SS7.,229304,5641
BMRB,5642,chemical shifts of SS9.,229304,5641
BMRB,5643,chemical shifts of SS10.,229304,5641
BMRB,5644,chemical shifts of SS11.,229304,5641
BMRB,5645,chemical shifts of SS12.,229304,5641
BMRB,5646,chemical shifts of SS13.,229304,5641
BMRB,5647,chemical shifts of SS14.,229304,5641
BMRB,5648,chemical shifts of SS15.,229304,5641
BMRB,5649,chemical shifts of SS16.,229304,5641
BMRB,5634,chemical shifts of SS1.,229318,5642
BMRB,5635,chemical shifts of SS2.,229318,5642
BMRB,5636,chemical shifts of SS3.,229318,5642
BMRB,5637,chemical shifts of SS4.,229318,5642
BMRB,5638,chemical shifts of SS5.,229318,5642
BMRB,5639,chemical shifts of SS6.,229318,5642
BMRB,5640,chemical shifts of SS7.,229318,5642
BMRB,5641,chemical shifts of SS8.,229318,5642
BMRB,5643,chemical shifts of SS10.,229318,5642
BMRB,5644,chemical shifts of SS11.,229318,5642
BMRB,5645,chemical shifts of SS12.,229318,5642
BMRB,5646,chemical shifts of SS13.,229318,5642
BMRB,5647,chemical shifts of SS14.,229318,5642
BMRB,5648,chemical shifts of SS15.,229318,5642
BMRB,5649,chemical shifts of SS16.,229318,5642
BMRB,5634,chemical shifts of SS1.,229332,5643
BMRB,5635,chemical shifts of SS2.,229332,5643
BMRB,5636,chemical shifts of SS3.,229332,5643
BMRB,5637,chemical shifts of SS4.,229332,5643
BMRB,5638,chemical shifts of SS5.,229332,5643
BMRB,5639,chemical shifts of SS6.,229332,5643
BMRB,5640,chemical shifts of SS7.,229332,5643
BMRB,5641,chemical shifts of SS8.,229332,5643
BMRB,5642,chemical shifts of SS9.,229332,5643
BMRB,5644,chemical shifts of SS11.,229332,5643
BMRB,5645,chemical shifts of SS12.,229332,5643
BMRB,5646,chemical shifts of SS13.,229332,5643
BMRB,5647,chemical shifts of SS14.,229332,5643
BMRB,5648,chemical shifts of SS15.,229332,5643
BMRB,5649,chemical shifts of SS16.,229332,5643
BMRB,5634,chemical shifts of SS1.,229346,5644
BMRB,5635,chemical shifts of SS2.,229346,5644
BMRB,5636,chemical shifts of SS3.,229346,5644
BMRB,5637,chemical shifts of SS4.,229346,5644
BMRB,5638,chemical shifts of SS5.,229346,5644
BMRB,5639,chemical shifts of SS6.,229346,5644
BMRB,5640,chemical shifts of SS7.,229346,5644
BMRB,5641,chemical shifts of SS8.,229346,5644
BMRB,5642,chemical shifts of SS9.,229346,5644
BMRB,5643,chemical shifts of SS10.,229346,5644
BMRB,5645,chemical shifts of SS12.,229346,5644
BMRB,5646,chemical shifts of SS13.,229346,5644
BMRB,5647,chemical shifts of SS14.,229346,5644
BMRB,5648,chemical shifts of SS15.,229346,5644
BMRB,5649,chemical shifts of SS16.,229346,5644
BMRB,5634,chemical shifts of SS1.,229360,5645
BMRB,5635,chemical shifts of SS2.,229360,5645
BMRB,5636,chemical shifts of SS3.,229360,5645
BMRB,5637,chemical shifts of SS4.,229360,5645
BMRB,5638,chemical shifts of SS5.,229360,5645
BMRB,5639,chemical shifts of SS6.,229360,5645
BMRB,5640,chemical shifts of SS7.,229360,5645
BMRB,5641,chemical shifts of SS8.,229360,5645
BMRB,5642,chemical shifts of SS9.,229360,5645
BMRB,5643,chemical shifts of SS10.,229360,5645
BMRB,5644,chemical shifts of SS11.,229360,5645
BMRB,5646,chemical shifts of SS13.,229360,5645
BMRB,5647,chemical shifts of SS14.,229360,5645
BMRB,5648,chemical shifts of SS15.,229360,5645
BMRB,5649,chemical shifts of SS16.,229360,5645
BMRB,5634,chemical shifts of SS1.,229374,5646
BMRB,5635,chemical shifts of SS2.,229374,5646
BMRB,5636,chemical shifts of SS3.,229374,5646
BMRB,5637,chemical shifts of SS4.,229374,5646
BMRB,5638,chemical shifts of SS5.,229374,5646
BMRB,5639,chemical shifts of SS6.,229374,5646
BMRB,5640,chemical shifts of SS7.,229374,5646
BMRB,5641,chemical shifts of SS8.,229374,5646
BMRB,5642,chemical shifts of SS9.,229374,5646
BMRB,5643,chemical shifts of SS10.,229374,5646
BMRB,5644,chemical shifts of SS11.,229374,5646
BMRB,5645,chemical shifts of SS12.,229374,5646
BMRB,5647,chemical shifts of SS14.,229374,5646
BMRB,5648,chemical shifts of SS15.,229374,5646
BMRB,5649,chemical shifts of SS16.,229374,5646
BMRB,5634,chemical shifts of SS1.,229388,5647
BMRB,5635,chemical shifts of SS2.,229388,5647
BMRB,5636,chemical shifts of SS3.,229388,5647
BMRB,5637,chemical shifts of SS4.,229388,5647
BMRB,5638,chemical shifts of SS5.,229388,5647
BMRB,5639,chemical shifts of SS6.,229388,5647
BMRB,5640,chemical shifts of SS7.,229388,5647
BMRB,5641,chemical shifts of SS8.,229388,5647
BMRB,5642,chemical shifts of SS9.,229388,5647
BMRB,5643,chemical shifts of SS10.,229388,5647
BMRB,5644,chemical shifts of SS11.,229388,5647
BMRB,5645,chemical shifts of SS12.,229388,5647
BMRB,5646,chemical shifts of SS13.,229388,5647
BMRB,5648,chemical shifts of SS15.,229388,5647
BMRB,5649,chemical shifts of SS16.,229388,5647
BMRB,5634,chemical shifts of SS1.,229402,5648
BMRB,5635,chemical shifts of SS2.,229402,5648
BMRB,5636,chemical shifts of SS3.,229402,5648
BMRB,5637,chemical shifts of SS4.,229402,5648
BMRB,5638,chemical shifts of SS5.,229402,5648
BMRB,5639,chemical shifts of SS6.,229402,5648
BMRB,5640,chemical shifts of SS7.,229402,5648
BMRB,5641,chemical shifts of SS8.,229402,5648
BMRB,5642,chemical shifts of SS9.,229402,5648
BMRB,5643,chemical shifts of SS10.,229402,5648
BMRB,5644,chemical shifts of SS11.,229402,5648
BMRB,5645,chemical shifts of SS12.,229402,5648
BMRB,5646,chemical shifts of SS13.,229402,5648
BMRB,5647,chemical shifts of SS14.,229402,5648
BMRB,5649,chemical shifts of SS16.,229402,5648
BMRB,5634,chemical shifts of SS1.,229416,5649
BMRB,5635,chemical shifts of SS2.,229416,5649
BMRB,5636,chemical shifts of SS3.,229416,5649
BMRB,5637,chemical shifts of SS4.,229416,5649
BMRB,5638,chemical shifts of SS5.,229416,5649
BMRB,5639,chemical shifts of SS6.,229416,5649
BMRB,5640,chemical shifts of SS7.,229416,5649
BMRB,5641,chemical shifts of SS8.,229416,5649
BMRB,5642,chemical shifts of SS9.,229416,5649
BMRB,5643,chemical shifts of SS10.,229416,5649
BMRB,5644,chemical shifts of SS11.,229416,5649
BMRB,5645,chemical shifts of SS12.,229416,5649
BMRB,5646,chemical shifts of SS13.,229416,5649
BMRB,5647,chemical shifts of SS14.,229416,5649
BMRB,5648,chemical shifts of SS15.,229416,5649
PDB,1MPE,BMRB Entry Tracking System,229531,5654
BMRB,5371,Wild Type U6 RNA,229559,5655
PDB,1NC0,BMRB Entry Tracking System,229559,5655
BMRB,5372,chemical shifts and coupling constants of reduced cytochrome c.,229657,5660
BMRB,5663,CPI-17 mutant T38D,229710,5662
BMRB,5662,CPI-17 22-120 domain (natural sequence),229723,5663
PDB,1N0Z,BMRB Entry Tracking System,229797,5667
BMRB,5398,3-methyladenine DNA glycosylase I (TAG) without zinc,229821,5668
PDB,1NJ3,BMRB Entry Tracking System,229861,5669
PDB,1NAJ,BMRB Entry Tracking System,229921,5671
PDB,1NAU,BMRB Entry Tracking System,229971,5673
BMRB,5675,HAINANTOXIN-I,229993,5674
PDB,1NIY,BMRB Entry Tracking System,229993,5674
BMRB,5674,HAINANTOXIN-IV,230014,5675
PDB,1NIX,BMRB Entry Tracking System,230014,5675
PDB,1N8M,BMRB Entry Tracking System,230031,5676
PDB,1N96,BMRB Entry Tracking System,230150,5681
BMRB,4849,Pheromone-binding protein from Bombyx mori,230334,5689
BMRB,5052,Chemical shifts by different group,230364,5690
PDB,1UAO,BMRB Entry Tracking System,230493,5694
BMRB,5697,ZASP-PDZ domain in complex with Alpha-Actinin-2 EF-hand domains,230531,5696
BMRB,5696,ZASP-PDZ domain,230561,5697
BMRB,5974,BopE from Burkholderia pseudomallei,230645,5701
BMRB,4233,H chemical shift by a different group,230681,5702
PDB,2KOC,BMRB Entry Tracking System,230742,5705
BMRB,7115,Cap-free structure of eIF4E,230897,5712
PDB,1HJM,BMRB Entry Tracking System,230919,5713
PDB,1ONM,BMRB Entry Tracking System,230932,5714
BMRB,5717,"XBY6:Same sequence, 6 dithioate substitutions",230974,5716
BMRB,5718,"XBY2:Same sequence, 2 dithioate substitutions",230974,5716
BMRB,5716,CK14 DNA 14-MER DUPLEX,230993,5717
BMRB,5718,XBY2 DNA 14-MER DUPLEX,230993,5717
BMRB,5716,CK14 DNA 14-MER DUPLEX,231011,5718
BMRB,5717,XBY6 DNA 14-MER DUPLEX,231011,5718
PDB,1S79,BMRB Entry Tracking System,231030,5719
BMRB,5746,adenylate kinase in complex with inhibitor Ap5A,231043,5720
BMRB,5724,R43A brazzein,231097,5723
BMRB,5725,Ala2ins brazzein,231097,5723
BMRB,5726,D50A brazzein,231097,5723
BMRB,5727,H31A brazzein,231097,5723
BMRB,5728,R33A brazzein,231097,5723
BMRB,5723,wt brazzein,231120,5724
BMRB,5725,Ala2ins brazzein,231120,5724
BMRB,5726,D50A brazzein,231120,5724
BMRB,5727,H31A brazzein,231120,5724
BMRB,5728,R33A brazzein,231120,5724
BMRB,5723,wt brazzein,231143,5725
BMRB,5724,R43A brazzein,231143,5725
BMRB,5726,D50A brazzein,231143,5725
BMRB,5727,H31A brazzein,231143,5725
BMRB,5728,R33A brazzein,231143,5725
BMRB,5723,wt brazzein,231164,5726
BMRB,5724,R43A brazzein,231164,5726
BMRB,5725,Ala2ins brazzein,231164,5726
BMRB,5727,H31A brazzein,231164,5726
BMRB,5728,R33A brazzein,231164,5726
BMRB,5723,wt brazzein,231188,5727
BMRB,5724,R43A brazzein,231188,5727
BMRB,5725,Ala2ins brazzein,231188,5727
BMRB,5726,D50A brazzein,231188,5727
BMRB,5728,R33A brazzein,231188,5727
BMRB,5723,wt brazzein,231211,5728
BMRB,5724,R43A brazzein,231211,5728
BMRB,5725,Ala2ins brazzein,231211,5728
BMRB,5726,D50A brazzein,231211,5728
BMRB,5727,H31A brazzein,231211,5728
BMRB,5732,SCR3(18-54) peptide,231287,5731
BMRB,5733,SCR3(34-54) peptide,231287,5731
BMRB,5734,SCR3(27-33) peptide,231287,5731
BMRB,5731,SCR3(18-54) peptide,231309,5732
BMRB,5733,SCR3(34-54) peptide,231309,5732
BMRB,5734,SCR3(27-33) peptide,231309,5732
BMRB,5731,SCR3(18-34) peptide,231327,5733
BMRB,5732,SCR3(18-54) peptide,231327,5733
BMRB,5734,SCR3(27-33) peptide,231327,5733
BMRB,5731,SCR3(18-34) peptide,231345,5734
BMRB,5732,SCR3(18-54) peptide,231345,5734
BMRB,5733,SCR3(34-54) peptide,231345,5734
PDB,1NP9,BMRB Entry Tracking System,231393,5737
PDB,1N1N,BMRB Entry Tracking System,231435,5739
BMRB,5741,DHFR:FOLATE:DHNADPH complex,231464,5740
BMRB,5740,DHFR:FOLATE:NADP+ complex,231487,5741
BMRB,5720,adenylate kinase in free form,231608,5746
PDB,1RYU,BMRB Entry Tracking System,231653,5748
BMRB,6182,FluA(R95K) complexed with fluorescein,231800,5756
BMRB,4972,Crh monomer in solution state,231830,5757
BMRB,5270,backbone assignment of YqgF,231850,5758
PDB,1ORL,BMRB Entry Tracking System,232045,5767
BMRB,5769,free form,232064,5768
PDB,1OQ6,BMRB Entry Tracking System,232064,5768
BMRB,5768,complex form with copper ion,232089,5769
PDB,1N8X,BMRB Entry Tracking System,232178,5773
BMRB,5776,modified sPrODN1:RNA duplex,232224,5775
BMRB,5777,modified PODN:RNA duplex,232224,5775
PDB,1NTQ,BMRB Entry Tracking System,232224,5775
BMRB,5775,unmodified DNA:RNA duplex,232244,5776
BMRB,5777,modified PODN:RNA duplex,232244,5776
PDB,1NTS,BMRB Entry Tracking System,232244,5776
BMRB,5775,unmodified DNA:RNA duplex,232266,5777
BMRB,5776,modified sPrODN1:RNA duplex,232266,5777
PDB,1NTT,BMRB Entry Tracking System,232266,5777
PDB,1OO7,BMRB Entry Tracking System,232353,5781
BMRB,5169,beta2-microglobulin with the first 3 residues,232374,5782
BMRB,5783,DN3 beta2-microglobulin (R3A mutant and with the first 3 residues),232374,5782
BMRB,5784,DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues),232374,5782
BMRB,5169,beta2-microglobulin with the first 3 residues,232392,5783
BMRB,5782,DN3 beta2-microglobulin without the first 3 residues,232392,5783
BMRB,5784,DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues),232392,5783
BMRB,5169,beta2-microglobulin with the first 3 residues,232408,5784
BMRB,5782,DN3 beta2-microglobulin (without the first 3 residue),232408,5784
BMRB,5783,DN3 beta2-microglobulin (R3A mutant with the first 3 residue),232408,5784
BMRB,5099,backbone and sidechain resonance assignments for N-TIMP-1,232424,5785
BMRB,5153,backbone dynamics data for N-TIMP-1,232424,5785
PDB,1OP4,BMRB Entry Tracking System,232446,5786
PDB,1P9J,BMRB Entry Tracking System,232810,5801
BMRB,5068,Recombinant hen lysozyme with extra N-terminal Met,232861,5803
BMRB,5069,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]",232861,5803
BMRB,5804,Three-disulfide variant of hen lysozyme: C76A/C94A,232861,5803
BMRB,5068,Recombinant hen lysozyme with extra N-terminal Met,232884,5804
BMRB,5069,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]",232884,5804
BMRB,5803,Three-disulfide variant of hen lysozyme: C64A/C80A,232884,5804
BMRB,5457,chemical shift assignment of SID24,232968,5808
BMRB,4841,chemical shift assignment of PAH2:SID13 complex,232968,5808
BMRB,5812,Chemical shift of GGYGGGRRDG,233040,5811
BMRB,5811,Chemical shift of GGRRDGGYGG,233058,5812
BMRB,6965,same protein in oxidized state,233224,5819
BMRB,5822,RPA70B,233270,5821
BMRB,5823,RPA70AB,233270,5821
BMRB,5821,RPA70A,233285,5822
BMRB,5823,RPA70AB,233285,5822
BMRB,5821,RPA70A,233310,5823
BMRB,5822,RPA70B,233310,5823
BMRB,5825,reduced form,233325,5824
BMRB,5824,oxidized form,233351,5825
BMRB,5828,"cytochrome c oxidized state of H26N, H33N mutant",233381,5827
BMRB,5829,cytochrome c reduced state of wild type,233381,5827
BMRB,5830,cytochrome c oxidized state of wild type,233381,5827
BMRB,5827,"cytochrome c reduced state of H26N, H33N mutant",233402,5828
BMRB,5829,cytochrome c reduced state of wild type,233402,5828
BMRB,5830,cytochrome c oxidized state of wild type,233402,5828
BMRB,5827,"cytochrome c reduced state of H26N, H33N mutant",233423,5829
BMRB,5828,"cytochrome c oxidized state of H26N, H33N mutant",233423,5829
BMRB,5830,cytochrome c oxidized state of wild type,233423,5829
BMRB,5827,"cytochrome c reduced state of H26N, H33N mutant",233440,5830
BMRB,5828,"cytochrome c oxidized state of H26N, H33N mutant",233440,5830
BMRB,5829,cytochrome c reduced state of wild type,233440,5830
PDB,1R3B,BMRB Entry Tracking System,233471,5833
PDB,1PJY,BMRB Entry Tracking System,233486,5834
BMRB,4371,chemical shifts of recombinant onconases,233509,5835
BMRB,15283,Solid-State C and N Chemical Shifts of GB3,233588,5839
BMRB,5564,Chemical shift data of the protein,233630,5841
BMRB,6474,relaxation data of CLV1 pT868 bound KI-FHA from KAPP,233630,5841
PDB,1UGL,BMRB Entry Tracking System,233867,5848
PDB,1P7A,BMRB Entry Tracking System,233928,5851
BMRB,5007,VS RIBOZYME SUBSTRATE STEM-LOOP,233953,5852
PDB,1OW9,BMRB Entry Tracking System,233953,5852
BMRB,5505,Chemical shifts and other data,234094,5858
PDB,1P9F,BMRB Entry Tracking System,234293,5864
PDB,1UHF,BMRB Entry Tracking System,234356,5867
PDB,1PVE,BMRB Entry Tracking System,234377,5868
PDB,1PQR,BMRB Entry Tracking System,234397,5869
PDB,1UGT,BMRB Entry Tracking System,234416,5870
BMRB,5876,"p47 residues 171-370, p47 monomer",234495,5874
PDB,1JRU,BMRB Entry Tracking System,234495,5874
PDB,1VAZ,BMRB Entry Tracking System,234495,5874
PDB,1Q1O,BMRB Entry Tracking System,234519,5875
BMRB,5874,"p47 residues 1-174, p47 monomer",234556,5876
BMRB,15138,13C and 15N resonance assignments,234580,5877
PDB,1UHU,BMRB Entry Tracking System,234654,5880
PDB,2OII,structure entry,234692,5882
PDB,2KA3,structure entry,234692,5882
BMRB,5916,free C-terminal EMP-AF-COOH,234717,5883
BMRB,4001,reduced apo-S100beta,235012,5895
BMRB,4099,S100B-Ca(2+)-p53 peptide complex,235012,5895
BMRB,4105,Reduced Calcium-Bound S100B from Rat,235012,5895
BMRB,5544,S100B(beta beta)-Ca2+-TRTK-12 peptide complex,235012,5895
PDB,1PPQ,BMRB Entry Tracking System,235115,5900
PDB,2I83,BMRB Entry Tracking System,235197,5903
BMRB,5908,Sac7d monomer mutant,235233,5905
BMRB,5909,Sso7d monomer,235233,5905
BMRB,5910,Sso7d monomer mutant,235233,5905
PDB,1RW2,BMRB Entry Tracking System,235282,5907
BMRB,5905,Sac7d monomer,235303,5908
BMRB,5909,Sso7d monomer,235303,5908
BMRB,5910,Sso7d monomer mutant,235303,5908
BMRB,4570,Sso7d-F31A mutant,235339,5909
BMRB,5905,Sac7d monomer,235339,5909
BMRB,5908,Sac7d monomer mutant,235339,5909
BMRB,5910,Sso7d I30V mutant,235339,5909
BMRB,4570,Sso7d-F31A mutant,235364,5910
BMRB,5905,Sac7d monomer,235364,5910
BMRB,5908,Sac7d monomer mutant,235364,5910
BMRB,5909,Sso7d monomer,235364,5910
PDB,1BBX,BMRB Entry Tracking System,235364,5910
PDB,1BF4,BMRB Entry Tracking System,235364,5910
PDB,1BNZ,BMRB Entry Tracking System,235364,5910
PDB,1C8C,BMRB Entry Tracking System,235364,5910
PDB,1CA5,BMRB Entry Tracking System,235364,5910
PDB,1CA6,BMRB Entry Tracking System,235364,5910
PDB,1JIC,BMRB Entry Tracking System,235364,5910
PDB,1SSO,BMRB Entry Tracking System,235364,5910
PDB,1PE4,BMRB Entry Tracking System,235433,5913
BMRB,5915,methionine-enkephalin in zwitterionic fast tumbling bicelles,235454,5914
PDB,1PLX,BMRB Entry Tracking System,235454,5914
BMRB,5914,methionine-enkephalin in fast tumbling Bic/PG,235473,5915
PDB,1PLW,BMRB Entry Tracking System,235473,5915
BMRB,5883,amidated C-terminal EMP-AF,235494,5916
PDB,1MNX,BMRB Entry Tracking System,235553,5919
BMRB,6232,the same protein but phosphorylated,235599,5921
BMRB,5925,wild type of the Drosophila protein drk,235634,5923
PDB,2A37,BMRB Entry Tracking System,235634,5923
BMRB,5923,T22G mutant of the Drosophila protein drk,235680,5925
PDB,2A36,BMRB Entry Tracking System,235680,5925
PDB,1VDY,BMRB Entry Tracking System,235734,5928
PDB,2DCP,BMRB Entry Tracking System,235734,5928
BMRB,5936,chmeical shifts of b-ADT,235795,5930
PDB,1Q75,BMRB Entry Tracking System,235840,5932
BMRB,5930,chmeical shifts of a-ADT,235938,5936
PDB,1Q7X,BMRB Entry Tracking System,235954,5937
BMRB,4552,The proton chemical shifts for the native parent peptide indolicidin,235983,5938
BMRB,5941,cycloCP-11,235983,5938
BMRB,4552,The proton chemical shifts for the native parent peptide indolicidin,236048,5941
BMRB,5938,CP-11in DPC micelles,236048,5941
BMRB,5945,CD8a cytoplasmic tail - Lck N terminus,236102,5944
BMRB,5944,CD4 cytoplasmic tail - Lck N terminus,236138,5945
PDB,1RXL,BMRB Entry Tracking System,236186,5947
BMRB,5949,"Disintegrin kistrin, ARGDWN Mutant",236212,5948
PDB,1Q7J,BMRB Entry Tracking System,236212,5948
BMRB,5948,"Disintegrin kistrin, AKGDWN Mutant",236237,5949
PDB,1Q7I,BMRB Entry Tracking System,236237,5949
PDB,2BN8,BMRB Entry Tracking System,236275,5950
BMRB,5954,"TGFB type II Receptor, free form",236317,5953
BMRB,5953,TGFB type II Receptor in complex with Monomeric TGFB3,236344,5954
PDB,1R05,BMRB Entry Tracking System,236395,5956
BMRB,5316,"HIV-1 gag, p55",236464,5960
PDB,2FYJ,BMRB Entry Tracking System,236481,5961
PDB,2FYL,BMRB Entry Tracking System,236481,5961
PDB,1R2P,BMRB Entry Tracking System,236501,5962
PDB,2APN,BMRB Entry Tracking System,236518,5963
BMRB,5965,human villin HP35 W64A mutant,236533,5964
BMRB,5966,human advillin HP36,236533,5964
BMRB,5964,human villin HP35,236548,5965
BMRB,5966,human advillin HP36,236548,5965
PDB,1UNC,BMRB Entry Tracking System,236548,5965
BMRB,5964,human villin HP35,236563,5966
BMRB,5965,human villin HP35 W64A mutant,236563,5966
BMRB,5701,SopE2 momomer,236757,5974
PDB,1R2L,BMRB Entry Tracking System,236855,5979
PDB,1V28,BMRB Entry Tracking System,237038,5986
BMRB,4948,A BUNGAROTOXIN,237084,5988
BMRB,5996,Relaxation data of complex form,237244,5995
BMRB,5995,Relaxation data of free form,237291,5996
PDB,1RG6,BMRB Entry Tracking System,237502,6002
PDB,1RGO,BMRB Entry Tracking System,237589,6005
BMRB,6008,Calcium bound form,237638,6007
BMRB,6007,Calcium free form,237652,6008
PDB,1RDE,BMRB Entry Tracking System,237668,6009
BMRB,6018,phosphorylated S100C/A11 fragment,237844,6017
BMRB,6017,S100C/A11,237860,6018
PDB,1V50,BMRB Entry Tracking System,237860,6018
BMRB,5226,Ssh10b dimer in Sac10b family,237874,6019
PDB,1RKK,BMRB Entry Tracking System,237890,6020
PDB,1Q8L,BMRB Entry Tracking System,237926,6022
BMRB,6357,"TEM-1 beta-lactamase, wild type",237974,6024
BMRB,7236,"TEM-1 beta-lactamase, mutant Y105W",237974,6024
BMRB,7237,"TEM-1 beta-lactamase, mutant Y105G",237974,6024
BMRB,7238,"TEM-1 beta-lactamase, mutant Y105N",237974,6024
BMRB,7239,"TEM-1 beta-lactamase, mutant Y105D",237974,6024
BMRB,16392,"TEM-1 beta-lactamase, dynamic data",237974,6024
BMRB,6030,KdpBN-ANP complex,238113,6029
PDB,1SVJ,BMRB Entry Tracking System,238113,6029
PDB,1U7Q,BMRB Entry Tracking System,238113,6029
PDB,2A29,BMRB Entry Tracking System,238113,6029
BMRB,6029,KdpBN free protein,238138,6030
PDB,1R9V,BMRB Entry Tracking System,238315,6039
PDB,1QVK,BMRB Entry Tracking System,238356,6041
PDB,1QVL,BMRB Entry Tracking System,238356,6041
PDB,1RFR,BMRB Entry Tracking System,238374,6042
PDB,1S04,BMRB Entry Tracking System,238431,6045
BMRB,6054,methylated protein,238596,6053
BMRB,6053,natural protein,238617,6054
BMRB,5131,Second PDZ domain of PTP-BL,238769,6060
BMRB,6091,PDZ2 from PTP-BL (complex with NTR),238769,6060
BMRB,6092,PDZ2 from PTP-BL (complex with RIL),238769,6060
PDB,1S2F,BMRB Entry Tracking System,238816,6062
PDB,1S34,BMRB Entry Tracking System,238816,6062
BMRB,6064,E6apc1 peptide,238835,6063
BMRB,6088,E6apn1 peptide,238835,6063
PDB,1RIM,BMRB Entry Tracking System,238835,6063
BMRB,6063,E6apc2 peptide,238853,6064
BMRB,6088,E6apn1 peptide,238853,6064
PDB,1RIK,BMRB Entry Tracking System,238853,6064
BMRB,6067,mutant at residue 27 and 29,238871,6066
PDB,1RYV,BMRB Entry Tracking System,238871,6066
BMRB,6066,mutant at residue 27 and 29,238887,6067
PDB,1RYG,BMRB Entry Tracking System,238887,6067
PDB,1V66,BMRB Entry Tracking System,238998,6072
BMRB,6077,"Mutant at residue 10, U replace C",239088,6076
PDB,1R7W,BMRB Entry Tracking System,239088,6076
BMRB,6076,"Wild type, C at residue 10",239117,6077
PDB,1R7Z,BMRB Entry Tracking System,239117,6077
BMRB,15949,Assignments of the Reduced and Active Form,239168,6080
PDB,1S4T,BMRB Entry Tracking System,239231,6083
PDB,1SQ8,BMRB Entry Tracking System,239244,6084
BMRB,15951,HCV p7 tm2 fragment,239301,6087
BMRB,6063,E6apc2 peptide,239322,6088
BMRB,6064,E6apc1 peptide,239322,6088
PDB,1RIJ,BMRB Entry Tracking System,239322,6088
PDB,1SIY,BMRB Entry Tracking System,239340,6089
BMRB,5131,Second PDZ domain of PTP-BL,239378,6091
BMRB,6060,PDZ2 from PTP-BL (complex with APC),239378,6091
BMRB,6092,PDZ2 from PTP-BL (complex with RIL),239378,6091
BMRB,5131,Second PDZ domain of PTP-BL,239398,6092
BMRB,6060,PDZ2 from PTP-BL (complex with APC),239398,6092
BMRB,6091,PDZ2 from PTP-BL (complex with NTR),239398,6092
PDB,1S1O,BMRB Entry Tracking System,239590,6101
BMRB,6104,CA2+-REGULATORY REGION (CLD),239628,6103
BMRB,6103,N-TERMINAL REGION,239648,6104
PDB,1S4A,BMRB Entry Tracking System,239672,6105
BMRB,6107,peptide from Leishmania braziliensis.,239690,6106
PDB,1S4J,BMRB Entry Tracking System,239690,6106
BMRB,6107,peptide from human.,239706,6107
PDB,2DHS,BMRB Entry Tracking System,239932,6121
PDB,1HEV,BMRB Entry Tracking System,239961,6123
PDB,1Q9B,BMRB Entry Tracking System,239961,6123
PDB,1T0W,BMRB Entry Tracking System,239961,6123
BMRB,6130,same protein in simple form,240066,6129
PDB,1S6U,BMRB Entry Tracking System,240066,6129
BMRB,6129,same protein in complex form with COPPER (I) ION,240097,6130
PDB,1S6O,BMRB Entry Tracking System,240097,6130
PDB,1SA8,BMRB Entry Tracking System,240169,6134
BMRB,6145,3LII in DMSO,240335,6144
BMRB,6146,nisin/3LII complex,240335,6144
BMRB,6144,nisin monomer,240358,6145
BMRB,6146,nisin/3LII complex,240358,6145
BMRB,6144,nisin monomer,240384,6146
BMRB,6145,3LII in DMSO,240384,6146
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),240514,6154
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),240514,6154
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),240514,6154
PDB,1VD9,BMRB Entry Tracking System,240514,6154
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),240530,6155
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),240530,6155
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),240530,6155
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),240546,6156
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),240546,6156
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),240546,6156
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),240565,6157
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),240565,6157
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),240565,6157
PDB,1SN6,BMRB Entry Tracking System,240581,6158
BMRB,6162,domain II,240630,6161
BMRB,6476,"GII loop mutant, GII-L",240630,6161
BMRB,6161,domain I,240646,6162
BMRB,6476,"GII loop mutant, GII-L",240646,6162
PDB,1SSL,BMRB Entry Tracking System,240677,6165
BMRB,6169,cyclic hexapeptide KKWWKF,240738,6168
BMRB,6170,cyclic hexapeptide RRYYRF,240738,6168
PDB,1SKL,BMRB Entry Tracking System,240738,6168
BMRB,6168,cyclic hexapeptide RR(NAL)(NAL)RF,240756,6169
BMRB,6170,cyclic hexapeptide RRYYRF,240756,6169
PDB,1SKK,BMRB Entry Tracking System,240756,6169
BMRB,6168,cyclic hexapeptide RR(NAL)(NAL)RF,240772,6170
BMRB,6169,cyclic hexapeptide KKWWKF,240772,6170
PDB,1SKI,BMRB Entry Tracking System,240772,6170
PDB,2LP6,BMRB Entry Tracking System,240827,6173
BMRB,5824,Chemical shifts of free ThKaiA180C (oxidized form),240857,6174
BMRB,5825,Chemical shifts of free ThKaiA180C (reduced form),240857,6174
PDB,1SZL,BMRB Entry Tracking System,240877,6175
BMRB,6178,Polypyrimidine tract-binding protein 1 domain 1,240931,6177
BMRB,6177,Polypyrimidine tract-binding protein 1 domain 2,240959,6178
BMRB,6180,LEKTI Domain 15,240978,6179
BMRB,6179,LEKTI Domain 15 short,240994,6180
BMRB,5756,complete resonance assignments of apo-protein,241023,6182
PDB,1SY8,BMRB Entry Tracking System,241094,6186
PDB,1SX0,BMRB Entry Tracking System,241193,6191
PDB,1SX1,BMRB Entry Tracking System,241193,6191
BMRB,4233,H chemical shift by a different group,241217,6192
BMRB,5702,chemical shifts at pH 6.0,241217,6192
BMRB,6194,chemical shifts at pH 6.0,241217,6192
BMRB,4233,H chemical shift by a different group,241252,6194
BMRB,5702,chemical shifts at pH 6.0,241252,6194
BMRB,6192,chemical shifts at pH 3.6,241252,6194
BMRB,6196,CYS131SER mutant,241271,6195
BMRB,6195,wild type protein,241292,6196
BMRB,5560,homologous T. maritima protein TM1290,241334,6198
PDB,1T6W,BMRB Entry Tracking System,241393,6201
BMRB,4567,catalytic domain of yUBC1,241409,6202
BMRB,6204,AlaB12-DKP-insulin,241434,6203
BMRB,6205,AbaB12-DKP-insulin,241434,6203
BMRB,6203,ThrB12-DKP-insulin,241454,6204
BMRB,6205,AbaB12-DKP-insulin,241454,6204
BMRB,6203,AlaB12-DKP-insulin,241477,6205
BMRB,6204,AbaB12-DKP-insulin,241477,6205
PDB,1SRK,BMRB Entry Tracking System,241641,6216
BMRB,6218,peptide ILGKIAEGIKSLF,241666,6217
BMRB,6219,peptide ILGKIWKGIKSLX,241666,6217
BMRB,6220,peptide ILGKIWEGIKSLF,241666,6217
PDB,1T55,BMRB Entry Tracking System,241666,6217
BMRB,6217,peptide ILGKIWKPIKKLF,241686,6218
BMRB,6219,peptide ILGKIWKGIKSLX,241686,6218
BMRB,6220,peptide ILGKIWEGIKSLF,241686,6218
PDB,1T54,BMRB Entry Tracking System,241686,6218
BMRB,6217,peptide ILGKIWKPIKKLF,241705,6219
BMRB,6218,peptide ILGKIAEGIKSLF,241705,6219
BMRB,6220,peptide ILGKIWEGIKSLF,241705,6219
PDB,1T52,BMRB Entry Tracking System,241705,6219
BMRB,6217,peptide ILGKIWKPIKKLF,241727,6220
BMRB,6218,peptide ILGKIAEGIKSLF,241727,6220
BMRB,6219,peptide ILGKIWKGIKSLX,241727,6220
PDB,1T51,BMRB Entry Tracking System,241727,6220
PDB,1T1T,BMRB Entry Tracking System,241763,6222
PDB,2RST,BMRB Entry Tracking System,241853,6226
BMRB,5293,16 mer aggregate,241869,6227
BMRB,5809,human hemglobin A,241947,6230
BMRB,5921,the same protein but unphosphorylated,241988,6232
BMRB,6281,Complexin/SNARE complex,242041,6235
BMRB,5276,Kazal-type Thrombin Inhibitor Dipetalin,242216,6242
PDB,1T5M,BMRB Entry Tracking System,242331,6246
PDB,1TH5,BMRB Entry Tracking System,242359,6247
PDB,1TTV,BMRB Entry Tracking System,242379,6248
BMRB,6251,V66W121,242418,6250
BMRB,6250,G88W121,242437,6251
BMRB,4771,C-terminal domain of the TolA protein,242606,6258
PDB,1U0I,BMRB Entry Tracking System,242640,6260
PDB,1SPW,BMRB Entry Tracking System,242706,6263
PDB,1T1H,BMRB Entry Tracking System,242747,6265
BMRB,5558,Same first author,242888,6271
BMRB,5592,Same first author,242888,6271
BMRB,6274,GTACACAGTAC mutant,242931,6273
BMRB,6273,GTTCACAGAAC mutant,242950,6274
BMRB,6276,MTF-1 in the DNA bound state (17bp),242968,6275
BMRB,6408,Two Zinc MTF-1,242968,6275
BMRB,6409,Four Zinc MTF-1,242968,6275
BMRB,6445,MTF-1 in the DNA bound state (22bp),242968,6275
BMRB,6275,MTF-1 in the free state,242999,6276
BMRB,6408,Two Zinc MTF-1,242999,6276
BMRB,6409,Four Zinc MTF-1,242999,6276
BMRB,6445,MTF-1 in the DNA bound state (22 bp),242999,6276
BMRB,6235,SNARE complex,243124,6281
PDB,1U5L,BMRB Entry Tracking System,243152,6282
PDB,2HAJ,BMRB Entry Tracking System,243191,6284
PDB,1XC5,BMRB Entry Tracking System,243221,6286
BMRB,5401,assignment and structure calculation for a different construct of the protein GABPa,243237,6287
BMRB,248,entry is now for chemically synthesized protein at 10C,243310,6290
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),243382,6293
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),243382,6293
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),243382,6293
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),243382,6293
BMRB,6294,tandem repeat 4 of FMBP-1 (residues 168-190) in 30% (v/v) TFE,243382,6293
BMRB,6296,tandem repeat 3 of FMBP-1 (residues 145-167) in 30% (v/v) TFE,243382,6293
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),243400,6294
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),243400,6294
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),243400,6294
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),243400,6294
BMRB,6293,tandem repeat 2 of FMBP-1 (residues 122-144) in 30% (v/v) TFE,243400,6294
BMRB,6296,tandem repeat 3 of FMBP-1 (residues 145-167) in 30% (v/v) TFE,243400,6294
BMRB,6154,tandem repeat 3 of FMBP-1 (residues 145-167),243456,6296
BMRB,6155,tandem repeat 4 of FMBP-1 (residues 168-190),243456,6296
BMRB,6156,tandem repeat 1 of FMBP-1 (residues 99-121),243456,6296
BMRB,6157,tandem repeat 2 of FMBP-1 (residues 122-144),243456,6296
BMRB,6293,tandem repeat 2 of FMBP-1 (residues 122-144) in 30% (v/v) TFE,243456,6296
BMRB,6294,tandem repeat 4 of FMBP-1 (residues 168-190) in 30% (v/v) TFE,243456,6296
PDB,1WNK,BMRB Entry Tracking System,243456,6296
PDB,1U5M,BMRB Entry Tracking System,243524,6299
PDB,1U3O,BMRB Entry Tracking System,243569,6300
PDB,1U2U,BMRB Entry Tracking System,243589,6301
BMRB,6303,DIIRON in DF2,243617,6302
PDB,1U7M,BMRB Entry Tracking System,243617,6302
BMRB,6302,DF2-TURN MUTANT,243638,6303
PDB,1U7J,BMRB Entry Tracking System,243638,6303
BMRB,6305,RanGAP1 C-domain,243659,6304
BMRB,6306,Sumoylated RanGAP1,243659,6304
BMRB,6304,SUMO-1,243678,6305
BMRB,6306,Sumoylated RanGAP1,243678,6305
BMRB,6304,SUMO-1,243699,6306
BMRB,6305,RanGAP1 C-domain,243699,6306
PDB,1U64,BMRB Entry Tracking System,243714,6307
BMRB,4849,Pheromone-binding Protein of Bombyx mori,243821,6313
PDB,2GZU,BMRB Entry Tracking System,243880,6317
PDB,1XHP,BMRB Entry Tracking System,243946,6320
BMRB,6322,Delta25-PYP light state,243971,6321
PDB,1XFN,BMRB Entry Tracking System,243971,6321
BMRB,6321,Delta25-PYP ground State,243985,6322
BMRB,6326,DFF5,244037,6325
BMRB,6327,DFF2,244037,6325
BMRB,6328,MM2,244037,6325
BMRB,6329,MM1,244037,6325
PDB,1WO7,BMRB Entry Tracking System,244037,6325
BMRB,6325,DFF7,244060,6326
BMRB,6327,DFF2,244060,6326
BMRB,6328,MM2,244060,6326
BMRB,6329,MM1,244060,6326
PDB,1WO6,BMRB Entry Tracking System,244060,6326
PDB,1WO5,BMRB Entry Tracking System,244082,6327
BMRB,6325,DFF7,244104,6328
BMRB,6326,DFF5,244104,6328
BMRB,6327,DFF2,244104,6328
BMRB,6329,MM1,244104,6328
PDB,1WO4,BMRB Entry Tracking System,244104,6328
BMRB,6325,DFF7,244127,6329
BMRB,6326,DFF5,244127,6329
BMRB,6327,DFF2,244127,6329
BMRB,6328,MM2,244127,6329
PDB,1WO3,BMRB Entry Tracking System,244127,6329
BMRB,6336,AP4A hydrolase monomer in complex with ATP,244151,6330
PDB,2XV9,BMRB Entry Tracking System,244223,6333
BMRB,6330,assignment of apo AP4A hydrolase monomer,244285,6336
PDB,1XPN,BMRB Entry Tracking System,244431,6343
PDB,1WPD,BMRB Entry Tracking System,244525,6347
BMRB,6350,LH1 Beta Polypeptide,244561,6349
BMRB,6349,LH1 alpha Polypeptide,244583,6350
BMRB,5041,chemical shifs of human DNA ligase iiialpha BRCT domain,244644,6353
PDB,2ga5,Yfh1 298K solution structure,244706,6356
BMRB,17068,Yfh1 272K chemical shift assignment,244706,6356
BMRB,6024,"TEM-1 beta-lactamase, mutant E28G",244735,6357
BMRB,7236,"TEM-1 beta-lactamase, mutant Y105W",244735,6357
BMRB,7237,"TEM-1 beta-lactamase, mutant Y105G",244735,6357
BMRB,7238,"TEM-1 beta-lactamase, mutant Y105N",244735,6357
BMRB,7239,"TEM-1 beta-lactamase, mutant Y105D",244735,6357
PDB,1XWH,BMRB Entry Tracking System,245112,6374
BMRB,6378,canine prion protein,245188,6377
BMRB,6377,feline prion protein,245203,6378
BMRB,6454,assignment of the free form,245216,6379
BMRB,6403,Ovine prion protein variant R168,245252,6381
BMRB,6387,aei-analogue monomer,245340,6386
PDB,1Y1B,BMRB Entry Tracking System,245340,6386
BMRB,6386,aei monomer,245357,6387
PDB,1Y1C,BMRB Entry Tracking System,245357,6387
PDB,1WT7,BMRB Entry Tracking System,245394,6389
BMRB,6393,Complex form with HA octasaccharide,245457,6392
BMRB,7221,"Link_TSG6 and hyaluronan octasaccharide complex, additional set of chemical shifts",245457,6392
BMRB,7222,"Link_TSG6 free form, additional set of chemical shifts",245457,6392
BMRB,6392,Free form,245479,6393
BMRB,7221,"Link_TSG6 and hyaluronan octasaccharide complex, additional set of chemical shifts",245479,6393
BMRB,7222,"Link_TSG6 free form, additional set of chemical shifts",245479,6393
BMRB,6401,R55F mutant,245612,6400
BMRB,6400,wt ma,245637,6401
PDB,1Y00,BMRB Entry Tracking System,245663,6402
BMRB,6381,"ovPrP,H168 monomer",245676,6403
PDB,2FK4,BMRB Entry Tracking System,245765,6407
BMRB,6275,MTF-1 in the free state,245785,6408
BMRB,6276,MTF-1 in the DNA bound state (17 bp),245785,6408
BMRB,6409,Four Zinc MTF-1,245785,6408
BMRB,6445,MTF-1 in the DNA bound state (22 bp),245785,6408
BMRB,6275,MTF-1 in the free state,245808,6409
BMRB,6276,MTF-1 in the DNA bound state (17 bp),245808,6409
BMRB,6408,Two Zinc MTF-1,245808,6409
BMRB,6445,MTF-1 in the DNA bound state (22 bp),245808,6409
BMRB,6412,Fragment 48-61 of bovine alpha-hemoglobin,245867,6411
BMRB,6413,Fragment 40-61,245867,6411
BMRB,6414,Amidated fragment 33-52,245867,6411
BMRB,6411,Amidated fragment 48-61 of bovine alpha-hemoglobin,245884,6412
BMRB,6413,Fragment 40-61,245884,6412
BMRB,6414,Amidated fragment 33-52,245884,6412
BMRB,6411,Amidated fragment 48-61 of bovine alpha-hemoglobin,245905,6413
BMRB,6412,Fragment 48-61 of bovine alpha-hemoglobin,245905,6413
BMRB,6414,Amidated fragment 33-52,245905,6413
BMRB,6411,Amidated fragment 48-61 of bovine alpha-hemoglobin,245925,6414
BMRB,6412,Fragment 48-61 of bovine alpha-hemoglobin,245925,6414
BMRB,6413,Fragment 40-61,245925,6414
BMRB,5068,Recombinant hen lysozyme with extra N-terminal Met,245946,6415
BMRB,5069,"Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]",245946,6415
BMRB,5803,Three-disulfide variant of hen lysozyme: C64A/C80A,245946,6415
BMRB,5804,Three-disulfide variant of hen lysozyme: C76A/C94A,245946,6415
PDB,1XT7,BMRB Entry Tracking System,246070,6420
BMRB,6422,sst1-selective somatostatin (SRIF) (analog 1),246093,6421
BMRB,6423,sst1-selective somatostatin (SRIF) (analog 1),246093,6421
BMRB,6424,sst1-selective somatostatin (SRIF) (analog 1),246093,6421
BMRB,6425,sst1-selective somatostatin (SRIF) (analog 1),246093,6421
BMRB,6426,sst1-selective somatostatin (SRIF) (analog 1),246093,6421
PDB,1XXZ,BMRB Entry Tracking System,246093,6421
BMRB,6421,sst1-selective somatostatin (SRIF) (analog 5),246110,6422
BMRB,6423,sst1-selective somatostatin (SRIF) (analog 1),246110,6422
BMRB,6424,sst1-selective somatostatin (SRIF) (analog 1),246110,6422
BMRB,6425,sst1-selective somatostatin (SRIF) (analog 1),246110,6422
BMRB,6426,sst1-selective somatostatin (SRIF) (analog 1),246110,6422
PDB,1XY4,BMRB Entry Tracking System,246110,6422
BMRB,6421,sst1-selective somatostatin (SRIF) (analog 5),246127,6423
BMRB,6422,sst1-selective somatostatin (SRIF) (analog 1),246127,6423
BMRB,6424,sst1-selective somatostatin (SRIF) (analog 1),246127,6423
BMRB,6425,sst1-selective somatostatin (SRIF) (analog 1),246127,6423
BMRB,6426,sst1-selective somatostatin (SRIF) (analog 1),246127,6423
PDB,1XY5,BMRB Entry Tracking System,246127,6423
BMRB,6421,sst1-selective somatostatin (SRIF) (analog 5),246145,6424
BMRB,6422,sst1-selective somatostatin (SRIF) (analog 1),246145,6424
BMRB,6423,sst1-selective somatostatin (SRIF) (analog 1),246145,6424
BMRB,6425,sst1-selective somatostatin (SRIF) (analog 1),246145,6424
BMRB,6426,sst1-selective somatostatin (SRIF) (analog 1),246145,6424
PDB,1XY6,BMRB Entry Tracking System,246145,6424
BMRB,6421,sst1-selective somatostatin (SRIF) (analog 5),246161,6425
BMRB,6422,sst1-selective somatostatin (SRIF) (analog 1),246161,6425
BMRB,6423,sst1-selective somatostatin (SRIF) (analog 1),246161,6425
BMRB,6424,sst1-selective somatostatin (SRIF) (analog 1),246161,6425
BMRB,6426,sst1-selective somatostatin (SRIF) (analog 1),246161,6425
PDB,1XY8,BMRB Entry Tracking System,246161,6425
BMRB,6421,sst1-selective somatostatin (SRIF) (analog 5),246178,6426
BMRB,6422,sst1-selective somatostatin (SRIF) (analog 1),246178,6426
BMRB,6423,sst1-selective somatostatin (SRIF) (analog 1),246178,6426
BMRB,6424,sst1-selective somatostatin (SRIF) (analog 1),246178,6426
BMRB,6425,sst1-selective somatostatin (SRIF) (analog 1),246178,6426
PDB,1XY9,BMRB Entry Tracking System,246178,6426
BMRB,6449,complex with 9-cis retinoic acid,246249,6429
PDB,2GMC,BMRB Entry Tracking System,246417,6437
PDB,2GMD,BMRB Entry Tracking System,246417,6437
BMRB,6440,PAS1-PAS2 domain,246468,6439
BMRB,6439,PAS1 domain,246509,6440
BMRB,6275,MTF-1 in the free state,246610,6445
BMRB,6276,MTF-1 in the DNA bound state (17 bp),246610,6445
BMRB,6408,Two Zinc MTF-1,246610,6445
BMRB,6409,Four Zinc MTF-1,246610,6445
PDB,1Y7X,BMRB Entry Tracking System,246659,6447
BMRB,6429,apo form of the protein,246725,6449
BMRB,6379,backbone assignment of the complex with HSL,246835,6454
BMRB,6504,crambin in DPC micelles,246851,6455
PDB,2MB8,BMRB Entry Tracking System,246895,6457
PDB,1YIU,BMRB Entry Tracking System,246923,6459
PDB,1Y5C,BMRB Entry Tracking System,246980,6462
PDB,1WXN,BMRB Entry Tracking System,247092,6467
BMRB,5564,Chemical shift data of the free protein,247181,6474
BMRB,5841,relaxation data of free KI-FHA from KAPP,247181,6474
BMRB,6161,GI domain of Hho1p,247231,6476
BMRB,6162,GII domain of Hho1p,247231,6476
PDB,1YMO,BMRB Entry Tracking System,247254,6477
BMRB,6382,COPPER FORM A69P MUTANT,247346,6480
BMRB,6481,APO FORM,247346,6480
BMRB,6483,APO FORM A69P MUTANT,247346,6480
PDB,1YJV,BMRB Entry Tracking System,247346,6480
BMRB,6382,COPPER FORM A69P MUTANT,247375,6481
BMRB,6480,CU(I) FORM,247375,6481
BMRB,6483,APO FORM   A69P MUTANT,247375,6481
PDB,1YJU,BMRB Entry Tracking System,247375,6481
BMRB,6480,CU(I) FORM,247402,6482
BMRB,6481,APO FORM,247402,6482
BMRB,6483,APO FORM A69P MUTANT,247402,6482
PDB,1YJT,BMRB Entry Tracking System,247402,6482
BMRB,6382,COPPER FORM A69P MUTANT,247431,6483
BMRB,6480,CU(I) FORM,247431,6483
BMRB,6481,APO FORM,247431,6483
PDB,1YJR,BMRB Entry Tracking System,247431,6483
PDB,2A3J,BMRB Entry Tracking System,247550,6493
BMRB,6495,BsCM protein with TSA,247565,6494
BMRB,6496,BsCM protein with prephenate,247565,6494
BMRB,6494,BsCM protein in free form,247592,6495
BMRB,6496,BsCM protein with prephenate,247592,6495
BMRB,6494,BsCM protein in free form,247617,6496
BMRB,6495,BsCM protein with TSA,247617,6496
PDB,1XKM,BMRB Entry Tracking System,247660,6499
BMRB,6455,the same protein in different solvent,247767,6504
PDB,2CA7,BMRB Entry Tracking System,247819,6506
BMRB,6508,PCAF with NP1,247841,6507
BMRB,6507,PCAF with NP2,247865,6508
PDB,1YG3,BMRB Entry Tracking System,247887,6509
PDB,1YG4,BMRB Entry Tracking System,247887,6509
PDB,1YT6,BMRB Entry Tracking System,247929,6511
PDB,2BIC,BMRB Entry Tracking System,248095,6520
,4048,Data were collected at a different pH for this molecular system.,248109,6521
,6522,Mutant p53 tetramerization domain (p53tet-R337H),248109,6521
BMRB,4048,Data were collected at a different pH for this molecular system.,248128,6522
BMRB,6521,p53 tetramer,248128,6522
,5982,ApoE C-terminal domain chemical shift assignment,248145,6524
PDB,1Z09,BMRB Entry Tracking System,248194,6527
PDB,2LVF,BMRB Entry Tracking System,248229,6529
PDB,1YMZ,BMRB Entry Tracking System,248267,6530
BMRB,6532,apo-S100A13,248291,6531
BMRB,6531,Calcium-S100A13,248311,6532
,4127,"Sequence-specific 1H, 13C, and 15N Resonance Assignment of Tag-OBD",248348,6535
PDB,2GTJ,BMRB Entry Tracking System,248365,6536
PDB,2GTO,BMRB Entry Tracking System,248409,6539
,6536,"Assignments of the same domain, in reduced form",248409,6539
PDB,1Z2J,BMRB Entry Tracking System,248501,6543
,5834,HIV-1 frameshift inducing stem-loop RNA,248501,6543
PDB,2QMV,BMRB Entry Tracking System,248557,6549
BMRB,6553,hidden folding intermediate,248597,6552
BMRB,6552,Multiple Folding Protein,248624,6553
PDB,1YZA,BMRB Entry Tracking System,248624,6553
PDB,1WZ4,BMRB Entry Tracking System,248718,6557
BMRB,6559,complexed to the peptide APPTPPPLPP,248740,6558
BMRB,6558,FBP11WW1 in simple form,248765,6559
PDB,1YYJ,BMRB Entry Tracking System,248793,6560
PDB,1YYX,BMRB Entry Tracking System,248793,6560
PDB,1Z30,BMRB Entry Tracking System,248836,6562
PDB,2BO5,BMRB Entry Tracking System,248891,6564
BMRB,6567,N protein bound to the measles virus P protein,248925,6566
BMRB,6568,P protein (amino acids 457-507),248925,6566
BMRB,6569,P protein bound to the measles virus N protein,248925,6566
,6566,N protein,248940,6567
,6568,P protein (amino acids 457-507),248940,6567
,6569,P protein bound to the measles virus N protein,248940,6567
,6566,N protein,248956,6568
,6567,N protein bound to the measles virus P protein,248956,6568
,6569,P protein bound to the measles virus N protein,248956,6568
,6566,N protein,248971,6569
,6567,N protein bound to the measles virus P protein,248971,6569
,6568,P protein (amino acids 457-507),248971,6569
,5333,reduced form,249037,6572
BMRB,4697,"same protein, different domain",249132,6577
PDB,2BBU,BMRB Entry Tracking System,249205,6580
BMRB,4285,chemical shifts for the apo form of the protein,249280,6583
BMRB,6588,apolipoprotein A-I(1-186),249367,6587
,6587,apolipoprotein A-I,249380,6588
PDB,1X32,BMRB Entry Tracking System,249391,6589
BMRB,6637,AcAMP2F18Nalb mutant,249428,6591
BMRB,6639,AcAMP2F18W mutant,249428,6591
BMRB,6647,AcAMP2F18Wb,249428,6591
BMRB,6656,AcAMP2F18Pff/F20Pfff,249428,6591
BMRB,6657,AcAMP2F18Nal mutant,249428,6591
PDB,1MMC,BMRB Entry Tracking System,249428,6591
,6593,Chromo 3 domain of cpSRP43,249458,6592
,7241,Chromo domain 2 complexed with cpSRP54 peptide,249458,6592
,6592,Chromo2 domain of cpSRP43,249472,6593
PDB,1Z2Q,BMRB Entry Tracking System,249486,6594
PDB,1ZA8,BMRB Entry Tracking System,249512,6596
BMRB,6600,simple protein form,249575,6599
BMRB,6599,complex form with BTI,249625,6600
PDB,1Z7T,BMRB Entry Tracking System,249625,6600
BMRB,6503,Apo form of the domain.,249697,6604
,6618,"chemical shifts from P6, peptide based on trialysin",249901,6616
,6619,"chemical shifts from P7, peptide based on trialysin",249901,6616
,6616,"chemical shifts from P5, peptide based on trialysin",249935,6618
,6619,"chemical shifts from P7, peptide based on trialysin",249935,6618
,6616,"chemical shifts from P5, peptide based on trialysin",249953,6619
,6618,"chemical shifts from P6, peptide based on trialysin",249953,6619
PDB,2BYE,BMRB Entry Tracking System,250062,6624
BMRB,5114,structure of KB1 in aqueous solution (ladder),250123,6627
BMRB,5609,"NMR structure of [Ala1,15]kalata B1 (knot)",250123,6627
BMRB,6779,FimD(25-125),250155,6629
PDB,1ZC5,BMRB Entry Tracking System,250192,6633
BMRB,5625,Wild-type ferricytochrome c3 chemical shift assignments.,250222,6634
PDB,1X5V,BMRB Entry Tracking System,250266,6636
BMRB,6591,AcAMP2F18Pff/Y20Pff,250285,6637
BMRB,6639,AcAMP2F18W mutant,250285,6637
BMRB,6647,AcAMP2F18Wb,250285,6637
BMRB,6656,AcAMP2F18Pff/F20Pfff,250285,6637
BMRB,6657,AcAMP2F18Nal mutant,250285,6637
PDB,1MMC,BMRB Entry Tracking System,250285,6637
BMRB,6591,AcAMP2F18Pff/Y20Pff,250324,6639
BMRB,6637,AcAMP2F18Nalb mutant,250324,6639
BMRB,6647,AcAMP2F18Wb,250324,6639
BMRB,6656,AcAMP2F18Pff/F20Pfff,250324,6639
BMRB,6657,AcAMP2F18Nal mutant,250324,6639
PDB,2ITH,BMRB Entry Tracking System,250436,6645
BMRB,6591,AcAMP2F18Pff/Y20Pff,250463,6647
BMRB,6637,AcAMP2F18Nalb mutant,250463,6647
BMRB,6639,AcAMP2F18W mutant,250463,6647
BMRB,6656,AcAMP2F18Pff/F20Pfff,250463,6647
BMRB,6657,AcAMP2F18Nal mutant,250463,6647
PDB,2ADT,BMRB Entry Tracking System,250605,6652
BMRB,6591,AcAMP2F18Pff/Y20Pff,250702,6656
BMRB,6637,AcAMP2F18Nalb mutant,250702,6656
BMRB,6639,AcAMP2F18W mutant,250702,6656
BMRB,6647,AcAMP2F18Wb,250702,6656
BMRB,6657,AcAMP2F18Nal mutant,250702,6656
PDB,1ZNT,BMRB Entry Tracking System,250702,6656
BMRB,6591,AcAMP2F18Pff/Y20Pff,250728,6657
BMRB,6637,AcAMP2F18Nalb mutant,250728,6657
BMRB,6639,AcAMP2F18W mutant,250728,6657
BMRB,6647,AcAMP2F18Wb,250728,6657
BMRB,6656,AcAMP2F18Pff/F20Pfff,250728,6657
,6659,wild-type rubredoxin oxidized state,250838,6662
,6660,ubredoxin (V8A) oxidized state,250838,6662
,6661,ubredoxin (V8A) reduced state,250838,6662
,6663,rubredoxin (V8G) oxidized state,250838,6662
,6664,ubredoxin (V8G) reduced state,250838,6662
,6665,ubredoxin (V8G/V44G) oxidized state,250838,6662
,6666,ubredoxin (V8G/V44G) reduced state,250838,6662
,6667,ubredoxin (V8I) oxidized state,250838,6662
,6668,ubredoxin (V8I) reduced state,250838,6662
,6669,ubredoxin (V8L) oxidized state,250838,6662
,6670,ubredoxin (V8L) reduced state,250838,6662
,6671,rubredoxin (V44A) oxidized state,250838,6662
,6672,rubredoxin (V44A) reduced state,250838,6662
,6673,rubredoxin (V44G) oxidized state,250838,6662
,6674,rubredoxin (V44G) reduced state,250838,6662
,6675,rubredoxin (V44I) oxidized state,250838,6662
,6676,rubredoxin (V44I)reduced state,250838,6662
,6677,rubredoxin (V44L) oxidized state,250838,6662
,6678,rubredoxin (V44L) reduced state,250838,6662
,6659,wild-type rubredoxin oxidized state,250854,6663
,6660,ubredoxin (V8A) oxidized state,250854,6663
,6661,ubredoxin (V8A) reduced state,250854,6663
,6662,wild-type rubredoxin reduced state,250854,6663
,6664,ubredoxin (V8G) reduced state,250854,6663
,6665,ubredoxin (V8G/V44G) oxidized state,250854,6663
,6666,ubredoxin (V8G/V44G) reduced state,250854,6663
,6667,ubredoxin (V8I) oxidized state,250854,6663
,6668,ubredoxin (V8I) reduced state,250854,6663
,6669,ubredoxin (V8L) oxidized state,250854,6663
,6670,ubredoxin (V8L) reduced state,250854,6663
,6671,rubredoxin (V44A) oxidized state,250854,6663
,6672,rubredoxin (V44A) reduced state,250854,6663
,6673,rubredoxin (V44G) oxidized state,250854,6663
,6674,rubredoxin (V44G) reduced state,250854,6663
,6675,rubredoxin (V44I) oxidized state,250854,6663
,6676,rubredoxin (V44I)reduced state,250854,6663
,6677,rubredoxin (V44L) oxidized state,250854,6663
,6678,rubredoxin (V44L) reduced state,250854,6663
,6659,wild-type rubredoxin oxidized state,250870,6664
,6660,ubredoxin (V8A) oxidized state,250870,6664
,6661,ubredoxin (V8A) reduced state,250870,6664
,6662,wild-type rubredoxin reduced state,250870,6664
,6663,rubredoxin (V8G) reduced state,250870,6664
,6665,ubredoxin (V8G/V44G) oxidized state,250870,6664
,6666,ubredoxin (V8G/V44G) reduced state,250870,6664
,6667,ubredoxin (V8I) oxidized state,250870,6664
,6668,ubredoxin (V8I) reduced state,250870,6664
,6669,ubredoxin (V8L) oxidized state,250870,6664
,6670,ubredoxin (V8L) reduced state,250870,6664
,6671,rubredoxin (V44A) oxidized state,250870,6664
,6672,rubredoxin (V44A) reduced state,250870,6664
,6673,rubredoxin (V44G) oxidized state,250870,6664
,6674,rubredoxin (V44G) reduced state,250870,6664
,6675,rubredoxin (V44I) oxidized state,250870,6664
,6676,rubredoxin (V44I)reduced state,250870,6664
,6677,rubredoxin (V44L) oxidized state,250870,6664
,6678,rubredoxin (V44L) reduced state,250870,6664
,6659,wild-type rubredoxin oxidized state,250886,6665
,6660,ubredoxin (V8A) oxidized state,250886,6665
,6661,ubredoxin (V8A) reduced state,250886,6665
,6662,wild-type rubredoxin reduced state,250886,6665
,6663,rubredoxin (V8G) oxidized state,250886,6665
,6664,ubredoxin (V8G) reduced state,250886,6665
,6666,ubredoxin (V8G/V44G) reduced state,250886,6665
,6667,ubredoxin (V8I) oxidized state,250886,6665
,6668,ubredoxin (V8I) reduced state,250886,6665
,6669,ubredoxin (V8L) oxidized state,250886,6665
,6670,ubredoxin (V8L) reduced state,250886,6665
,6671,rubredoxin (V44A) oxidized state,250886,6665
,6672,rubredoxin (V44A) reduced state,250886,6665
,6673,rubredoxin (V44G) oxidized state,250886,6665
,6674,rubredoxin (V44G) reduced state,250886,6665
,6675,rubredoxin (V44I) oxidized state,250886,6665
,6676,rubredoxin (V44I)reduced state,250886,6665
,6677,rubredoxin (V44L) oxidized state,250886,6665
,6678,rubredoxin (V44L) reduced state,250886,6665
,6659,wild-type rubredoxin oxidized state,250902,6666
,6660,rubredoxin (V8A) oxidized state,250902,6666
,6661,rubredoxin (V8A) reduced state,250902,6666
,6662,wild-type rubredoxin reduced state,250902,6666
,6663,rubredoxin (V8G) oxidized state,250902,6666
,6664,rubredoxin (V8G) reduced state,250902,6666
,6665,rubredoxin (V8G/V44G) oxidized state,250902,6666
,6667,rubredoxin (V8I) oxidized state,250902,6666
,6668,rubredoxin (V8I) reduced state,250902,6666
,6669,rubredoxin (V8L) oxidized state,250902,6666
,6670,rubredoxin (V8L) reduced state,250902,6666
,6671,rubredoxin (V44A) oxidized state,250902,6666
,6672,rubredoxin (V44A) reduced state,250902,6666
,6673,rubredoxin (V44G) oxidized state,250902,6666
,6674,rubredoxin (V44G) reduced state,250902,6666
,6675,rubredoxin (V44I) oxidized state,250902,6666
,6676,rubredoxin (V44I)reduced state,250902,6666
,6677,rubredoxin (V44L) oxidized state,250902,6666
,6678,rubredoxin (V44L) reduced state,250902,6666
,6659,wild-type rubredoxin oxidized state,250918,6667
,6660,ubredoxin (V8A) oxidized state,250918,6667
,6661,ubredoxin (V8A) reduced state,250918,6667
,6662,wild-type rubredoxin reduced state,250918,6667
,6663,rubredoxin (V8G) oxidized state,250918,6667
,6664,ubredoxin (V8G) reduced state,250918,6667
,6665,ubredoxin (V8G/V44G) oxidized state,250918,6667
,6666,ubredoxin (V8G/V44G) reduced state,250918,6667
,6668,ubredoxin (V8I) reduced state,250918,6667
,6669,ubredoxin (V8L) oxidized state,250918,6667
,6670,ubredoxin (V8L) reduced state,250918,6667
,6671,rubredoxin (V44A) oxidized state,250918,6667
,6672,rubredoxin (V44A) reduced state,250918,6667
,6673,rubredoxin (V44G) oxidized state,250918,6667
,6674,rubredoxin (V44G) reduced state,250918,6667
,6675,rubredoxin (V44I) oxidized state,250918,6667
,6676,rubredoxin (V44I)reduced state,250918,6667
,6677,rubredoxin (V44L) oxidized state,250918,6667
,6678,rubredoxin (V44L) reduced state,250918,6667
,6659,wild-type rubredoxin oxidized state,250934,6668
,6660,ubredoxin (V8A) oxidized state,250934,6668
,6661,ubredoxin (V8A) reduced state,250934,6668
,6662,wild-type rubredoxin reduced state,250934,6668
,6663,rubredoxin (V8G) oxidized state,250934,6668
,6664,ubredoxin (V8G) reduced state,250934,6668
,6665,ubredoxin (V8G/V44G) oxidized state,250934,6668
,6666,bredoxin (V8G/V44G) reduced state,250934,6668
,6667,ubredoxin (V8I) oxidized state,250934,6668
,6669,ubredoxin (V8L) oxidized state,250934,6668
,6670,ubredoxin (V8L) reduced state,250934,6668
,6671,rubredoxin (V44A) oxidized state,250934,6668
,6672,rubredoxin (V44A) reduced state,250934,6668
,6673,rubredoxin (V44G) oxidized state,250934,6668
,6674,rubredoxin (V44G) reduced state,250934,6668
,6675,rubredoxin (V44I) oxidized state,250934,6668
,6676,rubredoxin (V44I)reduced state,250934,6668
,6677,rubredoxin (V44L) oxidized state,250934,6668
,6678,rubredoxin (V44L) reduced state,250934,6668
,6659,wild-type rubredoxin oxidized state,250950,6669
,6660,ubredoxin (V8A) oxidized state,250950,6669
,6661,ubredoxin (V8A) reduced state,250950,6669
,6662,wild-type rubredoxin reduced state,250950,6669
,6663,rubredoxin (V8G) oxidized state,250950,6669
,6664,ubredoxin (V8G) reduced state,250950,6669
,6665,ubredoxin (V8G/V44G) oxidized state,250950,6669
,6666,ubredoxin (V8G/V44G) reduced state,250950,6669
,6667,ubredoxin (V8I) oxidized state,250950,6669
,6668,ubredoxin (V8I) reduced state,250950,6669
,6670,ubredoxin (V8L) reduced state,250950,6669
,6671,rubredoxin (V44A) oxidized state,250950,6669
,6672,rubredoxin (V44A) reduced state,250950,6669
,6673,rubredoxin (V44G) oxidized state,250950,6669
,6674,rubredoxin (V44G) reduced state,250950,6669
,6675,rubredoxin (V44I) oxidized state,250950,6669
,6676,rubredoxin (V44I)reduced state,250950,6669
,6677,rubredoxin (V44L) oxidized state,250950,6669
,6678,rubredoxin (V44L) reduced state,250950,6669
,6659,wild-type rubredoxin oxidized state,250982,6670
,6660,ubredoxin (V8A) oxidized state,250982,6670
,6661,ubredoxin (V8A) reduced state,250982,6670
,6662,wild-type rubredoxin reduced state,250982,6670
,6663,rubredoxin (V8G) oxidized state,250982,6670
,6664,ubredoxin (V8G) reduced state,250982,6670
,6665,ubredoxin (V8G/V44G) oxidized state,250982,6670
,6666,ubredoxin (V8G/V44G) reduced state,250982,6670
,6667,ubredoxin (V8I) oxidized state,250982,6670
,6668,ubredoxin (V8I) reduced state,250982,6670
,6669,ubredoxin (V8L) oxidized state,250982,6670
,6671,rubredoxin (V44A) oxidized state,250982,6670
,6672,rubredoxin (V44A) reduced state,250982,6670
,6673,rubredoxin (V44G) oxidized state,250982,6670
,6674,rubredoxin (V44G) reduced state,250982,6670
,6675,rubredoxin (V44I) oxidized state,250982,6670
,6676,rubredoxin (V44I)reduced state,250982,6670
,6677,rubredoxin (V44L) oxidized state,250982,6670
,6678,rubredoxin (V44L) reduced state,250982,6670
,6659,wild-type rubredoxin oxidized state,250998,6671
,6660,ubredoxin (V8A) oxidized state,250998,6671
,6661,ubredoxin (V8A) reduced state,250998,6671
,6662,wild-type rubredoxin reduced state,250998,6671
,6663,rubredoxin (V8G) oxidized state,250998,6671
,6664,ubredoxin (V8G) reduced state,250998,6671
,6665,ubredoxin (V8G/V44G) oxidized state,250998,6671
,6666,ubredoxin (V8G/V44G) reduced state,250998,6671
,6667,ubredoxin (V8I) oxidized state,250998,6671
,6668,ubredoxin (V8I) reduced state,250998,6671
,6669,ubredoxin (V8L) oxidized state,250998,6671
,6670,ubredoxin (V8L) reduced state,250998,6671
,6672,rubredoxin (V44A) reduced state,250998,6671
,6673,rubredoxin (V44G) oxidized state,250998,6671
,6674,rubredoxin (V44G) reduced state,250998,6671
,6675,rubredoxin (V44I) oxidized state,250998,6671
,6676,rubredoxin (V44I)reduced state,250998,6671
,6677,rubredoxin (V44L) oxidized state,250998,6671
,6678,rubredoxin (V44L) reduced state,250998,6671
,6659,wild-type rubredoxin oxidized state,251014,6672
,6660,ubredoxin (V8A) oxidized state,251014,6672
,6661,ubredoxin (V8A) reduced state,251014,6672
,6662,wild-type rubredoxin reduced state,251014,6672
,6663,rubredoxin (V8G) oxidized state,251014,6672
,6664,ubredoxin (V8G) reduced state,251014,6672
,6665,ubredoxin (V8G/V44G) oxidized state,251014,6672
,6666,ubredoxin (V8G/V44G) reduced state,251014,6672
,6667,ubredoxin (V8I) oxidized state,251014,6672
,6668,ubredoxin (V8I) reduced state,251014,6672
,6669,ubredoxin (V8L) oxidized state,251014,6672
,6670,ubredoxin (V8L) reduced state,251014,6672
,6671,rubredoxin (V44A) oxidized state,251014,6672
,6673,rubredoxin (V44G) oxidized state,251014,6672
,6674,rubredoxin (V44G) reduced state,251014,6672
,6675,rubredoxin (V44I) oxidized state,251014,6672
,6676,rubredoxin (V44I)reduced state,251014,6672
,6677,rubredoxin (V44L) oxidized state,251014,6672
,6678,rubredoxin (V44L) reduced state,251014,6672
,6659,wild-type rubredoxin oxidized state,251030,6673
,6660,ubredoxin (V8A) oxidized state,251030,6673
,6661,ubredoxin (V8A) reduced state,251030,6673
,6662,wild-type rubredoxin reduced state,251030,6673
,6663,rubredoxin (V8G) oxidized state,251030,6673
,6664,ubredoxin (V8G) reduced state,251030,6673
,6665,ubredoxin (V8G/V44G) oxidized state,251030,6673
,6666,ubredoxin (V8G/V44G) reduced state,251030,6673
,6667,ubredoxin (V8I) oxidized state,251030,6673
,6668,ubredoxin (V8I) reduced state,251030,6673
,6669,ubredoxin (V8L) oxidized state,251030,6673
,6670,ubredoxin (V8L) reduced state,251030,6673
,6671,rubredoxin (V44A) oxidized state,251030,6673
,6672,rubredoxin (V44A) reduced state,251030,6673
,6674,rubredoxin (V44G) reduced state,251030,6673
,6675,rubredoxin (V44I) oxidized state,251030,6673
,6676,rubredoxin (V44I)reduced state,251030,6673
,6677,rubredoxin (V44L) oxidized state,251030,6673
,6678,rubredoxin (V44L) reduced state,251030,6673
BMRB,6659,wild-type rubredoxin oxidized state,251046,6674
BMRB,6660,ubredoxin (V8A) oxidized state,251046,6674
BMRB,6661,ubredoxin (V8A) reduced state,251046,6674
BMRB,6662,wild-type rubredoxin reduced state,251046,6674
BMRB,6663,rubredoxin (V8G) oxidized state,251046,6674
BMRB,6664,ubredoxin (V8G) reduced state,251046,6674
BMRB,6665,ubredoxin (V8G/V44G) oxidized state,251046,6674
BMRB,6666,ubredoxin (V8G/V44G) reduced state,251046,6674
BMRB,6667,ubredoxin (V8I) oxidized state,251046,6674
BMRB,6668,ubredoxin (V8I) reduced state,251046,6674
BMRB,6669,ubredoxin (V8L) oxidized state,251046,6674
BMRB,6670,ubredoxin (V8L) reduced state,251046,6674
BMRB,6671,rubredoxin (V44A) oxidized state,251046,6674
BMRB,6672,rubredoxin (V44A) reduced state,251046,6674
BMRB,6673,rubredoxin (V44G) oxidized state,251046,6674
BMRB,6675,rubredoxin (V44I) oxidized state,251046,6674
BMRB,6676,rubredoxin (V44I)reduced state,251046,6674
BMRB,6677,rubredoxin (V44L) oxidized state,251046,6674
BMRB,6678,rubredoxin (V44L) reduced state,251046,6674
,6659,wild-type rubredoxin oxidized state,251062,6675
,6660,ubredoxin (V8A) oxidized state,251062,6675
,6661,ubredoxin (V8A) reduced state,251062,6675
,6662,wild-type rubredoxin reduced state,251062,6675
,6663,rubredoxin (V8G) oxidized state,251062,6675
,6664,ubredoxin (V8G) reduced state,251062,6675
,6665,ubredoxin (V8G/V44G) oxidized state,251062,6675
,6666,ubredoxin (V8G/V44G) reduced state,251062,6675
,6667,ubredoxin (V8I) oxidized state,251062,6675
,6668,ubredoxin (V8I) reduced state,251062,6675
,6669,ubredoxin (V8L) oxidized state,251062,6675
,6670,ubredoxin (V8L) reduced state,251062,6675
,6671,rubredoxin (V44A) oxidized state,251062,6675
,6672,rubredoxin (V44A) reduced state,251062,6675
,6673,rubredoxin (V44G) oxidized state,251062,6675
,6674,rubredoxin (V44G) reduced state,251062,6675
,6676,rubredoxin (V44I)reduced state,251062,6675
,6677,rubredoxin (V44L) oxidized state,251062,6675
,6678,rubredoxin (V44L) reduced state,251062,6675
,6659,wild-type rubredoxin oxidized state,251078,6676
,6660,ubredoxin (V8A) oxidized state,251078,6676
,6661,ubredoxin (V8A) reduced state,251078,6676
,6662,wild-type rubredoxin reduced state,251078,6676
,6663,rubredoxin (V8G) oxidized state,251078,6676
,6664,ubredoxin (V8G) reduced state,251078,6676
,6665,ubredoxin (V8G/V44G) oxidized state,251078,6676
,6666,ubredoxin (V8G/V44G) reduced state,251078,6676
,6667,ubredoxin (V8I) oxidized state,251078,6676
,6668,ubredoxin (V8I) reduced state,251078,6676
,6669,ubredoxin (V8L) oxidized state,251078,6676
,6670,ubredoxin (V8L) reduced state,251078,6676
,6671,rubredoxin (V44A) oxidized state,251078,6676
,6672,rubredoxin (V44A) reduced state,251078,6676
,6673,rubredoxin (V44G) oxidized state,251078,6676
,6674,rubredoxin (V44G) reduced state,251078,6676
,6675,rubredoxin (V44I) oxidized state,251078,6676
,6677,rubredoxin (V44L) oxidized state,251078,6676
,6678,rubredoxin (V44L) reduced state,251078,6676
,6659,wild-type rubredoxin oxidized state,251094,6677
,6660,ubredoxin (V8A) oxidized state,251094,6677
,6661,ubredoxin (V8A) reduced state,251094,6677
,6662,wild-type rubredoxin reduced state,251094,6677
,6663,rubredoxin (V8G) oxidized state,251094,6677
,6664,ubredoxin (V8G) reduced state,251094,6677
,6665,ubredoxin (V8G/V44G) oxidized state,251094,6677
,6666,ubredoxin (V8G/V44G) reduced state,251094,6677
,6667,ubredoxin (V8I) oxidized state,251094,6677
,6668,ubredoxin (V8I) reduced state,251094,6677
,6669,ubredoxin (V8L) oxidized state,251094,6677
,6670,ubredoxin (V8L) reduced state,251094,6677
,6671,rubredoxin (V44A) oxidized state,251094,6677
,6672,rubredoxin (V44A) reduced state,251094,6677
,6673,rubredoxin (V44G) oxidized state,251094,6677
,6674,rubredoxin (V44G) reduced state,251094,6677
,6675,rubredoxin (V44I) oxidized state,251094,6677
,6676,rubredoxin (V44I)reduced state,251094,6677
,6678,rubredoxin (V44L) reduced state,251094,6677
BMRB,6659,wild-type rubredoxin oxidized state,251110,6678
BMRB,6660,ubredoxin (V8A) oxidized state,251110,6678
BMRB,6661,ubredoxin (V8A) reduced state,251110,6678
BMRB,6662,wild-type rubredoxin reduced state,251110,6678
BMRB,6663,rubredoxin (V8G) oxidized state,251110,6678
BMRB,6664,ubredoxin (V8G) reduced state,251110,6678
BMRB,6665,ubredoxin (V8G/V44G) oxidized state,251110,6678
BMRB,6666,ubredoxin (V8G/V44G) reduced state,251110,6678
BMRB,6667,ubredoxin (V8I) oxidized state,251110,6678
BMRB,6668,ubredoxin (V8I) reduced state,251110,6678
BMRB,6669,ubredoxin (V8L) oxidized state,251110,6678
BMRB,6670,ubredoxin (V8L) reduced state,251110,6678
BMRB,6671,rubredoxin (V44A) oxidized state,251110,6678
BMRB,6672,rubredoxin (V44A) reduced state,251110,6678
BMRB,6673,rubredoxin (V44G) oxidized state,251110,6678
BMRB,6674,rubredoxin (V44G) reduced state,251110,6678
BMRB,6675,rubredoxin (V44I) oxidized state,251110,6678
BMRB,6676,rubredoxin (V44I)reduced state,251110,6678
BMRB,6677,rubredoxin (V44L) oxidized state,251110,6678
PDB,2BN5,BMRB Entry Tracking System,251351,6690
,6690,PSI AB complex with U1-70k proline-rich peptide,251384,6691
PDB,2BUN,BMRB Entry Tracking System,251414,6692
BMRB,6697,Tm 3+ substitute,251555,6699
BMRB,7015,Complex with Ca ion,251620,6707
,15280,oxidized form (Cys36-Cys39) of the N-terminal domain of PilB,251644,6709
PDB,1Z8S,BMRB Entry Tracking System,251761,6716
PDB,1ZV6,BMRB Entry Tracking System,251816,6718
PDB,1ZLC,BMRB Entry Tracking System,251884,6720
PDB,1ZXF,BMRB Entry Tracking System,252004,6726
PDB,2GKD,BMRB Entry Tracking System,252004,6726
PDB,2L65,BMRB Entry Tracking System,252004,6726
,5590,homolog,252020,6727
PDB,2E2F,BMRB Entry Tracking System,252050,6729
PDB,2AAV,BMRB Entry Tracking System,252082,6730
PDB,2BW2,BMRB Entry Tracking System,252092,6731
BMRB,6733,derCD23 complex with Ca,252106,6732
BMRB,6734,derCD23 complex with CD21,252106,6732
BMRB,6735,derCD23 complex with IgE,252106,6732
BMRB,6732,derCD23,252123,6733
BMRB,6734,derCD23 complex with CD21,252123,6733
BMRB,6735,derCD23 complex with IgE,252123,6733
BMRB,6732,derCD23,252136,6734
BMRB,6733,derCD23 complex with Ca,252136,6734
BMRB,6735,derCD23 complex with IgE,252136,6734
BMRB,6732,derCD23,252150,6735
BMRB,6733,derCD23 complex with Ca,252150,6735
BMRB,6734,derCD23 complex with CD21,252150,6735
PDB,2AGA,BMRB Entry Tracking System,252292,6742
,6241,indepdent assignments for same protein,252292,6742
PDB,2ADL,BMRB Entry Tracking System,252305,6743
PDB,2ADN,BMRB Entry Tracking System,252305,6743
,5959,NMR Assignments of Ki67FHA in a free form,252406,6748
PDB,2AGH,BMRB Entry Tracking System,252434,6750
PDB,2AFD,BMRB Entry Tracking System,252446,6751
PDB,2AFE,BMRB Entry Tracking System,252446,6751
PDB,1Z87,BMRB Entry Tracking System,252462,6752
PDB,2ADZ,BMRB Entry Tracking System,252476,6753
PDB,2ABY,BMRB Entry Tracking System,252503,6755
,5962,NMR data of the solution structure of domain 5 of ai5(gamma),252516,6756
PDB,2NPU,BMRB Entry Tracking System,252623,6760
PDB,2AL3,BMRB Entry Tracking System,252642,6761
PDB,2HST,BMRB Entry Tracking System,252688,6763
PDB,2AKL,BMRB Entry Tracking System,252708,6766
PDB,2A63,BMRB Entry Tracking System,252780,6771
PDB,2AP7,BMRB Entry Tracking System,252809,6774
,6775,mutant that contains D-ILE at position 2,252809,6774
PDB,2AP8,BMRB Entry Tracking System,252822,6775
,6774,all natural amino acid,252822,6775
PDB,2BZT,BMRB Entry Tracking System,252835,6776
BMRB,6629,FimD(25-139),252907,6779
PDB,2AQE,BMRB Entry Tracking System,252937,6781
PDB,2AQF,BMRB Entry Tracking System,252937,6781
,6788,data appears on same publication,253008,6784
PDB,2IEM,BMRB Entry Tracking System,253066,6786
BMRB,4360,C2B domain rabphilin,253088,6787
,6784,data appears on same publication,253104,6788
BMRB,7016,Complex with 1 Ca ion,253129,6789
BMRB,7017,Complex with 2 Ca ion,253129,6789
BMRB,5990,Structure for AST5 calculated at different concentration of SDS,253187,6791
BMRB,6792,Dippu Allatostatin 8,253187,6791
BMRB,5990,Structure for AST5 calculated at different concentration of SDS,253204,6792
BMRB,5991,Structures of Allatostatin Family Members AST5 and AST8 from 2D NMR Data,253204,6792
PDB,2C34,BMRB Entry Tracking System,253233,6794
PDB,2PXG,BMRB Entry Tracking System,253279,6797
BMRB,7018,CaM-Cys-CaMKI complex,253294,6798
PDB,2AWT,BMRB Entry Tracking System,253350,6801
BMRB,7028,CaM-WFF,253376,6802
BMRB,7029,CaM-FFF,253376,6802
BMRB,7030,CaM-FFW,253376,6802
BMRB,7031,CaM-WF10,253376,6802
PDB,2D1U,BMRB Entry Tracking System,253390,6803
PDB,2K1X,BMRB Entry Tracking System,253390,6803
PDB,2B88,BMRB Entry Tracking System,253402,6804
PDB,2K1W,BMRB Entry Tracking System,253402,6804
,6805,antiZtaq,253402,6804
,6806,Ztaq:anti-Ztaq,253402,6804
PDB,2B89,BMRB Entry Tracking System,253419,6805
,6804,Ztaq,253419,6805
,6806,Ztaq:anti-Ztaq,253419,6805
PDB,2B87,BMRB Entry Tracking System,253436,6806
BMRB,6804,Ztaq,253436,6806
BMRB,6805,anti-Ztaq,253436,6806
,4797,NMR structure of full length Equinatoxin II,253471,6808
PDB,2FFK,BMRB Entry Tracking System,253484,6809
PDB,2FIN,BMRB Entry Tracking System,253484,6809
PDB,2AYX,BMRB Entry Tracking System,253499,6810
PDB,2AU4,BMRB Entry Tracking System,253568,6814
PDB,2ATG,BMRB Entry Tracking System,253599,6815
PDB,2AK0,BMRB Entry Tracking System,253641,6817
PDB,2AJW,BMRB Entry Tracking System,253662,6818
PDB,2AMI,BMRB Entry Tracking System,253692,6820
,5659,Apo form,253775,6823
PDB,2FY9,BMRB Entry Tracking System,253846,6826
,4281,Sequence and structurally homologous proteins,253846,6826
BMRB,6831,CaM-cNOS,253933,6830
BMRB,6830,CaM,253947,6831
,6935,lipase WT,253963,6832
BMRB,6828,Entry containing apo-MazF(E24A) backbone assignment,253987,6833
PDB,2AMN,BMRB Entry Tracking System,254042,6835
BMRB,6024,"Another class A beta-lactamase, TEM-1 E28G",254103,6838
BMRB,6357,"Another class A beta-lactamase, TEM-1",254103,6838
,6608,Chemical shifts in the absence of DPC micelles,254160,6839
PDB,2B1U,BMRB Entry Tracking System,254194,6841
PDB,2AYM,BMRB Entry Tracking System,254243,6844
BMRB,6846,Nop10 from Saccharomyces cerevisiae,254263,6845
BMRB,6845,Nop10 from Methanocaldococcus jannaschii,254288,6846
,6603,assignment for the reduced state,254311,6847
PDB,2B68,BMRB Entry Tracking System,254324,6849
PDB,2B7E,BMRB Entry Tracking System,254338,6850
PDB,2AIZ,BMRB Entry Tracking System,254429,6856
,6465,Chemical shifts of Pal,254429,6856
,6858,Chemical shifts of Pal bound to PG-P,254429,6856
PDB,2AIZ,BMRB Entry Tracking System,254472,6858
,6465,Chemical shifts of Pal,254472,6858
,6856,Chemical shifts of free PG-P,254472,6858
,6616,"chemical shifts from P5, peptide based on trialysin",254491,6859
,6618,"chemical shifts from P6, peptide based on trialysin",254491,6859
,6619,"chemical shifts from P7, peptide based on trialysin",254491,6859
,6862,calcium bound calmodulin N-terminal domain,254538,6861
,6861,apo calmodulin N-terminal domain,254553,6862
PDB,2BAI,BMRB Entry Tracking System,254570,6863
PDB,2B38,BMRB Entry Tracking System,254744,6872
PDB,2FO8,BMRB Entry Tracking System,254830,6876
,5952,HPV-16 E2C free form,254851,6877
BMRB,5272,1H chemical shift assignments for Schistocerca gregaria chymotrypsin inhibitor,254902,6880
BMRB,5273,"1H chemical shift assignments for SGCI[L30R, K31M]",254902,6880
BMRB,5274,1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor,254902,6880
BMRB,6881,1H and 15N chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor complexed with bovine chymotrypsin,254902,6880
BMRB,5272,1H chemical shift assignments for Schistocerca gregaria chymotrypsin inhibitor,254919,6881
BMRB,5273,"1H chemical shift assignments for SGCI[L30R, K31M]",254919,6881
BMRB,5274,1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor,254919,6881
BMRB,6880,1H and 15N chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor at pH=6.0,254919,6881
PDB,2ERS,BMRB Entry Tracking System,254948,6882
PDB,2FHM,BMRB Entry Tracking System,254987,6884
PDB,2CKN,BMRB Entry Tracking System,255002,6885
PDB,2G0K,BMRB Entry Tracking System,255030,6888
PDB,2G0L,BMRB Entry Tracking System,255030,6888
,5343,Neocarzinostatin Apo-Protein,255030,6888
,5344,Apo-Protein Bound to a Synthetic Chromophore,255030,6888
,6889,Apo-Protein,255030,6888
PDB,2ESY,BMRB Entry Tracking System,255106,6892
BMRB,6897,"Alpha-conotoxin ImI, [Sec2,8]-ImI",255192,6896
PDB,2BC8,BMRB Entry Tracking System,255192,6896
BMRB,6896,"Alpha-conotoxin ImI, [Sec2,3,8,12]-ImI",255211,6897
PDB,2BC7,BMRB Entry Tracking System,255211,6897
BMRB,5457,chemical shift data of Mad1-complex,255250,6899
BMRB,5808,relaxation data of MAd1-complex,255250,6899
BMRB,6904,holo form,255328,6903
BMRB,15918,M-crystallin (calcium bound form) in presence of 4 M Gdn-Hcl,255344,6904
BMRB,15934,M-crystallin (calcium bound form) in presence of 6 M Gdn-Hcl,255344,6904
BMRB,6903,apo form,255344,6904
,6648,Structural isoform of the current wild type protein shown to be suitable for structure calculations,255364,6905
,6653,The first zinc finger and with the interfinger linker of the current wild type protein,255364,6905
PDB,2F3V,BMRB Entry Tracking System,255396,6907
,5536,G88W110 fragment of Staphylococcal Nuclease,255396,6907
,6908,SNase110 fragment of Staphylococcal Nuclease,255396,6907
PDB,2F3W,BMRB Entry Tracking System,255409,6908
,5536,G88W110 fragment of Staphylococcal Nuclease,255409,6908
,6907,V66W110 fragment of staphylococcal nuclease,255409,6908
PDB,2FE0,BMRB Entry Tracking System,255438,6910
PDB,2I9H,BMRB Entry Tracking System,255469,6912
,6913,thioredoxin 2,255469,6912
,6912,thioredoxin 1,255483,6913
PDB,2LA1,BMRB Entry Tracking System,255514,6915
PDB,2CH0,BMRB Entry Tracking System,255579,6919
BMRB,1324,proton assignement of the backbone,255609,6921
BMRB,295,proton assignment of cyt b5,255609,6921
PDB,2I96,BMRB Entry Tracking System,255609,6921
PDB,2MF9,BMRB Entry Tracking System,255638,6923
PDB,2AXK,BMRB Entry Tracking System,255653,6924
PDB,2C06,BMRB Entry Tracking System,255670,6925
,7071,entry containing NMR chemical shift data of Kis antitoxin that forms toxin-antitoxin system with Kid toxin,255670,6925
PDB,2FFT,BMRB Entry Tracking System,255682,6926
PDB,2G5M,BMRB Entry Tracking System,255694,6927
,15180,Spinophilin_PP1_binding_domain,255694,6927
,6933,protein isoform (Neurabin PDZ),255694,6927
PDB,2FGX,BMRB Entry Tracking System,255725,6929
,6844,Assignment of SNF RBD2,255747,6930
,6927,protein isoform,255773,6933
,7118,Neurabin SAM domain monomer,255773,6933
,6832,mutant,255806,6935
PDB,2M9B,BMRB Entry Tracking System,255901,6942
PDB,2JNT,BMRB Entry Tracking System,255915,6943
PDB,2FS1,BMRB Entry Tracking System,255946,6945
PDB,2LKC,BMRB Entry Tracking System,255959,6946
BMRB,6948,assignment of monomeric Fur,255977,6947
,6947,assignment of dimeric Fur,255997,6948
PDB,2DCI,BMRB Entry Tracking System,256099,6954
PDB,2D82,BMRB Entry Tracking System,256169,6960
PDB,2FVE,BMRB Entry Tracking System,256187,6962
PDB,2DDI,BMRB Entry Tracking System,256211,6963
PDB,2DDJ,BMRB Entry Tracking System,256211,6963
PDB,2FVT,BMRB Entry Tracking System,256225,6964
BMRB,5819,same protein in reduced state,256240,6965
BMRB,6967,same protein in oxidized state,256261,6966
BMRB,6966,same protein in reduced state,256278,6967
PDB,2FXP,BMRB Entry Tracking System,256311,6969
BMRB,6974,human p23(1-160),256370,6973
,6973,human p23(1-119),256384,6974
PDB,2F8U,BMRB Entry Tracking System,256398,6975
PDB,2G2B,BMRB Entry Tracking System,256450,6980
PDB,2G0U,BMRB Entry Tracking System,256466,6981
BMRB,6987,Heme-heme oxygenase-cyanide complex,256496,6983
PDB,2GJY,BMRB Entry Tracking System,256549,6986
BMRB,6983,heme-heme oxygenase-azide complex,256565,6987
PDB,2DEN,BMRB Entry Tracking System,256583,6988
BMRB,6993,Double phosphorylated variant of Tissue Factor Cytoplasmic Domain,256643,6991
BMRB,6996,Single 253 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256643,6991
BMRB,6998,Single 258 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256643,6991
BMRB,6991,unphosphorylated varian of Tissue Factor Cytoplasmic Domain,256680,6993
BMRB,6996,Single 253 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256680,6993
BMRB,6998,Single 258 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256680,6993
BMRB,7118,Neurabin SAM domain monomer,256680,6993
PDB,2LKD,BMRB Entry Tracking System,256696,6995
,6946,chemical shifts of a free IF2G2,256696,6995
BMRB,6991,unphosphorylated varian of Tissue Factor Cytoplasmic Domain,256716,6996
BMRB,6993,Double Phosphorylated Tissue Factor Cytoplasmic Domain,256716,6996
BMRB,6998,Single 258 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256716,6996
PDB,2G46,BMRB Entry Tracking System,256732,6997
BMRB,6991,unphosphorylated varian of Tissue Factor Cytoplasmic Domain,256751,6998
BMRB,6993,Double Phosphorylated Tissue Factor Cytoplasmic Domain,256751,6998
BMRB,6996,Single 253 phosphorylated variant of Tissue Factor Cytoplasmic Domain,256751,6998
PDB,2A7Y,BMRB Entry Tracking System,256808,7000
PDB,2G3Q,BMRB Entry Tracking System,256839,7002
PDB,2DF0,BMRB Entry Tracking System,256876,7005
PDB,2DEZ,BMRB Entry Tracking System,256898,7006
BMRB,7009,Ca-exchanger (NCX1),256942,7008
PDB,2FWU,BMRB Entry Tracking System,256942,7008
BMRB,7008,Ca-exchanger (NCX1),256964,7009
PDB,2FWS,BMRB Entry Tracking System,256964,7009
PDB,2FLG,BMRB Entry Tracking System,256986,7010
BMRB,7012,55-72 segment of staphylococcal nuclease,257005,7011
PDB,2FXZ,BMRB Entry Tracking System,257005,7011
BMRB,7011,13-mer peptide (97-109) segment of staphylococcal nuclease,257026,7012
PDB,2FXY,BMRB Entry Tracking System,257026,7012
PDB,2GDT,BMRB Entry Tracking System,257062,7014
BMRB,6707,Apo form,257075,7015
BMRB,6789,apo form,257100,7016
BMRB,7017,Complex with 2 Ca ion,257100,7016
BMRB,6789,apo form,257120,7017
BMRB,7016,Complex with 1 Ca ion,257120,7017
BMRB,6798,CaM-CaMKI complex,257138,7018
BMRB,6334,FKBB domain of LpMip,257182,7021
,6809,unliganded vCCI,257262,7024
BMRB,6802,CaM,257303,7028
BMRB,7029,CaM-FFF,257303,7028
BMRB,7030,CaM-FFW,257303,7028
BMRB,7031,CaM-WF10,257303,7028
BMRB,6802,CaM,257318,7029
BMRB,7028,CaM-WFF,257318,7029
BMRB,7030,CaM-FFW,257318,7029
BMRB,7031,CaM-WF10,257318,7029
BMRB,6802,CaM,257333,7030
BMRB,7028,CaM-WFF,257333,7030
BMRB,7029,CaM-FFF,257333,7030
BMRB,7031,CaM-WF10,257333,7030
BMRB,6802,CaM,257348,7031
BMRB,7028,CaM-WFF,257348,7031
BMRB,7029,CaM-FFF,257348,7031
BMRB,7030,CaM-FFW,257348,7031
PDB,3THK,BMRB Entry Tracking System,257390,7033
PDB,2FRW,BMRB Entry Tracking System,257434,7035
,5765,,257484,7049
PDB,2DJC,BMRB Entry Tracking System,257526,7051
PDB,2DK9,BMRB Entry Tracking System,257639,7058
PDB,2G35,BMRB Entry Tracking System,257717,7061
PDB,2G7J,BMRB Entry Tracking System,257735,7063
PDB,2GJ0,BMRB Entry Tracking System,257769,7064
PDB,2G9L,BMRB Entry Tracking System,257787,7065
PDB,2G31,BMRB Entry Tracking System,257833,7067
BMRB,7069,Copper-transporting ATPase 1 (E.C.3.6.3.4),257850,7068
PDB,2GA7,BMRB Entry Tracking System,257850,7068
BMRB,7068,Copper-transporting ATPase 1 (E.C.3.6.3.4) CU_1,257880,7069
PDB,2G9O,BMRB Entry Tracking System,257880,7069
,6925,entry containing NMR chemical shift data of Kid toxin that forms toxin-antitoxin system with Kis antitoxin,257938,7071
PDB,2GPF,BMRB Entry Tracking System,258027,7075
PDB,2AIH,BMRB Entry Tracking System,258053,7078
PDB,2G9J,BMRB Entry Tracking System,258084,7080
,4133,Unbound N-terminal model molecule with Gly replaceing the N-terminal Acetyl group,258084,7080
,5610,Unbound C-terminal model molecule,258084,7080
PDB,2GRG,BMRB Entry Tracking System,258205,7085
PDB,2H0P,BMRB Entry Tracking System,258264,7087
,4697,assignment of C-terminal domain,258278,7088
,6577,assignment of N-terminal domain,258278,7088
PDB,2POJ,BMRB Entry Tracking System,258299,7089
,6391,with inhibitor,258299,7089
,6444,with inhibitor,258299,7089
PDB,2GL1,BMRB Entry Tracking System,258344,7092
PDB,2GTV,BMRB Entry Tracking System,258359,7093
PDB,2GOW,BMRB Entry Tracking System,258390,7095
BMRB,7134,protein brkDBD in free form,258413,7097
PDB,2GLO,BMRB Entry Tracking System,258413,7097
PDB,2GM0,BMRB Entry Tracking System,258436,7098
PDB,2GJI,BMRB Entry Tracking System,258464,7099
PDB,2GJH,BMRB Entry Tracking System,258486,7101
PDB,2GJF,BMRB Entry Tracking System,258506,7102
PDB,2HJI,BMRB Entry Tracking System,258526,7103
,4313,mutant,258526,7103
PDB,2GZY,BMRB Entry Tracking System,258605,7108
,15028,Trx-ArsC complex,258605,7108
,7109,TrxA monomer (oxidized form),258605,7108
PDB,2GZZ,BMRB Entry Tracking System,258618,7109
,15028,Trx-ArsC complex,258618,7109
,7108,TrxA monomer (reduced form),258618,7109
BMRB,5387,"liquid state NMR 1H, 13C and 15N data (in micelles)",258651,7111
BMRB,68,liquid state NMR 1H data,258651,7111
PDB,2JZZ,BMRB Entry Tracking System,258651,7111
PDB,2HWT,BMRB Entry Tracking System,258665,7112
PDB,2H25,BMRB Entry Tracking System,258700,7114
,5712,"human eIF4E in complex with 7-methylguanosine diphosphate and a 17-amino acid
peptide derived from human eIF4GII",258715,7115
PDB,2GLW,BMRB Entry Tracking System,258729,7116
PDB,2H1Z,BMRB Entry Tracking System,258749,7117
,6933,PDZ domain from same protein,258762,7118
PDB,2GYT,BMRB Entry Tracking System,258799,7120
PDB,2DO8,BMRB Entry Tracking System,258819,7121
PDB,2G7H,BMRB Entry Tracking System,258839,7122
PDB,2DQ5,BMRB Entry Tracking System,258872,7124
BMRB,4964,chemical shifts of free barnase,258904,7126
BMRB,6227,chemical shifts of free barstar,258904,7126
BMRB,7139,relaxation data of free barnase,258904,7126
,7128,1F3-2F3 complex,258939,7127
PDB,2HA1,BMRB Entry Tracking System,258957,7128
,7127,Entry contains complete chemical shift assignments for 2F3,258957,7128
PDB,2GGR,BMRB Entry Tracking System,258976,7129
,7133,interacting protein CheA P4 domain,259023,7132
,7132,"interacting protein, CheA P1 domain",259036,7133
BMRB,7097,protein brkDBD in complex form with DNA,259049,7134
,7136,2SSbeta,259065,7135
,7135,2SS(alpha),259079,7136
PDB,2H7T,BMRB Entry Tracking System,259093,7137
BMRB,4964,chemical shifts of free barnase,259109,7139
BMRB,6227,chemical shifts of free barstar,259109,7139
BMRB,7126,complex of barnase and barstar,259109,7139
BMRB,7141,Csk with Cbp,259142,7140
,7140,Csk,259154,7141
,7143,"HEWL, complex form with chitosan",259180,7144
PDB,2H7B,BMRB Entry Tracking System,259191,7147
PDB,2H7D,BMRB Entry Tracking System,259219,7150
PDB,2H7E,BMRB Entry Tracking System,259219,7150
PDB,2H80,BMRB Entry Tracking System,259241,7151
,7155,helix G (lys 124-137),259284,7154
,7156,helix H (lys 136-157),259284,7154
,7157,helix F (lys 113-125),259284,7154
,7154,helix E (lys 92-107),259298,7155
,7156,helix H (lys 136-157),259298,7155
,7157,helix F (lys 113-125),259298,7155
,7154,helix E (lys 92-107),259311,7156
,7155,helix G (lys 124-137),259311,7156
,7157,helix F (lys 113-125),259311,7156
,7154,helix E (lys 92-107),259327,7157
,7155,helix G (lys 124-137),259327,7157
,7156,helix H (lys 136-157),259327,7157
BMRB,5669,A similar zinc finger that binds ubiquitin,259344,7158
PDB,2H9X,BMRB Entry Tracking System,259436,7166
PDB,2I3E,BMRB Entry Tracking System,259450,7167
,5202,rat CNPase,259450,7167
,7169,Dynorphin B in Bicelles,259466,7168
,7168,Dynorphin A in Bicelles,259482,7169
PDB,2HC5,BMRB Entry Tracking System,259497,7170
,7171,isopeptide,259545,7173
PDB,2H8S,BMRB Entry Tracking System,259600,7177
PDB,2GZP,BMRB Entry Tracking System,259618,7178
PDB,2GZO,BMRB Entry Tracking System,259657,7180
PDB,2H3J,BMRB Entry Tracking System,259676,7181
PDB,2H7A,BMRB Entry Tracking System,259696,7182
PDB,2GVS,BMRB Entry Tracking System,259715,7184
PDB,2GUT,BMRB Entry Tracking System,259733,7185
PDB,2GX1,BMRB Entry Tracking System,259749,7186
,7197,DHFR-Bdm6 complex,259912,7196
,7198,DHFR-Bdm4 complex,259912,7196
,7199,"DHFR-Bdm4,6 complex",259912,7196
,7200,DHFR-TMP complex,259912,7196
,7196,DHFR-MTX complex,259928,7199
,7197,DHFR-Bdm6 complex,259928,7199
,7198,DHFR-Bdm4 complex,259928,7199
,7200,DHFR-TMP complex,259928,7199
PDB,2HJQ,BMRB Entry Tracking System,259960,7201
PDB,2LCX,BMRB Entry Tracking System,260049,7205
PDB,2I85,BMRB Entry Tracking System,260409,7220
BMRB,6392,Link_TSG6 free form,260430,7221
BMRB,6393,Complex form with HA octasaccharide,260430,7221
BMRB,7222,Link_TSG6 free form,260430,7221
BMRB,6392,Link_TSG6 free form,260479,7222
BMRB,6393,Complex form with HA octasaccharide,260479,7222
BMRB,7221,Link_TSG6 and hyaluronan octasaccharide complex,260479,7222
PDB,2HJ8,BMRB Entry Tracking System,260514,7223
PDB,2HG7,BMRB Entry Tracking System,260547,7224
PDB,2HEP,BMRB Entry Tracking System,260571,7225
PDB,2HFI,BMRB Entry Tracking System,260631,7227
PDB,2HI6,BMRB Entry Tracking System,260658,7228
PDB,2HDL,BMRB Entry Tracking System,260682,7229
PDB,2H49,BMRB Entry Tracking System,260705,7230
BMRB,7233,The same peptide containing cis instead of trans-4-aminomethylphenylazobenzoic acid,260747,7232
PDB,2H3T,BMRB Entry Tracking System,260747,7232
BMRB,7232,The same peptide containing trans instead of cis-4-aminomethylphenylazobenzoic acid,260769,7233
PDB,2H3S,BMRB Entry Tracking System,260769,7233
PDB,2H4B,BMRB Entry Tracking System,260769,7233
,7235,open form,260798,7234
,7234,ternary complex with glucose-6-phosphate and MgF3-,260827,7235
,6024,"TEM-1 beta-lactamase, E28G mutant",260851,7236
,6357,"TEM-1 beta-lactamase, wild type",260851,7236
,7237,"TEM-1 beta-lactamase, mutant Y105G",260851,7236
,7238,"TEM-1 beta-lactamase, mutant Y105N",260851,7236
,7239,"TEM-1 beta-lactamase, mutant Y105D",260851,7236
,6024,"TEM-1 beta-lactamase, E28G mutant",260871,7237
,6357,"TEM-1 beta-lactamase, wild type",260871,7237
,7236,"TEM-1 beta-lactamase, mutant Y105W",260871,7237
,7238,"TEM-1 beta-lactamase, mutant Y105N",260871,7237
,7239,"TEM-1 beta-lactamase, mutant Y105D",260871,7237
,6024,"TEM-1 beta-lactamase, E28G mutant",260891,7238
,6357,"TEM-1 beta-lactamase, wild type",260891,7238
,7236,"TEM-1 beta-lactamase, mutant Y105W",260891,7238
,7237,"TEM-1 beta-lactamase, mutant Y105G",260891,7238
,7239,"TEM-1 beta-lactamase, mutant Y105D",260891,7238
,6024,"TEM-1 beta-lactamase, E28G mutant",260911,7239
,6357,"TEM-1 beta-lactamase, wild type",260911,7239
,7236,"TEM-1 beta-lactamase, mutant Y105W",260911,7239
,7237,"TEM-1 beta-lactamase, mutant Y105G",260911,7239
,7238,"TEM-1 beta-lactamase, mutant Y105N",260911,7239
PDB,2HUG,BMRB Entry Tracking System,260960,7241
,6592,Chromo 2 domain in free form,260960,7241
PDB,2IZ4,BMRB Entry Tracking System,261003,7243
,7304,proton shifts of the protein from natural source,261003,7243
,7267,"complex form with d-C8-PI(4,5)P2",261156,7250
,7275,"complex form with d-C4-PI(4,5)P2",261156,7250
PDB,2J0Z,BMRB Entry Tracking System,261175,7251
,7252,p53 tetramerization domain (mutant T329F Q331K),261175,7251
,7253,p53 tetramerization domain (mutant T329V Q331K),261175,7251
,7254,p53 tetramerization domain (mutant Y327S T329G Q331G),261175,7251
,7255,p53 tetramerization domain (mutant Y327S T329E Q331G),261175,7251
PDB,2J10,BMRB Entry Tracking System,261193,7252
PDB,2J11,BMRB Entry Tracking System,261193,7252
,7251,wild type p53 tetramerization domain,261193,7252
,7253,p53 tetramerization domain (mutant T329V Q331K),261193,7252
,7254,p53 tetramerization domain (mutant Y327S T329G Q331G),261193,7252
,7255,p53 tetramerization domain (mutant Y327S T329E Q331G),261193,7252
,7251,wild type p53 tetramerization domain,261211,7253
,7252,p53 tetramerization domain (mutant T329F Q331K),261211,7253
,7254,p53 tetramerization domain (mutant Y327S T329G Q331G),261211,7253
,7255,p53 tetramerization domain (mutant Y327S T329E Q331G),261211,7253
,7251,wild type p53 tetramerization domain,261229,7254
,7252,p53 tetramerization domain (mutant T329F Q331K),261229,7254
,7253,p53 tetramerization domain (mutant T329V Q331K),261229,7254
,7255,p53 tetramerization domain (mutant Y327S T329E Q331G),261229,7254
,7251,wild type p53 tetramerization domain,261247,7255
,7252,p53 tetramerization domain (mutant T329F Q331K),261247,7255
,7253,p53 tetramerization domain (mutant T329V Q331K),261247,7255
,7254,p53 tetramerization domain (mutant Y327S T329G Q331G),261247,7255
PDB,2HFD,BMRB Entry Tracking System,261264,7256
PDB,2HVZ,BMRB Entry Tracking System,261290,7257
BMRB,7289,Protein PB1-F2 (1-40),261311,7258
BMRB,7290,Protein PB1-F2 (30-70),261311,7258
PDB,2HN8,BMRB Entry Tracking System,261311,7258
PDB,2HTF,BMRB Entry Tracking System,261327,7259
PDB,2HGC,BMRB Entry Tracking System,261347,7260
PDB,2HJJ,BMRB Entry Tracking System,261386,7261
PDB,2JM2,BMRB Entry Tracking System,261418,7262
PDB,2I1P,BMRB Entry Tracking System,261439,7263
,7265,"covalently-inhibited beta-1,4-glycosidase Cex",261458,7264
PDB,2HFQ,BMRB Entry Tracking System,261480,7266
PDB,2V37,BMRB Entry Tracking System,261505,7268
PDB,2JNK,BMRB Entry Tracking System,261519,7269
PDB,2O4E,BMRB Entry Tracking System,261533,7270
PDB,2NNZ,BMRB Entry Tracking System,261546,7271
PDB,2I59,BMRB Entry Tracking System,261570,7272
PDB,2I1T,BMRB Entry Tracking System,261598,7273
PDB,2HH8,BMRB Entry Tracking System,261613,7274
PDB,2MEY,BMRB Entry Tracking System,261655,7276
,5918,non-mutant protein,261702,7277
,7278,iG80b ecRNH,261702,7277
,5918,non-mutant protein,261716,7278
,7277,dG85 ttRNH,261716,7278
BMRB,1639,related protein,261746,7280
BMRB,5875,related protein,261746,7280
PDB,2I9M,BMRB Entry Tracking System,261782,7282
,7283,MHB4A,261782,7282
,7284,MHB8A,261782,7282
PDB,2I9N,BMRB Entry Tracking System,261797,7283
,7282,MHA6,261797,7283
,7284,MHB8A,261797,7283
PDB,2I9O,BMRB Entry Tracking System,261811,7284
,7282,MHA6,261811,7284
,7283,MHB4A,261811,7284
PDB,2J4M,BMRB Entry Tracking System,261826,7285
PDB,2J4N,BMRB Entry Tracking System,261826,7285
,3322,first domain from this protein,261826,7285
PDB,2I7K,BMRB Entry Tracking System,261881,7287
PDB,2J5D,BMRB Entry Tracking System,261908,7288
BMRB,7258,NMR data of the C-terminal fragment PB(50-87) of the PB1-F2 protein,261931,7289
BMRB,7290,NMR data of the central fragment PB(30-70) of the PB1-F2 protein,261931,7289
BMRB,7258,NMR data of the C-terminal fragment PB(50-87) of the PB1-F2 protein,261948,7290
BMRB,7289,NMR data of the N-terminal fragment PB(1-40) of the PB1-F2 protein,261948,7290
PDB,2NPL,BMRB Entry Tracking System,261965,7291
PDB,2I94,BMRB Entry Tracking System,262010,7293
PDB,2IGZ,BMRB Entry Tracking System,262032,7294
,7295,Entry containing chemical shift assignments for the synthetic Cyclo Peptide (SCP),262032,7294
BMRB,7294,Entry containing chemical shift assignments for the bacillomycin Lc,262058,7295
PDB,2IGZ,BMRB Entry Tracking System,262058,7295
PDB,2I8F,BMRB Entry Tracking System,262083,7296
,4960,M61H mutant of PZ cyt c-551,262083,7296
PDB,2IDA,BMRB Entry Tracking System,262104,7297
PDB,2I50,BMRB Entry Tracking System,262130,7298
PDB,2J5H,BMRB Entry Tracking System,262155,7299
PDB,2O3D,BMRB Entry Tracking System,262196,7301
PDB,2I4K,BMRB Entry Tracking System,262219,7302
,7243,chemical shifts of the protein from recombinant technology,262249,7304
PDB,2JM8,BMRB Entry Tracking System,262262,7305
,7306,R21A Spc-SH3 bound,262262,7305
PDB,2JM9,BMRB Entry Tracking System,262276,7306
PDB,2JMA,BMRB Entry Tracking System,262276,7306
BMRB,7305,R21A Spc-SH3 free,262276,7306
,4965,Free L11 of Thermus thermophilus,262292,7307
,5513,Free L11 of Thermotoga maritima,262292,7307
,7308,L11-RNA-thiostrepton complex,262292,7307
BMRB,4965,Free L11 of Thermus thermophilus,262310,7308
BMRB,5513,Free L11 of Thermotoga maritima,262310,7308
BMRB,7307,L11-RNA complex,262310,7308
BMRB,17065,Tandem ubiquitin binding domains of STAM1,262384,7312
PDB,2IUE,BMRB Entry Tracking System,262414,7313
PDB,2E34,BMRB Entry Tracking System,262443,7314
PDB,2E35,BMRB Entry Tracking System,262463,7315
PDB,2E36,BMRB Entry Tracking System,262463,7315
,7317,L53AI54A_variant_of_Im7*,262485,7316
,7318,YY_variant_of_Im7*,262485,7316
,7316,"colicin_E7_inhibitor_polypeptide,_Im7*",262503,7317
,7318,YY_variant_of_Im7*,262503,7317
,7316,"colicin_E7_inhibitor_polypeptide,_Im7*",262521,7318
,7317,L53AI54A_variant_of_Im7*,262521,7318
PDB,2ITA,BMRB Entry Tracking System,262559,7320
PDB,2NRG,BMRB Entry Tracking System,262559,7320
PDB,2NLN,BMRB Entry Tracking System,262592,7322
BMRB,4115,homologous Immunity protein Im9 bound to DNase domain of colicin E9,262606,7323
BMRB,4116,homologous Immunity protein Im9,262606,7323
BMRB,4293,DNase domain of non cognate binding partner E9,262606,7323
BMRB,4352,Im9 bound DNase domain of non cognate binding partner E9,262606,7323
PDB,2NO8,BMRB Entry Tracking System,262606,7323
PDB,2NPB,BMRB Entry Tracking System,262619,7324
PDB,2NSV,BMRB Entry Tracking System,262664,7326
PDB,2NSW,BMRB Entry Tracking System,262677,7327
PDB,2E0H,BMRB Entry Tracking System,262694,7330
PDB,2I9Y,BMRB Entry Tracking System,262711,7339
PDB,2J15,BMRB Entry Tracking System,262747,7341
PDB,2IWJ,BMRB Entry Tracking System,262762,7342
PDB,2C0S,BMRB Entry Tracking System,262780,7349
PDB,2BZB,BMRB Entry Tracking System,262796,7350
PDB,2BZE,BMRB Entry Tracking System,262812,7351
PDB,2BL6,BMRB Entry Tracking System,262828,7352
PDB,2BJC,BMRB Entry Tracking System,262846,7354
BMRB,15082,apo,262864,7356
BMRB,7355,Clofibric_acid bound,262864,7356
BMRB,7357,tolfenamic bound,262864,7356
BMRB,15082,apo,262880,7357
BMRB,7355,Clofibric_acid bound,262880,7357
BMRB,7356,fenofibricAcid bound,262880,7357
BMRB,7360,"DsbA oxidoreductase, reduced form",262909,7359
BMRB,7359,"DsbA oxidoreductase, oxidized form",262949,7360
PDB,2IJY,BMRB Entry Tracking System,262949,7360
PDB,2IT8,BMRB Entry Tracking System,262976,7361
PDB,2NWT,BMRB Entry Tracking System,262996,7362
PDB,2E5E,BMRB Entry Tracking System,263014,7364
PDB,2E45,BMRB Entry Tracking System,263030,7365
PDB,2NOC,BMRB Entry Tracking System,263048,7366
PDB,2NS4,BMRB Entry Tracking System,263068,7367
PDB,2OA4,BMRB Entry Tracking System,263102,7371
BMRB,15164,ATP7A (apo form),263124,7375
BMRB,15177,CzrA in apo form,263141,7376
BMRB,7377,CzrA in complex with DNA,263141,7376
PDB,1R1U,,263141,7376
PDB,1R1V,,263141,7376
PDB,2M30,BMRB Entry Tracking System,263141,7376
BMRB,15177,CzrA in apo form,263162,7377
BMRB,7376,CzrA in complex with Zinc ion,263162,7377
PDB,1R1U,,263162,7377
PDB,1R1V,,263162,7377
PDB,2OSR,BMRB Entry Tracking System,263203,7382
PDB,2OSQ,BMRB Entry Tracking System,263220,7383
PDB,2P81,BMRB Entry Tracking System,263240,7386
PDB,2P5J,BMRB Entry Tracking System,263275,7388
PDB,2P5H,BMRB Entry Tracking System,263290,7389
BMRB,15301,oxidized form,263306,7390
PDB,1AYF,,263306,7390
PDB,1YCC,,263306,7390
PDB,2JQR,BMRB Entry Tracking System,263306,7390
BMRB,15316,native protein,263334,7391
PDB,2Z2G,BMRB Entry Tracking System,263348,7392
PDB,2PP4,BMRB Entry Tracking System,263367,7396
PDB,2YYF,BMRB Entry Tracking System,263382,7397
BMRB,7400,rhodostomin P48A mutant,263385,7399
PDB,2PJG,BMRB Entry Tracking System,263385,7399
BMRB,7399,rhodostomin D51E mutant,263388,7400
PDB,2PJI,BMRB Entry Tracking System,263388,7400
PDB,2P6J,BMRB Entry Tracking System,263391,7401
PDB,2PCO,BMRB Entry Tracking System,263411,7402
BMRB,7404,U64 H/ACA snoRNA 3',263429,7403
BMRB,7405,U85 C/D-H/ACA,263429,7403
PDB,2QH2,BMRB Entry Tracking System,263429,7403
BMRB,7403,CR7,263432,7404
BMRB,7405,U85 C/D-H/ACA,263432,7404
PDB,2QH3,BMRB Entry Tracking System,263432,7404
PDB,2QH4,BMRB Entry Tracking System,263435,7405
BMRB,15461,ccc2 (free form),263438,7406
BMRB,15497,MxiD (simple form),263457,7407
BMRB,15502,HMGB1,263474,7408
BMRB,7409,"HMGB1, delta5",263474,7408
BMRB,7410,"HMGB1, delta10",263474,7408
BMRB,7411,"HMGB1, delta15",263474,7408
BMRB,7412,"HMGB1, delta20",263474,7408
BMRB,7413,"HMGB1, delta25",263474,7408
BMRB,15502,HMGB1,263489,7409
BMRB,7408,"HMGB1, ABprime",263489,7409
BMRB,7410,"HMGB1, delta10",263489,7409
BMRB,7411,"HMGB1, delta15",263489,7409
BMRB,7412,"HMGB1, delta20",263489,7409
BMRB,7413,"HMGB1, delta25",263489,7409
BMRB,15502,HMGB1,263504,7410
BMRB,7408,"HMGB1, ABprime",263504,7410
BMRB,7409,"HMGB1, delta5",263504,7410
BMRB,7411,"HMGB1, delta15",263504,7410
BMRB,7412,"HMGB1, delta20",263504,7410
BMRB,7413,"HMGB1, delta25",263504,7410
BMRB,15502,HMGB1,263519,7411
BMRB,7408,"HMGB1, ABprime",263519,7411
BMRB,7409,"HMGB1, delta5",263519,7411
BMRB,7410,"HMGB1, delta10",263519,7411
BMRB,7412,"HMGB1, delta20",263519,7411
BMRB,7413,"HMGB1, delta25",263519,7411
BMRB,15502,HMGB1,263534,7412
BMRB,7408,"HMGB1, ABprime",263534,7412
BMRB,7409,"HMGB1, delta5",263534,7412
BMRB,7410,"HMGB1, delta10",263534,7412
BMRB,7411,"HMGB1, delta15",263534,7412
BMRB,7413,"HMGB1, delta25",263534,7412
BMRB,15502,HMGB1,263549,7413
BMRB,7408,"HMGB1, ABprime",263549,7413
BMRB,7409,"HMGB1, delta5",263549,7413
BMRB,7410,"HMGB1, delta10",263549,7413
BMRB,7411,"HMGB1, delta15",263549,7413
BMRB,7412,"HMGB1, delta20",263549,7413
PDB,2JXY,BMRB Entry Tracking System,263564,7414
BMRB,15650,calmodulin with Calcium,263628,7416
BMRB,7417,calmodulin with Dysprosium(III),263628,7416
BMRB,7418,calmodulin with Thulium(III),263628,7416
BMRB,15650,calmodulin with Calcium,263651,7417
BMRB,7416,calmodulin with Terbium(III),263651,7417
BMRB,7418,calmodulin with Thulium(III),263651,7417
BMRB,15650,calmodulin with Calcium,263674,7418
BMRB,7416,calmodulin with Terbium(III),263674,7418
BMRB,7417,calmodulin with Dysprosium(III),263674,7418
PDB,2V6Z,BMRB Entry Tracking System,263697,7419
BMRB,7421,COMPLEMENT FACTOR H (mutant),263713,7420
PDB,2JGW,BMRB Entry Tracking System,263713,7420
BMRB,7420,COMPLEMENT FACTOR H,263728,7421
PDB,2JGX,BMRB Entry Tracking System,263728,7421
BMRB,15705,Complex with paramagnetic Dysprosium,263743,7422
BMRB,15852,4Ca and CaM and DAPk complex,263761,7423
BMRB,7424,3CaTb and CaM and DAPk complex,263761,7423
BMRB,7425,3CaTm and CaM and DAPk complex,263761,7423
PDB,2K61,BMRB Entry Tracking System,263761,7423
BMRB,15852,4Ca and CaM and DAPk complex,263786,7424
BMRB,7423,3CaYb and CaM and DAPk complex,263786,7424
BMRB,7425,3CaTm and CaM and DAPk complex,263786,7424
PDB,2K61,BMRB Entry Tracking System,263786,7424
BMRB,15852,4Ca and CaM and DAPk complex,263811,7425
BMRB,7423,3CaYb and CaM and DAPk complex,263811,7425
BMRB,7424,3CaTb and CaM and DAPk complex,263811,7425
PDB,2K61,BMRB Entry Tracking System,263811,7425
BMRB,15878,SycE-YopE complex,263836,7426
BMRB,7427,n-terminal YopE effector domain,263836,7426
BMRB,15878,SycE-YopE complex,263850,7427
BMRB,7426,YopE free state,263850,7427
BMRB,15959,Apo Form,263880,7429
BMRB,15964,Oxidised ERp18,263896,7430
PDB,2K8V,BMRB Entry Tracking System,263896,7430
BMRB,15967,Chemical shifts of complex of IscU(D39A) with co-chaperone HscB,263918,7432
BMRB,16322,Extracellular CD147 Isoform-2,263939,7433
BMRB,16586,3F5 VHH,263960,7434
BMRB,16683,REF 54-155 with ICP27 103-138,263976,7435
BMRB,16698,REF 54-155 in free form,263976,7435
PDB,2F3J,REF in free form,263976,7435
PDB,2KT5,BMRB Entry Tracking System,263976,7435
BMRB,10012,Assigned chemical shift of actin-binding domain of troponin in Ca2+-free state,264963,9500
PDB,1VDI,Solution structure of actin-binding domain of troponin in Ca2+-free state,264963,9500
PDB,1VDJ,BMRB Entry Tracking System,264963,9500