HEADER    MEMBRANE PROTEIN                        17-MAY-12   XXXX              
TITLE     STRUCTURE AND FUNCTION OF THE PORB PORIN FROM DISSEMINATING N.        
TITLE    2 GONORRHOEAE                                                          
KEYWDS    MEMBRANE PROTEIN, OUTER MEMBRANE PROTEIN, INFECTION, INVASION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.ZETH, V.KOZJAK-PAVLOVIC, M.FAULSTICH, R.HURWITZ, O.KEPP, T.RUDEL    
JRNL        AUTH   K.ZETH, V.KOZJAK-PAVLOVIC, M.FAULSTICH, M.FRAUNHOLZ,         
JRNL        AUTH 2 R.HURWITZ, O.KEPP, T.RUDEL                                   
JRNL        TITL   STRUCTURE AND FUNCTION OF THE PORB PORIN FROM DISSEMINATING  
JRNL        TITL 2 NEISSERIA GONORRHOEAE.                                       
JRNL        REF    BIOCHEM.J.                    V. 449   631 2013              
JRNL        REFN   ASTM BIJOAK  UK ISSN 0264-6021                               
JRNL        PMID   23095086                                                     
JRNL        DOI    10.1042/BJ20121025                                           
SEQRES   1 A  327  MET LYS LYS SER LEU ILE ALA LEU THR LEU ALA ALA LEU          
SEQRES   2 A  327  PRO VAL ALA ALA MET ALA ASP VAL THR LEU TYR GLY THR          
SEQRES   3 A  327  ILE LYS ALA GLY VAL GLU THR SER ARG SER VAL ALA HIS          
SEQRES   4 A  327  HIS GLY ALA GLN ALA ASP ARG VAL LYS THR ALA THR GLU          
SEQRES   5 A  327  ILE ALA ASP LEU GLY SER LYS ILE GLY PHE LYS GLY GLN          
SEQRES   6 A  327  GLU ASP LEU GLY ASN GLY LEU LYS ALA ILE TRP GLN LEU          
SEQRES   7 A  327  GLU GLN LYS ALA TYR VAL SER GLY THR ASP THR GLY TRP          
SEQRES   8 A  327  GLY ASN ARG GLN SER PHE ILE GLY LEU LYS GLY GLY PHE          
SEQRES   9 A  327  GLY LYS VAL ARG VAL GLY ARG LEU ASN ASN ILE LEU LYS          
SEQRES  10 A  327  ASP THR GLY ASN PHE ASN PRO TRP GLU GLY LYS SER TYR          
SEQRES  11 A  327  TYR SER GLY LEU SER ASN ILE ALA GLN PRO GLU GLU ARG          
SEQRES  12 A  327  HIS VAL SER VAL ARG TYR ASP SER PRO GLU PHE ALA GLY          
SEQRES  13 A  327  PHE SER GLY SER VAL GLN TYR VAL PRO ASN ASP ASN SER          
SEQRES  14 A  327  GLY LYS ASN ARG SER GLU SER TYR HIS ALA GLY PHE ASN          
SEQRES  15 A  327  TYR LYS ASN ASP GLY PHE PHE VAL GLN TYR ALA GLY SER          
SEQRES  16 A  327  TYR LYS ARG HIS ASN TYR THR THR GLU LYS HIS GLN VAL          
SEQRES  17 A  327  HIS ARG LEU VAL GLY GLY TYR ASP HIS ASP ALA LEU TYR          
SEQRES  18 A  327  ALA SER VAL ALA VAL GLN GLN GLN ASP ALA LYS LEU THR          
SEQRES  19 A  327  TRP ARG ASP ASP ASN SER HIS ASN SER GLN THR GLU VAL          
SEQRES  20 A  327  ALA THR THR VAL ALA TYR ARG PHE GLY ASN VAL THR PRO          
SEQRES  21 A  327  ARG VAL SER TYR ALA HIS GLY PHE LYS GLY SER VAL TYR          
SEQRES  22 A  327  ASP ALA ASP HIS ASP ASN THR TYR ASP GLN VAL VAL VAL          
SEQRES  23 A  327  GLY ALA GLU TYR ASP PHE SER LYS ARG THR SER ALA LEU          
SEQRES  24 A  327  VAL SER ALA GLY TRP LEU GLN LYS GLY LYS GLY ALA GLU          
SEQRES  25 A  327  LYS PHE VAL ALA THR VAL GLY GLY VAL GLY LEU ARG HIS          
SEQRES  26 A  327  LYS PHE                                                      
SEQRES   1 B  327  MET LYS LYS SER LEU ILE ALA LEU THR LEU ALA ALA LEU          
SEQRES   2 B  327  PRO VAL ALA ALA MET ALA ASP VAL THR LEU TYR GLY THR          
SEQRES   3 B  327  ILE LYS ALA GLY VAL GLU THR SER ARG SER VAL ALA HIS          
SEQRES   4 B  327  HIS GLY ALA GLN ALA ASP ARG VAL LYS THR ALA THR GLU          
SEQRES   5 B  327  ILE ALA ASP LEU GLY SER LYS ILE GLY PHE LYS GLY GLN          
SEQRES   6 B  327  GLU ASP LEU GLY ASN GLY LEU LYS ALA ILE TRP GLN LEU          
SEQRES   7 B  327  GLU GLN LYS ALA TYR VAL SER GLY THR ASP THR GLY TRP          
SEQRES   8 B  327  GLY ASN ARG GLN SER PHE ILE GLY LEU LYS GLY GLY PHE          
SEQRES   9 B  327  GLY LYS VAL ARG VAL GLY ARG LEU ASN ASN ILE LEU LYS          
SEQRES  10 B  327  ASP THR GLY ASN PHE ASN PRO TRP GLU GLY LYS SER TYR          
SEQRES  11 B  327  TYR SER GLY LEU SER ASN ILE ALA GLN PRO GLU GLU ARG          
SEQRES  12 B  327  HIS VAL SER VAL ARG TYR ASP SER PRO GLU PHE ALA GLY          
SEQRES  13 B  327  PHE SER GLY SER VAL GLN TYR VAL PRO ASN ASP ASN SER          
SEQRES  14 B  327  GLY LYS ASN ARG SER GLU SER TYR HIS ALA GLY PHE ASN          
SEQRES  15 B  327  TYR LYS ASN ASP GLY PHE PHE VAL GLN TYR ALA GLY SER          
SEQRES  16 B  327  TYR LYS ARG HIS ASN TYR THR THR GLU LYS HIS GLN VAL          
SEQRES  17 B  327  HIS ARG LEU VAL GLY GLY TYR ASP HIS ASP ALA LEU TYR          
SEQRES  18 B  327  ALA SER VAL ALA VAL GLN GLN GLN ASP ALA LYS LEU THR          
SEQRES  19 B  327  TRP ARG ASP ASP ASN SER HIS ASN SER GLN THR GLU VAL          
SEQRES  20 B  327  ALA THR THR VAL ALA TYR ARG PHE GLY ASN VAL THR PRO          
SEQRES  21 B  327  ARG VAL SER TYR ALA HIS GLY PHE LYS GLY SER VAL TYR          
SEQRES  22 B  327  ASP ALA ASP HIS ASP ASN THR TYR ASP GLN VAL VAL VAL          
SEQRES  23 B  327  GLY ALA GLU TYR ASP PHE SER LYS ARG THR SER ALA LEU          
SEQRES  24 B  327  VAL SER ALA GLY TRP LEU GLN LYS GLY LYS GLY ALA GLU          
SEQRES  25 B  327  LYS PHE VAL ALA THR VAL GLY GLY VAL GLY LEU ARG HIS          
SEQRES  26 B  327  LYS PHE                                                      
SEQRES   1 C  327  MET LYS LYS SER LEU ILE ALA LEU THR LEU ALA ALA LEU          
SEQRES   2 C  327  PRO VAL ALA ALA MET ALA ASP VAL THR LEU TYR GLY THR          
SEQRES   3 C  327  ILE LYS ALA GLY VAL GLU THR SER ARG SER VAL ALA HIS          
SEQRES   4 C  327  HIS GLY ALA GLN ALA ASP ARG VAL LYS THR ALA THR GLU          
SEQRES   5 C  327  ILE ALA ASP LEU GLY SER LYS ILE GLY PHE LYS GLY GLN          
SEQRES   6 C  327  GLU ASP LEU GLY ASN GLY LEU LYS ALA ILE TRP GLN LEU          
SEQRES   7 C  327  GLU GLN LYS ALA TYR VAL SER GLY THR ASP THR GLY TRP          
SEQRES   8 C  327  GLY ASN ARG GLN SER PHE ILE GLY LEU LYS GLY GLY PHE          
SEQRES   9 C  327  GLY LYS VAL ARG VAL GLY ARG LEU ASN ASN ILE LEU LYS          
SEQRES  10 C  327  ASP THR GLY ASN PHE ASN PRO TRP GLU GLY LYS SER TYR          
SEQRES  11 C  327  TYR SER GLY LEU SER ASN ILE ALA GLN PRO GLU GLU ARG          
SEQRES  12 C  327  HIS VAL SER VAL ARG TYR ASP SER PRO GLU PHE ALA GLY          
SEQRES  13 C  327  PHE SER GLY SER VAL GLN TYR VAL PRO ASN ASP ASN SER          
SEQRES  14 C  327  GLY LYS ASN ARG SER GLU SER TYR HIS ALA GLY PHE ASN          
SEQRES  15 C  327  TYR LYS ASN ASP GLY PHE PHE VAL GLN TYR ALA GLY SER          
SEQRES  16 C  327  TYR LYS ARG HIS ASN TYR THR THR GLU LYS HIS GLN VAL          
SEQRES  17 C  327  HIS ARG LEU VAL GLY GLY TYR ASP HIS ASP ALA LEU TYR          
SEQRES  18 C  327  ALA SER VAL ALA VAL GLN GLN GLN ASP ALA LYS LEU THR          
SEQRES  19 C  327  TRP ARG ASP ASP ASN SER HIS ASN SER GLN THR GLU VAL          
SEQRES  20 C  327  ALA THR THR VAL ALA TYR ARG PHE GLY ASN VAL THR PRO          
SEQRES  21 C  327  ARG VAL SER TYR ALA HIS GLY PHE LYS GLY SER VAL TYR          
SEQRES  22 C  327  ASP ALA ASP HIS ASP ASN THR TYR ASP GLN VAL VAL VAL          
SEQRES  23 C  327  GLY ALA GLU TYR ASP PHE SER LYS ARG THR SER ALA LEU          
SEQRES  24 C  327  VAL SER ALA GLY TRP LEU GLN LYS GLY LYS GLY ALA GLU          
SEQRES  25 C  327  LYS PHE VAL ALA THR VAL GLY GLY VAL GLY LEU ARG HIS          
SEQRES  26 C  327  LYS PHE                                                      
SEQRES   1 D    8  ALA ALA ALA ALA ALA ALA ALA ALA                              
SEQRES   1 E    8  ALA ALA ALA ALA ALA ALA ALA ALA                              
SEQRES   1 F    8  ALA ALA ALA ALA ALA ALA ALA ALA                              
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   7  ATP    3(C10 H16 N5 O13 P3)                                         
FORMUL   8  PO4    6(O4 P 3-)                                                   
FORMUL  10   MG    MG 2+                                                        
HELIX    1   1 ASN B   95  GLY B  101  1                                   7    
SHEET    1  AA18 VAL A   2  HIS A  21  0                                        
SHEET    2  AA18 LYS A  40  GLU A  47 -1  O  LYS A  40   N  THR A   7           
SHEET    3  AA18 LYS A  54  LYS A  62 -1  O  ALA A  55   N  GLU A  47           
SHEET    4  AA18 PHE A  78  GLY A  83 -1  O  PHE A  78   N  GLN A  58           
SHEET    5  AA18 GLY A  86  ASN A  94 -1  O  GLY A  86   N  GLY A  83           
SHEET    6  AA18 ARG A 124  PHE A 135 -1  O  HIS A 125   N  LEU A  93           
SHEET    7  AA18 PHE A 138  VAL A 145 -1  O  PHE A 138   N  PHE A 135           
SHEET    8  AA18 SER A 157  LYS A 165 -1  O  SER A 157   N  VAL A 145           
SHEET    9  AA18 PHE A 169  LYS A 178 -1  O  VAL A 171   N  TYR A 164           
SHEET   10  AA18 GLU A 185  HIS A 198 -1  O  HIS A 187   N  LYS A 178           
SHEET   11  AA18 LEU A 201  LEU A 214 -1  O  LEU A 201   N  HIS A 198           
SHEET   12  AA18 SER A 221  TYR A 234 -1  O  SER A 221   N  LEU A 214           
SHEET   13  AA18 ARG A 242  GLY A 248 -1  O  VAL A 243   N  VAL A 232           
SHEET   14  AA18 TYR A 262  ASP A 272 -1  O  TYR A 262   N  GLY A 248           
SHEET   15  AA18 THR A 277  GLY A 289 -1  O  ALA A 279   N  TYR A 271           
SHEET   16  AA18 GLU A 293  PHE A 308 -1  O  PHE A 295   N  LYS A 288           
SHEET   17  AA18 VAL A   2  HIS A  21  1  O  SER A  17   N  ALA A  19           
SHEET    1  BA18 VAL B   2  ALA B  19  0                                        
SHEET    2  BA18 LYS B  40  GLU B  47 -1  O  LYS B  40   N  THR B   7           
SHEET    3  BA18 LYS B  54  LYS B  62 -1  O  ALA B  55   N  GLU B  47           
SHEET    4  BA18 PHE B  78  LYS B  82 -1  O  PHE B  78   N  GLN B  58           
SHEET    5  BA18 LYS B  87  ASN B  94 -1  O  VAL B  88   N  LEU B  81           
SHEET    6  BA18 ARG B 124  PHE B 135 -1  O  HIS B 125   N  LEU B  93           
SHEET    7  BA18 PHE B 138  VAL B 145 -1  O  PHE B 138   N  PHE B 135           
SHEET    8  BA18 SER B 157  LYS B 165 -1  O  SER B 157   N  VAL B 145           
SHEET    9  BA18 PHE B 169  ASN B 181 -1  O  VAL B 171   N  TYR B 164           
SHEET   10  BA18 THR B 184  HIS B 198 -1  O  THR B 184   N  ASN B 181           
SHEET   11  BA18 LEU B 201  LEU B 214 -1  O  LEU B 201   N  HIS B 198           
SHEET   12  BA18 SER B 221  TYR B 234 -1  O  SER B 221   N  LEU B 214           
SHEET   13  BA18 ARG B 242  GLY B 248 -1  O  VAL B 243   N  VAL B 232           
SHEET   14  BA18 TYR B 262  ASP B 272 -1  O  TYR B 262   N  GLY B 248           
SHEET   15  BA18 THR B 277  GLY B 289 -1  O  ALA B 279   N  TYR B 271           
SHEET   16  BA18 LYS B 294  PHE B 308 -1  O  PHE B 295   N  LYS B 288           
SHEET   17  BA18 VAL B   2  ALA B  19  1  O  SER B  17   N  ALA B  19           
SHEET    1  CA18 VAL C   2  ALA C  19  0                                        
SHEET    2  CA18 LYS C  40  GLU C  47 -1  O  LYS C  40   N  THR C   7           
SHEET    3  CA18 LYS C  54  LYS C  62 -1  O  ALA C  55   N  GLU C  47           
SHEET    4  CA18 PHE C  78  LYS C  82 -1  O  PHE C  78   N  GLN C  58           
SHEET    5  CA18 LYS C  87  ASN C  94 -1  O  VAL C  88   N  LEU C  81           
SHEET    6  CA18 ARG C 124  PHE C 135 -1  O  HIS C 125   N  LEU C  93           
SHEET    7  CA18 PHE C 138  VAL C 145 -1  O  PHE C 138   N  PHE C 135           
SHEET    8  CA18 SER C 157  LYS C 165 -1  O  SER C 157   N  VAL C 145           
SHEET    9  CA18 PHE C 169  ASN C 181 -1  O  VAL C 171   N  TYR C 164           
SHEET   10  CA18 THR C 184  HIS C 198 -1  O  THR C 184   N  ASN C 181           
SHEET   11  CA18 LEU C 201  LEU C 214 -1  O  LEU C 201   N  HIS C 198           
SHEET   12  CA18 SER C 221  TYR C 234 -1  O  SER C 221   N  LEU C 214           
SHEET   13  CA18 ARG C 242  GLY C 248 -1  O  VAL C 243   N  VAL C 232           
SHEET   14  CA18 TYR C 262  ASP C 272 -1  O  TYR C 262   N  GLY C 248           
SHEET   15  CA18 THR C 277  GLY C 289 -1  O  ALA C 279   N  TYR C 271           
SHEET   16  CA18 LYS C 294  PHE C 308 -1  O  PHE C 295   N  LYS C 288           
SHEET   17  CA18 VAL C   2  ALA C  19  1  O  SER C  17   N  ALA C  19           
LINK         O1A ATP A 400                MG    MG A 403     1555   1555  2.78  
LINK        MG    MG A 403                 OE1 GLU A 107     1555   1555  2.67  
CISPEP   1 HIS A   20    HIS A   21          1        -2.69                     
CISPEP   2 LEU A   49    GLY A   50          1         1.39                     
CISPEP   3 GLY A  114    LEU A  115          1       -12.38                     
CISPEP   4 ASN A  147    ASP A  148          1       -22.63                     
CISPEP   5 SER A  150    GLY A  151          1       -25.32                     
CISPEP   6 ASP A  219    ASN A  220          1         2.36                     
CISPEP   7 LEU B   49    GLY B   50          1         1.58                     
CISPEP   8 GLY B  114    LEU B  115          1       -17.70                     
CISPEP   9 ASN B  147    ASP B  148          1       -18.99                     
CISPEP  10 SER B  150    GLY B  151          1       -24.13                     
CISPEP  11 ASP B  219    ASN B  220          1         1.55                     
CISPEP  12 LEU C   49    GLY C   50          1         0.73                     
CISPEP  13 GLY C  114    LEU C  115          1       -17.82                     
CISPEP  14 ASN C  147    ASP C  148          1       -21.09                     
CISPEP  15 SER C  150    GLY C  151          1       -25.01                     
CISPEP  16 ASP C  219    ASN C  220          1         0.57                     
CISPEP  17 ALA D  400    ALA D  401          1        13.54                     
CISPEP  18 ALA D  401    ALA D  402          1       -28.11                     
CISPEP  19 ALA D  404    ALA D  405          1        26.01                     
CISPEP  20 ALA E  401    ALA E  402          1       -11.09                     
CISPEP  21 ALA F  404    ALA F  405          1        -4.13                     
SITE     1 AC1  9 LYS A   9  GLY A  38  LYS A  40  GLU A  60                    
SITE     2 AC1  9 LYS A  62  ARG A  75  LYS A  98  ARG A 124                    
SITE     3 AC1  9  MG A 403                                                     
SITE     1 AC2  5 ILE A  96  ASP A  99  ARG A 129  SER A 141                    
SITE     2 AC2  5 ASN A 163                                                     
SITE     1 AC3  3 ASN A  74  ARG A  92  ARG A 124                               
SITE     1 AC4  3 LYS A   9  GLU A 107  ATP A 400                               
SITE     1 AC5  9 LYS B   9  GLY B  38  LYS B  40  GLN B  58                    
SITE     2 AC5  9 GLU B  60  ARG B  75  GLN B  76  ARG B 124                    
SITE     3 AC5  9 LYS B 307                                                     
SITE     1 AC6  7 ILE B  96  ASP B  99  THR B 100  SER B 141                    
SITE     2 AC6  7 PHE B 162  ASN B 163  TYR B 173                               
SITE     1 AC7  4 LYS B  62  ASN B  74  ARG B  92  ARG B 124                    
SITE     1 AC8 10 LYS C   9  GLY C  38  LYS C  40  GLN C  58                    
SITE     2 AC8 10 GLU C  60  ARG C  75  GLN C  76  ASN C  94                    
SITE     3 AC8 10 LYS C  98  ARG C 124                                          
SITE     1 AC9  5 ILE C  96  ASP C  99  THR C 100  SER C 141                    
SITE     2 AC9  5 ASN C 163                                                     
SITE     1 BC1  3 ASN C  74  ARG C  92  ARG C 124                               
CRYST1  114.050  111.470   88.340  90.00 102.07  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008768  0.000000  0.001875        0.00000                         
SCALE2      0.000000  0.008971  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011576        0.00000                         
MODEL        1                                                                  
ATOM      1  N   ALA F 402       7.514   0.018  21.949  1.00118.59           N  
ANISOU    1  N   ALA F 402    14125  14933  16001    824    144    325       N  
ATOM      2  CA  ALA F 402       8.153   0.985  21.056  1.00 94.36           C  
ANISOU    2  CA  ALA F 402    11061  11851  12939    823     95    328       C  
ATOM      3  C   ALA F 402       9.677   0.739  20.917  1.00101.02           C  
ANISOU    3  C   ALA F 402    11982  12734  13667    799     48    284       C  
ATOM      4  O   ALA F 402      10.387   1.471  20.202  1.00104.91           O  
ANISOU    4  O   ALA F 402    12487  13223  14150    793      7    282       O  
ATOM      5  CB  ALA F 402       7.843   2.403  21.509  1.00 60.84           C  
ANISOU    5  CB  ALA F 402     6802   7548   8766    857    166    313       C  
ATOM      6  N   ALA F 403      10.153  -0.286  21.635  1.00 84.15           N  
ANISOU    6  N   ALA F 403     9892  10632  11448    785     57    252       N  
ATOM      7  CA  ALA F 403      11.437  -0.956  21.388  1.00 58.33           C  
ANISOU    7  CA  ALA F 403     6678   7406   8080    761      2    227       C  
ATOM      8  C   ALA F 403      11.300  -2.467  21.739  1.00 84.53           C  
ANISOU    8  C   ALA F 403    10008  10758  11352    746     -7    232       C  
ATOM      9  O   ALA F 403      10.654  -2.818  22.728  1.00 82.36           O  
ANISOU    9  O   ALA F 403     9732  10476  11086    753     50    226       O  
ATOM     10  CB  ALA F 403      12.570  -0.282  22.167  1.00 29.01           C  
ANISOU   10  CB  ALA F 403     3026   3691   4304    760     28    171       C  
ATOM     11  N   ALA F 404      11.879  -3.347  20.916  1.00 84.44           N  
ANISOU   11  N   ALA F 404    10010  10778  11295    726    -75    243       N  
ATOM     12  CA  ALA F 404      11.701  -4.818  21.005  1.00 82.61           C  
ANISOU   12  CA  ALA F 404     9787  10571  11031    710    -95    255       C  
ATOM     13  C   ALA F 404      12.798  -5.546  21.839  1.00101.16           C  
ANISOU   13  C   ALA F 404    12198  12947  13292    705    -90    215       C  
ATOM     14  O   ALA F 404      13.526  -4.878  22.567  1.00 91.52           O  
ANISOU   14  O   ALA F 404    11011  11725  12038    711    -62    178       O  
ATOM     15  CB  ALA F 404      11.575  -5.402  19.590  1.00 69.10           C  
ANISOU   15  CB  ALA F 404     8058   8870   9327    690   -169    292       C  
ATOM     16  N   ALA F 405      12.924  -6.881  21.805  1.00105.05           N  
ANISOU   16  N   ALA F 405    12707  13459  13747    692   -117    222       N  
ATOM     17  CA  ALA F 405      12.070  -7.841  21.106  1.00124.90           C  
ANISOU   17  CA  ALA F 405    15193  15973  16290    677   -150    262       C  
ATOM     18  C   ALA F 405      11.003  -8.195  22.107  1.00163.43           C  
ANISOU   18  C   ALA F 405    20052  20843  21200    679    -97    275       C  
ATOM     19  O   ALA F 405      10.195  -9.109  21.893  1.00179.61           O  
ANISOU   19  O   ALA F 405    22079  22891  23273    664   -113    308       O  
ATOM     20  CB  ALA F 405      12.869  -9.095  20.710  1.00 97.93           C  
ANISOU   20  CB  ALA F 405    11816  12578  12814    662   -195    255       C  
ATOM     21  N   ALA F 406      11.037  -7.440  23.205  1.00171.02           N  
ANISOU   21  N   ALA F 406    21026  21795  22158    695    -33    248       N  
ATOM     22  CA  ALA F 406      10.433  -7.804  24.484  1.00180.08           C  
ANISOU   22  CA  ALA F 406    22182  22938  23301    696     32    243       C  
ATOM     23  C   ALA F 406       8.972  -8.287  24.486  1.00192.61           C  
ANISOU   23  C   ALA F 406    23711  24512  24959    692     55    288       C  
ATOM     24  O   ALA F 406       8.694  -9.336  25.075  1.00209.18           O  
ANISOU   24  O   ALA F 406    25824  26621  27035    678     66    297       O  
ATOM     25  CB  ALA F 406      10.657  -6.697  25.512  1.00177.28           C  
ANISOU   25  CB  ALA F 406    21855  22570  22934    711    100    204       C  
ATOM     26  N   ALA F 407       8.032  -7.542  23.902  1.00174.78           N  
ANISOU   26  N   ALA F 407    21388  22230  22790    703     64    319       N  
ATOM     27  CA  ALA F 407       6.732  -8.165  23.591  1.00169.63           C  
ANISOU   27  CA  ALA F 407    20671  21569  22211    691     58    375       C  
ATOM     28  C   ALA F 407       5.796  -7.476  22.589  1.00179.54           C  
ANISOU   28  C   ALA F 407    21846  22801  23569    696     33    425       C  
ATOM     29  O   ALA F 407       5.903  -6.270  22.344  1.00182.09           O  
ANISOU   29  O   ALA F 407    22153  23105  23928    718     46    418       O  
ATOM     30  CB  ALA F 407       5.985  -8.571  24.858  1.00163.55           C  
ANISOU   30  CB  ALA F 407    19896  20795  21451    694    140    376       C  
ATOM     31  N   ALA F 408       4.866  -8.274  22.054  1.00183.20           N  
ANISOU   31  N   ALA F 408    22260  23265  24082    672     -7    479       N  
ATOM     32  CA  ALA F 408       3.865  -7.860  21.061  1.00175.76           C  
ANISOU   32  CA  ALA F 408    21236  22304  23241    665    -48    543       C  
ATOM     33  C   ALA F 408       4.198  -6.560  20.327  1.00160.79           C  
ANISOU   33  C   ALA F 408    19327  20392  21375    684    -70    542       C  
ATOM     34  O   ALA F 408       3.426  -5.600  20.356  1.00143.56           O  
ANISOU   34  O   ALA F 408    17079  18179  19290    708    -34    571       O  
ATOM     35  CB  ALA F 408       2.470  -7.782  21.696  1.00179.40           C  
ANISOU   35  CB  ALA F 408    21615  22743  23806    677     18    587       C  
TER      36      ALA F 408                                                      
ENDMDL                                                                          
MASTER        0    0    0    1   51    0   19    6 7329    6    0   81          
END                                                                             
