HEADER    ISOMERASE, CHAPERONE                    10-JAN-14   XXXX              
TITLE     STRUCTURE OF SLYD FROM THERMUS THERMOPHILUS IN COMPLEX WITH S2-W23A   
TITLE    2 PEPTIDE                                                              
KEYWDS    FKBP DOMAIN, IF DOMAIN, CHAPERONE, PEPTIDYL-PROLYL ISOMERASE, PPIASE, 
KEYWDS   2 ISOMERASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.QUISTGAARD, C.LOW, P.NORDLUND                                     
JRNL        AUTH   E.M.QUISTGAARD, C.LOW, P.NORDLUND                            
JRNL        TITL   STRUCTURE OF SLYD FROM THERMUS THERMOPHILUS IN COMPLEX WITH  
JRNL        TITL 2 S2-W23A PEPTIDE                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
SEQRES   1 A  153  MET LYS VAL GLY GLN ASP LYS VAL VAL THR ILE ARG TYR          
SEQRES   2 A  153  THR LEU GLN VAL GLU GLY GLU VAL LEU ASP GLN GLY GLU          
SEQRES   3 A  153  LEU SER TYR LEU HIS GLY HIS ARG ASN LEU ILE PRO GLY          
SEQRES   4 A  153  LEU GLU GLU ALA LEU GLU GLY ARG GLU GLU GLY GLU ALA          
SEQRES   5 A  153  PHE GLN ALA HIS VAL PRO ALA GLU LYS ALA TYR GLY PRO          
SEQRES   6 A  153  HIS ASP PRO GLU GLY VAL GLN VAL VAL PRO LEU SER ALA          
SEQRES   7 A  153  PHE PRO GLU ASP ALA GLU VAL VAL PRO GLY ALA GLN PHE          
SEQRES   8 A  153  TYR ALA GLN ASP MET GLU GLY ASN PRO MET PRO LEU THR          
SEQRES   9 A  153  VAL VAL ALA VAL GLU GLY GLU GLU VAL THR VAL ASP PHE          
SEQRES  10 A  153  ASN HIS PRO LEU ALA GLY LYS ASP LEU ASP PHE GLN VAL          
SEQRES  11 A  153  GLU VAL VAL LYS VAL ARG GLU ALA THR PRO GLU GLU LEU          
SEQRES  12 A  153  LEU HIS GLY HIS ALA HIS LEU VAL PRO LYS                      
SEQRES   1 B  153  MET LYS VAL GLY GLN ASP LYS VAL VAL THR ILE ARG TYR          
SEQRES   2 B  153  THR LEU GLN VAL GLU GLY GLU VAL LEU ASP GLN GLY GLU          
SEQRES   3 B  153  LEU SER TYR LEU HIS GLY HIS ARG ASN LEU ILE PRO GLY          
SEQRES   4 B  153  LEU GLU GLU ALA LEU GLU GLY ARG GLU GLU GLY GLU ALA          
SEQRES   5 B  153  PHE GLN ALA HIS VAL PRO ALA GLU LYS ALA TYR GLY PRO          
SEQRES   6 B  153  HIS ASP PRO GLU GLY VAL GLN VAL VAL PRO LEU SER ALA          
SEQRES   7 B  153  PHE PRO GLU ASP ALA GLU VAL VAL PRO GLY ALA GLN PHE          
SEQRES   8 B  153  TYR ALA GLN ASP MET GLU GLY ASN PRO MET PRO LEU THR          
SEQRES   9 B  153  VAL VAL ALA VAL GLU GLY GLU GLU VAL THR VAL ASP PHE          
SEQRES  10 B  153  ASN HIS PRO LEU ALA GLY LYS ASP LEU ASP PHE GLN VAL          
SEQRES  11 B  153  GLU VAL VAL LYS VAL ARG GLU ALA THR PRO GLU GLU LEU          
SEQRES  12 B  153  LEU HIS GLY HIS ALA HIS LEU VAL PRO LYS                      
SEQRES   1 C  153  MET LYS VAL GLY GLN ASP LYS VAL VAL THR ILE ARG TYR          
SEQRES   2 C  153  THR LEU GLN VAL GLU GLY GLU VAL LEU ASP GLN GLY GLU          
SEQRES   3 C  153  LEU SER TYR LEU HIS GLY HIS ARG ASN LEU ILE PRO GLY          
SEQRES   4 C  153  LEU GLU GLU ALA LEU GLU GLY ARG GLU GLU GLY GLU ALA          
SEQRES   5 C  153  PHE GLN ALA HIS VAL PRO ALA GLU LYS ALA TYR GLY PRO          
SEQRES   6 C  153  HIS ASP PRO GLU GLY VAL GLN VAL VAL PRO LEU SER ALA          
SEQRES   7 C  153  PHE PRO GLU ASP ALA GLU VAL VAL PRO GLY ALA GLN PHE          
SEQRES   8 C  153  TYR ALA GLN ASP MET GLU GLY ASN PRO MET PRO LEU THR          
SEQRES   9 C  153  VAL VAL ALA VAL GLU GLY GLU GLU VAL THR VAL ASP PHE          
SEQRES  10 C  153  ASN HIS PRO LEU ALA GLY LYS ASP LEU ASP PHE GLN VAL          
SEQRES  11 C  153  GLU VAL VAL LYS VAL ARG GLU ALA THR PRO GLU GLU LEU          
SEQRES  12 C  153  LEU HIS GLY HIS ALA HIS LEU VAL PRO LYS                      
SEQRES   1 D  153  MET LYS VAL GLY GLN ASP LYS VAL VAL THR ILE ARG TYR          
SEQRES   2 D  153  THR LEU GLN VAL GLU GLY GLU VAL LEU ASP GLN GLY GLU          
SEQRES   3 D  153  LEU SER TYR LEU HIS GLY HIS ARG ASN LEU ILE PRO GLY          
SEQRES   4 D  153  LEU GLU GLU ALA LEU GLU GLY ARG GLU GLU GLY GLU ALA          
SEQRES   5 D  153  PHE GLN ALA HIS VAL PRO ALA GLU LYS ALA TYR GLY PRO          
SEQRES   6 D  153  HIS ASP PRO GLU GLY VAL GLN VAL VAL PRO LEU SER ALA          
SEQRES   7 D  153  PHE PRO GLU ASP ALA GLU VAL VAL PRO GLY ALA GLN PHE          
SEQRES   8 D  153  TYR ALA GLN ASP MET GLU GLY ASN PRO MET PRO LEU THR          
SEQRES   9 D  153  VAL VAL ALA VAL GLU GLY GLU GLU VAL THR VAL ASP PHE          
SEQRES  10 D  153  ASN HIS PRO LEU ALA GLY LYS ASP LEU ASP PHE GLN VAL          
SEQRES  11 D  153  GLU VAL VAL LYS VAL ARG GLU ALA THR PRO GLU GLU LEU          
SEQRES  12 D  153  LEU HIS GLY HIS ALA HIS LEU VAL PRO LYS                      
SEQRES   1 E   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 E   16  GLY ALA NH2                                                  
SEQRES   1 F   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 F   16  GLY ALA NH2                                                  
SEQRES   1 G   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 G   16  GLY ALA NH2                                                  
SEQRES   1 H   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 H   16  GLY ALA NH2                                                  
SEQRES   1 I   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 I   16  GLY ALA NH2                                                  
SEQRES   1 J   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 J   16  GLY ALA NH2                                                  
SEQRES   1 K   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 K   16  GLY ALA NH2                                                  
SEQRES   1 L   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 L   16  GLY ALA NH2                                                  
SEQRES   1 M   16  THR ARG TYR ALA ASN PRO LYS MET LYS PRO PHE ILE PHE          
SEQRES   2 M   16  GLY ALA NH2                                                  
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   6  NH2    5(H2 N)                                                      
FORMUL  14   CL    4(CL 1-)                                                     
FORMUL  15  ACT    C2 H3 O2 1-                                                  
FORMUL  16  GOL    2(C3 H8 O3)                                                  
FORMUL  21  HOH   *606(H2 O)                                                    
HELIX    1   1 ILE A   37  GLU A   45  1                                   9    
HELIX    2   2 PRO A   58  ALA A   62  5                                   5    
HELIX    3   3 ASP A   67  GLU A   69  5                                   3    
HELIX    4   4 SER A   77  PHE A   79  5                                   3    
HELIX    5   5 THR A  139  GLY A  146  1                                   8    
HELIX    6   6 ILE B   37  GLU B   45  1                                   9    
HELIX    7   7 PRO B   58  ALA B   62  5                                   5    
HELIX    8   8 ASP B   67  GLU B   69  5                                   3    
HELIX    9   9 SER B   77  PHE B   79  5                                   3    
HELIX   10  10 THR B  139  GLY B  146  1                                   8    
HELIX   11  11 ILE C   37  GLU C   45  1                                   9    
HELIX   12  12 PRO C   58  ALA C   62  5                                   5    
HELIX   13  13 ASP C   67  GLU C   69  5                                   3    
HELIX   14  14 SER C   77  PHE C   79  5                                   3    
HELIX   15  15 THR C  139  GLY C  146  1                                   8    
HELIX   16  16 ILE D   37  GLU D   45  1                                   9    
HELIX   17  17 PRO D   58  ALA D   62  5                                   5    
HELIX   18  18 ASP D   67  GLU D   69  5                                   3    
HELIX   19  19 SER D   77  PHE D   79  5                                   3    
HELIX   20  20 THR D  139  GLY D  146  1                                   8    
SHEET    1   A 4 GLU A  20  LEU A  30  0                                        
SHEET    2   A 4 LYS A   7  VAL A  17 -1  N  LEU A  15   O  ASP A  23           
SHEET    3   A 4 LEU A 126  GLU A 137 -1  O  LYS A 134   N  THR A  10           
SHEET    4   A 4 ALA A  52  VAL A  57 -1  N  VAL A  57   O  LEU A 126           
SHEET    1   B 4 VAL A  71  PRO A  75  0                                        
SHEET    2   B 4 GLU A 112  ASP A 116 -1  O  VAL A 113   N  VAL A  74           
SHEET    3   B 4 PRO A 100  GLU A 109 -1  N  GLU A 109   O  GLU A 112           
SHEET    4   B 4 GLN A  90  GLN A  94 -1  N  ALA A  93   O  MET A 101           
SHEET    1   C 4 GLU B  20  LEU B  30  0                                        
SHEET    2   C 4 LYS B   7  VAL B  17 -1  N  LEU B  15   O  ASP B  23           
SHEET    3   C 4 LEU B 126  GLU B 137 -1  O  ASP B 127   N  GLN B  16           
SHEET    4   C 4 ALA B  52  VAL B  57 -1  N  VAL B  57   O  LEU B 126           
SHEET    1   D 5 VAL B  71  PRO B  75  0                                        
SHEET    2   D 5 GLU B 112  ASP B 116 -1  O  VAL B 115   N  GLN B  72           
SHEET    3   D 5 PRO B 100  GLU B 109 -1  N  VAL B 106   O  THR B 114           
SHEET    4   D 5 GLN B  90  GLN B  94 -1  N  ALA B  93   O  MET B 101           
SHEET    5   D 5 PHE H  32  GLY H  33 -1  O  PHE H  32   N  TYR B  92           
SHEET    1   E 4 GLU C  20  LEU C  30  0                                        
SHEET    2   E 4 LYS C   7  VAL C  17 -1  N  LEU C  15   O  ASP C  23           
SHEET    3   E 4 LEU C 126  GLU C 137 -1  O  ASP C 127   N  GLN C  16           
SHEET    4   E 4 ALA C  52  VAL C  57 -1  N  VAL C  57   O  LEU C 126           
SHEET    1   F 4 VAL C  71  PRO C  75  0                                        
SHEET    2   F 4 GLU C 112  ASP C 116 -1  O  VAL C 115   N  GLN C  72           
SHEET    3   F 4 PRO C 100  GLU C 109 -1  N  VAL C 106   O  THR C 114           
SHEET    4   F 4 GLN C  90  GLN C  94 -1  N  ALA C  93   O  MET C 101           
SHEET    1   G 4 GLU D  20  LEU D  30  0                                        
SHEET    2   G 4 LYS D   7  VAL D  17 -1  N  LEU D  15   O  LEU D  22           
SHEET    3   G 4 LEU D 126  GLU D 137 -1  O  ASP D 127   N  GLN D  16           
SHEET    4   G 4 ALA D  52  VAL D  57 -1  N  VAL D  57   O  LEU D 126           
SHEET    1   H 5 VAL D  71  PRO D  75  0                                        
SHEET    2   H 5 GLU D 112  ASP D 116 -1  O  VAL D 115   N  GLN D  72           
SHEET    3   H 5 PRO D 100  GLU D 109 -1  N  VAL D 106   O  THR D 114           
SHEET    4   H 5 GLN D  90  GLN D  94 -1  N  ALA D  93   O  MET D 101           
SHEET    5   H 5 PHE L  32  GLY L  33 -1  O  PHE L  32   N  TYR D  92           
LINK         C   ALA F  34                 N   NH2 F  35     1555   1555  1.33  
LINK         C   ALA H  34                 N   NH2 H  35     1555   1555  1.33  
LINK         C   ALA I  34                 N   NH2 I  35     1555   1555  1.33  
LINK         C   ALA K  34                 N   NH2 K  35     1555   1555  1.33  
LINK         C   ALA L  34                 N   NH2 L  35     1555   1555  1.33  
CISPEP   1 LYS E   28    PRO E   29          1         9.84                     
CISPEP   2 LYS G   28    PRO G   29          1        -0.82                     
CISPEP   3 LYS I   28    PRO I   29          1         5.46                     
CISPEP   4 LYS K   28    PRO K   29          1        -3.58                     
SITE     1 AC1  7 TYR A  29  LEU A  30  ASN A  35  HIS A 147                    
SITE     2 AC1  7 ALA A 148  HOH A 398  LYS E  28                               
SITE     1 AC2  5 SER A  28  LYS A 134  ARG A 136  HOH A 310                    
SITE     2 AC2  5 HOH A 385                                                     
SITE     1 AC3  8 ARG A  34  HOH A 388  HOH A 400  HOH A 445                    
SITE     2 AC3  8 GLN C   5  HOH C 387  ASN E  24  MET E  27                    
SITE     1 AC4  5 TYR B  29  LEU B  30  ASN B  35  HIS B 147                    
SITE     2 AC4  5 ALA B 148                                                     
SITE     1 AC5  6 TYR C  29  LEU C  30  ASN C  35  HIS C 147                    
SITE     2 AC5  6 ALA C 148  LYS I  28                                          
SITE     1 AC6  5 TYR D  29  LEU D  30  ASN D  35  ALA D 148                    
SITE     2 AC6  5 HOH D 352                                                     
SITE     1 AC7  9 ARG C  12  TYR C  13  THR C  14  GLN C 129                    
SITE     2 AC7  9 VAL C 130  GLU C 131  GLY D  98  ASN D  99                    
SITE     3 AC7  9 PRO D 100                                                     
CRYST1  184.120   41.200  131.520  90.00 123.13  90.00 C 1 2 1      36          
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      0.005431  0.000000  0.003544        0.00000                         
SCALE2      0.000000  0.024272  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009079        0.00000                         
MODEL        1                                                                  
ATOM      1  N   PRO M  29      25.954  10.616  18.382  1.00 66.44           N  
ANISOU    1  N   PRO M  29     8908   7337   8998   -899   -490   1639       N  
ATOM      2  CA  PRO M  29      25.757   9.842  19.611  1.00 66.40           C  
ANISOU    2  CA  PRO M  29     8893   7394   8942   -863   -459   1515       C  
ATOM      3  C   PRO M  29      25.249   8.431  19.318  1.00 66.09           C  
ANISOU    3  C   PRO M  29     8881   7468   8763   -859   -253   1465       C  
ATOM      4  O   PRO M  29      24.403   8.245  18.444  1.00 64.81           O  
ANISOU    4  O   PRO M  29     8750   7354   8522   -861   -206   1420       O  
ATOM      5  CB  PRO M  29      24.692  10.645  20.360  1.00 69.53           C  
ANISOU    5  CB  PRO M  29     9319   7762   9337   -806   -600   1341       C  
ATOM      6  CG  PRO M  29      24.896  12.046  19.896  1.00 70.74           C  
ANISOU    6  CG  PRO M  29     9462   7794   9620   -815   -770   1410       C  
ATOM      7  CD  PRO M  29      25.309  11.939  18.453  1.00 70.44           C  
ANISOU    7  CD  PRO M  29     9436   7757   9570   -865   -690   1584       C  
ATOM      8  N   PHE M  30      25.766   7.453  20.052  1.00 64.58           N  
ANISOU    8  N   PHE M  30     8685   7304   8549   -855   -154   1474       N  
ATOM      9  CA  PHE M  30      25.409   6.053  19.845  1.00 66.58           C  
ANISOU    9  CA  PHE M  30     8969   7636   8695   -858     59   1435       C  
ATOM     10  C   PHE M  30      24.392   5.607  20.895  1.00 68.09           C  
ANISOU   10  C   PHE M  30     9217   7864   8790   -824     94   1265       C  
ATOM     11  O   PHE M  30      24.759   5.156  21.981  1.00 63.91           O  
ANISOU   11  O   PHE M  30     8739   7317   8227   -804    106   1265       O  
ATOM     12  CB  PHE M  30      26.664   5.181  19.911  1.00 67.13           C  
ANISOU   12  CB  PHE M  30     8999   7680   8827   -866    173   1574       C  
ATOM     13  CG  PHE M  30      26.473   3.800  19.366  1.00 63.85           C  
ANISOU   13  CG  PHE M  30     8616   7314   8332   -878    417   1561       C  
ATOM     14  CD1 PHE M  30      26.682   3.539  18.021  1.00 64.09           C  
ANISOU   14  CD1 PHE M  30     8651   7350   8349   -922    562   1620       C  
ATOM     15  CD2 PHE M  30      26.097   2.757  20.199  1.00 63.60           C  
ANISOU   15  CD2 PHE M  30     8639   7303   8224   -852    516   1490       C  
ATOM     16  CE1 PHE M  30      26.510   2.259  17.514  1.00 64.02           C  
ANISOU   16  CE1 PHE M  30     8690   7370   8264   -939    790   1586       C  
ATOM     17  CE2 PHE M  30      25.924   1.478  19.700  1.00 63.48           C  
ANISOU   17  CE2 PHE M  30     8655   7307   8156   -869    746   1472       C  
ATOM     18  CZ  PHE M  30      26.130   1.228  18.355  1.00 63.66           C  
ANISOU   18  CZ  PHE M  30     8671   7338   8178   -913    878   1510       C  
ATOM     19  N   ILE M  31      23.112   5.750  20.562  1.00 63.67           N  
ANISOU   19  N   ILE M  31     8652   7343   8196   -821    109   1121       N  
ATOM     20  CA  ILE M  31      22.027   5.511  21.504  1.00 63.84           C  
ANISOU   20  CA  ILE M  31     8702   7380   8176   -798    176    939       C  
ATOM     21  C   ILE M  31      20.931   4.699  20.825  1.00 63.80           C  
ANISOU   21  C   ILE M  31     8653   7435   8151   -827    319    822       C  
ATOM     22  O   ILE M  31      20.363   5.136  19.825  1.00 64.06           O  
ANISOU   22  O   ILE M  31     8625   7485   8230   -831    224    792       O  
ATOM     23  CB  ILE M  31      21.405   6.848  22.000  1.00 67.17           C  
ANISOU   23  CB  ILE M  31     9104   7749   8670   -755     12    827       C  
ATOM     24  CG1 ILE M  31      22.490   7.885  22.315  1.00 65.68           C  
ANISOU   24  CG1 ILE M  31     8937   7482   8535   -745   -185    942       C  
ATOM     25  CG2 ILE M  31      20.506   6.614  23.210  1.00 65.99           C  
ANISOU   25  CG2 ILE M  31     9008   7589   8475   -734    136    642       C  
ATOM     26  CD1 ILE M  31      21.954   9.258  22.651  1.00 65.63           C  
ANISOU   26  CD1 ILE M  31     8920   7397   8621   -703   -348    839       C  
ATOM     27  N   PHE M  32      20.632   3.520  21.360  1.00 63.76           N  
ANISOU   27  N   PHE M  32     8692   7449   8085   -850    529    759       N  
ATOM     28  CA  PHE M  32      19.558   2.700  20.805  1.00 67.10           C  
ANISOU   28  CA  PHE M  32     9058   7912   8523   -896    669    624       C  
ATOM     29  C   PHE M  32      18.190   3.330  21.065  1.00 66.24           C  
ANISOU   29  C   PHE M  32     8844   7797   8529   -877    627    425       C  
ATOM     30  O   PHE M  32      17.904   3.780  22.176  1.00 66.76           O  
ANISOU   30  O   PHE M  32     8936   7820   8611   -843    661    345       O  
ATOM     31  CB  PHE M  32      19.600   1.280  21.374  1.00 64.02           C  
ANISOU   31  CB  PHE M  32     8747   7514   8064   -933    928    612       C  
ATOM     32  CG  PHE M  32      20.721   0.429  20.832  1.00 63.52           C  
ANISOU   32  CG  PHE M  32     8742   7446   7946   -949   1002    775       C  
ATOM     33  CD1 PHE M  32      20.474  -0.525  19.854  1.00 63.61           C  
ANISOU   33  CD1 PHE M  32     8742   7477   7949  -1009   1133    740       C  
ATOM     34  CD2 PHE M  32      22.019   0.567  21.316  1.00 63.30           C  
ANISOU   34  CD2 PHE M  32     8772   7380   7900   -905    941    949       C  
ATOM     35  CE1 PHE M  32      21.499  -1.325  19.361  1.00 63.44           C  
ANISOU   35  CE1 PHE M  32     8776   7431   7898  -1016   1243    872       C  
ATOM     36  CE2 PHE M  32      23.049  -0.229  20.832  1.00 63.20           C  
ANISOU   36  CE2 PHE M  32     8774   7343   7897   -907   1032   1090       C  
ATOM     37  CZ  PHE M  32      22.789  -1.176  19.850  1.00 63.25           C  
ANISOU   37  CZ  PHE M  32     8779   7363   7891   -959   1204   1051       C  
TER      38      PHE M  32                                                      
ENDMDL                                                                          
MASTER        0    0    0   20   34    0   15    6 5979   13    0   66          
END                                                                             
