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LongText Report for: 7w6c-pdb

Name Class
7w6c-pdb
HEADER    HYDROLASE                               01-DEC-21   7W6C              
TITLE     CRYSTAL STRUCTURE OF A PSH1 IN COMPLEX WITH LIGAND J1K                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PSH1;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE   3 ORGANISM_TAXID: 32644;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    ALPHA/BETA DEHYDROGENASE, PLASTIC DEGRADATION, THERMO-STABLE,         
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GAO,P.LARA,Z.S.LI,X.HAN,R.WEI,W.D.LIU                               
REVDAT   1   14-SEP-22 7W6C    0                                                
JRNL        AUTH   L.PFAFF,J.GAO,Z.LI,A.JACKERING,G.WEBER,J.MICAN,Y.CHEN,       
JRNL        AUTH 2 W.DONG,X.HAN,C.G.FEILER,Y.F.AO,C.P.S.BADENHORST,D.BEDNAR,    
JRNL        AUTH 3 G.J.PALM,M.LAMMERS,J.DAMBORSKY,B.STRODEL,W.LIU,              
JRNL        AUTH 4 U.T.BORNSCHEUER,R.WEI                                        
JRNL        TITL   MULTIPLE SUBSTRATE BINDING MODE-GUIDED ENGINEERING OF A      
JRNL        TITL 2 THERMOPHILIC PET HYDROLASE.                                  
JRNL        REF    ACS CATALYSIS                 V.  12  9790 2022              
JRNL        REFN                   ESSN 2155-5435                               
JRNL        PMID   35966606                                                     
JRNL        DOI    10.1021/ACSCATAL.2C02275                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.450                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50889                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2616                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5800 -  4.9500    0.99     4865   273  0.1855 0.2261        
REMARK   3     2  4.9500 -  3.9300    1.00     4922   257  0.1927 0.2277        
REMARK   3     3  3.9300 -  3.4300    1.00     4872   252  0.2217 0.2579        
REMARK   3     4  3.4300 -  3.1200    0.99     4825   274  0.2561 0.3217        
REMARK   3     5  3.1200 -  2.9000    0.99     4871   266  0.2727 0.3443        
REMARK   3     6  2.9000 -  2.7300    0.99     4871   276  0.2719 0.3429        
REMARK   3     7  2.7300 -  2.5900    0.99     4795   268  0.2586 0.3155        
REMARK   3     8  2.5900 -  2.4800    0.97     4731   256  0.2529 0.3073        
REMARK   3     9  2.4800 -  2.3800    0.97     4723   258  0.2657 0.3603        
REMARK   3    10  2.3800 -  2.3000    0.96     4798   236  0.2843 0.3114        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7W6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-DEC-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300026066.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51681                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 7NEI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PEG 1500, NAAC, PH 8.0, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       28.00550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ALA B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  33       46.08    -98.78                                   
REMARK 500    THR A  63       -9.71     76.08                                   
REMARK 500    SER A 130     -123.50     61.18                                   
REMARK 500    ALA A 179       70.31   -119.74                                   
REMARK 500    HIS A 184      -95.18   -130.93                                   
REMARK 500    PRO A 214      120.24    -37.54                                   
REMARK 500    PRO A 242     -151.12    -72.26                                   
REMARK 500    ASP A 246      -85.79   -118.94                                   
REMARK 500    PHE A 247      -46.39     77.86                                   
REMARK 500    THR B  63       -5.79     64.34                                   
REMARK 500    SER B 130     -125.68     57.51                                   
REMARK 500    ASN B 143       91.64   -160.35                                   
REMARK 500    ALA B 179       75.48   -110.68                                   
REMARK 500    HIS B 184      -96.66   -118.76                                   
REMARK 500    ALA B 199      143.30   -170.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7W6C A    1   258  PDB    7W6C     7W6C             1    258             
DBREF  7W6C B    1   258  PDB    7W6C     7W6C             1    258             
SEQRES   1 A  258  ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER          
SEQRES   2 A  258  SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN          
SEQRES   3 A  258  THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY GLY          
SEQRES   4 A  258  GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR          
SEQRES   5 A  258  PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY          
SEQRES   6 A  258  GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER          
SEQRES   7 A  258  GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR ARG          
SEQRES   8 A  258  LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN ALA          
SEQRES   9 A  258  ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG ASN          
SEQRES  10 A  258  ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER          
SEQRES  11 A  258  MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN ASN          
SEQRES  12 A  258  THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP HIS          
SEQRES  13 A  258  THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR LEU          
SEQRES  14 A  258  VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL SER          
SEQRES  15 A  258  SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER ASP          
SEQRES  16 A  258  LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS          
SEQRES  17 A  258  LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS TYR          
SEQRES  18 A  258  SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP LEU          
SEQRES  19 A  258  ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PHE          
SEQRES  20 A  258  ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE                  
SEQRES   1 B  258  ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER          
SEQRES   2 B  258  SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN          
SEQRES   3 B  258  THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY GLY          
SEQRES   4 B  258  GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR          
SEQRES   5 B  258  PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY          
SEQRES   6 B  258  GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER          
SEQRES   7 B  258  GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR ARG          
SEQRES   8 B  258  LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN ALA          
SEQRES   9 B  258  ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG ASN          
SEQRES  10 B  258  ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER          
SEQRES  11 B  258  MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN ASN          
SEQRES  12 B  258  THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP HIS          
SEQRES  13 B  258  THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR LEU          
SEQRES  14 B  258  VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL SER          
SEQRES  15 B  258  SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER ASP          
SEQRES  16 B  258  LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS          
SEQRES  17 B  258  LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS TYR          
SEQRES  18 B  258  SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP LEU          
SEQRES  19 B  258  ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PHE          
SEQRES  20 B  258  ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE                  
HET    J1K  A 301      15                                                       
HET    J1K  B 301      15                                                       
HETNAM     J1K 4-(2-HYDROXYETHYLCARBAMOYL)BENZOIC ACID                          
FORMUL   3  J1K    2(C10 H11 N O4)                                              
FORMUL   5  HOH   *165(H2 O)                                                    
HELIX    1 AA1 SER A   13  ALA A   17  5                                   5    
HELIX    2 AA2 GLY A   65  ALA A   70  5                                   6    
HELIX    3 AA3 TRP A   71  SER A   78  1                                   8    
HELIX    4 AA4 GLN A   94  ARG A  110  1                                  17    
HELIX    5 AA5 VAL A  115  ASN A  117  5                                   3    
HELIX    6 AA6 SER A  130  ASN A  142  1                                  13    
HELIX    7 AA7 HIS A  184  ASN A  190  1                                   7    
HELIX    8 AA8 SER A  207  THR A  213  5                                   7    
HELIX    9 AA9 ASP A  215  ASP A  231  1                                  17    
HELIX   10 AB1 ASP A  233  LEU A  240  5                                   8    
HELIX   11 AB2 THR B   11  ALA B   17  1                                   7    
HELIX   12 AB3 GLY B   65  ALA B   70  5                                   6    
HELIX   13 AB4 TRP B   71  SER B   78  1                                   8    
HELIX   14 AB5 GLN B   94  ASN B  112  1                                  19    
HELIX   15 AB6 SER B  130  ASN B  142  1                                  13    
HELIX   16 AB7 HIS B  184  LEU B  192  1                                   9    
HELIX   17 AB8 SER B  207  THR B  213  5                                   7    
HELIX   18 AB9 ASP B  215  ASP B  231  1                                  17    
HELIX   19 AC1 ASP B  233  LEU B  240  5                                   8    
SHEET    1 AA1 6 VAL A  24  VAL A  29  0                                        
SHEET    2 AA1 6 GLY A  40  PRO A  45 -1  O  ILE A  42   N  THR A  27           
SHEET    3 AA1 6 VAL A  82  ILE A  86 -1  O  VAL A  83   N  TYR A  43           
SHEET    4 AA1 6 PHE A  53  SER A  59  1  N  VAL A  56   O  VAL A  82           
SHEET    5 AA1 6 ILE A 119  HIS A 129  1  O  ALA A 125   N  ALA A  57           
SHEET    6 AA1 6 ALA A 148  LEU A 152  1  O  LEU A 152   N  GLY A 128           
SHEET    1 AA2 3 THR A 168  ALA A 173  0                                        
SHEET    2 AA2 3 LYS A 198  LEU A 203  1  O  LEU A 203   N  GLY A 172           
SHEET    3 AA2 3 ILE A 249  SER A 254 -1  O  GLU A 251   N  GLU A 202           
SHEET    1 AA3 6 VAL B  24  VAL B  29  0                                        
SHEET    2 AA3 6 GLY B  40  PRO B  45 -1  O  ILE B  42   N  THR B  27           
SHEET    3 AA3 6 PHE B  81  ILE B  86 -1  O  VAL B  83   N  TYR B  43           
SHEET    4 AA3 6 PHE B  53  SER B  59  1  N  VAL B  56   O  VAL B  82           
SHEET    5 AA3 6 ILE B 119  HIS B 129  1  O  MET B 127   N  SER B  59           
SHEET    6 AA3 6 ALA B 148  LEU B 152  1  O  LEU B 152   N  GLY B 128           
SHEET    1 AA4 3 THR B 168  ALA B 173  0                                        
SHEET    2 AA4 3 LYS B 198  LEU B 203  1  O  MET B 201   N  VAL B 170           
SHEET    3 AA4 3 ILE B 249  SER B 254 -1  O  ARG B 253   N  TYR B 200           
SSBOND   1 CYS A  241    CYS A  256                          1555   1555  1.99  
SSBOND   2 CYS B  241    CYS B  256                          1555   1555  2.02  
CISPEP   1 CYS A  241    PRO A  242          0       -17.90                     
CISPEP   2 CYS A  256    PRO A  257          0        -0.61                     
CISPEP   3 CYS B  241    PRO B  242          0         3.52                     
CISPEP   4 CYS B  256    PRO B  257          0        -4.43                     
CRYST1   52.506   56.011  102.321  90.00  94.42  90.00 P 1 21 1      4          
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      0.019045  0.000000  0.001471        0.00000                         
SCALE2      0.000000  0.017854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009802        0.00000                         
TER    1957      PHE A 258                                                      
TER    3914      PHE B 258                                                      
MASTER      236    0    2   19   18    0    0    6 4107    2   34   40          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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