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LongText Report for: 5i9i-pdb

Name Class
5i9i-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           20-FEB-16   5I9I              
TITLE     CRYSTAL STRUCTURE OF LP_PLA2 IN COMPLEX WITH DARAPLADIB               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 47-429;                                       
COMPND   5 SYNONYM: PAF ACETYLHYDROLASE,1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE   
COMPND   6 ESTERASE,2-ACETYL-1-ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA   
COMPND   7 PHOSPHOLIPASE A2,GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-     
COMPND   8 PLA(2),PAF 2-ACYLHYDROLASE;                                          
COMPND   9 EC: 3.1.1.47;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLA2G7, PAFAH;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    LP_PLA2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.F.LIU,Y.C.XU                                                        
REVDAT   1   15-JUN-16 5I9I    0                                                
JRNL        AUTH   Q.F.LIU,X.D.CHEN,W.Y.CHEN,X.J.YUAN,H.X.SU,J.H.SHEN,Y.C.XU    
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF             
JRNL        TITL 2 PROTEIN-LIGAND INTERACTIONS FORMED BETWEEN                   
JRNL        TITL 3 LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 AND INHIBITORS       
JRNL        REF    J.MED.CHEM.                   V.  59  5115 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27078579                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00282                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.930                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22260                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 668                             
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 44.0703 -  5.6126    0.95     4559   140  0.1925 0.2514        
REMARK   3     2  5.6126 -  4.4563    0.94     4438   138  0.1668 0.2395        
REMARK   3     3  4.4563 -  3.8934    0.94     4483   140  0.1615 0.1852        
REMARK   3     4  3.8934 -  3.5376    0.95     4523   135  0.1682 0.2490        
REMARK   3     5  3.5376 -  3.2841    0.96     4564   140  0.1880 0.2851        
REMARK   3     6  3.2841 -  3.0905    0.97     4597   144  0.2128 0.2880        
REMARK   3     7  3.0905 -  2.9358    0.97     4668   144  0.2268 0.3068        
REMARK   3     8  2.9358 -  2.8080    0.97     4654   141  0.2371 0.3835        
REMARK   3     9  2.8080 -  2.6999    0.97     4630   138  0.2540 0.3216        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.12                          
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      :  0.009           5789                                  
REMARK   3   ANGLE     :  1.208           7884                                  
REMARK   3   CHIRALITY :  0.046            848                                  
REMARK   3   PLANARITY :  0.006           1021                                  
REMARK   3   DIHEDRAL  : 15.192           1980                                  
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 5I9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218473.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22260                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.064                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 1.960                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.5900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3D59                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.6, 0.4M LI2SO4, 27%       
REMARK 280  (W/V) (NH4)2SO4, 1M NA-AC, 1.4% 1,4-BUTANEDIOL, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       57.95000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.95000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.20500            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 110 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
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     GLY A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     THR A   425                                                      
REMARK 465     ASN A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     ILE A   429                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     THR B    54                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     ASN B    90                                                      
REMARK 465     ASP B    91                                                      
REMARK 465     ARG B    92                                                      
REMARK 465     LEU B    93                                                      
REMARK 465     ASP B   338                                                      
REMARK 465     THR B   424                                                      
REMARK 465     THR B   425                                                      
REMARK 465     ASN B   426                                                      
REMARK 465     GLN B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     ILE B   429                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A  54    OG1  CG2                                            
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     SER A  64    OG                                                  
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     GLN A  88    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     ASP A  91    CG   OD1  OD2                                       
REMARK 470     ARG A  92    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     THR A 113    OG1  CG2                                            
REMARK 470     HIS A 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP A 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 115    CZ3  CH2                                            
REMARK 470     LEU A 116    CG   CD1  CD2                                       
REMARK 470     MET A 117    CG   SD   CE                                        
REMARK 470     ASN A 119    OD1  ND2                                            
REMARK 470     ILE A 120    CG1  CG2  CD1                                       
REMARK 470     LEU A 123    CG   CD1  CD2                                       
REMARK 470     LEU A 124    CG   CD1  CD2                                       
REMARK 470     SER A 127    OG                                                  
REMARK 470     THR A 129    OG1  CG2                                            
REMARK 470     LYS A 143    CE   NZ                                             
REMARK 470     VAL A 174    CG1  CG2                                            
REMARK 470     SER A 194    OG                                                  
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     GLN A 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 212    OE1  OE2                                            
REMARK 470     GLU A 220    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 227    CG   CD   CE   NZ                                   
REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     ASP A 250    CG   OD1  OD2                                       
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 259    CD   CE   NZ                                        
REMARK 470     GLU A 285    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 304    CG   OD1  OD2                                       
REMARK 470     LYS A 330    NZ                                                  
REMARK 470     LYS A 333    CE   NZ                                             
REMARK 470     ARG A 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 361    OG1  CG2                                            
REMARK 470     LYS A 363    CG   CD   CE   NZ                                   
REMARK 470     ILE A 364    CG1  CG2  CD1                                       
REMARK 470     ILE A 365    CG1  CG2  CD1                                       
REMARK 470     MET A 368    CG   SD   CE                                        
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     LYS A 394    CG   CD   CE   NZ                                   
REMARK 470     LYS A 400    CE   NZ                                             
REMARK 470     GLU A 414    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 417    CD1                                                 
REMARK 470     ASN A 423    CG   OD1  ND2                                       
REMARK 470     THR A 424    OG1  CG2                                            
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     ARG B  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  64    OG                                                  
REMARK 470     SER B  87    OG                                                  
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     HIS B 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP B 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 115    CZ3  CH2                                            
REMARK 470     LEU B 116    CG   CD1  CD2                                       
REMARK 470     LEU B 123    CG   CD1  CD2                                       
REMARK 470     LEU B 124    CD1  CD2                                            
REMARK 470     SER B 127    OG                                                  
REMARK 470     ASN B 133    CG   OD1  ND2                                       
REMARK 470     SER B 136    OG                                                  
REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
REMARK 470     ASP B 192    OD1  OD2                                            
REMARK 470     GLN B 193    CG   CD   OE1  NE2                                  
REMARK 470     SER B 194    OG                                                  
REMARK 470     ILE B 198    CG1  CG2  CD1                                       
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     GLN B 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 212    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 214    CG   CD   OE1  OE2                                  
REMARK 470     THR B 215    OG1  CG2                                            
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ASP B 250    CG   OD1  OD2                                       
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     GLU B 256    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 304    CG   OD1  OD2                                       
REMARK 470     GLU B 305    CG   CD   OE1  OE2                                  
REMARK 470     SER B 308    OG                                                  
REMARK 470     ARG B 309    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 329    CG1  CG2  CD1                                       
REMARK 470     LYS B 330    CD   CE   NZ                                        
REMARK 470     LYS B 332    CG   CD   CE   NZ                                   
REMARK 470     LYS B 333    CE   NZ                                             
REMARK 470     SER B 336    OG                                                  
REMARK 470     LYS B 339    CG   CD   CE   NZ                                   
REMARK 470     LYS B 342    CG   CD   CE   NZ                                   
REMARK 470     ARG B 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 363    CG   CD   CE   NZ                                   
REMARK 470     ILE B 364    CG1  CG2  CD1                                       
REMARK 470     ILE B 365    CD1                                                 
REMARK 470     MET B 368    CG   SD   CE                                        
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     ILE B 375    CG1  CG2  CD1                                       
REMARK 470     ASN B 378    CG   OD1  ND2                                       
REMARK 470     VAL B 379    CG1  CG2                                            
REMARK 470     LYS B 386    CE   NZ                                             
REMARK 470     LYS B 394    CD   CE   NZ                                        
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     ASP B 401    CG   OD1  OD2                                       
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 416    CG   CD1  CD2                                       
REMARK 470     ILE B 417    CD1                                                 
REMARK 470     ASN B 421    CG   OD1  ND2                                       
REMARK 470     ILE B 422    CG1  CG2  CD1                                       
REMARK 470     ASN B 423    CG   OD1  ND2                                       
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    ASP A  73     -167.81    -71.16                                   
REMARK 500    THR A 113      170.49    -49.26                                   
REMARK 500    HIS A 114     -106.87   -100.36                                   
REMARK 500    PRO A 131       68.82    -68.64                                   
REMARK 500    ALA A 155     -169.64   -111.03                                   
REMARK 500    MET A 255      -17.76    -47.64                                   
REMARK 500    SER A 273     -110.58     62.88                                   
REMARK 500    ASP A 296       64.99     36.18                                   
REMARK 500    ILE A 364      -70.45    -66.82                                   
REMARK 500    HIS A 399       67.66   -105.91                                   
REMARK 500    TRP B 115        0.29    -68.40                                   
REMARK 500    PRO B 131       75.88    -65.88                                   
REMARK 500    LYS B 266       77.15   -114.52                                   
REMARK 500    SER B 273     -108.55     55.61                                   
REMARK 500    ARG B 309       37.58   -141.53                                   
REMARK 500    LYS B 370       32.08     70.71                                   
REMARK 500    HIS B 399       77.70   -108.22                                   
REMARK 500    ASP B 413      140.05    -18.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HV A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HV B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5I8P   RELATED DB: PDB                                   
DBREF  5I9I A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  5I9I B   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
SEQADV 5I9I GLY A   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I PRO A   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I LEU A   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I GLY A   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I SER A   46  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I GLY B   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I PRO B   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I LEU B   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I GLY B   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5I9I SER B   46  UNP  Q13093              EXPRESSION TAG                 
SEQRES   1 A  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 A  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 A  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 A  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 A  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 A  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 A  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 A  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 A  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 A  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 A  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 A  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 A  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 A  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 A  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 A  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 A  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 A  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 A  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 A  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 A  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 A  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 A  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 A  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 A  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 A  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 A  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 A  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 A  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 A  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
SEQRES   1 B  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 B  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 B  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 B  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 B  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 B  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 B  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 B  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 B  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 B  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 B  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 B  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 B  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 B  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 B  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 B  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 B  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 B  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 B  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 B  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 B  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 B  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 B  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 B  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 B  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 B  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 B  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 B  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 B  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 B  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
HET    5HV  A 501      47                                                       
HET    5HV  B 501      47                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HETNAM     5HV N-[2-(DIETHYLAMINO)ETHYL]-2-{2-[(4-FLUOROBENZYL)                 
HETNAM   2 5HV  SULFANYL]-4-OXO-4,5,6,7-TETRAHYDRO-1H-                          
HETNAM   3 5HV  CYCLOPENTA[D]PYRIMIDIN-1-YL}-N-{[4'-(TRIFLUOROMETHYL)           
HETNAM   4 5HV  BIPHENYL-4-YL]METHYL}ACETAMIDE                                  
HETNAM     SO4 SULFATE ION                                                      
HETSYN     5HV DARAPLADIB                                                       
FORMUL   3  5HV    2(C36 H38 F4 N4 O2 S)                                        
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *6(H2 O)                                                      
HELIX    1 AA1 ASN A  100  GLY A  112  1                                  13    
HELIX    2 AA2 TRP A  115  GLY A  126  1                                  12    
HELIX    3 AA3 TYR A  160  SER A  169  1                                  10    
HELIX    4 AA4 ASP A  192  GLY A  199  1                                   8    
HELIX    5 AA5 LYS A  210  GLU A  212  5                                   3    
HELIX    6 AA6 GLU A  213  HIS A  241  1                                  29    
HELIX    7 AA7 ASP A  254  LYS A  259  5                                   6    
HELIX    8 AA8 SER A  273  ASP A  286  1                                  14    
HELIX    9 AA9 VAL A  306  ILE A  310  5                                   5    
HELIX   10 AB1 TYR A  324  LYS A  333  1                                  10    
HELIX   11 AB2 VAL A  350  ALA A  360  5                                  11    
HELIX   12 AB3 GLY A  362  LEU A  369  1                                   8    
HELIX   13 AB4 ASP A  376  GLY A  397  1                                  22    
HELIX   14 AB5 ASP A  401  GLN A  404  5                                   4    
HELIX   15 AB6 TRP A  405  GLU A  410  1                                   6    
HELIX   16 AB7 ASN B  100  GLY B  112  1                                  13    
HELIX   17 AB8 HIS B  114  GLY B  126  1                                  13    
HELIX   18 AB9 PHE B  156  LEU B  159  5                                   4    
HELIX   19 AC1 TYR B  160  SER B  169  1                                  10    
HELIX   20 AC2 ASP B  192  ILE B  198  1                                   7    
HELIX   21 AC3 LYS B  210  GLU B  212  5                                   3    
HELIX   22 AC4 GLU B  213  HIS B  241  1                                  29    
HELIX   23 AC5 ASP B  254  LYS B  259  5                                   6    
HELIX   24 AC6 SER B  273  ASP B  286  1                                  14    
HELIX   25 AC7 TYR B  324  LYS B  333  1                                  10    
HELIX   26 AC8 VAL B  350  PHE B  354  5                                   5    
HELIX   27 AC9 ALA B  355  PHE B  359  5                                   5    
HELIX   28 AD1 GLY B  362  LEU B  369  1                                   8    
HELIX   29 AD2 ASP B  376  GLY B  397  1                                  22    
HELIX   30 AD3 LYS B  400  GLN B  404  5                                   5    
HELIX   31 AD4 TRP B  405  GLY B  411  1                                   7    
SHEET    1 AA110 ASN A 133  TRP A 134  0                                        
SHEET    2 AA110 SER A  64  PHE A  72  1  N  VAL A  65   O  ASN A 133           
SHEET    3 AA110 THR A  79  SER A  87 -1  O  TYR A  85   N  GLY A  66           
SHEET    4 AA110 ILE A 173  VAL A 177 -1  O  ALA A 176   N  ARG A  82           
SHEET    5 AA110 TYR A 144  SER A 150  1  N  VAL A 147   O  ALA A 175           
SHEET    6 AA110 ILE A 262  HIS A 272  1  O  ALA A 268   N  VAL A 148           
SHEET    7 AA110 CYS A 291  LEU A 295  1  O  LEU A 295   N  GLY A 271           
SHEET    8 AA110 LEU A 314  SER A 319  1  O  PHE A 315   N  ALA A 294           
SHEET    9 AA110 ARG A 341  ILE A 346  1  O  LYS A 342   N  PHE A 316           
SHEET   10 AA110 LEU A 416  PRO A 418 -1  O  ILE A 417   N  THR A 345           
SHEET    1 AA2 2 THR A  95  LEU A  96  0                                        
SHEET    2 AA2 2 THR A 129  THR A 130 -1  O  THR A 130   N  THR A  95           
SHEET    1 AA3 2 ALA A 186  TYR A 189  0                                        
SHEET    2 AA3 2 SER A 202  TYR A 205 -1  O  LEU A 204   N  THR A 187           
SHEET    1 AA410 ASN B 133  TRP B 134  0                                        
SHEET    2 AA410 SER B  64  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3 AA410 THR B  79  SER B  87 -1  O  SER B  87   N  SER B  64           
SHEET    4 AA410 ILE B 173  VAL B 177 -1  O  ALA B 176   N  ARG B  82           
SHEET    5 AA410 TYR B 144  SER B 150  1  N  VAL B 147   O  ALA B 175           
SHEET    6 AA410 ILE B 262  HIS B 272  1  O  LYS B 266   N  LEU B 146           
SHEET    7 AA410 CYS B 291  LEU B 295  1  O  LEU B 295   N  GLY B 271           
SHEET    8 AA410 LEU B 314  SER B 319  1  O  PHE B 315   N  ALA B 294           
SHEET    9 AA410 ARG B 341  ILE B 346  1  O  LYS B 342   N  PHE B 316           
SHEET   10 AA410 LEU B 416  PRO B 418 -1  O  ILE B 417   N  THR B 345           
SHEET    1 AA5 2 THR B  95  LEU B  96  0                                        
SHEET    2 AA5 2 THR B 129  THR B 130 -1  O  THR B 130   N  THR B  95           
SHEET    1 AA6 2 ALA B 186  TYR B 189  0                                        
SHEET    2 AA6 2 SER B 202  TYR B 205 -1  O  LEU B 204   N  THR B 187           
CISPEP   1 PHE A   72    ASP A   73          0        -6.36                     
CISPEP   2 PHE B   72    ASP B   73          0        -7.57                     
SITE     1 AC1 17 LEU A 107  PHE A 110  LEU A 111  LEU A 121                    
SITE     2 AC1 17 GLY A 152  LEU A 153  GLY A 154  LEU A 159                    
SITE     3 AC1 17 TYR A 160  SER A 273  PHE A 274  TRP A 298                    
SITE     4 AC1 17 HIS A 351  GLN A 352  PHE A 357  LEU A 369                    
SITE     5 AC1 17 LEU A 371                                                     
SITE     1 AC2 16 LEU B 107  PHE B 110  LEU B 111  LEU B 121                    
SITE     2 AC2 16 GLY B 152  LEU B 153  GLY B 154  ALA B 155                    
SITE     3 AC2 16 LEU B 159  SER B 273  PHE B 274  TRP B 298                    
SITE     4 AC2 16 HIS B 351  GLN B 352  PHE B 357  LEU B 369                    
SITE     1 AC3  6 GLN A  88  ASP A  89  ASN A  90  ASN B 100                    
SITE     2 AC3  6 LYS B 101  ARG B 122                                          
SITE     1 AC4  1 ARG B 207                                                     
CRYST1  115.900   82.410   96.470  90.00 115.50  90.00 C 1 2 1       8          
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      0.008628  0.000000  0.004115        0.00000                         
SCALE2      0.000000  0.012134  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011484        0.00000                         
TER    2814      THR A 424                                                      
TER    5541      ASN B 423                                                      
MASTER      435    0    4   31   28    0   12    6 5649    2  104   60          
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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