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LongText Report for: 6m08-pdb

Name Class
6m08-pdb
HEADER    HYDROLASE                               20-FEB-20   6M08              
TITLE     CRYSTAL STRUCTURE OF LP-PLA2 IN COMPLEX WITH A NOVEL COVALENT         
TITLE    2 INHIBITOR.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PAF ACETYLHYDROLASE,1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE   
COMPND   5 ESTERASE,2-ACETYL-1-ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA   
COMPND   6 PHOSPHOLIPASE A2,GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-     
COMPND   7 PLA(2),PAF 2-ACYLHYDROLASE;                                          
COMPND   8 EC: 3.1.1.47;                                                        
COMPND   9 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    LP-PLA2, COVALENT INHIBITOR, COMPLEX STRUCTURE, SERINE                
KEYWDS   2 PHOSPHOLIPASE., HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.C.HU,Y.C.XU                                                         
REVDAT   2   13-JAN-21 6M08    1       COMPND REMARK HETNAM FORMUL              
REVDAT   2 2                   1       LINK                                     
REVDAT   1   30-DEC-20 6M08    0                                                
JRNL        AUTH   F.HUANG,H.HU,K.WANG,C.PENG,W.XU,Y.ZHANG,J.GAO,Y.LIU,H.ZHOU,  
JRNL        AUTH 2 R.HUANG,M.LI,J.SHEN,Y.XU                                     
JRNL        TITL   IDENTIFICATION OF HIGHLY SELECTIVE LIPOPROTEIN-ASSOCIATED    
JRNL        TITL 2 PHOSPHOLIPASE A2 (LP-PLA2) INHIBITORS BY A COVALENT          
JRNL        TITL 3 FRAGMENT-BASED APPROACH.                                     
JRNL        REF    J.MED.CHEM.                   V.  63  7052 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   32459096                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.0C00372                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0232                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37721                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1952                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1413                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5768                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 59                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34000                                             
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.281         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.213         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5950 ; 0.009 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  5322 ; 0.003 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8080 ; 1.565 ; 1.644       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12297 ; 1.387 ; 1.583       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   739 ; 7.793 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   303 ;35.613 ;22.376       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   939 ;15.248 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;18.419 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   782 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6748 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1315 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6M08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300015782.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42102                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.05600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
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: 5I9I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MOPS PH 6.6, 0.4 M LI2SO4, 22.5    
REMARK 280  -27% (W/V) (NH4)2SO4, 1 M NA-AC, 1.4 % 1,4-BUTANEDIOL, VAPOR        
REMARK 280  DIFFUSION, 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       58.17300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.17250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.17300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.17250            
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 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     THR A   424                                                      
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     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     ASP A  91    CG   OD1  OD2                                       
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     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     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     ARG A 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 363    CG   CD   CE   NZ                                   
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     GLU A 414    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 417    CD1                                                 
REMARK 470     THR B  54    OG1  CG2                                            
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  90    CG   OD1  ND2                                       
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     HIS B 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 116    CG   CD1  CD2                                       
REMARK 470     ASN B 133    CG   OD1  ND2                                       
REMARK 470     SER B 194    OG                                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     GLN B 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 212    OE1  OE2                                            
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ASP B 250    CG   OD1  OD2                                       
REMARK 470     LYS B 259    CD   CE   NZ                                        
REMARK 470     ASP B 304    CG   OD1  OD2                                       
REMARK 470     GLU B 305    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 330    NZ                                                  
REMARK 470     LYS B 333    CE   NZ                                             
REMARK 470     ASP B 338    CG   OD1  OD2                                       
REMARK 470     ARG B 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 368    CG   SD   CE                                        
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     LYS B 400    CE   NZ                                             
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 417    CD1                                                 
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     -177.47    -69.30                                   
REMARK 500    ASN A  90       59.70   -118.84                                   
REMARK 500    HIS A 114     -163.34   -107.37                                   
REMARK 500    LYS A 266       77.58   -115.72                                   
REMARK 500    SER A 273     -108.53     68.43                                   
REMARK 500    HIS A 399       56.45   -107.65                                   
REMARK 500    LYS A 400     -168.78   -121.84                                   
REMARK 500    ASP B  73     -169.63    -76.96                                   
REMARK 500    GLN B  88      -79.01    -79.22                                   
REMARK 500    ASP B  91      -72.79    -70.35                                   
REMARK 500    LEU B  93       69.85   -117.21                                   
REMARK 500    HIS B 114      172.25    -52.29                                   
REMARK 500    LYS B 252       48.08    -85.94                                   
REMARK 500    LYS B 266       70.59   -112.17                                   
REMARK 500    SER B 273     -117.16     63.10                                   
REMARK 500    SER B 336      135.62   -171.52                                   
REMARK 500    HIS B 399       59.07   -114.28                                   
REMARK 500    GLN B 404      -35.51    -32.95                                   
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 BWL B 501                 
DBREF  6M08 A   54   424  UNP    Q13093   PAFA_HUMAN      54    424             
DBREF  6M08 B   54   424  UNP    Q13093   PAFA_HUMAN      54    424             
SEQRES   1 A  371  THR LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY          
SEQRES   2 A  371  CYS THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR          
SEQRES   3 A  371  PHE LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG          
SEQRES   4 A  371  LEU ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP          
SEQRES   5 A  371  GLY LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY          
SEQRES   6 A  371  ASN ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO          
SEQRES   7 A  371  ALA ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR          
SEQRES   8 A  371  PRO LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG          
SEQRES   9 A  371  THR LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS          
SEQRES  10 A  371  GLY PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER          
SEQRES  11 A  371  ALA SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA          
SEQRES  12 A  371  GLU ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU          
SEQRES  13 A  371  LYS GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL          
SEQRES  14 A  371  ARG GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU          
SEQRES  15 A  371  ILE LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA          
SEQRES  16 A  371  LEU ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER          
SEQRES  17 A  371  ILE ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE          
SEQRES  18 A  371  GLY GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN          
SEQRES  19 A  371  ARG PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE          
SEQRES  20 A  371  PRO LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO          
SEQRES  21 A  371  LEU PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA          
SEQRES  22 A  371  ASN ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS          
SEQRES  23 A  371  GLU ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN          
SEQRES  24 A  371  ASN PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE          
SEQRES  25 A  371  GLY HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN          
SEQRES  26 A  371  VAL ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE          
SEQRES  27 A  371  LEU GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN          
SEQRES  28 A  371  TRP ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE          
SEQRES  29 A  371  PRO GLY THR ASN ILE ASN THR                                  
SEQRES   1 B  371  THR LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY          
SEQRES   2 B  371  CYS THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR          
SEQRES   3 B  371  PHE LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG          
SEQRES   4 B  371  LEU ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP          
SEQRES   5 B  371  GLY LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY          
SEQRES   6 B  371  ASN ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO          
SEQRES   7 B  371  ALA ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR          
SEQRES   8 B  371  PRO LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG          
SEQRES   9 B  371  THR LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS          
SEQRES  10 B  371  GLY PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER          
SEQRES  11 B  371  ALA SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA          
SEQRES  12 B  371  GLU ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU          
SEQRES  13 B  371  LYS GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL          
SEQRES  14 B  371  ARG GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU          
SEQRES  15 B  371  ILE LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA          
SEQRES  16 B  371  LEU ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER          
SEQRES  17 B  371  ILE ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE          
SEQRES  18 B  371  GLY GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN          
SEQRES  19 B  371  ARG PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE          
SEQRES  20 B  371  PRO LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO          
SEQRES  21 B  371  LEU PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA          
SEQRES  22 B  371  ASN ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS          
SEQRES  23 B  371  GLU ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN          
SEQRES  24 B  371  ASN PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE          
SEQRES  25 B  371  GLY HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN          
SEQRES  26 B  371  VAL ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE          
SEQRES  27 B  371  LEU GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN          
SEQRES  28 B  371  TRP ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE          
SEQRES  29 B  371  PRO GLY THR ASN ILE ASN THR                                  
HET    BWL  B 501      37                                                       
HETNAM     BWL (2S)-2-[(Z)-3-[2-(DIETHYLAMINO)ETHYL-[[4-[4-                     
HETNAM   2 BWL  (TRIFLUOROMETHYL)PHENYL]PHENYL]METHYL]AMINO]-1-                 
HETNAM   3 BWL  OXIDANYL-3-OXIDANYLIDENE-PROP-1-ENYL]PYRROLIDINE-1-             
HETNAM   4 BWL  CARBOXYLIC ACID                                                 
FORMUL   3  BWL    C28 H34 F3 N3 O4                                             
FORMUL   4  HOH   *59(H2 O)                                                     
HELIX    1 AA1 ASN A  100  LEU A  111  1                                  12    
HELIX    2 AA2 HIS A  114  GLY A  126  1                                  13    
HELIX    3 AA3 TYR A  160  HIS A  170  1                                  11    
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 GLY A  303  ARG A  309  5                                   7    
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  LYS A  370  1                                   9    
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 TRP B  115  GLY B  126  1                                  12    
HELIX   18 AB9 TYR B  160  SER B  169  1                                  10    
HELIX   19 AC1 ASP B  192  ILE B  198  1                                   7    
HELIX   20 AC2 LYS B  210  GLU B  212  5                                   3    
HELIX   21 AC3 GLU B  213  HIS B  241  1                                  29    
HELIX   22 AC4 ASP B  254  LYS B  259  5                                   6    
HELIX   23 AC5 PHE B  274  ASP B  286  1                                  13    
HELIX   24 AC6 GLY B  303  ARG B  309  5                                   7    
HELIX   25 AC7 TYR B  324  LYS B  333  1                                  10    
HELIX   26 AC8 VAL B  350  ALA B  360  5                                  11    
HELIX   27 AC9 GLY B  362  LEU B  369  1                                   8    
HELIX   28 AD1 ASP B  376  GLY B  397  1                                  22    
HELIX   29 AD2 ASP B  401  GLN B  404  5                                   4    
HELIX   30 AD3 TRP B  405  GLU B  410  1                                   6    
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  SER A  87   N  SER A  64           
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  PHE A 149   O  ALA A 175           
SHEET    6 AA110 ILE A 262  HIS A 272  1  O  ILE A 270   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 VAL B  65  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3 AA410 THR B  79  PRO B  86 -1  O  TYR B  85   N  GLY B  66           
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  ALA B 268   N  VAL B 148           
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  ILE B 317   N  ALA B 294           
SHEET    9 AA410 ARG B 341  ILE B 346  1  O  ILE B 344   N  ASN B 318           
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  SER B 202   N  TYR B 189           
LINK         OG  SER B 273                 C37 BWL B 501     1555   1555  1.67  
CISPEP   1 PHE A   72    ASP A   73          0       -10.03                     
CISPEP   2 PHE B   72    ASP B   73          0        -6.96                     
SITE     1 AC1 11 PHE B 110  LEU B 121  LEU B 153  SER B 273                    
SITE     2 AC1 11 PHE B 274  TRP B 298  PHE B 322  HIS B 351                    
SITE     3 AC1 11 GLN B 352  PHE B 357  LEU B 371                               
CRYST1  116.346   82.345   96.664  90.00 115.73  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      0.008595  0.000000  0.004142        0.00000                         
SCALE2      0.000000  0.012144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011483        0.00000                         
TER    2879      ASN A 423                                                      
TER    5770      THR B 424                                                      
MASTER      348    0    1   30   28    0    3    6 5864    2   38   58          
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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