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LongText Report for: 3D59-pdb

Name Class
3D59-pdb
HEADER    HYDROLASE                               16-MAY-08   3D59              
TITLE     CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING                 
TITLE    2 FACTOR ACETYLHYDROLASE                                               
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, PAF 2-ACYLHYDROLASE, LDL-              
COMPND   6 ASSOCIATED PHOSPHOLIPASE A2, LDL-PLA(2), 2-ACETYL-1-                 
COMPND   7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE, 1-ALKYL-2-                      
COMPND   8 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE;                                
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 GENE: PLA2G7, PAFAH;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PLASMA PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, SECRETED           
KEYWDS   2 PROTEIN, ALPHA/BETA-HYDROLASE-FOLD, LDL-BOUND; LIPOPROTEIN           
KEYWDS   3 ASSOCIATED PHOSPHOLIPASE A2, LP-PLA2, GROUP VIIA PLA2,               
KEYWDS   4 GLYCOPROTEIN, HYDROLASE, LIPID DEGRADATION, POLYMORPHISM,            
KEYWDS   5 SECRETED                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SAMANTA,B.J.BAHNSON                                                 
REVDAT   1   09-SEP-08 3D59    0                                                
JRNL        AUTH   U.SAMANTA,B.J.BAHNSON                                        
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET                   
JRNL        TITL 2 ACTIVATING FACTOR ACETYLHYDROLASE: STRUCTURAL                
JRNL        TITL 3 IMPLICATION TO LIPOPROTEIN BINDING AND CATALYSIS.            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.50 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.5                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.142                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.131                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.191                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 6384                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.131                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.179                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 5314                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 100893                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 6055                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 126                                           
REMARK   3   SOLVENT ATOMS      : 511                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 6556.52                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 38                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 57242                   
REMARK   3   NUMBER OF RESTRAINTS                     : 72220                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.027                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.053                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.068                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.031                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.061                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D59 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB047608.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-2006; 12-AUG-2006           
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; APS                          
REMARK 200  BEAMLINE                       : X29A; 19-ID                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100; 1.006, 1.009                
REMARK 200  MONOCHROMATOR                  : SI(111); SI(111)                   
REMARK 200  OPTICS                         : ROSENBAUM-ROCK; ROSENBAUM-ROCK     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC             
REMARK 200                                   QUANTUM 315                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127359                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.1900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.920                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: HKL2MAP, SOLVE, RESOLVE, CCP4I, ARP/WARP, SHELXL      
REMARK 200  -97                                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.6, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 293.0K, PH 6.60                                   
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   1/2+X,1/2+Y,Z                                           
REMARK 290       4555   1/2-X,1/2+Y,-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       58.09200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.53050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.09200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.53050            
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 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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 596   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A 652   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A 670   LIES ON A SPECIAL POSITION.                         
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
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     ASN A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     ILE A   429                                                      
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     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     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     LYS B  55    CG    CD    CE    NZ                                
REMARK 470     GLN B  88    CG    CD    OE1   NE2                               
REMARK 470     ASP B  89    CG    OD1   OD2                                     
REMARK 470     ASN B  90    CG    OD1   ND2                                     
REMARK 470     ASP B  91    CG    OD1   OD2                                     
REMARK 470     ARG B  92    CG    CD    NE    CZ    NH1   NH2                   
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     GLN B 427    CG    CD    OE1   NE2                               
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     -175.77    -68.57                                   
REMARK 500    LYS A 266       75.85   -117.61                                   
REMARK 500    SER A 273     -117.17     64.88                                   
REMARK 500    HIS A 399       57.46   -102.67                                   
REMARK 500    LYS A 400     -167.29   -118.77                                   
REMARK 500    ASP B  73     -169.63    -69.25                                   
REMARK 500    TRP B 115      -36.24    -38.25                                   
REMARK 500    LYS B 266       77.51   -118.13                                   
REMARK 500    SER B 273     -115.78     66.79                                   
REMARK 500    HIS B 399       65.50   -109.68                                   
REMARK 500    ASN B 426       41.17   -106.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 2                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 11                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 12                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 13                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 14                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 15                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 16                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 17                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 18                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 19                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 20                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 21                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 22                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 23                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 24                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 25                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 26                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 27                  
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 28                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 29                  
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 32                  
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 33                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 35                  
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 36                  
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 37                  
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 38                  
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 39                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D5E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING                
REMARK 900 FACTOR ACETYLHYDROLASE COVALENTLY INHIBITED BY PARAOXON              
DBREF  3D59 A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  3D59 B   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
SEQRES   1 A  383  ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY          
SEQRES   2 A  383  ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE          
SEQRES   3 A  383  ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR          
SEQRES   4 A  383  PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE          
SEQRES   5 A  383  PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU          
SEQRES   6 A  383  GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU          
SEQRES   7 A  383  PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO          
SEQRES   8 A  383  LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER          
SEQRES   9 A  383  HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE          
SEQRES  10 A  383  GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA          
SEQRES  11 A  383  VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR          
SEQRES  12 A  383  PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER          
SEQRES  13 A  383  TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR          
SEQRES  14 A  383  HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU          
SEQRES  15 A  383  CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS          
SEQRES  16 A  383  GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP          
SEQRES  17 A  383  MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE          
SEQRES  18 A  383  ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE          
SEQRES  19 A  383  GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE          
SEQRES  20 A  383  ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL          
SEQRES  21 A  383  TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER          
SEQRES  22 A  383  GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS          
SEQRES  23 A  383  LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR          
SEQRES  24 A  383  ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR          
SEQRES  25 A  383  PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU          
SEQRES  26 A  383  LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER          
SEQRES  27 A  383  ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY          
SEQRES  28 A  383  LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU          
SEQRES  29 A  383  GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN          
SEQRES  30 A  383  THR THR ASN GLN HIS ILE                                      
SEQRES   1 B  383  ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY          
SEQRES   2 B  383  ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE          
SEQRES   3 B  383  ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR          
SEQRES   4 B  383  PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE          
SEQRES   5 B  383  PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU          
SEQRES   6 B  383  GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU          
SEQRES   7 B  383  PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO          
SEQRES   8 B  383  LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER          
SEQRES   9 B  383  HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE          
SEQRES  10 B  383  GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA          
SEQRES  11 B  383  VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR          
SEQRES  12 B  383  PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER          
SEQRES  13 B  383  TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR          
SEQRES  14 B  383  HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU          
SEQRES  15 B  383  CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS          
SEQRES  16 B  383  GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP          
SEQRES  17 B  383  MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE          
SEQRES  18 B  383  ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE          
SEQRES  19 B  383  GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE          
SEQRES  20 B  383  ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL          
SEQRES  21 B  383  TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER          
SEQRES  22 B  383  GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS          
SEQRES  23 B  383  LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR          
SEQRES  24 B  383  ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR          
SEQRES  25 B  383  PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU          
SEQRES  26 B  383  LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER          
SEQRES  27 B  383  ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY          
SEQRES  28 B  383  LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU          
SEQRES  29 B  383  GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN          
SEQRES  30 B  383  THR THR ASN GLN HIS ILE                                      
HET    ACT  A  11       4                                                       
HET    ACT  A  12       4                                                       
HET    ACT  A  15       4                                                       
HET    ACT  A  16       4                                                       
HET    ACT  A  19       4                                                       
HET    ACT  A  20       4                                                       
HET    ACT  A  22       4                                                       
HET    ACT  A  24       4                                                       
HET    ACT  A  25       4                                                       
HET    ACT  A  28       4                                                       
HET    ACT  A  29       4                                                       
HET    ACT  A  30       4                                                       
HET    ACT  A  32       4                                                       
HET    ACT  A  33       4                                                       
HET    ACT  A  35       4                                                       
HET    ACT  A  36       4                                                       
HET    ACT  A  39       4                                                       
HET    SO4  B   1       5                                                       
HET    SO4  B   2       5                                                       
HET    ACT  B  13       4                                                       
HET    ACT  B  14       4                                                       
HET    ACT  B  17       4                                                       
HET    ACT  B  18       4                                                       
HET    ACT  B  21       4                                                       
HET    ACT  B  23       4                                                       
HET    ACT  B  26       4                                                       
HET    ACT  B  27       4                                                       
HET    ACT  B  31       4                                                       
HET    ACT  B  34       4                                                       
HET    ACT  B  37       4                                                       
HET    ACT  B  38       4                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  ACT    29(C2 H3 O2 1-)                                              
FORMUL  20  SO4    2(O4 S 2-)                                                   
FORMUL  34  HOH   *511(H2 O)                                                    
HELIX    1   1 ASN A  100  GLY A  112  1                                  13    
HELIX    2   2 HIS A  114  GLY A  126  1                                  13    
HELIX    3   3 TYR A  160  HIS A  170  1                                  11    
HELIX    4   4 ASP A  192  GLY A  199  1                                   8    
HELIX    5   5 LYS A  210  GLU A  212  5                                   3    
HELIX    6   6 GLU A  213  HIS A  241  1                                  29    
HELIX    7   7 ASP A  254  LYS A  259  5                                   6    
HELIX    8   8 SER A  273  ASP A  286  1                                  14    
HELIX    9   9 GLY A  303  ARG A  309  5                                   7    
HELIX   10  10 TYR A  324  LYS A  333  1                                  10    
HELIX   11  11 VAL A  350  ALA A  360  5                                  11    
HELIX   12  12 GLY A  362  LEU A  369  1                                   8    
HELIX   13  13 ASP A  376  GLY A  397  1                                  22    
HELIX   14  14 ASP A  401  GLN A  404  5                                   4    
HELIX   15  15 TRP A  405  GLU A  410  1                                   6    
HELIX   16  16 ASN B  100  GLY B  112  1                                  13    
HELIX   17  17 TRP B  115  GLY B  126  1                                  12    
HELIX   18  18 TYR B  160  HIS B  170  1                                  11    
HELIX   19  19 ASP B  192  ILE B  198  1                                   7    
HELIX   20  20 LYS B  210  GLU B  212  5                                   3    
HELIX   21  21 GLU B  213  HIS B  241  1                                  29    
HELIX   22  22 ASP B  254  LYS B  259  5                                   6    
HELIX   23  23 SER B  273  ASP B  286  1                                  14    
HELIX   24  24 GLU B  305  ARG B  309  5                                   5    
HELIX   25  25 TYR B  324  CYS B  334  1                                  11    
HELIX   26  26 VAL B  350  ALA B  360  5                                  11    
HELIX   27  27 GLY B  362  LEU B  369  1                                   8    
HELIX   28  28 ASP B  376  GLY B  397  1                                  22    
HELIX   29  29 ASP B  401  GLN B  404  5                                   4    
HELIX   30  30 TRP B  405  GLU B  410  1                                   6    
SHEET    1   A10 ASN A 133  TRP A 134  0                                        
SHEET    2   A10 SER A  64  PHE A  72  1  N  VAL A  65   O  ASN A 133           
SHEET    3   A10 THR A  79  SER A  87 -1  O  LEU A  83   N  THR A  68           
SHEET    4   A10 ILE A 173  VAL A 177 -1  O  ALA A 176   N  ARG A  82           
SHEET    5   A10 TYR A 144  SER A 150  1  N  VAL A 147   O  ALA A 175           
SHEET    6   A10 ILE A 262  HIS A 272  1  O  ASP A 263   N  TYR A 144           
SHEET    7   A10 CYS A 291  LEU A 295  1  O  LEU A 295   N  GLY A 271           
SHEET    8   A10 LEU A 314  SER A 319  1  O  PHE A 315   N  ALA A 294           
SHEET    9   A10 ARG A 341  ILE A 346  1  O  LYS A 342   N  PHE A 316           
SHEET   10   A10 LEU A 416  PRO A 418 -1  O  ILE A 417   N  THR A 345           
SHEET    1   B 2 THR A  95  LEU A  96  0                                        
SHEET    2   B 2 THR A 129  THR A 130 -1  O  THR A 130   N  THR A  95           
SHEET    1   C 2 ALA A 186  TYR A 189  0                                        
SHEET    2   C 2 SER A 202  TYR A 205 -1  O  LEU A 204   N  THR A 187           
SHEET    1   D10 ASN B 133  TRP B 134  0                                        
SHEET    2   D10 VAL B  65  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3   D10 THR B  79  PRO B  86 -1  O  LEU B  83   N  THR B  68           
SHEET    4   D10 ILE B 173  VAL B 177 -1  O  ALA B 176   N  ARG B  82           
SHEET    5   D10 TYR B 144  SER B 150  1  N  VAL B 147   O  ALA B 175           
SHEET    6   D10 ILE B 262  HIS B 272  1  O  ASP B 263   N  TYR B 144           
SHEET    7   D10 CYS B 291  LEU B 295  1  O  LEU B 295   N  GLY B 271           
SHEET    8   D10 LEU B 314  SER B 319  1  O  PHE B 315   N  ALA B 294           
SHEET    9   D10 ARG B 341  ILE B 346  1  O  ILE B 344   N  ASN B 318           
SHEET   10   D10 LEU B 416  PRO B 418 -1  O  ILE B 417   N  THR B 345           
SHEET    1   E 2 THR B  95  LEU B  96  0                                        
SHEET    2   E 2 THR B 129  THR B 130 -1  O  THR B 130   N  THR B  95           
SHEET    1   F 2 ALA B 186  TYR B 189  0                                        
SHEET    2   F 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       -10.74                     
CISPEP   2 PHE B   72    ASP B   73          0       -12.19                     
SITE     1 AC1  8 LYS A 143  HIS A 241  ARG A 264  HOH A 476                    
SITE     2 AC1  8 SER B 308  ARG B 309  PRO B 311  LYS B 339                    
SITE     1 AC2  4 SER A 230  GLN A 231  SER A 234  HOH A 494                    
SITE     1 AC3  4 LYS A 143  ILE A 262  ASP A 263  ARG A 264                    
SITE     1 AC4  4 SER A 202  TRP A 203  TYR B 189  LYS B 191                    
SITE     1 AC5  5 HIS A  74  ASP A 192  GLN A 193  HOH A 662                    
SITE     2 AC5  5 HOH A 713                                                     
SITE     1 AC6  6 LYS A 246  ASN A 247  PHE A 253  MET A 255                    
SITE     2 AC6  6 HOH A 490  HOH A 495                                          
SITE     1 AC7  2 PHE A  72  HOH A 481                                          
SITE     1 AC8  2 LEU A 124  THR A 361                                          
SITE     1 AC9  3 TRP A 298  TYR A 324  HOH A 446                               
SITE     1 BC1  5 LYS A 191  HOH A 534  TYR B 189  LYS B 191                    
SITE     2 BC1  5 HOH B 548                                                     
SITE     1 BC2  4 GLU A 305  SER A 308  ARG A 309  ASP B 260                    
SITE     1 BC3  2 LYS A 394  HIS A 395                                          
SITE     1 BC4  6 PRO A  57  ARG A  58  ASN A 378  HOH A 548                    
SITE     2 BC4  6 HOH A 566  HOH A 711                                          
SITE     1 BC5  3 ASN A 378  ASP A 382  HOH A 510                               
SITE     1 BC6  3 ARG A 182  HOH A 555  HOH A 700                               
SITE     1 BC7  7 ASP A 338  GLU A 410  ASP A 412  PRO A 418                    
SITE     2 BC7  7 HOH A 542  HOH A 635  HOH A 710                               
SITE     1 BC8  8 LYS A 101  LYS A 201  ARG B 182  ARG B 207                    
SITE     2 BC8  8 HOH B 471  HOH B 482  HOH B 490  HOH B 496                    
SITE     1 BC9  6 ASP A  89  ASN A  90  ASN B 100  LYS B 101                    
SITE     2 BC9  6 HOH B 521  HOH B 634                                          
SITE     1 CC1  3 TRP B 134  LEU B 251  HOH B 518                               
SITE     1 CC2  4 TYR B 321  PHE B 322  HIS B 351  HOH B 449                    
SITE     1 CC3  3 SER B 230  GLN B 231  SER B 234                               
SITE     1 CC4  3 LYS B 266  LEU B 398  HIS B 399                               
SITE     1 CC5  4 TRP B 298  PHE B 300  TYR B 324  HOH B 441                    
SITE     1 CC6  2 LEU B 107  PHE B 357                                          
SITE     1 CC7  3 LYS A 259  HOH A 679  ARG B 309                               
SITE     1 CC8  3 HIS B  74  ASP B 192  GLN B 193                               
SITE     1 CC9  4 LYS A 370  HOH A 620  ILE B 329  HOH B 639                    
SITE     1 DC1  3 PRO B 140  ASP B 412  HOH B 594                               
CRYST1  116.184   83.061   96.705  90.00 115.09  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      0.008607  0.000000  0.004030        0.00000                         
SCALE2      0.000000  0.012039  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011418        0.00000                         
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
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