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LongText Report for: 3D5E-pdb

Name Class
3D5E-pdb
HEADER    HYDROLASE                               16-MAY-08   3D5E              
TITLE     CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING                 
TITLE    2 FACTOR ACETYLHYDROLASE COVALENTLY INHIBITED BY PARAOXON              
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, PARAOXON                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SAMANTA,B.J.BAHNSON                                                 
REVDAT   1   09-SEP-08 3D5E    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. 2.10 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 45723                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2439                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2560                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 6365                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.249         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.980         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6224 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8391 ; 1.905 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   745 ; 7.414 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   301 ;39.843 ;23.920       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1080 ;17.460 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;15.648 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   894 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4709 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2759 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4145 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   356 ; 0.178 ; 0.200       
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):    73 ; 0.232 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.082 ; 0.200       
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):  3882 ; 1.604 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5985 ; 2.069 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2733 ; 3.385 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2406 ; 4.917 ; 4.500       
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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3D5E 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 RCSB047613.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : SI(111) ROSENBAUM-ROCK             
REMARK 200  OPTICS                         : SI(111) ROSENBAUM-ROCK             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48162                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.5900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.430                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP OF CCP4I, REFMAC5 OF CCP4I FOR FINAL           
REMARK 200  REFINEMENT                                                          
REMARK 200 STARTING MODEL: NATIVE STRUCTURE, PDB ENTRY 3D59                     
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 7.0, VAPOR DIFFUSION, HANGING         
REMARK 280  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   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       58.60650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.34800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.60650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.34800            
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 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     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     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 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     -170.71    -69.72                                   
REMARK 500    ASP A  89      152.94    177.90                                   
REMARK 500    ASP A  91      -82.52    -20.43                                   
REMARK 500    THR A 113     -164.78   -115.38                                   
REMARK 500    ALA A 155     -159.30    -97.93                                   
REMARK 500    PHE A 156     -178.89   -173.83                                   
REMARK 500    LEU A 209     -166.42   -106.96                                   
REMARK 500    SER A 273     -104.57     63.44                                   
REMARK 500    ASN B  90       14.33   -148.76                                   
REMARK 500    ASP B  91      -73.78    -54.84                                   
REMARK 500    THR B 113     -162.42   -106.12                                   
REMARK 500    HIS B 114     -152.75   -150.49                                   
REMARK 500    ALA B 155     -162.85   -106.77                                   
REMARK 500    LYS B 266       73.72   -109.33                                   
REMARK 500    SER B 273     -105.77     60.97                                   
REMARK 500    ILE B 422      170.30    -53.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: DEP BINDING SITE FOR RESIDUE A 473                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: DEP BINDING SITE FOR RESIDUE B 473                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 1                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 3                   
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 4                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 5                   
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 6                   
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 7                   
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 8                   
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 9                   
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 10                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 11                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 12                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 13                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 14                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 15                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 16                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D59   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING                
REMARK 900 FACTOR ACETYLHYDROLASE                                               
DBREF  3D5E A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  3D5E 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    DEP  A 473       8                                                       
HET    FMT  A   2       3                                                       
HET    FMT  A   3       3                                                       
HET    FMT  A   4       3                                                       
HET    FMT  A   5       3                                                       
HET    FMT  A  11       3                                                       
HET    FMT  A  12       3                                                       
HET    FMT  A  16       3                                                       
HET    DEP  B 473       8                                                       
HET    FMT  B   1       3                                                       
HET    FMT  B   6       3                                                       
HET    FMT  B   7       3                                                       
HET    FMT  B   8       3                                                       
HET    FMT  B   9       3                                                       
HET    FMT  B  10       3                                                       
HET    FMT  B  13       3                                                       
HET    FMT  B  14       3                                                       
HET    FMT  B  15       3                                                       
HETNAM     DEP DIETHYL PHOSPHONATE                                              
HETNAM     FMT FORMIC ACID                                                      
FORMUL   3  DEP    2(C4 H11 O3 P)                                               
FORMUL   4  FMT    16(C H2 O2)                                                  
FORMUL  21  HOH   *288(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  ILE A  198  1                                   7    
HELIX    5   5 GLU A  213  HIS A  241  1                                  29    
HELIX    6   6 ASP A  254  LYS A  259  5                                   6    
HELIX    7   7 SER A  273  ASP A  286  1                                  14    
HELIX    8   8 GLU A  305  ARG A  309  5                                   5    
HELIX    9   9 TYR A  324  CYS A  334  1                                  11    
HELIX   10  10 VAL A  350  ALA A  360  5                                  11    
HELIX   11  11 GLY A  362  LEU A  369  1                                   8    
HELIX   12  12 ASP A  376  GLY A  397  1                                  22    
HELIX   13  13 ASP A  401  GLN A  404  5                                   4    
HELIX   14  14 TRP A  405  GLU A  410  1                                   6    
HELIX   15  15 ASN B  100  GLY B  112  1                                  13    
HELIX   16  16 HIS B  114  GLY B  126  1                                  13    
HELIX   17  17 TYR B  160  HIS B  170  1                                  11    
HELIX   18  18 ASP B  192  GLY B  199  1                                   8    
HELIX   19  19 LYS B  210  GLU B  212  5                                   3    
HELIX   20  20 GLU B  213  HIS B  241  1                                  29    
HELIX   21  21 ASP B  254  LYS B  259  5                                   6    
HELIX   22  22 SER B  273  ASP B  286  1                                  14    
HELIX   23  23 GLY B  303  ARG B  309  5                                   7    
HELIX   24  24 TYR B  324  CYS B  334  1                                  11    
HELIX   25  25 VAL B  350  ALA B  360  5                                  11    
HELIX   26  26 GLY B  362  LEU B  369  1                                   8    
HELIX   27  27 ASP B  376  GLY B  397  1                                  22    
HELIX   28  28 ASP B  401  GLN B  404  5                                   4    
HELIX   29  29 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  THR A  79   N  PHE A  72           
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  ILE A 270   N  VAL A 148           
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  ILE A 344   N  ASN A 318           
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  SER A 202   N  TYR A 189           
SHEET    1   D10 ASN B 133  TRP B 134  0                                        
SHEET    2   D10 SER B  64  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3   D10 THR B  79  SER B  87 -1  O  SER B  87   N  SER B  64           
SHEET    4   D10 ILE B 173  VAL B 177 -1  O  VAL B 174   N  TYR B  84           
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  ILE B 270   N  VAL B 148           
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  ILE B 317   N  ALA B 294           
SHEET    9   D10 ARG B 341  ILE B 346  1  O  ILE B 346   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  SER B 202   N  TYR B 189           
LINK         OG  SER A 273                 P   DEP A 473   1555   1555    1.69  
LINK         OG  SER B 273                 P   DEP B 473   1555   1555    1.75  
CISPEP   1 PHE A   72    ASP A   73          0        -6.94                     
CISPEP   2 PHE B   72    ASP B   73          0        -6.50                     
SITE     1 AC1  7 GLY A 152  LEU A 153  SER A 273  PHE A 274                    
SITE     2 AC1  7 TRP A 298  PHE A 322  HIS A 351                               
SITE     1 AC2  4 ASN A 135  LYS A 252  ASP A 254  GLN A 257                    
SITE     1 AC3  4 GLU A 256  GLN A 257  LYS A 259  HOH A 509                    
SITE     1 AC4  4 PHE A 300  ALA A 326  LYS A 330  HOH A 528                    
SITE     1 AC5  3 THR A  54  MET A 128  THR A 129                               
SITE     1 AC6  2 ASP A 382  LYS A 386                                          
SITE     1 AC7  2 ARG A 182  THR A 208                                          
SITE     1 AC8  7 GLY B 152  LEU B 153  SER B 273  PHE B 274                    
SITE     2 AC8  7 TRP B 298  HIS B 351  GLN B 352                               
SITE     1 AC9  2 TRP B 298  TYR B 324                                          
SITE     1 BC1  4 TYR B 335  LYS B 342  MET B 343  HOH B 518                    
SITE     1 BC2  4 ARG B 182  TRP B 203  LEU B 204  TYR B 205                    
SITE     1 BC3  5 SER B 230  GLN B 231  SER B 234  ARG B 288                    
SITE     2 BC3  5 HOH B 554                                                     
SITE     1 BC4  6 ILE A 422  ASN A 423  GLU B 320  GLN B 323                    
SITE     2 BC4  6 ASN B 421  ILE B 422                                          
SITE     1 BC5  4 PRO B  57  ARG B  58  ALA B 162  ASP B 166                    
SITE     1 BC6  6 PRO A 311  LYS B 143  ILE B 262  ARG B 264                    
SITE     2 BC6  6 HOH B 605  HOH B 606                                          
SITE     1 BC7  3 SER B 234  ARG B 288  HOH B 590                               
SITE     1 BC8  4 GLN B 393  LYS B 394  ASP B 403  HOH B 498                    
CRYST1  117.213   78.696   97.340  90.00 101.61  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      0.008531  0.000000  0.001753        0.00000                         
SCALE2      0.000000  0.012707  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010488        0.00000                         
TER    3029      ASN A 426                                                      
TER    6015      ASN B 423                                                      
MASTER      342    0   18   29   28    0   22    6 6365    2   66   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.
For technical information about these pages see:
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