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LongText Report for: 3F98-pdb

Name Class
3F98-pdb
HEADER    HYDROLASE                               13-NOV-08   3F98              
TITLE     CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING FACTOR          
TITLE    2 ACETYLHYDROLASE COVALENTLY INHIBITED BY TABUN                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A, B, C;                                                      
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 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLA2G7, PAFAH;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 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 TABUN, DISEASE MUTATION, SECRETED                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SAMANTA,B.J.BAHNSON                                                 
REVDAT   1   23-JUN-09 3F98    0                                                
JRNL        AUTH   U.SAMANTA,S.D.KIRBY,P.SRINIVASAN,D.M.CERASOLI,               
JRNL        AUTH 2 B.J.BAHNSON                                                  
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN GROUP-VIIA                       
JRNL        TITL 2 PHOSPHOLIPASE A2 INHIBITED BY ORGANOPHOSPHORUS               
JRNL        TITL 3 NERVE AGENTS EXHIBIT NON-AGED COMPLEXES.                     
JRNL        REF    BIOCHEM.PHARM.                             2009              
JRNL        REFN                   ISSN 0006-2952                               
JRNL        PMID   19394314                                                     
JRNL        DOI    10.1016/J.BCP.2009.04.018                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 134355                         
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7097                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9769                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 497                          
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9351                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 1342                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.692         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9772 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13072 ; 1.349 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1126 ; 6.500 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   472 ;36.830 ;23.941       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1737 ;14.629 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;16.931 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1425 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7204 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5137 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6633 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1135 ; 0.138 ; 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):   183 ; 0.235 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    75 ; 0.171 ; 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):  5995 ; 0.887 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9246 ; 1.456 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4267 ; 1.941 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3826 ; 2.945 ; 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 : 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 : MASK                                                 
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3F98 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050305.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0055                             
REMARK 200  MONOCHROMATOR                  : SI(111) 0.990                      
REMARK 200  OPTICS                         : ROSENBAUM-ROCK                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141507                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
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     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 35.0250                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.43500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.590                              
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 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   (%): 51.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 293K, TEMPERATURE 293.0K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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      126.92750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      126.92750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       38.49200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.49200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      126.92750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.49200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      126.92750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.49200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
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 A1356  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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    47                                                      
REMARK 465     ALA A    48                                                      
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     ASN B   426                                                      
REMARK 465     GLN B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     ILE B   429                                                      
REMARK 465     ALA C    47                                                      
REMARK 465     ALA C    48                                                      
REMARK 465     ASN C   426                                                      
REMARK 465     GLN C   427                                                      
REMARK 465     HIS C   428                                                      
REMARK 465     ILE C   429                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O1   FMT C   579     O    HOH C  1817              2.16            
REMARK 500   NE2  GLN B   287     O    HOH B  1468              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 273   C     SER A 273   O       0.189                       
REMARK 500    HIS A 272   C     SER A 273   N       0.287                       
REMARK 500    SER B 273   C     SER B 273   O       0.189                       
REMARK 500    HIS B 272   C     SER B 273   N       0.287                       
REMARK 500    SER C 273   C     SER C 273   O       0.187                       
REMARK 500    HIS C 272   C     SER C 273   N       0.280                       
REMARK 500    SER C 273   C     PHE C 274   N       0.148                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 273   CA  -  C   -  N   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    SER A 273   O   -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    SER B 273   CA  -  C   -  N   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    SER B 273   O   -  C   -  N   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    SER C 273   CA  -  C   -  N   ANGL. DEV. =  18.7 DEGREES          
REMARK 500    SER C 273   O   -  C   -  N   ANGL. DEV. = -16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  53      -60.87   -133.40                                   
REMARK 500    PHE A 156     -177.11   -170.82                                   
REMARK 500    HIS A 216      -31.78   -135.08                                   
REMARK 500    SER A 273     -104.91     56.07                                   
REMARK 500    HIS A 399       56.12   -102.81                                   
REMARK 500    LYS A 400     -164.73   -116.98                                   
REMARK 500    THR A 424       66.59   -150.72                                   
REMARK 500    GLN B  53      -56.39   -132.75                                   
REMARK 500    ASP B  73     -168.41    -71.59                                   
REMARK 500    HIS B 216      -33.26   -137.40                                   
REMARK 500    SER B 273     -104.89     56.10                                   
REMARK 500    HIS B 399       58.01   -105.06                                   
REMARK 500    LYS B 400     -163.14   -117.84                                   
REMARK 500    THR B 424       63.66   -150.36                                   
REMARK 500    GLN C  53      -57.10   -135.12                                   
REMARK 500    ASP C  73     -168.80    -72.57                                   
REMARK 500    HIS C 216      -32.98   -135.75                                   
REMARK 500    SER C 273     -107.12     50.09                                   
REMARK 500    HIS C 399       57.82   -105.58                                   
REMARK 500    LYS C 400     -161.35   -118.90                                   
REMARK 500    THR C 424       73.92   -151.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A   91     ARG A   92                 -130.07                    
REMARK 500 ASP B   91     ARG B   92                 -131.62                    
REMARK 500 ASP C   91     ARG C   92                 -132.04                    
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 NTJ A 473                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 503                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 506                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 508                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 509                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 510                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 511                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 513                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 518                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 521                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 522                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 524                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 527                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 528                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 531                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 533                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 534                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 536                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 538                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 539                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 540                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 541                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 544                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 546                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 547                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 551                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 552                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 553                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 554                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 555                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 556                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 558                 
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTJ B 473                 
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 501                 
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 502                 
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 504                 
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 505                 
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 507                 
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 512                 
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 514                 
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 515                 
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 516                 
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 517                 
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 520                 
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 523                 
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 525                 
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 526                 
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 529                 
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 530                 
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 532                 
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 535                 
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 537                 
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 542                 
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 543                 
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 545                 
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 548                 
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 549                 
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 550                 
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 557                 
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 586                 
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTJ C 473                 
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 519                 
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 559                 
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 560                 
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 561                 
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 562                 
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 563                 
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 564                 
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 565                 
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 566                 
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 567                 
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 568                 
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 569                 
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 570                 
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 571                 
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 572                 
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 573                 
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 574                 
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 575                 
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 576                 
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 577                 
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 578                 
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 579                 
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 580                 
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 581                 
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 582                 
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 583                 
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 584                 
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 585                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D59   RELATED DB: PDB                                   
REMARK 900 THE SAME WILD TYPE PROTEIN                                           
REMARK 900 RELATED ID: 3D5E   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PARAOXON                             
REMARK 900 RELATED ID: 3F96   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SARIN                                
REMARK 900 RELATED ID: 3F97   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SOMAN                                
REMARK 900 RELATED ID: 3F98   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIISOPROPYLFLUOROPHOSPHATE           
DBREF  3F98 A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  3F98 B   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  3F98 C   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                                      
SEQRES   1 C  383  ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY          
SEQRES   2 C  383  ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE          
SEQRES   3 C  383  ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR          
SEQRES   4 C  383  PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE          
SEQRES   5 C  383  PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU          
SEQRES   6 C  383  GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU          
SEQRES   7 C  383  PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO          
SEQRES   8 C  383  LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER          
SEQRES   9 C  383  HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE          
SEQRES  10 C  383  GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA          
SEQRES  11 C  383  VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR          
SEQRES  12 C  383  PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER          
SEQRES  13 C  383  TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR          
SEQRES  14 C  383  HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU          
SEQRES  15 C  383  CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS          
SEQRES  16 C  383  GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP          
SEQRES  17 C  383  MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE          
SEQRES  18 C  383  ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE          
SEQRES  19 C  383  GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE          
SEQRES  20 C  383  ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL          
SEQRES  21 C  383  TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER          
SEQRES  22 C  383  GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS          
SEQRES  23 C  383  LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR          
SEQRES  24 C  383  ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR          
SEQRES  25 C  383  PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU          
SEQRES  26 C  383  LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER          
SEQRES  27 C  383  ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY          
SEQRES  28 C  383  LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU          
SEQRES  29 C  383  GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN          
SEQRES  30 C  383  THR THR ASN GLN HIS ILE                                      
HET    NTJ  A 473       8                                                       
HET    FMT  A 503       3                                                       
HET    FMT  A 506       3                                                       
HET    FMT  A 508       3                                                       
HET    FMT  A 509       3                                                       
HET    FMT  A 510       3                                                       
HET    FMT  A 511       3                                                       
HET    FMT  A 513       3                                                       
HET    FMT  A 518       3                                                       
HET    FMT  A 521       3                                                       
HET    FMT  A 522       3                                                       
HET    FMT  A 524       3                                                       
HET    FMT  A 527       3                                                       
HET    FMT  A 528       3                                                       
HET    FMT  A 531       3                                                       
HET    FMT  A 533       3                                                       
HET    FMT  A 534       3                                                       
HET    FMT  A 536       3                                                       
HET    FMT  A 538       3                                                       
HET    FMT  A 539       3                                                       
HET    FMT  A 540       3                                                       
HET    FMT  A 541       3                                                       
HET    FMT  A 544       3                                                       
HET    FMT  A 546       3                                                       
HET    FMT  A 547       3                                                       
HET    FMT  A 551       3                                                       
HET    FMT  A 552       3                                                       
HET    FMT  A 553       3                                                       
HET    FMT  A 554       3                                                       
HET    FMT  A 555       3                                                       
HET    FMT  A 556       3                                                       
HET    FMT  A 558       3                                                       
HET    NTJ  B 473       8                                                       
HET    FMT  B 501       3                                                       
HET    FMT  B 502       3                                                       
HET    FMT  B 504       3                                                       
HET    FMT  B 505       3                                                       
HET    FMT  B 507       3                                                       
HET    FMT  B 512       3                                                       
HET    FMT  B 514       3                                                       
HET    FMT  B 515       3                                                       
HET    FMT  B 516       3                                                       
HET    FMT  B 517       3                                                       
HET    FMT  B 520       3                                                       
HET    FMT  B 523       3                                                       
HET    FMT  B 525       3                                                       
HET    FMT  B 526       3                                                       
HET    FMT  B 529       3                                                       
HET    FMT  B 530       3                                                       
HET    FMT  B 532       3                                                       
HET    FMT  B 535       3                                                       
HET    FMT  B 537       3                                                       
HET    FMT  B 542       3                                                       
HET    FMT  B 543       3                                                       
HET    FMT  B 545       3                                                       
HET    FMT  B 548       3                                                       
HET    FMT  B 549       3                                                       
HET    FMT  B 550       3                                                       
HET    FMT  B 557       3                                                       
HET    FMT  B 586       3                                                       
HET    NTJ  C 473       8                                                       
HET    FMT  C 519       3                                                       
HET    FMT  C 559       3                                                       
HET    FMT  C 560       3                                                       
HET    FMT  C 561       3                                                       
HET    FMT  C 562       3                                                       
HET    FMT  C 563       3                                                       
HET    FMT  C 564       3                                                       
HET    FMT  C 565       3                                                       
HET    FMT  C 566       3                                                       
HET    FMT  C 567       3                                                       
HET    FMT  C 568       3                                                       
HET    FMT  C 569       3                                                       
HET    FMT  C 570       3                                                       
HET    FMT  C 571       3                                                       
HET    FMT  C 572       3                                                       
HET    FMT  C 573       3                                                       
HET    FMT  C 574       3                                                       
HET    FMT  C 575       3                                                       
HET    FMT  C 576       3                                                       
HET    FMT  C 577       3                                                       
HET    FMT  C 578       3                                                       
HET    FMT  C 579       3                                                       
HET    FMT  C 580       3                                                       
HET    FMT  C 581       3                                                       
HET    FMT  C 582       3                                                       
HET    FMT  C 583       3                                                       
HET    FMT  C 584       3                                                       
HET    FMT  C 585       3                                                       
HETNAM     NTJ R-ETHYL N,N-DIMETHYLPHOSPHONAMIDATE                              
HETNAM     FMT FORMIC ACID                                                      
FORMUL   4  NTJ    3(C4 H12 N O2 P)                                             
FORMUL   5  FMT    86(C H2 O2)                                                  
FORMUL  93  HOH   *1084(H2 O)                                                   
HELIX    1   1 ASN A  100  GLY A  112  1                                  13    
HELIX    2   2 TRP A  115  GLY A  126  1                                  12    
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  HIS A  241  1                                  32    
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 GLY A  303  ILE A  310  5                                   8    
HELIX    9   9 TYR A  324  LYS A  333  1                                  10    
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 TRP B  115  GLY B  126  1                                  12    
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  HIS B  241  1                                  32    
HELIX   20  20 ASP B  254  LYS B  259  5                                   6    
HELIX   21  21 SER B  273  ASP B  286  1                                  14    
HELIX   22  22 GLY B  303  ILE B  310  5                                   8    
HELIX   23  23 TYR B  324  LYS B  333  1                                  10    
HELIX   24  24 VAL B  350  ALA B  360  5                                  11    
HELIX   25  25 GLY B  362  LEU B  369  1                                   8    
HELIX   26  26 ASP B  376  GLY B  397  1                                  22    
HELIX   27  27 ASP B  401  GLN B  404  5                                   4    
HELIX   28  28 TRP B  405  GLU B  410  1                                   6    
HELIX   29  29 ASN C  100  GLY C  112  1                                  13    
HELIX   30  30 TRP C  115  GLY C  126  1                                  12    
HELIX   31  31 TYR C  160  HIS C  170  1                                  11    
HELIX   32  32 ASP C  192  GLY C  199  1                                   8    
HELIX   33  33 LYS C  210  HIS C  241  1                                  32    
HELIX   34  34 ASP C  254  LYS C  259  5                                   6    
HELIX   35  35 SER C  273  ASP C  286  1                                  14    
HELIX   36  36 GLY C  303  ILE C  310  5                                   8    
HELIX   37  37 TYR C  324  LYS C  333  1                                  10    
HELIX   38  38 VAL C  350  ALA C  360  5                                  11    
HELIX   39  39 GLY C  362  LEU C  369  1                                   8    
HELIX   40  40 ASP C  376  GLY C  397  1                                  22    
HELIX   41  41 ASP C  401  GLN C  404  5                                   4    
HELIX   42  42 TRP C  405  GLU C  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  GLY A 271  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  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  TYR B  85   N  GLY B  66           
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  GLY B 271  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  LYS B 342   N  PHE B 316           
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           
SHEET    1   G10 ASN C 133  TRP C 134  0                                        
SHEET    2   G10 SER C  64  PHE C  72  1  N  VAL C  65   O  ASN C 133           
SHEET    3   G10 THR C  79  SER C  87 -1  O  TYR C  85   N  GLY C  66           
SHEET    4   G10 ILE C 173  VAL C 177 -1  O  ALA C 176   N  ARG C  82           
SHEET    5   G10 TYR C 144  SER C 150  1  N  VAL C 147   O  ALA C 175           
SHEET    6   G10 ILE C 262  GLY C 271  1  O  ASP C 263   N  TYR C 144           
SHEET    7   G10 CYS C 291  LEU C 295  1  O  LEU C 295   N  GLY C 271           
SHEET    8   G10 LEU C 314  SER C 319  1  O  PHE C 315   N  ALA C 294           
SHEET    9   G10 ARG C 341  ILE C 346  1  O  LYS C 342   N  PHE C 316           
SHEET   10   G10 LEU C 416  PRO C 418 -1  O  ILE C 417   N  THR C 345           
SHEET    1   H 2 THR C  95  LEU C  96  0                                        
SHEET    2   H 2 THR C 129  THR C 130 -1  O  THR C 130   N  THR C  95           
SHEET    1   I 2 ALA C 186  TYR C 189  0                                        
SHEET    2   I 2 SER C 202  TYR C 205 -1  O  SER C 202   N  TYR C 189           
LINK         C   HIS A 272                 N   SER A 273     1555   1555  1.62  
LINK         C   SER A 273                 N   PHE A 274     1555   1555  1.44  
LINK         C   HIS B 272                 N   SER B 273     1555   1555  1.62  
LINK         C   SER B 273                 N   PHE B 274     1555   1555  1.44  
LINK         C   HIS C 272                 N   SER C 273     1555   1555  1.62  
LINK         C   SER C 273                 N   PHE C 274     1555   1555  1.48  
LINK         OG  SER A 273                 P1  NTJ A 473     1555   1555  1.63  
LINK         OG  SER B 273                 P1  NTJ B 473     1555   1555  1.61  
LINK         OG  SER C 273                 P1  NTJ C 473     1555   1555  1.63  
CISPEP   1 PHE A   72    ASP A   73          0        -9.02                     
CISPEP   2 PHE B   72    ASP B   73          0        -9.90                     
CISPEP   3 PHE C   72    ASP C   73          0        -9.38                     
SITE     1 AC1 11 GLY A 152  LEU A 153  SER A 273  PHE A 274                    
SITE     2 AC1 11 TRP A 298  PHE A 322  HIS A 351  GLN A 352                    
SITE     3 AC1 11 HOH A1210  HOH A1392  PHE C  51                               
SITE     1 AC2  4 ILE A  98  ARG A 122  GLY A 126  PRO C 337                    
SITE     1 AC3  7 TYR A 335  ARG A 341  LYS A 342  MET A 343                    
SITE     2 AC3  7 FMT A 522  HOH A1641  ASN B 423                               
SITE     1 AC4  5 ASP A 374  ILE A 375  HOH A1049  HOH A1166                    
SITE     2 AC4  5 HOH A1631                                                     
SITE     1 AC5  4 PHE A  72  ASP A  73  GLY A  78  HOH A1288                    
SITE     1 AC6  4 ARG A 207  HIS A 216  HOH A1323  HOH A1628                    
SITE     1 AC7  7 ALA A 390  GLN A 393  LYS A 394  ASP A 403                    
SITE     2 AC7  7 ASP A 406  HOH A1176  HOH A1428                               
SITE     1 AC8  6 ARG A 182  LEU A 204  TYR A 205  HOH A1290                    
SITE     2 AC8  6 HOH A1367  HOH A1713                                          
SITE     1 AC9  7 GLU A 320  ARG A 347  GLY A 348  HOH A1305                    
SITE     2 AC9  7 HOH A1362  HOH A1631  ASP B 412                               
SITE     1 BC1  5 ASN A 135  PRO A 137  PHE A 253  GLN A 257                    
SITE     2 BC1  5 HOH A1253                                                     
SITE     1 BC2  6 LYS A 339  GLU A 340  ARG A 341  FMT A 506                    
SITE     2 BC2  6 HOH A1130  HOH A1641                                          
SITE     1 BC3  4 GLN A  88  ARG A 139  HOH A1307  HOH A1662                    
SITE     1 BC4  2 ASN A 119  HOH A1610                                          
SITE     1 BC5  5 VAL A 245  ASN A 247  PHE A 253  MET A 255                    
SITE     2 BC5  5 HOH A1299                                                     
SITE     1 BC6  5 ASP A 181  ARG A 182  ARG A 207  FMT A 553                    
SITE     2 BC6  5 HOH A1485                                                     
SITE     1 BC7  8 HIS A 179  ASP A 181  ARG A 182  SER A 183                    
SITE     2 BC7  8 ALA A 184  THR A 187  LEU A 204  TYR A 205                    
SITE     1 BC8  4 PHE A 322  VAL A 350  HIS A 351  HOH A1684                    
SITE     1 BC9  2 LYS A 386  TRP A 405                                          
SITE     1 CC1  6 TRP A 105  TRP A 203  TYR A 205  HOH A1074                    
SITE     2 CC1  6 HOH A1206  HOH A1727                                          
SITE     1 CC2  3 LYS A 109  GLY A 112  THR A 113                               
SITE     1 CC3  4 ASP A 412  HOH A1271  HOH A1622  ARG B  92                    
SITE     1 CC4  5 ASP A 240  ASP A 260  ASP C 240  HIS C 241                    
SITE     2 CC4  5 ASP C 260                                                     
SITE     1 CC5  3 ASP A 406  CYS A 407  HOH A1622                               
SITE     1 CC6  7 ARG A  92  ASP A  94  ILE C 422  ASN C 423                    
SITE     2 CC6  7 FMT C 581  HOH C1749  HOH C1839                               
SITE     1 CC7  2 HIS A 367  ASP A 374                                          
SITE     1 CC8  7 ASN A 100  TYR A 188  LYS A 201  HOH A1115                    
SITE     2 CC8  7 HOH A1198  HOH A1490  ASP C 338                               
SITE     1 CC9  5 PRO A  62  HIS A 170  LYS A 400  PHE A 402                    
SITE     2 CC9  5 HOH A1726                                                     
SITE     1 DC1  6 GLU A 220  GLN A 221  GLN A 224  FMT A 531                    
SITE     2 DC1  6 HOH A1410  HOH A1702                                          
SITE     1 DC2  7 THR A 208  LEU A 209  GLU A 214  ARG A 218                    
SITE     2 DC2  7 HOH A1050  HOH A1624  SER C  50                               
SITE     1 DC3  8 LYS A  55  PRO A  57  ASN A 378  FMT A 556                    
SITE     2 DC3  8 HOH A1633  HOH A1657  THR C 215  HOH C1880                    
SITE     1 DC4  9 THR A  54  LYS A  55  FMT A 555  HOH A1633                    
SITE     2 DC4  9 THR C 215  PHE C 300  FMT C 582  HOH C1880                    
SITE     3 DC4  9 HOH C1909                                                     
SITE     1 DC5  5 GLU A 265  ARG A 290  HIS A 395  LEU A 396                    
SITE     2 DC5  5 HOH A1375                                                     
SITE     1 DC6 11 PHE B  51  GLY B 152  LEU B 153  SER B 273                    
SITE     2 DC6 11 PHE B 274  TRP B 298  PHE B 322  HIS B 351                    
SITE     3 DC6 11 GLN B 352  HOH B1112  HOH B1183                               
SITE     1 DC7  4 PHE B  72  ASP B  73  GLY B  78  HOH B1656                    
SITE     1 DC8  5 PHE B 322  VAL B 350  HIS B 351  HOH B1047                    
SITE     2 DC8  5 HOH B1595                                                     
SITE     1 DC9  4 ASP B 374  ILE B 375  FMT B 505  HOH B1637                    
SITE     1 EC1  5 ARG B 347  ASN B 415  FMT B 504  FMT B 515                    
SITE     2 EC1  5 HOH B1637                                                     
SITE     1 EC2  4 GLU B 142  LYS B 143  LYS B 259  HOH B1683                    
SITE     1 EC3  7 ASN A 423  TYR B 335  LYS B 342  MET B 343                    
SITE     2 EC3  7 GLY B 419  HOH B1453  HOH B1521                               
SITE     1 EC4  4 LYS B  55  PHE B 359  THR B 361  LYS B 372                    
SITE     1 EC5  8 ASP A 412  GLU B 320  TYR B 321  ARG B 347                    
SITE     2 EC5  8 GLY B 348  FMT B 505  HOH B1262  HOH B1301                    
SITE     1 EC6  6 PRO B  62  TYR B  63  HIS B 170  LYS B 400                    
SITE     2 EC6  6 PHE B 402  HOH B1400                                          
SITE     1 EC7  5 GLU B 212  VAL B 379  HOH B1111  HOH B1182                    
SITE     2 EC7  5 HOH B1236                                                     
SITE     1 EC8  3 GLN B 393  LEU B 398  HOH B1629                               
SITE     1 EC9  6 TYR B 335  LYS B 339  GLU B 340  ARG B 341                    
SITE     2 EC9  6 HOH B1141  HOH B1536                                          
SITE     1 FC1  3 ASN B  76  HOH B1533  HOH B1567                               
SITE     1 FC2  4 SER A 336  ARG B 122  FMT B 529  HOH B1325                    
SITE     1 FC3  9 SER A 336  PRO A 337  ASN B 100  LYS B 101                    
SITE     2 FC3  9 ARG B 122  FMT B 526  HOH B1048  HOH B1325                    
SITE     3 FC3  9 HOH B1482                                                     
SITE     1 FC4  6 LYS B  55  PRO B  57  GLN B 211  ASN B 378                    
SITE     2 FC4  6 HOH B1297  HOH B1572                                          
SITE     1 FC5  7 THR B  54  LYS B  55  MET B 128  THR B 129                    
SITE     2 FC5  7 HOH B1132  HOH B1153  HOH B1189                               
SITE     1 FC6  8 HIS B 179  ASP B 181  ARG B 182  SER B 183                    
SITE     2 FC6  8 ALA B 184  THR B 187  LEU B 204  TYR B 205                    
SITE     1 FC7  3 ARG B 309  FMT B 549  HOH B1480                               
SITE     1 FC8  8 PRO B  57  ASN B  60  GLN B 211  ASN B 378                    
SITE     2 FC8  8 ILE B 381  ASP B 382  HOH B1101  HOH B1598                    
SITE     1 FC9  3 HOH B1632  PHE C  72  ASP C  73                               
SITE     1 GC1  6 PRO A 418  THR B 420  ILE B 422  ASN B 423                    
SITE     2 GC1  6 HOH B1099  HOH B1663                                          
SITE     1 GC2  1 GLN B 257                                                     
SITE     1 GC3  5 GLU B 305  SER B 308  ARG B 309  FMT B 537                    
SITE     2 GC3  5 HOH B1157                                                     
SITE     1 GC4  7 ILE B 239  GLY B 242  LYS B 243  MET B 255                    
SITE     2 GC4  7 GLU B 256  LYS B 259  HOH B1486                               
SITE     1 GC5  4 GLU B 265  ARG B 290  HIS B 395  LEU B 396                    
SITE     1 GC6  8 ASN B 318  SER B 319  GLU B 320  GLN B 323                    
SITE     2 GC6  8 THR B 345  THR B 420  ASN B 421  ILE B 422                    
SITE     1 GC7 11 PHE A  51  GLY C 152  LEU C 153  SER C 273                    
SITE     2 GC7 11 PHE C 274  TRP C 298  PHE C 322  HIS C 351                    
SITE     3 GC7 11 GLN C 352  HOH C1842  HOH C1926                               
SITE     1 GC8  7 THR C  54  LYS C  55  MET C 128  THR C 129                    
SITE     2 GC8  7 HOH C1134  HOH C1195  HOH C1774                               
SITE     1 GC9  3 LYS C 386  TRP C 405  HOH C2047                               
SITE     1 HC1  3 ARG C 182  TYR C 205  FMT C 561                               
SITE     1 HC2  5 TRP C 203  TYR C 205  FMT C 560  HOH C1938                    
SITE     2 HC2  5 HOH C2031                                                     
SITE     1 HC3  3 GLU C 220  GLN C 224  HOH C1978                               
SITE     1 HC4  5 LYS C 363  LYS C 372  ASP C 376  SER C 377                    
SITE     2 HC4  5 HOH C1789                                                     
SITE     1 HC5  6 ASN C 135  SER C 136  PRO C 137  LYS C 252                    
SITE     2 HC5  6 GLN C 257  HOH C1822                                          
SITE     1 HC6  6 GLU C 320  TYR C 321  ARG C 347  GLY C 348                    
SITE     2 HC6  6 ASP C 412  HOH C2034                                          
SITE     1 HC7  4 ARG C 223  LYS C 227  GLU C 285  FMT C 573                    
SITE     1 HC8  4 TRP C 134  ASN C 135  LEU C 251  LYS C 252                    
SITE     1 HC9  6 THR C 420  ILE C 422  ASN C 423  HOH C1802                    
SITE     2 HC9  6 HOH C1897  HOH C2008                                          
SITE     1 IC1  4 ASN C 415  HOH C1762  HOH C1779  HOH C2034                    
SITE     1 IC2  3 THR C 208  FMT C 571  HOH C2021                               
SITE     1 IC3  2 THR C 208  FMT C 570                                          
SITE     1 IC4  4 PRO C  62  HIS C 170  LYS C 400  PHE C 402                    
SITE     1 IC5  3 ARG C 223  GLU C 285  FMT C 566                               
SITE     1 IC6  8 ASP A  91  HOH A1677  TYR C 321  PHE C 322                    
SITE     2 IC6  8 VAL C 350  HIS C 351  HOH C1875  HOH C2068                    
SITE     1 IC7  8 HIS C 179  ASP C 181  ARG C 182  SER C 183                    
SITE     2 IC7  8 ALA C 184  THR C 187  LEU C 204  TYR C 205                    
SITE     1 IC8  5 ASP C 181  ARG C 182  ARG C 207  GLN C 221                    
SITE     2 IC8  5 HOH C1981                                                     
SITE     1 IC9  3 LYS C 266  LEU C 396  GLY C 397                               
SITE     1 JC1  7 ILE C 239  GLY C 242  LYS C 243  MET C 255                    
SITE     2 JC1  7 GLU C 256  LYS C 259  HOH C1773                               
SITE     1 JC2  7 GLN A 211  PRO C  57  ASN C  60  ASN C 378                    
SITE     2 JC2  7 ILE C 381  ASP C 382  HOH C1817                               
SITE     1 JC3  5 LYS C 386  HOH C1456  HOH C1813  HOH C1949                    
SITE     2 JC3  5 HOH C2050                                                     
SITE     1 JC4  4 ARG A  92  FMT A 546  ASN C 421  ASN C 423                    
SITE     1 JC5  8 LYS A  55  FMT A 556  PHE C 300  LYS C 330                    
SITE     2 JC5  8 HOH C1857  HOH C1889  HOH C1909  HOH C1921                    
SITE     1 JC6  4 ARG C 309  HOH C1947  HOH C2063  HOH C2074                    
SITE     1 JC7  6 THR A 215  PHE A 300  THR C  54  LYS C  55                    
SITE     2 JC7  6 HOH C2016  HOH C2032                                          
SITE     1 JC8  8 ASN C 318  SER C 319  GLU C 320  GLN C 323                    
SITE     2 JC8  8 THR C 345  THR C 420  ASN C 421  ILE C 422                    
CRYST1   76.984  133.322  253.855  90.00  90.00  90.00 C 2 2 21     24          
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      0.012990  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003939        0.00000                         
TER    3113      THR A 425                                                      
TER    6239      THR B 425                                                      
TER    9354      THR C 425                                                      
MASTER      691    0   89   42   42    0  148    610717    3  297   90          
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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