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LongText Report for: 5jal-pdb

Name Class
5jal-pdb
HEADER    HYDROLASE                               12-APR-16   5JAL              
TITLE     EXPLOITATION OF A NOVEL BINDING POCKET IN HUMAN LIPOPROTEIN-ASSOCIATED
TITLE    2 PHOSPHOLIPASE A2 (LP-PLA2) DISCOVERED THROUGH X-RAY       
TITLE    3 FRAGMENT SCREENING                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PAF ACETYLHYDROLASE,1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE   
COMPND   5 ESTERASE,2-ACETYL-1-ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA   
COMPND   6 PHOSPHOLIPASE A2,GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-     
COMPND   7 PLA(2),PAF 2-ACYLHYDROLASE;                                          
COMPND   8 EC: 3.1.1.47;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLA2G7, PAFAH;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOLIPASE, LIPID METABOLISM, HYDROLASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.DAY                                                               
REVDAT   1   25-MAY-16 5JAL    0                                                
JRNL        AUTH   A.J.WOOLFORD,J.E.PERO,S.ARAVAPALLI,V.BERDINI,J.E.COYLE,      
JRNL        AUTH 2 P.J.DAY,A.M.DODSON,P.GRONDIN,F.P.HOLDING,L.Y.LEE,P.LI,       
JRNL        AUTH 3 E.S.MANAS,J.P.MARINO,A.C.MARTIN,B.W.MCCLELAND,R.L.MCMENAMIN, 
JRNL        AUTH 4 C.W.MURRAY,C.E.NEIPP,L.W.PAGE,V.K.PATEL,F.POTVAIN,S.J.RICH,  
JRNL        AUTH 5 R.A.RIVERO,K.SMITH,D.O.SOMERS,L.TROTTET,R.VELAGALETI,        
JRNL        AUTH 6 G.WILLIAMS,R.XIE                                             
JRNL        TITL   EXPLOITATION OF A NOVEL BINDING POCKET IN HUMAN              
JRNL        TITL 2 LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 (LP-PLA2) DISCOVERED 
JRNL        TITL 3 THROUGH X-RAY FRAGMENT SCREENING.                            
JRNL        REF    J.MED.CHEM.                                2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27167608                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00212                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.06 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 25759                          
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)  : 0.157                          
REMARK   3   R VALUE            (WORKING SET)  : 0.155                          
REMARK   3   FREE R VALUE                      : 0.196                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1308                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.06                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.14                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 88.66                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2523                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1670                   
REMARK   3   BIN FREE R VALUE                        : 0.2270                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.97                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 132                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2973                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 342                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.60670                                              
REMARK   3    B22 (A**2) : -7.80600                                             
REMARK   3    B33 (A**2) : 4.19930                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.10740                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.190               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.179               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.150               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.168               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.147               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3114   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4227   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1094   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 76     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 469    ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3114   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 398    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3748   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.012                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.52                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.65                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|55 - A|425 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   30.3993   14.6849    0.9569           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1006 T22:   -0.0540                                    
REMARK   3     T33:   -0.0902 T12:   -0.0044                                    
REMARK   3     T13:    0.0013 T23:   -0.0368                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4427 L22:    1.0683                                    
REMARK   3     L33:    1.2492 L12:   -0.1149                                    
REMARK   3     L13:    0.1503 L23:   -0.2560                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0442 S12:   -0.0210 S13:    0.0227                     
REMARK   3     S21:    0.0122 S22:   -0.0569 S23:    0.0804                     
REMARK   3     S31:   -0.0211 S32:    0.0732 S33:    0.0127                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220259.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M NACL, 0.1M HEPES/NAOHPH=7.4,        
REMARK 280  28.8%W/V PEG 3350, PH 7.4, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 297K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.83150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.66450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.83150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.66450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 550 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 MG    MG A 501  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 889  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 912  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     MET A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     THR A    54                                                      
REMARK 465     ASN A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 241    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  73     -172.97    -68.13                                   
REMARK 500    LYS A 266       73.81   -102.24                                   
REMARK 500    SER A 273     -114.55     65.62                                   
REMARK 500    HIS A 399       54.67   -109.28                                   
REMARK 500    LYS A 400     -164.46   -112.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 285   O                                                      
REMARK 620 2 HOH A 738   O   100.8                                              
REMARK 620 3 HOH A 889   O   123.3  91.0                                        
REMARK 620 4 GLU A 285   O     0.0 100.8 123.3                                  
REMARK 620 5 HOH A 889   O   123.6  91.6   0.7 123.6                            
REMARK 620 6 HOH A 738   O    77.6 177.0  92.0  77.6  91.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6HO A 505                 
DBREF  5JAL A   46   428  UNP    Q13093   PAFA_HUMAN      46    428             
SEQADV 5JAL HIS A  429  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAL HIS A  430  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAL HIS A  431  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAL HIS A  432  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAL HIS A  433  UNP  Q13093              EXPRESSION TAG                 
SEQRES   1 A  388  MET ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG          
SEQRES   2 A  388  GLY ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET          
SEQRES   3 A  388  PHE ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR          
SEQRES   4 A  388  TYR PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP          
SEQRES   5 A  388  ILE PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE          
SEQRES   6 A  388  LEU GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU          
SEQRES   7 A  388  LEU PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER          
SEQRES   8 A  388  PRO LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE          
SEQRES   9 A  388  SER HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA          
SEQRES  10 A  388  ILE GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA          
SEQRES  11 A  388  ALA VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR          
SEQRES  12 A  388  TYR PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS          
SEQRES  13 A  388  SER TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU          
SEQRES  14 A  388  THR HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS          
SEQRES  15 A  388  GLU CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP          
SEQRES  16 A  388  HIS GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE          
SEQRES  17 A  388  ASP MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS          
SEQRES  18 A  388  ILE ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL          
SEQRES  19 A  388  ILE GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY          
SEQRES  20 A  388  ILE ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU          
SEQRES  21 A  388  VAL TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN          
SEQRES  22 A  388  SER GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET          
SEQRES  23 A  388  LYS LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE          
SEQRES  24 A  388  THR ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE          
SEQRES  25 A  388  THR PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS          
SEQRES  26 A  388  LEU LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU          
SEQRES  27 A  388  SER ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU          
SEQRES  28 A  388  GLY LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE          
SEQRES  29 A  388  GLU GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE          
SEQRES  30 A  388  ASN THR THR ASN GLN HIS HIS HIS HIS HIS HIS                  
HET     MG  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     CL  A 503       1                                                       
HET    DMS  A 504       4                                                       
HET    6HO  A 505      24                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     6HO (2,5-DIHYDRO-1H-PYRROL-1-YL)(3-FLUOROPHENYL)METHANONE            
FORMUL   2   MG    MG 2+                                                        
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  DMS    C2 H6 O S                                                    
FORMUL   6  6HO    C11 H10 F N O                                                
FORMUL   7  HOH   *342(H2 O)                                                    
HELIX    1 AA1 ASN A  100  LEU A  111  1                                  12    
HELIX    2 AA2 TRP A  115  GLY A  126  1                                  12    
HELIX    3 AA3 TYR A  160  HIS A  170  1                                  11    
HELIX    4 AA4 ASP A  192  GLY A  199  1                                   8    
HELIX    5 AA5 LYS A  210  GLU A  212  5                                   3    
HELIX    6 AA6 GLU A  213  GLY A  242  1                                  30    
HELIX    7 AA7 ASP A  254  LYS A  259  5                                   6    
HELIX    8 AA8 SER A  273  ASP A  286  1                                  14    
HELIX    9 AA9 TYR A  324  LYS A  333  1                                  10    
HELIX   10 AB1 VAL A  350  ALA A  360  5                                  11    
HELIX   11 AB2 GLY A  362  LEU A  369  1                                   8    
HELIX   12 AB3 ASP A  376  GLY A  397  1                                  22    
HELIX   13 AB4 ASP A  401  GLN A  404  5                                   4    
HELIX   14 AB5 TRP A  405  GLU A  410  1                                   6    
SHEET    1 AA111 ASP A  94  LEU A  96  0                                        
SHEET    2 AA111 THR A 129  TRP A 134 -1  O  THR A 130   N  THR A  95           
SHEET    3 AA111 VAL A  65  PHE A  72  1  N  VAL A  65   O  ASN A 133           
SHEET    4 AA111 THR A  79  PRO A  86 -1  O  TYR A  85   N  GLY A  66           
SHEET    5 AA111 ILE A 173  VAL A 177 -1  O  VAL A 174   N  TYR A  84           
SHEET    6 AA111 TYR A 144  SER A 150  1  N  VAL A 147   O  ALA A 175           
SHEET    7 AA111 ILE A 262  HIS A 272  1  O  ASP A 263   N  TYR A 144           
SHEET    8 AA111 CYS A 291  LEU A 295  1  O  LEU A 295   N  GLY A 271           
SHEET    9 AA111 LEU A 314  SER A 319  1  O  PHE A 315   N  ALA A 294           
SHEET   10 AA111 ARG A 341  ILE A 346  1  O  ILE A 344   N  ASN A 318           
SHEET   11 AA111 LEU A 416  PRO A 418 -1  O  ILE A 417   N  THR A 345           
SHEET    1 AA2 2 ALA A 186  TYR A 189  0                                        
SHEET    2 AA2 2 SER A 202  TYR A 205 -1  O  LEU A 204   N  THR A 187           
LINK         O   GLU A 285                MG    MG A 501     1555   1555  2.33  
LINK        MG    MG A 501                 O   HOH A 738     1555   1555  2.43  
LINK        MG    MG A 501                 O   HOH A 889     1555   1555  2.24  
LINK         O   GLU A 285                MG    MG A 501     1555   2655  2.33  
LINK        MG    MG A 501                 O   HOH A 889     1555   2655  2.24  
LINK        MG    MG A 501                 O   HOH A 738     1555   2655  2.41  
CISPEP   1 PHE A   72    ASP A   73          0       -10.40                     
SITE     1 AC1  3 GLU A 285  HOH A 738  HOH A 889                               
SITE     1 AC2  1 HIS A 351                                                     
SITE     1 AC3  3 LEU A  93  PRO A 325  ALA A 326                               
SITE     1 AC4  6 LEU A 153  SER A 273  TRP A 298  PHE A 322                    
SITE     2 AC4  6 HOH A 607  HOH A 660                                          
SITE     1 AC5  7 PHE A 110  LEU A 111  LEU A 153  GLY A 154                    
SITE     2 AC5  7 GLN A 352  LEU A 369  HOH A 774                               
CRYST1   99.663   91.329   51.422  90.00 111.79  90.00 C 1 2 1       4          
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      0.010034  0.000000  0.004011        0.00000                         
SCALE2      0.000000  0.010949  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020943        0.00000                         
TER    3007      THR A 425                                                      
MASTER      332    0    5   14   13    0    7    6 3336    1   32   30          
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:
ESTHER Home Page and ACEDB Home Page
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