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LongText Report for: 5jar-pdb

Name Class
5jar-pdb
HEADER    HYDROLASE                               12-APR-16   5JAR              
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 5JAR    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.    2.11 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) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23576                          
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)  : 0.147                          
REMARK   3   R VALUE            (WORKING SET)  : 0.144                          
REMARK   3   FREE R VALUE                      : 0.204                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1198                           
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) : 2.11                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.21                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 91.04                    
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) : 2558                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1780                   
REMARK   3   BIN FREE R VALUE                        : 0.2650                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.36                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 145                      
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            : 2978                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 616                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.57450                                              
REMARK   3    B22 (A**2) : -5.27340                                             
REMARK   3    B33 (A**2) : 1.69890                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.35510                                              
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) : 0.246               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.182               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.195               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.171               
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      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3110   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4219   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1080   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 77     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 463    ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3110   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 395    ; 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   : 4170   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.012                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.89                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.48                    
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):   30.5120   14.7889    0.8225           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1012 T22:   -0.0212                                    
REMARK   3     T33:   -0.0766 T12:   -0.0026                                    
REMARK   3     T13:    0.0008 T23:   -0.0290                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1735 L22:    0.8197                                    
REMARK   3     L33:    1.0814 L12:    0.0156                                    
REMARK   3     L13:    0.1613 L23:   -0.1663                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0380 S12:   -0.0393 S13:    0.0264                     
REMARK   3     S21:   -0.0011 S22:   -0.0467 S23:    0.0507                     
REMARK   3     S31:   -0.0284 S32:    0.0783 S33:    0.0088                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JAR 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_1000220266.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-11                          
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   : 23576                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6000                            
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   (%): 49.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28.0%W/V PEG 3350, 0.1M                  
REMARK 280  HEPES/NAOHPH=7.4, 1.3M NACL, PH 7.4, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   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       49.88350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.39850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.88350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.39850            
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: 470 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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      HOH A 601  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 941  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1013  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1033  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 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     -173.34    -67.52                                   
REMARK 500    PHE A 156     -172.48   -171.86                                   
REMARK 500    LYS A 266       77.76   -101.23                                   
REMARK 500    SER A 273     -113.41     68.88                                   
REMARK 500    HIS A 399       52.36   -112.53                                   
REMARK 500    LYS A 400     -165.85   -112.11                                   
REMARK 500    THR A 424       65.48   -116.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1200        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A1201        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A1202        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A1203        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A1204        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A1205        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A1206        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH A1207        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH A1208        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH A1209        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH A1210        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A1211        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A1212        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH A1213        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH A1214        DISTANCE =  8.63 ANGSTROMS                       
REMARK 525    HOH A1215        DISTANCE =  8.84 ANGSTROMS                       
REMARK 525    HOH A1216        DISTANCE =  9.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS 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 6HV A 504                 
DBREF  5JAR A   46   428  UNP    Q13093   PAFA_HUMAN      46    428             
SEQADV 5JAR HIS A  429  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAR HIS A  430  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAR HIS A  431  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAR HIS A  432  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5JAR 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    DMS  A 501       4                                                       
HET     CL  A 502       1                                                       
HET     CL  A 503       1                                                       
HET    6HV  A 504      36                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     6HV (2',6-DIMETHYL[1,1'-BIPHENYL]-3-YL)(1,3-THIAZOL-2-YL)            
HETNAM   2 6HV  METHANONE                                                       
FORMUL   2  DMS    C2 H6 O S                                                    
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  6HV    C18 H15 N O S                                                
FORMUL   6  HOH   *616(H2 O)                                                    
HELIX    1 AA1 ASN A  100  LEU A  111  1                                  12    
HELIX    2 AA2 HIS A  114  GLY A  126  1                                  13    
HELIX    3 AA3 TYR A  160  HIS A  170  1                                  11    
HELIX    4 AA4 ASP A  192  GLY A  199  1                                   8    
HELIX    5 AA5 LYS A  210  GLU A  212  5                                   3    
HELIX    6 AA6 GLU A  213  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 GLU A  305  ARG A  309  5                                   5    
HELIX   10 AB1 TYR A  324  LYS A  333  1                                  10    
HELIX   11 AB2 VAL A  350  ALA A  360  5                                  11    
HELIX   12 AB3 GLY A  362  LEU A  369  1                                   8    
HELIX   13 AB4 ASP A  376  GLY A  397  1                                  22    
HELIX   14 AB5 ASP A  401  GLN A  404  5                                   4    
HELIX   15 AB6 TRP A  405  GLU A  410  1                                   6    
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  ILE A 270   N  VAL A 148           
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  LYS A 342   N  PHE A 316           
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  SER A 202   N  TYR A 189           
CISPEP   1 PHE A   72    ASP A   73          0       -12.05                     
SITE     1 AC1  4 LEU A 153  SER A 273  TRP A 298  HOH A 605                    
SITE     1 AC2  4 LEU A  93  PRO A 325  ALA A 326  HOH A 711                    
SITE     1 AC3  3 VAL A 350  HIS A 351  HOH A1174                               
SITE     1 AC4 10 LEU A 107  PHE A 110  LEU A 111  PHE A 125                    
SITE     2 AC4 10 LEU A 153  GLY A 154  GLN A 352  PHE A 357                    
SITE     3 AC4 10 LEU A 371  HOH A 668                                          
CRYST1   99.767   90.797   51.348  90.00 111.76  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      0.010023  0.000000  0.004001        0.00000                         
SCALE2      0.000000  0.011014  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020969        0.00000                         
TER    2993      THR A 425                                                      
MASTER      338    0    4   15   13    0    6    6 3621    1   40   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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