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LongText Report for: 5lz4-pdb

Name Class
5lz4-pdb
HEADER    HYDROLASE                               29-SEP-16   5LZ4              
TITLE     FRAGMENT-BASED INHIBITORS OF LIPOPROTEIN ASSOCIATED PHOSPHOLIPASE A2  
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;                                                     
COMPND  10 MUTATION: 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    LP-PLA2 PHOSPHOLIPASE, HYDROLASE, LIPID METABOLISM, INHIBITORS, LP-   
KEYWDS   2 PLA2#4                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.WOOLFORD,P.DAY                                                      
REVDAT   1   21-DEC-16 5LZ4    0                                                
JRNL        AUTH   A.J.WOOLFORD,P.J.DAY,V.BENETON,V.BERDINI,J.E.COYLE,Y.DUDIT,  
JRNL        AUTH 2 P.GRONDIN,P.HUET,L.Y.LEE,E.S.MANAS,R.L.MCMENAMIN,C.W.MURRAY, 
JRNL        AUTH 3 L.W.PAGE,V.K.PATEL,F.POTVAIN,S.J.RICH,Y.SANG,D.O.SOMERS,     
JRNL        AUTH 4 L.TROTTET,Z.WAN,X.ZHANG                                      
JRNL        TITL   FRAGMENT-BASED APPROACH TO THE DEVELOPMENT OF AN ORALLY      
JRNL        TITL 2 BIOAVAILABLE LACTAM INHIBITOR OF LIPOPROTEIN-ASSOCIATED      
JRNL        TITL 3 PHOSPHOLIPASE A2 (LP-PLA2).                                  
JRNL        REF    J. MED. CHEM.                 V.  59 10738 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27933945                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01427                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23972                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1284                            
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) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1657                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.2250                       
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          : 22                                      
REMARK   3   SOLVENT ATOMS            : 386                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.96000                                             
REMARK   3    B22 (A**2) : 1.50000                                              
REMARK   3    B33 (A**2) : -0.37000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.198         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.650         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3129 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2967 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4249 ; 1.455 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6840 ; 1.119 ; 2.987       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   389 ; 6.539 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;37.126 ;23.747       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   547 ;15.223 ;15.027       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;15.852 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   455 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3562 ; 0.001 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   753 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1509 ; 0.909 ; 2.937       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1508 ; 0.907 ; 2.935       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1620 ; 1.116 ; 3.230       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1621 ; 1.116 ; 3.231       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1106 ; 2.283 ; 6.704       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    55        A   425                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4898  14.6393   0.8151              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0014 T22:   0.0861                                     
REMARK   3      T33:   0.0178 T12:   0.0071                                     
REMARK   3      T13:  -0.0033 T23:  -0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0893 L22:   1.6784                                     
REMARK   3      L33:   2.0316 L12:  -0.0419                                     
REMARK   3      L13:   0.1615 L23:  -0.3426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0365 S12:  -0.0043 S13:   0.0178                       
REMARK   3      S21:  -0.0125 S22:  -0.0476 S23:   0.0821                       
REMARK   3      S31:  -0.0089 S32:   0.0660 S33:   0.0111                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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) : 1.5418                             
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 6.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
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       49.96750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.47400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.96750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.47400            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 230 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 602  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 920  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 941  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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     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     -176.63    -62.48                                   
REMARK 500    SER A 273     -107.76     65.93                                   
REMARK 500    HIS A 399       55.32   -114.73                                   
REMARK 500    LYS A 400     -164.06   -114.96                                   
REMARK 500    ASP A 413      148.14   -171.12                                   
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 A 979        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 980        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH A 981        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 982        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A 983        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 984        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 985        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A 986        DISTANCE =  8.50 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL 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 7BW A 503                 
DBREF  5LZ4 A   46   428  UNP    Q13093   PAFA_HUMAN      46    428             
SEQADV 5LZ4 HIS A  429  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5LZ4 HIS A  430  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5LZ4 HIS A  431  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5LZ4 HIS A  432  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5LZ4 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     CL  A 501       1                                                       
HET     CL  A 502       1                                                       
HET    7BW  A 503      37                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     7BW 5-[2-(4,4-DIMETHYL-2-OXIDANYLIDENE-PYRROLIDIN-1-YL)              
HETNAM   2 7BW  ETHOXY]-2-FLUORANYL-BENZENECARBONITRILE                         
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4  7BW    C15 H17 F N2 O2                                              
FORMUL   5  HOH   *386(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 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  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  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  SER A 202   N  TYR A 189           
CISPEP   1 PHE A   72    ASP A   73          0       -14.60                     
SITE     1 AC1  5 LEU A  93  PRO A 325  ALA A 326  HOH A 638                    
SITE     2 AC1  5 HOH A 931                                                     
SITE     1 AC2  3 PHE A 322  VAL A 350  HIS A 351                               
SITE     1 AC3 13 LEU A 107  GLY A 152  LEU A 153  GLY A 154                    
SITE     2 AC3 13 LEU A 159  SER A 273  PHE A 274  TRP A 298                    
SITE     3 AC3 13 HIS A 351  GLN A 352  ALA A 355  ASP A 356                    
SITE     4 AC3 13 PHE A 357                                                     
CRYST1   99.935   90.948   51.340  90.00 111.86  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      0.010007  0.000000  0.004015        0.00000                         
SCALE2      0.000000  0.010995  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020987        0.00000                         
TER    3030      THR A 425                                                      
MASTER      353    0    3   14   13    0    7    6 3386    1   37   30          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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