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LongText Report for: 5yea-pdb

Name Class
5yea-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-SEP-17   5YEA              
TITLE     THE CRYSTAL STRUCTURE OF LP-PLA2 IN COMPLEX WITH A NOVEL INHIBITOR    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 47-429;                                       
COMPND   5 SYNONYM: LP-PLA2,PAF ACETYLHYDROLASE,1-ALKYL-2-                      
COMPND   6 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE,2-ACETYL-1-                     
COMPND   7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA PHOSPHOLIPASE A2,     
COMPND   8 GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-PLA(2),PAF 2-         
COMPND   9 ACYLHYDROLASE;                                                       
COMPND  10 EC: 3.1.1.47;                                                        
COMPND  11 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    HYDROLASE INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.F.LIU,Y.C.XU                                                        
REVDAT   1   25-JUL-18 5YEA    0                                                
JRNL        AUTH   Q.LIU,F.HUANG,X.YUAN,K.WANG,Y.ZOU,J.SHEN,Y.XU                
JRNL        TITL   STRUCTURE-GUIDED DISCOVERY OF NOVEL, POTENT, AND ORALLY      
JRNL        TITL 2 BIOAVAILABLE INHIBITORS OF LIPOPROTEIN-ASSOCIATED            
JRNL        TITL 3 PHOSPHOLIPASE A2.                                            
JRNL        REF    J. MED. CHEM.                 V.  60 10231 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29193967                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01530                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 72308                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3564                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.7037 -  5.2723    1.00     3011   163  0.1794 0.2187        
REMARK   3     2  5.2723 -  4.1866    1.00     2958   151  0.1544 0.1792        
REMARK   3     3  4.1866 -  3.6579    1.00     2956   152  0.1526 0.1936        
REMARK   3     4  3.6579 -  3.3236    1.00     2940   142  0.1638 0.1699        
REMARK   3     5  3.3236 -  3.0855    0.99     2911   153  0.1827 0.2133        
REMARK   3     6  3.0855 -  2.9037    0.99     2885   166  0.1811 0.2248        
REMARK   3     7  2.9037 -  2.7583    0.98     2857   156  0.1852 0.2278        
REMARK   3     8  2.7583 -  2.6383    0.98     2869   147  0.1807 0.2246        
REMARK   3     9  2.6383 -  2.5367    0.97     2820   160  0.1834 0.2119        
REMARK   3    10  2.5367 -  2.4492    0.97     2865   143  0.1821 0.2009        
REMARK   3    11  2.4492 -  2.3726    0.96     2786   140  0.1759 0.2288        
REMARK   3    12  2.3726 -  2.3048    0.96     2820   142  0.1808 0.2105        
REMARK   3    13  2.3048 -  2.2442    0.97     2830   148  0.1768 0.1981        
REMARK   3    14  2.2442 -  2.1894    0.97     2845   141  0.1711 0.2055        
REMARK   3    15  2.1894 -  2.1397    0.97     2831   141  0.1722 0.1938        
REMARK   3    16  2.1397 -  2.0941    0.98     2852   135  0.1742 0.2343        
REMARK   3    17  2.0941 -  2.0522    0.97     2850   144  0.1808 0.2160        
REMARK   3    18  2.0522 -  2.0135    0.96     2816   154  0.1900 0.2112        
REMARK   3    19  2.0135 -  1.9776    0.96     2783   132  0.1903 0.2101        
REMARK   3    20  1.9776 -  1.9440    0.95     2808   139  0.1949 0.2642        
REMARK   3    21  1.9440 -  1.9127    0.93     2700   143  0.2024 0.2501        
REMARK   3    22  1.9127 -  1.8832    0.90     2588   151  0.2172 0.2627        
REMARK   3    23  1.8832 -  1.8556    0.82     2406   126  0.2246 0.2764        
REMARK   3    24  1.8556 -  1.8294    0.76     2171   118  0.2395 0.3012        
REMARK   3    25  1.8294 -  1.8047    0.53     1586    77  0.2660 0.2849        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.55                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           5979                                  
REMARK   3   ANGLE     :  0.952           8125                                  
REMARK   3   CHIRALITY :  0.055            878                                  
REMARK   3   PLANARITY :  0.006           1043                                  
REMARK   3   DIHEDRAL  :  7.383           3519                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005136.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.16300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.96100                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 5I8P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.6, 0.4M LI2SO4, 27%       
REMARK 280  (W/V) (NH4)2SO4, 1M NA-AC, 1.4% 1,4-BUTANEDIOL, VAPOR DIFFUSION,    
REMARK 280  HANGING 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       57.89550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.70400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.89550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.70400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 14330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 180 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER 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     THR A   425                                                      
REMARK 465     ASN A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     ILE A   429                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     THR B    54                                                      
REMARK 465     ASN B   426                                                      
REMARK 465     GLN B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     ILE B   429                                                      
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     GLN A  53    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     GLN A  88    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     ASP A  91    CG   OD1  OD2                                       
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     HIS A 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP A 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 115    CZ3  CH2                                            
REMARK 470     LEU A 116    CG   CD1  CD2                                       
REMARK 470     LEU A 123    CG   CD1  CD2                                       
REMARK 470     LYS A 143    CE   NZ                                             
REMARK 470     GLN A 193    CD   OE1  NE2                                       
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     GLN A 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 212    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 220    OE1  OE2                                            
REMARK 470     LYS A 227    CD   CE   NZ                                        
REMARK 470     LYS A 246    CD   CE   NZ                                        
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 304    CG   OD1  OD2                                       
REMARK 470     LYS A 363    CG   CD   CE   NZ                                   
REMARK 470     MET A 368    CG   SD   CE                                        
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     GLU A 414    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     ARG B  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  89    CG   OD1  OD2                                       
REMARK 470     ASN B  90    CG   OD1  ND2                                       
REMARK 470     ASP B  91    CG   OD1  OD2                                       
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  93    CG   CD1  CD2                                       
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     TRP B 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 115    CZ3  CH2                                            
REMARK 470     LEU B 116    CG   CD1  CD2                                       
REMARK 470     LEU B 123    CG   CD1  CD2                                       
REMARK 470     ASN B 133    OD1  ND2                                            
REMARK 470     GLU B 142    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 143    CE   NZ                                             
REMARK 470     GLN B 193    CD   OE1  NE2                                       
REMARK 470     GLU B 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     GLN B 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 212    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 227    CD   CE   NZ                                        
REMARK 470     LYS B 246    CD   CE   NZ                                        
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     GLU B 256    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 290    CZ   NH1  NH2                                       
REMARK 470     ASP B 304    CG   OD1  OD2                                       
REMARK 470     ARG B 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 363    CG   CD   CE   NZ                                   
REMARK 470     MET B 368    CG   SD   CE                                        
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A    92     O    HOH A   601              1.80            
REMARK 500   NH1  ARG A    92     O    HOH A   602              2.14            
REMARK 500   OG   SER A   336     OD1  ASP A   338              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE   ARG A    92     OD2  ASP B   200     3555     1.78            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  92   CB    ARG A  92   CG      0.276                       
REMARK 500    ARG A  92   CG    ARG A  92   CD      0.222                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  92   CA  -  CB  -  CG  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ARG A  92   CB  -  CG  -  CD  ANGL. DEV. =  26.2 DEGREES          
REMARK 500    ARG A  92   CD  -  NE  -  CZ  ANGL. DEV. =  20.0 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP B 200   CB  -  CG  -  OD2 ANGL. DEV. =  11.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  90       54.60   -119.54                                   
REMARK 500    HIS A 114     -166.45   -116.47                                   
REMARK 500    LYS A 252       36.47    -83.17                                   
REMARK 500    LYS A 266       74.79   -115.72                                   
REMARK 500    SER A 273     -114.85     63.54                                   
REMARK 500    HIS A 399       63.69   -108.62                                   
REMARK 500    ASP B  73     -165.30    -78.12                                   
REMARK 500    LEU B  93       72.85   -118.49                                   
REMARK 500    THR B 113     -165.44   -107.12                                   
REMARK 500    HIS B 114     -158.03   -135.53                                   
REMARK 500    LYS B 266       74.45   -115.46                                   
REMARK 500    SER B 273     -118.30     65.98                                   
REMARK 500    HIS B 399       61.02   -107.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8U9 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8U9 B 502                 
DBREF  5YEA A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  5YEA B   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
SEQADV 5YEA GLY A   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA PRO A   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA LEU A   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA GLY A   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA SER A   46  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA GLY B   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA PRO B   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA LEU B   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA GLY B   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YEA SER B   46  UNP  Q13093              EXPRESSION TAG                 
SEQRES   1 A  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 A  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 A  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 A  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 A  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 A  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 A  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 A  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 A  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 A  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 A  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 A  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 A  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 A  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 A  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 A  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 A  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 A  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 A  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 A  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 A  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 A  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 A  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 A  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 A  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 A  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 A  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 A  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 A  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 A  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
SEQRES   1 B  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 B  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 B  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 B  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 B  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 B  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 B  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 B  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 B  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 B  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 B  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 B  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 B  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 B  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 B  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 B  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 B  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 B  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 B  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 B  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 B  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 B  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 B  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 B  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 B  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 B  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 B  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 B  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 B  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 B  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    8U9  A 503      33                                                       
HET    SO4  B 501       5                                                       
HET    8U9  B 502      33                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     8U9 4-[[4-[4-CHLORANYL-3-(TRIFLUOROMETHYL)PHENOXY]-3-CYANO-          
HETNAM   2 8U9  PHENYL]SULFAMOYL]BENZOIC ACID                                   
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   5  8U9    2(C21 H12 CL F3 N2 O5 S)                                     
FORMUL   8  HOH   *395(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  HIS A  241  1                                  29    
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 GLY A  303  ARG A  309  5                                   7    
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    
HELIX   16 AB7 ASN B  100  GLY B  112  1                                  13    
HELIX   17 AB8 HIS B  114  GLY B  126  1                                  13    
HELIX   18 AB9 TYR B  160  HIS B  170  1                                  11    
HELIX   19 AC1 ASP B  192  ILE B  198  1                                   7    
HELIX   20 AC2 LYS B  210  GLU B  212  5                                   3    
HELIX   21 AC3 GLU B  213  HIS B  241  1                                  29    
HELIX   22 AC4 ASP B  254  LYS B  259  5                                   6    
HELIX   23 AC5 SER B  273  ASP B  286  1                                  14    
HELIX   24 AC6 GLY B  303  TYR B  307  5                                   5    
HELIX   25 AC7 TYR B  324  CYS B  334  1                                  11    
HELIX   26 AC8 VAL B  350  ALA B  360  5                                  11    
HELIX   27 AC9 GLY B  362  LEU B  369  1                                   8    
HELIX   28 AD1 ASP B  376  GLY B  397  1                                  22    
HELIX   29 AD2 ASP B  401  GLN B  404  5                                   4    
HELIX   30 AD3 TRP B  405  GLU B  410  1                                   6    
SHEET    1 AA110 ASN A 133  TRP A 134  0                                        
SHEET    2 AA110 VAL A  65  PHE A  72  1  N  VAL A  65   O  ASN A 133           
SHEET    3 AA110 THR A  79  PRO A  86 -1  O  TYR A  85   N  GLY A  66           
SHEET    4 AA110 ILE A 173  VAL A 177 -1  O  VAL A 174   N  TYR A  84           
SHEET    5 AA110 TYR A 144  SER A 150  1  N  VAL A 147   O  ALA A 175           
SHEET    6 AA110 ILE A 262  HIS A 272  1  O  ILE A 270   N  VAL A 148           
SHEET    7 AA110 CYS A 291  LEU A 295  1  O  LEU A 295   N  GLY A 271           
SHEET    8 AA110 LEU A 314  SER A 319  1  O  PHE A 315   N  ALA A 294           
SHEET    9 AA110 ARG A 341  ILE A 346  1  O  ILE A 344   N  ASN A 318           
SHEET   10 AA110 LEU A 416  PRO A 418 -1  O  ILE A 417   N  THR A 345           
SHEET    1 AA2 2 THR A  95  LEU A  96  0                                        
SHEET    2 AA2 2 THR A 129  THR A 130 -1  O  THR A 130   N  THR A  95           
SHEET    1 AA3 2 ALA A 186  TYR A 189  0                                        
SHEET    2 AA3 2 SER A 202  TYR A 205 -1  O  LEU A 204   N  THR A 187           
SHEET    1 AA410 ASN B 133  TRP B 134  0                                        
SHEET    2 AA410 VAL B  65  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3 AA410 THR B  79  PRO B  86 -1  O  LEU B  83   N  THR B  68           
SHEET    4 AA410 ILE B 173  VAL B 177 -1  O  VAL B 174   N  TYR B  84           
SHEET    5 AA410 TYR B 144  SER B 150  1  N  VAL B 147   O  ALA B 175           
SHEET    6 AA410 ILE B 262  HIS B 272  1  O  ASP B 263   N  TYR B 144           
SHEET    7 AA410 CYS B 291  LEU B 295  1  O  LEU B 295   N  GLY B 271           
SHEET    8 AA410 LEU B 314  SER B 319  1  O  PHE B 315   N  ALA B 294           
SHEET    9 AA410 ARG B 341  ILE B 346  1  O  ILE B 344   N  ASN B 318           
SHEET   10 AA410 LEU B 416  PRO B 418 -1  O  ILE B 417   N  THR B 345           
SHEET    1 AA5 2 THR B  95  LEU B  96  0                                        
SHEET    2 AA5 2 THR B 129  THR B 130 -1  O  THR B 130   N  THR B  95           
SHEET    1 AA6 2 ALA B 186  TYR B 189  0                                        
SHEET    2 AA6 2 SER B 202  TYR B 205 -1  O  SER B 202   N  TYR B 189           
CISPEP   1 PHE A   72    ASP A   73          0        -4.74                     
CISPEP   2 PHE B   72    ASP B   73          0        -2.93                     
SITE     1 AC1  7 ASP A  89  ASN A  90  HOH A 603  HOH A 648                    
SITE     2 AC1  7 ASN B 100  LYS B 101  ARG B 122                               
SITE     1 AC2  9 LYS A 101  GLY A 199  LYS A 201  HOH A 607                    
SITE     2 AC2  9 HOH A 614  HOH A 630  HOH A 721  ARG B 182                    
SITE     3 AC2  9 ARG B 207                                                     
SITE     1 AC3 14 LEU A 107  PHE A 110  LEU A 111  LEU A 121                    
SITE     2 AC3 14 GLY A 152  LEU A 153  GLY A 154  ALA A 155                    
SITE     3 AC3 14 HIS A 272  SER A 273  GLN A 352  ALA A 355                    
SITE     4 AC3 14 ASP A 356  PHE A 357                                          
SITE     1 AC4  9 HIS A 241  ARG A 264  HOH A 628  SER B 308                    
SITE     2 AC4  9 ARG B 309  ILE B 310  PRO B 311  LYS B 339                    
SITE     3 AC4  9 HOH B 603                                                     
SITE     1 AC5 15 LEU B 107  PHE B 110  LEU B 111  LEU B 121                    
SITE     2 AC5 15 GLY B 152  LEU B 153  GLY B 154  HIS B 272                    
SITE     3 AC5 15 SER B 273  GLN B 352  ALA B 355  ASP B 356                    
SITE     4 AC5 15 PHE B 357  LEU B 371  HOH B 606                               
CRYST1  115.791   83.408   96.889  90.00 114.57  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008636  0.000000  0.003948        0.00000                         
SCALE2      0.000000  0.011989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011348        0.00000                         
TER    2895      THR A 424                                                      
TER    5756      THR B 425                                                      
MASTER      459    0    5   30   28    0   16    6 6230    2   81   60          
END                                                                             

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