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LongText Report for: 3WK8-pdb

Name Class
3WK8-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           17-OCT-13   3WK8              
TITLE     CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH        
TITLE    2 FRAGMENT INHIBITOR                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOSOLIC EPOXIDE HYDROLASE 2, CEH, EPOXIDE HYDRATASE,      
COMPND   5 SOLUBLE EPOXIDE HYDROLASE, SEH, LIPID-PHOSPHATE PHOSPHATASE;         
COMPND   6 EC: 3.3.2.10, 3.1.3.76;                                              
COMPND   7 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: EPHX2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.AMANO,T.YAMAGUCHI,E.TANABE                                          
REVDAT   1   16-APR-14 3WK8    0                                                
JRNL        AUTH   Y.AMANO,T.YAMAGUCHI,E.TANABE                                 
JRNL        TITL   STRUCTURAL INSIGHTS INTO BINDING OF INHIBITORS TO SOLUBLE    
JRNL        TITL 2 EPOXIDE HYDROLASE GAINED BY FRAGMENT SCREENING AND X-RAY     
JRNL        TITL 3 CRYSTALLOGRAPHY                                              
JRNL        REF    BIOORG.MED.CHEM.                           2014              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   24656800                                                     
JRNL        DOI    10.1016/J.BMC.2014.03.001                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30641                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1634                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2189                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 119                          
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.264         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.668         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4447 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6029 ; 2.141 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   545 ; 7.052 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;34.730 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   783 ;18.634 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;27.713 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   659 ; 0.133 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3360 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3WK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096439.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30641                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M POTASSIUM PHOSPHATE, 0.2M           
REMARK 280  AMMONIUM DIHYDROGEN PHOSPHATE, 25%W/V PEG 3350, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      162.62333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.31167            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.96750            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.65583            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      203.27917            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      162.62333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       81.31167            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.65583            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      121.96750            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      203.27917            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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   BIOMT1   2 -1.000000  0.000000  0.000000      -92.47300            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      121.96750            
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     1                                                      
REMARK 465     ASN A   548                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     HIS A   556                                                      
REMARK 465     HIS A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     HIS A   561                                                      
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   OE1  GLU A    69     OE1  GLU A    69     7465     2.11            
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    ASP A  93   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU A 183   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    PRO A 225   C   -  N   -  CA  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU A 438   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG A 482   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 482   NE  -  CZ  -  NH2 ANGL. DEV. =   7.2 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    LEU A  10      -69.89    -90.12                                   
REMARK 500    VAL A  13      -69.15   -122.62                                   
REMARK 500    ASN A  85       -4.40     87.08                                   
REMARK 500    GLN A 204      -98.59    -98.11                                   
REMARK 500    GLU A 269     -136.02   -121.56                                   
REMARK 500    ASP A 335     -131.03     61.42                                   
REMARK 500    ASN A 359      -48.26     74.66                                   
REMARK 500    LEU A 514      133.70    -38.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A  291     ASP A  292                  140.30                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  19        23.7      L          L   OUTSIDE RANGE           
REMARK 500    SER A 432        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 A 602   O1                                                     
REMARK 620 2 ASP A   9   OD2  86.0                                              
REMARK 620 3 ASP A 185   OD1 159.6  99.4                                        
REMARK 620 4 ASP A  11   O   111.7  79.3  88.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S0E A 603                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WK4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WK5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WK6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WK7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WK9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WKA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WKB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WKC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WKD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WKE   RELATED DB: PDB                                   
DBREF  3WK8 A    1   555  UNP    P34913   HYES_HUMAN       1    555             
SEQADV 3WK8 HIS A  556  UNP  P34913              EXPRESSION TAG                 
SEQADV 3WK8 HIS A  557  UNP  P34913              EXPRESSION TAG                 
SEQADV 3WK8 HIS A  558  UNP  P34913              EXPRESSION TAG                 
SEQADV 3WK8 HIS A  559  UNP  P34913              EXPRESSION TAG                 
SEQADV 3WK8 HIS A  560  UNP  P34913              EXPRESSION TAG                 
SEQADV 3WK8 HIS A  561  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  561  MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL          
SEQRES   2 A  561  LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR          
SEQRES   3 A  561  GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP          
SEQRES   4 A  561  ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG          
SEQRES   5 A  561  LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO          
SEQRES   6 A  561  LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA          
SEQRES   7 A  561  LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE          
SEQRES   8 A  561  PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO          
SEQRES   9 A  561  MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE          
SEQRES  10 A  561  THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG          
SEQRES  11 A  561  ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU          
SEQRES  12 A  561  LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL          
SEQRES  13 A  561  GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU          
SEQRES  14 A  561  LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE          
SEQRES  15 A  561  LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP          
SEQRES  16 A  561  LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR          
SEQRES  17 A  561  ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU          
SEQRES  18 A  561  LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO          
SEQRES  19 A  561  SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG          
SEQRES  20 A  561  VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA          
SEQRES  21 A  561  VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER          
SEQRES  22 A  561  TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR          
SEQRES  23 A  561  ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER          
SEQRES  24 A  561  SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL          
SEQRES  25 A  561  LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY          
SEQRES  26 A  561  LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY          
SEQRES  27 A  561  MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG          
SEQRES  28 A  561  VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO          
SEQRES  29 A  561  ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA          
SEQRES  30 A  561  ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO          
SEQRES  31 A  561  GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG          
SEQRES  32 A  561  THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL          
SEQRES  33 A  561  LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE          
SEQRES  34 A  561  VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL          
SEQRES  35 A  561  THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS          
SEQRES  36 A  561  LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN          
SEQRES  37 A  561  MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY          
SEQRES  38 A  561  ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU          
SEQRES  39 A  561  LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET          
SEQRES  40 A  561  GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU          
SEQRES  41 A  561  ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU          
SEQRES  42 A  561  VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA          
SEQRES  43 A  561  ARG ASN PRO PRO VAL VAL SER LYS MET HIS HIS HIS HIS          
SEQRES  44 A  561  HIS HIS                                                      
HET     MG  A 601       1                                                       
HET    PO4  A 602       5                                                       
HET    S0E  A 603      14                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     S0E 6-(TRIFLUOROMETHYL)-1,3-BENZOTHIAZOL-2-AMINE                     
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  S0E    C8 H5 F3 N2 S                                                
FORMUL   5  HOH   *121(H2 O)                                                    
HELIX    1   1 ALA A   18  LEU A   30  1                                  13    
HELIX    2   2 GLY A   35  LYS A   43  1                                   9    
HELIX    3   3 GLY A   44  GLU A   47  5                                   4    
HELIX    4   4 GLY A   48  LYS A   55  1                                   8    
HELIX    5   5 THR A   59  ALA A   78  1                                  20    
HELIX    6   6 SER A   87  ARG A   99  1                                  13    
HELIX    7   7 ASN A  102  LYS A  115  1                                  14    
HELIX    8   8 ARG A  133  MET A  145  1                                  13    
HELIX    9   9 SER A  153  GLY A  157  1                                   5    
HELIX   10  10 GLU A  162  LYS A  174  1                                  13    
HELIX   11  11 SER A  176  SER A  178  5                                   3    
HELIX   12  12 ILE A  186  LEU A  196  1                                  11    
HELIX   13  13 ASP A  205  GLY A  218  1                                  14    
HELIX   14  14 ASN A  233  MET A  237  5                                   5    
HELIX   15  15 SER A  270  ARG A  275  5                                   6    
HELIX   16  16 GLN A  277  ALA A  284  1                                   8    
HELIX   17  17 GLU A  304  TYR A  308  5                                   5    
HELIX   18  18 CYS A  309  GLY A  325  1                                  17    
HELIX   19  19 ASP A  335  TYR A  348  1                                  14    
HELIX   20  20 SER A  370  ALA A  377  1                                   8    
HELIX   21  21 ASN A  378  VAL A  380  5                                   3    
HELIX   22  22 PHE A  381  PHE A  387  1                                   7    
HELIX   23  23 GLY A  391  ASN A  400  1                                  10    
HELIX   24  24 ASN A  400  PHE A  409  1                                  10    
HELIX   25  25 LYS A  421  GLY A  426  1                                   6    
HELIX   26  26 THR A  443  GLY A  458  1                                  16    
HELIX   27  27 PHE A  459  TRP A  465  1                                   7    
HELIX   28  28 ASN A  468  LYS A  478  1                                  11    
HELIX   29  29 VAL A  500  GLN A  505  5                                   6    
HELIX   30  30 HIS A  506  TRP A  510  5                                   5    
HELIX   31  31 TRP A  525  LYS A  530  1                                   6    
HELIX   32  32 LYS A  530  ALA A  546  1                                  17    
SHEET    1   A 5 PHE A 149  GLU A 152  0                                        
SHEET    2   A 5 THR A 118  THR A 123  1  N  ILE A 121   O  ILE A 151           
SHEET    3   A 5 ALA A   5  PHE A   8  1  N  PHE A   8   O  ALA A 120           
SHEET    4   A 5 VAL A 180  ASP A 184  1  O  LEU A 183   N  VAL A   7           
SHEET    5   A 5 VAL A 199  LEU A 202  1  O  VAL A 199   N  PHE A 182           
SHEET    1   B 2 ALA A  15  LEU A  16  0                                        
SHEET    2   B 2 LYS A 100  ILE A 101 -1  O  LYS A 100   N  LEU A  16           
SHEET    1   C 8 SER A 238  LYS A 245  0                                        
SHEET    2   C 8 VAL A 248  LEU A 255 -1  O  PHE A 252   N  GLY A 240           
SHEET    3   C 8 ARG A 287  MET A 291 -1  O  VAL A 288   N  LEU A 255           
SHEET    4   C 8 ALA A 260  CYS A 264  1  N  VAL A 261   O  LEU A 289           
SHEET    5   C 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6   C 8 VAL A 352  LEU A 358  1  O  ALA A 356   N  PHE A 331           
SHEET    7   C 8 ALA A 488  ALA A 493  1  O  VAL A 491   N  SER A 357           
SHEET    8   C 8 LYS A 515  ILE A 519  1  O  LYS A 515   N  ALA A 488           
LINK        MG    MG A 601                 O1  PO4 A 602     1555   1555  2.02  
LINK         OD2 ASP A   9                MG    MG A 601     1555   1555  2.33  
LINK         OD1 ASP A 185                MG    MG A 601     1555   1555  2.40  
LINK         O   ASP A  11                MG    MG A 601     1555   1555  2.63  
CISPEP   1 LEU A   16    PRO A   17          0       -11.84                     
CISPEP   2 LYS A  160    PRO A  161          0         2.25                     
CISPEP   3 PHE A  267    PRO A  268          0        -7.38                     
SITE     1 AC1  5 ASP A   9  ASP A  11  ASP A 185  ILE A 186                    
SITE     2 AC1  5 PO4 A 602                                                     
SITE     1 AC2  6 ASP A   9  ASP A  11  THR A 123  ASN A 124                    
SITE     2 AC2  6 LYS A 160   MG A 601                                          
SITE     1 AC3 11 PHE A 267  TYR A 383  PHE A 387  LEU A 408                    
SITE     2 AC3 11 MET A 419  LEU A 428  TYR A 466  ASP A 496                    
SITE     3 AC3 11 VAL A 498  HIS A 524  HOH A 720                               
CRYST1   92.473   92.473  243.935  90.00  90.00 120.00 P 65 2 2     12          
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      0.010814  0.006243  0.000000        0.00000                         
SCALE2      0.000000  0.012487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004099        0.00000                         
TER    4324      ARG A 547                                                      
MASTER      437    0    3   32   15    0    7    6 4464    1   23   44          
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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