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LongText Report for: 6i5g-pdb

Name Class
6i5g-pdb
HEADER    HYDROLASE                               13-NOV-18   6I5G              
TITLE     X-RAY STRUCTURE OF HUMAN SOLUBLE EPOXIDE HYDROLASE C-TERMINAL DOMAIN  
TITLE    2 (HSEH CTD)IN COMPLEX WITH 15D-PGJ2                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.3.2.10,3.1.3.76;                                               
COMPND   5 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                                         
KEYWDS    HSEH CTD, APOPROTEIN, ALPHA_BETA HYDROLASE FOLD, 15D-PGJ2, HYDROLASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.ABIS,J.KOPEC,W.W.YUE,M.R.CONTE                                      
REVDAT   1   29-MAY-19 6I5G    0                                                
JRNL        AUTH   G.ABIS,R.L.CHARLES,J.KOPEC,W.W.YUE,R.A.ATKINSON,T.T.T.BUI,   
JRNL        AUTH 2 S.LYNHAM,S.POPOVA,Y.-B.SUN,F.FRATERNALI,P.EATON,M.R.CONTE    
JRNL        TITL   15-DEOXY-DELTA12,14-PROSTAGLANDIN J2 INHIBITS HUMAN SOLUBLE  
JRNL        TITL 2 EPOXIDE HYDROLASE BY A DUAL ORTHOSTERIC AND ALLOSTERIC       
JRNL        TITL 3 MECHANISM                                                    
JRNL        REF    COMMUN BIOL                                2019              
JRNL        REFN                   ESSN 2399-3642                               
JRNL        DOI    10.1038/S42003-019-0426-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 46528                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2403                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3173                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47000                                              
REMARK   3    B22 (A**2) : -2.17000                                             
REMARK   3    B33 (A**2) : 1.35000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.33000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.594         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5341 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5007 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7220 ; 2.062 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11558 ; 1.212 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   638 ; 7.240 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;35.197 ;23.934       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   884 ;15.958 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;15.581 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   745 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5962 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1254 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2534 ; 2.769 ; 3.135       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2535 ; 2.768 ; 3.136       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3166 ; 3.910 ; 4.687       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3167 ; 3.909 ; 4.688       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2807 ; 3.679 ; 3.551       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2808 ; 3.678 ; 3.553       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4050 ; 5.546 ; 5.155       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6240 ; 7.349 ;25.585       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6241 ; 7.349 ;25.594       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6I5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012863.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48933                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.990                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70200                            
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: REFMAC                                                
REMARK 200 STARTING MODEL: 3ANS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 3350, 0.2 M MALIC ACID, PH     
REMARK 280  7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2                                       
REMARK 290       4555   -X+1/2,Y+1/2,-Z+1/2                                     
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       38.57391            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.99600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.90645            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.57391            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.99600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       51.90645            
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 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     THR A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     ASN A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     TYR A   224                                                      
REMARK 465     PHE A   225                                                      
REMARK 465     GLN A   226                                                      
REMARK 465     GLY A   227                                                      
REMARK 465     SER A   228                                                      
REMARK 465     SER A   229                                                      
REMARK 465     ALA A   546                                                      
REMARK 465     ARG A   547                                                      
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     MET B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     THR B   220                                                      
REMARK 465     GLU B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     LEU B   223                                                      
REMARK 465     TYR B   224                                                      
REMARK 465     PHE B   225                                                      
REMARK 465     GLN B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     SER B   228                                                      
REMARK 465     SER B   229                                                      
REMARK 465     ALA B   546                                                      
REMARK 465     ARG B   547                                                      
REMARK 465     ASN B   548                                                      
REMARK 465     PRO B   549                                                      
REMARK 465     PRO B   550                                                      
REMARK 465     VAL B   551                                                      
REMARK 465     VAL B   552                                                      
REMARK 465     SER B   553                                                      
REMARK 465     LYS B   554                                                      
REMARK 465     MET B   555                                                      
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     THR A 230    OG1  CG2                                            
REMARK 470     SER A 231    OG                                                  
REMARK 470     THR B 230    OG1  CG2                                            
REMARK 470     SER B 231    OG                                                  
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   OH   TYR B   466     O    HOH B   701              1.92            
REMARK 500   OG   SER A   432     O    HOH A   701              2.02            
REMARK 500   O    HOH A   706     O    HOH A   764              2.15            
REMARK 500   O    TRP A   510     O    HOH A   702              2.17            
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 275   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    LEU A 428   CB  -  CG  -  CD1 ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG A 440   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 440   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    LEU B 340   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG B 440   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG B 440   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG B 440   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    MET B 528   CG  -  SD  -  CE  ANGL. DEV. =  11.0 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    SER A 231     -169.39   -114.59                                   
REMARK 500    GLU A 269     -143.26   -116.56                                   
REMARK 500    ASP A 335     -126.75     60.05                                   
REMARK 500    ASN A 359      -37.93     75.00                                   
REMARK 500    ASN A 431       58.04   -117.29                                   
REMARK 500    LEU A 499       79.76   -102.88                                   
REMARK 500    HIS A 513        3.90    -64.47                                   
REMARK 500    SER B 231     -157.40   -103.72                                   
REMARK 500    GLU B 269     -143.92   -118.52                                   
REMARK 500    ASP B 335     -124.88     61.94                                   
REMARK 500    ASN B 359      -44.40     79.38                                   
REMARK 500    ASN B 368      -67.48   -102.31                                   
REMARK 500    PRO B 433      151.42    -47.69                                   
REMARK 500    VAL B 498      -61.71   -109.17                                   
REMARK 500    HIS B 513       41.81   -102.92                                   
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 ARG A  247     VAL A  248                 -144.72                    
REMARK 500 MET A  291     ASP A  292                  145.39                    
REMARK 500 MET B  291     ASP B  292                  141.56                    
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 EDO A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PTG A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PTG B 607                 
DBREF  6I5G A  230   555  UNP    P34913   HYES_HUMAN     177    502             
DBREF  6I5G B  230   555  UNP    P34913   HYES_HUMAN     177    502             
SEQADV 6I5G MET A  212  UNP  P34913              INITIATING METHIONINE          
SEQADV 6I5G HIS A  213  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS A  214  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS A  215  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS A  216  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS A  217  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS A  218  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER A  219  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G THR A  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLU A  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G ASN A  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G LEU A  223  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G TYR A  224  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G PHE A  225  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLN A  226  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLY A  227  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER A  228  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER A  229  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G MET B  212  UNP  P34913              INITIATING METHIONINE          
SEQADV 6I5G HIS B  213  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS B  214  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS B  215  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS B  216  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS B  217  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G HIS B  218  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER B  219  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G THR B  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLU B  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G ASN B  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G LEU B  223  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G TYR B  224  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G PHE B  225  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLN B  226  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G GLY B  227  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER B  228  UNP  P34913              EXPRESSION TAG                 
SEQADV 6I5G SER B  229  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  344  MET HIS HIS HIS HIS HIS HIS SER THR GLU ASN LEU TYR          
SEQRES   2 A  344  PHE GLN GLY SER SER THR SER CYS ASN PRO SER ASP MET          
SEQRES   3 A  344  SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG LEU          
SEQRES   4 A  344  HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS LEU          
SEQRES   5 A  344  CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG TYR          
SEQRES   6 A  344  GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL LEU          
SEQRES   7 A  344  ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA PRO          
SEQRES   8 A  344  PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS LYS          
SEQRES   9 A  344  GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER GLN          
SEQRES  10 A  344  ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU VAL          
SEQRES  11 A  344  TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG ALA          
SEQRES  12 A  344  VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN PRO          
SEQRES  13 A  344  ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO VAL          
SEQRES  14 A  344  PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL ALA          
SEQRES  15 A  344  GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE LYS          
SEQRES  16 A  344  SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER MET          
SEQRES  17 A  344  HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN SER          
SEQRES  18 A  344  PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU GLU          
SEQRES  19 A  344  GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER GLY          
SEQRES  20 A  344  PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU ARG          
SEQRES  21 A  344  ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS ILE          
SEQRES  22 A  344  LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP PHE          
SEQRES  23 A  344  VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP TRP          
SEQRES  24 A  344  ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS GLY          
SEQRES  25 A  344  HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN GLN          
SEQRES  26 A  344  ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN PRO          
SEQRES  27 A  344  PRO VAL VAL SER LYS MET                                      
SEQRES   1 B  344  MET HIS HIS HIS HIS HIS HIS SER THR GLU ASN LEU TYR          
SEQRES   2 B  344  PHE GLN GLY SER SER THR SER CYS ASN PRO SER ASP MET          
SEQRES   3 B  344  SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG LEU          
SEQRES   4 B  344  HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS LEU          
SEQRES   5 B  344  CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG TYR          
SEQRES   6 B  344  GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL LEU          
SEQRES   7 B  344  ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA PRO          
SEQRES   8 B  344  PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS LYS          
SEQRES   9 B  344  GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER GLN          
SEQRES  10 B  344  ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU VAL          
SEQRES  11 B  344  TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG ALA          
SEQRES  12 B  344  VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN PRO          
SEQRES  13 B  344  ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO VAL          
SEQRES  14 B  344  PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL ALA          
SEQRES  15 B  344  GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE LYS          
SEQRES  16 B  344  SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER MET          
SEQRES  17 B  344  HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN SER          
SEQRES  18 B  344  PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU GLU          
SEQRES  19 B  344  GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER GLY          
SEQRES  20 B  344  PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU ARG          
SEQRES  21 B  344  ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS ILE          
SEQRES  22 B  344  LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP PHE          
SEQRES  23 B  344  VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP TRP          
SEQRES  24 B  344  ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS GLY          
SEQRES  25 B  344  HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN GLN          
SEQRES  26 B  344  ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN PRO          
SEQRES  27 B  344  PRO VAL VAL SER LYS MET                                      
HET    EDO  A 601       4                                                       
HET    EDO  A 602       4                                                       
HET    EDO  A 603       4                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET    PTG  A 607      23                                                       
HET    EDO  B 601       4                                                       
HET    EDO  B 602       4                                                       
HET    EDO  B 603       4                                                       
HET    EDO  B 604       4                                                       
HET    EDO  B 605       4                                                       
HET    EDO  B 606       4                                                       
HET    PTG  B 607      23                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PTG (5E,14E)-11-OXOPROSTA-5,9,12,14-TETRAEN-1-OIC ACID               
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PTG 15-DEOXY-DELTA(12,14)-PROSTAGLANDIN J2                           
FORMUL   3  EDO    12(C2 H6 O2)                                                 
FORMUL   9  PTG    2(C20 H28 O3)                                                
FORMUL  17  HOH   *226(H2 O)                                                    
HELIX    1 AA1 ASN A  233  MET A  237  5                                   5    
HELIX    2 AA2 SER A  270  ARG A  275  5                                   6    
HELIX    3 AA3 TYR A  276  ALA A  284  1                                   9    
HELIX    4 AA4 GLU A  304  TYR A  308  5                                   5    
HELIX    5 AA5 CYS A  309  GLY A  325  1                                  17    
HELIX    6 AA6 ASP A  335  TYR A  348  1                                  14    
HELIX    7 AA7 SER A  370  ASN A  378  1                                   9    
HELIX    8 AA8 PHE A  381  PHE A  387  1                                   7    
HELIX    9 AA9 GLY A  391  ASN A  400  1                                  10    
HELIX   10 AB1 ASN A  400  PHE A  409  1                                  10    
HELIX   11 AB2 ALA A  411  SER A  415  5                                   5    
HELIX   12 AB3 LYS A  421  GLY A  426  1                                   6    
HELIX   13 AB4 THR A  443  LYS A  456  1                                  14    
HELIX   14 AB5 PHE A  459  TRP A  465  1                                   7    
HELIX   15 AB6 ASN A  468  LYS A  478  1                                  11    
HELIX   16 AB7 VAL A  500  GLN A  505  5                                   6    
HELIX   17 AB8 HIS A  506  TRP A  510  5                                   5    
HELIX   18 AB9 TRP A  525  LYS A  530  1                                   6    
HELIX   19 AC1 LYS A  530  ASP A  545  1                                  16    
HELIX   20 AC2 ASN B  233  MET B  237  5                                   5    
HELIX   21 AC3 SER B  270  ARG B  275  5                                   6    
HELIX   22 AC4 TYR B  276  ALA B  284  1                                   9    
HELIX   23 AC5 GLU B  304  TYR B  308  5                                   5    
HELIX   24 AC6 CYS B  309  GLY B  325  1                                  17    
HELIX   25 AC7 ASP B  335  TYR B  348  1                                  14    
HELIX   26 AC8 PRO B  371  ASN B  378  1                                   8    
HELIX   27 AC9 PHE B  381  PHE B  387  1                                   7    
HELIX   28 AD1 GLY B  391  ASN B  400  1                                  10    
HELIX   29 AD2 ASN B  400  PHE B  409  1                                  10    
HELIX   30 AD3 ALA B  411  SER B  415  5                                   5    
HELIX   31 AD4 LYS B  421  GLY B  426  1                                   6    
HELIX   32 AD5 THR B  443  LYS B  455  1                                  13    
HELIX   33 AD6 PHE B  459  TRP B  465  1                                   7    
HELIX   34 AD7 ASN B  468  LYS B  478  1                                  11    
HELIX   35 AD8 VAL B  500  GLN B  505  5                                   6    
HELIX   36 AD9 HIS B  506  TRP B  510  5                                   5    
HELIX   37 AE1 TRP B  525  LYS B  530  1                                   6    
HELIX   38 AE2 LYS B  530  ASP B  545  1                                  16    
SHEET    1 AA1 8 SER A 238  LYS A 245  0                                        
SHEET    2 AA1 8 VAL A 248  LEU A 255 -1  O  PHE A 252   N  GLY A 240           
SHEET    3 AA1 8 ARG A 287  MET A 291 -1  O  VAL A 288   N  LEU A 255           
SHEET    4 AA1 8 ALA A 260  CYS A 264  1  N  LEU A 263   O  LEU A 289           
SHEET    5 AA1 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6 AA1 8 VAL A 352  LEU A 358  1  O  LEU A 358   N  GLY A 333           
SHEET    7 AA1 8 ALA A 488  ALA A 493  1  O  VAL A 491   N  SER A 357           
SHEET    8 AA1 8 LYS A 515  ILE A 519  1  O  LYS A 515   N  ALA A 488           
SHEET    1 AA2 8 SER B 238  LYS B 245  0                                        
SHEET    2 AA2 8 VAL B 248  LEU B 255 -1  O  VAL B 248   N  LYS B 245           
SHEET    3 AA2 8 ARG B 287  MET B 291 -1  O  VAL B 288   N  LEU B 255           
SHEET    4 AA2 8 ALA B 260  CYS B 264  1  N  VAL B 261   O  LEU B 289           
SHEET    5 AA2 8 ALA B 329  HIS B 334  1  O  VAL B 330   N  CYS B 262           
SHEET    6 AA2 8 VAL B 352  LEU B 358  1  O  LEU B 358   N  GLY B 333           
SHEET    7 AA2 8 ALA B 488  ALA B 493  1  O  VAL B 491   N  SER B 357           
SHEET    8 AA2 8 LEU B 514  ILE B 519  1  O  LYS B 515   N  ALA B 488           
CISPEP   1 PHE A  267    PRO A  268          0        -8.87                     
CISPEP   2 PHE B  267    PRO B  268          0       -12.46                     
SITE     1 AC1  7 GLU A 269  SER A 273  HIS A 334  TRP A 525                    
SITE     2 AC1  7 THR A 526  GLN A 527  MET A 528                               
SITE     1 AC2  5 MET A 293  LYS A 294  LEU A 313  GLU A 316                    
SITE     2 AC2  5 MET A 317                                                     
SITE     1 AC3  8 GLU A 269  SER A 270  ASP A 292  TYR A 296                    
SITE     2 AC3  8 GLY A 297  GLN A 453  PHE A 454  HOH A 748                    
SITE     1 AC4  8 PRO A 390  GLY A 391  ARG A 460  HOH A 709                    
SITE     2 AC4  8 HOH A 758  PRO B 302  GLU B 304  GLU B 307                    
SITE     1 AC5  5 ASN A 468  MET A 469  GLU A 470  ARG A 471                    
SITE     2 AC5  5 HOH A 751                                                     
SITE     1 AC6  4 VAL A 318  GLU A 350  ARG A 351  HOH A 712                    
SITE     1 AC7 11 PHE A 387  LEU A 408  SER A 412  SER A 415                    
SITE     2 AC7 11 MET A 419  LYS A 495  ASP A 496  PHE A 497                    
SITE     3 AC7 11 VAL A 498  HIS A 524  HOH A 790                               
SITE     1 AC8  4 MET B 293  LYS B 294  LEU B 313  GLU B 316                    
SITE     1 AC9  8 SER A 238  GLY A 240  PHE A 252  GLU A 254                    
SITE     2 AC9  8 SER B 238  GLY B 240  PHE B 252  GLU B 254                    
SITE     1 AD1  8 ALA B 345  LEU B 346  PRO B 349  ASP B 413                    
SITE     2 AD1  8 LYS B 483  LEU B 485  HOH B 716  HOH B 737                    
SITE     1 AD2  7 HIS B 239  HIS B 251  TRP B 271  ASP B 292                    
SITE     2 AD2  7 GLU B 298  GLN B 453  HOH B 763                               
SITE     1 AD3  3 LYS B 315  THR B 319  GLU B 494                               
SITE     1 AD4  3 SER B 257  GLY B 258  GLY B 285                               
SITE     1 AD5 10 TYR B 383  PHE B 387  SER B 412  SER B 415                    
SITE     2 AD5 10 MET B 419  LYS B 495  ASP B 496  PHE B 497                    
SITE     3 AD5 10 VAL B 498  HIS B 524                                          
CRYST1   89.490   79.992  104.544  90.00  96.78  90.00 I 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      0.011174  0.000000  0.001328        0.00000                         
SCALE2      0.000000  0.012501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009633        0.00000                         
TER    2548      ASP A 545                                                      
TER    5103      ASP B 545                                                      
MASTER      454    0   14   38   16    0   26    6 5406    2   94   54          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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