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LongText Report for: 4HAI-pdb

Name Class
4HAI-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           26-SEP-12   4HAI              
TITLE     CRYSTAL STRUCTURE OF HUMAN SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH N-
TITLE    2 CYCLOHEPTYL-1-(MESITYLSULFONYL)PIPERIDINE-4-CARBOXAMIDE.             
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: ACHSEH1                                   
KEYWDS    DOMAIN-SWAPPED DIMER, HYDROLASE-HYDROLASE INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PECIC,S.PAKHOMOVA,M.E.NEWCOMER,C.MORISSEAU,B.D.HAMMOCK,Z.ZHU,S.DENG 
REVDAT   1   26-DEC-12 4HAI    0                                                
JRNL        AUTH   S.PECIC,S.PAKHOMOVA,M.E.NEWCOMER,C.MORISSEAU,B.D.HAMMOCK,    
JRNL        AUTH 2 Z.ZHU,A.RINDERSPACHER,S.X.DENG                               
JRNL        TITL   SYNTHESIS AND STRUCTURE-ACTIVITY RELATIONSHIP OF             
JRNL        TITL 2 PIPERIDINE-DERIVED NON-UREA SOLUBLE EPOXIDE HYDROLASE        
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.LETT.                      2012              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   23237835                                                     
JRNL        DOI    10.1016/J.BMCL.2012.11.084                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19762                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1068                            
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) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1142                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.60000                                              
REMARK   3    B22 (A**2) : 1.60000                                              
REMARK   3    B33 (A**2) : -2.40000                                             
REMARK   3    B12 (A**2) : 0.80000                                              
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): 0.662         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.289         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.226         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.694        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
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):  4472 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3090 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6056 ; 1.397 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7548 ; 0.880 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 7.225 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;35.159 ;24.219       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   780 ;15.951 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;18.541 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   664 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4895 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   888 ; 0.001 ; 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):  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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    23                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3377  49.6809 -11.3357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4033 T22:   0.1872                                     
REMARK   3      T33:   0.0814 T12:  -0.0853                                     
REMARK   3      T13:  -0.0432 T23:   0.0685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5365 L22:   4.5564                                     
REMARK   3      L33:   3.3731 L12:  -5.3762                                     
REMARK   3      L13:  -3.6154 L23:   3.6187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2781 S12:  -0.1294 S13:   0.2929                       
REMARK   3      S21:  -0.6649 S22:   0.0049 S23:  -0.2340                       
REMARK   3      S31:  -0.6691 S32:  -0.1647 S33:  -0.2830                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    24        A    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6851  70.0946  -5.6048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1840 T22:   0.1852                                     
REMARK   3      T33:   0.0484 T12:  -0.0633                                     
REMARK   3      T13:  -0.0682 T23:   0.0533                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8533 L22:   1.3983                                     
REMARK   3      L33:   2.2374 L12:  -1.2817                                     
REMARK   3      L13:   2.6630 L23:  -1.5977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2506 S12:   0.4989 S13:   0.4029                       
REMARK   3      S21:   0.2055 S22:   0.0141 S23:  -0.1890                       
REMARK   3      S31:  -0.1455 S32:   0.0113 S33:   0.2364                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    76        A   225                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.8709  51.2296  -8.8960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1137 T22:   0.1580                                     
REMARK   3      T33:   0.0381 T12:  -0.0881                                     
REMARK   3      T13:  -0.0152 T23:   0.0497                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5302 L22:   1.4340                                     
REMARK   3      L33:   0.6406 L12:   0.4286                                     
REMARK   3      L13:   0.5526 L23:   0.6338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1644 S12:   0.0467 S13:  -0.0085                       
REMARK   3      S21:  -0.1858 S22:   0.1979 S23:  -0.0214                       
REMARK   3      S31:  -0.1323 S32:   0.0220 S33:  -0.0335                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   226        A   368                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7678  25.6623  20.9651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0754 T22:   0.0909                                     
REMARK   3      T33:   0.0804 T12:  -0.0076                                     
REMARK   3      T13:  -0.0143 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2146 L22:   1.2320                                     
REMARK   3      L33:   0.4832 L12:   0.2238                                     
REMARK   3      L13:   0.0205 L23:   0.0311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0285 S12:   0.0021 S13:  -0.0432                       
REMARK   3      S21:   0.0237 S22:  -0.0290 S23:   0.0344                       
REMARK   3      S31:  -0.0545 S32:   0.0183 S33:   0.0005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   369        A   548                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.8857  13.5642  14.4605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0800 T22:   0.0583                                     
REMARK   3      T33:   0.0719 T12:  -0.0230                                     
REMARK   3      T13:  -0.0107 T23:  -0.0509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8636 L22:   1.2629                                     
REMARK   3      L33:   1.0200 L12:  -0.0236                                     
REMARK   3      L13:  -0.2709 L23:  -0.0964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0361 S12:   0.0981 S13:  -0.1849                       
REMARK   3      S21:  -0.1481 S22:   0.0028 S23:   0.0778                       
REMARK   3      S31:   0.1725 S32:  -0.0678 S33:   0.0333                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4HAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075224.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20842                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200   FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.70000                            
REMARK 200   FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1S8O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0-10% SUCROSE , PH 7.5,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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      162.65467            
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       81.32733            
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      121.99100            
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       40.66367            
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      203.31833            
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      162.65467            
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       81.32733            
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       40.66367            
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      121.99100            
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      203.31833            
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: 4920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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  0.500000 -0.866025  0.000000       46.16000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       79.95147            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.66367            
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     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 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     MET A   1    CG   SD   CE                                        
REMARK 470     MET A 419    CG   SD   CE                                        
REMARK 470     HIS A 420    CG   ND1  CD2  CE1  NE2                             
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   OD1  ASP A   322     NH2  ARG A   351              2.00            
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    PRO A  17   C   -  N   -  CD  ANGL. DEV. = -20.6 DEGREES          
REMARK 500    PRO A 161   C   -  N   -  CD  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ASP A 185   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 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    LEU A  10      -82.87    -97.51                                   
REMARK 500    VAL A  13      -70.39   -125.03                                   
REMARK 500    PRO A  17       90.63     38.87                                   
REMARK 500    LYS A  79       63.84     67.24                                   
REMARK 500    ASN A  85       52.21   -107.43                                   
REMARK 500    LYS A 160       68.99   -114.58                                   
REMARK 500    GLN A 204     -102.69   -101.11                                   
REMARK 500    GLU A 269     -137.72   -122.29                                   
REMARK 500    SER A 270      157.74    176.98                                   
REMARK 500    ASP A 335     -121.14     59.39                                   
REMARK 500    ASN A 359      -47.49     73.02                                   
REMARK 500    ASN A 368      -64.29    -92.21                                   
REMARK 500    ASN A 431       63.93   -117.39                                   
REMARK 500    ARG A 547      -94.68   -160.11                                   
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 LEU A   16     PRO A   17                 -118.42                    
REMARK 500 LYS A  160     PRO A  161                  121.35                    
REMARK 500 MET A  291     ASP A  292                  144.05                    
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 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 718   O                                                      
REMARK 620 2 ASP A   9   OD2 151.6                                              
REMARK 620 3 HOH A 721   O   108.3  87.7                                        
REMARK 620 4 PO4 A 601   O4   86.9 119.5  80.6                                  
REMARK 620 5 ASP A 185   OD1  82.4  73.8  91.0 163.6                            
REMARK 620 6 ASP A  11   O    75.1  90.1 175.9  97.5  91.8                      
REMARK 620 7 ASP A   9   OD1 151.4  50.2  84.4  69.6 123.9  91.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I23 A 603                 
DBREF  4HAI A    1   555  UNP    P34913   HYES_HUMAN       1    555             
SEQRES   1 A  555  MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL          
SEQRES   2 A  555  LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR          
SEQRES   3 A  555  GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP          
SEQRES   4 A  555  ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG          
SEQRES   5 A  555  LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO          
SEQRES   6 A  555  LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA          
SEQRES   7 A  555  LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE          
SEQRES   8 A  555  PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO          
SEQRES   9 A  555  MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE          
SEQRES  10 A  555  THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG          
SEQRES  11 A  555  ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU          
SEQRES  12 A  555  LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL          
SEQRES  13 A  555  GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU          
SEQRES  14 A  555  LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE          
SEQRES  15 A  555  LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP          
SEQRES  16 A  555  LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR          
SEQRES  17 A  555  ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU          
SEQRES  18 A  555  LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO          
SEQRES  19 A  555  SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG          
SEQRES  20 A  555  VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA          
SEQRES  21 A  555  VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER          
SEQRES  22 A  555  TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR          
SEQRES  23 A  555  ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER          
SEQRES  24 A  555  SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL          
SEQRES  25 A  555  LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY          
SEQRES  26 A  555  LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY          
SEQRES  27 A  555  MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG          
SEQRES  28 A  555  VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO          
SEQRES  29 A  555  ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA          
SEQRES  30 A  555  ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO          
SEQRES  31 A  555  GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG          
SEQRES  32 A  555  THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL          
SEQRES  33 A  555  LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE          
SEQRES  34 A  555  VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL          
SEQRES  35 A  555  THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS          
SEQRES  36 A  555  LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN          
SEQRES  37 A  555  MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY          
SEQRES  38 A  555  ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU          
SEQRES  39 A  555  LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET          
SEQRES  40 A  555  GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU          
SEQRES  41 A  555  ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU          
SEQRES  42 A  555  VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA          
SEQRES  43 A  555  ARG ASN PRO PRO VAL VAL SER LYS MET                          
HET    PO4  A 601       5                                                       
HET     MG  A 602       1                                                       
HET    I23  A 603      28                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     I23 N-CYCLOHEPTYL-1-[(2,4,6-TRIMETHYLPHENYL)                         
HETNAM   2 I23  SULFONYL]PIPERIDINE-4-CARBOXAMIDE                               
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  I23    C22 H34 N2 O3 S                                              
FORMUL   5  HOH   *27(H2 O)                                                     
HELIX    1   1 VAL A   19  ALA A   31  1                                  13    
HELIX    2   2 GLY A   35  GLN A   42  1                                   8    
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  GLY A  197  1                                  12    
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 TYR A  276  ALA A  284  1                                   9    
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  ASN A  378  1                                   9    
HELIX   21  21 PHE A  381  PHE A  387  1                                   7    
HELIX   22  22 GLY A  391  ASN A  400  1                                  10    
HELIX   23  23 ASN A  400  PHE A  409  1                                  10    
HELIX   24  24 ALA A  411  SER A  415  5                                   5    
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  VAL A 181   N  VAL A   7           
SHEET    5   A 5 VAL A 199  LEU A 202  1  O  VAL A 199   N  VAL A 180           
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  ASP A 292 -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 602                 O   HOH A 718     1555   1555  1.91  
LINK         OD2 ASP A   9                MG    MG A 602     1555   1555  1.91  
LINK        MG    MG A 602                 O   HOH A 721     1555   1555  1.92  
LINK         O4  PO4 A 601                MG    MG A 602     1555   1555  1.95  
LINK         OD1 ASP A 185                MG    MG A 602     1555   1555  1.96  
LINK         O   ASP A  11                MG    MG A 602     1555   1555  2.19  
LINK         OD1 ASP A   9                MG    MG A 602     1555   1555  2.83  
CISPEP   1 PHE A  267    PRO A  268          0       -15.10                     
SITE     1 AC1  9 ASP A   9  LEU A  10  ASP A  11  THR A 123                    
SITE     2 AC1  9 ASN A 124  LYS A 160   MG A 602  HOH A 718                    
SITE     3 AC1  9 HOH A 721                                                     
SITE     1 AC2  6 ASP A   9  ASP A  11  ASP A 185  PO4 A 601                    
SITE     2 AC2  6 HOH A 718  HOH A 721                                          
SITE     1 AC3  9 ASP A 335  TYR A 383  GLN A 384  LEU A 408                    
SITE     2 AC3  9 LEU A 417  MET A 419  LEU A 428  TYR A 466                    
SITE     3 AC3  9 TRP A 525                                                     
CRYST1   92.320   92.320  243.982  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      0.010832  0.006254  0.000000        0.00000                         
SCALE2      0.000000  0.012508  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004099        0.00000                         
TER    4329      ASN A 548                                                      
MASTER      486    0    3   32   15    0    8    6 4389    1   41   43          
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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