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Database: PDB
Entry: 5X0R
LinkDB: 5X0R
Original site: 5X0R 
HEADER    TRANSCRIPTION                           23-JAN-17   5X0R              
TITLE     CRYSTAL STRUCTURE OF PXR LBD COMPLEXED WITH SJB7                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 153-457;                                      
COMPND   5 SYNONYM: ORPHAN NUCLEAR RECEPTOR PAR1,ORPHAN NUCLEAR RECEPTOR PXR,   
COMPND   6 PREGNANE X RECEPTOR,STEROID AND XENOBIOTIC RECEPTOR,SXR;             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 SYNONYM: NCOA-1,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74,BHLHE74,   
COMPND  12 PROTEIN HIN-2,RIP160,RENAL CARCINOMA ANTIGEN NY-REN-52,STEROID       
COMPND  13 RECEPTOR COACTIVATOR 1,SRC-1;                                        
COMPND  14 EC: 2.3.1.48;                                                        
COMPND  15 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: NR1I2, PXR;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: NCOA1, BHLHE74, SRC1;                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSCRIPTION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LV,W.LIN,S.C.CHAI,Q.ZHANG,T.CHEN                                    
REVDAT   2   18-APR-18 5X0R    1       JRNL                                     
REVDAT   1   04-OCT-17 5X0R    0                                                
JRNL        AUTH   W.LIN,Y.M.WANG,S.C.CHAI,L.LV,J.ZHENG,J.WU,Q.ZHANG,Y.D.WANG,  
JRNL        AUTH 2 P.R.GRIFFIN,T.CHEN                                           
JRNL        TITL   SPA70 IS A POTENT ANTAGONIST OF HUMAN PREGNANE X RECEPTOR.   
JRNL        REF    NAT COMMUN                    V.   8   741 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28963450                                                     
JRNL        DOI    10.1038/S41467-017-00780-5                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19141                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1048                            
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) : 2.67                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1213                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4119                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 20                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.47000                                             
REMARK   3    B22 (A**2) : 2.32000                                              
REMARK   3    B33 (A**2) : -0.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.788         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.338         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.204         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.405         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4268 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4053 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5772 ; 1.538 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9261 ; 1.034 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   514 ; 5.781 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;35.670 ;23.462       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   729 ;16.065 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;18.337 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   649 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4719 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1000 ; 0.004 ; 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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   142    429       B   142    429   12870  0.11  0.05     
REMARK   3    2     C   682    696       D   682    696     654  0.18  0.05     
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 5X0R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002741.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : 7.2-7.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20453                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.665                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
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: 1NRL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, IMIDAZOLE,                     
REMARK 280  ISOPROPANOL,SODIUM CHLORIDE, GLYCEROL, EDTA, PH 7.2-7.8, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.0K, PH 7.8                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.16950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.37950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.65050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.37950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.16950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.65050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     GLY A   122                                                      
REMARK 465     HIS A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     HIS A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     HIS A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     SER A   130                                                      
REMARK 465     GLU A   131                                                      
REMARK 465     ARG A   132                                                      
REMARK 465     THR A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     THR A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     LEU A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     VAL A   140                                                      
REMARK 465     GLN A   141                                                      
REMARK 465     LEU A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     CYS A   182                                                      
REMARK 465     GLU A   183                                                      
REMARK 465     LEU A   184                                                      
REMARK 465     PRO A   185                                                      
REMARK 465     GLU A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     LEU A   188                                                      
REMARK 465     GLN A   189                                                      
REMARK 465     ALA A   190                                                      
REMARK 465     PRO A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     GLU A   194                                                      
REMARK 465     GLU A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     LYS A   198                                                      
REMARK 465     TRP A   199                                                      
REMARK 465     SER A   200                                                      
REMARK 465     GLN A   201                                                      
REMARK 465     VAL A   202                                                      
REMARK 465     ARG A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     ASP A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     CYS A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     LEU A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     PHE A   237                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     ASP A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     GLY A   314                                                      
REMARK 465     PHE A   315                                                      
REMARK 465     GLN A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     LEU A   318                                                      
REMARK 465     PRO A   382                                                      
REMARK 465     GLN A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     SER A   434                                                      
REMARK 465     MET B   119                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     LYS B   121                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     HIS B   123                                                      
REMARK 465     HIS B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     HIS B   127                                                      
REMARK 465     HIS B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     GLU B   131                                                      
REMARK 465     ARG B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     THR B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     LEU B   138                                                      
REMARK 465     LEU B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     CYS B   182                                                      
REMARK 465     GLU B   183                                                      
REMARK 465     LEU B   184                                                      
REMARK 465     PRO B   185                                                      
REMARK 465     GLU B   186                                                      
REMARK 465     SER B   187                                                      
REMARK 465     LEU B   188                                                      
REMARK 465     GLN B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     PRO B   191                                                      
REMARK 465     SER B   192                                                      
REMARK 465     ARG B   193                                                      
REMARK 465     GLU B   194                                                      
REMARK 465     GLU B   195                                                      
REMARK 465     ALA B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     TRP B   199                                                      
REMARK 465     SER B   200                                                      
REMARK 465     GLN B   201                                                      
REMARK 465     VAL B   202                                                      
REMARK 465     ARG B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     ASP B   205                                                      
REMARK 465     LEU B   206                                                      
REMARK 465     THR B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     PHE B   315                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     ILE B   431                                                      
REMARK 465     THR B   432                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     CYS C   676                                                      
REMARK 465     PRO C   677                                                      
REMARK 465     SER C   678                                                      
REMARK 465     SER C   679                                                      
REMARK 465     HIS C   680                                                      
REMARK 465     SER C   681                                                      
REMARK 465     GLY C   697                                                      
REMARK 465     SER C   698                                                      
REMARK 465     PRO C   699                                                      
REMARK 465     SER C   700                                                      
REMARK 465     CYS D   676                                                      
REMARK 465     PRO D   677                                                      
REMARK 465     SER D   678                                                      
REMARK 465     SER D   679                                                      
REMARK 465     HIS D   680                                                      
REMARK 465     SER D   681                                                      
REMARK 465     GLY D   697                                                      
REMARK 465     SER D   698                                                      
REMARK 465     PRO D   699                                                      
REMARK 465     SER D   700                                                      
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     ARG A 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 149    CE                                                  
REMARK 470     MET A 159    CE                                                  
REMARK 470     LEU A 215    CD1  CD2                                            
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     SER A 221    OG                                                  
REMARK 470     LYS A 226    CG   CD   CE   NZ                                   
REMARK 470     ILE A 254    CD1                                                 
REMARK 470     GLU A 270    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 319    CG   CD1  CD2                                       
REMARK 470     LEU A 320    CG   CD1  CD2                                       
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 324    CG   CD1  CD2                                       
REMARK 470     HIS A 359    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 368    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 406    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 409    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 431    CD1                                                 
REMARK 470     VAL B 140    CG1  CG2                                            
REMARK 470     GLN B 141    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 145    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 159    CE                                                  
REMARK 470     LYS B 170    CG   CD   CE   NZ                                   
REMARK 470     CYS B 207    SG                                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     ASP B 230    CG   OD1  OD2                                       
REMARK 470     SER B 231    OG                                                  
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     ILE B 236    CG1  CG2  CD1                                       
REMARK 470     PHE B 237    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B 254    CD1                                                 
REMARK 470     ILE B 255    CD1                                                 
REMARK 470     GLU B 270    CD   OE1  OE2                                       
REMARK 470     GLU B 295    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 303    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 316    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 317    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 318    CG   CD1  CD2                                       
REMARK 470     LEU B 320    CG   CD1  CD2                                       
REMARK 470     HIS B 359    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 383    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 399    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 401    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 406    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 409    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 410    CD   NE   CZ   NH1  NH2                             
REMARK 470     HIS B 418    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C 685    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 683    CD1  CD2                                            
REMARK 470     ARG D 686    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 688    CE   NZ                                             
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    CYS A 301       69.88   -105.04                                   
REMARK 500    PRO A 354       88.72    -54.16                                   
REMARK 500    GLN A 358       44.51    -80.60                                   
REMARK 500    HIS A 386       39.75    -91.89                                   
REMARK 500    VAL B 140      -66.25     67.01                                   
REMARK 500    LEU B 209       34.57    -98.62                                   
REMARK 500    SER B 231       51.82   -119.03                                   
REMARK 500    LYS B 234      -16.94     84.65                                   
REMARK 500    CYS B 301       67.93   -105.34                                   
REMARK 500    PRO B 354       88.62    -57.54                                   
REMARK 500    GLN B 358       44.87    -79.53                                   
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 4WH A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4WH B 501                 
DBREF  5X0R A  130   434  UNP    O75469   NR1I2_HUMAN    153    457             
DBREF  5X0R B  130   434  UNP    O75469   NR1I2_HUMAN    153    457             
DBREF  5X0R C  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
DBREF  5X0R D  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 5X0R MET A  119  UNP  O75469              INITIATING METHIONINE          
SEQADV 5X0R GLY A  120  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R LYS A  121  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R GLY A  122  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  123  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  124  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  125  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  126  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  127  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS A  128  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R GLY A  129  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R MET B  119  UNP  O75469              INITIATING METHIONINE          
SEQADV 5X0R GLY B  120  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R LYS B  121  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R GLY B  122  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  123  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  124  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  125  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  126  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  127  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R HIS B  128  UNP  O75469              EXPRESSION TAG                 
SEQADV 5X0R GLY B  129  UNP  O75469              EXPRESSION TAG                 
SEQRES   1 A  316  MET GLY LYS GLY HIS HIS HIS HIS HIS HIS GLY SER GLU          
SEQRES   2 A  316  ARG THR GLY THR GLN PRO LEU GLY VAL GLN GLY LEU THR          
SEQRES   3 A  316  GLU GLU GLN ARG MET MET ILE ARG GLU LEU MET ASP ALA          
SEQRES   4 A  316  GLN MET LYS THR PHE ASP THR THR PHE SER HIS PHE LYS          
SEQRES   5 A  316  ASN PHE ARG LEU PRO GLY VAL LEU SER SER GLY CYS GLU          
SEQRES   6 A  316  LEU PRO GLU SER LEU GLN ALA PRO SER ARG GLU GLU ALA          
SEQRES   7 A  316  ALA LYS TRP SER GLN VAL ARG LYS ASP LEU CYS SER LEU          
SEQRES   8 A  316  LYS VAL SER LEU GLN LEU ARG GLY GLU ASP GLY SER VAL          
SEQRES   9 A  316  TRP ASN TYR LYS PRO PRO ALA ASP SER GLY GLY LYS GLU          
SEQRES  10 A  316  ILE PHE SER LEU LEU PRO HIS MET ALA ASP MET SER THR          
SEQRES  11 A  316  TYR MET PHE LYS GLY ILE ILE SER PHE ALA LYS VAL ILE          
SEQRES  12 A  316  SER TYR PHE ARG ASP LEU PRO ILE GLU ASP GLN ILE SER          
SEQRES  13 A  316  LEU LEU LYS GLY ALA ALA PHE GLU LEU CYS GLN LEU ARG          
SEQRES  14 A  316  PHE ASN THR VAL PHE ASN ALA GLU THR GLY THR TRP GLU          
SEQRES  15 A  316  CYS GLY ARG LEU SER TYR CYS LEU GLU ASP THR ALA GLY          
SEQRES  16 A  316  GLY PHE GLN GLN LEU LEU LEU GLU PRO MET LEU LYS PHE          
SEQRES  17 A  316  HIS TYR MET LEU LYS LYS LEU GLN LEU HIS GLU GLU GLU          
SEQRES  18 A  316  TYR VAL LEU MET GLN ALA ILE SER LEU PHE SER PRO ASP          
SEQRES  19 A  316  ARG PRO GLY VAL LEU GLN HIS ARG VAL VAL ASP GLN LEU          
SEQRES  20 A  316  GLN GLU GLN PHE ALA ILE THR LEU LYS SER TYR ILE GLU          
SEQRES  21 A  316  CYS ASN ARG PRO GLN PRO ALA HIS ARG PHE LEU PHE LEU          
SEQRES  22 A  316  LYS ILE MET ALA MET LEU THR GLU LEU ARG SER ILE ASN          
SEQRES  23 A  316  ALA GLN HIS THR GLN ARG LEU LEU ARG ILE GLN ASP ILE          
SEQRES  24 A  316  HIS PRO PHE ALA THR PRO LEU MET GLN GLU LEU PHE GLY          
SEQRES  25 A  316  ILE THR GLY SER                                              
SEQRES   1 B  316  MET GLY LYS GLY HIS HIS HIS HIS HIS HIS GLY SER GLU          
SEQRES   2 B  316  ARG THR GLY THR GLN PRO LEU GLY VAL GLN GLY LEU THR          
SEQRES   3 B  316  GLU GLU GLN ARG MET MET ILE ARG GLU LEU MET ASP ALA          
SEQRES   4 B  316  GLN MET LYS THR PHE ASP THR THR PHE SER HIS PHE LYS          
SEQRES   5 B  316  ASN PHE ARG LEU PRO GLY VAL LEU SER SER GLY CYS GLU          
SEQRES   6 B  316  LEU PRO GLU SER LEU GLN ALA PRO SER ARG GLU GLU ALA          
SEQRES   7 B  316  ALA LYS TRP SER GLN VAL ARG LYS ASP LEU CYS SER LEU          
SEQRES   8 B  316  LYS VAL SER LEU GLN LEU ARG GLY GLU ASP GLY SER VAL          
SEQRES   9 B  316  TRP ASN TYR LYS PRO PRO ALA ASP SER GLY GLY LYS GLU          
SEQRES  10 B  316  ILE PHE SER LEU LEU PRO HIS MET ALA ASP MET SER THR          
SEQRES  11 B  316  TYR MET PHE LYS GLY ILE ILE SER PHE ALA LYS VAL ILE          
SEQRES  12 B  316  SER TYR PHE ARG ASP LEU PRO ILE GLU ASP GLN ILE SER          
SEQRES  13 B  316  LEU LEU LYS GLY ALA ALA PHE GLU LEU CYS GLN LEU ARG          
SEQRES  14 B  316  PHE ASN THR VAL PHE ASN ALA GLU THR GLY THR TRP GLU          
SEQRES  15 B  316  CYS GLY ARG LEU SER TYR CYS LEU GLU ASP THR ALA GLY          
SEQRES  16 B  316  GLY PHE GLN GLN LEU LEU LEU GLU PRO MET LEU LYS PHE          
SEQRES  17 B  316  HIS TYR MET LEU LYS LYS LEU GLN LEU HIS GLU GLU GLU          
SEQRES  18 B  316  TYR VAL LEU MET GLN ALA ILE SER LEU PHE SER PRO ASP          
SEQRES  19 B  316  ARG PRO GLY VAL LEU GLN HIS ARG VAL VAL ASP GLN LEU          
SEQRES  20 B  316  GLN GLU GLN PHE ALA ILE THR LEU LYS SER TYR ILE GLU          
SEQRES  21 B  316  CYS ASN ARG PRO GLN PRO ALA HIS ARG PHE LEU PHE LEU          
SEQRES  22 B  316  LYS ILE MET ALA MET LEU THR GLU LEU ARG SER ILE ASN          
SEQRES  23 B  316  ALA GLN HIS THR GLN ARG LEU LEU ARG ILE GLN ASP ILE          
SEQRES  24 B  316  HIS PRO PHE ALA THR PRO LEU MET GLN GLU LEU PHE GLY          
SEQRES  25 B  316  ILE THR GLY SER                                              
SEQRES   1 C   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 C   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
SEQRES   1 D   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 D   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    4WH  A 501      30                                                       
HET    4WH  B 501      30                                                       
HETNAM     4WH 4-[(4-TERT-BUTYLPHENYL)SULFONYL]-1-(2,4-DIMETHOXY-5-             
HETNAM   2 4WH  METHYLPHENYL)-5-METHYL-1H-1,2,3-TRIAZOLE                        
FORMUL   5  4WH    2(C22 H27 N3 O4 S)                                           
FORMUL   7  HOH   *20(H2 O)                                                     
HELIX    1 AA1 THR A  144  PHE A  162  1                                  19    
HELIX    2 AA2 LEU A  239  VAL A  260  1                                  22    
HELIX    3 AA3 ILE A  261  ASP A  266  1                                   6    
HELIX    4 AA4 PRO A  268  THR A  290  1                                  23    
HELIX    5 AA5 GLU A  321  LEU A  333  1                                  13    
HELIX    6 AA6 HIS A  336  PHE A  349  1                                  14    
HELIX    7 AA7 GLN A  358  ARG A  381  1                                  24    
HELIX    8 AA8 PHE A  388  HIS A  418  1                                  31    
HELIX    9 AA9 THR A  422  GLY A  430  1                                   9    
HELIX   10 AB1 THR B  144  PHE B  162  1                                  19    
HELIX   11 AB2 LEU B  239  VAL B  260  1                                  22    
HELIX   12 AB3 ILE B  261  ASP B  266  1                                   6    
HELIX   13 AB4 PRO B  268  THR B  290  1                                  23    
HELIX   14 AB5 GLN B  317  LEU B  320  5                                   4    
HELIX   15 AB6 GLU B  321  LEU B  333  1                                  13    
HELIX   16 AB7 HIS B  336  PHE B  349  1                                  14    
HELIX   17 AB8 GLN B  358  CYS B  379  1                                  22    
HELIX   18 AB9 GLN B  383  ARG B  387  5                                   5    
HELIX   19 AC1 PHE B  388  HIS B  418  1                                  31    
HELIX   20 AC2 THR B  422  PHE B  429  1                                   8    
HELIX   21 AC3 HIS C  687  GLU C  696  1                                  10    
HELIX   22 AC4 HIS D  687  GLU D  696  1                                  10    
SHEET    1 AA110 PHE A 292  ASN A 293  0                                        
SHEET    2 AA110 THR A 298  CYS A 301 -1  O  THR A 298   N  ASN A 293           
SHEET    3 AA110 LEU A 304  CYS A 307 -1  O  TYR A 306   N  TRP A 299           
SHEET    4 AA110 SER A 212  ARG A 216 -1  N  GLN A 214   O  SER A 305           
SHEET    5 AA110 VAL A 222  LYS A 226 -1  O  TYR A 225   N  LEU A 213           
SHEET    6 AA110 VAL B 222  LYS B 226 -1  O  VAL B 222   N  LYS A 226           
SHEET    7 AA110 VAL B 211  ARG B 216 -1  N  LEU B 213   O  TYR B 225           
SHEET    8 AA110 LEU B 304  LEU B 308 -1  O  CYS B 307   N  SER B 212           
SHEET    9 AA110 THR B 298  CYS B 301 -1  N  TRP B 299   O  TYR B 306           
SHEET   10 AA110 PHE B 292  ASN B 293 -1  N  ASN B 293   O  THR B 298           
SITE     1 AC1 11 VAL A 211  MET A 243  SER A 247  ALA A 280                    
SITE     2 AC1 11 PHE A 281  TRP A 299  HIS A 407  THR A 408                    
SITE     3 AC1 11 LEU A 411  LEU A 428  PHE A 429                               
SITE     1 AC2 10 MET B 243  ALA B 280  PHE B 281  TRP B 299                    
SITE     2 AC2 10 HIS B 407  THR B 408  LEU B 411  MET B 425                    
SITE     3 AC2 10 LEU B 428  PHE B 429                                          
CRYST1   84.339   89.301  106.759  90.00  90.00  90.00 P 21 21 21    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      0.011857  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011198  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009367        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system