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Database: PDB
Entry: 5Q1H
LinkDB: 5Q1H
Original site: 5Q1H 
HEADER    TRANSCRIPTION                           31-MAY-17   5Q1H              
TITLE     LIGAND BINDING TO FARNESOID-X-RECEPTOR                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BILE ACID RECEPTOR;                                        
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: FARNESOID X-ACTIVATED RECEPTOR,FARNESOL RECEPTOR HRR-1,     
COMPND   5 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4,RETINOID X RECEPTOR-   
COMPND   6 INTERACTING PROTEIN 14,RXR-INTERACTING PROTEIN 14;                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COACTIVATOR PEPTIDE SRC-1 HD3;                             
COMPND  10 CHAIN: B, D, F, H;                                                   
COMPND  11 FRAGMENT: UNP RESIDUES 744-757;                                      
COMPND  12 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: NR1H4, BAR, FXR, HRR1, RIP14;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    D3R, FXR, DOCKING, TRANSCRIPTION                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.G.RUDOLPH,J.BENZ,D.BURGER,R.THOMA,A.RUF,C.JOSEPH,B.KUHN,C.SHAO,     
AUTHOR   2 H.YANG,S.K.BURLEY                                                    
REVDAT   8   17-NOV-21 5Q1H    1       REMARK                                   
REVDAT   7   10-FEB-21 5Q1H    1       AUTHOR JRNL                              
REVDAT   6   21-FEB-18 5Q1H    1       REMARK                                   
REVDAT   5   31-JAN-18 5Q1H    1       JRNL                                     
REVDAT   4   20-DEC-17 5Q1H    1       JRNL                                     
REVDAT   3   04-OCT-17 5Q1H    1       REMARK                                   
REVDAT   2   19-JUL-17 5Q1H    1       AUTHOR JRNL                              
REVDAT   1   05-JUL-17 5Q1H    0                                                
JRNL        AUTH   Z.GAIEB,S.LIU,S.GATHIAKA,M.CHIU,H.YANG,C.SHAO,V.A.FEHER,     
JRNL        AUTH 2 W.P.WALTERS,B.KUHN,M.G.RUDOLPH,S.K.BURLEY,M.K.GILSON,        
JRNL        AUTH 3 R.E.AMARO                                                    
JRNL        TITL   D3R GRAND CHALLENGE 2: BLIND PREDICTION OF PROTEIN-LIGAND    
JRNL        TITL 2 POSES, AFFINITY RANKINGS, AND RELATIVE BINDING FREE          
JRNL        TITL 3 ENERGIES.                                                    
JRNL        REF    J. COMPUT. AIDED MOL. DES.    V.  32     1 2018              
JRNL        REFN                   ESSN 1573-4951                               
JRNL        PMID   29204945                                                     
JRNL        DOI    10.1007/S10822-017-0088-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 55294                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.180                          
REMARK   3   FREE R VALUE                      : 0.218                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2807                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 91.35                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3733                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2260                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3547                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2237                   
REMARK   3   BIN FREE R VALUE                        : 0.2718                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.98                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 186                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7837                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28850                                              
REMARK   3    B22 (A**2) : 0.99970                                              
REMARK   3    B33 (A**2) : -1.28820                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.26580                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.270               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.232               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.180               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.242               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.186               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8194   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11078  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2972   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 229    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1138   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8194   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1052   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9511   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.43                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.30                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   33.4576    8.3633    4.1871           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2146 T22:   -0.0513                                    
REMARK   3     T33:   -0.1491 T12:   -0.0151                                    
REMARK   3     T13:    0.0113 T23:   -0.0442                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6637 L22:    3.8219                                    
REMARK   3     L33:    2.4520 L12:   -0.4283                                    
REMARK   3     L13:    0.4620 L23:   -1.4976                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1287 S12:   -0.0633 S13:   -0.0134                     
REMARK   3     S21:    0.1255 S22:    0.2100 S23:   -0.0536                     
REMARK   3     S31:   -0.1419 S32:   -0.1677 S33:   -0.0813                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    4.0873   48.3604   18.8921           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0697 T22:   -0.1559                                    
REMARK   3     T33:   -0.2264 T12:   -0.0403                                    
REMARK   3     T13:   -0.0413 T23:   -0.0369                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1006 L22:    2.1431                                    
REMARK   3     L33:    3.8591 L12:   -0.2723                                    
REMARK   3     L13:   -0.3670 L23:    0.3214                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1233 S12:   -0.1911 S13:    0.1095                     
REMARK   3     S21:   -0.1394 S22:    0.1347 S23:   -0.0441                     
REMARK   3     S31:   -0.1660 S32:    0.3216 S33:   -0.0114                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1408   20.4977   32.1821           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1448 T22:   -0.0671                                    
REMARK   3     T33:   -0.1975 T12:    0.0053                                    
REMARK   3     T13:    0.0284 T23:    0.0177                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3264 L22:    4.0714                                    
REMARK   3     L33:    2.1195 L12:    1.0369                                    
REMARK   3     L13:    0.1524 L23:    0.9633                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0205 S12:    0.2606 S13:   -0.0753                     
REMARK   3     S21:   -0.0240 S22:    0.2552 S23:   -0.2018                     
REMARK   3     S31:   -0.1253 S32:    0.1040 S33:   -0.2348                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   20.1606  -19.8446    4.6162           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1883 T22:   -0.1595                                    
REMARK   3     T33:   -0.1046 T12:    0.0410                                    
REMARK   3     T13:   -0.0611 T23:    0.0471                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.0421 L22:    2.5157                                    
REMARK   3     L33:    2.8527 L12:    0.6337                                    
REMARK   3     L13:   -0.1456 L23:    0.7794                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0070 S12:   -0.1729 S13:   -0.2907                     
REMARK   3     S21:    0.1229 S22:    0.1919 S23:    0.0641                     
REMARK   3     S31:    0.3040 S32:    0.1286 S33:   -0.1849                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5Q1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1001401379.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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   : 55434                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 25%PEG3350,       
REMARK 280  EVAPORATION, HANGING DROP, TEMPERATURE 298K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       91.93950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 1090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 1070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   244                                                      
REMARK 465     SER A   245                                                      
REMARK 465     HIS A   246                                                      
REMARK 465     GLN A   476                                                      
REMARK 465     LYS B   744                                                      
REMARK 465     ASP B   756                                                      
REMARK 465     GLU B   757                                                      
REMARK 465     GLY C   244                                                      
REMARK 465     SER C   245                                                      
REMARK 465     HIS C   246                                                      
REMARK 465     VAL C   475                                                      
REMARK 465     GLN C   476                                                      
REMARK 465     LYS D   744                                                      
REMARK 465     ASP D   745                                                      
REMARK 465     ASP D   756                                                      
REMARK 465     GLU D   757                                                      
REMARK 465     GLY E   244                                                      
REMARK 465     SER E   245                                                      
REMARK 465     HIS E   246                                                      
REMARK 465     LYS F   744                                                      
REMARK 465     ASP F   745                                                      
REMARK 465     LYS F   755                                                      
REMARK 465     ASP F   756                                                      
REMARK 465     GLU F   757                                                      
REMARK 465     GLY G   244                                                      
REMARK 465     SER G   245                                                      
REMARK 465     HIS G   246                                                      
REMARK 465     GLN G   476                                                      
REMARK 465     LYS H   744                                                      
REMARK 465     ASP H   745                                                      
REMARK 465     ASP H   756                                                      
REMARK 465     GLU H   757                                                      
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 247    CG   SD   CE                                        
REMARK 470     MET C 247    CG   SD   CE                                        
REMARK 470     ASP E 462    CG   OD1  OD2                                       
REMARK 470     GLN E 476    CG   CD   OE1  NE2                                  
REMARK 470     MET G 247    CG   SD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 346      122.57    -37.40                                   
REMARK 500    LEU A 395       40.99    -82.11                                   
REMARK 500    ASP A 398       47.32    -88.57                                   
REMARK 500    TYR A 401       17.89     81.77                                   
REMARK 500    LYS A 424        1.57    -69.73                                   
REMARK 500    ILE A 425      -50.13   -122.27                                   
REMARK 500    LEU C 395       57.79    -92.36                                   
REMARK 500    ASP E 398       58.66    -94.12                                   
REMARK 500    TYR E 401        2.72     80.56                                   
REMARK 500    HIS G 348       16.06    -60.55                                   
REMARK 500    LEU G 395       45.27    -92.53                                   
REMARK 500    ASP G 398       31.78    -83.46                                   
REMARK 500    GLN G 427       58.81   -140.65                                   
REMARK 500    ASP G 474       67.43     61.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 668        DISTANCE =  5.98 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP E 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP G 500                 
DBREF  5Q1H A  248   476  UNP    Q96RI1   NR1H4_HUMAN    258    486             
DBREF  5Q1H B  744   757  UNP    A8K1V4   A8K1V4_HUMAN   744    757             
DBREF  5Q1H C  248   476  UNP    Q96RI1   NR1H4_HUMAN    258    486             
DBREF  5Q1H D  744   757  UNP    A8K1V4   A8K1V4_HUMAN   744    757             
DBREF  5Q1H E  248   476  UNP    Q96RI1   NR1H4_HUMAN    258    486             
DBREF  5Q1H F  744   757  UNP    A8K1V4   A8K1V4_HUMAN   744    757             
DBREF  5Q1H G  248   476  UNP    Q96RI1   NR1H4_HUMAN    258    486             
DBREF  5Q1H H  744   757  UNP    A8K1V4   A8K1V4_HUMAN   744    757             
SEQADV 5Q1H GLY A  244  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H SER A  245  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H HIS A  246  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H MET A  247  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H ALA A  281  UNP  Q96RI1    GLU   291 CONFLICT                       
SEQADV 5Q1H ALA A  354  UNP  Q96RI1    GLU   364 CONFLICT                       
SEQADV 5Q1H GLY C  244  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H SER C  245  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H HIS C  246  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H MET C  247  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H ALA C  281  UNP  Q96RI1    GLU   291 CONFLICT                       
SEQADV 5Q1H ALA C  354  UNP  Q96RI1    GLU   364 CONFLICT                       
SEQADV 5Q1H GLY E  244  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H SER E  245  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H HIS E  246  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H MET E  247  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H ALA E  281  UNP  Q96RI1    GLU   291 CONFLICT                       
SEQADV 5Q1H ALA E  354  UNP  Q96RI1    GLU   364 CONFLICT                       
SEQADV 5Q1H GLY G  244  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H SER G  245  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H HIS G  246  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H MET G  247  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 5Q1H ALA G  281  UNP  Q96RI1    GLU   291 CONFLICT                       
SEQADV 5Q1H ALA G  354  UNP  Q96RI1    GLU   364 CONFLICT                       
SEQRES   1 A  233  GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU          
SEQRES   2 A  233  LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET          
SEQRES   3 A  233  PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE          
SEQRES   4 A  233  SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA          
SEQRES   5 A  233  THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS          
SEQRES   6 A  233  LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE          
SEQRES   7 A  233  ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU          
SEQRES   8 A  233  ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY          
SEQRES   9 A  233  HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY          
SEQRES  10 A  233  ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR          
SEQRES  11 A  233  LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR          
SEQRES  12 A  233  ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG          
SEQRES  13 A  233  GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN          
SEQRES  14 A  233  GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE          
SEQRES  15 A  233  HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU          
SEQRES  16 A  233  GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS          
SEQRES  17 A  233  ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS          
SEQRES  18 A  233  PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN              
SEQRES   1 B   14  LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP          
SEQRES   2 B   14  GLU                                                          
SEQRES   1 C  233  GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU          
SEQRES   2 C  233  LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET          
SEQRES   3 C  233  PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE          
SEQRES   4 C  233  SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA          
SEQRES   5 C  233  THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS          
SEQRES   6 C  233  LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE          
SEQRES   7 C  233  ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU          
SEQRES   8 C  233  ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY          
SEQRES   9 C  233  HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY          
SEQRES  10 C  233  ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR          
SEQRES  11 C  233  LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR          
SEQRES  12 C  233  ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG          
SEQRES  13 C  233  GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN          
SEQRES  14 C  233  GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE          
SEQRES  15 C  233  HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU          
SEQRES  16 C  233  GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS          
SEQRES  17 C  233  ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS          
SEQRES  18 C  233  PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN              
SEQRES   1 D   14  LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP          
SEQRES   2 D   14  GLU                                                          
SEQRES   1 E  233  GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU          
SEQRES   2 E  233  LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET          
SEQRES   3 E  233  PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE          
SEQRES   4 E  233  SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA          
SEQRES   5 E  233  THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS          
SEQRES   6 E  233  LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE          
SEQRES   7 E  233  ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU          
SEQRES   8 E  233  ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY          
SEQRES   9 E  233  HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY          
SEQRES  10 E  233  ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR          
SEQRES  11 E  233  LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR          
SEQRES  12 E  233  ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG          
SEQRES  13 E  233  GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN          
SEQRES  14 E  233  GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE          
SEQRES  15 E  233  HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU          
SEQRES  16 E  233  GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS          
SEQRES  17 E  233  ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS          
SEQRES  18 E  233  PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN              
SEQRES   1 F   14  LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP          
SEQRES   2 F   14  GLU                                                          
SEQRES   1 G  233  GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU          
SEQRES   2 G  233  LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET          
SEQRES   3 G  233  PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE          
SEQRES   4 G  233  SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA          
SEQRES   5 G  233  THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS          
SEQRES   6 G  233  LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE          
SEQRES   7 G  233  ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU          
SEQRES   8 G  233  ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY          
SEQRES   9 G  233  HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY          
SEQRES  10 G  233  ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR          
SEQRES  11 G  233  LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR          
SEQRES  12 G  233  ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG          
SEQRES  13 G  233  GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN          
SEQRES  14 G  233  GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE          
SEQRES  15 G  233  HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU          
SEQRES  16 G  233  GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS          
SEQRES  17 G  233  ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS          
SEQRES  18 G  233  PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN              
SEQRES   1 H   14  LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP          
SEQRES   2 H   14  GLU                                                          
HET    9NP  A 500      36                                                       
HET    9NP  C 500      36                                                       
HET    9NP  E 500      36                                                       
HET    9NP  G 500      36                                                       
HETNAM     9NP (2S)-N,2-DICYCLOHEXYL-2-{2-[4-(1H-TETRAZOL-5-YL)                 
HETNAM   2 9NP  PHENYL]-1H-BENZIMIDAZOL-1-YL}ACETAMIDE                          
FORMUL   9  9NP    4(C28 H33 N7 O)                                              
FORMUL  13  HOH   *277(H2 O)                                                    
HELIX    1 AA1 THR A  250  ASN A  265  1                                  16    
HELIX    2 AA2 MET A  269  GLU A  280  1                                  12    
HELIX    3 AA3 SER A  283  LYS A  308  1                                  26    
HELIX    4 AA4 GLY A  311  LEU A  315  5                                   5    
HELIX    5 AA5 ASP A  316  ASN A  341  1                                  26    
HELIX    6 AA6 GLY A  347  ASN A  358  1                                  12    
HELIX    7 AA7 SER A  362  LEU A  379  1                                  18    
HELIX    8 AA8 THR A  382  LEU A  395  1                                  14    
HELIX    9 AA9 ASP A  404  GLN A  427  1                                  24    
HELIX   10 AB1 GLN A  432  HIS A  450  1                                  19    
HELIX   11 AB2 HIS A  450  SER A  457  1                                   8    
HELIX   12 AB3 THR A  466  ASP A  474  1                                   9    
HELIX   13 AB4 HIS B  746  LYS B  755  1                                  10    
HELIX   14 AB5 THR C  250  ASN C  265  1                                  16    
HELIX   15 AB6 MET C  269  GLU C  280  1                                  12    
HELIX   16 AB7 SER C  283  LYS C  308  1                                  26    
HELIX   17 AB8 GLY C  311  LEU C  315  5                                   5    
HELIX   18 AB9 ASP C  316  LYS C  342  1                                  27    
HELIX   19 AC1 GLY C  347  ASN C  358  1                                  12    
HELIX   20 AC2 SER C  362  LEU C  379  1                                  18    
HELIX   21 AC3 THR C  382  LEU C  395  1                                  14    
HELIX   22 AC4 ASP C  404  GLN C  427  1                                  24    
HELIX   23 AC5 GLN C  432  TRP C  458  1                                  27    
HELIX   24 AC6 THR C  466  ASP C  474  1                                   9    
HELIX   25 AC7 GLN D  747  ASP D  754  1                                   8    
HELIX   26 AC8 THR E  250  ASN E  265  1                                  16    
HELIX   27 AC9 MET E  269  GLU E  280  1                                  12    
HELIX   28 AD1 SER E  283  LEU E  309  1                                  27    
HELIX   29 AD2 GLY E  311  LEU E  315  5                                   5    
HELIX   30 AD3 ASP E  316  ASN E  341  1                                  26    
HELIX   31 AD4 GLY E  347  ASN E  358  1                                  12    
HELIX   32 AD5 SER E  362  LEU E  379  1                                  18    
HELIX   33 AD6 THR E  382  LEU E  395  1                                  14    
HELIX   34 AD7 ASP E  404  GLN E  427  1                                  24    
HELIX   35 AD8 GLN E  432  HIS E  450  1                                  19    
HELIX   36 AD9 HIS E  450  SER E  457  1                                   8    
HELIX   37 AE1 THR E  466  ASP E  474  1                                   9    
HELIX   38 AE2 GLN F  747  ASP F  754  1                                   8    
HELIX   39 AE3 THR G  250  ASN G  265  1                                  16    
HELIX   40 AE4 MET G  269  GLU G  280  1                                  12    
HELIX   41 AE5 SER G  283  LYS G  308  1                                  26    
HELIX   42 AE6 GLY G  311  LEU G  315  5                                   5    
HELIX   43 AE7 ASP G  316  ASN G  341  1                                  26    
HELIX   44 AE8 HIS G  348  ASN G  358  1                                  11    
HELIX   45 AE9 SER G  362  LEU G  379  1                                  18    
HELIX   46 AF1 THR G  382  LEU G  395  1                                  14    
HELIX   47 AF2 ASP G  404  GLN G  427  1                                  24    
HELIX   48 AF3 GLN G  432  HIS G  450  1                                  19    
HELIX   49 AF4 HIS G  450  SER G  457  1                                   8    
HELIX   50 AF5 THR G  466  ASP G  474  1                                   9    
HELIX   51 AF6 GLN H  747  LYS H  755  1                                   9    
SSBOND   1 CYS A  436    CYS G  436                          1555   1555  2.05  
SITE     1 AC1 15 ILE A 277  ASN A 287  LEU A 291  MET A 294                    
SITE     2 AC1 15 HIS A 298  PHE A 333  SER A 336  ILE A 339                    
SITE     3 AC1 15 ILE A 356  ILE A 361  TYR A 373  HIS A 451                    
SITE     4 AC1 15 MET A 454  LEU A 455  TRP A 458                               
SITE     1 AC2 14 ILE C 277  ILE C 290  LEU C 291  MET C 294                    
SITE     2 AC2 14 HIS C 298  MET C 332  SER C 336  ILE C 356                    
SITE     3 AC2 14 ILE C 361  TYR C 373  HIS C 451  MET C 454                    
SITE     4 AC2 14 LEU C 455  TRP C 458                                          
SITE     1 AC3 14 ILE E 277  LEU E 291  MET E 294  HIS E 298                    
SITE     2 AC3 14 PHE E 333  SER E 336  ILE E 356  SER E 359                    
SITE     3 AC3 14 ILE E 361  TYR E 373  HIS E 451  MET E 454                    
SITE     4 AC3 14 LEU E 455  TRP E 458                                          
SITE     1 AC4 12 LEU G 291  MET G 294  HIS G 298  MET G 332                    
SITE     2 AC4 12 PHE G 333  SER G 336  ILE G 356  TYR G 373                    
SITE     3 AC4 12 HIS G 451  MET G 454  LEU G 455  TRP G 458                    
CRYST1   55.414  183.879   55.787  90.00  98.36  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018046  0.000000  0.002652        0.00000                         
SCALE2      0.000000  0.005438  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018118        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system