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Database: PDB
Entry: 5Y7Y
LinkDB: 5Y7Y
Original site: 5Y7Y 
HEADER    TRANSCRIPTION                           18-AUG-17   5Y7Y              
TITLE     CRYSTAL STRUCTURE OF AHRR/ARNT COMPLEX                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARYL HYDROCARBON RECEPTOR REPRESSOR;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AHRR,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 77,BHLHE77;     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 82-147,154-230,257-271,301-312;               
COMPND  10 SYNONYM: ARNT PROTEIN;                                               
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AHRR, BHLHE77, KIAA1234;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  12 ORGANISM_COMMON: BOVINE;                                             
SOURCE  13 ORGANISM_TAXID: 9913;                                                
SOURCE  14 GENE: ARNT;                                                          
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSCRIPTIONAL REGULATION, TRANSCRIPTION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SAKURAI,T.SHIMIZU,U.OHTO                                            
REVDAT   2   21-FEB-18 5Y7Y    1       JRNL                                     
REVDAT   1   20-SEP-17 5Y7Y    0                                                
JRNL        AUTH   S.SAKURAI,T.SHIMIZU,U.OHTO                                   
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE AHRR-ARNT HETERODIMER REVEALS   
JRNL        TITL 2 THE STRUCTURAL BASIS OF THE REPRESSION OF AHR-MEDIATED       
JRNL        TITL 3 TRANSCRIPTION.                                               
JRNL        REF    J. BIOL. CHEM.                V. 292 17609 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28904176                                                     
JRNL        DOI    10.1074/JBC.M117.812974                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29016                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1542                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2095                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3742                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.27000                                              
REMARK   3    B22 (A**2) : 2.27000                                              
REMARK   3    B33 (A**2) : -4.54000                                             
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): 0.298         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.653         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3830 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3701 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5161 ; 0.967 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8487 ; 0.716 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   455 ; 5.513 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;32.753 ;22.967       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   680 ;13.602 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;11.639 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   583 ; 0.053 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4235 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   922 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1847 ; 2.092 ; 7.921       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1846 ; 2.086 ; 7.920       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2293 ; 3.784 ;11.837       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2294 ; 3.784 ;11.837       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1983 ; 1.635 ; 8.024       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1983 ; 1.635 ; 8.024       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2869 ; 2.966 ;11.986       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4160 ; 5.908 ;61.392       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4161 ; 5.908 ;61.395       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5Y7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004820.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30559                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, HEPES, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.89200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       32.44600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       97.33800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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 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    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     PHE A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     ASN A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     SER A    92                                                      
REMARK 465     ARG A    93                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     PRO A    95                                                      
REMARK 465     ALA A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     ALA A    99                                                      
REMARK 465     PRO A   100                                                      
REMARK 465     SER A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     ASP A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     CYS A   106                                                      
REMARK 465     PRO A   107                                                      
REMARK 465     LEU A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     VAL A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     VAL A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     PHE A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     GLN A   188                                                      
REMARK 465     PRO A   189                                                      
REMARK 465     PRO A   190                                                      
REMARK 465     PRO A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     THR A   194                                                      
REMARK 465     GLY A   195                                                      
REMARK 465     TRP A   209                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     THR A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     THR A   213                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     GLY B    78                                                      
REMARK 465     PRO B    79                                                      
REMARK 465     GLU B    80                                                      
REMARK 465     PHE B    81                                                      
REMARK 465     SER B    82                                                      
REMARK 465     SER B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     ASP B    85                                                      
REMARK 465     LYS B    86                                                      
REMARK 465     GLU B    87                                                      
REMARK 465     ARG B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     ALA B    90                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     ASN B    93                                                      
REMARK 465     HIS B    94                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     ASN B   256                                                      
REMARK 465     MET B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     PRO B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     PHE B   303                                                      
REMARK 465     VAL B   304                                                      
REMARK 465     ALA B   328                                                      
REMARK 465     TRP B   329                                                      
REMARK 465     PRO B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     SER B   333                                                      
REMARK 465     LYS B   334                                                      
REMARK 465     PHE B   335                                                      
REMARK 465     GLN B   344                                                      
REMARK 465     VAL B   345                                                      
REMARK 465     THR B   346                                                      
REMARK 465     SER B   347                                                      
REMARK 465     SER B   348                                                      
REMARK 465     PRO B   349                                                      
REMARK 465     ASN B   350                                                      
REMARK 465     CYS B   351                                                      
REMARK 465     THR B   352                                                      
REMARK 465     ASP B   353                                                      
REMARK 465     MET B   354                                                      
REMARK 465     SER B   355                                                      
REMARK 465     ASN B   356                                                      
REMARK 465     VAL B   357                                                      
REMARK 465     CYS B   358                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CZ   ARG A    41     OD1  ASP B   452     3555     1.56            
REMARK 500   NE   ARG A    41     OD1  ASP B   452     3555     1.84            
REMARK 500   NH2  ARG A    41     OD1  ASP B   452     3555     2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 236      -85.50   -104.94                                   
REMARK 500    GLU B  98       78.81   -107.84                                   
REMARK 500    ASN B 147      -71.37   -106.56                                   
REMARK 500    VAL B 186       72.21     33.08                                   
REMARK 500    ASP B 216       16.90   -140.65                                   
REMARK 500    ASP B 217      111.15   -165.59                                   
REMARK 500    VAL B 218       -9.28     76.67                                   
REMARK 500    TYR B 450      -49.56    115.30                                   
REMARK 500    ASP B 452       11.18     56.93                                   
REMARK 500    ILE B 454     -174.06    -68.70                                   
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 GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501                 
DBREF  5Y7Y A   27   280  UNP    A9YTQ3   AHRR_HUMAN      27    280             
DBREF  5Y7Y B   82   464  UNP    Q9BE97   ARNT_BOVIN      82    464             
SEQADV 5Y7Y GLY A   23  UNP  A9YTQ3              EXPRESSION TAG                 
SEQADV 5Y7Y PRO A   24  UNP  A9YTQ3              EXPRESSION TAG                 
SEQADV 5Y7Y GLU A   25  UNP  A9YTQ3              EXPRESSION TAG                 
SEQADV 5Y7Y PHE A   26  UNP  A9YTQ3              EXPRESSION TAG                 
SEQADV 5Y7Y GLY B   78  UNP  Q9BE97              EXPRESSION TAG                 
SEQADV 5Y7Y PRO B   79  UNP  Q9BE97              EXPRESSION TAG                 
SEQADV 5Y7Y GLU B   80  UNP  Q9BE97              EXPRESSION TAG                 
SEQADV 5Y7Y PHE B   81  UNP  Q9BE97              EXPRESSION TAG                 
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   148 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   149 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   150 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   151 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   152 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   153 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    TYR   154 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ALA   231 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   232 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   233 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   234 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   235 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ILE   236 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   237 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   238 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   239 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LYS   240 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   241 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   242 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    THR   243 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    VAL   244 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LYS   245 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LYS   246 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLU   247 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   248 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLN   249 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLN   250 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   251 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   252 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    MET   253 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   254 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    MET   255 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    CYS   256 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   272 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   273 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    VAL   274 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   275 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   276 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    VAL   277 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   278 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    MET   279 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASN   280 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   281 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   282 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   283 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    PHE   284 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    VAL   285 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   286 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASN   287 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   288 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    CYS   289 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ARG   290 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASN   291 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   292 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   293 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   294 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   295 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ALA   296 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LYS   297 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   298 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   299 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLU   300 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ALA   318 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   319 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    VAL   320 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    SER   321 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    LEU   322 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    PRO   323 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   324 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   325 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ASP   326 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    PRO   327 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLU   328 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    ALA   329 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLY   330 DELETION                       
SEQADV 5Y7Y     B       UNP  Q9BE97    GLN   331 DELETION                       
SEQRES   1 A  258  GLY PRO GLU PHE PRO ALA VAL GLY ALA GLU LYS SER ASN          
SEQRES   2 A  258  PRO SER LYS ARG HIS ARG ASP ARG LEU ASN ALA GLU LEU          
SEQRES   3 A  258  ASP HIS LEU ALA SER LEU LEU PRO PHE PRO PRO ASP ILE          
SEQRES   4 A  258  ILE SER LYS LEU ASP LYS LEU SER VAL LEU ARG LEU SER          
SEQRES   5 A  258  VAL SER TYR LEU ARG VAL LYS SER PHE PHE GLN VAL VAL          
SEQRES   6 A  258  GLN GLU GLN SER SER ARG GLN PRO ALA ALA GLY ALA PRO          
SEQRES   7 A  258  SER PRO GLY ASP SER CYS PRO LEU ALA GLY SER ALA VAL          
SEQRES   8 A  258  LEU GLU GLY ARG LEU LEU LEU GLU SER LEU ASN GLY PHE          
SEQRES   9 A  258  ALA LEU VAL VAL SER ALA GLU GLY THR ILE PHE TYR ALA          
SEQRES  10 A  258  SER ALA THR ILE VAL ASP TYR LEU GLY PHE HIS GLN THR          
SEQRES  11 A  258  ASP VAL MET HIS GLN ASN ILE TYR ASP TYR ILE HIS VAL          
SEQRES  12 A  258  ASP ASP ARG GLN ASP PHE CYS ARG GLN LEU HIS TRP ALA          
SEQRES  13 A  258  MET ASP PRO PRO GLN VAL VAL PHE GLY GLN PRO PRO PRO          
SEQRES  14 A  258  LEU GLU THR GLY ASP ASP ALA ILE LEU GLY ARG LEU LEU          
SEQRES  15 A  258  ARG ALA GLN GLU TRP GLY THR GLY THR PRO THR GLU TYR          
SEQRES  16 A  258  SER ALA PHE LEU THR ARG CYS PHE ILE CYS ARG VAL ARG          
SEQRES  17 A  258  CYS LEU LEU ASP SER THR SER GLY PHE LEU THR MET GLN          
SEQRES  18 A  258  PHE GLN GLY LYS LEU LYS PHE LEU PHE GLY GLN LYS LYS          
SEQRES  19 A  258  LYS ALA PRO SER GLY ALA MET LEU PRO PRO ARG LEU SER          
SEQRES  20 A  258  LEU PHE CYS ILE ALA ALA PRO VAL LEU LEU PRO                  
SEQRES   1 B  311  GLY PRO GLU PHE SER SER ALA ASP LYS GLU ARG LEU ALA          
SEQRES   2 B  311  ARG GLU ASN HIS SER GLU ILE GLU ARG ARG ARG ARG ASN          
SEQRES   3 B  311  LYS MET THR ALA TYR ILE THR GLU LEU SER ASP MET VAL          
SEQRES   4 B  311  PRO THR CYS SER ALA LEU ALA ARG LYS PRO ASP LYS LEU          
SEQRES   5 B  311  THR ILE LEU ARG MET ALA VAL SER HIS MET LYS SER LEU          
SEQRES   6 B  311  ARG GLY THR GLY ASN LYS PRO SER PHE LEU THR ASP GLN          
SEQRES   7 B  311  GLU LEU LYS HIS LEU ILE LEU GLU ALA ALA ASP GLY PHE          
SEQRES   8 B  311  LEU PHE ILE VAL SER CYS GLU THR GLY ARG VAL VAL TYR          
SEQRES   9 B  311  VAL SER ASP SER VAL THR PRO VAL LEU ASN GLN PRO GLN          
SEQRES  10 B  311  SER GLU TRP PHE GLY SER THR LEU TYR ASP GLN VAL HIS          
SEQRES  11 B  311  PRO ASP ASP VAL ASP LYS LEU ARG GLU GLN LEU SER THR          
SEQRES  12 B  311  SER GLU ASN MET GLY SER ARG ARG SER PHE ILE CYS ARG          
SEQRES  13 B  311  MET ARG CYS GLY ASN PRO HIS PHE VAL VAL VAL HIS CYS          
SEQRES  14 B  311  THR GLY TYR ILE LYS ALA TRP PRO PRO GLY SER LYS PHE          
SEQRES  15 B  311  CYS LEU VAL ALA ILE GLY ARG LEU GLN VAL THR SER SER          
SEQRES  16 B  311  PRO ASN CYS THR ASP MET SER ASN VAL CYS GLN PRO THR          
SEQRES  17 B  311  GLU PHE ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR          
SEQRES  18 B  311  PHE VAL ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN          
SEQRES  19 B  311  PRO GLN GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS          
SEQRES  20 B  311  HIS PRO GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN          
SEQRES  21 B  311  GLN VAL VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET          
SEQRES  22 B  311  PHE ARG PHE ARG SER LYS ASN ARG GLU TRP LEU TRP VAL          
SEQRES  23 B  311  ARG THR SER SER PHE THR PHE GLN ASN PRO TYR SER ASP          
SEQRES  24 B  311  GLU ILE GLU TYR ILE ILE CYS THR ASN THR ASN VAL              
HET    GOL  A 301       6                                                       
HET    GOL  A 302       6                                                       
HET    GOL  B 501       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *22(H2 O)                                                     
HELIX    1 AA1 LYS A   38  LEU A   54  1                                  17    
HELIX    2 AA2 PRO A   58  SER A   63  1                                   6    
HELIX    3 AA3 ASP A   66  GLN A   90  1                                  25    
HELIX    4 AA4 GLY A  116  LEU A  123  1                                   8    
HELIX    5 AA5 THR A  142  GLY A  148  1                                   7    
HELIX    6 AA6 HIS A  150  MET A  155  1                                   6    
HELIX    7 AA7 ASN A  158  ILE A  163  5                                   6    
HELIX    8 AA8 HIS A  164  ASP A  166  5                                   3    
HELIX    9 AA9 ASP A  167  HIS A  176  1                                  10    
HELIX   10 AB1 ASP A  197  GLN A  207  1                                  11    
HELIX   11 AB2 TYR A  217  PHE A  220  5                                   4    
HELIX   12 AB3 GLU B   98  VAL B  116  1                                  19    
HELIX   13 AB4 VAL B  116  ALA B  121  1                                   6    
HELIX   14 AB5 ASP B  127  GLY B  144  1                                  18    
HELIX   15 AB6 THR B  160  ALA B  172  1                                  13    
HELIX   16 AB7 SER B  192  LEU B  197  1                                   6    
HELIX   17 AB8 LEU B  209  VAL B  213  5                                   5    
HELIX   18 AB9 ASP B  219  LEU B  225  1                                   7    
HELIX   19 AC1 ARG B  379  GLY B  385  1                                   7    
HELIX   20 AC2 GLN B  387  LEU B  392  1                                   6    
HELIX   21 AC3 ASN B  395  CYS B  400  5                                   6    
HELIX   22 AC4 HIS B  401  GLU B  403  5                                   3    
HELIX   23 AC5 ASP B  404  LYS B  419  1                                  16    
SHEET    1 AA1 5 ILE A 136  ALA A 139  0                                        
SHEET    2 AA1 5 PHE A 126  VAL A 130 -1  N  VAL A 129   O  TYR A 138           
SHEET    3 AA1 5 LEU A 268  PRO A 276 -1  O  ALA A 274   N  PHE A 126           
SHEET    4 AA1 5 PHE A 239  PHE A 250 -1  N  GLN A 243   O  ALA A 275           
SHEET    5 AA1 5 THR A 222  ARG A 230 -1  N  VAL A 229   O  LEU A 240           
SHEET    1 AA2 5 TYR B 188  VAL B 189  0                                        
SHEET    2 AA2 5 GLY B 174  VAL B 179 -1  N  ILE B 178   O  TYR B 188           
SHEET    3 AA2 5 LEU B 337  ARG B 342 -1  O  ALA B 339   N  PHE B 177           
SHEET    4 AA2 5 VAL B 306  TYR B 311 -1  N  HIS B 307   O  ARG B 342           
SHEET    5 AA2 5 PHE B 263  CYS B 265 -1  N  PHE B 263   O  CYS B 308           
SHEET    1 AA3 5 PHE B 373  VAL B 376  0                                        
SHEET    2 AA3 5 GLU B 362  HIS B 367 -1  N  ARG B 366   O  THR B 374           
SHEET    3 AA3 5 GLU B 455  ASN B 463 -1  O  CYS B 459   N  SER B 365           
SHEET    4 AA3 5 TRP B 436  GLN B 447 -1  N  ARG B 440   O  THR B 462           
SHEET    5 AA3 5 LEU B 423  ARG B 430 -1  N  PHE B 429   O  LEU B 437           
CISPEP   1 GLU A  115    GLY A  116          0         4.26                     
CISPEP   2 SER B   95    GLU B   96          0        -2.77                     
CISPEP   3 GLY B  146    ASN B  147          0        -2.70                     
CISPEP   4 GLY B  184    ARG B  185          0        -4.57                     
CISPEP   5 HIS B  214    PRO B  215          0         2.64                     
CISPEP   6 PRO B  215    ASP B  216          0       -12.09                     
CISPEP   7 ASP B  217    VAL B  218          0         2.48                     
CISPEP   8 MET B  267    ARG B  268          0       -10.14                     
CISPEP   9 GLY B  270    ASN B  271          0        -0.36                     
SITE     1 AC1  7 SER A 131  GLU A 133  THR A 135  PHE A 137                    
SITE     2 AC1  7 GLN A 254  LYS A 256  HOH A 406                               
SITE     1 AC2  4 ARG A 230  SER A 237  PHE A 239  ARG B 434                    
SITE     1 AC3  5 PHE A 149  ASP A 161  ARG A 230  LYS B 394                    
SITE     2 AC3  5 GLU B 398                                                     
CRYST1   78.362   78.362  129.784  90.00  90.00  90.00 P 41          4          
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      0.012761  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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