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Entry: 1ENX
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END                                                                             
HEADER    TRANSCRIPTION                           15-FEB-11   3AUQ              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN VITAMIN D RECEPTOR LIGAND BINDING      
TITLE    2 DOMAIN COMPLEXED WITH YNE-DIENE TYPE ANALOG OF ACTIVE 14-EPI-2ALPHA- 
TITLE    3 METHYL-19-NORVITAMIN D3                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VITAMIN D3 RECEPTOR;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN;                                     
COMPND   5 SYNONYM: VDR, 1,25-DIHYDROXYVITAMIN D3 RECEPTOR, NUCLEAR RECEPTOR    
COMPND   6 SUBFAMILY 1 GROUP I MEMBER 1;                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: VDR;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HORMONE RECEPTOR, TRANSCRIPTION                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KAKUDA,M.TAKIMOTO-KAMIMURA                                          
REVDAT   2   16-AUG-17 3AUQ    1       SOURCE REMARK                            
REVDAT   1   14-SEP-11 3AUQ    0                                                
JRNL        AUTH   D.SAWADA,Y.TSUKUDA,H.SAITO,S.KAKUDA,M.TAKIMOTO-KAMIMURA,     
JRNL        AUTH 2 E.OCHIAI,K.TAKENOUCHI,A.KITTAKA                              
JRNL        TITL   DEVELOPMENT OF 14-EPI-19-NORTACHYSTEROL AND ITS              
JRNL        TITL 2 UNPRECEDENTED BINDING CONFIGURATION FOR THE HUMAN VITAMIN D  
JRNL        TITL 3 RECEPTOR                                                     
JRNL        REF    J.AM.CHEM.SOC.                V. 133  7215 2011              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   21500802                                                     
JRNL        DOI    10.1021/JA201481J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 8816                           
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 442                             
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) : 2.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.71                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 625                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2018                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): 1.197         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.375         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.268         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.687        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.907                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2090 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2832 ; 1.024 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   251 ; 4.469 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    91 ;37.485 ;24.286       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   383 ;16.222 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;12.879 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   328 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1535 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   986 ; 0.169 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1463 ; 0.291 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    57 ; 0.093 ; 0.200       
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):    32 ; 0.163 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.101 ; 0.200       
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):  1316 ; 0.305 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2065 ; 0.546 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   863 ; 0.438 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   767 ; 0.761 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AUQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000029718.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9559                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 2.550                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1DB1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 1.2-1.6M AMMONIUM SULFATE,     
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.15650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.28850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.05400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.28850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.15650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.05400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     MET A   117                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     ASN A   424                                                      
REMARK 465     GLU A   425                                                      
REMARK 465     ILE A   426                                                      
REMARK 465     SER A   427                                                      
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    ASP A 283       13.04   -141.69                                   
REMARK 500    CYS A 288       52.20   -112.98                                   
REMARK 500    GLN A 291      -44.52   -175.46                                   
REMARK 500    ASP A 342       57.22    -92.06                                   
REMARK 500    GLN A 347      -73.87    -90.14                                   
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 CA9 A 1                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS ENTRY IS DELETION MUTANT. REISDUES 165-215 WERE DELETED.        
DBREF  3AUQ A  118   164  UNP    P11473   VDR_HUMAN      118    164             
DBREF  3AUQ A  216   427  UNP    P11473   VDR_HUMAN      216    427             
SEQADV 3AUQ GLY A  114  UNP  P11473              EXPRESSION TAG                 
SEQADV 3AUQ SER A  115  UNP  P11473              EXPRESSION TAG                 
SEQADV 3AUQ HIS A  116  UNP  P11473              EXPRESSION TAG                 
SEQADV 3AUQ MET A  117  UNP  P11473              EXPRESSION TAG                 
SEQRES   1 A  263  GLY SER HIS MET ASP SER LEU ARG PRO LYS LEU SER GLU          
SEQRES   2 A  263  GLU GLN GLN ARG ILE ILE ALA ILE LEU LEU ASP ALA HIS          
SEQRES   3 A  263  HIS LYS THR TYR ASP PRO THR TYR SER ASP PHE CYS GLN          
SEQRES   4 A  263  PHE ARG PRO PRO VAL ARG VAL ASN ASP GLY GLY GLY SER          
SEQRES   5 A  263  VAL THR LEU GLU LEU SER GLN LEU SER MET LEU PRO HIS          
SEQRES   6 A  263  LEU ALA ASP LEU VAL SER TYR SER ILE GLN LYS VAL ILE          
SEQRES   7 A  263  GLY PHE ALA LYS MET ILE PRO GLY PHE ARG ASP LEU THR          
SEQRES   8 A  263  SER GLU ASP GLN ILE VAL LEU LEU LYS SER SER ALA ILE          
SEQRES   9 A  263  GLU VAL ILE MET LEU ARG SER ASN GLU SER PHE THR MET          
SEQRES  10 A  263  ASP ASP MET SER TRP THR CYS GLY ASN GLN ASP TYR LYS          
SEQRES  11 A  263  TYR ARG VAL SER ASP VAL THR LYS ALA GLY HIS SER LEU          
SEQRES  12 A  263  GLU LEU ILE GLU PRO LEU ILE LYS PHE GLN VAL GLY LEU          
SEQRES  13 A  263  LYS LYS LEU ASN LEU HIS GLU GLU GLU HIS VAL LEU LEU          
SEQRES  14 A  263  MET ALA ILE CYS ILE VAL SER PRO ASP ARG PRO GLY VAL          
SEQRES  15 A  263  GLN ASP ALA ALA LEU ILE GLU ALA ILE GLN ASP ARG LEU          
SEQRES  16 A  263  SER ASN THR LEU GLN THR TYR ILE ARG CYS ARG HIS PRO          
SEQRES  17 A  263  PRO PRO GLY SER HIS LEU LEU TYR ALA LYS MET ILE GLN          
SEQRES  18 A  263  LYS LEU ALA ASP LEU ARG SER LEU ASN GLU GLU HIS SER          
SEQRES  19 A  263  LYS GLN TYR ARG CYS LEU SER PHE GLN PRO GLU CYS SER          
SEQRES  20 A  263  MET LYS LEU THR PRO LEU VAL LEU GLU VAL PHE GLY ASN          
SEQRES  21 A  263  GLU ILE SER                                                  
HET    CA9  A   1      30                                                       
HETNAM     CA9 (1R,2S,3R)-5-[2-[(1R,3AS,7AR)-1-[(2R)-6-HYDROXY-6-               
HETNAM   2 CA9  METHYL-HEPTAN-2-YL]-7A-METHYL-1,2,3,3A,6,7-                     
HETNAM   3 CA9  HEXAHYDROINDEN-4-YL]ETHYNYL]-2-METHYL-CYCLOHEX-4-ENE-           
HETNAM   4 CA9  1,3-DIOL                                                        
FORMUL   2  CA9    C27 H42 O3                                                   
FORMUL   3  HOH   *10(H2 O)                                                     
HELIX    1   1 SER A  125  TYR A  143  1                                  19    
HELIX    2   2 ASP A  149  PHE A  153  5                                   5    
HELIX    3   3 SER A  216  LEU A  224  1                                   9    
HELIX    4   4 MET A  226  MET A  247  1                                  22    
HELIX    5   5 GLY A  250  LEU A  254  5                                   5    
HELIX    6   6 THR A  255  SER A  275  1                                  21    
HELIX    7   7 ARG A  296  LYS A  302  1                                   7    
HELIX    8   8 SER A  306  LYS A  322  1                                  17    
HELIX    9   9 HIS A  326  VAL A  339  1                                  14    
HELIX   10  10 ASP A  348  HIS A  371  1                                  24    
HELIX   11  11 LEU A  378  SER A  405  1                                  28    
HELIX   12  12 CYS A  410  LEU A  414  5                                   5    
HELIX   13  13 THR A  415  GLY A  423  1                                   9    
SHEET    1   A 3 PHE A 279  THR A 280  0                                        
SHEET    2   A 3 SER A 285  THR A 287 -1  O  SER A 285   N  THR A 280           
SHEET    3   A 3 LYS A 294  TYR A 295 -1  O  TYR A 295   N  TRP A 286           
CISPEP   1 GLY A  289    ASN A  290          0       -20.06                     
CISPEP   2 PRO A  372    PRO A  373          0        -5.27                     
CISPEP   3 PRO A  373    PRO A  374          0        -1.68                     
SITE     1 AC1  9 TYR A 143  PHE A 150  SER A 237  ARG A 274                    
SITE     2 AC1  9 SER A 275  SER A 278  TRP A 286  HIS A 305                    
SITE     3 AC1  9 HIS A 397                                                     
CRYST1   44.313   52.108  132.577  90.00  90.00  90.00 P 21 21 21    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      0.022567  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019191  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007543        0.00000                         
(ATOM LINES ARE NOT SHOWN.)

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