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Database: PDB
Entry: 3N00
LinkDB: 3N00
Original site: 3N00 
HEADER    TRANSCRIPTION REGULATOR                 13-MAY-10   3N00              
TITLE     CRYSTAL STRUCTURE OF A DELETION MUTANT OF HUMAN REVERBA LIGAND BINDING
TITLE    2 DOMAIN BOUND WITH AN NCOR ID1 PEPTIDE DETERMINED TO 2.60A            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REV-ERBA-ALPHA;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NUCLEAR RECEPTOR SUBFAMILY 1 GROUP D MEMBER 1, V-ERBA-      
COMPND   5 RELATED PROTEIN 1, EAR-1;                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COREPRESSOR 1;                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: CORNR BOX 2 RESIDUES 2045-2065;                            
COMPND  11 SYNONYM: N-COR1, N-COR;                                              
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: NR1D1, EAR1, HREV, THRAL;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24;                                
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    REVERBA NCORID1, ANTI-PARALLEL B-SHEET, TRANSCRIPTION REGULATOR       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.GAMPE,R.NOLTE                                                       
REVDAT   3   16-AUG-17 3N00    1       SOURCE REMARK                            
REVDAT   2   21-JUL-10 3N00    1       JRNL                                     
REVDAT   1   30-JUN-10 3N00    0                                                
JRNL        AUTH   C.A.PHELAN,R.T.GAMPE,M.H.LAMBERT,D.J.PARKS,V.MONTANA,        
JRNL        AUTH 2 J.BYNUM,T.M.BRODERICK,X.HU,S.P.WILLIAMS,R.T.NOLTE,M.A.LAZAR  
JRNL        TITL   STRUCTURE OF REV-ERBALPHA BOUND TO N-COR REVEALS A UNIQUE    
JRNL        TITL 2 MECHANISM OF NUCLEAR RECEPTOR-CO-REPRESSOR INTERACTION.      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   808 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20581824                                                     
JRNL        DOI    10.1038/NSMB.1860                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 6.0.2                                         
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 7693                           
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 225                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 554                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 16                           
REMARK   3   BIN FREE R VALUE                    : 0.2620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1549                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.320         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.206         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.170        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1570 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1055 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2116 ; 1.126 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2564 ; 0.837 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   201 ; 5.433 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    63 ;28.156 ;23.175       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   274 ;15.115 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;22.934 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   255 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1730 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   318 ; 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):  1012 ; 0.604 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   417 ; 0.067 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1610 ; 1.184 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   558 ; 1.591 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   506 ; 2.900 ; 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 : BABINET MODEL WITH 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 3N00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059207.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7921                               
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 50.5000                            
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) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1DB1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1UL OF PRECIPITANT COMPOSED OF 6-9% OF   
REMARK 280  PEG 3350, 8% GLYCEROL, 200MM PROLINE, 80MM HEPES WAS MIXED WITH     
REMARK 280  1UL OF THE REV-ERBA NCOR COMPLEX AT 5-6 MG/LIT TO OBTAIN            
REMARK 280  DIFFRACTION GRADE CRYSTALS, PH 7.5, VAPOR DIFFUSION, TEMPERATURE    
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       56.27500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       32.49039            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       34.61100            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       56.27500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       32.49039            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       34.61100            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       56.27500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       32.49039            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       34.61100            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       56.27500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       32.49039            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       34.61100            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       56.27500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       32.49039            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       34.61100            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       56.27500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       32.49039            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       34.61100            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       64.98077            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       69.22200            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       64.98077            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       69.22200            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       64.98077            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       69.22200            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       64.98077            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       69.22200            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       64.98077            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       69.22200            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       64.98077            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       69.22200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      194.94232            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      103.83300            
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: 2040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     MET A   271                                                      
REMARK 465     LYS A   272                                                      
REMARK 465     LYS A   273                                                      
REMARK 465     HIS A   274                                                      
REMARK 465     HIS A   275                                                      
REMARK 465     HIS A   276                                                      
REMARK 465     HIS A   277                                                      
REMARK 465     HIS A   278                                                      
REMARK 465     HIS A   279                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     THR A   400                                                      
REMARK 465     TYR A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     HIS A   403                                                      
REMARK 465     ASP A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     GLY A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     SER A   409                                                      
REMARK 465     PRO A   410                                                      
REMARK 465     GLY A   411                                                      
REMARK 465     ASN A   412                                                      
REMARK 465     PHE A   413                                                      
REMARK 465     ASN A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     ASN A   416                                                      
REMARK 465     HIS A   417                                                      
REMARK 465     ALA A   418                                                      
REMARK 465     SER A   419                                                      
REMARK 465     GLY A   420                                                      
REMARK 465     SER A   421                                                      
REMARK 465     PRO A   422                                                      
REMARK 465     TYR A   423                                                      
REMARK 465     PRO A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     GLY A   426                                                      
REMARK 465     ARG A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     THR A   431                                                      
REMARK 465     GLN A   493                                                      
REMARK 465     THR A   494                                                      
REMARK 465     VAL A   495                                                      
REMARK 465     MET A   496                                                      
REMARK 465     PHE A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     THR A   501                                                      
REMARK 465     THR A   502                                                      
REMARK 465     TYR A   503                                                      
REMARK 465     SER A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     GLN A   506                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     ALA A   613                                                      
REMARK 465     GLN A   614                                                      
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     GLU A 286    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 294    CZ   NH1  NH2                                       
REMARK 470     GLU A 434    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 435    CG2  CD1                                            
REMARK 470     ASP A 438    CB   CG   OD1  OD2                                  
REMARK 470     SER A 442    OG                                                  
REMARK 470     PHE A 484    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ALA A 485    CB                                                  
REMARK 470     LEU A 487    CG   CD1  CD2                                       
REMARK 470     PHE A 488    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 489    CB   CG   OD1  ND2                                  
REMARK 470     VAL A 490    CB   CG1  CG2                                       
REMARK 470     LYS A 491    CB   CG   CD   CE   NZ                              
REMARK 470     ASP A 492    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 507    CB   CG   CD   OE1  OE2                             
REMARK 470     MET A 513    CG   SD   CE                                        
REMARK 470     LEU A 517    CG   CD1  CD2                                       
REMARK 470     SER A 518    CB   OG                                             
REMARK 470     PHE A 521    CE1  CE2  CZ                                        
REMARK 470     ASP A 522    OD1  OD2                                            
REMARK 470     GLU A 525    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 564    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 576    NZ                                                  
REMARK 470     ARG A 610    CZ   NH1  NH2                                       
REMARK 470     GLN B2061    CG   CD   OE1  NE2                                  
REMARK 470     ARG B2065    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 487       24.81    -75.07                                   
REMARK 500    PHE A 488     -128.97    -94.00                                   
REMARK 500    ASN A 489     -151.69   -171.08                                   
REMARK 500    LYS A 491      -73.86    -67.98                                   
REMARK 500    LEU A 516      -72.79    -73.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  432     GLN A  433                  149.73                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VOV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A DELETION MUTANT OF APO HUMAN REVERBB LIGAND   
REMARK 900 BINDING DOMAIN DETERMINED TO 2.40A                                   
REMARK 900 RELATED ID: 3CQV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEME BOUND HUMAN REVERBB LIGAND BINDING DOMAIN  
REMARK 900 BOUND DETERMINED TO 1.90A                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 324-422 WERE DELETED IN THIS CONSTRUCT.                     
DBREF  3N00 A  281   422  UNP    P20393   NR1D1_HUMAN    281    323             
DBREF  3N00 A  423   614  UNP    P20393   NR1D1_HUMAN    423    614             
DBREF  3N00 B 2045  2065  UNP    O75376   NCOR1_HUMAN   2045   2065             
SEQADV 3N00 MET A  271  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 LYS A  272  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 LYS A  273  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  274  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  275  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  276  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  277  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  278  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 HIS A  279  UNP  P20393              EXPRESSION TAG                 
SEQADV 3N00 GLY A  280  UNP  P20393              EXPRESSION TAG                 
SEQRES   1 A  245  MET LYS LYS HIS HIS HIS HIS HIS HIS GLY PRO GLU PRO          
SEQRES   2 A  245  THR VAL GLU ASP VAL ILE SER GLN VAL ALA ARG ALA HIS          
SEQRES   3 A  245  ARG GLU ILE PHE THR TYR ALA HIS ASP LYS LEU GLY SER          
SEQRES   4 A  245  SER PRO GLY ASN PHE ASN ALA ASN HIS ALA SER GLY SER          
SEQRES   5 A  245  PRO TYR PRO HIS GLY ARG SER GLY ARG THR VAL GLN GLU          
SEQRES   6 A  245  ILE TRP GLU ASP PHE SER MET SER PHE THR PRO ALA VAL          
SEQRES   7 A  245  ARG GLU VAL VAL GLU PHE ALA LYS HIS ILE PRO GLY PHE          
SEQRES   8 A  245  ARG ASP LEU SER GLN HIS ASP GLN VAL THR LEU LEU LYS          
SEQRES   9 A  245  ALA GLY THR PHE GLU VAL LEU MET VAL ARG PHE ALA SER          
SEQRES  10 A  245  LEU PHE ASN VAL LYS ASP GLN THR VAL MET PHE LEU SER          
SEQRES  11 A  245  ARG THR THR TYR SER LEU GLN GLU LEU GLY ALA MET GLY          
SEQRES  12 A  245  MET GLY ASP LEU LEU SER ALA MET PHE ASP PHE SER GLU          
SEQRES  13 A  245  LYS LEU ASN SER LEU ALA LEU THR GLU GLU GLU LEU GLY          
SEQRES  14 A  245  LEU PHE THR ALA VAL VAL LEU VAL SER ALA ASP ARG SER          
SEQRES  15 A  245  GLY MET GLU ASN SER ALA SER VAL GLU GLN LEU GLN GLU          
SEQRES  16 A  245  THR LEU LEU ARG ALA LEU ARG ALA LEU VAL LEU LYS ASN          
SEQRES  17 A  245  ARG PRO LEU GLU THR SER ARG PHE THR LYS LEU LEU LEU          
SEQRES  18 A  245  LYS LEU PRO ASP LEU ARG THR LEU ASN ASN MET HIS SER          
SEQRES  19 A  245  GLU LYS LEU LEU SER PHE ARG VAL ASP ALA GLN                  
SEQRES   1 B   21  THR HIS ARG LEU ILE THR LEU ALA ASP HIS ILE CYS GLN          
SEQRES   2 B   21  ILE ILE THR GLN ASP PHE ALA ARG                              
FORMUL   3  HOH   *62(H2 O)                                                     
HELIX    1   1 THR A  284  PHE A  300  1                                  17    
HELIX    2   2 GLN A  433  ILE A  457  1                                  25    
HELIX    3   3 GLY A  459  LEU A  463  5                                   5    
HELIX    4   4 SER A  464  LEU A  487  1                                  24    
HELIX    5   5 LEU A  508  GLY A  512  5                                   5    
HELIX    6   6 MET A  513  LEU A  530  1                                  18    
HELIX    7   7 THR A  533  SER A  547  1                                  15    
HELIX    8   8 ASN A  555  ARG A  578  1                                  24    
HELIX    9   9 SER A  583  LEU A  590  1                                   8    
HELIX   10  10 LEU A  590  SER A  603  1                                  14    
HELIX   11  11 LEU B 2051  ARG B 2065  1                                  15    
SHEET    1   A 2 LEU A 606  ARG A 610  0                                        
SHEET    2   A 2 HIS B2046  THR B2050 -1  O  ILE B2049   N  LEU A 607           
CRYST1  112.550  112.550  103.833  90.00  90.00 120.00 H 3 2        18          
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      0.008885  0.005130  0.000000        0.00000                         
SCALE2      0.000000  0.010259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009631        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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