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
