HEADER TRANSCRIPTION 01-AUG-06 2DVQ
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE N-TERMINAL BROMODOMAIN OF HUMAN BRD2
TITLE 2 COMPLEXED WITH ACETYLATED HISTONE H4 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: N-TERMINAL BROMODOMAIN, BD1;
COMPND 5 SYNONYM: RING3 PROTEIN, O27.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H4;
COMPND 9 CHAIN: P, Q;
COMPND 10 FRAGMENT: N-TERM TAIL;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCR2.1-TOPO VECTOR;
SOURCE 9 OTHER_DETAILS: EXPRESSED BY CELL-FREE SYSTEM;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS ALPHA-HELICAL DOMAIN, BROMODOMAIN, BINDS TO ACETYLATED HISTONES,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKAMURA,T.UMEHARA,M.SHIROUZU,B.PADMANABHAN,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 03-APR-24 2DVQ 1 SEQADV LINK
REVDAT 3 16-MAR-10 2DVQ 1 JRNL
REVDAT 2 24-FEB-09 2DVQ 1 VERSN
REVDAT 1 07-AUG-07 2DVQ 0
JRNL AUTH T.UMEHARA,Y.NAKAMURA,M.K.JANG,K.NAKANO,A.TANAKA,K.OZATO,
JRNL AUTH 2 B.PADMANABHAN,S.YOKOYAMA
JRNL TITL STRUCTURAL BASIS FOR ACETYLATED HISTONE H4 RECOGNITION BY
JRNL TITL 2 THE HUMAN BRD2 BROMODOMAIN.
JRNL REF J.BIOL.CHEM. V. 285 7610 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20048151
JRNL DOI 10.1074/JBC.M109.062422
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 24375
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1301
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) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.14000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : -0.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.188
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.840
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2987 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4028 ; 1.547 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 351 ; 6.491 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2248 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1550 ; 0.237 ; 0.200
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): 194 ; 0.168 ; 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): 71 ; 0.266 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.351 ; 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): 1776 ; 1.011 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2860 ; 1.878 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1211 ; 3.304 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1168 ; 4.730 ; 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000025901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
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 (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06800
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) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: BD1 NATIVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME 5K, AS, PH 6.50, VAPOR
REMARK 280 DIFFUSION, CO-CRYSTALLIZAATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 56.90550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.57150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.90550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.57150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 APPLY THE FOLLOWING TO CHAINS: A, B, P, Q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 113.81100
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 195 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 204 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 229 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 257 LIES ON A SPECIAL POSITION.
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 LEU A 187
REMARK 465 VAL A 188
REMARK 465 VAL A 189
REMARK 465 THR A 190
REMARK 465 ILE A 191
REMARK 465 PRO A 192
REMARK 465 LYS A 193
REMARK 465 ASN A 194
REMARK 465 GLN B 185
REMARK 465 GLU B 186
REMARK 465 LEU B 187
REMARK 465 VAL B 188
REMARK 465 VAL B 189
REMARK 465 THR B 190
REMARK 465 ILE B 191
REMARK 465 PRO B 192
REMARK 465 LYS B 193
REMARK 465 ASN B 194
REMARK 465 GLY C 73
REMARK 465 ARG C 74
REMARK 465 VAL C 75
REMARK 465 GLU C 183
REMARK 465 GLU C 184
REMARK 465 GLN C 185
REMARK 465 GLU C 186
REMARK 465 LEU C 187
REMARK 465 VAL C 188
REMARK 465 VAL C 189
REMARK 465 THR C 190
REMARK 465 ILE C 191
REMARK 465 PRO C 192
REMARK 465 LYS C 193
REMARK 465 ASN C 194
REMARK 465 SER P 1
REMARK 465 GLY P 2
REMARK 465 ARG P 3
REMARK 465 GLY P 4
REMARK 465 LYS P 5
REMARK 465 GLY P 6
REMARK 465 GLY P 7
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 LYS P 8 CG CD CE NZ
REMARK 470 ARG Q 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS Q 5 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 208 O HOH C 208 2655 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 GLY Q 7 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 184 93.17 -57.63
REMARK 500 VAL B 75 113.29 69.35
REMARK 500 LEU B 110 68.21 -118.43
REMARK 500 LEU C 110 67.60 -116.05
REMARK 500 LEU P 10 -39.62 -141.87
REMARK 500 ARG Q 3 -52.88 -141.21
REMARK 500 LYS Q 8 93.03 -174.32
REMARK 500 LEU Q 10 -40.43 -175.85
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 GLY Q 2 ARG Q 3 -143.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X0J RELATED DB: PDB
REMARK 900 NATIVE
REMARK 900 RELATED ID: 2DVR RELATED DB: PDB
REMARK 900 RELATED ID: 2DVS RELATED DB: PDB
REMARK 900 RELATED ID: AR_001000221.4 RELATED DB: TARGETDB
DBREF 2DVQ A 73 194 UNP P25440 BRD2_HUMAN 73 194
DBREF 2DVQ B 73 194 UNP P25440 BRD2_HUMAN 73 194
DBREF 2DVQ C 73 194 UNP P25440 BRD2_HUMAN 73 194
DBREF 2DVQ P 1 15 PDB 2DVQ 2DVQ 1 15
DBREF 2DVQ Q 1 15 PDB 2DVQ 2DVQ 1 15
SEQADV 2DVQ MSE A 87 UNP P25440 MET 87 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 121 UNP P25440 MET 121 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 123 UNP P25440 MET 123 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 142 UNP P25440 MET 142 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 148 UNP P25440 MET 148 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 165 UNP P25440 MET 165 MODIFIED RESIDUE
SEQADV 2DVQ MSE A 180 UNP P25440 MET 180 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 87 UNP P25440 MET 87 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 121 UNP P25440 MET 121 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 123 UNP P25440 MET 123 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 142 UNP P25440 MET 142 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 148 UNP P25440 MET 148 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 165 UNP P25440 MET 165 MODIFIED RESIDUE
SEQADV 2DVQ MSE B 180 UNP P25440 MET 180 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 87 UNP P25440 MET 87 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 121 UNP P25440 MET 121 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 123 UNP P25440 MET 123 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 142 UNP P25440 MET 142 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 148 UNP P25440 MET 148 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 165 UNP P25440 MET 165 MODIFIED RESIDUE
SEQADV 2DVQ MSE C 180 UNP P25440 MET 180 MODIFIED RESIDUE
SEQRES 1 A 122 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 2 A 122 VAL MSE LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 A 122 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 4 A 122 ASP TYR HIS LYS ILE ILE LYS GLN PRO MSE ASP MSE GLY
SEQRES 5 A 122 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 6 A 122 ALA SER GLU CYS MSE GLN ASP PHE ASN THR MSE PHE THR
SEQRES 7 A 122 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 8 A 122 LEU MSE ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 9 A 122 VAL ALA SER MSE PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 10 A 122 THR ILE PRO LYS ASN
SEQRES 1 B 122 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 2 B 122 VAL MSE LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 B 122 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 4 B 122 ASP TYR HIS LYS ILE ILE LYS GLN PRO MSE ASP MSE GLY
SEQRES 5 B 122 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 6 B 122 ALA SER GLU CYS MSE GLN ASP PHE ASN THR MSE PHE THR
SEQRES 7 B 122 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 8 B 122 LEU MSE ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 9 B 122 VAL ALA SER MSE PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 10 B 122 THR ILE PRO LYS ASN
SEQRES 1 C 122 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 2 C 122 VAL MSE LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 C 122 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 4 C 122 ASP TYR HIS LYS ILE ILE LYS GLN PRO MSE ASP MSE GLY
SEQRES 5 C 122 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 6 C 122 ALA SER GLU CYS MSE GLN ASP PHE ASN THR MSE PHE THR
SEQRES 7 C 122 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 8 C 122 LEU MSE ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 9 C 122 VAL ALA SER MSE PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 10 C 122 THR ILE PRO LYS ASN
SEQRES 1 P 15 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY ALY GLY
SEQRES 2 P 15 GLY ALA
SEQRES 1 Q 15 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY ALY GLY
SEQRES 2 Q 15 GLY ALA
MODRES 2DVQ MSE A 87 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 121 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 123 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 142 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 148 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 165 MET SELENOMETHIONINE
MODRES 2DVQ MSE A 180 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 87 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 121 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 123 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 142 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 148 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 165 MET SELENOMETHIONINE
MODRES 2DVQ MSE B 180 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 87 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 121 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 123 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 142 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 148 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 165 MET SELENOMETHIONINE
MODRES 2DVQ MSE C 180 MET SELENOMETHIONINE
MODRES 2DVQ ALY P 12 LYS N(6)-ACETYLLYSINE
MODRES 2DVQ ALY Q 12 LYS N(6)-ACETYLLYSINE
HET MSE A 87 8
HET MSE A 121 8
HET MSE A 123 8
HET MSE A 142 8
HET MSE A 148 8
HET MSE A 165 8
HET MSE A 180 8
HET MSE B 87 8
HET MSE B 121 8
HET MSE B 123 8
HET MSE B 142 8
HET MSE B 148 8
HET MSE B 165 8
HET MSE B 180 8
HET MSE C 87 8
HET MSE C 121 8
HET MSE C 123 8
HET MSE C 142 8
HET MSE C 148 8
HET MSE C 165 8
HET MSE C 180 8
HET ALY P 12 12
HET ALY Q 12 12
HETNAM MSE SELENOMETHIONINE
HETNAM ALY N(6)-ACETYLLYSINE
FORMUL 1 MSE 21(C5 H11 N O2 SE)
FORMUL 4 ALY 2(C8 H16 N2 O3)
FORMUL 6 HOH *250(H2 O)
HELIX 1 1 THR A 76 VAL A 85 1 10
HELIX 2 2 VAL A 85 LYS A 92 1 8
HELIX 3 3 ALA A 96 ARG A 100 5 5
HELIX 4 4 ASP A 104 GLY A 109 1 6
HELIX 5 5 ASP A 112 ILE A 117 1 6
HELIX 6 6 ASP A 122 ASN A 132 1 11
HELIX 7 7 ALA A 137 ASN A 156 1 20
HELIX 8 8 ASP A 160 SER A 179 1 20
HELIX 9 9 THR B 76 VAL B 85 1 10
HELIX 10 10 VAL B 85 LYS B 92 1 8
HELIX 11 11 ALA B 96 ARG B 100 5 5
HELIX 12 12 ASP B 104 GLY B 109 1 6
HELIX 13 13 ASP B 112 ILE B 117 1 6
HELIX 14 14 ASP B 122 ASN B 132 1 11
HELIX 15 15 ALA B 137 ASN B 156 1 20
HELIX 16 16 ASP B 160 ALA B 178 1 19
HELIX 17 17 THR C 76 VAL C 85 1 10
HELIX 18 18 VAL C 85 HIS C 93 1 9
HELIX 19 19 GLN C 94 ARG C 100 5 7
HELIX 20 20 ASP C 112 ILE C 117 1 6
HELIX 21 21 ASP C 122 ASN C 132 1 11
HELIX 22 22 ALA C 137 ASN C 156 1 20
HELIX 23 23 ASP C 160 SER C 179 1 20
LINK C VAL A 86 N MSE A 87 1555 1555 1.33
LINK C MSE A 87 N LYS A 88 1555 1555 1.34
LINK C PRO A 120 N MSE A 121 1555 1555 1.33
LINK C MSE A 121 N ASP A 122 1555 1555 1.33
LINK C ASP A 122 N MSE A 123 1555 1555 1.33
LINK C MSE A 123 N GLY A 124 1555 1555 1.33
LINK C CYS A 141 N MSE A 142 1555 1555 1.32
LINK C MSE A 142 N GLN A 143 1555 1555 1.33
LINK C THR A 147 N MSE A 148 1555 1555 1.34
LINK C MSE A 148 N PHE A 149 1555 1555 1.33
LINK C LEU A 164 N MSE A 165 1555 1555 1.31
LINK C MSE A 165 N ALA A 166 1555 1555 1.33
LINK C SER A 179 N MSE A 180 1555 1555 1.33
LINK C MSE A 180 N PRO A 181 1555 1555 1.34
LINK C VAL B 86 N MSE B 87 1555 1555 1.33
LINK C MSE B 87 N LYS B 88 1555 1555 1.33
LINK C PRO B 120 N MSE B 121 1555 1555 1.33
LINK C MSE B 121 N ASP B 122 1555 1555 1.33
LINK C ASP B 122 N MSE B 123 1555 1555 1.35
LINK C MSE B 123 N GLY B 124 1555 1555 1.33
LINK C CYS B 141 N MSE B 142 1555 1555 1.32
LINK C MSE B 142 N GLN B 143 1555 1555 1.33
LINK C THR B 147 N MSE B 148 1555 1555 1.33
LINK C MSE B 148 N PHE B 149 1555 1555 1.34
LINK C LEU B 164 N MSE B 165 1555 1555 1.33
LINK C MSE B 165 N ALA B 166 1555 1555 1.34
LINK C SER B 179 N MSE B 180 1555 1555 1.32
LINK C MSE B 180 N PRO B 181 1555 1555 1.34
LINK C VAL C 86 N MSE C 87 1555 1555 1.34
LINK C MSE C 87 N LYS C 88 1555 1555 1.34
LINK C PRO C 120 N MSE C 121 1555 1555 1.33
LINK C MSE C 121 N ASP C 122 1555 1555 1.32
LINK C ASP C 122 N MSE C 123 1555 1555 1.34
LINK C MSE C 123 N GLY C 124 1555 1555 1.33
LINK C CYS C 141 N MSE C 142 1555 1555 1.32
LINK C MSE C 142 N GLN C 143 1555 1555 1.33
LINK C THR C 147 N MSE C 148 1555 1555 1.32
LINK C MSE C 148 N PHE C 149 1555 1555 1.33
LINK C LEU C 164 N MSE C 165 1555 1555 1.33
LINK C MSE C 165 N ALA C 166 1555 1555 1.34
LINK C SER C 179 N MSE C 180 1555 1555 1.32
LINK C MSE C 180 N PRO C 181 1555 1555 1.34
LINK C GLY P 11 N ALY P 12 1555 1555 1.32
LINK C ALY P 12 N GLY P 13 1555 1555 1.33
LINK C GLY Q 11 N ALY Q 12 1555 1555 1.33
LINK C ALY Q 12 N GLY Q 13 1555 1555 1.34
CISPEP 1 GLY P 14 ALA P 15 0 3.37
CISPEP 2 SER Q 1 GLY Q 2 0 -14.85
CRYST1 113.811 55.143 67.489 90.00 94.06 90.00 C 1 2 1 12
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 0.008786 0.000000 0.000624 0.00000
SCALE2 0.000000 0.018135 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014855 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
