HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 17-SEP-13 4MR5
TITLE CRYSTAL STRUCTURE OF THE SECOND BROMODOMAIN OF HUMAN BRD2 IN COMPLEX
TITLE 2 WITH A QUINAZOLINONE LIGAND (RVX-OH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 344-455;
COMPND 5 SYNONYM: O27.1.1, REALLY INTERESTING NEW GENE 3 PROTEIN;
COMPND 6 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: BRD2, KIAA9001, RING3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BRD2, RING3, SMALL MOLECULE INHIBITOR, RVX-OH, INHIBITOR COMPLEX,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSCRIPTION-TRANSCRIPTION
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,S.MARTIN,O.FEDOROV,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 3 28-FEB-24 4MR5 1 REMARK SEQADV
REVDAT 2 22-JAN-14 4MR5 1 JRNL
REVDAT 1 27-NOV-13 4MR5 0
JRNL AUTH S.PICAUD,C.WELLS,I.FELLETAR,D.BROTHERTON,S.MARTIN,
JRNL AUTH 2 P.SAVITSKY,B.DIEZ-DACAL,M.PHILPOTT,C.BOUNTRA,H.LINGARD,
JRNL AUTH 3 O.FEDOROV,S.MULLER,P.E.BRENNAN,S.KNAPP,P.FILIPPAKOPOULOS
JRNL TITL RVX-208, AN INHIBITOR OF BET TRANSCRIPTIONAL REGULATORS WITH
JRNL TITL 2 SELECTIVITY FOR THE SECOND BROMODOMAIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 19754 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 24248379
JRNL DOI 10.1073/PNAS.1310658110
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 15580
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) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 780
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1012
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.1500
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.1950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 910
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : -0.48000
REMARK 3 B33 (A**2) : 0.40000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.532
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 976 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 927 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1309 ; 1.626 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2128 ; 0.863 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 109 ; 5.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;33.242 ;23.542
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 167 ;11.487 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;27.847 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 129 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1172 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 230 ; 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): 439 ; 2.745 ; 1.397
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 440 ; 2.747 ; 1.407
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 547 ; 2.968 ; 2.566
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 346 A 455
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3254 2.6082 16.9172
REMARK 3 T TENSOR
REMARK 3 T11: 0.0387 T22: 0.0384
REMARK 3 T33: 0.0308 T12: 0.0018
REMARK 3 T13: -0.0025 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2470 L22: 0.6253
REMARK 3 L33: 0.0304 L12: 0.0334
REMARK 3 L13: 0.0519 L23: -0.1005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0210 S12: -0.0080 S13: -0.0089
REMARK 3 S21: -0.0178 S22: 0.0271 S23: -0.0048
REMARK 3 S31: -0.0009 S32: -0.0033 S33: -0.0061
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4MR5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.52
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 19.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : 0.03800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : 0.17000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M NA(FORMATE), 0.1M BTPROP, 20.0%
REMARK 280 PEG 3350 10.0% ETGLY, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 26.11000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.00400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.11000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.00400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 A 741 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 SER A 342
REMARK 465 MET A 343
REMARK 465 GLY A 344
REMARK 465 LYS A 345
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 347 O HOH A 735 2.11
REMARK 500 O HOH A 675 O HOH A 682 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 A 740 O HOH A 740 2655 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1K0 A 506
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1K0 A 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MR3 RELATED DB: PDB
REMARK 900 RELATED ID: 4MR4 RELATED DB: PDB
REMARK 900 RELATED ID: 4MR6 RELATED DB: PDB
DBREF 4MR5 A 344 455 UNP P25440 BRD2_HUMAN 344 455
SEQADV 4MR5 SER A 342 UNP P25440 EXPRESSION TAG
SEQADV 4MR5 MET A 343 UNP P25440 EXPRESSION TAG
SEQRES 1 A 114 SER MET GLY LYS LEU SER GLU GLN LEU LYS HIS CYS ASN
SEQRES 2 A 114 GLY ILE LEU LYS GLU LEU LEU SER LYS LYS HIS ALA ALA
SEQRES 3 A 114 TYR ALA TRP PRO PHE TYR LYS PRO VAL ASP ALA SER ALA
SEQRES 4 A 114 LEU GLY LEU HIS ASP TYR HIS ASP ILE ILE LYS HIS PRO
SEQRES 5 A 114 MET ASP LEU SER THR VAL LYS ARG LYS MET GLU ASN ARG
SEQRES 6 A 114 ASP TYR ARG ASP ALA GLN GLU PHE ALA ALA ASP VAL ARG
SEQRES 7 A 114 LEU MET PHE SER ASN CYS TYR LYS TYR ASN PRO PRO ASP
SEQRES 8 A 114 HIS ASP VAL VAL ALA MET ALA ARG LYS LEU GLN ASP VAL
SEQRES 9 A 114 PHE GLU PHE ARG TYR ALA LYS MET PRO ASP
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET DMS A 505 4
HET 1K0 A 506 24
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 1K0 2-[4-(2-HYDROXYETHOXY)-3,5-DIMETHYLPHENYL]-5,7-
HETNAM 2 1K0 DIMETHOXYQUINAZOLIN-4(3H)-ONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 DMS C2 H6 O S
FORMUL 7 1K0 C20 H22 N2 O5
FORMUL 8 HOH *141(H2 O)
HELIX 1 1 LEU A 346 LEU A 361 1 16
HELIX 2 2 SER A 362 LYS A 364 5 3
HELIX 3 3 HIS A 365 TRP A 370 1 6
HELIX 4 4 PRO A 371 TYR A 373 5 3
HELIX 5 5 ASP A 377 GLY A 382 1 6
HELIX 6 6 ASP A 385 ILE A 390 1 6
HELIX 7 7 ASP A 395 ASN A 405 1 11
HELIX 8 8 ASP A 410 ASN A 429 1 20
HELIX 9 9 HIS A 433 ALA A 451 1 19
SITE 1 AC1 6 TYR A 368 LYS A 402 ASP A 407 MET A 438
SITE 2 AC1 6 LYS A 441 HOH A 626
SITE 1 AC2 5 TYR A 426 ARG A 440 GLN A 443 ASP A 444
SITE 2 AC2 5 HOH A 657
SITE 1 AC3 2 ASP A 385 TYR A 428
SITE 1 AC4 7 ILE A 389 ILE A 390 LYS A 391 HIS A 392
SITE 2 AC4 7 ASN A 424 LYS A 427 ASP A 455
SITE 1 AC5 5 TRP A 370 HIS A 433 HOH A 691 HOH A 694
SITE 2 AC5 5 HOH A 695
SITE 1 AC6 11 LYS A 351 TRP A 370 PRO A 371 PHE A 372
SITE 2 AC6 11 VAL A 376 LEU A 381 LEU A 383 ASN A 429
SITE 3 AC6 11 HIS A 433 HOH A 604 HOH A 691
CRYST1 52.220 72.008 32.039 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.031212 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
