HEADER SIGNALING PROTEIN 25-MAR-11 2YEM
TITLE CRYSTAL STRUCTURE OF THE SECOND BROMODOMAIN OF HUMAN BRD4 WITH THE
TITLE 2 INHIBITOR GW841819X
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL BROMODOMAIN, RESIDUES 333-460;
COMPND 5 SYNONYM: PROTEIN HUNK1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SIGNALING PROTEIN, HISTONE, EPIGENETIC READER
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.CHUNG
REVDAT 4 20-DEC-23 2YEM 1 REMARK
REVDAT 3 21-AUG-19 2YEM 1 REMARK
REVDAT 2 08-MAY-13 2YEM 1 COMPND
REVDAT 1 15-JUN-11 2YEM 0
JRNL AUTH C.W.CHUNG,H.COSTE,J.H.WHITE,O.MIRGUET,J.WILDE,R.L.GOSMINI,
JRNL AUTH 2 C.DELVES,S.M.MAGNY,R.WOODWARD,S.A.HUGHES,E.V.BOURSIER,
JRNL AUTH 3 H.FLYNN,A.M.BOUILLOT,P.BAMBOROUGH,J.M.BRUSQ,F.J.GELLIBERT,
JRNL AUTH 4 E.J.JONES,A.M.RIOU,P.HOMES,S.L.MARTIN,I.J.UINGS,J.TOUM,
JRNL AUTH 5 C.A.CLEMENT,A.B.BOULLAY,R.L.GRIMLEY,F.M.BLANDEL,R.K.PRINJHA,
JRNL AUTH 6 K.LEE,J.KIRILOVSKY,E.NICODEME
JRNL TITL DISCOVERY AND CHARACTERIZATION OF SMALL MOLECULE INHIBITORS
JRNL TITL 2 OF THE BET FAMILY BROMODOMAINS.
JRNL REF J.MED.CHEM. V. 54 3827 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21568322
JRNL DOI 10.1021/JM200108T
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 14004
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 745
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 998
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1802
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.13000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -2.23000
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): 0.250
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.205
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.062
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1966 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1386 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2652 ; 1.081 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3363 ; 0.820 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 231 ; 4.524 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;31.148 ;23.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;15.899 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.170 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 261 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2269 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 452 ; 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): 1136 ; 0.721 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 443 ; 0.090 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1833 ; 1.435 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 830 ; 1.792 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 816 ; 2.756 ; 6.000
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 : 2
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 349 A 458
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7633 6.4512 -24.0448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0138 T22: 0.0439
REMARK 3 T33: 0.0833 T12: -0.0109
REMARK 3 T13: 0.0005 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.7726 L22: 3.5029
REMARK 3 L33: 3.1457 L12: -0.1314
REMARK 3 L13: 0.2766 L23: 0.0924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: -0.0586 S13: 0.0249
REMARK 3 S21: 0.0114 S22: 0.0895 S23: -0.0672
REMARK 3 S31: -0.1683 S32: 0.1675 S33: -0.0280
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 349 B 459
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9962 3.6294 -45.0215
REMARK 3 T TENSOR
REMARK 3 T11: 0.0320 T22: 0.1269
REMARK 3 T33: 0.0375 T12: -0.0376
REMARK 3 T13: 0.0259 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 3.6045 L22: 2.8329
REMARK 3 L33: 4.9280 L12: -1.2955
REMARK 3 L13: 2.4160 L23: -1.5470
REMARK 3 S TENSOR
REMARK 3 S11: -0.1143 S12: 0.2679 S13: 0.0460
REMARK 3 S21: -0.1892 S22: 0.0090 S23: -0.2127
REMARK 3 S31: -0.0754 S32: 0.6317 S33: 0.1053
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2YEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1290047844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 73.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OUO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M (NH4)2SO4, 0.1 M TRIS PH 8.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.83700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.18100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.74600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.18100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.83700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.74600
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 331
REMARK 465 MET A 332
REMARK 465 LYS A 333
REMARK 465 ASP A 334
REMARK 465 VAL A 335
REMARK 465 PRO A 336
REMARK 465 ASP A 337
REMARK 465 SER A 338
REMARK 465 GLN A 339
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 PRO A 342
REMARK 465 ALA A 343
REMARK 465 PRO A 344
REMARK 465 GLU A 345
REMARK 465 LYS A 346
REMARK 465 SER A 347
REMARK 465 SER A 348
REMARK 465 ASP A 459
REMARK 465 GLU A 460
REMARK 465 SER B 331
REMARK 465 MET B 332
REMARK 465 LYS B 333
REMARK 465 ASP B 334
REMARK 465 VAL B 335
REMARK 465 PRO B 336
REMARK 465 ASP B 337
REMARK 465 SER B 338
REMARK 465 GLN B 339
REMARK 465 GLN B 340
REMARK 465 HIS B 341
REMARK 465 PRO B 342
REMARK 465 ALA B 343
REMARK 465 PRO B 344
REMARK 465 GLU B 345
REMARK 465 LYS B 346
REMARK 465 SER B 347
REMARK 465 SER B 348
REMARK 465 GLU B 460
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WSH A 1459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WSH B 1460
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YEL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 WITH THE
REMARK 900 INHIBITOR GW841819X
REMARK 900 RELATED ID: 2YEK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD2 WITH THE
REMARK 900 INHIBITOR GSK525762 (IBET)
DBREF 2YEM A 333 460 UNP O60885 BRD4_HUMAN 333 460
DBREF 2YEM B 333 460 UNP O60885 BRD4_HUMAN 333 460
SEQADV 2YEM SER A 331 UNP O60885 EXPRESSION TAG
SEQADV 2YEM MET A 332 UNP O60885 EXPRESSION TAG
SEQADV 2YEM SER B 331 UNP O60885 EXPRESSION TAG
SEQADV 2YEM MET B 332 UNP O60885 EXPRESSION TAG
SEQRES 1 A 130 SER MET LYS ASP VAL PRO ASP SER GLN GLN HIS PRO ALA
SEQRES 2 A 130 PRO GLU LYS SER SER LYS VAL SER GLU GLN LEU LYS CYS
SEQRES 3 A 130 CYS SER GLY ILE LEU LYS GLU MET PHE ALA LYS LYS HIS
SEQRES 4 A 130 ALA ALA TYR ALA TRP PRO PHE TYR LYS PRO VAL ASP VAL
SEQRES 5 A 130 GLU ALA LEU GLY LEU HIS ASP TYR CYS ASP ILE ILE LYS
SEQRES 6 A 130 HIS PRO MET ASP MET SER THR ILE LYS SER LYS LEU GLU
SEQRES 7 A 130 ALA ARG GLU TYR ARG ASP ALA GLN GLU PHE GLY ALA ASP
SEQRES 8 A 130 VAL ARG LEU MET PHE SER ASN CYS TYR LYS TYR ASN PRO
SEQRES 9 A 130 PRO ASP HIS GLU VAL VAL ALA MET ALA ARG LYS LEU GLN
SEQRES 10 A 130 ASP VAL PHE GLU MET ARG PHE ALA LYS MET PRO ASP GLU
SEQRES 1 B 130 SER MET LYS ASP VAL PRO ASP SER GLN GLN HIS PRO ALA
SEQRES 2 B 130 PRO GLU LYS SER SER LYS VAL SER GLU GLN LEU LYS CYS
SEQRES 3 B 130 CYS SER GLY ILE LEU LYS GLU MET PHE ALA LYS LYS HIS
SEQRES 4 B 130 ALA ALA TYR ALA TRP PRO PHE TYR LYS PRO VAL ASP VAL
SEQRES 5 B 130 GLU ALA LEU GLY LEU HIS ASP TYR CYS ASP ILE ILE LYS
SEQRES 6 B 130 HIS PRO MET ASP MET SER THR ILE LYS SER LYS LEU GLU
SEQRES 7 B 130 ALA ARG GLU TYR ARG ASP ALA GLN GLU PHE GLY ALA ASP
SEQRES 8 B 130 VAL ARG LEU MET PHE SER ASN CYS TYR LYS TYR ASN PRO
SEQRES 9 B 130 PRO ASP HIS GLU VAL VAL ALA MET ALA ARG LYS LEU GLN
SEQRES 10 B 130 ASP VAL PHE GLU MET ARG PHE ALA LYS MET PRO ASP GLU
HET WSH A1459 32
HET WSH B1460 32
HETNAM WSH BENZYL [(4R)-1-METHYL-6-PHENYL-4H-[1,2,4]TRIAZOLO[4,3-
HETNAM 2 WSH A][1,4]BENZODIAZEPIN-4-YL]CARBAMATE
FORMUL 3 WSH 2(C25 H21 N5 O2)
FORMUL 5 HOH *133(H2 O)
HELIX 1 1 LYS A 349 PHE A 365 1 17
HELIX 2 2 ALA A 366 LYS A 368 5 3
HELIX 3 3 HIS A 369 TRP A 374 1 6
HELIX 4 4 PRO A 375 TYR A 377 5 3
HELIX 5 5 ASP A 381 GLY A 386 1 6
HELIX 6 6 ASP A 389 ILE A 394 1 6
HELIX 7 7 ASP A 399 ALA A 409 1 11
HELIX 8 8 ASP A 414 ASN A 433 1 20
HELIX 9 9 HIS A 437 LYS A 456 1 20
HELIX 10 10 LYS B 349 PHE B 365 1 17
HELIX 11 11 ALA B 366 LYS B 368 5 3
HELIX 12 12 HIS B 369 TRP B 374 1 6
HELIX 13 13 PRO B 375 TYR B 377 5 3
HELIX 14 14 ASP B 381 GLY B 386 1 6
HELIX 15 15 ASP B 389 ILE B 394 1 6
HELIX 16 16 ASP B 399 ALA B 409 1 11
HELIX 17 17 ASP B 414 ASN B 433 1 20
HELIX 18 18 HIS B 437 LYS B 456 1 20
SITE 1 AC1 7 PRO A 375 ARG A 413 ASN A 433 VAL A 439
SITE 2 AC1 7 HOH A2034 HOH A2067 WSH B1460
SITE 1 AC2 10 TRP A 374 WSH A1459 TRP B 374 PRO B 375
SITE 2 AC2 10 LEU B 387 ASN B 433 HIS B 437 GLU B 438
SITE 3 AC2 10 VAL B 439 HOH B2021
CRYST1 59.674 73.492 74.362 90.00 90.00 90.00 P 21 21 21 8
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 0.016758 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013607 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013448 0.00000
(ATOM LINES ARE NOT SHOWN.)
END