HEADER SIGNALING PROTEIN/INHIBITOR 11-OCT-11 3U5K
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH MIDAZOLAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PROTEIN HUNK1;
COMPND 5 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: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BROMODOMAIN-CONTAINING PROTEIN 4 ISOFORM LONG, BRD4, BROMODOMAIN
KEYWDS 2 CONTAINING PROTEIN 4, CAP, HUNK1, MCAP, MITOTIC CHROMOSOME
KEYWDS 3 ASSOCIATED PROTEIN, STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNALING
KEYWDS 4 PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,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 4 13-SEP-23 3U5K 1 REMARK SEQADV
REVDAT 3 21-MAR-12 3U5K 1 JRNL
REVDAT 2 07-MAR-12 3U5K 1 JRNL
REVDAT 1 23-NOV-11 3U5K 0
JRNL AUTH P.FILIPPAKOPOULOS,S.PICAUD,O.FEDOROV,M.KELLER,M.WROBEL,
JRNL AUTH 2 O.MORGENSTERN,F.BRACHER,S.KNAPP
JRNL TITL BENZODIAZEPINES AND BENZOTRIAZEPINES AS PROTEIN INTERACTION
JRNL TITL 2 INHIBITORS TARGETING BROMODOMAINS OF THE BET FAMILY.
JRNL REF BIOORG.MED.CHEM. V. 20 1878 2012
JRNL REFN ISSN 0968-0896
JRNL PMID 22137933
JRNL DOI 10.1016/J.BMC.2011.10.080
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 51217
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1921
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3088
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.4340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4035
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -0.76000
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): 0.030
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.613
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4278 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2876 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5848 ; 1.640 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7023 ; 1.011 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 491 ; 6.135 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;34.941 ;25.344
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 713 ;15.961 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.955 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 624 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4624 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 772 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.505
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.495
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 42 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): 79.4670 8.8604 11.4359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.1021
REMARK 3 T33: 0.1445 T12: 0.0048
REMARK 3 T13: 0.0125 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.1470 L22: 0.5590
REMARK 3 L33: 0.1032 L12: 0.2349
REMARK 3 L13: -0.0830 L23: -0.0570
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: 0.0415 S13: 0.0050
REMARK 3 S21: 0.0448 S22: 0.0320 S23: 0.0076
REMARK 3 S31: 0.0042 S32: -0.0004 S33: -0.0289
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 43 B 166
REMARK 3 ORIGIN FOR THE GROUP (A): 86.9520 39.2403 -1.8961
REMARK 3 T TENSOR
REMARK 3 T11: 0.1017 T22: 0.1192
REMARK 3 T33: 0.1251 T12: 0.0141
REMARK 3 T13: 0.0089 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.4530 L22: 0.3778
REMARK 3 L33: 0.0280 L12: -0.0621
REMARK 3 L13: 0.0581 L23: 0.0329
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.0260 S13: 0.0081
REMARK 3 S21: 0.0299 S22: 0.0536 S23: 0.0198
REMARK 3 S31: -0.0146 S32: -0.0055 S33: -0.0379
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 43 C 165
REMARK 3 ORIGIN FOR THE GROUP (A): 65.1478 25.3132 32.9712
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.1061
REMARK 3 T33: 0.1332 T12: -0.0169
REMARK 3 T13: 0.0171 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.3760 L22: 0.4689
REMARK 3 L33: 0.2669 L12: -0.2074
REMARK 3 L13: -0.0171 L23: -0.2923
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.0501 S13: 0.0131
REMARK 3 S21: -0.0772 S22: 0.0526 S23: 0.0216
REMARK 3 S31: 0.0538 S32: -0.0362 S33: -0.0538
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 42 D 167
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4514 46.8087 11.4293
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.0906
REMARK 3 T33: 0.1529 T12: -0.0181
REMARK 3 T13: 0.0159 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.3897 L22: 0.4822
REMARK 3 L33: 0.0968 L12: -0.4151
REMARK 3 L13: -0.1865 L23: 0.2034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: -0.0339 S13: 0.0118
REMARK 3 S21: -0.0472 S22: -0.0235 S23: -0.0220
REMARK 3 S31: -0.0321 S32: 0.0082 S33: -0.0414
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS; U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3U5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51230
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 26.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : 0.52200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 2OSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 0.1M MGCL, 15% PEG
REMARK 280 6000, 10% ETGLY, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,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 21.47033
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 42.94067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: 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
REMARK 350 BIOMOLECULE: 3
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: 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
REMARK 350 BIOMOLECULE: 4
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: D
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 GLU A 168
REMARK 465 SER B 42
REMARK 465 GLU B 167
REMARK 465 GLU B 168
REMARK 465 SER C 42
REMARK 465 THR C 166
REMARK 465 GLU C 167
REMARK 465 GLU C 168
REMARK 465 ASN D 54
REMARK 465 LYS D 55
REMARK 465 PRO D 56
REMARK 465 GLU D 168
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 163 CG CD OE1 OE2
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 LYS B 76 CD CE NZ
REMARK 470 GLU C 49 CG CD OE1 OE2
REMARK 470 ASN C 52 CG OD1 ND2
REMARK 470 ASN C 54 CG OD1 ND2
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 GLN C 59 CG CD OE1 NE2
REMARK 470 ASN C 61 CG OD1 ND2
REMARK 470 GLN C 62 CD OE1 NE2
REMARK 470 LYS C 76 CG CD CE NZ
REMARK 470 LYS C 112 CG CD CE NZ
REMARK 470 GLU C 124 CD OE1 OE2
REMARK 470 GLU C 151 CD OE1 OE2
REMARK 470 ASN C 162 CG OD1 ND2
REMARK 470 GLU C 163 CG CD OE1 OE2
REMARK 470 LEU C 164 CG CD1 CD2
REMARK 470 SER D 42 OG
REMARK 470 GLU D 49 CG CD OE1 OE2
REMARK 470 SER D 51 OG
REMARK 470 ASN D 52 CG OD1 ND2
REMARK 470 LYS D 57 CG CD CE NZ
REMARK 470 GLN D 59 CG CD OE1 NE2
REMARK 470 ASN D 61 CG OD1 ND2
REMARK 470 GLN D 62 CG CD OE1 NE2
REMARK 470 LYS D 76 NZ
REMARK 470 LYS D 91 CE NZ
REMARK 470 LYS D 155 CD CE NZ
REMARK 470 GLN D 159 CD OE1 NE2
REMARK 470 LYS D 160 CE NZ
REMARK 470 ASN D 162 CG OD1 ND2
REMARK 470 GLU D 163 CG CD OE1 OE2
REMARK 470 LEU D 164 CG CD1 CD2
REMARK 470 GLU D 167 CG CD OE1 OE2
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 O HOH B 193 O HOH B 214 2.02
REMARK 500 NE2 GLN A 159 O HOH A 178 2.12
REMARK 500 OD1 ASP C 144 O HOH C 213 2.15
REMARK 500 OE1 GLN D 85 O HOH D 179 2.16
REMARK 500 OG1 THR C 109 O HOH C 197 2.19
REMARK 500 O HOH B 179 O HOH B 210 2.19
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 VAL A 69 -62.99 -127.02
REMARK 500 ASN B 52 105.80 -166.15
REMARK 500 VAL B 69 -50.71 -122.64
REMARK 500 LEU B 94 76.84 -113.75
REMARK 500 ASP B 145 -55.24 -24.88
REMARK 500 ASN B 162 -38.89 -31.73
REMARK 500 ASN D 52 107.58 -160.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J D 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U5J RELATED DB: PDB
REMARK 900 RELATED ID: 3U5L RELATED DB: PDB
DBREF 3U5K A 42 168 UNP O60885 BRD4_HUMAN 42 168
DBREF 3U5K B 42 168 UNP O60885 BRD4_HUMAN 42 168
DBREF 3U5K C 42 168 UNP O60885 BRD4_HUMAN 42 168
DBREF 3U5K D 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQADV 3U5K MET A 43 UNP O60885 THR 43 CLONING ARTIFACT
SEQADV 3U5K MET B 43 UNP O60885 THR 43 CLONING ARTIFACT
SEQADV 3U5K MET C 43 UNP O60885 THR 43 CLONING ARTIFACT
SEQADV 3U5K MET D 43 UNP O60885 THR 43 CLONING ARTIFACT
SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 B 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 B 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 B 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 B 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 B 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 B 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 B 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 B 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 B 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 B 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 C 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 C 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 C 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 C 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 C 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 C 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 C 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 C 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 C 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 C 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 D 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 D 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 D 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 D 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 D 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 D 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 D 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 D 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 D 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 D 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET 08J A 1 23
HET 08J B 2 23
HET 08J C 3 23
HET 08J D 4 23
HETNAM 08J 8-CHLORO-6-(2-FLUOROPHENYL)-1-METHYL-4H-IMIDAZO[1,5-
HETNAM 2 08J A][1,4]BENZODIAZEPINE
HETSYN 08J MIDAZOLAM
FORMUL 5 08J 4(C18 H13 CL F N3)
FORMUL 9 HOH *231(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 LYS A 76 1 8
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 96 ILE A 101 1 6
HELIX 5 5 ASP A 106 ASN A 116 1 11
HELIX 6 6 ASN A 121 ASN A 140 1 20
HELIX 7 7 ASP A 144 ILE A 161 1 18
HELIX 8 8 ASN A 162 LEU A 164 5 3
HELIX 9 9 THR B 60 VAL B 69 1 10
HELIX 10 10 VAL B 69 LYS B 76 1 8
HELIX 11 11 ALA B 80 GLN B 84 5 5
HELIX 12 12 ASP B 96 ILE B 101 1 6
HELIX 13 13 ASP B 106 ASN B 116 1 11
HELIX 14 14 ASN B 121 ASN B 140 1 20
HELIX 15 15 ASP B 144 ASN B 162 1 19
HELIX 16 16 THR C 60 VAL C 69 1 10
HELIX 17 17 VAL C 69 LYS C 76 1 8
HELIX 18 18 ALA C 80 GLN C 84 5 5
HELIX 19 19 ASP C 96 ILE C 101 1 6
HELIX 20 20 ASP C 106 ASN C 116 1 11
HELIX 21 21 ASN C 121 ASN C 140 1 20
HELIX 22 22 ASP C 144 ILE C 161 1 18
HELIX 23 23 THR D 60 VAL D 69 1 10
HELIX 24 24 VAL D 69 LYS D 76 1 8
HELIX 25 25 ALA D 80 GLN D 84 5 5
HELIX 26 26 ASP D 96 ILE D 101 1 6
HELIX 27 27 ASP D 106 ASN D 116 1 11
HELIX 28 28 ASN D 121 ASN D 140 1 20
HELIX 29 29 ASP D 144 GLU D 163 1 20
SITE 1 AC1 10 HOH A 5 TRP A 81 PRO A 82 VAL A 87
SITE 2 AC1 10 LEU A 92 LEU A 94 ASN A 140 ILE A 146
SITE 3 AC1 10 HOH A 169 HOH A 187
SITE 1 AC2 9 TRP B 81 PRO B 82 LEU B 92 LEU B 94
SITE 2 AC2 9 ASN B 140 ILE B 146 HOH B 169 HOH B 231
SITE 3 AC2 9 HOH B 232
SITE 1 AC3 9 HOH C 28 TRP C 81 PRO C 82 VAL C 87
SITE 2 AC3 9 LEU C 92 ASN C 140 ILE C 146 MET C 149
SITE 3 AC3 9 HOH C 199
SITE 1 AC4 8 TRP D 81 PRO D 82 PHE D 83 LEU D 92
SITE 2 AC4 8 LEU D 94 ASN D 140 ILE D 146 MET D 149
CRYST1 89.550 89.550 64.411 90.00 90.00 120.00 P 31 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 0.011167 0.006447 0.000000 0.00000
SCALE2 0.000000 0.012895 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015525 0.00000
(ATOM LINES ARE NOT SHOWN.)
END