HEADER TRANSCRIPTION 27-MAR-15 4Z1Q
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 BOUND TO
TITLE 2 BENZOTRIAZOLO-DIAZEPINE SCAFFOLD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
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
KEYWDS BROMODOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SETSER,F.POY,Y.TANG,S.F.BELLON
REVDAT 3 06-MAR-24 4Z1Q 1 REMARK
REVDAT 2 30-MAR-16 4Z1Q 1 JRNL
REVDAT 1 08-APR-15 4Z1Q 0
JRNL AUTH A.M.TAYLOR,R.G.VASWANI,V.S.GEHLING,M.C.HEWITT,Y.LEBLANC,
JRNL AUTH 2 J.E.AUDIA,S.BELLON,R.T.CUMMINGS,A.COTE,J.C.HARMANGE,
JRNL AUTH 3 H.JAYARAM,S.JOSHI,J.M.LORA,J.A.MERTZ,A.NEISS,E.PARDO,
JRNL AUTH 4 C.G.NASVESCHUK,F.POY,P.SANDY,J.W.SETSER,R.J.SIMS,Y.TANG,
JRNL AUTH 5 B.K.ALBRECHT
JRNL TITL DISCOVERY OF BENZOTRIAZOLO[4,3-D][1,4]DIAZEPINES AS ORALLY
JRNL TITL 2 ACTIVE INHIBITORS OF BET BROMODOMAINS.
JRNL REF ACS MED.CHEM.LETT. V. 7 145 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 26985289
JRNL DOI 10.1021/ML500411H
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 3 NUMBER OF REFLECTIONS : 40551
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2084
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2091
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.67000
REMARK 3 B33 (A**2) : 0.54000
REMARK 3 B12 (A**2) : -0.18000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : -0.22000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.152
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2318 ; 0.022 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2194 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3182 ; 2.064 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5074 ; 0.987 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 271 ; 5.325 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;37.981 ;25.926
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 404 ;15.914 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;20.550 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2652 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 532 ; 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): 1057 ; 1.054 ; 0.944
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1056 ; 1.054 ; 0.941
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1337 ; 1.653 ; 1.404
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 : 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 43 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5735 -52.3493 148.0565
REMARK 3 T TENSOR
REMARK 3 T11: 0.0052 T22: 0.0689
REMARK 3 T33: 0.0098 T12: 0.0104
REMARK 3 T13: 0.0046 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.0528 L22: 0.1982
REMARK 3 L33: 0.6187 L12: -0.1776
REMARK 3 L13: -0.2715 L23: -0.0662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.0318 S13: -0.0326
REMARK 3 S21: 0.0051 S22: -0.0216 S23: 0.0175
REMARK 3 S31: -0.0264 S32: 0.0348 S33: -0.0157
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 41 B 167
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5975 -32.7761 173.2828
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: 0.0745
REMARK 3 T33: 0.0142 T12: 0.0169
REMARK 3 T13: 0.0091 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 1.2011 L22: 0.3223
REMARK 3 L33: 0.8043 L12: 0.1697
REMARK 3 L13: -0.4331 L23: -0.0888
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: 0.0290 S13: 0.0714
REMARK 3 S21: 0.0183 S22: -0.0207 S23: -0.0078
REMARK 3 S31: -0.0480 S32: -0.0513 S33: -0.0452
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
REMARK 4
REMARK 4 4Z1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42635
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.399
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.10
REMARK 200 R MERGE FOR SHELL (I) : 0.42800
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: PHASER
REMARK 200 STARTING MODEL: INTERNAL MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M BIS-TRIS
REMARK 280 PH 6.5, AND 25% POLYETHYLENE GLYCOL (PEG) 3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 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 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 GLY A 41
REMARK 465 SER A 42
REMARK 465 GLU A 167
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 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ASN A 52 112.29 -163.26
REMARK 500 LEU A 94 75.62 -110.42
REMARK 500 ASN B 52 100.65 -175.65
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 558 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 558 B 201
DBREF 4Z1Q A 42 167 UNP O60885 BRD4_HUMAN 42 167
DBREF 4Z1Q B 42 167 UNP O60885 BRD4_HUMAN 42 167
SEQADV 4Z1Q GLY A 41 UNP O60885 EXPRESSION TAG
SEQADV 4Z1Q GLY B 41 UNP O60885 EXPRESSION TAG
SEQRES 1 A 127 GLY SER THR ASN PRO PRO PRO PRO GLU THR SER ASN PRO
SEQRES 2 A 127 ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU
SEQRES 3 A 127 LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE
SEQRES 4 A 127 ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU
SEQRES 5 A 127 ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET
SEQRES 6 A 127 ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR
SEQRES 7 A 127 TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR
SEQRES 8 A 127 MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP
SEQRES 9 A 127 ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE
SEQRES 10 A 127 LEU GLN LYS ILE ASN GLU LEU PRO THR GLU
SEQRES 1 B 127 GLY SER THR ASN PRO PRO PRO PRO GLU THR SER ASN PRO
SEQRES 2 B 127 ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU
SEQRES 3 B 127 LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE
SEQRES 4 B 127 ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU
SEQRES 5 B 127 ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET
SEQRES 6 B 127 ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR
SEQRES 7 B 127 TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR
SEQRES 8 B 127 MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP
SEQRES 9 B 127 ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE
SEQRES 10 B 127 LEU GLN LYS ILE ASN GLU LEU PRO THR GLU
HET 558 A 201 30
HET 558 B 201 30
HETNAM 558 5-[(4R)-6-(4-CHLOROPHENYL)-1,4-DIMETHYL-5,6-DIHYDRO-4H-
HETNAM 2 558 [1,2,4]TRIAZOLO[4,3-A][1,5]BENZODIAZEPIN-8-YL]PYRIDIN-
HETNAM 3 558 2-AMINE
FORMUL 3 558 2(C23 H21 CL N6)
FORMUL 5 HOH *209(H2 O)
HELIX 1 AA1 THR A 60 VAL A 69 1 10
HELIX 2 AA2 VAL A 69 LYS A 76 1 8
HELIX 3 AA3 ALA A 80 GLN A 84 5 5
HELIX 4 AA4 ASP A 96 ILE A 101 1 6
HELIX 5 AA5 ASP A 106 ASN A 116 1 11
HELIX 6 AA6 ASN A 121 ASN A 140 1 20
HELIX 7 AA7 ASP A 144 ASN A 162 1 19
HELIX 8 AA8 THR B 60 VAL B 69 1 10
HELIX 9 AA9 VAL B 69 LYS B 76 1 8
HELIX 10 AB1 ALA B 80 GLN B 84 5 5
HELIX 11 AB2 ASP B 96 ILE B 101 1 6
HELIX 12 AB3 ASP B 106 ASN B 116 1 11
HELIX 13 AB4 ASN B 121 ASN B 140 1 20
HELIX 14 AB5 ASP B 144 ASN B 162 1 19
SITE 1 AC1 7 TRP A 81 PRO A 82 LEU A 92 TYR A 139
SITE 2 AC1 7 ASN A 140 ILE A 146 HOH A 318
SITE 1 AC2 10 HIS A 77 PHE A 79 ASP A 145 PRO B 82
SITE 2 AC2 10 PHE B 83 LEU B 92 TYR B 139 ASN B 140
SITE 3 AC2 10 ILE B 146 HOH B 318
CRYST1 30.293 39.501 57.230 83.07 75.35 89.85 P 1 2
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 0.033011 -0.000088 -0.008687 0.00000
SCALE2 0.000000 0.025316 -0.003163 0.00000
SCALE3 0.000000 0.000000 0.018201 0.00000
(ATOM LINES ARE NOT SHOWN.)
END