HEADER TRANSCRIPTION 03-APR-15 4UIX
TITLE N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 7-(3,4-DIMETHOXYPHENYL)-N-
TITLE 2 (1,1-DIOXO-1-THIAN-4-YL)-5-METHYL-4-OXO-4H,5H-THIENO-3,2-C-PYRIDINE-
TITLE 3 2- CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: N-TERMINAL BROMODOMAIN, RESIDUES 44-168;
COMPND 5 SYNONYM: PROTEIN HUNK1, NHUMAN BRD4;
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 TRANSCRIPTION, INHIBITOR, HISTONE, EPIGENETIC READER, BROMODOMAIN,
KEYWDS 2 BRD4, BROMODOMAIN CONTAINING PROTEIN 4, ANTAGONIST
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG,N.T.THEODOULOU,P.BAMBOROUGH,P.G.HUMPHREYS
REVDAT 4 15-MAY-19 4UIX 1 REMARK
REVDAT 3 27-SEP-17 4UIX 1 REMARK
REVDAT 2 09-MAR-16 4UIX 1 JRNL
REVDAT 1 22-APR-15 4UIX 0
JRNL AUTH N.H.THEODOULOU,P.BAMBOROUGH,A.J.BANNISTER,I.BECHER,R.A.BIT,
JRNL AUTH 2 K.H.CHE,C.CHUNG,A.DITTMANN,G.DREWES,D.H.DREWRY,L.GORDON,
JRNL AUTH 3 P.GRANDI,M.LEVERIDGE,M.LINDON,A.MICHON,J.MOLNAR,S.C.ROBSON,
JRNL AUTH 4 N.C.O.TOMKINSON,T.KOUZARIDES,R.K.PRINJHA,P.G.HUMPHREYS
JRNL TITL THE DISCOVERY OF I-BRD9, A SELECTIVE CELL ACTIVE CHEMICAL
JRNL TITL 2 PROBE FOR BROMODOMAIN CONTAINING PROTEIN 9 INHIBITION.
JRNL REF J.MED.CHEM. V. 59 1425 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 25856009
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00256
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 55517
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2958
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3973
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3071
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 428
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.92000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.25000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.272
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
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): 3299 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2267 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4496 ; 1.127 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5574 ; 0.836 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 371 ; 5.042 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;37.913 ;25.742
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 582 ;11.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;18.803 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 469 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3821 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 608 ; 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 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 168
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9376 6.0906 28.2101
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.0064
REMARK 3 T33: 0.0421 T12: -0.0041
REMARK 3 T13: -0.0169 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.1746 L22: 0.4602
REMARK 3 L33: 0.6026 L12: 0.0128
REMARK 3 L13: 0.1220 L23: 0.3412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.0077 S13: -0.0109
REMARK 3 S21: -0.0230 S22: -0.0127 S23: 0.0356
REMARK 3 S31: -0.0674 S32: 0.0310 S33: 0.0538
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 42 B 167
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6475 27.7246 23.2063
REMARK 3 T TENSOR
REMARK 3 T11: 0.0327 T22: 0.0206
REMARK 3 T33: 0.0425 T12: 0.0010
REMARK 3 T13: 0.0055 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.3147 L22: 0.1286
REMARK 3 L33: 0.8627 L12: -0.0615
REMARK 3 L13: 0.1392 L23: -0.3209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: -0.0109 S13: -0.0108
REMARK 3 S21: -0.0141 S22: 0.0283 S23: -0.0144
REMARK 3 S31: 0.0274 S32: -0.0588 S33: -0.0105
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 42 C 163
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4513 14.2986 7.1332
REMARK 3 T TENSOR
REMARK 3 T11: 0.0229 T22: 0.0447
REMARK 3 T33: 0.0715 T12: -0.0028
REMARK 3 T13: 0.0108 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 1.4118 L22: 1.3195
REMARK 3 L33: 1.5158 L12: 0.3474
REMARK 3 L13: -1.3530 L23: -0.8422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0719 S12: -0.0926 S13: -0.1979
REMARK 3 S21: -0.0206 S22: -0.0674 S23: 0.0971
REMARK 3 S31: 0.0604 S32: 0.1229 S33: 0.1393
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 : 1.20
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 4UIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063543.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-13
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 : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58489
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 49.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1M HEPES, PEG 6K 20C,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 22.33500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 42
REMARK 465 GLU B 168
REMARK 465 SER C 51
REMARK 465 ASN C 52
REMARK 465 PRO C 53
REMARK 465 ASN C 54
REMARK 465 LYS C 55
REMARK 465 PRO C 56
REMARK 465 LYS C 57
REMARK 465 LEU C 164
REMARK 465 PRO C 165
REMARK 465 THR C 166
REMARK 465 GLU C 167
REMARK 465 GLU C 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 C 163 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 OH TYR C 65 O HOH C 2031 2.13
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 52 114.10 -160.88
REMARK 500 LEU A 94 72.86 -119.85
REMARK 500 ASN B 52 117.26 -160.07
REMARK 500 ASN C 162 93.80 -62.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2063 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH B2025 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH B2048 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH C2110 DISTANCE = 7.91 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1169 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 EDO A1170 O1
REMARK 620 2 EDO A1170 O2 63.7
REMARK 620 3 HOH A2148 O 121.2 80.5
REMARK 620 4 HOH A2167 O 126.6 73.0 77.8
REMARK 620 5 ASP A 145 OD2 79.7 114.2 74.7 149.6
REMARK 620 6 HOH A2147 O 143.2 152.4 84.9 81.1 83.8
REMARK 620 7 HOH A2145 O 75.5 93.4 155.3 77.5 128.9 90.2
REMARK 620 8 ASP A 145 OD1 71.1 134.6 123.3 143.7 52.0 72.8 77.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1168 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 145 OD1
REMARK 620 2 ASP B 145 OD2 51.9
REMARK 620 3 HOH B2131 O 75.7 127.6
REMARK 620 4 HOH B2133 O 70.3 79.9 83.9
REMARK 620 5 EDO B1169 O2 71.7 83.3 79.1 141.1
REMARK 620 6 HOH B2134 O 122.1 75.7 147.8 78.8 130.1
REMARK 620 7 HOH B2146 O 134.2 145.4 72.4 74.3 130.9 76.9
REMARK 620 8 EDO B1169 O1 134.7 109.0 107.0 154.1 64.8 80.1 86.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TVU A 1171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TVU B 1170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TVU C 1165
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UIT RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH 7-(3,4-DIMETHOXYPHENYL )-2-(4-
REMARK 900 METHANESULFONYLPIPERAZINE-1-CARBONYL)-5-METHYL- 4H,5H-THIENO-3,2-C-
REMARK 900 PYRIDIN-4-ONE
REMARK 900 RELATED ID: 4UIU RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH 7-(3,4-DIMETHOXYPHENYL )-N-(1,1-
REMARK 900 DIOXO-1-THIAN-4-YL)-5-METHYL-4-OXO- 4H,5H-THIENO-3,2-C-PYRIDINE-2-
REMARK 900 CARBOXAMIDE
REMARK 900 RELATED ID: 4UIV RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH N-(1,1-DIOXO-1- THIAN-4-YL)-5-METHYL-
REMARK 900 4-OXO-7-3-(TRIFLUOROMETHYL) PHENYL-4H,5H-THIENO-3,2-C-PYRIDINE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UIW RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRD9 WITH N-(1,1-DIOXO-1- THIAN-4-YL)-5-ETHYL-
REMARK 900 4-OXO-7-3-(TRIFLUOROMETHYL) PHENYL-4H,5H-THIENO-3,2-C-PYRIDINE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UIY RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH N-(1,1- DIOXO-1-THIAN-4-
REMARK 900 YL)-5-METHYL-4-OXO-7-3-( TRIFLUOROMETHYL)PHENYL-4H,5H-THIENO-3,2-C-
REMARK 900 PYRIDINE-2 -CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UIZ RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 7-(3,4- DIMETHOXYPHENYL)-
REMARK 900 2-(4-METHANESULFONYLPIPERAZINE-1-CARBONYL )-5-METHYL-4H,5H-THIENO-3,
REMARK 900 2-C-PYRIDIN-4-ONE
DBREF 4UIX A 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 4UIX B 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 4UIX C 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 4UIX SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 4UIX MET A 43 UNP O60885 EXPRESSION TAG
SEQADV 4UIX LYS A 78 UNP O60885 GLN 78 CONFLICT
SEQADV 4UIX SER B 42 UNP O60885 EXPRESSION TAG
SEQADV 4UIX MET B 43 UNP O60885 EXPRESSION TAG
SEQADV 4UIX LYS B 78 UNP O60885 GLN 78 CONFLICT
SEQADV 4UIX SER C 42 UNP O60885 EXPRESSION TAG
SEQADV 4UIX MET C 43 UNP O60885 EXPRESSION TAG
SEQADV 4UIX LYS C 78 UNP O60885 GLN 78 CONFLICT
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 LYS 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 LYS 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 LYS 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
HET CA A1169 1
HET EDO A1170 4
HET TVU A1171 32
HET CA B1168 1
HET EDO B1169 4
HET TVU B1170 32
HET EDO C1164 4
HET TVU C1165 32
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM TVU N-[1,1-BIS(OXIDANYLIDENE)THIAN-4-YL]-7-(3,4-
HETNAM 2 TVU DIMETHOXYPHENYL)-5-METHYL-4-OXIDANYLIDENE-THIENO[3,2-
HETNAM 3 TVU C]PYRIDINE-2-CARBOXAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 CA 2(CA 2+)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 6 TVU 3(C22 H24 N2 O6 S2)
FORMUL 12 HOH *428(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 HIS A 77 1 9
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 ASN A 162 1 19
HELIX 8 8 THR B 60 VAL B 69 1 10
HELIX 9 9 VAL B 69 HIS B 77 1 9
HELIX 10 10 ALA B 80 GLN B 84 5 5
HELIX 11 11 ASP B 88 ASN B 93 1 6
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 ASN C 162 1 19
LINK CA CA A1169 O1 EDO A1170 1555 1555 2.53
LINK CA CA A1169 O2 EDO A1170 1555 1555 2.39
LINK CA CA A1169 O HOH A2148 1555 1555 2.46
LINK CA CA A1169 O HOH A2167 1555 1555 2.34
LINK CA CA A1169 OD2 ASP A 145 1555 1555 2.49
LINK CA CA A1169 O HOH A2147 1555 1555 2.41
LINK CA CA A1169 O HOH A2145 1555 1555 2.49
LINK CA CA A1169 OD1 ASP A 145 1555 1555 2.50
LINK CA CA B1168 OD1 ASP B 145 1555 1555 2.47
LINK CA CA B1168 OD2 ASP B 145 1555 1555 2.54
LINK CA CA B1168 O HOH B2131 1555 1555 2.41
LINK CA CA B1168 O HOH B2133 1555 1555 2.39
LINK CA CA B1168 O2 EDO B1169 1555 1555 2.45
LINK CA CA B1168 O HOH B2134 1555 1555 2.39
LINK CA CA B1168 O HOH B2146 1555 1555 2.49
LINK CA CA B1168 O1 EDO B1169 1555 1555 2.54
SITE 1 AC1 6 ASP A 145 EDO A1170 HOH A2145 HOH A2147
SITE 2 AC1 6 HOH A2148 HOH A2167
SITE 1 AC2 6 ASP B 145 EDO B1169 HOH B2131 HOH B2133
SITE 2 AC2 6 HOH B2134 HOH B2146
SITE 1 AC3 7 ASP A 144 ASP A 145 CA A1169 TVU A1171
SITE 2 AC3 7 HOH A2145 HOH A2167 HOH A2168
SITE 1 AC4 6 ILE C 100 ILE C 101 LYS C 102 THR C 103
SITE 2 AC4 6 ASN C 135 HOH C2109
SITE 1 AC5 5 ASP B 144 ASP B 145 CA B1168 TVU B1170
SITE 2 AC5 5 HOH B2131
SITE 1 AC6 12 TRP A 81 PRO A 82 PHE A 83 LEU A 92
SITE 2 AC6 12 TYR A 139 ASN A 140 LYS A 141 ASP A 144
SITE 3 AC6 12 EDO A1170 HOH A2098 HOH A2107 HOH A2169
SITE 1 AC7 12 TRP B 81 PRO B 82 PHE B 83 VAL B 87
SITE 2 AC7 12 LEU B 92 TYR B 139 ASN B 140 LYS B 141
SITE 3 AC7 12 ASP B 144 EDO B1169 HOH B2090 HOH B2148
SITE 1 AC8 10 TRP C 81 PRO C 82 VAL C 87 LEU C 92
SITE 2 AC8 10 LEU C 94 TYR C 139 ASN C 140 LYS C 141
SITE 3 AC8 10 ASP C 144 HOH C2067
CRYST1 63.640 44.670 77.550 90.00 90.09 90.00 P 1 21 1 6
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 0.015713 0.000000 0.000025 0.00000
SCALE2 0.000000 0.022386 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012895 0.00000
(ATOM LINES ARE NOT SHOWN.)
END