HEADER SIGNALING PROTEIN/INHIBITOR 20-FEB-17 5UVW
TITLE BRD4_BROMODOMAIN1-A1376855
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 57-165;
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 GENE: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HELIX BUNDLE BRD4 BROMODOMAIN 1 - INHIBITOR COMPLEX THREE COMPLEXES
KEYWDS 2 PER ASYMMETRIC UNIT, SIGNALING PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.PARK
REVDAT 2 06-MAR-24 5UVW 1 REMARK
REVDAT 1 21-JUN-17 5UVW 0
JRNL AUTH C.H.PARK
JRNL TITL BRD4_BROMODOMAIN1-A1376855
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 122.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 43603
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2195
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3155
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2384
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2997
REMARK 3 BIN R VALUE (WORKING SET) : 0.2371
REMARK 3 BIN FREE R VALUE : 0.2628
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2744
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.00740
REMARK 3 B22 (A**2) : 10.00740
REMARK 3 B33 (A**2) : -20.01470
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.273
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.147
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.134
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.139
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.129
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2986 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4104 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1009 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 86 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 434 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2986 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 357 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3606 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.06
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.73
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-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 : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 2.11.4
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43728
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 122.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.60
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER : 10 MM HEPES PH 7.5
REMARK 280 100 MM NACL 5 MM DTT CRYSTALLIZATION : 15 % (V/V) ETHANOL TRIS
REMARK 280 PH 7.0, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 44.20467
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 88.40933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.30700
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.51167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.10233
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.20467
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 88.40933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 110.51167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 66.30700
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 22.10233
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 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: 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: 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: 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: 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 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 S SO4 C 202 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 LYS B 57
REMARK 465 ARG B 58
REMARK 465 GLN B 59
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 LYS B 141 CE NZ
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 ARG A 58 105.72 -175.49
REMARK 500 ASN C 93 64.22 60.23
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 B 420 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 421 DISTANCE = 6.96 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NG C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UVV RELATED DB: PDB
REMARK 900 RELATED ID: 5UVZ RELATED DB: PDB
REMARK 900 RELATED ID: 5UVX RELATED DB: PDB
REMARK 900 RELATED ID: 5UVY RELATED DB: PDB
REMARK 900 RELATED ID: 5UVS RELATED DB: PDB
REMARK 900 RELATED ID: 5UVU RELATED DB: PDB
REMARK 900 RELATED ID: 5UVT RELATED DB: PDB
DBREF 5UVW A 57 165 UNP O60885 BRD4_HUMAN 57 165
DBREF 5UVW B 57 165 UNP O60885 BRD4_HUMAN 57 165
DBREF 5UVW C 57 165 UNP O60885 BRD4_HUMAN 57 165
SEQRES 1 A 109 LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG VAL
SEQRES 2 A 109 VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 A 109 PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU PRO
SEQRES 4 A 109 ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET GLY
SEQRES 5 A 109 THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP ASN
SEQRES 6 A 109 ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE THR
SEQRES 7 A 109 ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE VAL
SEQRES 8 A 109 LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN LYS
SEQRES 9 A 109 ILE ASN GLU LEU PRO
SEQRES 1 B 109 LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG VAL
SEQRES 2 B 109 VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 B 109 PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU PRO
SEQRES 4 B 109 ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET GLY
SEQRES 5 B 109 THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP ASN
SEQRES 6 B 109 ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE THR
SEQRES 7 B 109 ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE VAL
SEQRES 8 B 109 LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN LYS
SEQRES 9 B 109 ILE ASN GLU LEU PRO
SEQRES 1 C 109 LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG VAL
SEQRES 2 C 109 VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 3 C 109 PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU PRO
SEQRES 4 C 109 ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET GLY
SEQRES 5 C 109 THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP ASN
SEQRES 6 C 109 ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE THR
SEQRES 7 C 109 ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE VAL
SEQRES 8 C 109 LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN LYS
SEQRES 9 C 109 ILE ASN GLU LEU PRO
HET 8NG A 201 51
HET SO4 A 202 5
HET 8NG B 201 51
HET 8NG C 201 51
HET SO4 C 202 5
HETNAM 8NG N-[4-(2,4-DIFLUOROPHENOXY)-3-(6-METHYL-7-OXO-6,7-
HETNAM 2 8NG DIHYDRO-1H-PYRROLO[2,3-C]PYRIDIN-4-YL)
HETNAM 3 8NG PHENYL]ETHANESULFONAMIDE
HETNAM SO4 SULFATE ION
FORMUL 4 8NG 3(C22 H19 F2 N3 O4 S)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 HOH *294(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 GLU A 163 1 20
HELIX 8 AA8 ASN B 61 VAL B 69 1 9
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 GLU B 163 1 20
HELIX 15 AB6 ASN C 61 VAL C 69 1 9
HELIX 16 AB7 VAL C 69 HIS C 77 1 9
HELIX 17 AB8 ALA C 80 GLN C 84 5 5
HELIX 18 AB9 ASP C 88 ASN C 93 1 6
HELIX 19 AC1 ASP C 96 ILE C 101 1 6
HELIX 20 AC2 ASP C 106 ASN C 116 1 11
HELIX 21 AC3 ASN C 121 ASN C 140 1 20
HELIX 22 AC4 ASP C 144 GLU C 163 1 20
SITE 1 AC1 15 TRP A 81 PRO A 82 PHE A 83 GLN A 85
SITE 2 AC1 15 PRO A 86 VAL A 87 ASP A 88 LYS A 91
SITE 3 AC1 15 LEU A 92 ASN A 140 ILE A 146 SO4 A 202
SITE 4 AC1 15 HOH A 303 TRP B 81 8NG B 201
SITE 1 AC2 6 TRP A 81 LYS A 91 8NG A 201 TRP B 81
SITE 2 AC2 6 LYS B 91 8NG B 201
SITE 1 AC3 15 TRP A 81 8NG A 201 SO4 A 202 TRP B 81
SITE 2 AC3 15 PRO B 82 GLN B 85 PRO B 86 VAL B 87
SITE 3 AC3 15 ASP B 88 LYS B 91 LEU B 92 LEU B 94
SITE 4 AC3 15 ASN B 140 ILE B 146 HOH B 302
SITE 1 AC4 13 TRP C 81 PRO C 82 PHE C 83 GLN C 85
SITE 2 AC4 13 PRO C 86 VAL C 87 ASP C 88 LYS C 91
SITE 3 AC4 13 LEU C 92 ASN C 140 ILE C 146 SO4 C 202
SITE 4 AC4 13 HOH C 301
SITE 1 AC5 3 TRP C 81 LYS C 91 8NG C 201
CRYST1 141.438 141.438 132.614 90.00 90.00 120.00 P 61 2 2 36
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 0.007070 0.004082 0.000000 0.00000
SCALE2 0.000000 0.008164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END