HEADER DNA BINDING PROTEIN 04-SEP-17 5OWW
TITLE CRYSTAL STRUCTURE OF HUMAN BRD4(1) BROMODOMAIN IN COMPLEX WITH UT22B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: BROMO DOMAIN 1, UNP RESIDUES 44-168;
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 BRD4 BROMODOMAIN 1(BRP4(1)), INHIBITOR, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHU,A.CAFLISCH
REVDAT 3 17-JAN-24 5OWW 1 REMARK
REVDAT 2 23-OCT-19 5OWW 1 COMPND JRNL
REVDAT 1 10-OCT-18 5OWW 0
JRNL AUTH L.BATISTE,A.UNZUE,A.DOLBOIS,F.HASSLER,X.WANG,N.DEERAIN,
JRNL AUTH 2 J.ZHU,D.SPILIOTOPOULOS,C.NEVADO,A.CAFLISCH
JRNL TITL CHEMICAL SPACE EXPANSION OF BROMODOMAIN LIGANDS GUIDED BY IN
JRNL TITL 2 SILICO VIRTUAL COUPLINGS (AUTOCOUPLE).
JRNL REF ACS CENT.SCI. V. 4 180 2018
JRNL REFN ESSN 2374-7951
JRNL PMID 29532017
JRNL DOI 10.1021/ACSCENTSCI.7B00401
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 85369
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.340
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.1095 - 3.6145 0.95 6015 147 0.1560 0.1731
REMARK 3 2 3.6145 - 2.8691 0.97 5962 138 0.1660 0.1734
REMARK 3 3 2.8691 - 2.5065 0.96 5895 141 0.1809 0.1888
REMARK 3 4 2.5065 - 2.2774 0.97 5929 144 0.1839 0.2284
REMARK 3 5 2.2774 - 2.1141 0.98 5958 148 0.1825 0.2194
REMARK 3 6 2.1141 - 1.9895 0.99 6018 149 0.1880 0.2097
REMARK 3 7 1.9895 - 1.8899 1.00 6077 140 0.1973 0.1963
REMARK 3 8 1.8899 - 1.8076 0.98 5978 141 0.2068 0.2282
REMARK 3 9 1.8076 - 1.7380 0.97 5874 145 0.2033 0.2381
REMARK 3 10 1.7380 - 1.6780 0.98 5948 138 0.2007 0.2325
REMARK 3 11 1.6780 - 1.6256 0.98 5937 146 0.2134 0.2222
REMARK 3 12 1.6256 - 1.5791 0.98 5951 144 0.2410 0.2500
REMARK 3 13 1.5791 - 1.5375 0.98 5907 135 0.2654 0.3060
REMARK 3 14 1.5375 - 1.5000 0.98 5920 144 0.3009 0.3116
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 4548
REMARK 3 ANGLE : 0.897 6206
REMARK 3 CHIRALITY : 0.046 648
REMARK 3 PLANARITY : 0.006 802
REMARK 3 DIHEDRAL : 12.887 2790
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3469 -6.9740 27.4421
REMARK 3 T TENSOR
REMARK 3 T11: 0.0987 T22: 0.0684
REMARK 3 T33: 0.0857 T12: -0.0029
REMARK 3 T13: 0.0012 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.2854 L22: 0.0620
REMARK 3 L33: 0.1886 L12: -0.0136
REMARK 3 L13: 0.0097 L23: 0.0599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0192 S12: 0.0232 S13: 0.0153
REMARK 3 S21: 0.0016 S22: -0.0134 S23: -0.0001
REMARK 3 S31: -0.0203 S32: -0.0039 S33: -0.0006
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OWW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-16
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999989
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85408
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
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: MOLREP
REMARK 200 STARTING MODEL: 2OSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 10% V/V 2
REMARK 280 -PROPANOL, 20% W/V POLYETHYLENE GLYCOL 4,000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 20.96200
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, 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 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 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 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 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 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 GLN B 59 CD OE1 NE2
REMARK 470 LYS B 111 CE NZ
REMARK 470 GLN B 123 CD OE1 NE2
REMARK 470 LYS C 91 NZ
REMARK 470 GLN C 123 CD OE1 NE2
REMARK 470 GLU C 168 CG CD OE1 OE2
REMARK 470 GLU D 49 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 A 310 O HOH A 386 1.80
REMARK 500 O HOH A 460 O HOH A 463 1.81
REMARK 500 O HOH C 438 O HOH C 464 1.85
REMARK 500 O HOH D 442 O HOH D 484 1.86
REMARK 500 O HOH B 479 O HOH B 498 1.88
REMARK 500 O HOH C 378 O HOH D 479 1.90
REMARK 500 O HOH C 463 O HOH C 483 1.90
REMARK 500 OE2 GLU A 163 O HOH A 301 1.90
REMARK 500 O HOH A 422 O HOH A 431 1.90
REMARK 500 O HOH C 304 O HOH C 330 1.91
REMARK 500 O HOH C 478 O HOH D 459 1.91
REMARK 500 O HOH C 405 O HOH C 475 1.93
REMARK 500 O HOH A 329 O HOH A 455 1.94
REMARK 500 O HOH D 350 O HOH D 451 1.97
REMARK 500 O HOH D 409 O HOH D 504 2.01
REMARK 500 O HOH C 362 O HOH C 409 2.01
REMARK 500 O HOH B 301 O HOH B 404 2.03
REMARK 500 O HOH D 317 O HOH D 443 2.04
REMARK 500 O HOH A 500 O HOH C 441 2.05
REMARK 500 O HOH C 437 O HOH C 475 2.06
REMARK 500 O HOH B 385 O HOH B 452 2.06
REMARK 500 O HOH A 442 O HOH B 334 2.06
REMARK 500 O HOH A 451 O HOH A 480 2.07
REMARK 500 NZ LYS A 72 O HOH A 302 2.07
REMARK 500 O HOH C 436 O HOH C 462 2.08
REMARK 500 O HOH D 449 O HOH D 499 2.10
REMARK 500 OH TYR B 98 O HOH B 301 2.10
REMARK 500 O HOH B 445 O HOH B 452 2.11
REMARK 500 O HOH D 457 O HOH D 482 2.11
REMARK 500 O HOH B 455 O HOH B 486 2.12
REMARK 500 O HOH D 305 O HOH D 341 2.13
REMARK 500 O HOH B 413 O HOH B 438 2.14
REMARK 500 O HOH D 361 O HOH D 453 2.17
REMARK 500 O HOH B 328 O HOH B 450 2.17
REMARK 500 O HOH B 351 O HOH B 456 2.18
REMARK 500 O HOH B 390 O HOH B 455 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 466 O HOH B 420 2456 1.94
REMARK 500 O HOH C 437 O HOH D 499 1655 2.01
REMARK 500 O HOH A 390 O HOH B 353 2456 2.06
REMARK 500 O HOH C 475 O HOH D 499 1655 2.06
REMARK 500 O HOH A 308 O HOH B 385 1655 2.07
REMARK 500 O HOH A 464 O HOH B 329 1655 2.11
REMARK 500 O HOH A 313 O HOH B 432 2446 2.12
REMARK 500 O HOH A 451 O HOH A 472 1565 2.12
REMARK 500 O HOH C 363 O HOH D 450 1655 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 LEU B 94 76.13 -112.73
REMARK 500 ASN B 140 -164.77 -103.56
REMARK 500 ASN C 140 -168.81 -104.54
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 502 DISTANCE = 5.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B0Q A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B0Q B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B0Q C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B0Q D 201
DBREF 5OWW A 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 5OWW B 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 5OWW C 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 5OWW D 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5OWW SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 5OWW MET A 43 UNP O60885 EXPRESSION TAG
SEQADV 5OWW SER B 42 UNP O60885 EXPRESSION TAG
SEQADV 5OWW MET B 43 UNP O60885 EXPRESSION TAG
SEQADV 5OWW SER C 42 UNP O60885 EXPRESSION TAG
SEQADV 5OWW MET C 43 UNP O60885 EXPRESSION TAG
SEQADV 5OWW SER D 42 UNP O60885 EXPRESSION TAG
SEQADV 5OWW MET D 43 UNP O60885 EXPRESSION TAG
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 B0Q A 201 25
HET B0Q B 201 25
HET B0Q C 201 25
HET B0Q D 201 25
HETNAM B0Q ~{N}-(3-METHYLBENZOTRIAZOL-5-YL)-1-(PHENYLMETHYL)
HETNAM 2 B0Q IMIDAZOLE-2-CARBOXAMIDE
FORMUL 5 B0Q 4(C18 H16 N6 O)
FORMUL 9 HOH *844(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 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 GLU B 163 1 20
HELIX 15 AB6 THR C 60 VAL C 69 1 10
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 96 ILE C 101 1 6
HELIX 19 AC1 ASP C 106 ASN C 116 1 11
HELIX 20 AC2 ASN C 121 ASN C 140 1 20
HELIX 21 AC3 ASP C 144 GLU C 163 1 20
HELIX 22 AC4 THR D 60 VAL D 69 1 10
HELIX 23 AC5 VAL D 69 HIS D 77 1 9
HELIX 24 AC6 ALA D 80 GLN D 84 5 5
HELIX 25 AC7 ASP D 96 ILE D 101 1 6
HELIX 26 AC8 ASP D 106 ASN D 116 1 11
HELIX 27 AC9 ASN D 121 ASN D 140 1 20
HELIX 28 AD1 ASP D 144 GLU D 163 1 20
SITE 1 AC1 8 TRP A 81 PRO A 82 VAL A 87 LEU A 92
SITE 2 AC1 8 LEU A 94 ASN A 140 HOH A 315 GLN C 78
SITE 1 AC2 12 TRP B 81 PRO B 82 GLN B 85 VAL B 87
SITE 2 AC2 12 LEU B 92 LEU B 94 ASN B 140 HOH B 330
SITE 3 AC2 12 HOH B 384 HOH B 402 GLN D 78 HOH D 494
SITE 1 AC3 11 ASP A 145 TRP C 81 PRO C 82 GLN C 85
SITE 2 AC3 11 VAL C 87 LEU C 92 TYR C 139 ASN C 140
SITE 3 AC3 11 HOH C 336 HOH C 392 HOH C 394
SITE 1 AC4 10 ASP B 145 MET B 149 PRO D 82 GLN D 85
SITE 2 AC4 10 VAL D 87 LEU D 92 ASN D 140 HOH D 324
SITE 3 AC4 10 HOH D 326 HOH D 403
CRYST1 59.877 41.924 109.416 90.00 92.03 90.00 P 1 21 1 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 0.016701 0.000000 0.000592 0.00000
SCALE2 0.000000 0.023853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009145 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
