HEADER TRANSCRIPTION/INHIBITOR 08-FEB-18 6CD4
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH THE INHIBITOR JWG046
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 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 KINASE, INHIBITOR, BRD4, TRANSCRIPTION, TRANSCRIPTION-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XU,S.C.BLACKLOW
REVDAT 6 04-OCT-23 6CD4 1 REMARK
REVDAT 5 01-JAN-20 6CD4 1 REMARK
REVDAT 4 17-APR-19 6CD4 1 REMARK
REVDAT 3 20-FEB-19 6CD4 1 REMARK
REVDAT 2 03-OCT-18 6CD4 1 JRNL
REVDAT 1 29-AUG-18 6CD4 0
JRNL AUTH J.WANG,T.ERAZO,F.M.FERGUSON,D.L.BUCKLEY,N.GOMEZ,
JRNL AUTH 2 P.MUNOZ-GUARDIOLA,N.DIEGUEZ-MARTINEZ,X.DENG,M.HAO,
JRNL AUTH 3 W.MASSEFSKI,O.FEDOROV,N.K.OFFEI-ADDO,P.M.PARK,L.DAI,
JRNL AUTH 4 A.DIBONA,K.BECHT,N.D.KIM,M.R.MCKEOWN,J.M.ROBERTS,J.ZHANG,
JRNL AUTH 5 T.SIM,D.R.ALESSI,J.E.BRADNER,J.M.LIZCANO,S.C.BLACKLOW,J.QI,
JRNL AUTH 6 X.XU,N.S.GRAY
JRNL TITL STRUCTURAL AND ATROPISOMERIC FACTORS GOVERNING THE
JRNL TITL 2 SELECTIVITY OF PYRIMIDO-BENZODIAZIPINONES AS INHIBITORS OF
JRNL TITL 3 KINASES AND BROMODOMAINS.
JRNL REF ACS CHEM. BIOL. V. 13 2438 2018
JRNL REFN ESSN 1554-8937
JRNL PMID 30102854
JRNL DOI 10.1021/ACSCHEMBIO.7B00638
REMARK 2
REMARK 2 RESOLUTION. 1.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
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) : 1.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 35909
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1794
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 38.1081 - 2.8909 0.98 2853 159 0.1642 0.1776
REMARK 3 2 2.8909 - 2.2947 0.98 2721 161 0.1446 0.1664
REMARK 3 3 2.2947 - 2.0046 0.99 2717 155 0.1321 0.1367
REMARK 3 4 2.0046 - 1.8214 0.99 2715 128 0.1414 0.1369
REMARK 3 5 1.8214 - 1.6908 0.99 2710 144 0.1485 0.1454
REMARK 3 6 1.6908 - 1.5911 0.99 2713 134 0.1476 0.1715
REMARK 3 7 1.5911 - 1.5114 1.00 2713 135 0.1483 0.1478
REMARK 3 8 1.5114 - 1.4456 1.00 2708 136 0.1565 0.1779
REMARK 3 9 1.4456 - 1.3900 1.00 2691 128 0.1740 0.1770
REMARK 3 10 1.3900 - 1.3420 1.00 2700 134 0.1847 0.2168
REMARK 3 11 1.3420 - 1.3000 1.00 2703 149 0.1985 0.2033
REMARK 3 12 1.3000 - 1.2629 0.91 2437 127 0.2459 0.2643
REMARK 3 13 1.2629 - 1.2296 0.65 1734 104 0.3209 0.3507
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.060
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 : 0.007 1104
REMARK 3 ANGLE : 1.124 1508
REMARK 3 CHIRALITY : 0.068 160
REMARK 3 PLANARITY : 0.009 194
REMARK 3 DIHEDRAL : 16.238 419
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1043 -11.9323 -20.1617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.1808
REMARK 3 T33: 0.1752 T12: -0.0134
REMARK 3 T13: 0.0172 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 5.7588 L22: 0.8633
REMARK 3 L33: 2.2201 L12: -0.1672
REMARK 3 L13: -3.4947 L23: 0.3717
REMARK 3 S TENSOR
REMARK 3 S11: -0.1315 S12: -0.1558 S13: 0.1181
REMARK 3 S21: 0.4647 S22: 0.1406 S23: -0.0074
REMARK 3 S31: -0.1870 S32: 0.2868 S33: 0.0260
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3380 -5.8898 -31.0356
REMARK 3 T TENSOR
REMARK 3 T11: 0.1620 T22: 0.1784
REMARK 3 T33: 0.1623 T12: -0.0085
REMARK 3 T13: 0.0109 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.5732 L22: 0.5547
REMARK 3 L33: 0.9597 L12: 0.2930
REMARK 3 L13: 0.6363 L23: -0.3167
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: 0.1890 S13: -0.0994
REMARK 3 S21: -0.0999 S22: -0.0041 S23: -0.0239
REMARK 3 S31: -0.0138 S32: 0.1287 S33: 0.0557
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3136 -2.3716 -20.8051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1244 T22: 0.1382
REMARK 3 T33: 0.1594 T12: 0.0086
REMARK 3 T13: 0.0101 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 2.3764 L22: 2.1383
REMARK 3 L33: 3.2795 L12: -0.4861
REMARK 3 L13: 1.1323 L23: 1.2568
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: -0.0496 S13: -0.0577
REMARK 3 S21: -0.0784 S22: -0.0014 S23: 0.0309
REMARK 3 S31: 0.0229 S32: -0.2048 S33: 0.1581
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7027 -2.5241 -12.1763
REMARK 3 T TENSOR
REMARK 3 T11: 0.1642 T22: 0.1668
REMARK 3 T33: 0.1539 T12: 0.0264
REMARK 3 T13: -0.0058 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 3.9168 L22: 1.1196
REMARK 3 L33: 2.0804 L12: -0.1162
REMARK 3 L13: 1.5409 L23: 0.1494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: -0.1468 S13: 0.0821
REMARK 3 S21: 0.0335 S22: 0.0665 S23: 0.0483
REMARK 3 S31: -0.2721 S32: -0.3830 S33: -0.0246
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4060 -5.8109 -4.8169
REMARK 3 T TENSOR
REMARK 3 T11: 0.1918 T22: 0.1642
REMARK 3 T33: 0.1380 T12: -0.0109
REMARK 3 T13: 0.0034 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 2.1865 L22: 2.0011
REMARK 3 L33: 1.5364 L12: -0.6036
REMARK 3 L13: 0.5766 L23: -0.4984
REMARK 3 S TENSOR
REMARK 3 S11: -0.0694 S12: -0.3461 S13: 0.0029
REMARK 3 S21: 0.2726 S22: 0.0472 S23: 0.0676
REMARK 3 S31: -0.0755 S32: 0.0375 S33: -0.0124
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2067 -14.7736 -13.6407
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.2017
REMARK 3 T33: 0.1308 T12: 0.0111
REMARK 3 T13: -0.0086 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.4392 L22: 1.9519
REMARK 3 L33: 1.5931 L12: -0.2389
REMARK 3 L13: -0.7339 L23: 0.7488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0516 S12: -0.2573 S13: -0.0847
REMARK 3 S21: 0.1400 S22: 0.1530 S23: -0.0934
REMARK 3 S31: 0.0947 S32: 0.3090 S33: -0.0777
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7516 -3.8321 -20.2195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1455 T22: 0.1288
REMARK 3 T33: 0.1366 T12: -0.0080
REMARK 3 T13: 0.0130 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.6819 L22: 1.7464
REMARK 3 L33: 2.7627 L12: -0.8515
REMARK 3 L13: 0.4250 L23: -0.7963
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.1274 S13: 0.1874
REMARK 3 S21: 0.1702 S22: 0.0079 S23: -0.0868
REMARK 3 S31: -0.2869 S32: 0.0304 S33: -0.0467
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8063 -6.4184 -28.6573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1310 T22: 0.1414
REMARK 3 T33: 0.1443 T12: 0.0107
REMARK 3 T13: -0.0077 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.4623 L22: 0.8386
REMARK 3 L33: 1.3134 L12: 0.2865
REMARK 3 L13: 0.5216 L23: 0.2438
REMARK 3 S TENSOR
REMARK 3 S11: 0.0650 S12: 0.0967 S13: -0.0327
REMARK 3 S21: -0.0872 S22: 0.0092 S23: 0.0274
REMARK 3 S31: -0.0616 S32: -0.1025 S33: -0.0526
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8797 -15.8056 -15.6367
REMARK 3 T TENSOR
REMARK 3 T11: 0.1154 T22: 0.1188
REMARK 3 T33: 0.1351 T12: -0.0129
REMARK 3 T13: 0.0021 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.9909 L22: 1.7465
REMARK 3 L33: 1.7449 L12: -0.7174
REMARK 3 L13: 0.6307 L23: -0.9679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.0442 S13: -0.0333
REMARK 3 S21: 0.0499 S22: -0.0084 S23: 0.0539
REMARK 3 S31: -0.0140 S32: -0.0167 S33: -0.0374
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1368 -21.3583 -1.5917
REMARK 3 T TENSOR
REMARK 3 T11: 0.2386 T22: 0.1790
REMARK 3 T33: 0.1716 T12: -0.0429
REMARK 3 T13: 0.0092 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.5062 L22: 3.2728
REMARK 3 L33: 4.1749 L12: 1.7338
REMARK 3 L13: -0.3770 L23: -0.9663
REMARK 3 S TENSOR
REMARK 3 S11: -0.0624 S12: -0.2558 S13: -0.0798
REMARK 3 S21: 0.4249 S22: -0.1968 S23: -0.0508
REMARK 3 S31: 0.2223 S32: 0.2505 S33: 0.1884
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1636 -11.4663 -8.7934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.1425
REMARK 3 T33: 0.1613 T12: -0.0136
REMARK 3 T13: 0.0316 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 4.6439 L22: 2.1954
REMARK 3 L33: 4.2973 L12: -1.6233
REMARK 3 L13: 2.2933 L23: -1.3106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1125 S12: -0.1403 S13: -0.3223
REMARK 3 S21: 0.1269 S22: 0.0895 S23: 0.2239
REMARK 3 S31: 0.0606 S32: -0.4139 S33: -0.1734
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 6CD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-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 : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35971
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.230
REMARK 200 RESOLUTION RANGE LOW (A) : 56.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.68900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4WIV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM NITRATE, 5% ETHYLENE
REMARK 280 GLYCOL, 18% (W/V) PEG3350, VAPOR DIFFUSION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 21.57850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.30900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.74100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.30900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.57850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.74100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 A 167
REMARK 465 GLU A 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 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 LYS A 155 CG CD CE NZ
REMARK 470 GLU A 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 O HOH A 436 O HOH A 444 1.83
REMARK 500 O HOH A 420 O HOH A 423 1.86
REMARK 500 O HOH A 332 O HOH A 428 1.90
REMARK 500 O HOH A 418 O HOH A 427 2.08
REMARK 500 O HOH A 378 O HOH A 419 2.11
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 EX1 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
DBREF 6CD4 A 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQRES 1 A 127 SER THR 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
HET EX1 A 201 86
HET EDO A 202 10
HET EDO A 203 10
HET EDO A 204 10
HETNAM EX1 2-({2-METHOXY-4-[4-(4-METHYLPIPERAZIN-1-YL)PIPERIDINE-
HETNAM 2 EX1 1-CARBONYL]PHENYL}AMINO)-5-METHYL-11-(PROPAN-2-YL)-5,
HETNAM 3 EX1 11-DIHYDRO-6H-PYRIMIDO[4,5-B][1,4]BENZODIAZEPIN-6-ONE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EX1 C33 H42 N8 O3
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 HOH *151(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
SITE 1 AC1 14 TRP A 81 PRO A 82 PHE A 83 LEU A 94
SITE 2 AC1 14 GLU A 115 ASN A 116 TYR A 139 ASN A 140
SITE 3 AC1 14 ILE A 146 EDO A 204 HOH A 317 HOH A 329
SITE 4 AC1 14 HOH A 370 HOH A 412
SITE 1 AC2 5 SER A 51 ASN A 52 LYS A 57 TYR A 118
SITE 2 AC2 5 HOH A 335
SITE 1 AC3 6 ILE A 100 ILE A 101 LYS A 102 THR A 103
SITE 2 AC3 6 ASN A 135 HOH A 315
SITE 1 AC4 3 GLU A 115 ASN A 116 EX1 A 201
CRYST1 43.157 51.482 56.618 90.00 90.00 90.00 P 21 21 21 4
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 0.023171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019424 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END