HEADER TRANSCRIPTION 06-AUG-15 5D3N
TITLE FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST BROMODOMAIN, 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 GENE REGULATION, BROMODOMAIN, INHIBITOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WOHLWEND,M.HUEGLE
REVDAT 3 06-SEP-17 5D3N 1 REMARK
REVDAT 2 09-MAR-16 5D3N 1 JRNL
REVDAT 1 20-JAN-16 5D3N 0
JRNL AUTH M.HUGLE,X.LUCAS,G.WEITZEL,D.OSTROVSKYI,B.BREIT,S.GERHARDT,
JRNL AUTH 2 O.EINSLE,S.GUNTHER,D.WOHLWEND
JRNL TITL 4-ACYL PYRROLE DERIVATIVES YIELD NOVEL VECTORS FOR DESIGNING
JRNL TITL 2 INHIBITORS OF THE ACETYL-LYSINE RECOGNITION SITE OF BRD4(1).
JRNL REF J.MED.CHEM. V. 59 1518 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26731611
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01267
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 6975
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 764
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 509
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.4540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.93000
REMARK 3 B22 (A**2) : -1.74000
REMARK 3 B33 (A**2) : -2.19000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.327
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.302
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1131 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1074 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1546 ; 1.322 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2481 ; 0.789 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 129 ; 5.525 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;35.529 ;26.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 199 ;16.776 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;13.604 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 161 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1281 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 256 ; 0.006 ; 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): 513 ; 1.111 ; 2.419
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 512 ; 1.105 ; 2.414
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 643 ; 1.703 ; 3.623
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 644 ; 1.702 ; 3.628
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 618 ; 1.061 ; 2.510
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 619 ; 1.060 ; 2.511
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 904 ; 1.641 ; 3.744
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4812 ; 4.210 ;22.898
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4768 ; 4.152 ;22.794
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 : 12
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 51
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5441 8.9128 15.7204
REMARK 3 T TENSOR
REMARK 3 T11: 0.3407 T22: 0.1093
REMARK 3 T33: 0.0808 T12: 0.0695
REMARK 3 T13: -0.0748 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 6.1700 L22: 0.4470
REMARK 3 L33: 4.7989 L12: -1.4284
REMARK 3 L13: 1.1119 L23: -0.2148
REMARK 3 S TENSOR
REMARK 3 S11: 0.1255 S12: -0.1593 S13: 0.1384
REMARK 3 S21: 0.1471 S22: 0.1011 S23: -0.1128
REMARK 3 S31: -0.4165 S32: -0.3937 S33: -0.2265
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 : A 52 A 59
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6208 -6.0668 27.0579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.1243
REMARK 3 T33: 0.1792 T12: -0.0430
REMARK 3 T13: -0.0031 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.1476 L22: 9.6614
REMARK 3 L33: 1.2301 L12: 1.0472
REMARK 3 L13: 0.0042 L23: -1.6208
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: -0.0315 S13: 0.0042
REMARK 3 S21: 0.2814 S22: 0.0253 S23: 0.1452
REMARK 3 S31: 0.0632 S32: -0.1827 S33: -0.0701
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 : A 60 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2853 -14.4333 15.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.3543 T22: 0.2524
REMARK 3 T33: 0.3002 T12: 0.0927
REMARK 3 T13: -0.0155 T23: 0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 6.3512 L22: 8.6556
REMARK 3 L33: 4.6280 L12: -0.8425
REMARK 3 L13: -1.2201 L23: 3.6582
REMARK 3 S TENSOR
REMARK 3 S11: 0.1469 S12: -0.1479 S13: 0.0489
REMARK 3 S21: 0.8169 S22: 0.0630 S23: -0.4128
REMARK 3 S31: 0.7895 S32: 0.8465 S33: -0.2098
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 71 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1918 -2.8478 4.0114
REMARK 3 T TENSOR
REMARK 3 T11: 0.0480 T22: 0.1417
REMARK 3 T33: 0.3927 T12: 0.0450
REMARK 3 T13: 0.0738 T23: 0.0810
REMARK 3 L TENSOR
REMARK 3 L11: 2.0272 L22: 10.7152
REMARK 3 L33: 7.6066 L12: -2.7389
REMARK 3 L13: 1.2718 L23: 2.1557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: -0.0159 S13: -0.4050
REMARK 3 S21: -0.0260 S22: 0.0840 S23: -0.5808
REMARK 3 S31: 0.4698 S32: 0.6346 S33: -0.1050
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 87 A 98
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9706 13.0136 3.3182
REMARK 3 T TENSOR
REMARK 3 T11: 0.0926 T22: 0.1633
REMARK 3 T33: 0.0698 T12: 0.0335
REMARK 3 T13: 0.0369 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 7.1479 L22: 1.9210
REMARK 3 L33: 4.7917 L12: 0.7564
REMARK 3 L13: 3.4251 L23: 0.0986
REMARK 3 S TENSOR
REMARK 3 S11: -0.2741 S12: 0.6785 S13: 0.1537
REMARK 3 S21: -0.0272 S22: 0.3833 S23: -0.1714
REMARK 3 S31: -0.6287 S32: -0.0595 S33: -0.1092
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 99 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2367 4.7282 8.3910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.1339
REMARK 3 T33: 0.0817 T12: 0.0033
REMARK 3 T13: -0.0032 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 5.7045 L22: 2.3596
REMARK 3 L33: 2.3386 L12: -2.2119
REMARK 3 L13: 1.7015 L23: -2.2935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1467 S12: -0.0116 S13: 0.1068
REMARK 3 S21: 0.0837 S22: 0.1174 S23: -0.0557
REMARK 3 S31: -0.1037 S32: -0.1983 S33: 0.0293
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 110 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7000 -3.3324 17.5940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1159 T22: 0.1807
REMARK 3 T33: 0.2151 T12: -0.0617
REMARK 3 T13: -0.0766 T23: 0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 7.6269 L22: 5.5886
REMARK 3 L33: 9.1337 L12: -6.5227
REMARK 3 L13: 2.3110 L23: -1.9335
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: -0.4055 S13: 0.5510
REMARK 3 S21: 0.0663 S22: 0.3070 S23: -0.5080
REMARK 3 S31: 0.1100 S32: 0.4019 S33: -0.2528
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 118 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6053 -9.5072 17.7995
REMARK 3 T TENSOR
REMARK 3 T11: 0.1443 T22: 0.1596
REMARK 3 T33: 0.0620 T12: -0.0402
REMARK 3 T13: 0.0558 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.0427 L22: 5.9574
REMARK 3 L33: 6.1169 L12: 0.4988
REMARK 3 L13: -0.3481 L23: -3.5101
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: 0.0126 S13: 0.0126
REMARK 3 S21: -0.0595 S22: 0.0962 S23: 0.1852
REMARK 3 S31: 0.5105 S32: -0.4782 S33: -0.0693
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 128 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9461 -1.0458 1.8050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0497 T22: 0.3691
REMARK 3 T33: 0.0348 T12: -0.0536
REMARK 3 T13: 0.0042 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 1.5094 L22: 10.2042
REMARK 3 L33: 10.2158 L12: -2.1096
REMARK 3 L13: 3.4180 L23: -5.1416
REMARK 3 S TENSOR
REMARK 3 S11: 0.1605 S12: 0.2339 S13: -0.0284
REMARK 3 S21: -0.5549 S22: -0.1345 S23: 0.1735
REMARK 3 S31: 0.5722 S32: -0.3761 S33: -0.0260
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 143 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1139 -0.0683 -6.0490
REMARK 3 T TENSOR
REMARK 3 T11: 0.2397 T22: 0.1626
REMARK 3 T33: 0.1051 T12: 0.0325
REMARK 3 T13: 0.1128 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 3.5375 L22: 2.0776
REMARK 3 L33: 8.2965 L12: -1.3103
REMARK 3 L13: 0.8610 L23: -3.8875
REMARK 3 S TENSOR
REMARK 3 S11: -0.1992 S12: 0.2699 S13: -0.0979
REMARK 3 S21: 0.0050 S22: 0.0358 S23: -0.0772
REMARK 3 S31: -0.0317 S32: -0.3014 S33: 0.1634
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3122 -10.2786 -0.0011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0910 T22: 0.1124
REMARK 3 T33: 0.1429 T12: 0.0131
REMARK 3 T13: 0.0181 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 5.0551 L22: 6.9976
REMARK 3 L33: 6.0986 L12: -0.1503
REMARK 3 L13: -4.9523 L23: -2.8000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0797 S12: 0.1902 S13: -0.1693
REMARK 3 S21: -0.0542 S22: -0.0466 S23: 0.0490
REMARK 3 S31: 0.1108 S32: -0.1589 S33: 0.1262
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 159 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8674 -19.5711 10.6974
REMARK 3 T TENSOR
REMARK 3 T11: 0.2017 T22: 0.1022
REMARK 3 T33: 0.2536 T12: -0.0036
REMARK 3 T13: 0.0090 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 3.8111 L22: 0.7332
REMARK 3 L33: 8.2303 L12: 0.1023
REMARK 3 L13: 0.1820 L23: -2.3865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: 0.1775 S13: -0.1176
REMARK 3 S21: -0.0102 S22: -0.0010 S23: -0.0707
REMARK 3 S31: 0.1754 S32: -0.0271 S33: -0.0296
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 5D3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9604
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TACSIMATE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 19.54000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.55500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.55500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.54000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.75000
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 NE2 GLN A 123 O HOH A 301 2.15
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 52 104.71 -165.13
REMARK 500 LEU A 94 77.52 -113.93
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 L40 A 201
DBREF 5D3N A 43 168 UNP O60885 BRD4_HUMAN 43 168
SEQADV 5D3N MET A 43 UNP O60885 THR 43 ENGINEERED MUTATION
SEQRES 1 A 126 MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN LYS
SEQRES 2 A 126 PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG
SEQRES 3 A 126 VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP
SEQRES 4 A 126 PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU
SEQRES 5 A 126 PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET
SEQRES 6 A 126 GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP
SEQRES 7 A 126 ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE
SEQRES 8 A 126 THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE
SEQRES 9 A 126 VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN
SEQRES 10 A 126 LYS ILE ASN GLU LEU PRO THR GLU GLU
HET L40 A 201 26
HETNAM L40 4-ACETYL-3-ETHYL-5-METHYL-N-[2-METHYL-5-
HETNAM 2 L40 (METHYLSULFAMOYL)PHENYL]-1H-PYRROLE-2-CARBOXAMIDE
FORMUL 2 L40 C18 H23 N3 O4 S
FORMUL 3 HOH *62(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
SITE 1 AC1 12 TRP A 81 PRO A 82 VAL A 87 LYS A 91
SITE 2 AC1 12 LEU A 92 ASP A 96 LYS A 99 ASN A 140
SITE 3 AC1 12 ILE A 146 HOH A 316 HOH A 325 HOH A 341
CRYST1 39.080 43.500 79.110 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 0.025589 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END