HEADER TRANSCRIPTION 06-AUG-15 5D3H
TITLE FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD29
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,G.WEITZEL
REVDAT 3 06-SEP-17 5D3H 1 REMARK
REVDAT 2 09-MAR-16 5D3H 1 JRNL
REVDAT 1 20-JAN-16 5D3H 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. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 10137
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1115
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 610
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.22000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : -0.09000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.612
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1151 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1089 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1577 ; 1.314 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2520 ; 0.767 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 134 ; 4.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;35.911 ;26.071
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 202 ;14.376 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;12.117 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 162 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1320 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 261 ; 0.004 ; 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): 524 ; 0.421 ; 0.580
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 523 ; 0.417 ; 0.579
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 662 ; 0.523 ; 0.870
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 663 ; 0.523 ; 0.870
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 627 ; 0.558 ; 0.670
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 625 ; 0.556 ; 0.666
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 916 ; 0.686 ; 0.993
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5019 ; 1.297 ; 6.282
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4890 ; 0.979 ; 5.911
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2240 ; 1.377 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 18 ;13.536 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2332 ; 3.128 ; 5.000
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 : 10
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): 0.6209 59.0922 6.7226
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.3692
REMARK 3 T33: 0.0454 T12: -0.0154
REMARK 3 T13: -0.0248 T23: 0.0941
REMARK 3 L TENSOR
REMARK 3 L11: 5.4240 L22: 7.7861
REMARK 3 L33: 6.6985 L12: -2.0584
REMARK 3 L13: -0.9461 L23: 5.0531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: 0.7422 S13: 0.0910
REMARK 3 S21: -0.0459 S22: 0.0559 S23: 0.2509
REMARK 3 S31: 0.0592 S32: -0.8261 S33: -0.0839
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 61
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3386 54.1199 -5.8058
REMARK 3 T TENSOR
REMARK 3 T11: 0.1118 T22: 0.0650
REMARK 3 T33: 0.0992 T12: -0.0506
REMARK 3 T13: 0.0087 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 4.7699 L22: 0.8427
REMARK 3 L33: 5.2562 L12: 1.7952
REMARK 3 L13: 3.1574 L23: 1.9151
REMARK 3 S TENSOR
REMARK 3 S11: -0.1474 S12: 0.1062 S13: 0.2522
REMARK 3 S21: -0.0376 S22: -0.0214 S23: 0.0994
REMARK 3 S31: -0.0152 S32: -0.2143 S33: 0.1687
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 62 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6718 49.7011 9.2058
REMARK 3 T TENSOR
REMARK 3 T11: 0.0686 T22: 0.0144
REMARK 3 T33: 0.0814 T12: 0.0150
REMARK 3 T13: 0.0142 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 4.3013 L22: 0.3369
REMARK 3 L33: 6.1843 L12: 1.1928
REMARK 3 L13: -1.8308 L23: -0.5852
REMARK 3 S TENSOR
REMARK 3 S11: -0.0849 S12: -0.0679 S13: -0.0943
REMARK 3 S21: -0.0391 S22: -0.0272 S23: -0.0425
REMARK 3 S31: 0.2198 S32: 0.1794 S33: 0.1121
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 76 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3041 52.8958 19.8013
REMARK 3 T TENSOR
REMARK 3 T11: 0.0756 T22: 0.0332
REMARK 3 T33: 0.0296 T12: -0.0126
REMARK 3 T13: 0.0121 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 6.7689 L22: 2.6427
REMARK 3 L33: 2.0495 L12: -3.3234
REMARK 3 L13: 0.7704 L23: -0.4352
REMARK 3 S TENSOR
REMARK 3 S11: -0.1327 S12: -0.2088 S13: -0.0602
REMARK 3 S21: 0.2277 S22: 0.0065 S23: 0.0106
REMARK 3 S31: 0.1300 S32: -0.0558 S33: 0.1262
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 90 A 96
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7383 61.0989 20.9740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1359 T22: 0.1944
REMARK 3 T33: 0.0628 T12: 0.0337
REMARK 3 T13: 0.0501 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 6.6294 L22: 6.5700
REMARK 3 L33: 1.7525 L12: 3.3170
REMARK 3 L13: -1.3876 L23: -1.1885
REMARK 3 S TENSOR
REMARK 3 S11: 0.1172 S12: 0.0207 S13: -0.0030
REMARK 3 S21: 0.3134 S22: -0.0885 S23: -0.0641
REMARK 3 S31: 0.1404 S32: -0.2025 S33: -0.0287
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 97 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3424 60.5287 10.9444
REMARK 3 T TENSOR
REMARK 3 T11: 0.0333 T22: 0.0264
REMARK 3 T33: 0.0191 T12: -0.0129
REMARK 3 T13: -0.0149 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 2.3693 L22: 0.9529
REMARK 3 L33: 3.2959 L12: -0.0918
REMARK 3 L13: -1.5787 L23: 1.5189
REMARK 3 S TENSOR
REMARK 3 S11: 0.0847 S12: -0.0269 S13: 0.0759
REMARK 3 S21: 0.0071 S22: -0.1044 S23: 0.0465
REMARK 3 S31: -0.0310 S32: -0.1568 S33: 0.0197
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 115 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9914 60.7002 8.9956
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: 0.0124
REMARK 3 T33: 0.0162 T12: -0.0070
REMARK 3 T13: -0.0168 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.0502 L22: 2.2742
REMARK 3 L33: 5.5996 L12: -1.3023
REMARK 3 L13: -2.5030 L23: 2.7374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: -0.0454 S13: 0.0605
REMARK 3 S21: -0.0210 S22: 0.0563 S23: -0.0677
REMARK 3 S31: -0.1579 S32: -0.0077 S33: -0.0949
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 141 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0978 61.7096 26.3315
REMARK 3 T TENSOR
REMARK 3 T11: 0.1387 T22: 0.0756
REMARK 3 T33: 0.0468 T12: 0.0063
REMARK 3 T13: -0.0325 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 3.2666 L22: 4.6123
REMARK 3 L33: 8.7018 L12: -2.1401
REMARK 3 L13: -4.0492 L23: 6.0896
REMARK 3 S TENSOR
REMARK 3 S11: 0.2082 S12: -0.0483 S13: 0.0843
REMARK 3 S21: 0.0257 S22: -0.0594 S23: -0.0941
REMARK 3 S31: -0.0640 S32: -0.0466 S33: -0.1487
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 154 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2812 56.5148 17.4436
REMARK 3 T TENSOR
REMARK 3 T11: 0.0787 T22: 0.0805
REMARK 3 T33: 0.0816 T12: 0.0000
REMARK 3 T13: -0.0219 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 6.4268 L22: 2.5046
REMARK 3 L33: 3.2636 L12: -0.6351
REMARK 3 L13: -1.7250 L23: 1.3692
REMARK 3 S TENSOR
REMARK 3 S11: 0.0383 S12: -0.1253 S13: 0.0840
REMARK 3 S21: 0.0564 S22: -0.0180 S23: -0.2267
REMARK 3 S31: 0.0405 S32: 0.0714 S33: -0.0203
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 162 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4146 54.8826 6.7891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1047 T22: 0.1490
REMARK 3 T33: 0.1711 T12: 0.0059
REMARK 3 T13: 0.0154 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 3.5746 L22: 1.8261
REMARK 3 L33: 12.4034 L12: -0.1806
REMARK 3 L13: 0.2588 L23: 1.6823
REMARK 3 S TENSOR
REMARK 3 S11: -0.2292 S12: -0.0495 S13: -0.0974
REMARK 3 S21: -0.1399 S22: -0.1831 S23: -0.1720
REMARK 3 S31: 0.4641 S32: 0.4023 S33: 0.4123
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 5D3H 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_1000212611.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.0.9
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11275
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 27.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26600
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: IN-HOUSE MODEL OF APO-BRD4(1)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, BIS-TRIS, VAPOR DIFFUSION,
REMARK 280 SITTING 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 19.67500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.98000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.98000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.67500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.54500
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: 7570 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 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 GLU A 168
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 A 94 71.76 -117.13
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 A 446 DISTANCE = 6.52 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 57G A 201
DBREF 5D3H A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5D3H MET A 43 UNP O60885 INITIATING METHIONINE
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 57G A 201 30
HETNAM 57G N-[5-(DIETHYLSULFAMOYL)-2-HYDROXYPHENYL]-3-ETHYL-4-
HETNAM 2 57G (HYDROXYACETYL)-5-METHYL-1H-PYRROLE-2-CARBOXAMIDE
FORMUL 2 57G C20 H27 N3 O6 S
FORMUL 3 HOH *146(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 16 GLN A 59 PRO A 82 PHE A 83 GLN A 85
SITE 2 AC1 16 VAL A 87 LYS A 91 LEU A 92 TYR A 97
SITE 3 AC1 16 ASN A 117 TYR A 139 ASN A 140 ILE A 146
SITE 4 AC1 16 HOH A 306 HOH A 314 HOH A 324 HOH A 382
CRYST1 39.350 49.090 57.960 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 0.025413 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017253 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
