HEADER TRANSCRIPTION 06-AUG-15 5D3J
TITLE FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD33
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 43-168;
COMPND 5 SYNONYM: PROTEIN HUNK1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 5D3J 1 REMARK
REVDAT 2 09-MAR-16 5D3J 1 JRNL
REVDAT 1 20-JAN-16 5D3J 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 5.8.0073
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) : 32.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11689
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1296
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) : 851
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1055
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.45000
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): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.509
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1147 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1571 ; 1.355 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 133 ; 4.377 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;36.157 ;26.071
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 200 ;13.215 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;11.089 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 163 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 903 ; 0.007 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 523 ; 0.393 ; 0.899
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 659 ; 0.659 ; 1.342
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 624 ; 0.748 ; 1.033
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4997 ; 3.396 ; 9.362
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 9
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 49
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3993 60.5266 7.6339
REMARK 3 T TENSOR
REMARK 3 T11: 0.0385 T22: 0.0638
REMARK 3 T33: 0.0437 T12: -0.0133
REMARK 3 T13: -0.0291 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 12.5708 L22: 7.3062
REMARK 3 L33: 9.1287 L12: -1.6854
REMARK 3 L13: -8.1836 L23: 0.4843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: 0.4228 S13: -0.0573
REMARK 3 S21: 0.0749 S22: -0.0638 S23: 0.1553
REMARK 3 S31: 0.1849 S32: -0.5247 S33: 0.0377
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 50 A 56
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5418 56.9483 -6.1771
REMARK 3 T TENSOR
REMARK 3 T11: 0.1162 T22: 0.2027
REMARK 3 T33: 0.2141 T12: -0.0462
REMARK 3 T13: -0.0223 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 4.4113 L22: 0.0597
REMARK 3 L33: 11.2071 L12: -0.4581
REMARK 3 L13: -3.9817 L23: 0.5273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: 0.4202 S13: 0.7322
REMARK 3 S21: 0.0011 S22: -0.0947 S23: -0.0500
REMARK 3 S31: -0.7724 S32: -0.5671 S33: 0.0413
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 57 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4216 50.3333 2.3599
REMARK 3 T TENSOR
REMARK 3 T11: 0.0426 T22: 0.0330
REMARK 3 T33: 0.0685 T12: -0.0013
REMARK 3 T13: 0.0186 T23: -0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 0.6529 L22: 2.3747
REMARK 3 L33: 8.4189 L12: 0.1285
REMARK 3 L13: 1.5156 L23: -2.2175
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: 0.1363 S13: -0.1465
REMARK 3 S21: -0.1216 S22: 0.0237 S23: -0.0881
REMARK 3 S31: 0.2094 S32: 0.2847 S33: -0.0072
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 70 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0960 51.3738 18.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0544 T22: 0.0047
REMARK 3 T33: 0.0214 T12: 0.0019
REMARK 3 T13: -0.0030 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 7.5937 L22: 2.1331
REMARK 3 L33: 2.5532 L12: -1.2540
REMARK 3 L13: -0.1237 L23: 0.1375
REMARK 3 S TENSOR
REMARK 3 S11: 0.0243 S12: -0.1726 S13: -0.3344
REMARK 3 S21: 0.1453 S22: 0.0048 S23: -0.0144
REMARK 3 S31: 0.2874 S32: 0.0215 S33: -0.0291
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 103
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4991 64.9383 17.3845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0698
REMARK 3 T33: 0.0404 T12: 0.0221
REMARK 3 T13: 0.0078 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 6.6962 L22: 4.7473
REMARK 3 L33: 6.0885 L12: 3.2275
REMARK 3 L13: -4.2758 L23: -2.3069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: 0.0556 S13: 0.0180
REMARK 3 S21: 0.1922 S22: 0.0467 S23: 0.3170
REMARK 3 S31: -0.2137 S32: -0.2861 S33: -0.0613
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 104 A 133
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4467 57.6290 6.0896
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: 0.0427
REMARK 3 T33: 0.0096 T12: -0.0328
REMARK 3 T13: -0.0150 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 2.7250 L22: 0.5660
REMARK 3 L33: 5.0370 L12: -1.0963
REMARK 3 L13: -2.6656 L23: 1.6087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: 0.0949 S13: 0.0042
REMARK 3 S21: -0.0355 S22: 0.0027 S23: 0.0006
REMARK 3 S31: -0.0855 S32: 0.0043 S33: -0.0252
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 134 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9100 65.1614 24.1860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: 0.0560
REMARK 3 T33: 0.0019 T12: -0.0046
REMARK 3 T13: -0.0038 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.4618 L22: 2.8834
REMARK 3 L33: 5.2373 L12: 0.0876
REMARK 3 L13: 1.8401 L23: -0.6588
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.1666 S13: 0.0189
REMARK 3 S21: 0.2063 S22: -0.0240 S23: -0.0093
REMARK 3 S31: -0.0426 S32: -0.0280 S33: 0.0234
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 151 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5240 57.4380 18.3874
REMARK 3 T TENSOR
REMARK 3 T11: 0.0412 T22: 0.0566
REMARK 3 T33: 0.0550 T12: -0.0069
REMARK 3 T13: -0.0376 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 11.5120 L22: 3.8548
REMARK 3 L33: 9.7059 L12: -2.8212
REMARK 3 L13: -7.8916 L23: 1.4535
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.1738 S13: 0.1631
REMARK 3 S21: 0.0421 S22: 0.1168 S23: -0.3046
REMARK 3 S31: -0.0346 S32: 0.3428 S33: -0.1359
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 163 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5806 54.8874 3.7331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.1645
REMARK 3 T33: 0.1861 T12: -0.0000
REMARK 3 T13: 0.0106 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 4.2414 L22: 5.0978
REMARK 3 L33: 8.9820 L12: -0.4712
REMARK 3 L13: 1.0415 L23: 1.3469
REMARK 3 S TENSOR
REMARK 3 S11: -0.2262 S12: 0.2108 S13: -0.0785
REMARK 3 S21: -0.3625 S22: -0.1746 S23: -0.0672
REMARK 3 S31: 0.4583 S32: 0.3307 S33: 0.4008
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5D3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-12
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 : 14195
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 32.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 34.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, HEPES, MAGNESIUM CHLORIDE,
REMARK 280 VAPOR DIFFUSION, 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 19.64500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.07500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.76000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.07500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.64500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.76000
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: 7820 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 OD1 ASP A 96 O HOH A 301 2.15
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 L33 A 201
DBREF 5D3J A 43 168 UNP O60885 BRD4_HUMAN 43 168
SEQADV 5D3J 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 L33 A 201 28
HETNAM L33 4-ACETYL-N-[3-(DIETHYLSULFAMOYL)PHENYL]-3-ETHYL-5-
HETNAM 2 L33 METHYL-1H-PYRROLE-2-CARBOXAMIDE
FORMUL 2 L33 C20 H27 N3 O4 S
FORMUL 3 HOH *148(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 9 PRO A 82 VAL A 87 LYS A 91 LEU A 92
SITE 2 AC1 9 ASN A 117 ASN A 140 HOH A 319 HOH A 353
SITE 3 AC1 9 HOH A 382
CRYST1 39.290 49.520 58.150 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 0.025452 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END