HEADER TRANSCRIPTION 06-AUG-15 5D3L
TITLE FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD35
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST BROMODOMAIN, UNP RESIDUES 42-168;
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 5D3L 1 REMARK
REVDAT 2 09-MAR-16 5D3L 1 JRNL
REVDAT 1 20-JAN-16 5D3L 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 16718
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1850
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1226
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1062
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.06000
REMARK 3 B22 (A**2) : -1.42000
REMARK 3 B33 (A**2) : 0.36000
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): 0.094
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.741
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1157 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1096 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1585 ; 1.362 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2535 ; 0.791 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 134 ; 4.809 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;38.609 ;26.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 203 ;12.875 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;26.865 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 165 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1318 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 259 ; 0.003 ; 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): 527 ; 0.249 ; 0.671
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 526 ; 0.248 ; 0.671
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 664 ; 0.424 ; 1.007
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 665 ; 0.424 ; 1.008
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 630 ; 0.345 ; 0.729
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 631 ; 0.344 ; 0.730
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 922 ; 0.545 ; 1.083
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5105 ; 3.429 ; 7.347
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4875 ; 3.065 ; 6.627
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 : 7
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 42 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0563 -8.9396 -26.8132
REMARK 3 T TENSOR
REMARK 3 T11: 0.0089 T22: 0.0450
REMARK 3 T33: 0.0296 T12: 0.0084
REMARK 3 T13: 0.0119 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 2.3809 L22: 1.4400
REMARK 3 L33: 5.9882 L12: -0.7764
REMARK 3 L13: 2.9493 L23: -1.1861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: 0.3155 S13: -0.0193
REMARK 3 S21: -0.0591 S22: -0.0640 S23: -0.0991
REMARK 3 S31: 0.0201 S32: 0.4190 S33: 0.0015
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 56 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4623 -1.8666 -27.9674
REMARK 3 T TENSOR
REMARK 3 T11: 0.0154 T22: 0.0316
REMARK 3 T33: 0.0891 T12: -0.0002
REMARK 3 T13: 0.0138 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.1326 L22: 1.0964
REMARK 3 L33: 7.5529 L12: -0.0848
REMARK 3 L13: -1.4073 L23: 1.7270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: -0.0062 S13: 0.2896
REMARK 3 S21: -0.1071 S22: 0.0147 S23: 0.0116
REMARK 3 S31: -0.2935 S32: -0.1693 S33: -0.0925
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 70 A 85
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5106 -1.3127 -10.9506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0707 T22: 0.1041
REMARK 3 T33: 0.0979 T12: -0.0023
REMARK 3 T13: 0.0468 T23: -0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 7.0996 L22: 1.3209
REMARK 3 L33: 2.4568 L12: -1.2192
REMARK 3 L13: 4.1374 L23: -0.5101
REMARK 3 S TENSOR
REMARK 3 S11: -0.1140 S12: -0.2632 S13: 0.3456
REMARK 3 S21: 0.2539 S22: -0.1478 S23: 0.2329
REMARK 3 S31: -0.0387 S32: -0.2125 S33: 0.2617
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 86 A 123
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0885 -9.8267 -18.8271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0267 T22: 0.0161
REMARK 3 T33: 0.0136 T12: -0.0002
REMARK 3 T13: -0.0169 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 2.3694 L22: 1.4991
REMARK 3 L33: 2.6220 L12: -0.3875
REMARK 3 L13: 2.0040 L23: -0.1653
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: -0.0528 S13: 0.0376
REMARK 3 S21: 0.1896 S22: -0.0022 S23: -0.1325
REMARK 3 S31: 0.0590 S32: 0.0508 S33: -0.0111
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 124 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4300 -13.1560 -16.7879
REMARK 3 T TENSOR
REMARK 3 T11: 0.0245 T22: 0.0358
REMARK 3 T33: 0.0299 T12: -0.0207
REMARK 3 T13: 0.0192 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 3.6794 L22: 3.9189
REMARK 3 L33: 6.7999 L12: -2.1651
REMARK 3 L13: 4.7950 L23: -3.0490
REMARK 3 S TENSOR
REMARK 3 S11: 0.1339 S12: -0.1687 S13: -0.0195
REMARK 3 S21: 0.1428 S22: -0.0189 S23: 0.2420
REMARK 3 S31: 0.1460 S32: -0.1501 S33: -0.1150
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 138 A 151
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2294 -14.4884 -3.6263
REMARK 3 T TENSOR
REMARK 3 T11: 0.4653 T22: 0.2404
REMARK 3 T33: 0.0184 T12: -0.0830
REMARK 3 T13: -0.0032 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 4.0861 L22: 7.5426
REMARK 3 L33: 3.9640 L12: -3.8095
REMARK 3 L13: -2.8195 L23: -0.2037
REMARK 3 S TENSOR
REMARK 3 S11: -0.5995 S12: -0.5412 S13: -0.0950
REMARK 3 S21: 1.4963 S22: 0.5104 S23: 0.0689
REMARK 3 S31: -0.1995 S32: 0.3395 S33: 0.0891
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 152 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1584 -7.0266 -15.8596
REMARK 3 T TENSOR
REMARK 3 T11: 0.0657 T22: 0.1146
REMARK 3 T33: 0.1190 T12: -0.0205
REMARK 3 T13: 0.0480 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 3.3349 L22: 0.8182
REMARK 3 L33: 7.1997 L12: -0.2647
REMARK 3 L13: 4.1901 L23: -0.2001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: -0.3121 S13: 0.1860
REMARK 3 S21: 0.1333 S22: -0.0944 S23: 0.1304
REMARK 3 S31: 0.1888 S32: -0.2918 S33: 0.0999
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 5D3L 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_1000212617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-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) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
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) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18300
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, BIS-TRIS, AMMONIUM ACETATE,
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 20.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.16000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.16000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.97000
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: 7940 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 O HOH A 329 O HOH A 455 2.19
REMARK 500 O HOH A 455 O HOH A 458 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 A 94 70.16 -117.37
REMARK 500 LEU A 94 70.16 -117.73
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 57F A 201
DBREF 5D3L A 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQADV 5D3L MET A 43 UNP O60885 THR 43 ENGINEERED MUTATION
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
HET 57F A 201 30
HETNAM 57F 4-ACETYL-N-[5-(DIETHYLSULFAMOYL)-2-HYDROXY-4-
HETNAM 2 57F METHYLPHENYL]-3-ETHYL-5-METHYL-1H-PYRROLE-2-
HETNAM 3 57F CARBOXAMIDE
FORMUL 2 57F C21 H29 N3 O5 S
FORMUL 3 HOH *195(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 LYS A 57 GLN A 59 TRP A 81 PRO A 82
SITE 2 AC1 14 PHE A 83 VAL A 87 LEU A 92 ASN A 117
SITE 3 AC1 14 TYR A 139 ASN A 140 ILE A 146 HOH A 317
SITE 4 AC1 14 HOH A 319 HOH A 340
CRYST1 41.580 47.940 58.320 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 0.024050 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020859 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017147 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
