HEADER TRANSCRIPTION 06-AUG-15 5D3T
TITLE FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD47
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 5D3T 1 REMARK
REVDAT 2 09-MAR-16 5D3T 1 JRNL
REVDAT 1 20-JAN-16 5D3T 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. 1.93 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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 9284
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1006
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 677
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.2480
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 : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.93000
REMARK 3 B22 (A**2) : -1.14000
REMARK 3 B33 (A**2) : 0.21000
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): 0.191
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.208
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1141 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1089 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1556 ; 1.325 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2514 ; 0.763 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 130 ; 5.597 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;39.479 ;25.636
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 201 ;14.312 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;26.889 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 161 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1289 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 255 ; 0.001 ; 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): 517 ; 0.582 ; 1.203
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 516 ; 0.576 ; 1.198
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 648 ; 0.991 ; 1.794
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 649 ; 0.993 ; 1.800
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 624 ; 0.655 ; 1.316
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 624 ; 0.638 ; 1.316
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 909 ; 1.051 ; 1.946
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5018 ; 4.318 ;12.371
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4806 ; 3.939 ;11.603
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 49
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5918 11.0875 -13.3151
REMARK 3 T TENSOR
REMARK 3 T11: 0.0546 T22: 0.0280
REMARK 3 T33: 0.0498 T12: -0.0267
REMARK 3 T13: 0.0032 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 3.1700 L22: 5.9000
REMARK 3 L33: 5.3864 L12: 0.9758
REMARK 3 L13: 1.2966 L23: 3.1232
REMARK 3 S TENSOR
REMARK 3 S11: 0.0498 S12: 0.0363 S13: 0.1860
REMARK 3 S21: -0.1188 S22: 0.0701 S23: -0.3788
REMARK 3 S31: -0.2698 S32: 0.0343 S33: -0.1199
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 63
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9723 -7.7120 -25.1008
REMARK 3 T TENSOR
REMARK 3 T11: 0.2487 T22: 0.0492
REMARK 3 T33: 0.0499 T12: 0.0561
REMARK 3 T13: 0.0356 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 1.2851 L22: 1.2849
REMARK 3 L33: 5.2643 L12: 0.0479
REMARK 3 L13: -1.6484 L23: -2.0040
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: 0.1176 S13: -0.1733
REMARK 3 S21: -0.3163 S22: -0.0072 S23: 0.0690
REMARK 3 S31: 0.2652 S32: -0.2478 S33: 0.0138
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 64 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0952 -9.3034 -9.2888
REMARK 3 T TENSOR
REMARK 3 T11: 0.1558 T22: 0.2134
REMARK 3 T33: 0.2869 T12: -0.1241
REMARK 3 T13: 0.0661 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 1.1415 L22: 1.1331
REMARK 3 L33: 3.0615 L12: -0.3624
REMARK 3 L13: -1.1789 L23: 1.6602
REMARK 3 S TENSOR
REMARK 3 S11: -0.1908 S12: 0.1088 S13: -0.2365
REMARK 3 S21: 0.3221 S22: -0.2987 S23: 0.4048
REMARK 3 S31: 0.5954 S32: -0.6122 S33: 0.4896
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 81 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0693 5.5818 -6.7874
REMARK 3 T TENSOR
REMARK 3 T11: 0.0691 T22: 0.0152
REMARK 3 T33: 0.0162 T12: 0.0246
REMARK 3 T13: -0.0248 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.1756 L22: 4.6410
REMARK 3 L33: 2.7169 L12: 0.0052
REMARK 3 L13: -0.7380 L23: 1.3767
REMARK 3 S TENSOR
REMARK 3 S11: -0.1641 S12: -0.1245 S13: 0.0765
REMARK 3 S21: 0.0274 S22: 0.0665 S23: 0.1701
REMARK 3 S31: -0.1817 S32: 0.0548 S33: 0.0976
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 114 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0663 -8.4469 -19.3734
REMARK 3 T TENSOR
REMARK 3 T11: 0.0617 T22: 0.0456
REMARK 3 T33: 0.0695 T12: -0.0203
REMARK 3 T13: 0.0279 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.0545 L22: 3.5231
REMARK 3 L33: 5.6270 L12: 0.3261
REMARK 3 L13: -1.8775 L23: 2.2136
REMARK 3 S TENSOR
REMARK 3 S11: -0.1367 S12: 0.1490 S13: 0.0596
REMARK 3 S21: -0.1705 S22: 0.0901 S23: 0.2342
REMARK 3 S31: 0.1049 S32: -0.2132 S33: 0.0466
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 128 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9383 -1.6653 0.4776
REMARK 3 T TENSOR
REMARK 3 T11: 0.0416 T22: 0.0511
REMARK 3 T33: 0.0102 T12: 0.0285
REMARK 3 T13: 0.0028 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 2.5403 L22: 4.6813
REMARK 3 L33: 6.3795 L12: 0.6807
REMARK 3 L13: 0.0233 L23: 0.7428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0980 S12: -0.3159 S13: -0.0880
REMARK 3 S21: 0.3602 S22: 0.0320 S23: -0.0911
REMARK 3 S31: 0.1673 S32: 0.1821 S33: 0.0661
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 149 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8702 -14.3358 -5.2626
REMARK 3 T TENSOR
REMARK 3 T11: 0.0587 T22: 0.0656
REMARK 3 T33: 0.0792 T12: 0.0011
REMARK 3 T13: 0.0171 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.7218 L22: 5.5347
REMARK 3 L33: 8.1392 L12: 0.1411
REMARK 3 L13: 0.0986 L23: 4.5489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0829 S12: 0.0234 S13: -0.1205
REMARK 3 S21: 0.2672 S22: -0.0555 S23: 0.0553
REMARK 3 S31: 0.4741 S32: -0.0705 S33: -0.0273
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 5D3T 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_1000212627.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-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
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12248
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 13.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 (%): 43.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SUCCINIC ACID, VAPOR
REMARK 280 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 19.22000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.36500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.22000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.36500
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: 260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 OE2 GLU A 168 O HOH A 301 1.99
REMARK 500 O PRO A 142 O HOH A 302 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 LEU A 94 68.30 -119.82
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 496 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 497 DISTANCE = 7.26 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 138 O
REMARK 620 2 ASN A 140 O 91.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 56Y A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA 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
DBREF 5D3T A 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQADV 5D3T 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 56Y A 201 25
HET NA A 202 1
HET EDO A 203 4
HETNAM 56Y 4-ACETYL-N-(3-CARBAMOYLBENZYL)-3-ETHYL-N,5-DIMETHYL-1H-
HETNAM 2 56Y PYRROLE-2-CARBOXAMIDE
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 56Y C19 H23 N3 O3
FORMUL 3 NA NA 1+
FORMUL 4 EDO C2 H6 O2
FORMUL 5 HOH *197(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
LINK O ILE A 138 NA NA A 202 1555 1555 3.03
LINK O ASN A 140 NA NA A 202 1555 1555 2.68
SITE 1 AC1 16 TRP A 81 PRO A 82 PHE A 83 VAL A 87
SITE 2 AC1 16 LYS A 91 LEU A 92 LEU A 94 ASP A 96
SITE 3 AC1 16 ILE A 100 TYR A 139 ASN A 140 HOH A 305
SITE 4 AC1 16 HOH A 312 HOH A 320 HOH A 397 HOH A 398
SITE 1 AC2 4 TYR A 137 ILE A 138 ASN A 140 GLU A 163
SITE 1 AC3 6 ARG A 58 GLN A 59 LYS A 102 THR A 103
SITE 2 AC3 6 HOH A 328 HOH A 425
CRYST1 38.440 42.730 79.500 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 0.026015 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012579 0.00000
(ATOM LINES ARE NOT SHOWN.)
END