HEADER PROTEIN BINDING/INHIBITOR 31-JUL-13 4LYS
TITLE CRYSTAL STRUCTURE OF BRD4(1) BOUND TO COLCHICEINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST BROMODOMAIN DOMAIN (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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BROMODOMAIN, BRD4 INHIBITOR, EPIGENETIC READER PROTEIN, ACETYLATED
KEYWDS 2 LYSINE, HISTONE TAIL, NUCLEUS, PROTEIN BINDING-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WOHLWEND,S.GERHARDT,O.EINSLE
REVDAT 2 29-JAN-14 4LYS 1 HETATM HETNAM HETSYN FORMUL
REVDAT 2 2 1 LINK SITE TITLE REMARK
REVDAT 1 15-JAN-14 4LYS 0
JRNL AUTH X.LUCAS,D.WOHLWEND,M.HUGLE,K.SCHMIDTKUNZ,S.GERHARDT,
JRNL AUTH 2 R.SCHULE,M.JUNG,O.EINSLE,S.GUNTHER
JRNL TITL 4-ACYL PYRROLES: MIMICKING ACETYLATED LYSINES IN HISTONE
JRNL TITL 2 CODE READING.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 52 14055 2013
JRNL REFN ISSN 1433-7851
JRNL PMID 24272870
JRNL DOI 10.1002/ANIE.201307652
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 9566
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 464
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) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 34
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1037
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : -0.28000
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): 0.231
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.507
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1097 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 23 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1495 ; 1.314 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48 ; 1.974 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 123 ; 4.696 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;36.113 ;25.769
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 192 ;17.125 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;22.835 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 156 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 851 ; 0.007 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): 9 ; 0.007 ; 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): 495 ; 0.132 ; 0.575
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 617 ; 0.234 ; 0.862
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 601 ; 0.192 ; 0.621
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): NULL ; NULL ; NULL
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 : 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 43 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2899 34.5894 13.0498
REMARK 3 T TENSOR
REMARK 3 T11: 0.1387 T22: 0.1506
REMARK 3 T33: 0.4575 T12: -0.0299
REMARK 3 T13: 0.1180 T23: 0.1638
REMARK 3 L TENSOR
REMARK 3 L11: 9.2414 L22: 2.7086
REMARK 3 L33: 4.3156 L12: 2.9524
REMARK 3 L13: -1.0332 L23: 2.3714
REMARK 3 S TENSOR
REMARK 3 S11: -0.4560 S12: 0.1679 S13: -0.6886
REMARK 3 S21: -0.0989 S22: 0.0815 S23: 0.1226
REMARK 3 S31: 0.0303 S32: 0.0771 S33: 0.3744
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 59
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6497 25.1561 24.4974
REMARK 3 T TENSOR
REMARK 3 T11: 0.2613 T22: 0.1969
REMARK 3 T33: 0.2102 T12: 0.0344
REMARK 3 T13: 0.0181 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 12.1848 L22: 3.3814
REMARK 3 L33: 1.3029 L12: -5.8618
REMARK 3 L13: 2.0913 L23: -1.7338
REMARK 3 S TENSOR
REMARK 3 S11: 0.2451 S12: 0.0421 S13: -0.1770
REMARK 3 S21: -0.1169 S22: -0.0644 S23: 0.1949
REMARK 3 S31: 0.0472 S32: 0.0617 S33: -0.1808
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 88
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7150 44.0036 17.8180
REMARK 3 T TENSOR
REMARK 3 T11: 0.0697 T22: 0.0851
REMARK 3 T33: 0.0910 T12: 0.0065
REMARK 3 T13: -0.0390 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 2.3726 L22: 4.6850
REMARK 3 L33: 1.7008 L12: -0.0212
REMARK 3 L13: 0.4728 L23: -0.1405
REMARK 3 S TENSOR
REMARK 3 S11: -0.2547 S12: -0.2390 S13: 0.0913
REMARK 3 S21: 0.3060 S22: -0.0023 S23: -0.4804
REMARK 3 S31: -0.1242 S32: 0.0833 S33: 0.2569
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 89 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6848 40.6476 3.7154
REMARK 3 T TENSOR
REMARK 3 T11: 0.1577 T22: 0.1418
REMARK 3 T33: 0.1560 T12: -0.0809
REMARK 3 T13: -0.0397 T23: 0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 8.7127 L22: 6.1238
REMARK 3 L33: 4.1462 L12: -1.9348
REMARK 3 L13: 0.9357 L23: -1.3856
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: 0.4114 S13: -0.1173
REMARK 3 S21: -0.3880 S22: 0.2594 S23: 0.9289
REMARK 3 S31: 0.4570 S32: -0.4518 S33: -0.2667
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 104 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3003 33.6094 19.2697
REMARK 3 T TENSOR
REMARK 3 T11: 0.0777 T22: 0.0588
REMARK 3 T33: 0.0279 T12: 0.0221
REMARK 3 T13: 0.0167 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 5.3398 L22: 3.6245
REMARK 3 L33: 1.2539 L12: -1.4037
REMARK 3 L13: 0.9840 L23: -0.1885
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: -0.2605 S13: -0.2768
REMARK 3 S21: 0.2027 S22: 0.0845 S23: 0.2573
REMARK 3 S31: 0.1865 S32: 0.1077 S33: -0.0729
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 122 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0591 31.4525 13.1318
REMARK 3 T TENSOR
REMARK 3 T11: 0.1323 T22: 0.0750
REMARK 3 T33: 0.1155 T12: 0.0039
REMARK 3 T13: 0.0391 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 5.7205 L22: 12.4304
REMARK 3 L33: 18.7816 L12: -8.3780
REMARK 3 L13: 4.5426 L23: -5.1002
REMARK 3 S TENSOR
REMARK 3 S11: 0.2635 S12: 0.0637 S13: -0.1082
REMARK 3 S21: -0.2949 S22: -0.0583 S23: 0.1327
REMARK 3 S31: 0.6607 S32: 0.1625 S33: -0.2052
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 128 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4703 43.4368 6.8064
REMARK 3 T TENSOR
REMARK 3 T11: 0.0771 T22: 0.0576
REMARK 3 T33: 0.0706 T12: -0.0010
REMARK 3 T13: 0.0332 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.6069 L22: 2.3642
REMARK 3 L33: 2.5468 L12: -0.2191
REMARK 3 L13: 0.7302 L23: -1.2049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: 0.0033 S13: 0.1549
REMARK 3 S21: -0.0580 S22: -0.0921 S23: -0.3412
REMARK 3 S31: 0.0681 S32: 0.2583 S33: 0.1401
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 4LYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 1.54187
REMARK 200 MONOCHROMATOR : VARIMAX VHF FOCUSING MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12331
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 41.047
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
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) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40900
REMARK 200 R SYM FOR SHELL (I) : 0.40900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS TRIS, PEG 3350, NACL, PH 6.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 20.52350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.03600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.52350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.03600
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NA NA A 201 LIES ON A SPECIAL POSITION.
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 167
REMARK 465 GLU A 168
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 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 302 O
REMARK 620 2 2SJ A 203 O6 101.8
REMARK 620 3 2SJ A 203 O5 83.9 68.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 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 2SJ A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LYI RELATED DB: PDB
REMARK 900 RELATED ID: 4LYW RELATED DB: PDB
REMARK 900 RELATED ID: 4LZR RELATED DB: PDB
REMARK 900 RELATED ID: 4LZS RELATED DB: PDB
DBREF 4LYS A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 4LYS 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 NA A 201 1
HET NA A 202 1
HET 2SJ A 203 28
HETNAM NA SODIUM ION
HETNAM 2SJ N-[(7S)-10-HYDROXY-1,2,3-TRIMETHOXY-9-OXO-5,6,7,9-
HETNAM 2 2SJ TETRAHYDROBENZO[A]HEPTALEN-7-YL]ACETAMIDE
HETSYN 2SJ COLCHICEINE
FORMUL 2 NA 2(NA 1+)
FORMUL 4 2SJ C21 H23 N O6
FORMUL 5 HOH *121(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 LYS A 76 1 8
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 88 ASN A 93 1 6
HELIX 5 5 ASP A 96 ILE A 101 1 6
HELIX 6 6 ASP A 106 ASN A 116 1 11
HELIX 7 7 ASN A 121 ASN A 140 1 20
HELIX 8 8 ASP A 144 ASN A 162 1 19
LINK ND2 ASN A 140 C4 2SJ A 203 1555 1555 2.09
LINK NA NA A 201 O HOH A 302 1555 1555 2.01
LINK NA NA A 202 O HOH A 365 1555 1555 2.75
LINK NA NA A 201 O6 2SJ A 203 1555 1555 2.22
LINK NA NA A 201 O5 2SJ A 203 1555 1555 2.33
SITE 1 AC1 2 2SJ A 203 HOH A 302
SITE 1 AC2 2 HIS A 77 HOH A 365
SITE 1 AC3 11 PRO A 82 PHE A 83 LEU A 92 ASN A 140
SITE 2 AC3 11 ILE A 146 NA A 201 HOH A 302 HOH A 320
SITE 3 AC3 11 HOH A 322 HOH A 351 HOH A 379
CRYST1 41.047 108.072 30.464 90.00 90.00 90.00 P 21 21 2 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 0.024362 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009253 0.000000 0.00000
SCALE3 0.000000 0.000000 0.032826 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
