HEADER TRANSCRIPTION/INHIBITOR 08-FEB-18 6CD5
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH THE INHIBITOR XMD17-26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 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 KINASE, INHIBITOR, BRD4, TRANSCRIPTION, TRANSCRIPTION-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XU,S.C.BLACKLOW
REVDAT 5 04-OCT-23 6CD5 1 REMARK
REVDAT 4 21-JUL-21 6CD5 1 REMARK
REVDAT 3 01-JAN-20 6CD5 1 REMARK
REVDAT 2 20-FEB-19 6CD5 1 REMARK
REVDAT 1 16-JAN-19 6CD5 0
JRNL AUTH J.WANG,T.ERAZO,F.M.FERGUSON,D.L.BUCKLEY,N.GOMEZ,
JRNL AUTH 2 P.MUNOZ-GUARDIOLA,N.DIEGUEZ-MARTINEZ,X.DENG,M.HAO,
JRNL AUTH 3 W.MASSEFSKI,O.FEDOROV,N.K.OFFEI-ADDO,P.M.PARK,L.DAI,
JRNL AUTH 4 A.DIBONA,K.BECHT,N.D.KIM,M.R.MCKEOWN,J.M.ROBERTS,J.ZHANG,
JRNL AUTH 5 T.SIM,D.R.ALESSI,J.E.BRADNER,J.M.LIZCANO,S.C.BLACKLOW,J.QI,
JRNL AUTH 6 X.XU,N.S.GRAY
JRNL TITL STRUCTURAL AND ATROPISOMERIC FACTORS GOVERNING THE
JRNL TITL 2 SELECTIVITY OF PYRIMIDO-BENZODIAZIPINONES AS INHIBITORS OF
JRNL TITL 3 KINASES AND BROMODOMAINS.
JRNL REF ACS CHEM. BIOL. V. 13 2438 2018
JRNL REFN ESSN 1554-8937
JRNL PMID 30102854
JRNL DOI 10.1021/ACSCHEMBIO.7B00638
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20429
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1045
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.2817 - 3.0221 1.00 2923 147 0.1630 0.1694
REMARK 3 2 3.0221 - 2.3988 1.00 2815 141 0.1747 0.1967
REMARK 3 3 2.3988 - 2.0956 1.00 2761 141 0.1621 0.1932
REMARK 3 4 2.0956 - 1.9041 1.00 2720 171 0.1546 0.1836
REMARK 3 5 1.9041 - 1.7676 1.00 2724 151 0.1718 0.1948
REMARK 3 6 1.7676 - 1.6634 1.00 2740 133 0.1959 0.2328
REMARK 3 7 1.6634 - 1.5801 1.00 2701 161 0.2363 0.2845
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 1133
REMARK 3 ANGLE : 1.313 1540
REMARK 3 CHIRALITY : 0.071 160
REMARK 3 PLANARITY : 0.010 197
REMARK 3 DIHEDRAL : 7.162 689
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8003 4.5349 -23.1748
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.0814
REMARK 3 T33: 0.0959 T12: -0.0113
REMARK 3 T13: 0.0151 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0087 L22: 0.0627
REMARK 3 L33: 0.0884 L12: -0.0681
REMARK 3 L13: 0.0177 L23: 0.0084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.0288 S13: -0.0005
REMARK 3 S21: -0.0559 S22: 0.0253 S23: -0.0697
REMARK 3 S31: -0.0288 S32: 0.0172 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9463 -12.1474 -21.4471
REMARK 3 T TENSOR
REMARK 3 T11: 0.1312 T22: 0.1070
REMARK 3 T33: 0.0976 T12: -0.0291
REMARK 3 T13: 0.0040 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.0436 L22: 0.0038
REMARK 3 L33: 0.0118 L12: 0.0177
REMARK 3 L13: -0.0277 L23: -0.0079
REMARK 3 S TENSOR
REMARK 3 S11: -0.0192 S12: 0.0460 S13: -0.0923
REMARK 3 S21: -0.2295 S22: 0.0656 S23: -0.0584
REMARK 3 S31: 0.0974 S32: -0.1434 S33: 0.0003
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5562 -6.8003 -13.8584
REMARK 3 T TENSOR
REMARK 3 T11: 0.0969 T22: 0.0897
REMARK 3 T33: 0.1005 T12: -0.0133
REMARK 3 T13: -0.0108 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0041
REMARK 3 L33: 0.0065 L12: -0.0044
REMARK 3 L13: -0.0043 L23: 0.0075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: 0.0104 S13: 0.0008
REMARK 3 S21: 0.0041 S22: -0.0787 S23: -0.0234
REMARK 3 S31: -0.0374 S32: -0.0929 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9577 -0.6703 -5.8388
REMARK 3 T TENSOR
REMARK 3 T11: 0.0850 T22: 0.0909
REMARK 3 T33: 0.0929 T12: -0.0071
REMARK 3 T13: -0.0049 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.0126 L22: 0.0030
REMARK 3 L33: 0.0007 L12: 0.0096
REMARK 3 L13: 0.0058 L23: 0.0021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: 0.0716 S13: 0.0382
REMARK 3 S21: 0.0228 S22: 0.0318 S23: 0.1203
REMARK 3 S31: 0.0477 S32: -0.0913 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7266 11.3736 -7.2844
REMARK 3 T TENSOR
REMARK 3 T11: 0.0686 T22: 0.0650
REMARK 3 T33: 0.0790 T12: -0.0017
REMARK 3 T13: 0.0003 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.0856 L22: 0.1081
REMARK 3 L33: 0.0520 L12: 0.0984
REMARK 3 L13: -0.0485 L23: -0.0870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: -0.0243 S13: 0.0125
REMARK 3 S21: 0.0187 S22: -0.0003 S23: 0.0397
REMARK 3 S31: -0.0094 S32: -0.0133 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4513 -1.9873 -22.0060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.0865
REMARK 3 T33: 0.0837 T12: -0.0091
REMARK 3 T13: -0.0010 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0179 L22: 0.0222
REMARK 3 L33: 0.0729 L12: 0.0161
REMARK 3 L13: -0.0584 L23: -0.0153
REMARK 3 S TENSOR
REMARK 3 S11: -0.0484 S12: 0.0713 S13: 0.0199
REMARK 3 S21: -0.2068 S22: 0.0125 S23: 0.0436
REMARK 3 S31: 0.0059 S32: -0.1058 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7181 -1.9532 -8.8909
REMARK 3 T TENSOR
REMARK 3 T11: 0.0889 T22: 0.0913
REMARK 3 T33: 0.0852 T12: -0.0110
REMARK 3 T13: -0.0058 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.1132 L22: 0.0154
REMARK 3 L33: 0.0568 L12: 0.0273
REMARK 3 L13: 0.0500 L23: -0.0137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: -0.0225 S13: -0.0054
REMARK 3 S21: -0.0230 S22: 0.0439 S23: -0.0418
REMARK 3 S31: 0.0674 S32: -0.0331 S33: 0.0200
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4617 3.4508 6.1773
REMARK 3 T TENSOR
REMARK 3 T11: 0.0844 T22: 0.1601
REMARK 3 T33: 0.1061 T12: -0.0046
REMARK 3 T13: 0.0073 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.0048 L22: 0.0058
REMARK 3 L33: 0.0002 L12: 0.0037
REMARK 3 L13: -0.0016 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0984 S12: -0.0653 S13: -0.1421
REMARK 3 S21: 0.0735 S22: 0.1528 S23: 0.0491
REMARK 3 S31: -0.0215 S32: 0.1284 S33: -0.0004
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1511 -9.9467 -5.7618
REMARK 3 T TENSOR
REMARK 3 T11: 0.0784 T22: 0.0593
REMARK 3 T33: 0.0782 T12: 0.0071
REMARK 3 T13: 0.0166 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.0646 L22: 0.0663
REMARK 3 L33: 0.0592 L12: -0.0751
REMARK 3 L13: 0.0892 L23: -0.0300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: -0.0771 S13: -0.0161
REMARK 3 S21: 0.0306 S22: -0.0303 S23: 0.0887
REMARK 3 S31: 0.0609 S32: 0.0702 S33: -0.0110
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232567.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20478
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 84.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.63400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4WIV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM NITRATE, 5% ETHYLENE
REMARK 280 GLYCOL, 18% (W/V) PEG3350, VAPOR DIFFUSION, TEMPERATURE 295K
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 20.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.43950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.13900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.43950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.13900
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 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 167
REMARK 465 GLU A 168
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 91 CG CD CE NZ
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 434 O HOH A 455 1.78
REMARK 500 O HOH A 417 O HOH A 523 1.91
REMARK 500 NZ LYS A 55 O HOH A 301 1.93
REMARK 500 O HOH A 419 O HOH A 462 1.95
REMARK 500 O HOH A 434 O HOH A 539 2.01
REMARK 500 O HOH A 304 O HOH A 322 2.03
REMARK 500 O HOH A 541 O HOH A 546 2.08
REMARK 500 O HOH A 433 O HOH A 534 2.08
REMARK 500 O HOH A 333 O HOH A 466 2.09
REMARK 500 O HOH A 438 O HOH A 472 2.12
REMARK 500 O HOH A 389 O HOH A 480 2.15
REMARK 500 O THR A 166 O HOH A 302 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 422 O HOH A 431 3644 2.03
REMARK 500 O HOH A 345 O HOH A 357 3654 2.18
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 ASN A 52 112.18 -160.41
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 R4L A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 205
DBREF 6CD5 A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 6CD5 SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 6CD5 MET A 43 UNP O60885 EXPRESSION TAG
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 R4L A 201 46
HET EDO A 202 4
HET EDO A 203 4
HET EDO A 204 4
HET NO3 A 205 4
HETNAM R4L 11-CYCLOPENTYL-2-[[2-METHOXY-4-[4-(4-METHYLPIPERAZIN-1-
HETNAM 2 R4L YL)PIPERIDIN-1-YL]CARBONYL-PHENYL]AMINO]-5-METHYL-
HETNAM 3 R4L PYRIMIDO[4,5-B][1,4]BENZODIAZEPIN-6-ONE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NO3 NITRATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 R4L C35 H44 N8 O3
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 NO3 N O3 1-
FORMUL 7 HOH *249(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 GLU A 163 1 20
SITE 1 AC1 13 TRP A 81 PRO A 82 PHE A 83 LEU A 92
SITE 2 AC1 13 ASP A 96 ILE A 100 TYR A 139 ASN A 140
SITE 3 AC1 13 ILE A 146 HOH A 314 HOH A 323 HOH A 336
SITE 4 AC1 13 HOH A 358
SITE 1 AC2 7 MET A 43 ASN A 52 GLN A 62 ALA A 122
SITE 2 AC2 7 ILE A 126 HOH A 330 HOH A 338
SITE 1 AC3 7 ILE A 100 ILE A 101 LYS A 102 THR A 103
SITE 2 AC3 7 ASN A 135 HOH A 318 HOH A 339
SITE 1 AC4 5 LYS A 57 ASP A 144 ASP A 145 HOH A 342
SITE 2 AC4 5 HOH A 366
SITE 1 AC5 8 PHE A 79 TRP A 81 PRO A 95 ASP A 96
SITE 2 AC5 8 LYS A 99 MET A 149 HOH A 346 HOH A 352
CRYST1 40.120 42.278 84.879 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 0.024925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END