HEADER TRANSCRIPTION/INHIBITOR 08-JUN-16 5KDH
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH A DIHYDROPYRIDOPYRIMIDINE SCAFFOLD INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 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)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BROMODOMAIN, CAP, HUNK1, MCAP, PROTEIN BINDING-INHIBITOR COMPLEX,
KEYWDS 2 MITOTIC CHROMOSOME ASSOCIATED PROTEIN, CELL CYCLE, INHIBITOR,
KEYWDS 3 TRANSCRIPTION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZHU,E.SCHONBRUNN
REVDAT 4 27-SEP-23 5KDH 1 REMARK
REVDAT 3 11-DEC-19 5KDH 1 REMARK
REVDAT 2 13-SEP-17 5KDH 1 REMARK
REVDAT 1 02-AUG-17 5KDH 0
JRNL AUTH A.M.AYOUB,L.M.L.HAWK,R.J.HERZIG,J.JIANG,A.J.WISNIEWSKI,
JRNL AUTH 2 C.T.GEE,P.ZHAO,J.Y.ZHU,N.BERNDT,N.K.OFFEI-ADDO,T.G.SCOTT,
JRNL AUTH 3 J.QI,J.E.BRADNER,T.R.WARD,E.SCHONBRUNN,G.I.GEORG,
JRNL AUTH 4 W.C.K.POMERANTZ
JRNL TITL BET BROMODOMAIN INHIBITORS WITH ONE-STEP SYNTHESIS
JRNL TITL 2 DISCOVERED FROM VIRTUAL SCREEN.
JRNL REF J. MED. CHEM. V. 60 4805 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28535045
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01336
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 20641
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1033
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 38.1478 - 2.8692 1.00 2972 157 0.1589 0.1815
REMARK 3 2 2.8692 - 2.2774 1.00 2843 149 0.1610 0.1944
REMARK 3 3 2.2774 - 1.9896 0.99 2798 148 0.1457 0.1768
REMARK 3 4 1.9896 - 1.8077 0.99 2784 146 0.1534 0.1641
REMARK 3 5 1.8077 - 1.6781 0.99 2748 145 0.1572 0.1813
REMARK 3 6 1.6781 - 1.5791 0.98 2736 144 0.1612 0.1717
REMARK 3 7 1.5791 - 1.5001 0.98 2727 144 0.1835 0.2504
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.54
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 : 0.009 1178
REMARK 3 ANGLE : 1.269 1614
REMARK 3 CHIRALITY : 0.052 165
REMARK 3 PLANARITY : 0.007 210
REMARK 3 DIHEDRAL : 13.538 455
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9734 -7.4044 1.3021
REMARK 3 T TENSOR
REMARK 3 T11: 0.1558 T22: 0.1377
REMARK 3 T33: 0.1595 T12: 0.0392
REMARK 3 T13: 0.0365 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 3.5829 L22: 0.8925
REMARK 3 L33: 5.3511 L12: -1.4218
REMARK 3 L13: 4.3291 L23: -1.5366
REMARK 3 S TENSOR
REMARK 3 S11: -0.1125 S12: -0.0562 S13: -0.2115
REMARK 3 S21: 0.1297 S22: 0.1808 S23: -0.0208
REMARK 3 S31: -0.0111 S32: -0.0693 S33: -0.0403
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4398 -0.0654 -2.7629
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.2104
REMARK 3 T33: 0.2754 T12: -0.0778
REMARK 3 T13: -0.0900 T23: 0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 4.4502 L22: 5.3036
REMARK 3 L33: 2.7417 L12: -3.3674
REMARK 3 L13: 0.1205 L23: 0.2354
REMARK 3 S TENSOR
REMARK 3 S11: 0.1440 S12: -0.2929 S13: -0.3162
REMARK 3 S21: 0.2681 S22: -0.2040 S23: -0.9531
REMARK 3 S31: -0.4296 S32: 0.4566 S33: -0.0171
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9935 3.8926 -15.2873
REMARK 3 T TENSOR
REMARK 3 T11: 0.1693 T22: 0.0638
REMARK 3 T33: 0.1849 T12: -0.0269
REMARK 3 T13: 0.0097 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 7.5845 L22: 1.4176
REMARK 3 L33: 4.1821 L12: -0.7882
REMARK 3 L13: 1.9298 L23: -1.8182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: 0.1066 S13: 0.3747
REMARK 3 S21: -0.0915 S22: 0.1026 S23: -0.2098
REMARK 3 S31: -0.3641 S32: 0.3529 S33: -0.0529
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9844 -3.2800 -16.8699
REMARK 3 T TENSOR
REMARK 3 T11: 0.1391 T22: 0.2859
REMARK 3 T33: 0.1647 T12: 0.0282
REMARK 3 T13: -0.0257 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 3.9727 L22: 1.8211
REMARK 3 L33: 1.2848 L12: -0.7610
REMARK 3 L13: -0.2147 L23: -1.3650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: 0.4563 S13: 0.3317
REMARK 3 S21: -0.1523 S22: 0.1892 S23: 0.4455
REMARK 3 S31: -0.1863 S32: -0.6967 S33: 0.0147
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1046 -8.7003 -8.5616
REMARK 3 T TENSOR
REMARK 3 T11: 0.0778 T22: 0.0746
REMARK 3 T33: 0.0943 T12: 0.0145
REMARK 3 T13: 0.0159 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 1.9327 L22: 2.1827
REMARK 3 L33: 4.7408 L12: 0.3701
REMARK 3 L13: 0.5394 L23: -0.2433
REMARK 3 S TENSOR
REMARK 3 S11: -0.0823 S12: -0.0402 S13: 0.0207
REMARK 3 S21: 0.0062 S22: 0.0012 S23: -0.0788
REMARK 3 S31: 0.0921 S32: 0.0714 S33: 0.0643
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0998 -10.3868 -28.1435
REMARK 3 T TENSOR
REMARK 3 T11: 0.5400 T22: 0.2865
REMARK 3 T33: 0.1927 T12: -0.0190
REMARK 3 T13: -0.0139 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 2.2600 L22: 3.8132
REMARK 3 L33: 1.6290 L12: -2.1271
REMARK 3 L13: -1.9104 L23: 1.9635
REMARK 3 S TENSOR
REMARK 3 S11: 0.0256 S12: 1.0158 S13: -0.1124
REMARK 3 S21: -1.6089 S22: -0.0274 S23: -0.0798
REMARK 3 S31: 0.7825 S32: -0.9551 S33: 0.1184
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2632 -4.4863 -15.6892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1097 T22: 0.1860
REMARK 3 T33: 0.1974 T12: -0.0120
REMARK 3 T13: 0.0447 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 5.3528 L22: 2.4072
REMARK 3 L33: 3.7497 L12: -0.0198
REMARK 3 L13: 3.1120 L23: 0.1809
REMARK 3 S TENSOR
REMARK 3 S11: 0.2684 S12: 0.1196 S13: 0.3672
REMARK 3 S21: -0.0669 S22: -0.2815 S23: -0.4169
REMARK 3 S31: 0.2521 S32: 0.4278 S33: -0.0185
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 5KDH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20642
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 38.135
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.7800
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) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.430
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: 4O7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5 MG/ML BRD4, 5MM HEPES PH 7.5,
REMARK 280 50MM SODIUM CHLORIDE, 0.5MM DTT, 50MM TRIS PH8.5, 0.1M AMMONIUM,
REMARK 280 SULFATE, 12.5% PEG 3,350, 10% DMSO, 1 MM INHIBITOR, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 21.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.28000
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 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 OG1 THR A 103 O HOH A 301 1.98
REMARK 500 O HOH A 301 O HOH A 319 2.09
REMARK 500 O HOH A 374 O HOH A 380 2.10
REMARK 500 OD1 ASN A 130 O HOH A 302 2.14
REMARK 500 OE2 GLU A 168 O HOH A 303 2.16
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 378 O HOH A 382 4545 2.12
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 52 113.57 -163.28
REMARK 500 ASN A 93 76.15 58.86
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 6RX 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 SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KJ0 RELATED DB: PDB
DBREF 5KDH A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5KDH SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 5KDH 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 6RX A 201 42
HET EDO A 202 10
HET SO4 A 203 5
HET SO4 A 204 5
HETNAM 6RX (5~{S})-1-ETHYL-5-(4-METHYLPHENYL)-8,9-DIHYDRO-5~{H}-
HETNAM 2 6RX FURO[3,4]PYRIDO[3,5-~{B}]PYRIMIDINE-2,4,6-TRIONE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 6RX C18 H17 N3 O4
FORMUL 3 EDO C2 H6 O2
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 HOH *96(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 88 ASN A 93 1 6
HELIX 5 AA5 ASP A 96 ILE A 101 1 6
HELIX 6 AA6 ASP A 106 ASN A 116 1 11
HELIX 7 AA7 ASN A 121 ASN A 140 1 20
HELIX 8 AA8 ASP A 144 ASN A 162 1 19
SITE 1 AC1 10 TRP A 81 PRO A 82 VAL A 87 LEU A 92
SITE 2 AC1 10 ASN A 116 ASN A 140 ILE A 146 HOH A 307
SITE 3 AC1 10 HOH A 320 HOH A 342
SITE 1 AC2 6 SER A 51 ASN A 52 LYS A 57 TRP A 81
SITE 2 AC2 6 TYR A 118 HOH A 313
SITE 1 AC3 5 LYS A 57 LYS A 91 LYS A 99 LYS A 102
SITE 2 AC3 5 HOH A 306
SITE 1 AC4 2 ASP A 145 MET A 149
CRYST1 42.120 48.560 61.600 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 0.023742 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020593 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016234 0.00000
(ATOM LINES ARE NOT SHOWN.)
END