HEADER GENE REGULATION 07-FEB-17 5PO8
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF BRD1 IN
TITLE 2 COMPLEX WITH N07808B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BR140-LIKE PROTEIN,BROMODOMAIN AND PHD FINGER-CONTAINING
COMPND 5 PROTEIN 2;
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: BRD1, BRL, BRPF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PANDDA, SGC - DIAMOND I04-1 FRAGMENT SCREENING, BROMODOMAIN,
KEYWDS 2 EPIGENETICS, XCHEMEXPLORER, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.PEARCE,T.KROJER,R.TALON,A.R.BRADLEY,M.FAIRHEAD,R.SETHI,N.WRIGHT,
AUTHOR 2 E.MACLEAN,P.COLLINS,J.BRANDAO-NETO,A.DOUANGAMATH,Z.RENJIE,A.DIAS,
AUTHOR 3 J.NG,P.E.BRENNAN,O.COX,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,F.VON
AUTHOR 4 DELFT
REVDAT 4 06-MAR-24 5PO8 1 LINK
REVDAT 3 04-OCT-17 5PO8 1 REMARK
REVDAT 2 27-SEP-17 5PO8 1 JRNL REMARK
REVDAT 1 15-MAR-17 5PO8 0
JRNL AUTH N.M.PEARCE,T.KROJER,A.R.BRADLEY,P.COLLINS,R.P.NOWAK,R.TALON,
JRNL AUTH 2 B.D.MARSDEN,S.KELM,J.SHI,C.M.DEANE,F.VON DELFT
JRNL TITL A MULTI-CRYSTAL METHOD FOR EXTRACTING OBSCURED
JRNL TITL 2 CRYSTALLOGRAPHIC STATES FROM CONVENTIONALLY UNINTERPRETABLE
JRNL TITL 3 ELECTRON DENSITY.
JRNL REF NAT COMMUN V. 8 15123 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28436492
JRNL DOI 10.1038/NCOMMS15123
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1682
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 50935
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2484
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 28.9384 - 3.9294 0.98 2855 152 0.1652 0.1863
REMARK 3 2 3.9294 - 3.1201 0.99 2749 143 0.1692 0.1751
REMARK 3 3 3.1201 - 2.7260 1.00 2744 146 0.1748 0.1926
REMARK 3 4 2.7260 - 2.4769 1.00 2741 119 0.1824 0.2077
REMARK 3 5 2.4769 - 2.2995 0.99 2693 142 0.1754 0.2227
REMARK 3 6 2.2995 - 2.1639 0.98 2663 125 0.1721 0.2080
REMARK 3 7 2.1639 - 2.0556 0.99 2707 108 0.1808 0.2024
REMARK 3 8 2.0556 - 1.9661 1.00 2684 130 0.1793 0.2077
REMARK 3 9 1.9661 - 1.8905 1.00 2674 139 0.2021 0.2538
REMARK 3 10 1.8905 - 1.8252 1.00 2697 135 0.1858 0.2362
REMARK 3 11 1.8252 - 1.7682 1.00 2674 142 0.1872 0.2238
REMARK 3 12 1.7682 - 1.7176 1.00 2645 156 0.1923 0.2299
REMARK 3 13 1.7176 - 1.6724 1.00 2646 156 0.2017 0.2370
REMARK 3 14 1.6724 - 1.6316 0.99 2624 175 0.2214 0.2437
REMARK 3 15 1.6316 - 1.5945 0.99 2675 141 0.2290 0.3048
REMARK 3 16 1.5945 - 1.5606 1.00 2648 130 0.2358 0.2942
REMARK 3 17 1.5606 - 1.5294 1.00 2660 129 0.2702 0.3053
REMARK 3 18 1.5294 - 1.5005 0.98 2672 116 0.3047 0.3648
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.67
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 : 0.006 2205
REMARK 3 ANGLE : 0.960 2996
REMARK 3 CHIRALITY : 0.037 320
REMARK 3 PLANARITY : 0.004 404
REMARK 3 DIHEDRAL : 13.465 983
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5PO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1001400907.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51008
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 28.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3000
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 : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 1.11800
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 5AMF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 7.0 -- 30% PEG3350,
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 27.63350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.60950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.12200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.60950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.63350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.12200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 VAL A 11
REMARK 465 ASP A 12
REMARK 465 LEU A 13
REMARK 465 GLY A 14
REMARK 465 THR A 15
REMARK 465 GLU A 16
REMARK 465 ASN A 17
REMARK 465 LEU A 18
REMARK 465 TYR A 19
REMARK 465 PHE A 20
REMARK 465 GLN A 21
REMARK 465 GLU A 145
REMARK 465 ALA A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 MET A 149
REMARK 465 HIS A 150
REMARK 465 LEU A 151
REMARK 465 PRO A 152
REMARK 465 GLU A 153
REMARK 465 ARG A 154
REMARK 465 PRO A 155
REMARK 465 ALA A 156
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 VAL B 11
REMARK 465 ASP B 12
REMARK 465 LEU B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 GLU B 16
REMARK 465 ASN B 17
REMARK 465 LEU B 18
REMARK 465 TYR B 19
REMARK 465 PHE B 20
REMARK 465 GLN B 21
REMARK 465 GLU B 145
REMARK 465 ALA B 146
REMARK 465 SER B 147
REMARK 465 GLY B 148
REMARK 465 MET B 149
REMARK 465 HIS B 150
REMARK 465 LEU B 151
REMARK 465 PRO B 152
REMARK 465 GLU B 153
REMARK 465 ARG B 154
REMARK 465 PRO B 155
REMARK 465 ALA B 156
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 GLU A 24 CG CD OE1 OE2
REMARK 470 MET A 28 CE
REMARK 470 LEU A 30 CG CD1 CD2
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 62 CD CE NZ
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 141 CG1 CG2 CD1
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 ARG B 136 NE CZ NH1 NH2
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 ASP A 113 35.02 -93.29
REMARK 500 ASP B 113 59.30 -92.46
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 B 462 DISTANCE = 8.23 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 <BRD1A-X083> <USED_FOR_STATISTICAL_MAP>YES</USED_FOR_STATISTICAL_
REMARK 600 MAP> <SMILES_OF_COMPOUND_ADDED>CN1C(CCC2CC(CCC12)N)=O</SMILES_OF_
REMARK 600 COMPOUND_ADDED> <SITE1> <LABEL>NONE</LABEL> <COORDINATE>-5 12 12</
REMARK 600 COORDINATE> <SMILES>CN1C(CCC2CC(CCC12)N)=O</SMILES> <CONFIDENCE>4 -
REMARK 600 HIGH CONFIDENCE</CONFIDENCE> <COMMENT>NONE</COMMENT> <OCCUPANCY>
REMARK 600 0.99</OCCUPANCY> <B_AVERAGE>22.385384615384613</B_AVERAGE> <B_RATIO>
REMARK 600 1.384948522296429</B_RATIO> <RSCC>0.96099999999999997</RSCC> <RSR>
REMARK 600 0.065000000000000002</RSR> <RSZD>0.40000000000000002</RSZD> <RMSD>
REMARK 600 0.1074175891627552</RMSD> </SITE1> <SITE2> <LABEL>NONE</LABEL> <
REMARK 600 COORDINATE>-30 2.21 2.21</COORDINATE> <SMILES>CN1C(CCC2CC(CCC12)N)=
REMARK 600 O</SMILES> <CONFIDENCE>4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>
REMARK 600 NONE</COMMENT> <OCCUPANCY>0.95</OCCUPANCY> <B_AVERAGE>
REMARK 600 20.993668016194334</B_AVERAGE> <B_RATIO>1.1681152107226629</B_RATIO>
REMARK 600 <RSCC>0.93500000000000005</RSCC> <RSR>0.098000000000000004</RSR> <
REMARK 600 RSZD>1.8</RSZD> <RMSD>0.3007849346677405</RMSD> </SITE2> <SITE4> <
REMARK 600 LABEL>NONE</LABEL> <COORDINATE>-20.32 -12.08 -12.08</COORDINATE> <
REMARK 600 SMILES>CN1C(CCC2CC(CCC12)N)=O</SMILES> <CONFIDENCE>4 - HIGH
REMARK 600 CONFIDENCE</CONFIDENCE> <COMMENT>NONE</COMMENT> <OCCUPANCY>0.69</
REMARK 600 OCCUPANCY> <B_AVERAGE>26.424069119286518</B_AVERAGE> <B_RATIO>
REMARK 600 1.2973953430292597</B_RATIO> <RSCC>0.90600000000000003</RSCC> <RSR>
REMARK 600 0.126</RSR> <RSZD>0.10000000000000001</RSZD> <RMSD>
REMARK 600 0.28707510408360937</RMSD> </SITE4> </BRD1A-X083>
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 B 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 108 O
REMARK 620 2 HOH A 342 O 105.8
REMARK 620 3 HOH A 370 O 75.8 89.8
REMARK 620 4 MET B 107 O 89.1 103.9 162.0
REMARK 620 5 ASN B 110 O 153.1 101.1 102.6 86.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8SY A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8SY B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8SY B 205
DBREF 5PO8 A 23 156 UNP O95696 BRD1_HUMAN 555 688
DBREF 5PO8 B 23 156 UNP O95696 BRD1_HUMAN 555 688
SEQADV 5PO8 MET A 1 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 2 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 3 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 4 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 5 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 6 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS A 7 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER A 8 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER A 9 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLY A 10 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 VAL A 11 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 ASP A 12 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 LEU A 13 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLY A 14 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 THR A 15 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLU A 16 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 ASN A 17 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 LEU A 18 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 TYR A 19 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 PHE A 20 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLN A 21 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER A 22 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 MET A 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5PO8 GLU A 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5PO8 ARG A 37 UNP O95696 VAL 569 ENGINEERED MUTATION
SEQADV 5PO8 MET B 1 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 2 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 3 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 4 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 5 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 6 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 HIS B 7 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER B 8 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER B 9 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLY B 10 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 VAL B 11 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 ASP B 12 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 LEU B 13 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLY B 14 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 THR B 15 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLU B 16 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 ASN B 17 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 LEU B 18 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 TYR B 19 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 PHE B 20 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 GLN B 21 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 SER B 22 UNP O95696 EXPRESSION TAG
SEQADV 5PO8 MET B 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5PO8 GLU B 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5PO8 ARG B 37 UNP O95696 VAL 569 ENGINEERED MUTATION
SEQRES 1 A 156 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 156 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU GLN VAL
SEQRES 3 A 156 ALA MET GLU LEU ARG LEU THR GLU LEU THR ARG LEU LEU
SEQRES 4 A 156 ARG SER VAL LEU ASP GLN LEU GLN ASP LYS ASP PRO ALA
SEQRES 5 A 156 ARG ILE PHE ALA GLN PRO VAL SER LEU LYS GLU VAL PRO
SEQRES 6 A 156 ASP TYR LEU ASP HIS ILE LYS HIS PRO MET ASP PHE ALA
SEQRES 7 A 156 THR MET ARG LYS ARG LEU GLU ALA GLN GLY TYR LYS ASN
SEQRES 8 A 156 LEU HIS GLU PHE GLU GLU ASP PHE ASP LEU ILE ILE ASP
SEQRES 9 A 156 ASN CYS MET LYS TYR ASN ALA ARG ASP THR VAL PHE TYR
SEQRES 10 A 156 ARG ALA ALA VAL ARG LEU ARG ASP GLN GLY GLY VAL VAL
SEQRES 11 A 156 LEU ARG GLN ALA ARG ARG GLU VAL ASP SER ILE GLY LEU
SEQRES 12 A 156 GLU GLU ALA SER GLY MET HIS LEU PRO GLU ARG PRO ALA
SEQRES 1 B 156 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 156 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU GLN VAL
SEQRES 3 B 156 ALA MET GLU LEU ARG LEU THR GLU LEU THR ARG LEU LEU
SEQRES 4 B 156 ARG SER VAL LEU ASP GLN LEU GLN ASP LYS ASP PRO ALA
SEQRES 5 B 156 ARG ILE PHE ALA GLN PRO VAL SER LEU LYS GLU VAL PRO
SEQRES 6 B 156 ASP TYR LEU ASP HIS ILE LYS HIS PRO MET ASP PHE ALA
SEQRES 7 B 156 THR MET ARG LYS ARG LEU GLU ALA GLN GLY TYR LYS ASN
SEQRES 8 B 156 LEU HIS GLU PHE GLU GLU ASP PHE ASP LEU ILE ILE ASP
SEQRES 9 B 156 ASN CYS MET LYS TYR ASN ALA ARG ASP THR VAL PHE TYR
SEQRES 10 B 156 ARG ALA ALA VAL ARG LEU ARG ASP GLN GLY GLY VAL VAL
SEQRES 11 B 156 LEU ARG GLN ALA ARG ARG GLU VAL ASP SER ILE GLY LEU
SEQRES 12 B 156 GLU GLU ALA SER GLY MET HIS LEU PRO GLU ARG PRO ALA
HET 8SY A 201 13
HET NA B 201 1
HET EDO B 202 4
HET EDO B 203 4
HET 8SY B 204 26
HET 8SY B 205 26
HETNAM 8SY 6-AMINO-1-METHYL-3,4-DIHYDROQUINOLIN-2(1H)-ONE
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 8SY 3(C10 H12 N2 O)
FORMUL 4 NA NA 1+
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 9 HOH *280(H2 O)
HELIX 1 AA1 SER A 22 ASP A 48 1 27
HELIX 2 AA2 ASP A 66 ILE A 71 1 6
HELIX 3 AA3 ASP A 76 ALA A 86 1 11
HELIX 4 AA4 ASN A 91 ASN A 110 1 20
HELIX 5 AA5 THR A 114 GLY A 142 1 29
HELIX 6 AA6 MET B 23 LYS B 49 1 27
HELIX 7 AA7 ASP B 66 ILE B 71 1 6
HELIX 8 AA8 ASP B 76 ALA B 86 1 11
HELIX 9 AA9 ASN B 91 ASN B 110 1 20
HELIX 10 AB1 THR B 114 GLY B 142 1 29
LINK O LYS A 108 NA NA B 201 1555 1555 2.35
LINK O HOH A 342 NA NA B 201 1555 1555 2.37
LINK O HOH A 370 NA NA B 201 1555 1555 2.34
LINK O MET B 107 NA NA B 201 1555 1555 2.32
LINK O ASN B 110 NA NA B 201 1555 1555 2.34
SITE 1 AC1 3 ILE A 54 ASN A 110 HOH A 315
SITE 1 AC2 6 LYS A 108 HOH A 342 HOH A 370 MET B 107
SITE 2 AC2 6 ASN B 110 TYR B 117
SITE 1 AC3 5 PHE B 55 ASN B 110 8SY B 204 HOH B 301
SITE 2 AC3 5 HOH B 317
SITE 1 AC4 5 LEU B 92 GLU B 96 LEU B 131 ARG B 135
SITE 2 AC4 5 HOH B 375
SITE 1 AC5 14 GLN B 25 ILE B 54 VAL B 59 SER B 60
SITE 2 AC5 14 VAL B 64 TYR B 109 ASN B 110 PHE B 116
SITE 3 AC5 14 EDO B 202 HOH B 301 HOH B 317 HOH B 320
SITE 4 AC5 14 HOH B 342 HOH B 367
SITE 1 AC6 13 MET B 28 ARG B 31 LEU B 32 LEU B 35
SITE 2 AC6 13 PRO B 51 GLN B 87 TYR B 89 LYS B 90
SITE 3 AC6 13 HOH B 307 HOH B 368 HOH B 431 HOH B 441
SITE 4 AC6 13 HOH B 460
CRYST1 55.267 56.244 101.219 90.00 90.00 90.00 P 21 21 21 8
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 0.018094 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009880 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
