HEADER GENE REGULATION 07-FEB-17 5POP
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF BRD1 IN
TITLE 2 COMPLEX WITH N10987A
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 5POP 1 LINK
REVDAT 3 04-OCT-17 5POP 1 REMARK
REVDAT 2 27-SEP-17 5POP 1 JRNL REMARK
REVDAT 1 15-MAR-17 5POP 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. 1.58 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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 44774
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2211
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 29.0904 - 3.9754 1.00 2844 152 0.1666 0.1984
REMARK 3 2 3.9754 - 3.1566 1.00 2716 143 0.1762 0.1953
REMARK 3 3 3.1566 - 2.7580 1.00 2702 148 0.1988 0.2231
REMARK 3 4 2.7580 - 2.5059 1.00 2700 114 0.2051 0.2522
REMARK 3 5 2.5059 - 2.3264 1.00 2650 143 0.2116 0.2687
REMARK 3 6 2.3264 - 2.1893 1.00 2671 122 0.2090 0.2553
REMARK 3 7 2.1893 - 2.0797 1.00 2677 104 0.2215 0.2486
REMARK 3 8 2.0797 - 1.9892 1.00 2654 127 0.2261 0.3053
REMARK 3 9 1.9892 - 1.9126 1.00 2669 136 0.2471 0.3087
REMARK 3 10 1.9126 - 1.8466 1.00 2613 137 0.2451 0.2947
REMARK 3 11 1.8466 - 1.7889 1.00 2633 140 0.2394 0.3114
REMARK 3 12 1.7889 - 1.7378 1.00 2619 145 0.2624 0.2785
REMARK 3 13 1.7378 - 1.6920 1.00 2610 150 0.2817 0.3457
REMARK 3 14 1.6920 - 1.6508 1.00 2572 181 0.3071 0.3069
REMARK 3 15 1.6508 - 1.6132 1.00 2622 138 0.3242 0.4278
REMARK 3 16 1.6132 - 1.5789 0.99 2611 131 0.3667 0.3758
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.23
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 : 0.007 2189
REMARK 3 ANGLE : 0.985 2971
REMARK 3 CHIRALITY : 0.036 322
REMARK 3 PLANARITY : 0.004 405
REMARK 3 DIHEDRAL : 14.786 912
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 5POP 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_1001400924.
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 : 44837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 29.086
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
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) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.72400
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 (%): 43.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
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 27.80750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.86500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.28750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.86500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.80750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.28750
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 LEU A 143
REMARK 465 GLU A 144
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 MET A 28 CE
REMARK 470 LEU A 30 CG CD1 CD2
REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 62 CD CE NZ
REMARK 470 LYS A 82 CG 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: 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 OD2 ASP B 48 O HOH B 301 2.15
REMARK 500 O HOH B 327 O HOH B 449 2.19
REMARK 500 OE1 GLN A 126 O HOH A 301 2.19
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 SD MET A 23 O HOH B 313 1655 2.19
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 ASP A 113 42.33 -95.73
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 417 DISTANCE = 5.96 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 <BRD1A-X261> <USED_FOR_STATISTICAL_MAP>YES</USED_FOR_STATISTICAL_
REMARK 600 MAP> <SMILES_OF_COMPOUND_ADDED>CC(N1CCN(CC1)C1CCNCC1)=O</SMILES_OF_
REMARK 600 COMPOUND_ADDED> <SITE1> <LABEL>NONE</LABEL> <COORDINATE>-7.94 14.67
REMARK 600 14.67</COORDINATE> <SMILES>CC(N1CCN(CC1)C1CCNCC1)=O</SMILES> <
REMARK 600 CONFIDENCE>4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>NONE</COMMENT>
REMARK 600 <OCCUPANCY>0.74</OCCUPANCY> <B_AVERAGE>30.199333333333325</B_
REMARK 600 AVERAGE> <B_RATIO>1.1709716923740339</B_RATIO> <RSCC>
REMARK 600 0.89000000000000001</RSCC> <RSR>0.121</RSR> <RSZD>1.0</RSZD> <RMSD>
REMARK 600 0.2300996885410033</RMSD> </SITE1> <SITE2> <LABEL>NONE</LABEL> <
REMARK 600 COORDINATE>-32 4 4</COORDINATE> <SMILES>CC(N1CCN(CC1)C1CCNCC1)=O</
REMARK 600 SMILES> <CONFIDENCE>4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>NONE</
REMARK 600 COMMENT> <OCCUPANCY>1.0</OCCUPANCY> <B_AVERAGE>32.18466666666667</B_
REMARK 600 AVERAGE> <B_RATIO>1.3300059690527575</B_RATIO> <RSCC>
REMARK 600 0.95099999999999996</RSCC> <RSR>0.074999999999999997</RSR> <RSZD>
REMARK 600 0.29999999999999999</RSZD> <RMSD>0.23612524924991263</RMSD> </SITE2>
REMARK 600 </BRD1A-X261>
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 100.7
REMARK 620 3 HOH A 372 O 77.0 90.7
REMARK 620 4 MET B 107 O 87.1 102.9 160.8
REMARK 620 5 ASN B 110 O 156.2 103.0 100.7 89.6
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 EDO 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 8TV A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8TV B 203
DBREF 5POP A 23 156 UNP O95696 BRD1_HUMAN 555 688
DBREF 5POP B 23 156 UNP O95696 BRD1_HUMAN 555 688
SEQADV 5POP MET A 1 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 2 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 3 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 4 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 5 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 6 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS A 7 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER A 8 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER A 9 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLY A 10 UNP O95696 EXPRESSION TAG
SEQADV 5POP VAL A 11 UNP O95696 EXPRESSION TAG
SEQADV 5POP ASP A 12 UNP O95696 EXPRESSION TAG
SEQADV 5POP LEU A 13 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLY A 14 UNP O95696 EXPRESSION TAG
SEQADV 5POP THR A 15 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLU A 16 UNP O95696 EXPRESSION TAG
SEQADV 5POP ASN A 17 UNP O95696 EXPRESSION TAG
SEQADV 5POP LEU A 18 UNP O95696 EXPRESSION TAG
SEQADV 5POP TYR A 19 UNP O95696 EXPRESSION TAG
SEQADV 5POP PHE A 20 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLN A 21 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER A 22 UNP O95696 EXPRESSION TAG
SEQADV 5POP MET A 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5POP GLU A 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5POP ARG A 37 UNP O95696 VAL 569 ENGINEERED MUTATION
SEQADV 5POP MET B 1 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 2 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 3 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 4 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 5 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 6 UNP O95696 EXPRESSION TAG
SEQADV 5POP HIS B 7 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER B 8 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER B 9 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLY B 10 UNP O95696 EXPRESSION TAG
SEQADV 5POP VAL B 11 UNP O95696 EXPRESSION TAG
SEQADV 5POP ASP B 12 UNP O95696 EXPRESSION TAG
SEQADV 5POP LEU B 13 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLY B 14 UNP O95696 EXPRESSION TAG
SEQADV 5POP THR B 15 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLU B 16 UNP O95696 EXPRESSION TAG
SEQADV 5POP ASN B 17 UNP O95696 EXPRESSION TAG
SEQADV 5POP LEU B 18 UNP O95696 EXPRESSION TAG
SEQADV 5POP TYR B 19 UNP O95696 EXPRESSION TAG
SEQADV 5POP PHE B 20 UNP O95696 EXPRESSION TAG
SEQADV 5POP GLN B 21 UNP O95696 EXPRESSION TAG
SEQADV 5POP SER B 22 UNP O95696 EXPRESSION TAG
SEQADV 5POP MET B 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5POP GLU B 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5POP 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 EDO A 201 4
HET EDO A 202 4
HET 8TV A 203 15
HET NA B 201 1
HET EDO B 202 4
HET 8TV B 203 15
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 8TV 1-[4-(PYRIDIN-4-YL)PIPERAZIN-1-YL]ETHAN-1-ONE
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 5 8TV 2(C11 H15 N3 O)
FORMUL 6 NA NA 1+
FORMUL 9 HOH *269(H2 O)
HELIX 1 AA1 SER A 22 LYS A 49 1 28
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 ILE A 141 1 28
HELIX 6 AA6 MET B 23 ASP B 48 1 26
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 2.34
LINK O HOH A 342 NA NA B 201 1555 1555 2.34
LINK O HOH A 372 NA NA B 201 1555 1555 2.36
LINK O MET B 107 NA NA B 201 1555 1555 2.36
LINK O ASN B 110 NA NA B 201 1555 1555 2.35
SITE 1 AC1 5 TYR A 109 ASN A 110 EDO A 202 8TV A 203
SITE 2 AC1 5 MET B 23
SITE 1 AC2 7 ILE A 54 PHE A 55 PHE A 116 EDO A 201
SITE 2 AC2 7 8TV A 203 HOH A 308 HOH A 347
SITE 1 AC3 10 VAL A 59 GLU A 63 VAL A 64 ASN A 110
SITE 2 AC3 10 EDO A 201 EDO A 202 HOH A 315 HOH A 322
SITE 3 AC3 10 MET B 23 VAL B 26
SITE 1 AC4 6 LYS A 108 HOH A 342 HOH A 372 MET B 107
SITE 2 AC4 6 ASN B 110 TYR B 117
SITE 1 AC5 5 LEU B 92 GLU B 96 LEU B 131 ARG B 135
SITE 2 AC5 5 HOH B 334
SITE 1 AC6 5 LYS A 62 ASN B 110 PHE B 116 HOH B 314
SITE 2 AC6 5 HOH B 413
CRYST1 55.615 56.575 101.730 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 0.017981 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009830 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
