HEADER DNA BINDING PROTEIN 03-FEB-17 5PBB
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF BAZ2B IN
TITLE 2 COMPLEX WITH N09496A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HWALP4;
COMPND 5 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: BAZ2B, KIAA1476;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PANDDA, SGC - DIAMOND I04-1 FRAGMENT SCREENING, BROMODOMAIN,
KEYWDS 2 EPIGENETICS, DNA BINDING PROTEIN
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 M.VOLLMAR,J.NG,P.E.BRENNAN,O.COX,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,
AUTHOR 4 F.VON DELFT
REVDAT 4 06-MAR-24 5PBB 1 REMARK
REVDAT 3 04-OCT-17 5PBB 1 REMARK
REVDAT 2 27-SEP-17 5PBB 1 JRNL REMARK
REVDAT 1 15-MAR-17 5PBB 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. 1.78 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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22203
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1100
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 30.0729 - 3.5650 0.99 2787 143 0.1461 0.1719
REMARK 3 2 3.5650 - 2.8304 1.00 2676 165 0.1717 0.2237
REMARK 3 3 2.8304 - 2.4728 1.00 2677 131 0.1752 0.1932
REMARK 3 4 2.4728 - 2.2468 1.00 2629 139 0.1803 0.2030
REMARK 3 5 2.2468 - 2.0858 1.00 2644 134 0.1910 0.2406
REMARK 3 6 2.0858 - 1.9628 1.00 2662 119 0.2080 0.2460
REMARK 3 7 1.9628 - 1.8645 1.00 2575 150 0.2516 0.2667
REMARK 3 8 1.8645 - 1.7834 0.92 2453 119 0.3222 0.3669
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.15
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 1041
REMARK 3 ANGLE : 1.063 1408
REMARK 3 CHIRALITY : 0.039 149
REMARK 3 PLANARITY : 0.005 183
REMARK 3 DIHEDRAL : 12.463 425
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 5PBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1001400447.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-13
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 0.1.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22220
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 30.069
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.81100
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: 3G0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG600 -- 0.1M MES PH 6.0, PH 7,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 28.98900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.98900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.08750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.46400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.08750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.46400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.98900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.08750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.46400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.98900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.08750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.46400
REMARK 290 SMTRY3 8 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 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 1835
REMARK 465 HIS A 1836
REMARK 465 HIS A 1837
REMARK 465 HIS A 1838
REMARK 465 HIS A 1839
REMARK 465 HIS A 1840
REMARK 465 HIS A 1841
REMARK 465 SER A 1842
REMARK 465 SER A 1843
REMARK 465 GLY A 1844
REMARK 465 VAL A 1845
REMARK 465 ASP A 1846
REMARK 465 LEU A 1847
REMARK 465 GLY A 1848
REMARK 465 THR A 1849
REMARK 465 GLU A 1850
REMARK 465 ASN A 1851
REMARK 465 LEU A 1852
REMARK 465 TYR A 1853
REMARK 465 PHE A 1854
REMARK 465 GLN A 1855
REMARK 465 VAL A 1971
REMARK 465 SER A 1972
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 A1863 CG CD CE NZ
REMARK 470 LYS A1868 CE NZ
REMARK 470 LYS A1970 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 2218 O HOH A 2276 2.10
REMARK 500 O HOH A 2192 O HOH A 2203 2.18
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 2229 O HOH A 2251 4566 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 ASP A1947 58.53 -100.36
REMARK 500 ASP A1947 62.58 -103.54
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 A2298 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A2299 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A2300 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A2301 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH A2302 DISTANCE = 8.12 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 <BAZ2BA-X529> <USED_FOR_STATISTICAL_MAP>YES</USED_FOR_STATISTICAL_
REMARK 600 MAP> <SMILES_OF_COMPOUND_ADDED>C1CCC2C(C1)C(CCN2)O</SMILES_OF_
REMARK 600 COMPOUND_ADDED> <SITE1> <LABEL>NONE</LABEL> <COORDINATE>13.74 37.93
REMARK 600 37.93</COORDINATE> <SMILES>C1CCC2C(C1)C(CCN2)O</SMILES> <CONFIDENCE>
REMARK 600 4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>NONE</COMMENT> <OCCUPANCY>
REMARK 600 0.61</OCCUPANCY> <B_AVERAGE>32.85636363636363</B_AVERAGE> <B_RATIO>
REMARK 600 1.0729803046070092</B_RATIO> <RSCC>0.97499999999999998</RSCC> <RSR>
REMARK 600 0.099000000000000005</RSR> <RSZD>1.2</RSZD> <RMSD>
REMARK 600 0.21645427818699847</RMSD> </SITE1> </BAZ2BA-X529>
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 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ES1 A 2004
DBREF 5PBB A 1858 1972 UNP Q9UIF8 BAZ2B_HUMAN 1954 2068
SEQADV 5PBB MET A 1835 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1836 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1837 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1838 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1839 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1840 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB HIS A 1841 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB SER A 1842 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB SER A 1843 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB GLY A 1844 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB VAL A 1845 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB ASP A 1846 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB LEU A 1847 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB GLY A 1848 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB THR A 1849 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB GLU A 1850 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB ASN A 1851 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB LEU A 1852 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB TYR A 1853 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB PHE A 1854 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB GLN A 1855 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB SER A 1856 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PBB MET A 1857 UNP Q9UIF8 EXPRESSION TAG
SEQRES 1 A 138 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 138 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER VAL LYS
SEQRES 3 A 138 LYS PRO LYS ARG ASP ASP SER LYS ASP LEU ALA LEU CYS
SEQRES 4 A 138 SER MET ILE LEU THR GLU MET GLU THR HIS GLU ASP ALA
SEQRES 5 A 138 TRP PRO PHE LEU LEU PRO VAL ASN LEU LYS LEU VAL PRO
SEQRES 6 A 138 GLY TYR LYS LYS VAL ILE LYS LYS PRO MET ASP PHE SER
SEQRES 7 A 138 THR ILE ARG GLU LYS LEU SER SER GLY GLN TYR PRO ASN
SEQRES 8 A 138 LEU GLU THR PHE ALA LEU ASP VAL ARG LEU VAL PHE ASP
SEQRES 9 A 138 ASN CYS GLU THR PHE ASN GLU ASP ASP SER ASP ILE GLY
SEQRES 10 A 138 ARG ALA GLY HIS ASN MET ARG LYS TYR PHE GLU LYS LYS
SEQRES 11 A 138 TRP THR ASP THR PHE LYS VAL SER
HET EDO A2001 4
HET EDO A2002 10
HET EDO A2003 10
HET ES1 A2004 18
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ES1 QUINOLIN-4-OL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 3(C2 H6 O2)
FORMUL 5 ES1 C9 H7 N O
FORMUL 6 HOH *202(H2 O)
HELIX 1 AA1 LYS A 1868 THR A 1882 1 15
HELIX 2 AA2 HIS A 1883 LEU A 1890 5 8
HELIX 3 AA3 GLY A 1900 ILE A 1905 1 6
HELIX 4 AA4 ASP A 1910 SER A 1920 1 11
HELIX 5 AA5 ASN A 1925 ASN A 1944 1 20
HELIX 6 AA6 SER A 1948 LYS A 1970 1 23
SITE 1 AC1 3 ASN A1944 ES1 A2004 HOH A2104
SITE 1 AC2 2 GLU A1879 THR A1968
SITE 1 AC3 2 HIS A1883 GLU A1884
SITE 1 AC4 9 PRO A1888 TYR A1901 ASN A1944 EDO A2001
SITE 2 AC4 9 HOH A2104 HOH A2190 HOH A2235 HOH A2245
SITE 3 AC4 9 HOH A2249
CRYST1 82.175 96.928 57.978 90.00 90.00 90.00 C 2 2 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 0.012169 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
