HEADER TRANSCRIPTION 25-JAN-15 4XUB
TITLE CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BAZ2B IN COMPLEX WITH
TITLE 2 BAZ2-ICR CHEMICAL PROBE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1858-1972;
COMPND 5 SYNONYM: HWALP4;
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: BAZ2B, KIAA1476;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: R3;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSCRIPTION, BROMODOMAIN, ACETYLATED LYSINE BINDING PROTEIN,
KEYWDS 2 KIAA1476, WALP4, SGC, STRUCTURAL GENOMICS CONSORTIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,I.FELLETAR,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 C.BOUNTRA,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 10-JAN-24 4XUB 1 REMARK
REVDAT 2 25-MAR-15 4XUB 1 JRNL
REVDAT 1 11-MAR-15 4XUB 0
JRNL AUTH L.DROUIN,S.MCGRATH,L.R.VIDLER,A.CHAIKUAD,O.MONTEIRO,
JRNL AUTH 2 C.TALLANT,M.PHILPOTT,C.ROGERS,O.FEDOROV,M.LIU,W.AKHTAR,
JRNL AUTH 3 A.HAYES,F.RAYNAUD,S.MULLER,S.KNAPP,S.HOELDER
JRNL TITL STRUCTURE ENABLED DESIGN OF BAZ2-ICR, A CHEMICAL PROBE
JRNL TITL 2 TARGETING THE BROMODOMAINS OF BAZ2A AND BAZ2B.
JRNL REF J.MED.CHEM. V. 58 2553 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25719566
JRNL DOI 10.1021/JM501963E
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15385
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 814
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1110
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 943
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.29000
REMARK 3 B22 (A**2) : -0.61000
REMARK 3 B33 (A**2) : -1.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.228
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1017 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 971 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1366 ; 1.543 ; 2.022
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2252 ; 0.831 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 119 ; 5.871 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 44 ;32.561 ;24.545
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 188 ;15.587 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;18.731 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 144 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1098 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 218 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 467 ; 1.749 ; 2.555
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 466 ; 1.749 ; 2.545
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 583 ; 2.727 ; 3.810
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 584 ; 2.725 ; 3.822
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 550 ; 2.130 ; 2.885
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 550 ; 2.114 ; 2.885
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 782 ; 3.232 ; 4.174
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1357 ; 8.231 ;23.806
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1358 ; 8.228 ;23.842
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1856 A 1863
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6565 15.0737 11.0494
REMARK 3 T TENSOR
REMARK 3 T11: 0.2836 T22: 0.4947
REMARK 3 T33: 0.2712 T12: 0.1287
REMARK 3 T13: -0.1160 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 22.8679 L22: 22.1324
REMARK 3 L33: 23.9700 L12: -10.2117
REMARK 3 L13: -20.0860 L23: 19.5109
REMARK 3 S TENSOR
REMARK 3 S11: -0.2703 S12: -0.0130 S13: -0.4904
REMARK 3 S21: -0.4692 S22: 0.5997 S23: -1.0704
REMARK 3 S31: -0.1483 S32: 0.3778 S33: -0.3294
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1864 A 1971
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7550 29.4266 1.4525
REMARK 3 T TENSOR
REMARK 3 T11: 0.0589 T22: 0.0527
REMARK 3 T33: 0.0192 T12: -0.0039
REMARK 3 T13: -0.0050 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 5.0391 L22: 5.0668
REMARK 3 L33: 4.5596 L12: 2.1002
REMARK 3 L13: -0.3946 L23: -0.9255
REMARK 3 S TENSOR
REMARK 3 S11: -0.0415 S12: 0.1229 S13: -0.2968
REMARK 3 S21: -0.1737 S22: 0.0544 S23: -0.1062
REMARK 3 S31: -0.1400 S32: -0.1625 S33: -0.0128
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : FLAT GRAPHITE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16214
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 33.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.73800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3G0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34% LOW MOLECULAR WEIGHT PEG SMEARS
REMARK 280 (LMW PEG SMEARS), 0.1M MES PH 6.0 (LIGAND SOAKING PERFORMED IN
REMARK 280 LOW-MOLECULAR-WEIGHT PEG SMEARS STABILIZING SOLUTION), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.14K
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 28.90500
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 28.90500
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 40.58500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.34500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.58500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.34500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.90500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.58500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.34500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.90500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.58500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.34500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL
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 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 CE NZ
REMARK 470 VAL A1971 CG1 CG2
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 A2242 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A2243 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A2251 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A2255 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A2257 DISTANCE = 7.00 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 43D 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 EDO A 2004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XUA RELATED DB: PDB
REMARK 900 4XUA - THE COMPLEX WITH AN ANALOGUE OF THE BAZ2-ICR PROBE
DBREF 4XUB A 1858 1972 UNP Q9UIF8 BAZ2B_HUMAN 1858 1972
SEQADV 4XUB SER A 1856 UNP Q9UIF8 EXPRESSION TAG
SEQADV 4XUB MET A 1857 UNP Q9UIF8 EXPRESSION TAG
SEQRES 1 A 117 SER MET SER VAL LYS LYS PRO LYS ARG ASP ASP SER LYS
SEQRES 2 A 117 ASP LEU ALA LEU CYS SER MET ILE LEU THR GLU MET GLU
SEQRES 3 A 117 THR HIS GLU ASP ALA TRP PRO PHE LEU LEU PRO VAL ASN
SEQRES 4 A 117 LEU LYS LEU VAL PRO GLY TYR LYS LYS VAL ILE LYS LYS
SEQRES 5 A 117 PRO MET ASP PHE SER THR ILE ARG GLU LYS LEU SER SER
SEQRES 6 A 117 GLY GLN TYR PRO ASN LEU GLU THR PHE ALA LEU ASP VAL
SEQRES 7 A 117 ARG LEU VAL PHE ASP ASN CYS GLU THR PHE ASN GLU ASP
SEQRES 8 A 117 ASP SER ASP ILE GLY ARG ALA GLY HIS ASN MET ARG LYS
SEQRES 9 A 117 TYR PHE GLU LYS LYS TRP THR ASP THR PHE LYS VAL SER
HET 43D A2001 27
HET EDO A2002 8
HET EDO A2003 4
HET EDO A2004 4
HETNAM 43D 4-{4-(1-METHYL-1H-PYRAZOL-4-YL)-1-[2-(4-METHYL-1H-1,2,
HETNAM 2 43D 3-TRIAZOL-1-YL)ETHYL]-1H-IMIDAZOL-5-YL}BENZONITRILE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 43D C19 H18 N8
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 HOH *165(H2 O)
HELIX 1 AA1 LYS A 1868 HIS A 1883 1 16
HELIX 2 AA2 GLU A 1884 LEU A 1890 5 7
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 12 TRP A1887 PRO A1888 PHE A1889 LEU A1890
SITE 2 AC1 12 LEU A1891 PRO A1892 ASN A1894 LEU A1897
SITE 3 AC1 12 VAL A1898 ASN A1944 HOH A2112 HOH A2199
SITE 1 AC2 3 HIS A1883 GLU A1884 HOH A2175
SITE 1 AC3 5 ARG A1864 LEU A1872 THR A1968 HOH A2232
SITE 2 AC3 5 HOH A2233
SITE 1 AC4 7 LEU A1895 LYS A1896 VAL A1898 PRO A1899
SITE 2 AC4 7 GLY A1900 HOH A2109 HOH A2219
CRYST1 81.170 96.690 57.810 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 0.012320 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017298 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
