HEADER TRANSCRIPTION 26-NOV-13 4NRB
TITLE CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BAZ2B IN COMPLEX WITH
TITLE 2 COMPOUND-1 N01197
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN (RESIDUES 2054-2168);
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)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS SGC, STRUCTURAL GENOMICS CONSORTIUM, TRANSCRIPTION, BROMODOMAIN,
KEYWDS 2 ACETYLATED LYSINE BINDING PROTEIN, KIAA1476, WALP4
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.C.MUNIZ,I.FELLETAR,A.CHAIKUAD,P.FILIPPAKOPOULOS,F.M.FERGUSON,
AUTHOR 2 O.FEDOROV,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,A.CIULLI,
AUTHOR 3 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 20-SEP-23 4NRB 1 REMARK SEQADV
REVDAT 2 02-JUL-14 4NRB 1
REVDAT 1 25-DEC-13 4NRB 0
JRNL AUTH F.M.FERGUSON,O.FEDOROV,A.CHAIKUAD,M.PHILPOTT,J.R.MUNIZ,
JRNL AUTH 2 I.FELLETAR,F.VON DELFT,T.HEIGHTMAN,S.KNAPP,C.ABELL,A.CIULLI
JRNL TITL TARGETING LOW-DRUGGABILITY BROMODOMAINS: FRAGMENT BASED
JRNL TITL 2 SCREENING AND INHIBITOR DESIGN AGAINST THE BAZ2B
JRNL TITL 3 BROMODOMAIN.
JRNL REF J.MED.CHEM. V. 56 10183 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 24304323
JRNL DOI 10.1021/JM401582C
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 14004
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 696
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.25
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2839
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2265
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2695
REMARK 3 BIN R VALUE (WORKING SET) : 0.2242
REMARK 3 BIN FREE R VALUE : 0.2683
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.02260
REMARK 3 B22 (A**2) : 2.94260
REMARK 3 B33 (A**2) : 1.07990
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.237
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 976 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 1314 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 456 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 28 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 141 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 976 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 124 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1329 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.92
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.08
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.64
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1856 - A|1863 }
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9796 32.9152 -11.1086
REMARK 3 T TENSOR
REMARK 3 T11: 0.0475 T22: 0.0936
REMARK 3 T33: -0.0137 T12: -0.0513
REMARK 3 T13: 0.0051 T23: -0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 0.1734 L22: 1.8560
REMARK 3 L33: 0.6777 L12: 0.7584
REMARK 3 L13: 0.2682 L23: -2.9026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -0.1692 S13: 0.2344
REMARK 3 S21: -0.1629 S22: 0.0489 S23: -0.1756
REMARK 3 S31: 0.1017 S32: 0.1653 S33: -0.0358
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1864 - A|1894 }
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8077 25.2165 -2.2762
REMARK 3 T TENSOR
REMARK 3 T11: 0.0073 T22: -0.1049
REMARK 3 T33: -0.0841 T12: 0.0001
REMARK 3 T13: 0.0281 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.1282 L22: 2.3682
REMARK 3 L33: 1.9987 L12: -0.6157
REMARK 3 L13: 0.5189 L23: -0.2860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0405 S12: -0.0728 S13: 0.2814
REMARK 3 S21: 0.1193 S22: 0.0071 S23: -0.2111
REMARK 3 S31: -0.0781 S32: -0.0479 S33: 0.0334
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|1895 - A|1903 }
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3357 2.2539 -6.4663
REMARK 3 T TENSOR
REMARK 3 T11: 0.1121 T22: -0.0661
REMARK 3 T33: 0.0235 T12: 0.0387
REMARK 3 T13: 0.0147 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.5880 L22: 1.8550
REMARK 3 L33: 0.6813 L12: 2.0987
REMARK 3 L13: 2.9029 L23: 0.5530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: -0.0051 S13: -0.0746
REMARK 3 S21: -0.1629 S22: -0.0834 S23: -0.4126
REMARK 3 S31: 0.2263 S32: -0.0794 S33: 0.0320
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|1904 - A|1908 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3890 5.8114 -6.3807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: -0.0821
REMARK 3 T33: -0.0012 T12: -0.0033
REMARK 3 T13: -0.0318 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.1364
REMARK 3 L33: 0.4679 L12: -0.2506
REMARK 3 L13: -1.0735 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.0547 S13: -0.0749
REMARK 3 S21: -0.0282 S22: -0.0024 S23: 0.0169
REMARK 3 S31: 0.0168 S32: -0.0200 S33: -0.0171
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|1909 - A|1961 }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8240 17.1598 -0.8789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0411 T22: -0.0674
REMARK 3 T33: -0.0916 T12: 0.0057
REMARK 3 T13: 0.0166 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.2299 L22: 1.9618
REMARK 3 L33: 2.5304 L12: -0.7380
REMARK 3 L13: 0.1412 L23: -0.9279
REMARK 3 S TENSOR
REMARK 3 S11: 0.0362 S12: -0.0362 S13: 0.0322
REMARK 3 S21: 0.0159 S22: -0.0011 S23: 0.0004
REMARK 3 S31: 0.0117 S32: -0.0585 S33: -0.0351
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { A|1962 - A|1969 }
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6762 29.0275 3.7882
REMARK 3 T TENSOR
REMARK 3 T11: 0.1845 T22: -0.0270
REMARK 3 T33: -0.0644 T12: 0.0962
REMARK 3 T13: 0.0306 T23: -0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.8553
REMARK 3 L33: 0.0000 L12: -1.2959
REMARK 3 L13: 0.6351 L23: -2.6561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0179 S12: -0.0259 S13: 0.0555
REMARK 3 S21: 0.1814 S22: 0.0368 S23: 0.1111
REMARK 3 S31: -0.1667 S32: -0.1744 S33: -0.0190
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 : 14004
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 29.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.78700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 3G0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 1000, 15% GLYCEROL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
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 28.84000
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 28.84000
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 40.72000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.27500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.72000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.27500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.84000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.72000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.27500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.84000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.72000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.27500
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2270 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2301 LIES ON A SPECIAL POSITION.
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 LYS A 1970
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 GLU A1927 CD OE1 OE2
REMARK 470 LYS A1959 CE NZ
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2LX 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NR9 RELATED DB: PDB
REMARK 900 RELATED ID: 4NRA RELATED DB: PDB
REMARK 900 RELATED ID: 4NRC RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDS TO ISOFORM 4
DBREF 4NRB A 1858 1972 UNP Q9UIF8 BAZ2B_HUMAN 2054 2168
SEQADV 4NRB SER A 1856 UNP Q9UIF8 EXPRESSION TAG
SEQADV 4NRB 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 2LX A2001 17
HET EDO A2002 4
HETNAM 2LX N-METHYL-2-(TETRAHYDRO-2H-PYRAN-4-YLOXY)BENZAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 2LX C13 H17 N O3
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *202(H2 O)
HELIX 1 1 LYS A 1868 HIS A 1883 1 16
HELIX 2 2 GLU A 1884 LEU A 1890 5 7
HELIX 3 3 GLY A 1900 ILE A 1905 1 6
HELIX 4 4 ASP A 1910 SER A 1920 1 11
HELIX 5 5 ASN A 1925 ASN A 1944 1 20
HELIX 6 6 SER A 1948 PHE A 1969 1 22
SITE 1 AC1 8 PRO A1888 VAL A1893 VAL A1898 PHE A1943
SITE 2 AC1 8 ASN A1944 ILE A1950 HOH A2268 HOH A2277
SITE 1 AC2 3 LYS A1917 HOH A2169 HOH A2288
CRYST1 81.440 96.550 57.680 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 0.012279 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010357 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
