HEADER DNA BINDING PROTEIN 03-FEB-17 5PC5
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF BAZ2B AFTER
TITLE 2 INITIAL REFINEMENT WITH NO LIGAND MODELLED (STRUCTURE 26)
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 5PC5 1 REMARK
REVDAT 3 04-OCT-17 5PC5 1 REMARK
REVDAT 2 27-SEP-17 5PC5 1 JRNL REMARK
REVDAT 1 22-MAR-17 5PC5 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. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 18565
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 976
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1125
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.39000
REMARK 3 B22 (A**2) : -1.76000
REMARK 3 B33 (A**2) : -1.62000
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): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.099
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 968 ; 0.021 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 916 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1305 ; 1.803 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2126 ; 1.028 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 116 ; 5.872 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ;35.380 ;24.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 181 ;11.588 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;17.885 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 142 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1064 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 209 ; 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): 464 ; 3.321 ; 3.150
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 463 ; 3.321 ; 3.141
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 580 ; 4.483 ; 4.697
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5PC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1001400477.
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 : 19600
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 28.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 1.08000
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 (%): 65.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
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 28.86900
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 28.86900
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 40.83650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.19050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.83650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.19050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.86900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.83650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.19050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.86900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.83650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.19050
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 OE1 GLU A 1945 O HOH A 2101 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A1934 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A1958 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
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 A2300 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2301 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A2302 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A2303 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH A2304 DISTANCE = 7.47 ANGSTROMS
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
DBREF 5PC5 A 1858 1972 UNP Q9UIF8 BAZ2B_HUMAN 1954 2068
SEQADV 5PC5 MET A 1835 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1836 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1837 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1838 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1839 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1840 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 HIS A 1841 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 SER A 1842 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 SER A 1843 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 GLY A 1844 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 VAL A 1845 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 ASP A 1846 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 LEU A 1847 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 GLY A 1848 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 THR A 1849 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 GLU A 1850 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 ASN A 1851 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 LEU A 1852 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 TYR A 1853 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 PHE A 1854 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 GLN A 1855 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 SER A 1856 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5PC5 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
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 HOH *204(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 3 ASN A1944 HOH A2128 HOH A2129
CRYST1 81.673 96.381 57.738 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 0.012244 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
