HEADER OXIDOREDUCTASE/DNA 31-DEC-07 3BTX
TITLE X-RAY STRUCTURE OF HUMAN ABH2 BOUND TO DSDNA THROUGH ACTIVE SITE
TITLE 2 CROSS-LINKING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALKYLATED DNA REPAIR PROTEIN ALKB HOMOLOG 2, OXY DC1;
COMPND 5 EC: 1.14.11.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*CP*TP*GP*TP*AP*TP*(2YR)P*AP*TP*TP*GP*CP*G)-3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-
COMPND 14 D(*DTP*DCP*DGP*DCP*DAP*DAP*DTP*DAP*DAP*DTP*DAP*DCP*DA)-3');
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: 12Q24.11;
SOURCE 6 GENE: ALKBH2, ABH2;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES
KEYWDS PROTEIN/DNA INTERACTION, HUMAN DIOXYGENASE, DNA REPAIR, CROSS-
KEYWDS 2 LINKING, DNA DAMAGE, IRON, METAL-BINDING, NUCLEUS, OXIDOREDUCTASE,
KEYWDS 3 OXIDOREDUCTASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-G.YANG,C.YI,C.HE
REVDAT 6 20-OCT-21 3BTX 1 REMARK SEQADV LINK
REVDAT 5 21-MAY-14 3BTX 1 COMPND REMARK SEQRES HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 HETATM ATOM
REVDAT 4 13-JUL-11 3BTX 1 VERSN
REVDAT 3 24-FEB-09 3BTX 1 VERSN
REVDAT 2 10-JUN-08 3BTX 1 JRNL
REVDAT 1 22-APR-08 3BTX 0
JRNL AUTH C.G.YANG,C.YI,E.M.DUGUID,C.T.SULLIVAN,X.JIAN,P.A.RICE,C.HE
JRNL TITL CRYSTAL STRUCTURES OF DNA/RNA REPAIR ENZYMES ALKB AND ABH2
JRNL TITL 2 BOUND TO DSDNA.
JRNL REF NATURE V. 452 961 2008
JRNL REFN ISSN 0028-0836
JRNL PMID 18432238
JRNL DOI 10.1038/NATURE06889
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 26213
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1423
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1608
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1636
REMARK 3 NUCLEIC ACID ATOMS : 527
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : 0.42000
REMARK 3 B12 (A**2) : -0.14000
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): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.452
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2340 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3285 ; 1.206 ; 2.234
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 220 ; 5.485 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;26.241 ;21.205
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;12.988 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;15.157 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 356 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1624 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 858 ; 0.171 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1485 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 205 ; 0.121 ; 0.200
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): 37 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.190 ; 0.200
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): 1080 ; 0.384 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1705 ; 0.669 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1597 ; 1.004 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1573 ; 1.624 ; 4.500
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 : 3
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 55 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): 110.5076 -2.4455-194.9771
REMARK 3 T TENSOR
REMARK 3 T11: -0.1568 T22: -0.1853
REMARK 3 T33: -0.1434 T12: -0.0166
REMARK 3 T13: 0.0552 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 5.2437 L22: 3.7851
REMARK 3 L33: 1.5170 L12: -2.2613
REMARK 3 L13: 0.4794 L23: -0.7521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0972 S12: 0.3139 S13: -0.2067
REMARK 3 S21: -0.5901 S22: 0.0930 S23: -0.0939
REMARK 3 S31: 0.1978 S32: -0.0014 S33: -0.1902
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 : B 259 B 271
REMARK 3 ORIGIN FOR THE GROUP (A): 87.9091 2.4348-195.3908
REMARK 3 T TENSOR
REMARK 3 T11: -0.0712 T22: -0.1027
REMARK 3 T33: -0.1193 T12: 0.0405
REMARK 3 T13: 0.0245 T23: 0.1817
REMARK 3 L TENSOR
REMARK 3 L11: 4.1413 L22: 1.2854
REMARK 3 L33: 2.0222 L12: 1.4087
REMARK 3 L13: 1.1010 L23: 1.2687
REMARK 3 S TENSOR
REMARK 3 S11: -0.1789 S12: -0.2030 S13: -0.1360
REMARK 3 S21: -0.1472 S22: 0.2430 S23: 0.3376
REMARK 3 S31: 0.0658 S32: -0.3868 S33: -0.0641
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 272 C 284
REMARK 3 ORIGIN FOR THE GROUP (A): 90.0645 4.0602-194.8220
REMARK 3 T TENSOR
REMARK 3 T11: -0.1328 T22: 0.0006
REMARK 3 T33: -0.1319 T12: -0.0411
REMARK 3 T13: 0.0096 T23: 0.1271
REMARK 3 L TENSOR
REMARK 3 L11: 2.7178 L22: 3.2106
REMARK 3 L33: 16.1318 L12: -1.4418
REMARK 3 L13: 3.3653 L23: -5.1379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0902 S12: -0.3987 S13: -0.1611
REMARK 3 S21: -0.1325 S22: 0.3980 S23: 0.5003
REMARK 3 S31: -0.2811 S32: -0.4573 S33: -0.3077
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
REMARK 4
REMARK 4 3BTX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000045951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9266
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28880
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 44.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 0.1M SODIUM CHLORIDE,
REMARK 280 0.05M MAGNESIUM CHLORIDE, 0.1M CACODYLATE, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.06000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.53000
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 114.79500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 38.26500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 191.32500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 153.06000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 76.53000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 38.26500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 114.79500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 191.32500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4020 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 DT B 262 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT B 267 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT B 268 O4' - C1' - N1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 DC C 275 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT C 278 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DA C 279 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DA C 280 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC C 283 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
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 ARG A 110 -171.71 176.37
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 173 OD1
REMARK 620 2 ASP A 173 OD2 49.3
REMARK 620 3 HOH A 518 O 69.1 100.1
REMARK 620 4 HOH A 519 O 131.4 108.4 75.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FD8 RELATED DB: PDB
REMARK 900 E. COLI HOMOLOG
REMARK 900 RELATED ID: 2IUW RELATED DB: PDB
REMARK 900 HUMAN HOMOLOG
REMARK 900 RELATED ID: 3BTY RELATED DB: PDB
REMARK 900 RELATED ID: 3BTZ RELATED DB: PDB
REMARK 900 RELATED ID: 3BU0 RELATED DB: PDB
REMARK 900 RELATED ID: 3BUC RELATED DB: PDB
DBREF 3BTX A 56 258 UNP Q6NS38 ALKB2_HUMAN 56 258
DBREF 3BTX B 259 271 PDB 3BTX 3BTX 259 271
DBREF 3BTX C 272 284 PDB 3BTX 3BTX 272 284
SEQADV 3BTX ALA A 55 UNP Q6NS38 EXPRESSION TAG
SEQADV 3BTX SER A 67 UNP Q6NS38 CYS 67 ENGINEERED MUTATION
SEQADV 3BTX SER A 165 UNP Q6NS38 CYS 165 ENGINEERED MUTATION
SEQADV 3BTX CYS A 175 UNP Q6NS38 GLU 175 ENGINEERED MUTATION
SEQADV 3BTX SER A 192 UNP Q6NS38 CYS 192 ENGINEERED MUTATION
SEQRES 1 A 204 ALA SER TRP ARG HIS ILE ARG ALA GLU GLY LEU ASP SER
SEQRES 2 A 204 SER TYR THR VAL LEU PHE GLY LYS ALA GLU ALA ASP GLU
SEQRES 3 A 204 ILE PHE GLN GLU LEU GLU LYS GLU VAL GLU TYR PHE THR
SEQRES 4 A 204 GLY ALA LEU ALA ARG VAL GLN VAL PHE GLY LYS TRP HIS
SEQRES 5 A 204 SER VAL PRO ARG LYS GLN ALA THR TYR GLY ASP ALA GLY
SEQRES 6 A 204 LEU THR TYR THR PHE SER GLY LEU THR LEU SER PRO LYS
SEQRES 7 A 204 PRO TRP ILE PRO VAL LEU GLU ARG ILE ARG ASP HIS VAL
SEQRES 8 A 204 SER GLY VAL THR GLY GLN THR PHE ASN PHE VAL LEU ILE
SEQRES 9 A 204 ASN ARG TYR LYS ASP GLY SER ASP HIS ILE GLY GLU HIS
SEQRES 10 A 204 ARG ASP ASP CYS ARG GLU LEU ALA PRO GLY SER PRO ILE
SEQRES 11 A 204 ALA SER VAL SER PHE GLY ALA SER ARG ASP PHE VAL PHE
SEQRES 12 A 204 ARG HIS LYS ASP SER ARG GLY LYS SER PRO SER ARG ARG
SEQRES 13 A 204 VAL ALA VAL VAL ARG LEU PRO LEU ALA HIS GLY SER LEU
SEQRES 14 A 204 LEU MET MET ASN HIS PRO THR ASN THR HIS TRP TYR HIS
SEQRES 15 A 204 SER LEU PRO VAL ARG LYS LYS VAL LEU ALA PRO ARG VAL
SEQRES 16 A 204 ASN LEU THR PHE ARG LYS ILE LEU LEU
SEQRES 1 B 13 DC DT DG DT DA DT 2YR DA DT DT DG DC DG
SEQRES 1 C 13 DT DC DG DC DA DA DT DA DA DT DA DC DA
HET 2YR B 265 22
HET MG A 301 1
HETNAM 2YR 2'-DEOXY-N-(2-SULFANYLETHYL)CYTIDINE 5'-(DIHYDROGEN
HETNAM 2 2YR PHOSPHATE)
HETNAM MG MAGNESIUM ION
FORMUL 2 2YR C11 H18 N3 O7 P S
FORMUL 4 MG MG 2+
FORMUL 5 HOH *192(H2 O)
HELIX 1 1 GLY A 74 VAL A 89 1 16
HELIX 2 2 THR A 93 LEU A 96 5 4
HELIX 3 3 ILE A 135 GLY A 150 1 16
HELIX 4 4 ASP A 201 ARG A 203 5 3
HELIX 5 5 PRO A 229 HIS A 233 1 5
SHEET 1 A 7 ARG A 58 ALA A 62 0
SHEET 2 A 7 LEU A 65 VAL A 71 -1 O SER A 67 N ILE A 60
SHEET 3 A 7 SER A 222 MET A 226 -1 O LEU A 223 N THR A 70
SHEET 4 A 7 ILE A 184 GLY A 190 -1 N SER A 186 O LEU A 224
SHEET 5 A 7 ARG A 248 ARG A 254 -1 O LEU A 251 N VAL A 187
SHEET 6 A 7 PHE A 155 TYR A 161 -1 N LEU A 157 O THR A 252
SHEET 7 A 7 LYS A 111 GLY A 116 -1 N ALA A 113 O ILE A 158
SHEET 1 B 2 ARG A 98 VAL A 101 0
SHEET 2 B 2 LYS A 104 SER A 107 -1 O HIS A 106 N VAL A 99
SHEET 1 C 2 TYR A 122 PHE A 124 0
SHEET 2 C 2 LEU A 127 LEU A 129 -1 O LEU A 129 N TYR A 122
SHEET 1 D 4 ILE A 168 HIS A 171 0
SHEET 2 D 4 TRP A 234 LEU A 238 -1 O HIS A 236 N HIS A 171
SHEET 3 D 4 ARG A 193 HIS A 199 -1 N ARG A 198 O TYR A 235
SHEET 4 D 4 VAL A 214 LEU A 218 -1 O VAL A 214 N PHE A 197
LINK SG CYS A 175 S 2YR B 265 1555 1555 2.03
LINK O3' DT B 264 P 2YR B 265 1555 1555 1.60
LINK O3' 2YR B 265 P DA B 266 1555 1555 1.59
LINK OD1 ASP A 173 MG MG A 301 1555 1555 2.58
LINK OD2 ASP A 173 MG MG A 301 1555 1555 2.67
LINK MG MG A 301 O HOH A 518 1555 1555 2.40
LINK MG MG A 301 O HOH A 519 1555 1555 2.43
CISPEP 1 HIS A 228 PRO A 229 0 2.21
SITE 1 AC1 5 HIS A 171 ASP A 173 HIS A 236 HOH A 518
SITE 2 AC1 5 HOH A 519
CRYST1 78.140 78.140 229.590 90.00 90.00 120.00 P 65 2 2 12
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 0.012798 0.007389 0.000000 0.00000
SCALE2 0.000000 0.014777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004356 0.00000
(ATOM LINES ARE NOT SHOWN.)
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