HEADER HYDROLASE 29-SEP-09 3A7N
TITLE CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URACIL-DNA GLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UDG;
COMPND 5 EC: 3.2.2.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: UNG, RV2976C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETB MTUUDG
KEYWDS UNG-UGI INTERACTIONS, UNG-DNA COMPLEX, CITRATE AS PROTEIN LIGAND,
KEYWDS 2 LIGAND BINDING, INHIBITOR DESIGN, DNA DAMAGE, DNA REPAIR,
KEYWDS 3 GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.KAUSHAL,R.K.TALAWAR,U.VARSHNEY,M.VIJAYAN
REVDAT 3 01-NOV-23 3A7N 1 REMARK SEQADV
REVDAT 2 18-AUG-10 3A7N 1 JRNL
REVDAT 1 11-AUG-10 3A7N 0
JRNL AUTH P.S.KAUSHAL,R.K.TALAWAR,U.VARSHNEY,M.VIJAYAN
JRNL TITL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS: INSIGHTS INTO INTERACTIONS WITH LIGANDS
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 66 887 2010
JRNL REFN ESSN 1744-3091
JRNL PMID 20693660
JRNL DOI 10.1107/S1744309110023043
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.S.KAUSHAL,R.K.TALAWAR,P.D.V.KRISHNA,U.VARSHNEY,M.VIJAYAN
REMARK 1 TITL UNIQUE FEATURES OF THE STRUCTURE AND INTERACTIONS OF
REMARK 1 TITL 2 MYCOBACTERIAL URACIL-DNA GLYCOSYLASE: STRUCTURE OF A COMPLEX
REMARK 1 TITL 3 OF THE MYCOBACTERIUM TUBERCULOSIS ENZYME IN COMPARISON WITH
REMARK 1 TITL 4 THOSE FROM OTHER SOURCES
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 64 551 2008
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 18453691
REMARK 1 DOI 10.1107/S090744490800512X
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.SAIKRISHNAN,M.BIDYA SAGAR,R.RAVISHANKAR,S.ROY,
REMARK 1 AUTH 2 K.PURNAPATRE,P.HANDA,U.VARSHNEY,M.VIJAYAN
REMARK 1 TITL DOMAIN CLOSURE AND ACTION OF URACIL DNA GLYCOSYLASE (UDG):
REMARK 1 TITL 2 STRUCTURES OF NEW CRYSTAL FORMS CONTAINING THE ESCHERICHIA
REMARK 1 TITL 3 COLI ENZYME AND A COMPARATIVE STUDY OF THE KNOWN STRUCTURES
REMARK 1 TITL 4 INVOLVING UDG
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1269 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 12136137
REMARK 1 DOI 10.1107/S0907444902009599
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.RAVISHANKAR,M.BIDYA SAGAR,S.ROY,K.PURNAPATRE,P.HANDA,
REMARK 1 AUTH 2 U.VARSHNEY,M.VIJAYAN
REMARK 1 TITL X-RAY ANALYSIS OF A COMPLEX OF ESCHERICHIA COLI URACIL DNA
REMARK 1 TITL 2 GLYCOSYLASE (ECUDG) WITH A PROTEINACEOUS INHIBITOR. THE
REMARK 1 TITL 3 STRUCTURE ELUCIDATION OF A PROKARYOTIC UDG
REMARK 1 REF NUCLEIC ACIDS RES. V. 26 4880 1998
REMARK 1 REFN ISSN 0305-1048
REMARK 1 PMID 9776748
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 17319
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) : 0.181
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 885
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1255
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1764
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : 0.47000
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): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.309
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1841 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2521 ; 1.139 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 232 ; 5.050 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;34.631 ;21.757
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 257 ;12.806 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.539 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 273 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1453 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 897 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1254 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 161 ; 0.115 ; 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): 62 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.141 ; 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): 1200 ; 0.337 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1884 ; 0.591 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 733 ; 0.919 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 637 ; 1.550 ; 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 : 6
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 -4 A 7
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6111 -8.3295 23.3935
REMARK 3 T TENSOR
REMARK 3 T11: -0.1022 T22: -0.0240
REMARK 3 T33: -0.0104 T12: -0.0154
REMARK 3 T13: 0.0470 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 6.5457 L22: 1.6157
REMARK 3 L33: 20.1559 L12: 2.1053
REMARK 3 L13: 11.2815 L23: 2.8110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.3617 S13: -0.0211
REMARK 3 S21: 0.1179 S22: -0.0708 S23: 0.1190
REMARK 3 S31: -0.0509 S32: -0.3558 S33: 0.1002
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 8 A 41
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8103 -3.5814 19.4602
REMARK 3 T TENSOR
REMARK 3 T11: -0.0371 T22: -0.0292
REMARK 3 T33: -0.0147 T12: 0.0108
REMARK 3 T13: 0.0199 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 2.0481 L22: 0.5274
REMARK 3 L33: 2.5586 L12: 0.2632
REMARK 3 L13: 1.8469 L23: -0.1633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0547 S12: -0.0549 S13: 0.0611
REMARK 3 S21: 0.0222 S22: 0.0098 S23: 0.1159
REMARK 3 S31: -0.0834 S32: -0.0415 S33: 0.0449
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 : A 42 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8588 -13.5983 13.4629
REMARK 3 T TENSOR
REMARK 3 T11: -0.0082 T22: -0.0153
REMARK 3 T33: -0.0117 T12: 0.0005
REMARK 3 T13: -0.0045 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.3084 L22: 0.4309
REMARK 3 L33: 0.6013 L12: -0.1586
REMARK 3 L13: 0.0911 L23: 0.0722
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: -0.0062 S13: -0.0179
REMARK 3 S21: 0.0065 S22: 0.0139 S23: 0.0341
REMARK 3 S31: 0.0449 S32: 0.0215 S33: -0.0030
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 125
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7650 -19.3417 11.3439
REMARK 3 T TENSOR
REMARK 3 T11: -0.0109 T22: -0.0313
REMARK 3 T33: 0.0022 T12: 0.0073
REMARK 3 T13: 0.0061 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.0005 L22: 0.1073
REMARK 3 L33: 0.9245 L12: -0.0396
REMARK 3 L13: -0.1297 L23: 0.2120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: -0.0061 S13: -0.0926
REMARK 3 S21: 0.0045 S22: 0.0224 S23: -0.0105
REMARK 3 S31: 0.0273 S32: -0.0009 S33: -0.0245
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 126 A 170
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0618 -2.5201 15.1012
REMARK 3 T TENSOR
REMARK 3 T11: -0.0011 T22: -0.0097
REMARK 3 T33: -0.0222 T12: -0.0068
REMARK 3 T13: -0.0063 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.5522 L22: 0.6446
REMARK 3 L33: 0.0848 L12: 0.1203
REMARK 3 L13: -0.0332 L23: 0.2190
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.0285 S13: 0.0772
REMARK 3 S21: -0.0535 S22: 0.0248 S23: 0.0299
REMARK 3 S31: -0.0379 S32: 0.0463 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 171 A 227
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1557 -8.8977 14.8366
REMARK 3 T TENSOR
REMARK 3 T11: -0.0377 T22: -0.0182
REMARK 3 T33: -0.0231 T12: 0.0008
REMARK 3 T13: -0.0013 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.8861 L22: 0.8595
REMARK 3 L33: 1.1676 L12: -0.1213
REMARK 3 L13: -0.2407 L23: 0.0645
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0435 S13: 0.0488
REMARK 3 S21: -0.0150 S22: 0.0461 S23: -0.0932
REMARK 3 S31: -0.0631 S32: 0.1051 S33: -0.0430
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: NULL
REMARK 4
REMARK 4 3A7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000028913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18238
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 2ZHX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M TRI-AMMONIUM CITRATE PH 7.0, 10%
REMARK 280 ISOPROPANOL, MICROBATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 22.42000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.42000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.83500
REMARK 290 SMTRY3 4 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 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 -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
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 ARG A 12 NE CZ NH1 NH2
REMARK 470 ARG A 170 CD NE CZ NH1 NH2
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 PHE A 81 -16.75 74.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 229
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZHX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS IN COMPLEX WITH A PROTEINACEOUS INHIBITOR
DBREF 3A7N A 1 227 UNP P67071 UNG_MYCTU 1 227
SEQADV 3A7N MET A -10 UNP P67071 INITIATING METHIONINE
SEQADV 3A7N HIS A -9 UNP P67071 EXPRESSION TAG
SEQADV 3A7N HIS A -8 UNP P67071 EXPRESSION TAG
SEQADV 3A7N HIS A -7 UNP P67071 EXPRESSION TAG
SEQADV 3A7N HIS A -6 UNP P67071 EXPRESSION TAG
SEQADV 3A7N HIS A -5 UNP P67071 EXPRESSION TAG
SEQADV 3A7N HIS A -4 UNP P67071 EXPRESSION TAG
SEQADV 3A7N GLY A -3 UNP P67071 EXPRESSION TAG
SEQADV 3A7N MET A -2 UNP P67071 EXPRESSION TAG
SEQADV 3A7N ALA A -1 UNP P67071 EXPRESSION TAG
SEQADV 3A7N SER A 0 UNP P67071 EXPRESSION TAG
SEQRES 1 A 238 MET HIS HIS HIS HIS HIS HIS GLY MET ALA SER MET THR
SEQRES 2 A 238 ALA ARG PRO LEU SER GLU LEU VAL GLU ARG GLY TRP ALA
SEQRES 3 A 238 ALA ALA LEU GLU PRO VAL ALA ASP GLN VAL ALA HIS MET
SEQRES 4 A 238 GLY GLN PHE LEU ARG ALA GLU ILE ALA ALA GLY ARG ARG
SEQRES 5 A 238 TYR LEU PRO ALA GLY SER ASN VAL LEU ARG ALA PHE THR
SEQRES 6 A 238 PHE PRO PHE ASP ASN VAL ARG VAL LEU ILE VAL GLY GLN
SEQRES 7 A 238 ASP PRO TYR PRO THR PRO GLY HIS ALA VAL GLY LEU SER
SEQRES 8 A 238 PHE SER VAL ALA PRO ASP VAL ARG PRO TRP PRO ARG SER
SEQRES 9 A 238 LEU ALA ASN ILE PHE ASP GLU TYR THR ALA ASP LEU GLY
SEQRES 10 A 238 TYR PRO LEU PRO SER ASN GLY ASP LEU THR PRO TRP ALA
SEQRES 11 A 238 GLN ARG GLY VAL LEU LEU LEU ASN ARG VAL LEU THR VAL
SEQRES 12 A 238 ARG PRO SER ASN PRO ALA SER HIS ARG GLY LYS GLY TRP
SEQRES 13 A 238 GLU ALA VAL THR GLU CYS ALA ILE ARG ALA LEU ALA ALA
SEQRES 14 A 238 ARG ALA ALA PRO LEU VAL ALA ILE LEU TRP GLY ARG ASP
SEQRES 15 A 238 ALA SER THR LEU LYS PRO MET LEU ALA ALA GLY ASN CYS
SEQRES 16 A 238 VAL ALA ILE GLU SER PRO HIS PRO SER PRO LEU SER ALA
SEQRES 17 A 238 SER ARG GLY PHE PHE GLY SER ARG PRO PHE SER ARG ALA
SEQRES 18 A 238 ASN GLU LEU LEU VAL GLY MET GLY ALA GLU PRO ILE ASP
SEQRES 19 A 238 TRP ARG LEU PRO
HET FLC A 228 13
HET FLC A 229 13
HETNAM FLC CITRATE ANION
FORMUL 2 FLC 2(C6 H5 O7 3-)
FORMUL 4 HOH *193(H2 O)
HELIX 1 1 GLY A -3 ARG A 4 1 8
HELIX 2 2 PRO A 5 LEU A 9 5 5
HELIX 3 3 GLU A 11 LEU A 18 1 8
HELIX 4 4 VAL A 21 ALA A 38 1 18
HELIX 5 5 ALA A 45 VAL A 49 5 5
HELIX 6 6 LEU A 50 THR A 54 5 5
HELIX 7 7 PRO A 56 VAL A 60 5 5
HELIX 8 8 PRO A 91 GLY A 106 1 16
HELIX 9 9 LEU A 115 ARG A 121 1 7
HELIX 10 10 GLY A 144 ARG A 159 1 16
HELIX 11 11 GLY A 169 THR A 174 1 6
HELIX 12 12 LEU A 175 ALA A 180 1 6
HELIX 13 13 ARG A 205 MET A 217 1 13
SHEET 1 A 4 VAL A 123 ASN A 127 0
SHEET 2 A 4 VAL A 62 GLY A 66 1 N VAL A 62 O LEU A 124
SHEET 3 A 4 LEU A 163 TRP A 168 1 O ILE A 166 N LEU A 63
SHEET 4 A 4 CYS A 184 SER A 189 1 O ILE A 187 N LEU A 167
CISPEP 1 LEU A 43 PRO A 44 0 0.24
CISPEP 2 ARG A 88 PRO A 89 0 -7.23
SITE 1 AC1 10 GLN A 67 ASP A 68 TYR A 70 SER A 80
SITE 2 AC1 10 PHE A 81 SER A 93 ASN A 127 HIS A 191
SITE 3 AC1 10 HOH A 230 HOH A 380
SITE 1 AC2 12 MET A -2 HIS A -5 GLY A -3 TYR A 42
SITE 2 AC2 12 ALA A 45 GLY A 46 ARG A 92 ARG A 205
SITE 3 AC2 12 HOH A 277 HOH A 292 HOH A 334 HOH A 402
CRYST1 44.840 63.670 86.400 90.00 90.00 90.00 P 21 21 21 4
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 0.022302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011574 0.00000
(ATOM LINES ARE NOT SHOWN.)
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