HEADER HYDROLASE 13-AUG-07 2QXX
TITLE BIFUNCTIONAL DCTP DEAMINASE: DUTPASE FROM MYCOBACTERIUM TUBERCULOSIS
TITLE 2 IN COMPLEX WITH DTTP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYCYTIDINE TRIPHOSPHATE DEAMINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DCTP DEAMINASE;
COMPND 5 EC: 3.5.4.13;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DCD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET11A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTBDCD7
KEYWDS DISTORTED BETA BARREL, HYDROLASE, NUCLEOTIDE METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHRISTOPHERSEN,P.HARRIS,M.WILLEMOES
REVDAT 4 30-AUG-23 2QXX 1 REMARK LINK
REVDAT 3 13-JUL-11 2QXX 1 VERSN
REVDAT 2 24-FEB-09 2QXX 1 VERSN
REVDAT 1 19-FEB-08 2QXX 0
JRNL AUTH S.S.HELT,M.THYMARK,P.HARRIS,C.AAGAARD,J.DIETRICH,S.LARSEN,
JRNL AUTH 2 M.WILLEMOES
JRNL TITL MECHANISM OF DTTP INHIBITION OF THE BIFUNCTIONAL DCTP
JRNL TITL 2 DEAMINASE:DUTPASE ENCODED BY MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J.MOL.BIOL. V. 376 554 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18164314
JRNL DOI 10.1016/J.JMB.2007.11.099
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 19.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22234
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1112
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) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1535
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2924
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 169
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.71000
REMARK 3 B22 (A**2) : 0.71000
REMARK 3 B33 (A**2) : 0.71000
REMARK 3 B12 (A**2) : -1.08000
REMARK 3 B13 (A**2) : -1.08000
REMARK 3 B23 (A**2) : -1.08000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.201
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.257
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3071 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4170 ; 1.378 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 5.953 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;27.765 ;23.182
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 494 ;15.348 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.603 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 460 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2308 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1166 ; 0.227 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2060 ; 0.320 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 341 ; 0.220 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.009 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 179 ; 0.250 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 68 ; 0.238 ; 0.500
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): 1921 ; 2.070 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3040 ; 2.995 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1263 ; 2.434 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1130 ; 3.299 ; 6.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 112 4
REMARK 3 1 B 1 B 112 4
REMARK 3 2 A 118 A 180 4
REMARK 3 2 B 118 B 180 4
REMARK 3 3 A 201 A 202 4
REMARK 3 3 B 201 B 202 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1377 ; 0.190 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1377 ; 0.870 ; 2.000
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: NULL
REMARK 4
REMARK 4 2QXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000044183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0100
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.59500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1XS1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 MG/ML ENZYME IN 20 MM MGCL2, 5MM
REMARK 280 DTTP, 50MM HEPES PH 6.8 RESERVOIR SOLUTION: 45% PEG 400, 200MM
REMARK 280 MGCL2, 100 MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: R 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 Z,X,Y
REMARK 290 3555 Y,Z,X
REMARK 290 4555 -Y,-X,-Z
REMARK 290 5555 -X,-Z,-Y
REMARK 290 6555 -Z,-Y,-X
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 0.329691 0.234083 0.914609 0.00000
REMARK 290 SMTRY2 2 0.944089 -0.081745 -0.319396 0.00000
REMARK 290 SMTRY3 2 0.000000 0.968774 -0.247945 0.00000
REMARK 290 SMTRY1 3 0.329691 0.944089 0.000000 0.00000
REMARK 290 SMTRY2 3 0.234083 -0.081745 0.968774 0.00000
REMARK 290 SMTRY3 3 0.914609 -0.319396 -0.247945 0.00000
REMARK 290 SMTRY1 4 -0.329691 -0.944089 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.944089 0.329691 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -0.247945 -0.968774 0.00000
REMARK 290 SMTRY3 5 0.000000 -0.968774 0.247945 0.00000
REMARK 290 SMTRY1 6 -0.329691 -0.234083 -0.914609 0.00000
REMARK 290 SMTRY2 6 -0.234083 -0.918255 0.319396 0.00000
REMARK 290 SMTRY3 6 -0.914609 0.319396 0.247945 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 15550 ANGSTROM**2
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 350 BIOMT1 2 0.329691 0.234083 0.914609 0.00000
REMARK 350 BIOMT2 2 0.944089 -0.081745 -0.319396 0.00000
REMARK 350 BIOMT3 2 0.000000 0.968774 -0.247945 0.00000
REMARK 350 BIOMT1 3 0.329691 0.944089 0.000000 0.00000
REMARK 350 BIOMT2 3 0.234083 -0.081745 0.968774 0.00000
REMARK 350 BIOMT3 3 0.914609 -0.319396 -0.247945 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 15680 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 0.329691 0.234083 0.914609 0.00000
REMARK 350 BIOMT2 2 0.944089 -0.081745 -0.319396 0.00000
REMARK 350 BIOMT3 2 0.000000 0.968774 -0.247945 0.00000
REMARK 350 BIOMT1 3 0.329691 0.944089 0.000000 0.00000
REMARK 350 BIOMT2 3 0.234083 -0.081745 0.968774 0.00000
REMARK 350 BIOMT3 3 0.914609 -0.319396 -0.247945 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 THR A 190
REMARK 465 THR B 190
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 O HOH A 213 O HOH A 285 1.65
REMARK 500 O HOH B 235 O HOH B 282 1.95
REMARK 500 O HOH A 232 O HOH A 243 2.07
REMARK 500 O LEU B 98 O HOH B 285 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP B 119 O HOH B 272 2555 2.19
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 SER A 30 15.52 -145.93
REMARK 500 SER A 113 57.67 36.67
REMARK 500 ASN A 185 6.94 53.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 203
REMARK 610 1PE B 203
REMARK 610 1PE B 204
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 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TTP A 201 O2B
REMARK 620 2 TTP A 201 O1A 90.1
REMARK 620 3 TTP A 201 O3G 88.3 95.6
REMARK 620 4 HOH A 239 O 175.9 85.9 91.2
REMARK 620 5 HOH A 265 O 89.3 172.7 91.7 94.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TTP B 201 O1A
REMARK 620 2 TTP B 201 O3G 107.7
REMARK 620 3 TTP B 201 O2B 87.2 88.0
REMARK 620 4 HOH B 229 O 85.9 166.1 90.5
REMARK 620 5 HOH B 247 O 96.2 88.1 175.5 92.7
REMARK 620 6 HOH B 268 O 168.1 82.5 87.2 83.6 90.0
REMARK 620 N 1 2 3 4 5
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 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QLP RELATED DB: PDB
REMARK 900 BIFUNCTIONAL DCTP DEAMINASE:DUTPASE FROM MYCOBACTERIUM TUBERCULOSIS,
REMARK 900 APO FORM
DBREF 2QXX A 1 190 UNP O07247 DCD_MYCTU 1 190
DBREF 2QXX B 1 190 UNP O07247 DCD_MYCTU 1 190
SEQRES 1 A 190 MET LEU LEU SER ASP ARG ASP LEU ARG ALA GLU ILE SER
SEQRES 2 A 190 SER GLY ARG LEU GLY ILE ASP PRO PHE ASP ASP THR LEU
SEQRES 3 A 190 VAL GLN PRO SER SER ILE ASP VAL ARG LEU ASP CYS LEU
SEQRES 4 A 190 PHE ARG VAL PHE ASN ASN THR ARG TYR THR HIS ILE ASP
SEQRES 5 A 190 PRO ALA LYS GLN GLN ASP GLU LEU THR SER LEU VAL GLN
SEQRES 6 A 190 PRO VAL ASP GLY GLU PRO PHE VAL LEU HIS PRO GLY GLU
SEQRES 7 A 190 PHE VAL LEU GLY SER THR LEU GLU LEU PHE THR LEU PRO
SEQRES 8 A 190 ASP ASN LEU ALA GLY ARG LEU GLU GLY LYS SER SER LEU
SEQRES 9 A 190 GLY ARG LEU GLY LEU LEU THR HIS SER THR ALA GLY PHE
SEQRES 10 A 190 ILE ASP PRO GLY PHE SER GLY HIS ILE THR LEU GLU LEU
SEQRES 11 A 190 SER ASN VAL ALA ASN LEU PRO ILE THR LEU TRP PRO GLY
SEQRES 12 A 190 MET LYS ILE GLY GLN LEU CYS MET LEU ARG LEU THR SER
SEQRES 13 A 190 PRO SER GLU HIS PRO TYR GLY SER SER ARG ALA GLY SER
SEQRES 14 A 190 LYS TYR GLN GLY GLN ARG GLY PRO THR PRO SER ARG SER
SEQRES 15 A 190 TYR GLN ASN PHE ILE ARG SER THR
SEQRES 1 B 190 MET LEU LEU SER ASP ARG ASP LEU ARG ALA GLU ILE SER
SEQRES 2 B 190 SER GLY ARG LEU GLY ILE ASP PRO PHE ASP ASP THR LEU
SEQRES 3 B 190 VAL GLN PRO SER SER ILE ASP VAL ARG LEU ASP CYS LEU
SEQRES 4 B 190 PHE ARG VAL PHE ASN ASN THR ARG TYR THR HIS ILE ASP
SEQRES 5 B 190 PRO ALA LYS GLN GLN ASP GLU LEU THR SER LEU VAL GLN
SEQRES 6 B 190 PRO VAL ASP GLY GLU PRO PHE VAL LEU HIS PRO GLY GLU
SEQRES 7 B 190 PHE VAL LEU GLY SER THR LEU GLU LEU PHE THR LEU PRO
SEQRES 8 B 190 ASP ASN LEU ALA GLY ARG LEU GLU GLY LYS SER SER LEU
SEQRES 9 B 190 GLY ARG LEU GLY LEU LEU THR HIS SER THR ALA GLY PHE
SEQRES 10 B 190 ILE ASP PRO GLY PHE SER GLY HIS ILE THR LEU GLU LEU
SEQRES 11 B 190 SER ASN VAL ALA ASN LEU PRO ILE THR LEU TRP PRO GLY
SEQRES 12 B 190 MET LYS ILE GLY GLN LEU CYS MET LEU ARG LEU THR SER
SEQRES 13 B 190 PRO SER GLU HIS PRO TYR GLY SER SER ARG ALA GLY SER
SEQRES 14 B 190 LYS TYR GLN GLY GLN ARG GLY PRO THR PRO SER ARG SER
SEQRES 15 B 190 TYR GLN ASN PHE ILE ARG SER THR
HET MG A 202 1
HET TTP A 201 29
HET 1PE A 203 10
HET MG B 202 1
HET TTP B 201 29
HET 1PE B 203 7
HET 1PE B 204 7
HETNAM MG MAGNESIUM ION
HETNAM TTP THYMIDINE-5'-TRIPHOSPHATE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 MG 2(MG 2+)
FORMUL 4 TTP 2(C10 H17 N2 O14 P3)
FORMUL 5 1PE 3(C10 H22 O6)
FORMUL 10 HOH *169(H2 O)
HELIX 1 1 SER A 4 SER A 14 1 11
HELIX 2 2 ASP A 23 THR A 25 5 3
HELIX 3 3 GLN A 57 THR A 61 5 5
HELIX 4 4 LYS A 101 ARG A 106 1 6
HELIX 5 5 SER B 4 SER B 14 1 11
HELIX 6 6 ASP B 23 THR B 25 5 3
HELIX 7 7 GLN B 57 THR B 61 5 5
HELIX 8 8 LYS B 101 ARG B 106 1 6
SHEET 1 A 3 GLY A 18 ASP A 20 0
SHEET 2 A 3 LEU A 87 THR A 89 -1 O THR A 89 N GLY A 18
SHEET 3 A 3 SER A 123 GLY A 124 -1 O GLY A 124 N PHE A 88
SHEET 1 B 5 VAL A 27 GLN A 28 0
SHEET 2 B 5 SER A 31 ARG A 35 -1 O SER A 31 N GLN A 28
SHEET 3 B 5 LYS A 145 ARG A 153 -1 O LEU A 149 N ILE A 32
SHEET 4 B 5 LEU A 94 GLU A 99 -1 N ALA A 95 O LEU A 152
SHEET 5 B 5 PHE A 117 ILE A 118 -1 O ILE A 118 N GLY A 96
SHEET 1 C 2 PHE A 40 VAL A 42 0
SHEET 2 C 2 SER A 62 VAL A 64 -1 O VAL A 64 N PHE A 40
SHEET 1 D 2 PHE A 72 LEU A 74 0
SHEET 2 D 2 ILE A 138 LEU A 140 -1 O LEU A 140 N PHE A 72
SHEET 1 E 3 PHE A 79 SER A 83 0
SHEET 2 E 3 THR A 127 ASN A 132 -1 O LEU A 128 N GLY A 82
SHEET 3 E 3 LEU A 109 THR A 111 -1 N LEU A 110 O SER A 131
SHEET 1 F 3 GLY B 18 ASP B 20 0
SHEET 2 F 3 LEU B 87 THR B 89 -1 O LEU B 87 N ASP B 20
SHEET 3 F 3 SER B 123 GLY B 124 -1 O GLY B 124 N PHE B 88
SHEET 1 G 5 VAL B 27 GLN B 28 0
SHEET 2 G 5 SER B 31 ARG B 35 -1 O SER B 31 N GLN B 28
SHEET 3 G 5 LYS B 145 ARG B 153 -1 O LEU B 149 N ILE B 32
SHEET 4 G 5 LEU B 94 GLU B 99 -1 N ALA B 95 O LEU B 152
SHEET 5 G 5 PHE B 117 ILE B 118 -1 O ILE B 118 N GLY B 96
SHEET 1 H 5 SER B 62 VAL B 64 0
SHEET 2 H 5 PHE B 40 VAL B 42 -1 N PHE B 40 O VAL B 64
SHEET 3 H 5 PHE B 79 SER B 83 -1 O LEU B 81 N ARG B 41
SHEET 4 H 5 THR B 127 ASN B 132 -1 O LEU B 128 N GLY B 82
SHEET 5 H 5 LEU B 109 THR B 111 -1 N LEU B 110 O SER B 131
SHEET 1 I 2 PHE B 72 LEU B 74 0
SHEET 2 I 2 ILE B 138 LEU B 140 -1 O LEU B 140 N PHE B 72
LINK O2B TTP A 201 MG MG A 202 1555 1555 2.12
LINK O1A TTP A 201 MG MG A 202 1555 1555 2.04
LINK O3G TTP A 201 MG MG A 202 1555 1555 2.01
LINK MG MG A 202 O HOH A 239 1555 1555 2.02
LINK MG MG A 202 O HOH A 265 1555 1555 1.98
LINK O1A TTP B 201 MG MG B 202 1555 1555 2.01
LINK O3G TTP B 201 MG MG B 202 1555 1555 2.08
LINK O2B TTP B 201 MG MG B 202 1555 1555 2.11
LINK MG MG B 202 O HOH B 229 1555 1555 2.09
LINK MG MG B 202 O HOH B 247 1555 1555 2.01
LINK MG MG B 202 O HOH B 268 1555 1555 2.14
CISPEP 1 ASP A 20 PRO A 21 0 -2.70
CISPEP 2 ASP B 20 PRO B 21 0 0.53
SITE 1 AC1 4 TTP A 201 HOH A 237 HOH A 239 HOH A 265
SITE 1 AC2 4 TTP B 201 HOH B 229 HOH B 247 HOH B 268
SITE 1 AC3 25 LYS A 101 SER A 102 SER A 103 ARG A 106
SITE 2 AC3 25 ALA A 115 GLY A 116 PHE A 117 ILE A 118
SITE 3 AC3 25 ASP A 119 ILE A 126 THR A 127 GLN A 148
SITE 4 AC3 25 TYR A 162 SER A 169 LYS A 170 TYR A 171
SITE 5 AC3 25 GLN A 174 MG A 202 HOH A 233 HOH A 237
SITE 6 AC3 25 HOH A 239 HOH A 240 HOH A 243 HOH A 265
SITE 7 AC3 25 HOH A 288
SITE 1 AC4 4 ARG A 47 TYR A 48 THR A 49 GLN A 57
SITE 1 AC5 25 LYS B 101 SER B 102 SER B 103 ARG B 106
SITE 2 AC5 25 ALA B 115 GLY B 116 PHE B 117 ASP B 119
SITE 3 AC5 25 ILE B 126 THR B 127 GLN B 148 TYR B 162
SITE 4 AC5 25 SER B 169 LYS B 170 TYR B 171 GLN B 174
SITE 5 AC5 25 MG B 202 HOH B 228 HOH B 229 HOH B 234
SITE 6 AC5 25 HOH B 235 HOH B 237 HOH B 247 HOH B 268
SITE 7 AC5 25 HOH B 279
SITE 1 AC6 3 GLY B 15 ARG B 16 THR B 89
SITE 1 AC7 5 ARG B 47 TYR B 48 THR B 49 GLN B 57
SITE 2 AC7 5 SER B 165
CRYST1 82.640 82.640 82.640 70.75 70.75 70.75 R 3 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 0.012101 -0.004226 -0.003280 0.00000
SCALE2 0.000000 0.012817 -0.003280 0.00000
SCALE3 0.000000 0.000000 0.013230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
