HEADER TRANSFERASE 14-AUG-09 3IOM
TITLE CRYSTAL STRUCTURE OF PURINE NUCLEOSIDE PHOSPHORYLASE FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH 2'-DEOXYGUANOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE NUCLEOSIDE PHOSPHORYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PNP, INOSINE PHOSPHORYLASE;
COMPND 5 EC: 2.4.2.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 5 GENE: DEOD, MT3406, MTV016.06, PUNA, PUNA (DEOD) (RV3307) (MT3406)
SOURCE 6 (MTV016.06), RV3307;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PURINE NUCLEOSIDE PHOSPHORYLASE, MYCOBACTERIUM TUBERCULOSIS, 2 -
KEYWDS 2 DEOXYGUANOSINE, GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.F.DE AZEVEDO JR.,L.A.BASSO,D.S.SANTOS
REVDAT 3 06-SEP-23 3IOM 1 REMARK
REVDAT 2 22-JUN-11 3IOM 1 JRNL
REVDAT 1 12-JAN-11 3IOM 0
JRNL AUTH R.G.DUCATI,L.A.BASSO,D.S.SANTOS,W.F.DE AZEVEDO
JRNL TITL CRYSTALLOGRAPHIC AND DOCKING STUDIES OF PURINE NUCLEOSIDE
JRNL TITL 2 PHOSPHORYLASE FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF BIOORG.MED.CHEM. V. 18 4769 2010
JRNL REFN ISSN 0968-0896
JRNL PMID 20570524
JRNL DOI 10.1016/J.BMC.2010.05.009
REMARK 2
REMARK 2 RESOLUTION. 2.14 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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 21023
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
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) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1406
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.1690
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.352
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.239
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3914 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5362 ; 1.976 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 7.205 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;38.750 ;22.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 556 ;16.849 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;20.874 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2984 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2228 ; 0.252 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2684 ; 0.319 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 324 ; 0.193 ; 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): 146 ; 0.237 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.207 ; 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): 2598 ; 1.023 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4132 ; 1.780 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1316 ; 2.904 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1230 ; 4.563 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3IOM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : D03B-MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.42800
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22163
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 28.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.13800
REMARK 200 R SYM FOR SHELL (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1G2O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS COCRYSTALLIZED WITH A
REMARK 280 1:0.5:1 STOICHIOMETRY OF 500 MM NA2SO4 (MERCK) AND 3 MM 2DGUO
REMARK 280 (FLUKA BIOCHEMIKA), RESPECTIVELY, BY HANGING-DROP VAPOR
REMARK 280 DIFFUSION AT 18 C. MTPNP PROTEIN (1 L OF 25 MG ML-1 IN 50 MM
REMARK 280 TRIS(HYDROXYMETHYL)AMINOMETHANE (TRIS) PH 7.6) HAD BEEN
REMARK 280 PREVIOUSLY MIXED WITH AN EQUAL VOLUME OF THE RESERVOIR SOLUTION
REMARK 280 CONTAINING 100 MM TRIS PH 8.0, 25% POLY(ETHYLENE GLYCOL) (PEG)
REMARK 280 3350, AND 25 MM MGCL2 AND HANGING DROPS (3.5 L) WERE
REMARK 280 EQUILIBRATED AGAINST 400 L OF THE RESERVOIR SOLUTION. , VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.74000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.75885
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.33700
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 56.74000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 32.75885
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.33700
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 56.74000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 32.75885
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.33700
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.51771
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 56.67400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 65.51771
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 56.67400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 65.51771
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 56.67400
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 300 REMARK: 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
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 -0.500000 -0.866025 0.000000 56.74000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -98.27656
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 113.48000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
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 -0.500000 -0.866025 0.000000 56.74000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -98.27656
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 113.48000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 29 CB ASP A 29 CG 0.241
REMARK 500 GLU A 152 CG GLU A 152 CD 0.103
REMARK 500 GLU A 166 CB GLU A 166 CG 0.156
REMARK 500 GLU A 166 CG GLU A 166 CD 0.103
REMARK 500 GLU A 245 CG GLU A 245 CD 0.092
REMARK 500 GLU B 166 CB GLU B 166 CG 0.114
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 A 81 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU A 135 CB - CG - CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU B 11 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG B 13 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 108 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 125 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 217 NE - CZ - NH2 ANGL. DEV. = -3.1 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 THR A 64 -148.60 -100.10
REMARK 500 ALA A 65 84.61 12.56
REMARK 500 HIS A 68 73.39 -68.52
REMARK 500 ALA A 69 171.63 -40.83
REMARK 500 ALA A 79 39.33 -88.66
REMARK 500 SER A 208 -151.92 -145.00
REMARK 500 THR A 209 -44.38 71.89
REMARK 500 ALA B 55 -57.00 -20.54
REMARK 500 VAL B 61 90.35 -68.95
REMARK 500 THR B 64 104.48 -24.55
REMARK 500 ALA B 65 173.74 164.48
REMARK 500 ALA B 66 -137.24 106.00
REMARK 500 HIS B 68 -150.12 -149.88
REMARK 500 ALA B 69 -164.82 -165.30
REMARK 500 SER B 161 113.23 -35.95
REMARK 500 SER B 208 -152.28 -150.68
REMARK 500 THR B 209 -49.57 71.37
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNG A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNG B 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G2O RELATED DB: PDB
DBREF 3IOM A 1 268 UNP P0A538 PUNA_MYCTU 1 268
DBREF 3IOM B 1 268 UNP P0A538 PUNA_MYCTU 1 268
SEQRES 1 A 268 MET ALA ASP PRO ARG PRO ASP PRO ASP GLU LEU ALA ARG
SEQRES 2 A 268 ARG ALA ALA GLN VAL ILE ALA ASP ARG THR GLY ILE GLY
SEQRES 3 A 268 GLU HIS ASP VAL ALA VAL VAL LEU GLY SER GLY TRP LEU
SEQRES 4 A 268 PRO ALA VAL ALA ALA LEU GLY SER PRO THR THR VAL LEU
SEQRES 5 A 268 PRO GLN ALA GLU LEU PRO GLY PHE VAL PRO PRO THR ALA
SEQRES 6 A 268 ALA GLY HIS ALA GLY GLU LEU LEU SER VAL PRO ILE GLY
SEQRES 7 A 268 ALA HIS ARG VAL LEU VAL LEU ALA GLY ARG ILE HIS ALA
SEQRES 8 A 268 TYR GLU GLY HIS ASP LEU ARG TYR VAL VAL HIS PRO VAL
SEQRES 9 A 268 ARG ALA ALA ARG ALA ALA GLY ALA GLN ILE MET VAL LEU
SEQRES 10 A 268 THR ASN ALA ALA GLY GLY LEU ARG ALA ASP LEU GLN VAL
SEQRES 11 A 268 GLY GLN PRO VAL LEU ILE SER ASP HIS LEU ASN LEU THR
SEQRES 12 A 268 ALA ARG SER PRO LEU VAL GLY GLY GLU PHE VAL ASP LEU
SEQRES 13 A 268 THR ASP ALA TYR SER PRO ARG LEU ARG GLU LEU ALA ARG
SEQRES 14 A 268 GLN SER ASP PRO GLN LEU ALA GLU GLY VAL TYR ALA GLY
SEQRES 15 A 268 LEU PRO GLY PRO HIS TYR GLU THR PRO ALA GLU ILE ARG
SEQRES 16 A 268 MET LEU GLN THR LEU GLY ALA ASP LEU VAL GLY MET SER
SEQRES 17 A 268 THR VAL HIS GLU THR ILE ALA ALA ARG ALA ALA GLY ALA
SEQRES 18 A 268 GLU VAL LEU GLY VAL SER LEU VAL THR ASN LEU ALA ALA
SEQRES 19 A 268 GLY ILE THR GLY GLU PRO LEU SER HIS ALA GLU VAL LEU
SEQRES 20 A 268 ALA ALA GLY ALA ALA SER ALA THR ARG MET GLY ALA LEU
SEQRES 21 A 268 LEU ALA ASP VAL ILE ALA ARG PHE
SEQRES 1 B 268 MET ALA ASP PRO ARG PRO ASP PRO ASP GLU LEU ALA ARG
SEQRES 2 B 268 ARG ALA ALA GLN VAL ILE ALA ASP ARG THR GLY ILE GLY
SEQRES 3 B 268 GLU HIS ASP VAL ALA VAL VAL LEU GLY SER GLY TRP LEU
SEQRES 4 B 268 PRO ALA VAL ALA ALA LEU GLY SER PRO THR THR VAL LEU
SEQRES 5 B 268 PRO GLN ALA GLU LEU PRO GLY PHE VAL PRO PRO THR ALA
SEQRES 6 B 268 ALA GLY HIS ALA GLY GLU LEU LEU SER VAL PRO ILE GLY
SEQRES 7 B 268 ALA HIS ARG VAL LEU VAL LEU ALA GLY ARG ILE HIS ALA
SEQRES 8 B 268 TYR GLU GLY HIS ASP LEU ARG TYR VAL VAL HIS PRO VAL
SEQRES 9 B 268 ARG ALA ALA ARG ALA ALA GLY ALA GLN ILE MET VAL LEU
SEQRES 10 B 268 THR ASN ALA ALA GLY GLY LEU ARG ALA ASP LEU GLN VAL
SEQRES 11 B 268 GLY GLN PRO VAL LEU ILE SER ASP HIS LEU ASN LEU THR
SEQRES 12 B 268 ALA ARG SER PRO LEU VAL GLY GLY GLU PHE VAL ASP LEU
SEQRES 13 B 268 THR ASP ALA TYR SER PRO ARG LEU ARG GLU LEU ALA ARG
SEQRES 14 B 268 GLN SER ASP PRO GLN LEU ALA GLU GLY VAL TYR ALA GLY
SEQRES 15 B 268 LEU PRO GLY PRO HIS TYR GLU THR PRO ALA GLU ILE ARG
SEQRES 16 B 268 MET LEU GLN THR LEU GLY ALA ASP LEU VAL GLY MET SER
SEQRES 17 B 268 THR VAL HIS GLU THR ILE ALA ALA ARG ALA ALA GLY ALA
SEQRES 18 B 268 GLU VAL LEU GLY VAL SER LEU VAL THR ASN LEU ALA ALA
SEQRES 19 B 268 GLY ILE THR GLY GLU PRO LEU SER HIS ALA GLU VAL LEU
SEQRES 20 B 268 ALA ALA GLY ALA ALA SER ALA THR ARG MET GLY ALA LEU
SEQRES 21 B 268 LEU ALA ASP VAL ILE ALA ARG PHE
HET SO4 A 301 5
HET GNG A 800 19
HET SO4 B 302 5
HET GNG B 801 19
HETNAM SO4 SULFATE ION
HETNAM GNG 2'-DEOXY-GUANOSINE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 GNG 2(C10 H13 N5 O4)
FORMUL 7 HOH *209(H2 O)
HELIX 1 1 ASP A 7 GLY A 24 1 18
HELIX 2 2 TRP A 38 PRO A 40 5 3
HELIX 3 3 ALA A 41 GLY A 46 1 6
HELIX 4 4 ALA A 55 LEU A 57 5 3
HELIX 5 5 HIS A 90 GLY A 94 5 5
HELIX 6 6 ASP A 96 ALA A 110 1 15
HELIX 7 7 SER A 161 ASP A 172 1 12
HELIX 8 8 THR A 190 GLY A 201 1 12
HELIX 9 9 THR A 209 ALA A 219 1 11
HELIX 10 10 SER A 242 PHE A 268 1 27
HELIX 11 11 ASP B 7 GLY B 24 1 18
HELIX 12 12 TRP B 38 PRO B 40 5 3
HELIX 13 13 ALA B 41 GLY B 46 1 6
HELIX 14 14 ALA B 55 LEU B 57 5 3
HELIX 15 15 HIS B 90 GLY B 94 5 5
HELIX 16 16 ASP B 96 VAL B 101 1 6
HELIX 17 17 VAL B 101 ALA B 110 1 10
HELIX 18 18 SER B 161 ASP B 172 1 12
HELIX 19 19 THR B 190 LEU B 200 1 11
HELIX 20 20 THR B 209 ALA B 219 1 11
HELIX 21 21 SER B 242 PHE B 268 1 27
SHEET 1 A10 THR A 50 PRO A 53 0
SHEET 2 A10 GLU A 71 ILE A 77 -1 O LEU A 72 N LEU A 52
SHEET 3 A10 HIS A 80 ALA A 86 -1 O VAL A 84 N LEU A 73
SHEET 4 A10 VAL A 30 VAL A 33 1 N VAL A 32 O LEU A 85
SHEET 5 A10 ILE A 114 GLY A 123 1 O VAL A 116 N ALA A 31
SHEET 6 A10 GLU A 222 LEU A 232 1 O GLU A 222 N MET A 115
SHEET 7 A10 PRO A 133 ASN A 141 -1 N VAL A 134 O SER A 227
SHEET 8 A10 ALA A 176 GLY A 182 1 O GLY A 182 N LEU A 140
SHEET 9 A10 LEU A 204 GLY A 206 1 O GLY A 206 N ALA A 181
SHEET 10 A10 ILE A 114 GLY A 123 -1 N GLY A 122 O VAL A 205
SHEET 1 B10 THR B 50 PRO B 53 0
SHEET 2 B10 GLU B 71 ILE B 77 -1 O LEU B 72 N LEU B 52
SHEET 3 B10 HIS B 80 ALA B 86 -1 O VAL B 84 N LEU B 73
SHEET 4 B10 VAL B 30 LEU B 34 1 N VAL B 32 O LEU B 85
SHEET 5 B10 ILE B 114 GLY B 123 1 O VAL B 116 N VAL B 33
SHEET 6 B10 GLU B 222 LEU B 232 1 O LEU B 228 N ASN B 119
SHEET 7 B10 PRO B 133 ASN B 141 -1 N VAL B 134 O SER B 227
SHEET 8 B10 ALA B 176 GLY B 182 1 O GLY B 182 N LEU B 140
SHEET 9 B10 LEU B 204 GLY B 206 1 O LEU B 204 N ALA B 181
SHEET 10 B10 ILE B 114 GLY B 123 -1 N GLY B 122 O VAL B 205
CISPEP 1 GLY A 185 PRO A 186 0 4.11
CISPEP 2 GLY B 185 PRO B 186 0 4.94
SITE 1 AC1 9 GLY A 35 SER A 36 ARG A 88 HIS A 90
SITE 2 AC1 9 THR A 118 ASN A 119 SER A 208 HOH A 334
SITE 3 AC1 9 GNG A 800
SITE 1 AC2 15 SER A 36 ALA A 120 GLY A 122 TYR A 188
SITE 2 AC2 15 GLU A 189 VAL A 205 GLY A 206 MET A 207
SITE 3 AC2 15 THR A 230 ASN A 231 LEU A 241 HIS A 243
SITE 4 AC2 15 VAL A 246 SO4 A 301 HOH A 369
SITE 1 AC3 10 GLY B 35 SER B 36 ARG B 88 HIS B 90
SITE 2 AC3 10 ASN B 119 ALA B 120 SER B 208 HOH B 296
SITE 3 AC3 10 HOH B 299 GNG B 801
SITE 1 AC4 17 SER B 36 ALA B 120 ALA B 121 GLY B 122
SITE 2 AC4 17 TYR B 188 GLU B 189 VAL B 205 GLY B 206
SITE 3 AC4 17 MET B 207 THR B 230 ASN B 231 LEU B 241
SITE 4 AC4 17 HIS B 243 VAL B 246 HOH B 293 HOH B 299
SITE 5 AC4 17 SO4 B 302
CRYST1 113.480 113.480 85.011 90.00 90.00 120.00 H 3 18
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 0.008812 0.005088 0.000000 0.00000
SCALE2 0.000000 0.010175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011763 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
