HEADER HYDROLASE 15-OCT-09 2WV9
TITLE CRYSTAL STRUCTURE OF THE NS3 PROTEASE-HELICASE FROM MURRAY VALLEY
TITLE 2 ENCEPHALITIS VIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVIVIRIN PROTEASE NS2B REGULATORY SUBUNIT, FLAVIVIRIN
COMPND 3 PROTEASE NS3 CATALYTIC SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: NS2B, RESIDUES 1421-1465;
COMPND 6 EC: 3.4.21.91;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: PARTIAL POLYPROTEIN FRAGMENT OF NS2B FRAGMENT
COMPND 9 SEPARATED FROM NS3 BY A SEQUENCE ENCODING A NINE AMINO ACID LINKER
COMPND 10 (GGGGSGGGG).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MURRAY VALLEY ENCEPHALITIS VIRUS;
SOURCE 3 ORGANISM_TAXID: 301478;
SOURCE 4 STRAIN: MVE-1-51;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: OPPF4631
KEYWDS NUCLEOTIDE-BINDING, CAPSID PROTEIN, RNA REPLICATION, ENVELOPE
KEYWDS 2 PROTEIN, VIRION, HELICASE, HYDROLASE, FLAVIVIRUS,
KEYWDS 3 NUCLEOTIDYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ASSENBERG,E.MASTRANGELO,T.S.WALTER,A.VERMA,M.MILANI,R.J.OWENS,
AUTHOR 2 D.I.STUART,J.M.GRIMES,E.J.MANCINI
REVDAT 4 20-DEC-23 2WV9 1 REMARK
REVDAT 3 13-JUL-11 2WV9 1 VERSN
REVDAT 2 02-FEB-10 2WV9 1 KEYWDS REMARK
REVDAT 1 01-DEC-09 2WV9 0
JRNL AUTH R.ASSENBERG,E.MASTRANGELO,T.S.WALTER,A.VERMA,M.MILANI,
JRNL AUTH 2 R.J.OWENS,D.I.STUART,J.M.GRIMES,E.J.MANCINI
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL CONFORMATIONAL STATE OF THE
JRNL TITL 2 FLAVIVIRUS NS3 PROTEIN: IMPLICATIONS FOR POLYPROTEIN
JRNL TITL 3 PROCESSING AND VIRAL REPLICATION.
JRNL REF J.VIROL. V. 83 12895 2009
JRNL REFN ISSN 0022-538X
JRNL PMID 19793813
JRNL DOI 10.1128/JVI.00942-09
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 16866
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) : 0.268
REMARK 3 R VALUE (WORKING SET) : 0.267
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 884
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1226
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4677
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 89
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) : 6.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : 2.68000
REMARK 3 B33 (A**2) : -2.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.448
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.353
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.858
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4785 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6496 ; 0.899 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 596 ; 4.431 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;30.945 ;23.349
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 783 ;13.854 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;13.516 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 708 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3659 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1975 ; 0.169 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3158 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.112 ; 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): 56 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.084 ; 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): 2977 ; 0.145 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4792 ; 0.267 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1808 ; 0.246 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1704 ; 0.434 ; 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 18 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4570 18.7450 -3.2840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2974 T22: 0.3084
REMARK 3 T33: 0.3836 T12: 0.0630
REMARK 3 T13: 0.0130 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 6.2672 L22: 1.9974
REMARK 3 L33: 9.5093 L12: -1.8811
REMARK 3 L13: 0.9212 L23: 2.3319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: 0.0395 S13: -0.5225
REMARK 3 S21: 0.2787 S22: 0.1116 S23: 0.1606
REMARK 3 S31: 0.7028 S32: -0.1374 S33: -0.0980
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 178 A 618
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0800 1.8400 36.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5660 T22: 0.5197
REMARK 3 T33: 0.4979 T12: 0.0454
REMARK 3 T13: -0.0094 T23: -0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 1.1220 L22: 1.1232
REMARK 3 L33: 1.6620 L12: -0.3592
REMARK 3 L13: -0.3278 L23: -0.7861
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: -0.2287 S13: -0.2115
REMARK 3 S21: -0.1027 S22: -0.0566 S23: 0.1819
REMARK 3 S31: 0.3450 S32: 0.0528 S33: 0.0837
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 -52 A -33
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3470 28.8930 -8.0850
REMARK 3 T TENSOR
REMARK 3 T11: 0.7643 T22: 0.3206
REMARK 3 T33: 0.9305 T12: -0.0214
REMARK 3 T13: -0.5065 T23: 0.2131
REMARK 3 L TENSOR
REMARK 3 L11: 38.0168 L22: 4.5175
REMARK 3 L33: 22.9086 L12: 0.4849
REMARK 3 L13: 2.2513 L23: 6.4686
REMARK 3 S TENSOR
REMARK 3 S11: -2.0526 S12: 2.8620 S13: 4.9487
REMARK 3 S21: -0.1339 S22: 0.4021 S23: -0.1866
REMARK 3 S31: -2.9047 S32: -0.2462 S33: 1.6505
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2WV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12710
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17750
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 43.937
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : NULL
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 ENTRIES 2V8O, 2IJO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 20% POLYETHYLENE
REMARK 280 GLYCOL 6000, 200 MM MAGNESIUM CHLORIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 52.73000
REMARK 290 SMTRY3 2 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 GLY A -32
REMARK 465 THR A -31
REMARK 465 SER A -30
REMARK 465 GLU A -29
REMARK 465 ARG A -28
REMARK 465 LEU A -27
REMARK 465 ASP A -26
REMARK 465 VAL A -25
REMARK 465 GLN A -24
REMARK 465 LEU A -23
REMARK 465 ASP A -22
REMARK 465 ASP A -21
REMARK 465 ASP A -20
REMARK 465 GLY A -19
REMARK 465 ASP A -18
REMARK 465 PHE A -17
REMARK 465 HIS A -16
REMARK 465 LEU A -15
REMARK 465 LEU A -14
REMARK 465 ASN A -13
REMARK 465 ASP A -12
REMARK 465 PRO A -11
REMARK 465 GLY A -10
REMARK 465 VAL A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLY A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 GLY A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 GLY A 0
REMARK 465 GLY A 1
REMARK 465 GLY A 2
REMARK 465 VAL A 3
REMARK 465 PHE A 4
REMARK 465 TRP A 5
REMARK 465 ASP A 6
REMARK 465 THR A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 LYS A 11
REMARK 465 VAL A 12
REMARK 465 TYR A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 GLY A 16
REMARK 465 ASP A 17
REMARK 465 GLU A 169
REMARK 465 ARG A 170
REMARK 465 VAL A 171
REMARK 465 GLU A 172
REMARK 465 GLU A 173
REMARK 465 PRO A 174
REMARK 465 VAL A 175
REMARK 465 ALA A 247
REMARK 465 VAL A 248
REMARK 465 GLN A 249
REMARK 465 ILE A 582
REMARK 465 ILE A 583
REMARK 465 THR A 584
REMARK 465 ARG A 585
REMARK 465 ILE A 586
REMARK 465 GLY A 587
REMARK 465 GLU A 588
REMARK 465 ARG A 589
REMARK 465 LYS A 590
REMARK 465 VAL A 591
REMARK 465 LEU A 592
REMARK 465 ARG A 619
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 THR A -33 O
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 LYS A 186 O ALA A 310 2.14
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 ASN A 158 -47.16 27.29
REMARK 500 LYS A 200 -71.13 -56.43
REMARK 500 LYS A 539 -60.79 -90.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V8O RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MURRAY VALLEY ENCEPHALITIS VIRUS RNA HELICASE TO
REMARK 900 1.9A RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 49-93 OF PROTEIN NS2B WERE LINKED TO
REMARK 999 RESIDUES 1-618 OF NS3 VIA A SYNTHETIC LINKER (GGGGSGGGG)
REMARK 999 ADDED AT THE C-TERMINUS OF NS2B
DBREF 2WV9 A -53 -9 UNP P05769 POLG_MVEV5 1421 1465
DBREF 2WV9 A -8 0 PDB 2WV9 2WV9 -8 0
DBREF 2WV9 A 1 619 UNP P05769 POLG_MVEV5 1504 2122
SEQRES 1 A 673 ALA THR ASP MET TRP LEU GLU ARG ALA ALA ASP VAL SER
SEQRES 2 A 673 TRP GLU ALA GLY ALA ALA ILE THR GLY THR SER GLU ARG
SEQRES 3 A 673 LEU ASP VAL GLN LEU ASP ASP ASP GLY ASP PHE HIS LEU
SEQRES 4 A 673 LEU ASN ASP PRO GLY VAL GLY GLY GLY GLY SER GLY GLY
SEQRES 5 A 673 GLY GLY GLY GLY VAL PHE TRP ASP THR PRO SER PRO LYS
SEQRES 6 A 673 VAL TYR PRO LYS GLY ASP THR THR PRO GLY VAL TYR ARG
SEQRES 7 A 673 ILE MET ALA ARG GLY ILE LEU GLY ARG TYR GLN ALA GLY
SEQRES 8 A 673 VAL GLY VAL MET HIS GLU GLY VAL PHE HIS THR LEU TRP
SEQRES 9 A 673 HIS THR THR ARG GLY ALA ALA ILE MET SER GLY GLU GLY
SEQRES 10 A 673 ARG LEU THR PRO TYR TRP GLY ASN VAL LYS GLU ASP ARG
SEQRES 11 A 673 VAL THR TYR GLY GLY PRO TRP LYS LEU ASP GLN LYS TRP
SEQRES 12 A 673 ASN GLY VAL ASP ASP VAL GLN MET ILE VAL VAL GLU PRO
SEQRES 13 A 673 GLY LYS PRO ALA ILE ASN VAL GLN THR LYS PRO GLY ILE
SEQRES 14 A 673 PHE LYS THR ALA HIS GLY GLU ILE GLY ALA VAL SER LEU
SEQRES 15 A 673 ASP TYR PRO ILE GLY THR SER GLY SER PRO ILE VAL ASN
SEQRES 16 A 673 SER ASN GLY GLU ILE ILE GLY LEU TYR GLY ASN GLY VAL
SEQRES 17 A 673 ILE LEU GLY ASN GLY ALA TYR VAL SER ALA ILE VAL GLN
SEQRES 18 A 673 GLY GLU ARG VAL GLU GLU PRO VAL PRO GLU ALA TYR ASN
SEQRES 19 A 673 PRO GLU MET LEU LYS LYS ARG GLN LEU THR VAL LEU ASP
SEQRES 20 A 673 LEU HIS PRO GLY ALA GLY LYS THR ARG ARG ILE LEU PRO
SEQRES 21 A 673 GLN ILE ILE LYS ASP ALA ILE GLN LYS ARG LEU ARG THR
SEQRES 22 A 673 ALA VAL LEU ALA PRO THR ARG VAL VAL ALA ALA GLU MET
SEQRES 23 A 673 ALA GLU ALA LEU ARG GLY LEU PRO VAL ARG TYR LEU THR
SEQRES 24 A 673 PRO ALA VAL GLN ARG GLU HIS SER GLY ASN GLU ILE VAL
SEQRES 25 A 673 ASP VAL MET CYS HIS ALA THR LEU THR HIS ARG LEU MET
SEQRES 26 A 673 SER PRO LEU ARG VAL PRO ASN TYR ASN LEU PHE VAL MET
SEQRES 27 A 673 ASP GLU ALA HIS PHE THR ASP PRO ALA SER ILE ALA ALA
SEQRES 28 A 673 ARG GLY TYR ILE ALA THR ARG VAL GLU ALA GLY GLU ALA
SEQRES 29 A 673 ALA ALA ILE PHE MET THR ALA THR PRO PRO GLY THR SER
SEQRES 30 A 673 ASP PRO PHE PRO ASP THR ASN SER PRO VAL HIS ASP VAL
SEQRES 31 A 673 SER SER GLU ILE PRO ASP ARG ALA TRP SER SER GLY PHE
SEQRES 32 A 673 GLU TRP ILE THR ASP TYR ALA GLY LYS THR VAL TRP PHE
SEQRES 33 A 673 VAL ALA SER VAL LYS MET SER ASN GLU ILE ALA GLN CYS
SEQRES 34 A 673 LEU GLN ARG ALA GLY LYS ARG VAL ILE GLN LEU ASN ARG
SEQRES 35 A 673 LYS SER TYR ASP THR GLU TYR PRO LYS CYS LYS ASN GLY
SEQRES 36 A 673 ASP TRP ASP PHE VAL ILE THR THR ASP ILE SER GLU MET
SEQRES 37 A 673 GLY ALA ASN PHE GLY ALA SER ARG VAL ILE ASP CYS ARG
SEQRES 38 A 673 LYS SER VAL LYS PRO THR ILE LEU ASP GLU GLY GLU GLY
SEQRES 39 A 673 ARG VAL ILE LEU SER VAL PRO SER ALA ILE THR SER ALA
SEQRES 40 A 673 SER ALA ALA GLN ARG ARG GLY ARG VAL GLY ARG ASN PRO
SEQRES 41 A 673 SER GLN ILE GLY ASP GLU TYR HIS TYR GLY GLY GLY THR
SEQRES 42 A 673 SER GLU ASP ASP THR MET LEU ALA HIS TRP THR GLU ALA
SEQRES 43 A 673 LYS ILE LEU LEU ASP ASN ILE HIS LEU PRO ASN GLY LEU
SEQRES 44 A 673 VAL ALA GLN LEU TYR GLY PRO GLU ARG ASP LYS THR TYR
SEQRES 45 A 673 THR MET ASP GLY GLU TYR ARG LEU ARG GLY GLU GLU ARG
SEQRES 46 A 673 LYS THR PHE LEU GLU LEU ILE LYS THR ALA ASP LEU PRO
SEQRES 47 A 673 VAL TRP LEU ALA TYR LYS VAL ALA SER ASN GLY ILE GLN
SEQRES 48 A 673 TYR ASN ASP ARG LYS TRP CYS PHE ASP GLY PRO ARG SER
SEQRES 49 A 673 ASN ILE ILE LEU GLU ASP ASN ASN GLU VAL GLU ILE ILE
SEQRES 50 A 673 THR ARG ILE GLY GLU ARG LYS VAL LEU LYS PRO ARG TRP
SEQRES 51 A 673 LEU ASP ALA ARG VAL TYR SER ASP HIS GLN SER LEU LYS
SEQRES 52 A 673 TRP PHE LYS ASP PHE ALA ALA GLY LYS ARG
FORMUL 2 HOH *89(H2 O)
HELIX 1 1 LEU A 49 ARG A 54 1 6
HELIX 2 2 PRO A 131 SER A 135 5 5
HELIX 3 3 ASN A 180 LYS A 185 5 6
HELIX 4 4 ARG A 203 LYS A 215 1 13
HELIX 5 5 THR A 225 LEU A 236 1 12
HELIX 6 6 HIS A 263 SER A 272 1 10
HELIX 7 7 ASP A 291 ALA A 307 1 17
HELIX 8 8 PHE A 349 ASP A 354 1 6
HELIX 9 9 SER A 365 ARG A 378 1 14
HELIX 10 10 SER A 390 TYR A 395 1 6
HELIX 11 11 PRO A 396 ASN A 400 5 5
HELIX 12 12 ASP A 410 MET A 414 5 5
HELIX 13 13 THR A 451 GLY A 460 1 10
HELIX 14 14 ALA A 487 ASN A 498 1 12
HELIX 15 15 TYR A 510 THR A 517 5 8
HELIX 16 16 ARG A 527 THR A 540 1 14
HELIX 17 17 PRO A 544 GLY A 555 1 12
HELIX 18 18 ARG A 561 PHE A 565 5 5
HELIX 19 19 ARG A 600 TYR A 602 5 3
HELIX 20 20 ASP A 604 GLY A 617 1 14
SHEET 1 AA 8 ARG A 64 LEU A 65 0
SHEET 2 AA 8 ILE A 58 MET A 59 -1 O ILE A 58 N LEU A 65
SHEET 3 AA 8 MET A -50 ALA A -44 1 O MET A -50 N MET A 59
SHEET 4 AA 8 GLY A 21 ARG A 28 -1 O VAL A 22 N ALA A -45
SHEET 5 AA 8 ARG A 33 HIS A 42 -1 O TYR A 34 N ALA A 27
SHEET 6 AA 8 VAL A 45 THR A 48 -1 O VAL A 45 N HIS A 42
SHEET 7 AA 8 ARG A 76 TYR A 79 -1 O VAL A 77 N THR A 48
SHEET 8 AA 8 PRO A 67 ASN A 71 -1 N TYR A 68 O THR A 78
SHEET 1 AB 8 ALA A -35 ILE A -34 0
SHEET 2 AB 8 ILE A 107 THR A 111 -1 O ASN A 108 N ILE A -34
SHEET 3 AB 8 VAL A 95 VAL A 99 -1 O VAL A 95 N THR A 111
SHEET 4 AB 8 PRO A 138 VAL A 140 -1 O PRO A 138 N ILE A 98
SHEET 5 AB 8 ILE A 146 ILE A 155 -1 N ILE A 147 O ILE A 139
SHEET 6 AB 8 TYR A 161 VAL A 166 -1 O VAL A 162 N VAL A 154
SHEET 7 AB 8 ILE A 123 VAL A 126 -1 O GLY A 124 N ILE A 165
SHEET 8 AB 8 GLY A 114 PHE A 116 -1 O GLY A 114 N ALA A 125
SHEET 1 AC 6 LEU A 189 LEU A 192 0
SHEET 2 AC 6 ALA A 311 MET A 315 1 O ALA A 312 N THR A 190
SHEET 3 AC 6 LEU A 281 ASP A 285 1 O PHE A 282 N ILE A 313
SHEET 4 AC 6 THR A 219 ALA A 223 1 O ALA A 220 N VAL A 283
SHEET 5 AC 6 VAL A 258 CYS A 262 1 O ASP A 259 N VAL A 221
SHEET 6 AC 6 ARG A 242 TYR A 243 1 O ARG A 242 N VAL A 260
SHEET 1 AD 6 VAL A 333 SER A 337 0
SHEET 2 AD 6 ASP A 471 TYR A 475 1 O ASP A 471 N HIS A 334
SHEET 3 AD 6 ARG A 422 ASP A 425 1 O VAL A 423 N HIS A 474
SHEET 4 AD 6 THR A 359 PHE A 362 1 O VAL A 360 N ILE A 424
SHEET 5 AD 6 PHE A 405 THR A 408 1 O VAL A 406 N TRP A 361
SHEET 6 AD 6 VAL A 383 LEU A 386 1 O ILE A 384 N ILE A 407
SHEET 1 AE 2 LYS A 428 SER A 429 0
SHEET 2 AE 2 SER A 448 ALA A 449 -1 O SER A 448 N SER A 429
SHEET 1 AF 3 PRO A 432 LEU A 435 0
SHEET 2 AF 3 ARG A 441 LEU A 444 -1 O ARG A 441 N LEU A 435
SHEET 3 AF 3 LEU A 597 ASP A 598 1 O LEU A 597 N VAL A 442
CRYST1 41.910 105.460 80.068 90.00 97.42 90.00 P 1 21 1 2
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 0.023861 0.000000 0.003107 0.00000
SCALE2 0.000000 0.009482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
