HEADER TRANSFERASE 11-DEC-13 4NYZ
TITLE THE EMCV 3DPOL STRUCTURE WITH ALTERED MOTIF A CONFORMATION AT 2.15A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1834-2293;
COMPND 5 SYNONYM: LEADER PROTEIN, PROTEIN VP0, VP4-VP2, PROTEIN VP4, P1A, RHO,
COMPND 6 VIRION PROTEIN 4, PROTEIN VP2, BETA, P1B, VIRION PROTEIN 2, PROTEIN
COMPND 7 VP3, GAMMA, P1C, VIRION PROTEIN 3, PROTEIN VP1, ALPHA, P1D, VIRION
COMPND 8 PROTEIN 1, PROTEIN 2A, P2A, G, PROTEIN 2B, I, P2B, PROTEIN 2C, C,
COMPND 9 P2C, PROTEIN 3A, P3A, PROTEIN 3B, P3B, H, VPG, PROTEASE 3C, P3C,
COMPND 10 PICORNAIN 3C, P22, RNA-DIRECTED RNA POLYMERASE 3D-POL, E, P3D-POL;
COMPND 11 EC: 3.6.1.15, 3.4.22.28, 2.7.7.48;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MENGO VIRUS;
SOURCE 3 ORGANISM_TAXID: 12107;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETG20A
KEYWDS ENCEPHALOMYOCARDITIS VIRUS, CLOSE RIGHT HAND, RNA DEPENDENT RNA
KEYWDS 2 POLYMERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.VIVES-ADRIAN,C.LUJAN,C.FERRER-ORTA,N.VERDAGUER
REVDAT 3 08-NOV-23 4NYZ 1 REMARK LINK
REVDAT 2 10-DEC-14 4NYZ 1 JRNL
REVDAT 1 19-MAR-14 4NYZ 0
JRNL AUTH L.VIVES-ADRIAN,C.LUJAN,B.OLIVA,L.VAN DER LINDEN,B.SELISKO,
JRNL AUTH 2 B.COUTARD,B.CANARD,F.J.VAN KUPPEVELD,C.FERRER-ORTA,
JRNL AUTH 3 N.VERDAGUER
JRNL TITL THE CRYSTAL STRUCTURE OF A CARDIOVIRUS RNA-DEPENDENT RNA
JRNL TITL 2 POLYMERASE REVEALS AN UNUSUAL CONFORMATION OF THE POLYMERASE
JRNL TITL 3 ACTIVE SITE
JRNL REF J.VIROL. V. 88 5595 2014
JRNL REFN ISSN 0022-538X
JRNL PMID 24600002
JRNL DOI 10.1128/JVI.03502-13
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 104.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 38457
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2036
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2816
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3680
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : 0.96000
REMARK 3 B33 (A**2) : -1.93000
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): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.575
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3806 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3623 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5158 ; 0.877 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8337 ; 0.700 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 463 ; 4.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;30.172 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 646 ;14.240 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;14.787 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 567 ; 0.052 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4286 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 891 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1852 ; 0.528 ; 2.478
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1851 ; 0.528 ; 2.477
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2315 ; 0.976 ; 3.713
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2316 ; 0.976 ; 3.714
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1953 ; 0.413 ; 2.494
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1953 ; 0.414 ; 2.494
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2844 ; 0.750 ; 3.721
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4274 ; 2.871 ;19.515
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4275 ; 2.871 ;19.519
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 : 1
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 1 A 460
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6644 -29.2899 -23.9081
REMARK 3 T TENSOR
REMARK 3 T11: 0.0629 T22: 0.0695
REMARK 3 T33: 0.0350 T12: -0.0018
REMARK 3 T13: 0.0182 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.6692 L22: 1.3987
REMARK 3 L33: 2.0261 L12: -0.2524
REMARK 3 L13: 0.3984 L23: -0.0213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: 0.0185 S13: 0.1301
REMARK 3 S21: -0.1688 S22: -0.0111 S23: -0.0899
REMARK 3 S31: -0.0865 S32: 0.3273 S33: 0.0330
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 4NYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083832.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-13
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 : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : CHANNEL-CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40499
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 104.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
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 (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : 0.77000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 18.70
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: 1U09(THE HOMOLOGY MODEL HAS BEEN USED.)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%PEG6000 AND 2.0M NACL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 61.27650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 61.27650
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.39850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.69925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.27650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 149.09775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 149.09775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.27650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.69925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 61.27650
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 99.39850
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 61.27650
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 99.39850
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 61.27650
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 149.09775
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 49.69925
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 61.27650
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 49.69925
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 149.09775
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 61.27650
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 61.27650
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 99.39850
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 612 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 658 LIES ON A SPECIAL POSITION.
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 ALA A 32 45.52 -82.85
REMARK 500 LEU A 99 -149.30 -134.77
REMARK 500 MET A 102 132.71 67.17
REMARK 500 THR A 130 -9.68 66.51
REMARK 500 ASN A 146 33.48 -93.47
REMARK 500 PHE A 255 -68.47 -108.58
REMARK 500 GLU A 281 -124.07 56.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 159 O
REMARK 620 2 GLU A 161 OE2 104.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U09 RELATED DB: PDB
REMARK 900 FOOT AND MOUTH DISEASE VIRUS RNA-DEPENDENT RNA POLYMERASE
REMARK 900 RELATED ID: 4NZ0 RELATED DB: PDB
DBREF 4NYZ A 1 460 UNP P12296 POLG_ENMGO 1834 2293
SEQRES 1 A 460 GLY ALA LEU GLU ARG LEU PRO ASP GLY PRO ARG ILE HIS
SEQRES 2 A 460 VAL PRO ARG LYS THR ALA LEU ARG PRO THR VAL ALA ARG
SEQRES 3 A 460 GLN VAL PHE GLN PRO ALA PHE ALA PRO ALA VAL LEU SER
SEQRES 4 A 460 LYS PHE ASP PRO ARG THR ASP ALA ASP VAL ASP GLU VAL
SEQRES 5 A 460 ALA PHE SER LYS HIS THR SER ASN GLN GLU THR LEU PRO
SEQRES 6 A 460 PRO VAL PHE ARG MET VAL ALA ARG GLU TYR ALA ASN ARG
SEQRES 7 A 460 VAL PHE ALA LEU LEU GLY ARG ASP ASN GLY ARG LEU SER
SEQRES 8 A 460 VAL LYS GLN ALA LEU ASP GLY LEU GLU GLY MET ASP PRO
SEQRES 9 A 460 MET ASP LYS ASN THR SER PRO GLY LEU PRO TYR THR THR
SEQRES 10 A 460 LEU GLY MET ARG ARG THR ASP VAL VAL ASP TRP GLU THR
SEQRES 11 A 460 ALA THR LEU ILE PRO PHE ALA ALA GLU ARG LEU GLU LYS
SEQRES 12 A 460 MET ASN ASN LYS ASP PHE SER ASP ILE VAL TYR GLN THR
SEQRES 13 A 460 PHE LEU LYS ASP GLU LEU ARG PRO ILE GLU LYS VAL GLN
SEQRES 14 A 460 ALA ALA LYS THR ARG ILE VAL ASP VAL PRO PRO PHE GLU
SEQRES 15 A 460 HIS CYS ILE LEU GLY ARG GLN LEU LEU GLY LYS PHE ALA
SEQRES 16 A 460 SER LYS PHE GLN THR GLN PRO GLY LEU GLU LEU GLY SER
SEQRES 17 A 460 ALA ILE GLY CYS ASP PRO ASP VAL HIS TRP THR ALA PHE
SEQRES 18 A 460 GLY VAL ALA MET GLN GLY PHE GLU ARG VAL TYR ASP VAL
SEQRES 19 A 460 ASP TYR SER ASN PHE ASP SER THR HIS SER VAL ALA VAL
SEQRES 20 A 460 PHE ARG LEU LEU ALA GLU GLU PHE PHE SER GLU GLU ASN
SEQRES 21 A 460 GLY PHE ASP PRO LEU VAL LYS ASP TYR LEU GLU SER LEU
SEQRES 22 A 460 ALA ILE SER LYS HIS ALA TYR GLU GLU LYS ARG TYR LEU
SEQRES 23 A 460 ILE THR GLY GLY LEU PRO SER GLY CYS ALA ALA THR SER
SEQRES 24 A 460 MET LEU ASN THR ILE MET ASN ASN ILE ILE ILE ARG ALA
SEQRES 25 A 460 GLY LEU TYR LEU THR TYR LYS ASN PHE GLU PHE ASP ASP
SEQRES 26 A 460 VAL LYS VAL LEU SER TYR GLY ASP ASP LEU LEU VAL ALA
SEQRES 27 A 460 THR ASN TYR GLN LEU ASN PHE ASP ARG VAL ARG THR SER
SEQRES 28 A 460 LEU ALA LYS THR GLY TYR LYS ILE THR PRO ALA ASN LYS
SEQRES 29 A 460 THR SER THR PHE PRO LEU GLU SER THR LEU GLU ASP VAL
SEQRES 30 A 460 VAL PHE LEU LYS ARG LYS PHE LYS LYS GLU GLY PRO LEU
SEQRES 31 A 460 TYR ARG PRO VAL MET ASN ARG GLU ALA LEU GLU ALA MET
SEQRES 32 A 460 LEU SER TYR TYR ARG PRO GLY THR LEU SER GLU LYS LEU
SEQRES 33 A 460 THR SER ILE THR MET LEU ALA VAL HIS SER GLY LYS GLN
SEQRES 34 A 460 GLU TYR ASP ARG LEU PHE ALA PRO PHE ARG GLU VAL GLY
SEQRES 35 A 460 VAL ILE VAL PRO THR PHE GLU SER VAL GLU TYR ARG TRP
SEQRES 36 A 460 ARG SER LEU PHE TRP
HET GLN A 501 10
HET MG A 502 1
HET GOL A 503 6
HETNAM GLN GLUTAMINE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GLN C5 H10 N2 O3
FORMUL 3 MG MG 2+
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *110(H2 O)
HELIX 1 1 ALA A 25 GLN A 30 1 6
HELIX 2 2 ASP A 48 ALA A 53 1 6
HELIX 3 3 PHE A 54 THR A 58 5 5
HELIX 4 4 PRO A 65 GLY A 84 1 20
HELIX 5 5 SER A 91 GLY A 98 1 8
HELIX 6 6 ARG A 121 VAL A 125 1 5
HELIX 7 7 ILE A 134 ASN A 146 1 13
HELIX 8 8 ILE A 165 ALA A 170 1 6
HELIX 9 9 PRO A 180 GLN A 199 1 20
HELIX 10 10 ASP A 213 GLN A 226 1 14
HELIX 11 11 SER A 244 PHE A 255 1 12
HELIX 12 12 SER A 257 GLY A 261 5 5
HELIX 13 13 LEU A 265 ALA A 274 1 10
HELIX 14 14 ALA A 297 TYR A 318 1 22
HELIX 15 15 GLU A 322 VAL A 326 5 5
HELIX 16 16 ASN A 344 LYS A 354 1 11
HELIX 17 17 ASN A 396 SER A 405 1 10
HELIX 18 18 THR A 411 VAL A 424 1 14
HELIX 19 19 GLY A 427 VAL A 441 1 15
HELIX 20 20 THR A 447 LEU A 458 1 12
SHEET 1 A 5 LEU A 3 ARG A 5 0
SHEET 2 A 5 LYS A 283 THR A 288 -1 O LEU A 286 N GLU A 4
SHEET 3 A 5 ILE A 275 TYR A 280 -1 N HIS A 278 O TYR A 285
SHEET 4 A 5 TYR A 154 LEU A 158 1 N TYR A 154 O ALA A 279
SHEET 5 A 5 ILE A 175 VAL A 178 -1 O VAL A 176 N PHE A 157
SHEET 1 B 2 ARG A 21 PRO A 22 0
SHEET 2 B 2 TYR A 406 TYR A 407 -1 O TYR A 407 N ARG A 21
SHEET 1 C 2 PHE A 33 PRO A 35 0
SHEET 2 C 2 LEU A 162 PRO A 164 -1 O ARG A 163 N ALA A 34
SHEET 1 D 2 VAL A 126 ASP A 127 0
SHEET 2 D 2 THR A 132 LEU A 133 -1 O THR A 132 N ASP A 127
SHEET 1 E 3 ARG A 230 ASP A 235 0
SHEET 2 E 3 ASP A 334 THR A 339 -1 O LEU A 335 N VAL A 234
SHEET 3 E 3 LYS A 327 TYR A 331 -1 N LYS A 327 O ALA A 338
SHEET 1 F 2 ARG A 382 GLU A 387 0
SHEET 2 F 2 LEU A 390 MET A 395 -1 O LEU A 390 N GLU A 387
LINK O LYS A 159 MG MG A 502 1555 1555 2.82
LINK OE2 GLU A 161 MG MG A 502 1555 1555 2.72
CISPEP 1 LEU A 113 PRO A 114 0 0.28
SITE 1 AC1 14 TYR A 236 ASN A 238 SER A 241 THR A 242
SITE 2 AC1 14 HIS A 243 GLY A 290 LEU A 291 ASP A 333
SITE 3 AC1 14 HOH A 625 HOH A 642 HOH A 692 HOH A 695
SITE 4 AC1 14 HOH A 698 HOH A 707
SITE 1 AC2 6 ALA A 36 LYS A 159 GLU A 161 ARG A 163
SITE 2 AC2 6 THR A 173 ARG A 174
SITE 1 AC3 4 PHE A 33 LYS A 381 ALA A 399 HOH A 677
CRYST1 122.553 122.553 198.797 90.00 90.00 90.00 I 41 2 2 16
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 0.008160 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005030 0.00000
(ATOM LINES ARE NOT SHOWN.)
END