HEADER TRANSFERASE 02-APR-09 3A1G
TITLE HIGH-RESOLUTION CRYSTAL STRUCTURE OF RNA POLYMERASE PB1-PB2 SUBUNITS
TITLE 2 FROM INFLUENZA A VIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: PB1 C-TERMINAL FRAGMENT, UNP RESIDUES 678-757;
COMPND 5 SYNONYM: POLYMERASE BASIC PROTEIN 1, PB1, RNA-DIRECTED RNA POLYMERASE
COMPND 6 SUBUNIT P1;
COMPND 7 EC: 2.7.7.48;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: POLYMERASE BASIC PROTEIN 2;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: PB2 N-TERMINAL RAGMENT, UNP RESIDUES 1-37;
COMPND 13 SYNONYM: RNA POLYMERASE PB2 SUBUNIT, RNA-DIRECTED RNA POLYMERASE
COMPND 14 SUBUNIT P3;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/PUERTO RICO/8/34(H1N1));
SOURCE 3 ORGANISM_TAXID: 211044;
SOURCE 4 STRAIN: STRAIN A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: PB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RILCODONPLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/PUERTO RICO/8/34(H1N1));
SOURCE 13 ORGANISM_TAXID: 211044;
SOURCE 14 STRAIN: STRAIN A/PUERTO RICO/8/1934 H1N1;
SOURCE 15 GENE: PB2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RILCODONPLUS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: MIDIFIED PET28
KEYWDS INFLUENZA VIRUS, RNA POLYMERASE, NUCLEOTIDE-BINDING,
KEYWDS 2 NUCLEOTIDYLTRANSFERASE, NUCLEUS, RNA REPLICATION, RNA-DIRECTED RNA
KEYWDS 3 POLYMERASE, TRANSFERASE, MITOCHONDRION, MRNA CAPPING, MRNA
KEYWDS 4 PROCESSING, VIRION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SUGIYAMA,S.-Y.PARK,E.OBAYASHI
REVDAT 4 15-NOV-23 3A1G 1 REMARK
REVDAT 3 01-NOV-23 3A1G 1 SEQADV LINK
REVDAT 2 07-JUL-09 3A1G 1 JRNL
REVDAT 1 09-JUN-09 3A1G 0
JRNL AUTH K.SUGIYAMA,E.OBAYASHI,A.KAWAGUCHI,Y.SUZUKI,J.R.H.TAME,
JRNL AUTH 2 K.NAGATA,S.-Y.PARK
JRNL TITL STRUCTURAL INSIGHT INTO THE ESSENTIAL PB1-PB2 SUBUNIT
JRNL TITL 2 CONTACT OF THE INFLUENZA VIRUS RNA POLYMERASE
JRNL REF EMBO J. V. 28 1803 2009
JRNL REFN ISSN 0261-4189
JRNL PMID 19461581
JRNL DOI 10.1038/EMBOJ.2009.138
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24512
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1315
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1399
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1826
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.34000
REMARK 3 B22 (A**2) : -2.46000
REMARK 3 B33 (A**2) : -1.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.70000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.709
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1844 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2448 ; 1.845 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 218 ; 6.734 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;37.835 ;22.045
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 400 ;18.170 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.653 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 268 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1332 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 948 ; 0.247 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1291 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 85 ; 0.158 ; 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): 50 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.264 ; 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): 1152 ; 1.503 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1792 ; 2.164 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 777 ; 3.729 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 656 ; 4.906 ; 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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3A1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000028691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25865
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 0.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.12400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 25.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZTT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 80MM SODIUM CITRATE, 20% PEG 4000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 30.35050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.99350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 30.35050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.99350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 SER A 678
REMARK 465 GLN A 679
REMARK 465 ARG A 680
REMARK 465 GLY A 681
REMARK 465 VAL A 682
REMARK 465 LEU A 683
REMARK 465 GLU A 684
REMARK 465 SER B 36
REMARK 465 GLY B 37
REMARK 465 SER C 678
REMARK 465 GLN C 679
REMARK 465 ARG C 680
REMARK 465 GLY C 681
REMARK 465 VAL C 682
REMARK 465 LEU C 683
REMARK 465 GLU C 684
REMARK 465 SER D 36
REMARK 465 GLY D 37
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 CYS A 693 CB CYS A 693 SG -0.096
REMARK 500 MSE B 1 SE MSE B 1 CE -0.427
REMARK 500 GLU B 2 CB GLU B 2 CG 0.122
REMARK 500 GLU B 2 CG GLU B 2 CD 0.107
REMARK 500 CYS C 693 CB CYS C 693 SG -0.107
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 MSE A 718 CG - SE - CE ANGL. DEV. = -19.9 DEGREES
REMARK 500 LEU B 10 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG C 723 NE - CZ - NH2 ANGL. DEV. = -3.3 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 SER A 703 57.07 -60.77
REMARK 500 TYR A 705 57.49 -92.60
REMARK 500 ARG C 706 98.07 -68.30
REMARK 500 ILE D 30 -70.06 -51.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 703 SER A 704 -147.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZTT RELATED DB: PDB
DBREF 3A1G A 678 757 UNP P03431 RDRP_I34A1 678 757
DBREF 3A1G B 1 37 UNP P03428 PB2_I34A1 1 37
DBREF 3A1G C 678 757 UNP P03431 RDRP_I34A1 678 757
DBREF 3A1G D 1 37 UNP P03428 PB2_I34A1 1 37
SEQADV 3A1G GLY B -2 UNP P03428 EXPRESSION TAG
SEQADV 3A1G GLY B -1 UNP P03428 EXPRESSION TAG
SEQADV 3A1G SER B 0 UNP P03428 EXPRESSION TAG
SEQADV 3A1G GLY D -2 UNP P03428 EXPRESSION TAG
SEQADV 3A1G GLY D -1 UNP P03428 EXPRESSION TAG
SEQADV 3A1G SER D 0 UNP P03428 EXPRESSION TAG
SEQRES 1 A 80 SER GLN ARG GLY VAL LEU GLU ASP GLU GLN MSE TYR GLN
SEQRES 2 A 80 ARG CYS CYS ASN LEU PHE GLU LYS PHE PHE PRO SER SER
SEQRES 3 A 80 SER TYR ARG ARG PRO VAL GLY ILE SER SER MSE VAL GLU
SEQRES 4 A 80 ALA MSE VAL SER ARG ALA ARG ILE ASP ALA ARG ILE ASP
SEQRES 5 A 80 PHE GLU SER GLY ARG ILE LYS LYS GLU GLU PHE THR GLU
SEQRES 6 A 80 ILE MSE LYS ILE CYS SER THR ILE GLU GLU LEU ARG ARG
SEQRES 7 A 80 GLN LYS
SEQRES 1 B 40 GLY GLY SER MSE GLU ARG ILE LYS GLU LEU ARG ASN LEU
SEQRES 2 B 40 MSE SER GLN SER ARG THR ARG GLU ILE LEU THR LYS THR
SEQRES 3 B 40 THR VAL ASP HIS MSE ALA ILE ILE LYS LYS TYR THR SER
SEQRES 4 B 40 GLY
SEQRES 1 C 80 SER GLN ARG GLY VAL LEU GLU ASP GLU GLN MSE TYR GLN
SEQRES 2 C 80 ARG CYS CYS ASN LEU PHE GLU LYS PHE PHE PRO SER SER
SEQRES 3 C 80 SER TYR ARG ARG PRO VAL GLY ILE SER SER MSE VAL GLU
SEQRES 4 C 80 ALA MSE VAL SER ARG ALA ARG ILE ASP ALA ARG ILE ASP
SEQRES 5 C 80 PHE GLU SER GLY ARG ILE LYS LYS GLU GLU PHE THR GLU
SEQRES 6 C 80 ILE MSE LYS ILE CYS SER THR ILE GLU GLU LEU ARG ARG
SEQRES 7 C 80 GLN LYS
SEQRES 1 D 40 GLY GLY SER MSE GLU ARG ILE LYS GLU LEU ARG ASN LEU
SEQRES 2 D 40 MSE SER GLN SER ARG THR ARG GLU ILE LEU THR LYS THR
SEQRES 3 D 40 THR VAL ASP HIS MSE ALA ILE ILE LYS LYS TYR THR SER
SEQRES 4 D 40 GLY
MODRES 3A1G MSE A 688 MET SELENOMETHIONINE
MODRES 3A1G MSE A 714 MET SELENOMETHIONINE
MODRES 3A1G MSE A 718 MET SELENOMETHIONINE
MODRES 3A1G MSE A 744 MET SELENOMETHIONINE
MODRES 3A1G MSE B 1 MET SELENOMETHIONINE
MODRES 3A1G MSE B 11 MET SELENOMETHIONINE
MODRES 3A1G MSE B 28 MET SELENOMETHIONINE
MODRES 3A1G MSE C 688 MET SELENOMETHIONINE
MODRES 3A1G MSE C 714 MET SELENOMETHIONINE
MODRES 3A1G MSE C 718 MET SELENOMETHIONINE
MODRES 3A1G MSE C 744 MET SELENOMETHIONINE
MODRES 3A1G MSE D 1 MET SELENOMETHIONINE
MODRES 3A1G MSE D 11 MET SELENOMETHIONINE
MODRES 3A1G MSE D 28 MET SELENOMETHIONINE
HET MSE A 688 8
HET MSE A 714 8
HET MSE A 718 8
HET MSE A 744 8
HET MSE B 1 8
HET MSE B 11 8
HET MSE B 28 8
HET MSE C 688 8
HET MSE C 714 8
HET MSE C 718 8
HET MSE C 744 8
HET MSE D 1 8
HET MSE D 11 8
HET MSE D 28 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 5 HOH *63(H2 O)
HELIX 1 1 GLU A 686 PHE A 700 1 15
HELIX 2 2 SER A 713 SER A 732 1 20
HELIX 3 3 LYS A 736 GLN A 756 1 21
HELIX 4 4 GLY B -2 MSE B 11 1 14
HELIX 5 5 GLN B 13 THR B 23 1 11
HELIX 6 6 ASP B 26 TYR B 34 1 9
HELIX 7 7 ASP C 685 PHE C 700 1 16
HELIX 8 8 SER C 713 SER C 732 1 20
HELIX 9 9 LYS C 736 GLN C 756 1 21
HELIX 10 10 GLY D -2 MSE D 11 1 14
HELIX 11 11 GLN D 13 THR D 23 1 11
HELIX 12 12 ASP D 26 TYR D 34 1 9
LINK C GLN A 687 N MSE A 688 1555 1555 1.34
LINK C MSE A 688 N TYR A 689 1555 1555 1.34
LINK C SER A 713 N MSE A 714 1555 1555 1.33
LINK C MSE A 714 N VAL A 715 1555 1555 1.33
LINK C ALA A 717 N MSE A 718 1555 1555 1.34
LINK C MSE A 718 N VAL A 719 1555 1555 1.33
LINK C ILE A 743 N MSE A 744 1555 1555 1.34
LINK C MSE A 744 N LYS A 745 1555 1555 1.33
LINK C SER B 0 N MSE B 1 1555 1555 1.34
LINK C MSE B 1 N GLU B 2 1555 1555 1.35
LINK C LEU B 10 N MSE B 11 1555 1555 1.31
LINK C MSE B 11 N SER B 12 1555 1555 1.33
LINK C HIS B 27 N MSE B 28 1555 1555 1.35
LINK C MSE B 28 N ALA B 29 1555 1555 1.33
LINK C GLN C 687 N MSE C 688 1555 1555 1.34
LINK C MSE C 688 N TYR C 689 1555 1555 1.33
LINK C SER C 713 N MSE C 714 1555 1555 1.33
LINK C MSE C 714 N VAL C 715 1555 1555 1.33
LINK C ALA C 717 N MSE C 718 1555 1555 1.32
LINK C MSE C 718 N VAL C 719 1555 1555 1.33
LINK C ILE C 743 N MSE C 744 1555 1555 1.35
LINK C MSE C 744 N LYS C 745 1555 1555 1.34
LINK C SER D 0 N MSE D 1 1555 1555 1.34
LINK C MSE D 1 N GLU D 2 1555 1555 1.33
LINK C LEU D 10 N MSE D 11 1555 1555 1.33
LINK C MSE D 11 N SER D 12 1555 1555 1.34
LINK C HIS D 27 N MSE D 28 1555 1555 1.35
LINK C MSE D 28 N ALA D 29 1555 1555 1.33
CRYST1 60.701 69.987 61.348 90.00 97.94 90.00 C 1 2 1 8
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 0.016474 0.000000 0.002297 0.00000
SCALE2 0.000000 0.014288 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016458 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
