HEADER VIRAL PROTEIN 14-APR-08 2JJL
TITLE STRUCTURE OF AVIAN REOVIRUS SIGMAC117-326, P321 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIGMA-C CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 117-326;
COMPND 5 SYNONYM: SIGMA-3 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AVIAN REOVIRUS;
SOURCE 3 ORGANISM_TAXID: 38170;
SOURCE 4 STRAIN: S1133;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: DE3;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28C-PLUS;
SOURCE 10 OTHER_DETAILS: THE AVIAN REOVIRUS STRAIN S1133 WAS ORIGINALLY
SOURCE 11 PROVIDED BY DR. PHILIP I.MARCUS WHEN DR. J.BENAVENTE WAS A ROCHE
SOURCE 12 VISITING SCIENTIST IN THE LABORATORY OF DR. A.SHATKIN
KEYWDS ALPHA-HELICAL COILED COIL, RECEPTOR-BINDING, TRIPLE BETA-SPIRAL,
KEYWDS 2 VIRAL PROTEIN, VIRION, COILED COIL, BETA-BARREL
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GUARDADO-CALVO,G.C.FOX,A.L.LLAMAS-SAIZ,J.BENAVENTE,M.J.VAN RAAIJ
REVDAT 4 13-DEC-23 2JJL 1 REMARK LINK
REVDAT 3 07-FEB-18 2JJL 1 JRNL
REVDAT 2 15-SEP-09 2JJL 1 JRNL REMARK
REVDAT 1 13-JAN-09 2JJL 0
JRNL AUTH P.GUARDADO-CALVO,G.C.FOX,A.L.LLAMAS-SAIZ,M.J.VAN RAAIJ
JRNL TITL CRYSTALLOGRAPHIC STRUCTURE OF THE ALPHA-HELICAL TRIPLE
JRNL TITL 2 COILED-COIL DOMAIN OF AVIAN REOVIRUS S1133 FIBRE.
JRNL REF J. GEN. VIROL. V. 90 672 2009
JRNL REFN ISSN 0022-1317
JRNL PMID 19218213
JRNL DOI 10.1099/VIR.0.008276-0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.J.VAN RAAIJ,X.L.HERMO-PARRADO,P.GUARDADO-CALVO,G.C.FOX,
REMARK 1 AUTH 2 A.L.LLAMAS-SAIZ,C.COSTAS,J.MARTINEZ-COSTAS,J.BENAVENTE
REMARK 1 TITL CRYSTALLIZATION OF THE C-TERMINAL GLOBULAR DOMAIN OF AVIAN
REMARK 1 TITL 2 REOVIRUS FIBRE.
REMARK 1 REF ACTA CRYSTALLOGR., SECT.F V. 61 651 2005
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 16511119
REMARK 1 DOI 10.1107/S1744309105016933
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.GUARDADO-CALVO,G.C.FOX,X.L.HERMO-PARRADO,A.L.LLAMAS-SAIZ,
REMARK 1 AUTH 2 C.COSTAS,J.MARTINEZ-COSTAS,J.BENAVENTE,M.J.VAN RAAIJ
REMARK 1 TITL STRUCTURE OF THE CARBOXY-TERMINAL RECEPTOR-BINDING DOMAIN OF
REMARK 1 TITL 2 AVIAN REOVIRUS FIBRE SIGMAC.
REMARK 1 REF J.MOL.BIOL. V. 354 137 2005
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 16236316
REMARK 1 DOI 10.1016/J.JMB.2005.09.034
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 17714
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 268
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1550
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.19000
REMARK 3 B22 (A**2) : 2.19000
REMARK 3 B33 (A**2) : -3.29000
REMARK 3 B12 (A**2) : 1.10000
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): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.700
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1586 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2157 ; 1.509 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 206 ; 6.499 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;36.864 ;23.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 243 ;13.095 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.644 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 257 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1194 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 594 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1112 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 126 ; 0.163 ; 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): 80 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.214 ; 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): 1056 ; 3.225 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1666 ; 4.852 ; 7.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 594 ; 7.171 ;10.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 491 ; 8.862 ;15.000
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 : 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 : 1.40
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 2JJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1290035918.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9840
REMARK 200 MONOCHROMATOR : SI111 DOUBLE-CRYSTAL
REMARK 200 OPTICS : RD COATED FLAT AND TOROIDAL
REMARK 200 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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19318
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 52.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 20.30
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.40
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: CHAIN C OF PDB ENTRY 2VRS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6-0.75 M AMMONIUM SULPHATE, 0.1 M
REMARK 280 TRIS-HCL PH 8.4, 25% GLYCEROL, 50 MM ZINC SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 12620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.8 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 77.65700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 38.82850
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 67.25293
REMARK 350 BIOMT3 3 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 CL CL A1327 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL A1328 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN A1331 LIES ON A SPECIAL POSITION.
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 ILE A 116
REMARK 465 LEU A 117
REMARK 465 GLN A 118
REMARK 465 THR A 119
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 VAL A 186 -65.26 68.91
REMARK 500 ASN A 208 139.20 -170.39
REMARK 500 HIS A 255 75.77 58.00
REMARK 500 ALA A 291 -163.78 -122.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2073 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A2120 DISTANCE = 5.89 ANGSTROMS
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 ZN A1332 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 122 OD1
REMARK 620 2 HIS A 287 ND1 112.4
REMARK 620 3 TYR A 289 OH 114.6 101.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1330 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 158 NE2
REMARK 620 2 HIS A 158 NE2 116.6
REMARK 620 3 HIS A 158 NE2 108.5 127.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1331 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 212 OD1
REMARK 620 2 ASP A 212 OD1 102.3
REMARK 620 N 1
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1329
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1330
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1332
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BSF RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN
REMARK 900 REOVIRUS FIBRE SIGMAC, ZN CRYSTAL FORM.
REMARK 900 RELATED ID: 2VRS RELATED DB: PDB
REMARK 900 STRUCTURE OF AVIAN REOVIRUS SIGMAC117-326, C2 CRYSTAL FORM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST RESIDUE, ILE-116, IS A REMNANT OF THE EXPRESSION
REMARK 999 TAG.
DBREF 2JJL A 116 116 PDB 2JJL 2JJL 116 116
DBREF 2JJL A 117 326 UNP Q992I2 SIGC_ARVS1 117 326
SEQRES 1 A 211 ILE LEU GLN THR THR VAL ASP GLY ASN SER THR ALA ILE
SEQRES 2 A 211 SER ASN LEU LYS SER ASP ILE SER SER ASN GLY LEU ALA
SEQRES 3 A 211 ILE THR ASP LEU GLN ASP ARG VAL LYS SER LEU GLU SER
SEQRES 4 A 211 THR ALA SER HIS GLY LEU SER PHE SER PRO PRO LEU SER
SEQRES 5 A 211 VAL ALA ASP GLY VAL VAL SER LEU ASP MET ASP PRO TYR
SEQRES 6 A 211 PHE CYS SER GLN ARG VAL SER LEU THR SER TYR SER ALA
SEQRES 7 A 211 GLU ALA GLN LEU MET GLN PHE ARG TRP MET ALA ARG GLY
SEQRES 8 A 211 THR ASN GLY SER SER ASP THR ILE ASP MET THR VAL ASN
SEQRES 9 A 211 ALA HIS CYS HIS GLY ARG ARG THR ASP TYR MET MET SER
SEQRES 10 A 211 SER THR GLY ASN LEU THR VAL THR SER ASN VAL VAL LEU
SEQRES 11 A 211 LEU THR PHE ASP LEU SER ASP ILE THR HIS ILE PRO SER
SEQRES 12 A 211 ASP LEU ALA ARG LEU VAL PRO SER ALA GLY PHE GLN ALA
SEQRES 13 A 211 ALA SER PHE PRO VAL ASP VAL SER PHE THR ARG ASP SER
SEQRES 14 A 211 ALA THR HIS ALA TYR GLN ALA TYR GLY VAL TYR SER SER
SEQRES 15 A 211 SER ARG VAL PHE THR ILE THR PHE PRO THR GLY GLY ASP
SEQRES 16 A 211 GLY THR ALA ASN ILE ARG SER LEU THR VAL ARG THR GLY
SEQRES 17 A 211 ILE ASP THR
HET CL A1327 1
HET CL A1328 1
HET SO4 A1329 5
HET ZN A1330 1
HET ZN A1331 1
HET ZN A1332 1
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 ZN 3(ZN 2+)
FORMUL 8 HOH *202(H2 O)
HELIX 1 1 THR A 120 THR A 155 1 36
HELIX 2 2 ASP A 259 VAL A 264 5 6
HELIX 3 3 SER A 266 ALA A 271 1 6
SHEET 1 AA 2 LEU A 166 ALA A 169 0
SHEET 2 AA 2 VAL A 172 LEU A 175 -1 O VAL A 172 N ALA A 169
SHEET 1 AB 2 CYS A 182 GLN A 184 0
SHEET 2 AB 2 LEU A 188 SER A 190 -1 O THR A 189 N SER A 183
SHEET 1 AC 5 ASN A 236 VAL A 239 0
SHEET 2 AC 5 ALA A 313 ASP A 325 -1 O ALA A 313 N VAL A 239
SHEET 3 AC 5 ARG A 226 THR A 234 -1 O THR A 227 N ILE A 324
SHEET 4 AC 5 THR A 213 HIS A 223 -1 O ASP A 215 N THR A 234
SHEET 5 AC 5 GLN A 196 ASN A 208 -1 O GLN A 196 N CYS A 222
SHEET 1 AD 7 ASN A 236 VAL A 239 0
SHEET 2 AD 7 ALA A 313 ASP A 325 -1 O ALA A 313 N VAL A 239
SHEET 3 AD 7 PHE A 274 ARG A 282 -1 O ASP A 277 N ARG A 321
SHEET 4 AD 7 ALA A 285 SER A 297 -1 O ALA A 285 N ARG A 282
SHEET 5 AD 7 VAL A 300 PRO A 306 -1 O VAL A 300 N SER A 296
SHEET 6 AD 7 VAL A 243 ASP A 249 -1 O VAL A 244 N PHE A 305
SHEET 7 AD 7 GLN A 196 ASN A 208 -1 O ARG A 205 N THR A 247
LINK OD1 ASP A 122 ZN ZN A1332 1555 1555 1.98
LINK NE2 HIS A 158 ZN ZN A1330 1555 1555 2.12
LINK NE2 HIS A 158 ZN ZN A1330 2655 1555 1.74
LINK NE2 HIS A 158 ZN ZN A1330 3665 1555 1.93
LINK OD1 ASP A 212 ZN ZN A1331 5555 1555 2.11
LINK OD1 ASP A 212 ZN ZN A1331 1555 1555 2.01
LINK ND1 HIS A 287 ZN ZN A1332 3666 1555 2.21
LINK OH TYR A 289 ZN ZN A1332 3666 1555 2.29
CISPEP 1 PRO A 164 PRO A 165 0 6.96
SITE 1 AC1 1 ASN A 124
SITE 1 AC2 1 ASN A 138
SITE 1 AC3 3 ARG A 201 THR A 281 SER A 284
SITE 1 AC4 2 HIS A 158 HOH A2202
SITE 1 AC5 2 ASP A 212 THR A 213
SITE 1 AC6 3 ASP A 122 HIS A 287 TYR A 289
CRYST1 77.657 77.657 121.449 90.00 90.00 120.00 P 3 2 1 6
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 0.012877 0.007435 0.000000 0.00000
SCALE2 0.000000 0.014869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008234 0.00000
(ATOM LINES ARE NOT SHOWN.)
END