HEADER VIRAL PROTEIN 05-MAY-96 1KXF
TITLE SINDBIS VIRUS CAPSID, (WILD-TYPE) RESIDUES 1-264, TETRAGONAL CRYSTAL
TITLE 2 FORM (FORM II)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SINDBIS VIRUS CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MET 1 - ALA 264 OF THE NATIVE SINDBIS CAPSID;
COMPND 5 SYNONYM: SINDBIS VIRUS CORE PROTEIN;
COMPND 6 EC: 3.4.21.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINDBIS VIRUS;
SOURCE 3 ORGANISM_TAXID: 11034;
SOURCE 4 ORGAN: KIDNEY;
SOURCE 5 EXPRESSION_SYSTEM: CRICETINAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HAMSTERS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10026
KEYWDS SINDBIS VIRUS CAPSID PROTEIN, CHYMOTRYPSIN-LIKE SERINE PROTEINASE,
KEYWDS 2 WILD TYPE, VIRUS CAPSID PROTEIN, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-K.CHOI,M.G.ROSSMANN
REVDAT 5 14-FEB-24 1KXF 1 REMARK
REVDAT 4 12-OCT-16 1KXF 1 REMARK SEQRES VERSN
REVDAT 3 24-FEB-09 1KXF 1 VERSN
REVDAT 2 01-APR-03 1KXF 1 JRNL
REVDAT 1 07-DEC-96 1KXF 0
JRNL AUTH H.K.CHOI,S.LEE,Y.P.ZHANG,B.R.MCKINNEY,G.WENGLER,
JRNL AUTH 2 M.G.ROSSMANN,R.J.KUHN
JRNL TITL STRUCTURAL ANALYSIS OF SINDBIS VIRUS CAPSID MUTANTS
JRNL TITL 2 INVOLVING ASSEMBLY AND CATALYSIS.
JRNL REF J.MOL.BIOL. V. 262 151 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8831786
JRNL DOI 10.1006/JMBI.1996.0505
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.TONG,G.WENGLER,M.G.ROSSMANN
REMARK 1 TITL REFINED STRUCTURE OF SINDBIS VIRUS CORE PROTEIN AND
REMARK 1 TITL 2 COMPARISON WITH OTHER CHYMOTRYPSIN-LIKE SERINE PROTEINASE
REMARK 1 TITL 3 STRUCTURES
REMARK 1 REF J.MOL.BIOL. V. 230 228 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.TONG,H.-K.CHOI,W.MINOR,M.G.ROSSMANN
REMARK 1 TITL THE STRUCTURE DETERMINATION OF SINDBIS VIRUS CORE PROTEIN
REMARK 1 TITL 2 USING ISOMORPHOUS REPLACEMENT AND MOLECULAR REPLACEMENT
REMARK 1 TITL 3 AVERAGING BETWEEN TWO CRYSTAL FORMS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 48 430 1992
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.K.CHOI,L.TONG,W.MINOR,P.DUMAS,U.BOEGE,M.G.ROSSMANN,
REMARK 1 AUTH 2 G.WENGLER
REMARK 1 TITL STRUCTURE OF SINDBIS VIRUS CORE PROTEIN REVEALS A
REMARK 1 TITL 2 CHYMOTRYPSIN-LIKE SERINE PROTEINASE AND THE ORGANIZATION OF
REMARK 1 TITL 3 THE VIRION
REMARK 1 REF NATURE V. 354 37 1991
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 6383
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1224
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-92
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7908
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 2.420
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.90000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.50000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.35000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.50000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.45000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 82.35000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.45000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 54.90000
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 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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: TRI
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SINDBIS CAPSID PROTEIN HAS THE CATALYTIC TRIAD
REMARK 800 OF THE SERINE PROTEINASE. THE RESIDUES ARE SER 215, HIS 141, AND
REMARK 800 ASP 163.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CRYSTALLIZED CONSTRUCT 1-264 WAS POSSIBLY CLEAVED DURING
REMARK 999 CRYSTALLIZATION SOMEWHERE BEFORE RESIDUE 106. THE ENTRY WAS
REMARK 999 ANNOTATED AS 106-264 FRAGMENT
DBREF 1KXF A 106 264 UNP P03316 POLS_SINDV 106 264
SEQRES 1 A 159 MET ALA LEU LYS LEU GLU ALA ASP ARG LEU PHE ASP VAL
SEQRES 2 A 159 LYS ASN GLU ASP GLY ASP VAL ILE GLY HIS ALA LEU ALA
SEQRES 3 A 159 MET GLU GLY LYS VAL MET LYS PRO LEU HIS VAL LYS GLY
SEQRES 4 A 159 THR ILE ASP HIS PRO VAL LEU SER LYS LEU LYS PHE THR
SEQRES 5 A 159 LYS SER SER ALA TYR ASP MET GLU PHE ALA GLN LEU PRO
SEQRES 6 A 159 VAL ASN MET ARG SER GLU ALA PHE THR TYR THR SER GLU
SEQRES 7 A 159 HIS PRO GLU GLY PHE TYR ASN TRP HIS HIS GLY ALA VAL
SEQRES 8 A 159 GLN TYR SER GLY GLY ARG PHE THR ILE PRO ARG GLY VAL
SEQRES 9 A 159 GLY GLY ARG GLY ASP SER GLY ARG PRO ILE MET ASP ASN
SEQRES 10 A 159 SER GLY ARG VAL VAL ALA ILE VAL LEU GLY GLY ALA ASP
SEQRES 11 A 159 GLU GLY THR ARG THR ALA LEU SER VAL VAL THR TRP ASN
SEQRES 12 A 159 SER LYS GLY LYS THR ILE LYS THR THR PRO GLU GLY THR
SEQRES 13 A 159 GLU GLU TRP
FORMUL 2 HOH *16(H2 O)
HELIX 1 1 LEU A 151 LYS A 153 5 3
SHEET 1 A1 6 LEU A 115 LYS A 119 0
SHEET 2 A1 6 VAL A 125 MET A 132 -1
SHEET 3 A1 6 LYS A 135 PRO A 139 -1
SHEET 4 A1 6 THR A 145 ILE A 146 -1
SHEET 5 A1 6 THR A 157 SER A 159 -1
SHEET 6 A1 6 MET A 164 GLN A 168 -1
SHEET 1 A2 8 GLY A 187 TRP A 191 0
SHEET 2 A2 8 GLY A 194 SER A 199 -1
SHEET 3 A2 8 ARG A 202 PRO A 206 -1
SHEET 4 A2 8 PRO A 218 MET A 220 -1
SHEET 5 A2 8 VAL A 226 GLU A 236 -1
SHEET 6 A2 8 ARG A 239 TRP A 247 -1
SHEET 7 A2 8 THR A 253 THR A 256 -1
SHEET 8 A2 8 GLU A 262 GLU A 263 -1
SITE 1 TRI 3 SER A 215 HIS A 141 ASP A 163
CRYST1 57.000 57.000 109.800 90.00 90.00 90.00 P 43 21 2 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 0.017544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
