HEADER VIRAL PROTEIN 22-MAR-96 1SVP
TITLE SINDBIS VIRUS CAPSID PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SINDBIS VIRUS CAPSID PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MET 106 - ALA 264 OF THE NATIVE SINDBIS CAPSID PROTEIN;
COMPND 5 SYNONYM: SINDBIS VIRUS COAT PROTEIN;
COMPND 6 EC: 3.4.21.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINDBIS VIRUS;
SOURCE 3 ORGANISM_TAXID: 11034;
SOURCE 4 GENE: SINDBIS VIRUS CAPSID PROTEIN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 9 EXPRESSION_SYSTEM_GENE: SINDBIS VIRUS CAPSID PROTEIN;
SOURCE 10 OTHER_DETAILS: T7 RNA POLYMERASE
KEYWDS SINDBIS VIRUS CAPSID PROTEIN, CHYMOTRYPSIN-LIKE SERINE, MUTANT, COAT
KEYWDS 2 PROTEIN, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEE,M.G.ROSSMANN
REVDAT 4 14-FEB-24 1SVP 1 REMARK
REVDAT 3 03-NOV-21 1SVP 1 SEQADV
REVDAT 2 24-FEB-09 1SVP 1 VERSN
REVDAT 1 17-AUG-96 1SVP 0
JRNL AUTH S.LEE,K.E.OWEN,H.K.CHOI,H.LEE,G.LU,G.WENGLER,D.T.BROWN,
JRNL AUTH 2 M.G.ROSSMANN,R.J.KUHN
JRNL TITL IDENTIFICATION OF A PROTEIN BINDING SITE ON THE SURFACE OF
JRNL TITL 2 THE ALPHAVIRUS NUCLEOCAPSID AND ITS IMPLICATION IN VIRUS
JRNL TITL 3 ASSEMBLY.
JRNL REF STRUCTURE V. 4 531 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8736552
JRNL DOI 10.1016/S0969-2126(96)00059-7
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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 15488
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) : 0.184
REMARK 3 FREE R VALUE : 0.279
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 : 2452
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.50
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) : 0.25
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.700
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 1SVP 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_1000176533.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-94
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.630
REMARK 200 R MERGE (I) : 0.03600
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 (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
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: DIMERIC
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 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 MET A 106
REMARK 465 MET B 106
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 HH21 ARG A 174 H1 HOH A 283 1.23
REMARK 500 H LYS B 255 H2 HOH B 328 1.34
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 LEU A 110 100.08 -162.90
REMARK 500 ASP A 147 68.93 -69.01
REMARK 500 HIS A 184 80.58 -153.17
REMARK 500 GLU A 236 40.08 -107.24
REMARK 500 SER A 265 84.24 63.61
REMARK 500 GLU B 186 123.31 -36.32
REMARK 500 SER B 265 -93.03 -122.00
REMARK 500
REMARK 500 REMARK: NULL
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 IN THE WILD-TYPE. IN THIS MUTANT STRUCTURE, THE ACTIVE
REMARK 800 SITE SER 215 WAS MUTATED TO ALA TO PREVENT AUTO-CATALYTIC
REMARK 800 CLEAVAGE BETWEEN TRP 264 AND SER 265.
DBREF 1SVP A 106 266 UNP P03316 POLS_SINDV 106 266
DBREF 1SVP B 106 266 UNP P03316 POLS_SINDV 106 266
SEQADV 1SVP ALA A 215 UNP P03316 SER 215 ENGINEERED MUTATION
SEQADV 1SVP ALA B 215 UNP P03316 SER 215 ENGINEERED MUTATION
SEQRES 1 A 161 MET ALA LEU LYS LEU GLU ALA ASP ARG LEU PHE ASP VAL
SEQRES 2 A 161 LYS ASN GLU ASP GLY ASP VAL ILE GLY HIS ALA LEU ALA
SEQRES 3 A 161 MET GLU GLY LYS VAL MET LYS PRO LEU HIS VAL LYS GLY
SEQRES 4 A 161 THR ILE ASP HIS PRO VAL LEU SER LYS LEU LYS PHE THR
SEQRES 5 A 161 LYS SER SER ALA TYR ASP MET GLU PHE ALA GLN LEU PRO
SEQRES 6 A 161 VAL ASN MET ARG SER GLU ALA PHE THR TYR THR SER GLU
SEQRES 7 A 161 HIS PRO GLU GLY PHE TYR ASN TRP HIS HIS GLY ALA VAL
SEQRES 8 A 161 GLN TYR SER GLY GLY ARG PHE THR ILE PRO ARG GLY VAL
SEQRES 9 A 161 GLY GLY ARG GLY ASP ALA GLY ARG PRO ILE MET ASP ASN
SEQRES 10 A 161 SER GLY ARG VAL VAL ALA ILE VAL LEU GLY GLY ALA ASP
SEQRES 11 A 161 GLU GLY THR ARG THR ALA LEU SER VAL VAL THR TRP ASN
SEQRES 12 A 161 SER LYS GLY LYS THR ILE LYS THR THR PRO GLU GLY THR
SEQRES 13 A 161 GLU GLU TRP SER ALA
SEQRES 1 B 161 MET ALA LEU LYS LEU GLU ALA ASP ARG LEU PHE ASP VAL
SEQRES 2 B 161 LYS ASN GLU ASP GLY ASP VAL ILE GLY HIS ALA LEU ALA
SEQRES 3 B 161 MET GLU GLY LYS VAL MET LYS PRO LEU HIS VAL LYS GLY
SEQRES 4 B 161 THR ILE ASP HIS PRO VAL LEU SER LYS LEU LYS PHE THR
SEQRES 5 B 161 LYS SER SER ALA TYR ASP MET GLU PHE ALA GLN LEU PRO
SEQRES 6 B 161 VAL ASN MET ARG SER GLU ALA PHE THR TYR THR SER GLU
SEQRES 7 B 161 HIS PRO GLU GLY PHE TYR ASN TRP HIS HIS GLY ALA VAL
SEQRES 8 B 161 GLN TYR SER GLY GLY ARG PHE THR ILE PRO ARG GLY VAL
SEQRES 9 B 161 GLY GLY ARG GLY ASP ALA GLY ARG PRO ILE MET ASP ASN
SEQRES 10 B 161 SER GLY ARG VAL VAL ALA ILE VAL LEU GLY GLY ALA ASP
SEQRES 11 B 161 GLU GLY THR ARG THR ALA LEU SER VAL VAL THR TRP ASN
SEQRES 12 B 161 SER LYS GLY LYS THR ILE LYS THR THR PRO GLU GLY THR
SEQRES 13 B 161 GLU GLU TRP SER ALA
FORMUL 3 HOH *133(H2 O)
HELIX 1 1 LEU A 151 LYS A 153 5 3
HELIX 2 3 VAL A 171 MET A 173 5 3
HELIX 3 4 LEU B 151 LYS B 153 5 3
HELIX 4 6 VAL B 171 MET B 173 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 ASP A 147 -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 GLY A 216 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 THR A 261 GLU A 262 -1
SHEET 1 B1 6 LEU B 115 LYS B 119 0
SHEET 2 B1 6 VAL B 125 MET B 132 -1
SHEET 3 B1 6 LYS B 135 PRO B 139 -1
SHEET 4 B1 6 THR B 145 ASP B 147 -1
SHEET 5 B1 6 THR B 157 SER B 159 -1
SHEET 6 B1 6 MET B 164 GLN B 168 -1
SHEET 1 B2 8 GLY B 187 TRP B 191 0
SHEET 2 B2 8 GLY B 194 SER B 199 -1
SHEET 3 B2 8 ARG B 202 PRO B 206 -1
SHEET 4 B2 8 GLY B 216 MET B 220 -1
SHEET 5 B2 8 VAL B 226 GLU B 236 -1
SHEET 6 B2 8 ARG B 239 TRP B 247 -1
SHEET 7 B2 8 THR B 253 THR B 256 -1
SHEET 8 B2 8 THR B 261 GLU B 262 -1
SITE 1 TRI 6 ALA A 215 HIS A 141 ASP A 163 ALA B 215
SITE 2 TRI 6 HIS B 141 ASP B 163
CRYST1 29.000 56.500 60.830 93.10 96.73 94.93 P 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 0.034483 0.002974 0.004271 0.00000
SCALE2 0.000000 0.017765 0.001154 0.00000
SCALE3 0.000000 0.000000 0.016588 0.00000
MTRIX1 1 0.999566 0.003141 -0.029297 8.50972 1
MTRIX2 1 -0.010181 0.969880 -0.243369 25.86226 1
MTRIX3 1 0.027650 0.243561 0.969491 30.28011 1
(ATOM LINES ARE NOT SHOWN.)
END
