HEADER VIRUS 11-FEB-03 1NY7
TITLE COWPEA MOSAIC VIRUS (CPMV)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COWPEA MOSAIC VIRUS, SMALL (S) SUBUNIT;
COMPND 3 CHAIN: 1;
COMPND 4 SYNONYM: CPMV, GENOME POLYPROTEIN M [CONTAINS: COAT PROTEIN VP37;
COMPND 5 COAT PROTEIN VP23];
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: COWPEA MOSAIC VIRUS, LARGE (L) SUBUNIT;
COMPND 8 CHAIN: 2;
COMPND 9 SYNONYM: CPMV, GENOME POLYPROTEIN M [CONTAINS: COAT PROTEIN VP37;
COMPND 10 COAT PROTEIN VP23]
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COWPEA MOSAIC VIRUS;
SOURCE 3 ORGANISM_TAXID: 12264;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: COWPEA MOSAIC VIRUS;
SOURCE 6 ORGANISM_TAXID: 12264
KEYWDS COMOVIRUS, VIRUS, VIRAL COAT PROTEIN, COWPEA MOSAIC VIRUS (CPMV),
KEYWDS 2 ICOSAHEDRAL VIRUS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LIN,Z.CHEN,R.USHA,C.V.STAUFFACHER,J.-B.DAI,T.SCHMIDT,J.E.JOHNSON
REVDAT 6 11-OCT-17 1NY7 1 REMARK
REVDAT 5 09-APR-14 1NY7 1 JRNL VERSN
REVDAT 4 24-FEB-09 1NY7 1 VERSN
REVDAT 3 26-AUG-03 1NY7 1 REMARK
REVDAT 2 25-MAR-03 1NY7 1 SOURCE
REVDAT 1 18-MAR-03 1NY7 0
JRNL AUTH T.LIN,Z.CHEN,R.USHA,C.V.STAUFFACHER,J.-B.DAI,T.SCHMIDT,
JRNL AUTH 2 J.E.JOHNSON
JRNL TITL THE REFINED CRYSTAL STRUCTURE OF COWPEA MOSAIC VIRUS AT 2.8A
JRNL TITL 2 RESOLUTION
JRNL REF VIROLOGY V. 265 20 1999
JRNL REFN ISSN 0042-6822
JRNL PMID 10603314
JRNL DOI 10.1006/VIRO.1999.0038
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.V.STAUFFACHER,R.USHA,M.HARRINGTON,T.SCHMIDT,M.HOSUR,
REMARK 1 AUTH 2 J.E.JOHNSON
REMARK 1 TITL THE STRUCTURE OF COWPEA MOSAIC VIRUS AT 3.5 A RESOLUTION
REMARK 1 REF CRYSTALLOGRAPHY IN MOLECULAR 293 1987
REMARK 1 REF 2 BIOLOGY
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.2
REMARK 3 NUMBER OF REFLECTIONS : 88089
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : NULL
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12129
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
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 : 4343
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.750
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : CONSTR
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 10
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : FILM
REMARK 200 DETECTOR MANUFACTURER : KODAK
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MGROSC
REMARK 200 DATA SCALING SOFTWARE : MGROSC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89846
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR AND MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: IN-HOUSE AVERAGING PROGRAM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASIUM PHOSPHATE, AMMONIUM
REMARK 280 SULFATE, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 158.50000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 158.50000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 158.50000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 158.50000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 158.50000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 158.50000
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).
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 APPLY THE FOLLOWING TO CHAINS: 1, 2
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 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT2 2 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT3 2 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT1 3 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT2 3 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT3 3 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT1 4 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 4 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT3 4 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT1 5 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 5 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT3 5 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT1 6 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 6 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT3 6 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 8 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 8 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT1 9 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 9 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 9 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT1 10 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 10 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT3 10 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT1 11 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT2 11 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT3 11 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 12 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT2 12 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT3 12 0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 13 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 13 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 13 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 14 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT2 14 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 14 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 15 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT2 15 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 15 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 16 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT2 16 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 16 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 17 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 17 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 17 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 18 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 18 0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 18 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 19 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 19 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 19 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 20 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT2 20 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 20 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 21 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT2 21 0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 21 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT1 22 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 22 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 23 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 23 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 23 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT1 24 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 24 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 24 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT1 25 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT2 25 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 25 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT1 26 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 26 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 26 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 27 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT2 27 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 27 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 28 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT2 28 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 28 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 29 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT2 29 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 29 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT1 30 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT2 30 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 30 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT1 31 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 31 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT3 31 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 32 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 32 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT3 32 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT1 33 0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 33 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT3 33 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT1 34 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 34 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 34 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 35 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 35 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT3 35 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 36 0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT2 36 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT3 36 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 37 -0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT2 37 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT3 37 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 38 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 38 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 38 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 39 -0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 39 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT3 39 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 40 0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 40 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT3 40 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 41 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT2 41 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT3 41 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT1 42 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT2 42 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 42 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT1 43 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT2 43 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 43 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT1 44 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 44 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 44 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 45 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT2 45 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT3 45 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT1 46 -0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT2 46 0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT3 46 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 47 -0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT2 47 0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT3 47 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 48 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 48 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 48 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 49 0.809017 0.500000 0.309017 0.00000
REMARK 350 BIOMT2 49 -0.500000 0.309017 0.809017 0.00000
REMARK 350 BIOMT3 49 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT1 50 0.500000 -0.309017 0.809017 0.00000
REMARK 350 BIOMT2 50 -0.309017 0.809017 0.500000 0.00000
REMARK 350 BIOMT3 50 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT1 51 0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 51 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 51 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT1 52 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 52 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 52 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 53 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT2 53 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT3 53 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT1 54 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 54 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 54 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT1 55 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 55 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 55 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 56 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 56 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 56 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 57 0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 57 0.309017 -0.809017 0.500000 0.00000
REMARK 350 BIOMT3 57 -0.809017 -0.500000 -0.309017 0.00000
REMARK 350 BIOMT1 58 0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 58 -0.809017 -0.500000 0.309017 0.00000
REMARK 350 BIOMT3 58 -0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 59 -0.309017 -0.809017 -0.500000 0.00000
REMARK 350 BIOMT2 59 -0.809017 0.500000 -0.309017 0.00000
REMARK 350 BIOMT3 59 0.500000 0.309017 -0.809017 0.00000
REMARK 350 BIOMT1 60 -0.500000 -0.309017 -0.809017 0.00000
REMARK 350 BIOMT2 60 0.309017 0.809017 -0.500000 0.00000
REMARK 350 BIOMT3 60 0.809017 -0.500000 -0.309017 0.00000
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 MET 2 1 SD MET 2 1 CE 2.467
REMARK 500 CYS 2 132 CB CYS 2 132 SG -0.108
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 TRP 1 47 N - CA - C ANGL. DEV. = -29.0 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 ASP 1 9 171.63 73.37
REMARK 500 SER 1 25 15.91 -158.42
REMARK 500 ASP 1 45 -159.05 -52.72
REMARK 500 ASN 1 46 45.61 75.45
REMARK 500 SER 1 111 89.55 -165.54
REMARK 500 SER 1 129 47.80 176.73
REMARK 500 ALA 1 134 108.89 -39.88
REMARK 500 TRP 1 138 -96.10 -45.34
REMARK 500 ALA 1 139 33.30 -87.80
REMARK 500 ASN 1 152 88.31 -152.01
REMARK 500 PRO 1 153 -8.83 -57.68
REMARK 500 SER 2 9 47.71 -84.34
REMARK 500 ASP 2 11 39.10 -91.28
REMARK 500 ASN 2 52 -86.44 -56.98
REMARK 500 ASP 2 55 54.58 -144.10
REMARK 500 THR 2 78 156.49 178.08
REMARK 500 ASP 2 82 0.12 -61.27
REMARK 500 CYS 2 86 -173.37 179.87
REMARK 500 GLN 2 110 -77.20 -84.99
REMARK 500 ASN 2 122 154.91 179.78
REMARK 500 PRO 2 129 0.23 -69.85
REMARK 500 ASN 2 174 32.12 -85.14
REMARK 500 LEU 2 184 46.08 -94.66
REMARK 500 THR 2 224 98.22 -59.67
REMARK 500 ASP 2 332 -80.11 -122.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN 1 46 13.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BMV RELATED DB: PDB
REMARK 900 A VIRUS IN THE SAME FAMILY
DBREF 1NY7 1 1 189 UNP P03599 VGNM_CPMV 834 1022
DBREF 1NY7 2 1 369 UNP P03599 VGNM_CPMV 460 828
SEQRES 1 1 189 GLY PRO VAL CYS ALA GLU ALA SER ASP VAL TYR SER PRO
SEQRES 2 1 189 CYS MET ILE ALA SER THR PRO PRO ALA PRO PHE SER ASP
SEQRES 3 1 189 VAL THR ALA VAL THR PHE ASP LEU ILE ASN GLY LYS ILE
SEQRES 4 1 189 THR PRO VAL GLY ASP ASP ASN TRP ASN THR HIS ILE TYR
SEQRES 5 1 189 ASN PRO PRO ILE MET ASN VAL LEU ARG THR ALA ALA TRP
SEQRES 6 1 189 LYS SER GLY THR ILE HIS VAL GLN LEU ASN VAL ARG GLY
SEQRES 7 1 189 ALA GLY VAL LYS ARG ALA ASP TRP ASP GLY GLN VAL PHE
SEQRES 8 1 189 VAL TYR LEU ARG GLN SER MET ASN PRO GLU SER TYR ASP
SEQRES 9 1 189 ALA ARG THR PHE VAL ILE SER GLN PRO GLY SER ALA MET
SEQRES 10 1 189 LEU ASN PHE SER PHE ASP ILE ILE GLY PRO ASN SER GLY
SEQRES 11 1 189 PHE GLU PHE ALA GLU SER PRO TRP ALA ASN GLN THR THR
SEQRES 12 1 189 TRP TYR LEU GLU CYS VAL ALA THR ASN PRO ARG GLN ILE
SEQRES 13 1 189 GLN GLN PHE GLU VAL ASN MET ARG PHE ASP PRO ASN PHE
SEQRES 14 1 189 ARG VAL ALA GLY ASN ILE LEU MET PRO PRO PHE PRO LEU
SEQRES 15 1 189 SER THR GLU THR PRO PRO LEU
SEQRES 1 2 369 MET GLU GLN ASN LEU PHE ALA LEU SER LEU ASP ASP THR
SEQRES 2 2 369 SER SER VAL ARG GLY SER LEU LEU ASP THR LYS PHE ALA
SEQRES 3 2 369 GLN THR ARG VAL LEU LEU SER LYS ALA MET ALA GLY GLY
SEQRES 4 2 369 ASP VAL LEU LEU ASP GLU TYR LEU TYR ASP VAL VAL ASN
SEQRES 5 2 369 GLY GLN ASP PHE ARG ALA THR VAL ALA PHE LEU ARG THR
SEQRES 6 2 369 HIS VAL ILE THR GLY LYS ILE LYS VAL THR ALA THR THR
SEQRES 7 2 369 ASN ILE SER ASP ASN SER GLY CYS CYS LEU MET LEU ALA
SEQRES 8 2 369 ILE ASN SER GLY VAL ARG GLY LYS TYR SER THR ASP VAL
SEQRES 9 2 369 TYR THR ILE CYS SER GLN ASP SER MET THR TRP ASN PRO
SEQRES 10 2 369 GLY CYS LYS LYS ASN PHE SER PHE THR PHE ASN PRO ASN
SEQRES 11 2 369 PRO CYS GLY ASP SER TRP SER ALA GLU MET ILE SER ARG
SEQRES 12 2 369 SER ARG VAL ARG MET THR VAL ILE CYS VAL SER GLY TRP
SEQRES 13 2 369 THR LEU SER PRO THR THR ASP VAL ILE ALA LYS LEU ASP
SEQRES 14 2 369 TRP SER ILE VAL ASN GLU LYS CYS GLU PRO THR ILE TYR
SEQRES 15 2 369 HIS LEU ALA ASP CYS GLN ASN TRP LEU PRO LEU ASN ARG
SEQRES 16 2 369 TRP MET GLY LYS LEU THR PHE PRO GLN GLY VAL THR SER
SEQRES 17 2 369 GLU VAL ARG ARG MET PRO LEU SER ILE GLY GLY GLY ALA
SEQRES 18 2 369 GLY ALA THR GLN ALA PHE LEU ALA ASN MET PRO ASN SER
SEQRES 19 2 369 TRP ILE SER MET TRP ARG TYR PHE ARG GLY GLU LEU HIS
SEQRES 20 2 369 PHE GLU VAL THR LYS MET SER SER PRO TYR ILE LYS ALA
SEQRES 21 2 369 THR VAL THR PHE LEU ILE ALA PHE GLY ASN LEU SER ASP
SEQRES 22 2 369 ALA PHE GLY PHE TYR GLU SER PHE PRO HIS ARG ILE VAL
SEQRES 23 2 369 GLN PHE ALA GLU VAL GLU GLU LYS CYS THR LEU VAL PHE
SEQRES 24 2 369 SER GLN GLN GLU PHE VAL THR ALA TRP SER THR GLN VAL
SEQRES 25 2 369 ASN PRO ARG THR THR LEU GLU ALA ASP GLY CYS PRO TYR
SEQRES 26 2 369 LEU TYR ALA ILE ILE HIS ASP SER THR THR GLY THR ILE
SEQRES 27 2 369 SER GLY ASP PHE ASN LEU GLY VAL LYS LEU VAL GLY ILE
SEQRES 28 2 369 LYS ASP PHE CYS GLY ILE GLY SER ASN PRO GLY ILE ASP
SEQRES 29 2 369 GLY SER ARG LEU LEU
FORMUL 3 HOH *64(H2 O)
HELIX 1 1 PRO 1 54 THR 1 62 1 9
HELIX 2 2 LYS 1 82 TRP 1 86 5 5
HELIX 3 3 ASN 2 4 ASP 2 12 5 9
HELIX 4 4 TYR 2 48 ASN 2 52 5 5
HELIX 5 5 ALA 2 58 THR 2 65 1 8
HELIX 6 6 ASP 2 103 CYS 2 108 1 6
HELIX 7 7 SER 2 137 SER 2 144 1 8
HELIX 8 8 ASN 2 230 SER 2 237 1 8
HELIX 9 9 PHE 2 277 PHE 2 281 5 5
HELIX 10 10 SER 2 300 PHE 2 304 5 5
HELIX 11 11 THR 2 317 ASP 2 321 5 5
SHEET 1 A10 ASN 1 48 ILE 1 51 0
SHEET 2 A10 SER 1 12 SER 1 18 -1 N ILE 1 16 O HIS 1 50
SHEET 3 A10 ILE 1 156 PHE 1 165 -1 N PHE 1 159 O ALA 1 17
SHEET 4 A10 ALA 1 63 GLY 1 78 -1 N HIS 1 71 O ARG 1 164
SHEET 5 A10 ALA 1 116 ILE 1 124 -1 O ALA 1 116 N VAL 1 76
SHEET 6 A10 ALA 1 63 GLY 1 78 -1 O GLY 1 68 N ILE 1 124
SHEET 7 A10 ARG 1 170 LEU 1 176 -1 O ARG 1 170 N SER 1 67
SHEET 8 A10 GLY 2 95 VAL 2 96 1 O GLY 2 95 N LEU 1 176
SHEET 9 A10 ARG 1 170 LEU 1 176 1 O ASN 1 174 N GLY 2 95
SHEET 10 A10 TYR 2 182 HIS 2 183 -1 N TYR 2 182 O VAL 1 171
SHEET 1 B 5 LYS 1 38 PRO 1 41 0
SHEET 2 B 5 THR 1 28 ASP 1 33 -1 N THR 1 31 O THR 1 40
SHEET 3 B 5 TYR 1 145 ALA 1 150 -1 O LEU 1 146 N PHE 1 32
SHEET 4 B 5 VAL 1 90 ARG 1 95 -1 O PHE 1 91 N VAL 1 149
SHEET 5 B 5 ARG 1 106 ILE 1 110 -1 O ARG 1 106 N LEU 1 94
SHEET 1 C 3 PHE 1 180 PRO 1 181 0
SHEET 2 C 3 ALA 2 226 LEU 2 228 -1 O PHE 2 227 N PHE 1 180
SHEET 3 C 3 ALA 2 221 ALA 2 223 -1 O ALA 2 221 N LEU 2 228
SHEET 1 D 4 LYS 2 24 LEU 2 32 0
SHEET 2 D 4 VAL 2 164 VAL 2 173 -1 N VAL 2 164 O LEU 2 32
SHEET 3 D 4 LYS 2 71 THR 2 77 -1 O LYS 2 71 N VAL 2 173
SHEET 4 D 4 ASN 2 122 PHE 2 127 -1 O PHE 2 123 N ALA 2 76
SHEET 1 E 4 VAL 2 41 TYR 2 46 0
SHEET 2 E 4 ARG 2 147 SER 2 154 -1 N MET 2 148 O GLU 2 45
SHEET 3 E 4 CYS 2 87 ASN 2 93 -1 O CYS 2 87 N VAL 2 153
SHEET 4 E 4 ASP 2 111 TRP 2 115 -1 O ASP 2 111 N ILE 2 92
SHEET 1 F 6 CYS 2 187 PHE 2 202 0
SHEET 2 F 6 PHE 2 342 SER 2 359 -1 N PHE 2 342 O PHE 2 202
SHEET 3 F 6 TRP 2 239 LYS 2 252 -1 N ARG 2 240 O GLY 2 358
SHEET 4 F 6 TRP 2 308 SER 2 309 -1 O TRP 2 308 N PHE 2 242
SHEET 5 F 6 TRP 2 239 LYS 2 252 -1 N PHE 2 242 O TRP 2 308
SHEET 6 F 6 LYS 2 294 PHE 2 299 -1 O CYS 2 295 N VAL 2 250
SHEET 1 G 4 VAL 2 210 PRO 2 214 0
SHEET 2 G 4 PRO 2 324 ILE 2 330 -1 N LEU 2 326 O MET 2 213
SHEET 3 G 4 VAL 2 262 PHE 2 268 -1 N THR 2 263 O ILE 2 329
SHEET 4 G 4 HIS 2 283 VAL 2 286 -1 N ARG 2 284 O PHE 2 264
SSBOND 1 CYS 2 187 CYS 2 355 1555 1555 2.89
CISPEP 1 ALA 1 22 PRO 1 23 0 0.80
CRYST1 317.000 317.000 317.000 90.00 90.00 90.00 I 2 3 120
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 0.003155 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003155 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.309017 -0.809017 0.500000 0.00000
MTRIX2 2 0.809017 0.500000 0.309017 0.00000
MTRIX3 2 -0.500000 0.309017 0.809017 0.00000
MTRIX1 3 -0.809017 -0.500000 0.309017 0.00000
MTRIX2 3 0.500000 -0.309017 0.809017 0.00000
MTRIX3 3 -0.309017 0.809017 0.500000 0.00000
MTRIX1 4 -0.809017 0.500000 -0.309017 0.00000
MTRIX2 4 -0.500000 -0.309017 0.809017 0.00000
MTRIX3 4 0.309017 0.809017 0.500000 0.00000
MTRIX1 5 0.309017 0.809017 -0.500000 0.00000
MTRIX2 5 -0.809017 0.500000 0.309017 0.00000
MTRIX3 5 0.500000 0.309017 0.809017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
