HEADER VIRUS 02-MAR-95 1HRV
TITLE HRV14/SDZ 35-682 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1);
COMPND 3 CHAIN: 1;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2);
COMPND 7 CHAIN: 2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3);
COMPND 11 CHAIN: 3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP4);
COMPND 15 CHAIN: 4;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;
SOURCE 3 ORGANISM_TAXID: 12131;
SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;
SOURCE 10 ORGANISM_TAXID: 12131;
SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;
SOURCE 17 ORGANISM_TAXID: 12131;
SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;
SOURCE 24 ORGANISM_TAXID: 12131;
SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 26 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS
KEYWDS ANTIVIRAL AGENTS, ICOSAHEDRAL VIRUS, VIRUS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.OREN,A.ZHANG,E.ARNOLD
REVDAT 4 15-MAR-23 1HRV 1 REMARK
REVDAT 3 18-JAN-23 1HRV 1 REMARK SEQADV CRYST1 MTRIX
REVDAT 3 2 1 ATOM
REVDAT 2 24-FEB-09 1HRV 1 VERSN
REVDAT 1 03-JUN-95 1HRV 0
JRNL AUTH B.ROSENWIRTH,D.A.OREN,E.ARNOLD,Z.L.KIS,H.J.EGGERS
JRNL TITL SDZ 35-682, A NEW PICORNAVIRUS CAPSID-BINDING AGENT WITH
JRNL TITL 2 POTENT ANTIVIRAL ACTIVITY.
JRNL REF ANTIVIRAL RES. V. 26 65 1995
JRNL REFN ISSN 0166-3542
JRNL PMID 7741522
JRNL DOI 10.1016/0166-3542(94)00066-H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.ZHANG,R.G.NANNI,T.LI,G.F.ARNOLD,D.A.OREN,A.JACOBO-MOLINA,
REMARK 1 AUTH 2 R.L.WILLIAMS,G.KAMER,D.A.RUBENSTEIN,Y.LI,E.ROZHON,S.COX,
REMARK 1 AUTH 3 P.BUONTEMPO,J.O'CONNELL,J.SCHWARTZ,G.MILLER,B.BAUER,
REMARK 1 AUTH 4 R.VERSACE,P.PINTO,A.GANGULY,V.GIRIJAVALLABHAN,E.ARNOLD
REMARK 1 TITL STRUCTURE DETERMINATION OF ANTIVIRAL COMPOUND SCH 38057
REMARK 1 TITL 2 COMPLEXED WITH HUMAN RHINOVIRUS 14
REMARK 1 REF J.MOL.BIOL. V. 230 857 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.ZHANG,R.G.NANNI,D.A.OREN,E.J.ROZHON,E.ARNOLD
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE-ACTIVITY RELATIONSHIPS FOR
REMARK 1 TITL 2 ANTIVIRAL AGENTS THAT INTERACT WITH PICORNAVIRUS CAPSIDS
REMARK 1 REF SEMIN.VIROL. V. 3 453 1992
REMARK 1 REFN ISSN 1044-5773
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.ARNOLD,M.G.ROSSMANN
REMARK 1 TITL ANALYSIS OF THE STRUCTURE OF A COMMON COLD VIRUS, HUMAN
REMARK 1 TITL 2 RHINOVIRUS 14, REFINED AT A RESOLUTION OF 3.0 ANGSTROMS
REMARK 1 REF J.MOL.BIOL. V. 211 763 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH E.ARNOLD,M.G.ROSSMANN
REMARK 1 TITL THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT
REMARK 1 TITL 2 OF THE HUMAN RHINOVIRUS 14 STRUCTURE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 44 270 1988
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.G.ROSSMANN,E.ARNOLD,J.W.ERICKSON,E.A.FRANKENBERGER,
REMARK 1 AUTH 2 J.P.GRIFFITH,H.-J.HECHT,J.E.JOHNSON,G.KAMER,M.LUO,
REMARK 1 AUTH 3 A.G.MOSSER,R.R.RUECKERT,B.SHERRY,G.VRIEND
REMARK 1 TITL STRUCTURE OF A HUMAN COMMON COLD VIRUS AND FUNCTIONAL
REMARK 1 TITL 2 RELATIONSHIP TO OTHER PICORNAVIRUSES
REMARK 1 REF NATURE V. 317 145 1985
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFI IN O
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : NULL
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) : NULL
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 : 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 : 6268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 1HRV 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_1000173986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-90; JAN-91
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : CHESS; CHESS
REMARK 200 BEAMLINE : A1; F1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : FILM; FILM
REMARK 200 DETECTOR MANUFACTURER : NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PURDUE DATA PROCESSING PACKAGE
REMARK 200 DATA SCALING SOFTWARE : NULL
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 : NULL
REMARK 200 R MERGE (I) : 0.12300
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; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: OSCILLATION RANGE 0.3 DEGREES, DISTANCE=100 AND 168 MM
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: 3-4 CRYSTALS SOAKED IN 200 MICROLITER
REMARK 280 DROPS OF SDZ 35-682 (5 MICROGRAM/ML).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,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 222.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 222.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 222.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 222.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 222.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 222.55000
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 222.55000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 222.55000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 222.55000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 222.55000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 222.55000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 222.55000
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 222.55000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 222.55000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 222.55000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 222.55000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 222.55000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 222.55000
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, 3, 4
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 0.464282 -0.829905 0.309355 0.18336
REMARK 350 BIOMT2 2 0.844397 0.309355 -0.437372 0.04923
REMARK 350 BIOMT3 2 0.267276 0.464282 0.844397 -0.09998
REMARK 350 BIOMT1 3 -0.402527 -0.498417 0.767823 0.19670
REMARK 350 BIOMT2 3 0.536358 -0.808132 -0.243400 0.26302
REMARK 350 BIOMT3 3 0.741817 0.313853 0.592625 -0.11254
REMARK 350 BIOMT1 4 -0.402527 0.536358 0.741817 0.02159
REMARK 350 BIOMT2 4 -0.498417 -0.808132 0.313853 0.34591
REMARK 350 BIOMT3 4 0.767823 -0.243400 0.592625 -0.02032
REMARK 350 BIOMT1 5 0.464282 0.844397 0.267276 -0.09998
REMARK 350 BIOMT2 5 -0.829905 0.309355 0.464282 0.18336
REMARK 350 BIOMT3 5 0.309355 -0.437372 0.844397 0.04923
REMARK 350 BIOMT1 6 -0.829905 0.309355 0.464282 0.18336
REMARK 350 BIOMT2 6 0.309355 -0.437372 0.844397 0.04923
REMARK 350 BIOMT3 6 0.464282 0.844397 0.267276 -0.09998
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.844397 0.309355 -0.437372 0.04923
REMARK 350 BIOMT2 8 0.267276 0.464282 0.844397 -0.09998
REMARK 350 BIOMT3 8 0.464282 -0.829905 0.309355 0.18336
REMARK 350 BIOMT1 9 0.536358 -0.808132 -0.243400 0.26302
REMARK 350 BIOMT2 9 0.741817 0.313853 0.592625 -0.11254
REMARK 350 BIOMT3 9 -0.402527 -0.498417 0.767823 0.19670
REMARK 350 BIOMT1 10 -0.498417 -0.808132 0.313853 0.34591
REMARK 350 BIOMT2 10 0.767823 -0.243400 0.592625 -0.02032
REMARK 350 BIOMT3 10 -0.402527 0.536358 0.741817 0.02159
REMARK 350 BIOMT1 11 -0.630565 -0.701509 0.332074 0.34718
REMARK 350 BIOMT2 11 -0.701509 0.332074 -0.630565 0.34718
REMARK 350 BIOMT3 11 0.332074 -0.630565 -0.701509 0.34718
REMARK 350 BIOMT1 12 -0.796357 0.460470 0.392154 0.16382
REMARK 350 BIOMT2 12 -0.213831 0.392154 -0.894702 0.29795
REMARK 350 BIOMT3 12 -0.565768 -0.796357 -0.213831 0.44716
REMARK 350 BIOMT1 13 0.123898 0.985418 -0.116620 0.00127
REMARK 350 BIOMT2 13 -0.007277 -0.116620 -0.993150 0.36750
REMARK 350 BIOMT3 13 -0.992269 0.123898 -0.007277 0.32559
REMARK 350 BIOMT1 14 0.858438 0.147876 -0.491140 0.08416
REMARK 350 BIOMT2 14 -0.367298 -0.491140 -0.789857 0.45972
REMARK 350 BIOMT3 14 -0.358019 0.858438 -0.367298 0.15048
REMARK 350 BIOMT1 15 0.392154 -0.894702 -0.213831 0.29795
REMARK 350 BIOMT2 15 -0.796357 -0.213831 -0.565768 0.44716
REMARK 350 BIOMT3 15 0.460470 0.392154 -0.796357 0.16382
REMARK 350 BIOMT1 16 0.460470 0.392154 -0.796357 0.16382
REMARK 350 BIOMT2 16 0.392154 -0.894702 -0.213831 0.29795
REMARK 350 BIOMT3 16 -0.796357 -0.213831 -0.565768 0.44716
REMARK 350 BIOMT1 17 0.332074 -0.630565 -0.701509 0.34718
REMARK 350 BIOMT2 17 -0.630565 -0.701509 0.332074 0.34718
REMARK 350 BIOMT3 17 -0.701509 0.332074 -0.630565 0.34718
REMARK 350 BIOMT1 18 -0.565768 -0.796357 -0.213831 0.44716
REMARK 350 BIOMT2 18 -0.796357 0.460470 0.392154 0.16382
REMARK 350 BIOMT3 18 -0.213831 0.392154 -0.894702 0.29795
REMARK 350 BIOMT1 19 -0.992269 0.123898 -0.007277 0.32559
REMARK 350 BIOMT2 19 0.123898 0.985418 -0.116620 0.00127
REMARK 350 BIOMT3 19 -0.007277 -0.116620 -0.993150 0.36750
REMARK 350 BIOMT1 20 -0.358019 0.858438 -0.367298 0.15048
REMARK 350 BIOMT2 20 0.858438 0.147876 -0.491140 0.08416
REMARK 350 BIOMT3 20 -0.367298 -0.491140 -0.789857 0.45972
REMARK 350 BIOMT1 21 -0.491140 -0.789857 -0.367298 0.45972
REMARK 350 BIOMT2 21 0.858438 -0.367298 -0.358019 0.15048
REMARK 350 BIOMT3 21 0.147876 -0.491140 0.858438 0.08416
REMARK 350 BIOMT1 22 -0.993150 -0.007277 -0.116620 0.36750
REMARK 350 BIOMT2 22 -0.007277 -0.992269 0.123898 0.32559
REMARK 350 BIOMT3 22 -0.116620 0.123898 0.985418 0.00127
REMARK 350 BIOMT1 23 -0.498417 0.767823 -0.402527 0.19670
REMARK 350 BIOMT2 23 -0.808132 -0.243400 0.536358 0.26302
REMARK 350 BIOMT3 23 0.313853 0.592625 0.741817 -0.11254
REMARK 350 BIOMT1 24 0.309355 0.464282 -0.829905 0.18336
REMARK 350 BIOMT2 24 -0.437372 0.844397 0.309355 0.04923
REMARK 350 BIOMT3 24 0.844397 0.267276 0.464282 -0.09998
REMARK 350 BIOMT1 25 0.313853 -0.498417 -0.808132 0.34591
REMARK 350 BIOMT2 25 0.592625 0.767823 -0.243400 -0.02032
REMARK 350 BIOMT3 25 0.741817 -0.402527 0.536358 0.02159
REMARK 350 BIOMT1 26 -0.007277 -0.116620 -0.993150 0.36750
REMARK 350 BIOMT2 26 -0.992269 0.123898 -0.007277 0.32559
REMARK 350 BIOMT3 26 0.123898 0.985418 -0.116620 0.00127
REMARK 350 BIOMT1 27 -0.367298 -0.491140 -0.789857 0.45972
REMARK 350 BIOMT2 27 -0.358019 0.858438 -0.367298 0.15048
REMARK 350 BIOMT3 27 0.858438 0.147876 -0.491140 0.08416
REMARK 350 BIOMT1 28 -0.796357 -0.213831 -0.565768 0.44716
REMARK 350 BIOMT2 28 0.460470 0.392154 -0.796357 0.16382
REMARK 350 BIOMT3 28 0.392154 -0.894702 -0.213831 0.29795
REMARK 350 BIOMT1 29 -0.701509 0.332074 -0.630565 0.34718
REMARK 350 BIOMT2 29 0.332074 -0.630565 -0.701509 0.34718
REMARK 350 BIOMT3 29 -0.630565 -0.701509 0.332074 0.34718
REMARK 350 BIOMT1 30 -0.213831 0.392154 -0.894702 0.29795
REMARK 350 BIOMT2 30 -0.565768 -0.796357 -0.213831 0.44716
REMARK 350 BIOMT3 30 -0.796357 0.460470 0.392154 0.16382
REMARK 350 BIOMT1 31 0.741817 0.313853 0.592625 -0.11254
REMARK 350 BIOMT2 31 -0.402527 -0.498417 0.767823 0.19670
REMARK 350 BIOMT3 31 0.536358 -0.808132 -0.243400 0.26302
REMARK 350 BIOMT1 32 0.767823 -0.243400 0.592625 -0.02032
REMARK 350 BIOMT2 32 -0.402527 0.536358 0.741817 0.02159
REMARK 350 BIOMT3 32 -0.498417 -0.808132 0.313853 0.34591
REMARK 350 BIOMT1 33 0.309355 -0.437372 0.844397 0.04923
REMARK 350 BIOMT2 33 0.464282 0.844397 0.267276 -0.09998
REMARK 350 BIOMT3 33 -0.829905 0.309355 0.464282 0.18336
REMARK 350 BIOMT1 34 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 34 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 34 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 35 0.267276 0.464282 0.844397 -0.09998
REMARK 350 BIOMT2 35 0.464282 -0.829905 0.309355 0.18336
REMARK 350 BIOMT3 35 0.844397 0.309355 -0.437372 0.04923
REMARK 350 BIOMT1 36 -0.243400 0.592625 0.767823 -0.02032
REMARK 350 BIOMT2 36 0.536358 0.741817 -0.402527 0.02159
REMARK 350 BIOMT3 36 -0.808132 0.313853 -0.498417 0.34591
REMARK 350 BIOMT1 37 0.592625 0.741817 0.313853 -0.11254
REMARK 350 BIOMT2 37 0.767823 -0.402527 -0.498417 0.19670
REMARK 350 BIOMT3 37 -0.243400 0.536358 -0.808132 0.26302
REMARK 350 BIOMT1 38 0.985418 -0.116620 0.123898 0.00127
REMARK 350 BIOMT2 38 -0.116620 -0.993150 -0.007277 0.36750
REMARK 350 BIOMT3 38 0.123898 -0.007277 -0.992269 0.32559
REMARK 350 BIOMT1 39 0.392154 -0.796357 0.460470 0.16382
REMARK 350 BIOMT2 39 -0.894702 -0.213831 0.392154 0.29795
REMARK 350 BIOMT3 39 -0.213831 -0.565768 -0.796357 0.44716
REMARK 350 BIOMT1 40 -0.367298 -0.358019 0.858438 0.15048
REMARK 350 BIOMT2 40 -0.491140 0.858438 0.147876 0.08416
REMARK 350 BIOMT3 40 -0.789857 -0.367298 -0.491140 0.45972
REMARK 350 BIOMT1 41 -0.491140 0.858438 0.147876 0.08416
REMARK 350 BIOMT2 41 -0.789857 -0.367298 -0.491140 0.45972
REMARK 350 BIOMT3 41 -0.367298 -0.358019 0.858438 0.15048
REMARK 350 BIOMT1 42 0.536358 0.741817 -0.402527 0.02159
REMARK 350 BIOMT2 42 -0.808132 0.313853 -0.498417 0.34591
REMARK 350 BIOMT3 42 -0.243400 0.592625 0.767823 -0.02032
REMARK 350 BIOMT1 43 0.767823 -0.402527 -0.498417 0.19670
REMARK 350 BIOMT2 43 -0.243400 0.536358 -0.808132 0.26302
REMARK 350 BIOMT3 43 0.592625 0.741817 0.313853 -0.11254
REMARK 350 BIOMT1 44 -0.116620 -0.993150 -0.007277 0.36750
REMARK 350 BIOMT2 44 0.123898 -0.007277 -0.992269 0.32559
REMARK 350 BIOMT3 44 0.985418 -0.116620 0.123898 0.00127
REMARK 350 BIOMT1 45 -0.894702 -0.213831 0.392154 0.29795
REMARK 350 BIOMT2 45 -0.213831 -0.565768 -0.796357 0.44716
REMARK 350 BIOMT3 45 0.392154 -0.796357 0.460470 0.16382
REMARK 350 BIOMT1 46 0.741817 -0.402527 0.536358 0.02159
REMARK 350 BIOMT2 46 0.313853 -0.498417 -0.808132 0.34591
REMARK 350 BIOMT3 46 0.592625 0.767823 -0.243400 -0.02032
REMARK 350 BIOMT1 47 0.147876 -0.491140 0.858438 0.08416
REMARK 350 BIOMT2 47 -0.491140 -0.789857 -0.367298 0.45972
REMARK 350 BIOMT3 47 0.858438 -0.367298 -0.358019 0.15048
REMARK 350 BIOMT1 48 -0.116620 0.123898 0.985418 0.00127
REMARK 350 BIOMT2 48 -0.993150 -0.007277 -0.116620 0.36750
REMARK 350 BIOMT3 48 -0.007277 -0.992269 0.123898 0.32559
REMARK 350 BIOMT1 49 0.313853 0.592625 0.741817 -0.11254
REMARK 350 BIOMT2 49 -0.498417 0.767823 -0.402527 0.19670
REMARK 350 BIOMT3 49 -0.808132 -0.243400 0.536358 0.26302
REMARK 350 BIOMT1 50 0.844397 0.267276 0.464282 -0.09998
REMARK 350 BIOMT2 50 0.309355 0.464282 -0.829905 0.18336
REMARK 350 BIOMT3 50 -0.437372 0.844397 0.309355 0.04923
REMARK 350 BIOMT1 51 -0.243400 0.536358 -0.808132 0.26302
REMARK 350 BIOMT2 51 0.592625 0.741817 0.313853 -0.11254
REMARK 350 BIOMT3 51 0.767823 -0.402527 -0.498417 0.19670
REMARK 350 BIOMT1 52 0.123898 -0.007277 -0.992269 0.32559
REMARK 350 BIOMT2 52 0.985418 -0.116620 0.123898 0.00127
REMARK 350 BIOMT3 52 -0.116620 -0.993150 -0.007277 0.36750
REMARK 350 BIOMT1 53 -0.213831 -0.565768 -0.796357 0.44716
REMARK 350 BIOMT2 53 0.392154 -0.796357 0.460470 0.16382
REMARK 350 BIOMT3 53 -0.894702 -0.213831 0.392154 0.29795
REMARK 350 BIOMT1 54 -0.789857 -0.367298 -0.491140 0.45972
REMARK 350 BIOMT2 54 -0.367298 -0.358019 0.858438 0.15048
REMARK 350 BIOMT3 54 -0.491140 0.858438 0.147876 0.08416
REMARK 350 BIOMT1 55 -0.808132 0.313853 -0.498417 0.34591
REMARK 350 BIOMT2 55 -0.243400 0.592625 0.767823 -0.02032
REMARK 350 BIOMT3 55 0.536358 0.741817 -0.402527 0.02159
REMARK 350 BIOMT1 56 -0.007277 -0.992269 0.123898 0.32559
REMARK 350 BIOMT2 56 -0.116620 0.123898 0.985418 0.00127
REMARK 350 BIOMT3 56 -0.993150 -0.007277 -0.116620 0.36750
REMARK 350 BIOMT1 57 -0.808132 -0.243400 0.536358 0.26302
REMARK 350 BIOMT2 57 0.313853 0.592625 0.741817 -0.11254
REMARK 350 BIOMT3 57 -0.498417 0.767823 -0.402527 0.19670
REMARK 350 BIOMT1 58 -0.437372 0.844397 0.309355 0.04923
REMARK 350 BIOMT2 58 0.844397 0.267276 0.464282 -0.09998
REMARK 350 BIOMT3 58 0.309355 0.464282 -0.829905 0.18336
REMARK 350 BIOMT1 59 0.592625 0.767823 -0.243400 -0.02032
REMARK 350 BIOMT2 59 0.741817 -0.402527 0.536358 0.02159
REMARK 350 BIOMT3 59 0.313853 -0.498417 -0.808132 0.34591
REMARK 350 BIOMT1 60 0.858438 -0.367298 -0.358019 0.15048
REMARK 350 BIOMT2 60 0.147876 -0.491140 0.858438 0.08416
REMARK 350 BIOMT3 60 -0.491140 -0.789857 -0.367298 0.45972
REMARK 450
REMARK 450 SOURCE
REMARK 450 MOLECULE_NAME: HRV14. GROWN IN HELA CELLS.
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 GLY 1 1
REMARK 465 LEU 1 2
REMARK 465 GLY 1 3
REMARK 465 ASP 1 4
REMARK 465 GLU 1 5
REMARK 465 LEU 1 6
REMARK 465 GLU 1 7
REMARK 465 GLU 1 8
REMARK 465 VAL 1 9
REMARK 465 ILE 1 10
REMARK 465 VAL 1 11
REMARK 465 GLU 1 12
REMARK 465 LYS 1 13
REMARK 465 THR 1 14
REMARK 465 LYS 1 15
REMARK 465 GLN 1 16
REMARK 465 SER 2 1
REMARK 465 PRO 2 2
REMARK 465 ASN 2 3
REMARK 465 VAL 2 4
REMARK 465 GLU 2 5
REMARK 465 ALA 2 6
REMARK 465 CYS 2 7
REMARK 465 GLY 4 1
REMARK 465 ALA 4 2
REMARK 465 GLN 4 3
REMARK 465 VAL 4 4
REMARK 465 SER 4 5
REMARK 465 THR 4 6
REMARK 465 GLN 4 7
REMARK 465 LYS 4 8
REMARK 465 SER 4 9
REMARK 465 GLY 4 10
REMARK 465 SER 4 11
REMARK 465 HIS 4 12
REMARK 465 GLU 4 13
REMARK 465 ASN 4 14
REMARK 465 GLN 4 15
REMARK 465 ASN 4 16
REMARK 465 ILE 4 17
REMARK 465 LEU 4 18
REMARK 465 THR 4 19
REMARK 465 ASN 4 20
REMARK 465 GLY 4 21
REMARK 465 SER 4 22
REMARK 465 ASN 4 23
REMARK 465 GLN 4 24
REMARK 465 THR 4 25
REMARK 465 PHE 4 26
REMARK 465 THR 4 27
REMARK 465 VAL 4 28
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 OG1 THR 1 129 NH1 ARG 1 185 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 LYS 1 30 CD LYS 1 30 CE 0.157
REMARK 500 LYS 1 30 CE LYS 1 30 NZ 0.162
REMARK 500 GLU 1 38 CB GLU 1 38 CG -0.172
REMARK 500 GLU 1 52 C GLU 1 52 O 0.120
REMARK 500 SER 1 63 CB SER 1 63 OG -0.114
REMARK 500 GLY 1 72 C GLY 1 72 O 0.104
REMARK 500 GLU 1 81 CD GLU 1 81 OE1 0.071
REMARK 500 GLU 1 95 CB GLU 1 95 CG 0.193
REMARK 500 GLU 1 117 CD GLU 1 117 OE1 0.103
REMARK 500 SER 1 139 CB SER 1 139 OG 0.094
REMARK 500 SER 1 143 CB SER 1 143 OG 0.088
REMARK 500 SER 1 144 N SER 1 144 CA 0.120
REMARK 500 LYS 1 161 CE LYS 1 161 NZ 0.165
REMARK 500 SER 1 170 CB SER 1 170 OG -0.186
REMARK 500 SER 1 175 CB SER 1 175 OG -0.119
REMARK 500 GLU 1 234 CD GLU 1 234 OE1 0.081
REMARK 500 ARG 1 282 CD ARG 1 282 NE 0.126
REMARK 500 LYS 1 283 N LYS 1 283 CA 0.153
REMARK 500 LYS 1 283 CE LYS 1 283 NZ 0.159
REMARK 500 ASP 1 285 CA ASP 1 285 CB 0.260
REMARK 500 SER 1 288 CA SER 1 288 CB 0.121
REMARK 500 GLY 2 8 N GLY 2 8 CA 0.096
REMARK 500 ARG 2 12 NE ARG 2 12 CZ 0.083
REMARK 500 GLU 2 40 CD GLU 2 40 OE1 0.090
REMARK 500 LYS 2 52 CE LYS 2 52 NZ 0.198
REMARK 500 LYS 2 87 CB LYS 2 87 CG -0.170
REMARK 500 HIS 2 135 CE1 HIS 2 135 NE2 -0.073
REMARK 500 GLU 2 136 CB GLU 2 136 CG 0.144
REMARK 500 ARG 2 152 CD ARG 2 152 NE 0.122
REMARK 500 ARG 2 152 CZ ARG 2 152 NH2 0.091
REMARK 500 ASN 2 194 CA ASN 2 194 CB 0.181
REMARK 500 SER 2 219 CA SER 2 219 CB -0.115
REMARK 500 CYS 2 248 CB CYS 2 248 SG -0.141
REMARK 500 SER 2 256 CB SER 2 256 OG 0.132
REMARK 500 SER 2 256 C SER 2 256 O 0.127
REMARK 500 GLY 3 1 N GLY 3 1 CA 0.117
REMARK 500 SER 3 21 CA SER 3 21 CB 0.131
REMARK 500 ASP 3 50 CA ASP 3 50 CB -0.134
REMARK 500 ASN 3 57 CA ASN 3 57 CB 0.219
REMARK 500 LYS 3 61 CE LYS 3 61 NZ 0.168
REMARK 500 GLU 3 63 CD GLU 3 63 OE1 0.085
REMARK 500 SER 3 108 CB SER 3 108 OG 0.097
REMARK 500 GLY 3 138 N GLY 3 138 CA 0.094
REMARK 500 THR 3 164 C THR 3 164 O 0.130
REMARK 500 SER 3 194 CB SER 3 194 OG -0.080
REMARK 500 LYS 4 33 CD LYS 4 33 CE 0.153
REMARK 500 LYS 4 33 CE LYS 4 33 NZ 0.185
REMARK 500 SER 4 40 CB SER 4 40 OG 0.140
REMARK 500 ALA 4 41 C ALA 4 41 O 0.179
REMARK 500 GLY 4 42 N GLY 4 42 CA 0.176
REMARK 500
REMARK 500 THIS ENTRY HAS 53 BOND DEVIATIONS.
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 SER 1 22 N - CA - CB ANGL. DEV. = -9.7 DEGREES
REMARK 500 LYS 1 26 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 THR 1 28 CB - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 GLU 1 38 CA - CB - CG ANGL. DEV. = 19.5 DEGREES
REMARK 500 GLU 1 38 CB - CG - CD ANGL. DEV. = 21.6 DEGREES
REMARK 500 THR 1 42 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 THR 1 53 CA - CB - OG1 ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG 1 54 CD - NE - CZ ANGL. DEV. = -13.2 DEGREES
REMARK 500 SER 1 63 CB - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP 1 66 CB - CG - OD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLU 1 68 CG - CD - OE1 ANGL. DEV. = -13.1 DEGREES
REMARK 500 GLU 1 68 CG - CD - OE2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP 1 86 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG 1 94 CD - NE - CZ ANGL. DEV. = -16.9 DEGREES
REMARK 500 ARG 1 94 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG 1 94 NE - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLU 1 95 CB - CG - CD ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLU 1 95 OE1 - CD - OE2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 LYS 1 97 CD - CE - NZ ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG 1 113 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG 1 113 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 GLU 1 117 CG - CD - OE1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 GLU 1 117 CG - CD - OE2 ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU 1 118 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 TYR 1 121 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 VAL 1 122 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 ASP 1 138 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 SER 1 144 N - CA - CB ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASN 1 145 CA - CB - CG ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASN 1 145 OD1 - CG - ND2 ANGL. DEV. = 17.9 DEGREES
REMARK 500 MET 1 151 CG - SD - CE ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASP 1 165 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP 1 165 CB - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 ASP 1 165 CB - CG - OD1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP 1 165 CB - CG - OD2 ANGL. DEV. = 11.7 DEGREES
REMARK 500 SER 1 170 CA - CB - OG ANGL. DEV. = 30.0 DEGREES
REMARK 500 ASN 1 173 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 SER 1 175 CB - CA - C ANGL. DEV. = 16.0 DEGREES
REMARK 500 VAL 1 176 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP 1 182 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TYR 1 197 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 TYR 1 197 N - CA - CB ANGL. DEV. = -23.3 DEGREES
REMARK 500 TYR 1 197 CA - CB - CG ANGL. DEV. = 20.1 DEGREES
REMARK 500 ASP 1 208 CB - CG - OD1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 MET 1 224 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG 1 242 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG 1 246 CD - NE - CZ ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG 1 246 NE - CZ - NH1 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG 1 246 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 GLU 1 251 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 167 ANGLE DEVIATIONS.
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 HIS 1 78 134.95 -171.82
REMARK 500 ILE 1 104 125.25 -27.70
REMARK 500 SER 1 139 102.44 24.61
REMARK 500 PRO 1 154 171.64 -58.81
REMARK 500 PRO 1 155 96.60 -67.85
REMARK 500 ASP 1 165 168.76 -46.13
REMARK 500 ALA 1 194 -155.62 -93.95
REMARK 500 HIS 1 249 52.31 70.90
REMARK 500 ILE 1 254 89.12 56.72
REMARK 500 ASN 1 274 78.18 42.79
REMARK 500 ASP 1 285 171.37 -59.45
REMARK 500 GLU 2 27 54.19 -148.92
REMARK 500 ASN 2 30 -157.54 58.08
REMARK 500 SER 2 48 -60.14 -131.62
REMARK 500 ASP 2 57 -126.64 58.08
REMARK 500 ALA 2 114 -134.64 -145.97
REMARK 500 LEU 2 170 -8.63 -57.39
REMARK 500 ASN 2 174 16.35 -156.09
REMARK 500 PRO 2 227 150.31 -48.89
REMARK 500 PRO 2 236 42.45 -79.60
REMARK 500 ARG 2 255 -134.24 -173.03
REMARK 500 LYS 2 257 100.70 104.05
REMARK 500 LEU 3 25 75.33 -106.43
REMARK 500 ILE 3 47 0.39 -68.13
REMARK 500 ASN 3 56 34.86 -81.15
REMARK 500 ASN 3 57 -7.17 -31.01
REMARK 500 ASN 3 74 23.12 48.10
REMARK 500 ASN 3 77 -14.35 38.75
REMARK 500 LEU 3 85 61.06 -112.41
REMARK 500 THR 3 193 -82.97 -124.71
REMARK 500 SER 3 194 158.46 173.32
REMARK 500 LEU 3 221 82.57 62.23
REMARK 500 SER 4 46 -74.50 -96.88
REMARK 500 MET 4 47 94.73 60.34
REMARK 500 GLU 4 54 58.67 -143.73
REMARK 500 PRO 4 55 38.49 -82.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG 1 259 0.12 SIDE CHAIN
REMARK 500 ARG 1 268 0.12 SIDE CHAIN
REMARK 500 ARG 2 12 0.10 SIDE CHAIN
REMARK 500 ARG 2 255 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SDZ 1 682
DBREF 1HRV 1 1 289 UNP P03303 POLG_HRV14 567 855
DBREF 1HRV 2 1 262 UNP P03303 POLG_HRV14 69 330
DBREF 1HRV 3 1 236 UNP P03303 POLG_HRV14 331 566
DBREF 1HRV 4 1 68 UNP P03303 POLG_HRV14 1 68
SEQADV 1HRV LEU 2 170 UNP P03303 ILE 239 CONFLICT
SEQRES 1 1 289 GLY LEU GLY ASP GLU LEU GLU GLU VAL ILE VAL GLU LYS
SEQRES 2 1 289 THR LYS GLN THR VAL ALA SER ILE SER SER GLY PRO LYS
SEQRES 3 1 289 HIS THR GLN LYS VAL PRO ILE LEU THR ALA ASN GLU THR
SEQRES 4 1 289 GLY ALA THR MET PRO VAL LEU PRO SER ASP SER ILE GLU
SEQRES 5 1 289 THR ARG THR THR TYR MET HIS PHE ASN GLY SER GLU THR
SEQRES 6 1 289 ASP VAL GLU CYS PHE LEU GLY ARG ALA ALA CYS VAL HIS
SEQRES 7 1 289 VAL THR GLU ILE GLN ASN LYS ASP ALA THR GLY ILE ASP
SEQRES 8 1 289 ASN HIS ARG GLU ALA LYS LEU PHE ASN ASP TRP LYS ILE
SEQRES 9 1 289 ASN LEU SER SER LEU VAL GLN LEU ARG LYS LYS LEU GLU
SEQRES 10 1 289 LEU PHE THR TYR VAL ARG PHE ASP SER GLU TYR THR ILE
SEQRES 11 1 289 LEU ALA THR ALA SER GLN PRO ASP SER ALA ASN TYR SER
SEQRES 12 1 289 SER ASN LEU VAL VAL GLN ALA MET TYR VAL PRO PRO GLY
SEQRES 13 1 289 ALA PRO ASN PRO LYS GLU TRP ASP ASP TYR THR TRP GLN
SEQRES 14 1 289 SER ALA SER ASN PRO SER VAL PHE PHE LYS VAL GLY ASP
SEQRES 15 1 289 THR SER ARG PHE SER VAL PRO TYR VAL GLY LEU ALA SER
SEQRES 16 1 289 ALA TYR ASN CYS PHE TYR ASP GLY TYR SER HIS ASP ASP
SEQRES 17 1 289 ALA GLU THR GLN TYR GLY ILE THR VAL LEU ASN HIS MET
SEQRES 18 1 289 GLY SER MET ALA PHE ARG ILE VAL ASN GLU HIS ASP GLU
SEQRES 19 1 289 HIS LYS THR LEU VAL LYS ILE ARG VAL TYR HIS ARG ALA
SEQRES 20 1 289 LYS HIS VAL GLU ALA TRP ILE PRO ARG ALA PRO ARG ALA
SEQRES 21 1 289 LEU PRO TYR THR SER ILE GLY ARG THR ASN TYR PRO LYS
SEQRES 22 1 289 ASN THR GLU PRO VAL ILE LYS LYS ARG LYS GLY ASP ILE
SEQRES 23 1 289 LYS SER TYR
SEQRES 1 2 262 SER PRO ASN VAL GLU ALA CYS GLY TYR SER ASP ARG VAL
SEQRES 2 2 262 GLN GLN ILE THR LEU GLY ASN SER THR ILE THR THR GLN
SEQRES 3 2 262 GLU ALA ALA ASN ALA VAL VAL CYS TYR ALA GLU TRP PRO
SEQRES 4 2 262 GLU TYR LEU PRO ASP VAL ASP ALA SER ASP VAL ASN LYS
SEQRES 5 2 262 THR SER LYS PRO ASP THR SER VAL CYS ARG PHE TYR THR
SEQRES 6 2 262 LEU ASP SER LYS THR TRP THR THR GLY SER LYS GLY TRP
SEQRES 7 2 262 CYS TRP LYS LEU PRO ASP ALA LEU LYS ASP MET GLY VAL
SEQRES 8 2 262 PHE GLY GLN ASN MET PHE PHE HIS SER LEU GLY ARG SER
SEQRES 9 2 262 GLY TYR THR VAL HIS VAL GLN CYS ASN ALA THR LYS PHE
SEQRES 10 2 262 HIS SER GLY CYS LEU LEU VAL VAL VAL ILE PRO GLU HIS
SEQRES 11 2 262 GLN LEU ALA SER HIS GLU GLY GLY ASN VAL SER VAL LYS
SEQRES 12 2 262 TYR THR PHE THR HIS PRO GLY GLU ARG GLY ILE ASP LEU
SEQRES 13 2 262 SER SER ALA ASN GLU VAL GLY GLY PRO VAL LYS ASP VAL
SEQRES 14 2 262 LEU TYR ASN MET ASN GLY THR LEU LEU GLY ASN LEU LEU
SEQRES 15 2 262 ILE PHE PRO HIS GLN PHE ILE ASN LEU ARG THR ASN ASN
SEQRES 16 2 262 THR ALA THR ILE VAL ILE PRO TYR ILE ASN SER VAL PRO
SEQRES 17 2 262 ILE ASP SER MET THR ARG HIS ASN ASN VAL SER LEU MET
SEQRES 18 2 262 VAL ILE PRO ILE ALA PRO LEU THR VAL PRO THR GLY ALA
SEQRES 19 2 262 THR PRO SER LEU PRO ILE THR VAL THR ILE ALA PRO MET
SEQRES 20 2 262 CYS THR GLU PHE SER GLY ILE ARG SER LYS SER ILE VAL
SEQRES 21 2 262 PRO GLN
SEQRES 1 3 236 GLY LEU PRO THR THR THR LEU PRO GLY SER GLY GLN PHE
SEQRES 2 3 236 LEU THR THR ASP ASP ARG GLN SER PRO SER ALA LEU PRO
SEQRES 3 3 236 ASN TYR GLU PRO THR PRO ARG ILE HIS ILE PRO GLY LYS
SEQRES 4 3 236 VAL HIS ASN LEU LEU GLU ILE ILE GLN VAL ASP THR LEU
SEQRES 5 3 236 ILE PRO MET ASN ASN THR HIS THR LYS ASP GLU VAL ASN
SEQRES 6 3 236 SER TYR LEU ILE PRO LEU ASN ALA ASN ARG GLN ASN GLU
SEQRES 7 3 236 GLN VAL PHE GLY THR ASN LEU PHE ILE GLY ASP GLY VAL
SEQRES 8 3 236 PHE LYS THR THR LEU LEU GLY GLU ILE VAL GLN TYR TYR
SEQRES 9 3 236 THR HIS TRP SER GLY SER LEU ARG PHE SER LEU MET TYR
SEQRES 10 3 236 THR GLY PRO ALA LEU SER SER ALA LYS LEU ILE LEU ALA
SEQRES 11 3 236 TYR THR PRO PRO GLY ALA ARG GLY PRO GLN ASP ARG ARG
SEQRES 12 3 236 GLU ALA MET LEU GLY THR HIS VAL VAL TRP ASP ILE GLY
SEQRES 13 3 236 LEU GLN SER THR ILE VAL MET THR ILE PRO TRP THR SER
SEQRES 14 3 236 GLY VAL GLN PHE ARG TYR THR ASP PRO ASP THR TYR THR
SEQRES 15 3 236 SER ALA GLY PHE LEU SER CYS TRP TYR GLN THR SER LEU
SEQRES 16 3 236 ILE LEU PRO PRO GLU THR THR GLY GLN VAL TYR LEU LEU
SEQRES 17 3 236 SER PHE ILE SER ALA CYS PRO ASP PHE LYS LEU ARG LEU
SEQRES 18 3 236 MET LYS ASP THR GLN THR ILE SER GLN THR VAL ALA LEU
SEQRES 19 3 236 THR GLU
SEQRES 1 4 68 GLY ALA GLN VAL SER THR GLN LYS SER GLY SER HIS GLU
SEQRES 2 4 68 ASN GLN ASN ILE LEU THR ASN GLY SER ASN GLN THR PHE
SEQRES 3 4 68 THR VAL ILE ASN TYR TYR LYS ASP ALA ALA SER THR SER
SEQRES 4 4 68 SER ALA GLY GLN SER LEU SER MET ASP PRO SER LYS PHE
SEQRES 5 4 68 THR GLU PRO VAL LYS ASP LEU MET LEU LYS GLY ALA PRO
SEQRES 6 4 68 ALA LEU ASN
HET SDZ 1 682 58
HETNAM SDZ 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-
HETNAM 2 SDZ PYRIDYL)-PIPERAZINE
FORMUL 5 SDZ C24 H33 N3 O2
HELIX 1 1 ASN 1 37 THR 1 39 5 3
HELIX 2 2 PRO 1 47 ASP 1 49 5 3
HELIX 3 3 SER 1 63 THR 1 65 5 3
HELIX 4 4 VAL 1 67 PHE 1 70 1 4
HELIX 5 5 VAL 1 110 LEU 1 118 1 9
HELIX 6 6 TYR 1 166 GLN 1 169 5 4
HELIX 7 7 CYS 2 34 ALA 2 36 5 3
HELIX 8 8 ASP 2 44 ASP 2 46 5 3
HELIX 9 9 ASP 2 57 SER 2 59 5 3
HELIX 10 10 ASP 2 84 LEU 2 86 5 3
HELIX 11 11 GLY 2 90 PHE 2 98 1 9
HELIX 12 12 TYR 2 144 THR 2 147 5 4
HELIX 13 13 GLY 2 150 ARG 2 152 5 3
HELIX 14 14 VAL 2 169 TYR 2 171 5 3
HELIX 15 15 LEU 2 178 ILE 2 183 5 6
HELIX 16 16 LEU 3 43 GLN 3 48 1 6
HELIX 17 17 VAL 3 64 SER 3 66 5 3
HELIX 18 18 GLY 3 90 THR 3 94 5 5
HELIX 19 19 LEU 3 96 TYR 3 103 1 8
HELIX 20 20 ARG 3 142 LEU 3 147 1 6
HELIX 21 21 ALA 4 35 SER 4 37 5 3
HELIX 22 22 PRO 4 49 THR 4 53 5 5
SHEET 1 A 4 PHE 1 99 TRP 1 102 0
SHEET 2 A 4 SER 1 223 ILE 1 228 -1 N PHE 1 226 O ASN 1 100
SHEET 3 A 4 VAL 1 147 VAL 1 153 -1 N VAL 1 153 O SER 1 223
SHEET 4 A 4 SER 1 175 LYS 1 179 -1 N PHE 1 178 O VAL 1 148
SHEET 1 B 2 TYR 1 121 ARG 1 123 0
SHEET 2 B 2 GLU 1 251 TRP 1 253 -1 N TRP 1 253 O TYR 1 121
SHEET 1 C 4 THR 1 183 VAL 1 188 0
SHEET 2 C 4 ASP 1 125 SER 1 135 -1 N ILE 1 130 O SER 1 184
SHEET 3 C 4 THR 1 237 LYS 1 248 -1 N LYS 1 248 O ASP 1 125
SHEET 4 C 4 ALA 1 75 ASN 1 84 -1 N ASN 1 84 O THR 1 237
SHEET 1 D 2 GLN 2 14 LEU 2 18 0
SHEET 2 D 2 SER 2 21 THR 2 25 -1 N THR 2 25 O GLN 2 14
SHEET 1 E 4 PHE 2 63 THR 2 65 0
SHEET 2 E 4 THR 2 241 MET 2 247 -1 N ILE 2 244 O TYR 2 64
SHEET 3 E 4 GLY 2 105 GLN 2 111 -1 N GLN 2 111 O THR 2 241
SHEET 4 E 4 THR 2 196 ILE 2 201 -1 N ILE 2 201 O TYR 2 106
SHEET 1 F 2 LYS 2 69 THR 2 72 0
SHEET 2 F 2 SER 2 237 ILE 2 240 -1 N ILE 2 240 O LYS 2 69
SHEET 1 G 4 TRP 2 78 LEU 2 82 0
SHEET 2 G 4 VAL 2 218 ALA 2 226 -1 N VAL 2 222 O TRP 2 78
SHEET 3 G 4 CYS 2 121 PRO 2 128 -1 N ILE 2 127 O SER 2 219
SHEET 4 G 4 HIS 2 186 ASN 2 190 -1 N ILE 2 189 O LEU 2 122
SHEET 1 H 2 LEU 2 101 ARG 2 103 0
SHEET 2 H 2 GLU 2 250 SER 2 252 -1 N SER 2 252 O LEU 2 101
SHEET 1 I 4 LEU 3 68 ASN 3 72 0
SHEET 2 I 4 GLN 3 204 ALA 3 213 -1 N LEU 3 207 O ILE 3 69
SHEET 3 I 4 LEU 3 111 TYR 3 117 -1 N MET 3 116 O LEU 3 208
SHEET 4 I 4 THR 3 160 ILE 3 165 -1 N ILE 3 165 O LEU 3 111
SHEET 1 J 2 HIS 3 106 SER 3 108 0
SHEET 2 J 2 LYS 3 218 ARG 3 220 -1 N ARG 3 220 O HIS 3 106
SHEET 1 K 4 THR 3 149 ASP 3 154 0
SHEET 2 K 4 LYS 3 126 THR 3 132 -1 N TYR 3 131 O THR 3 149
SHEET 3 K 4 PHE 3 186 TYR 3 191 -1 N TRP 3 190 O ILE 3 128
SHEET 4 K 4 GLN 3 79 ASN 3 84 -1 N THR 3 83 O LEU 3 187
CISPEP 1 LEU 2 82 PRO 2 83 0 2.69
SITE 1 AC1 15 ILE 1 104 LEU 1 106 SER 1 107 LEU 1 116
SITE 2 AC1 15 PHE 1 124 SER 1 126 TYR 1 128 TYR 1 152
SITE 3 AC1 15 PRO 1 174 PHE 1 186 VAL 1 188 TYR 1 197
SITE 4 AC1 15 ILE 1 215 MET 1 224 ALA 3 24
CRYST1 445.100 445.100 445.100 90.00 90.00 90.00 P 21 3 240
ORIGX1 0.996348 -0.058524 0.062176 -0.17359
ORIGX2 0.062176 0.996348 -0.058524 -0.17359
ORIGX3 -0.058524 0.062176 0.996348 -0.17359
SCALE1 0.002247 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002247 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002247 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 0.464282 -0.829905 0.309355 0.18336
MTRIX2 2 0.844397 0.309355 -0.437372 0.04923
MTRIX3 2 0.267276 0.464282 0.844397 -0.09998
MTRIX1 3 -0.402527 -0.498417 0.767824 0.19670
MTRIX2 3 0.536358 -0.808132 -0.243400 0.26302
MTRIX3 3 0.741817 0.313853 0.592625 -0.11254
MTRIX1 4 -0.402527 0.536358 0.741817 0.02159
MTRIX2 4 -0.498417 -0.808132 0.313853 0.34591
MTRIX3 4 0.767824 -0.243400 0.592625 -0.02032
MTRIX1 5 0.464282 0.844397 0.267276 -0.09998
MTRIX2 5 -0.829905 0.309355 0.464282 0.18336
MTRIX3 5 0.309355 -0.437372 0.844397 0.04923
MTRIX1 6 -0.630565 -0.701509 0.332074 0.34718
MTRIX2 6 -0.701509 0.332074 -0.630565 0.34718
MTRIX3 6 0.332074 -0.630565 -0.701509 0.34718
MTRIX1 7 -0.796357 0.460470 0.392154 0.16382
MTRIX2 7 -0.213831 0.392154 -0.894702 0.29795
MTRIX3 7 -0.565768 -0.796357 -0.213831 0.44716
MTRIX1 8 0.123898 0.985418 -0.116620 0.00127
MTRIX2 8 -0.007277 -0.116620 -0.993150 0.36750
MTRIX3 8 -0.992269 0.123898 -0.007277 0.32559
MTRIX1 9 0.858438 0.147876 -0.491140 0.08416
MTRIX2 9 -0.367298 -0.491140 -0.789857 0.45972
MTRIX3 9 -0.358019 0.858438 -0.367298 0.15048
MTRIX1 10 0.392154 -0.894702 -0.213831 0.29795
MTRIX2 10 -0.796357 -0.213831 -0.565768 0.44716
MTRIX3 10 0.460470 0.392154 -0.796357 0.16382
MTRIX1 11 -0.491140 -0.789857 -0.367298 0.45972
MTRIX2 11 0.858438 -0.367298 -0.358019 0.15048
MTRIX3 11 0.147876 -0.491140 0.858438 0.08416
MTRIX1 12 -0.993150 -0.007277 -0.116620 0.36750
MTRIX2 12 -0.007277 -0.992269 0.123898 0.32559
MTRIX3 12 -0.116620 0.123898 0.985418 0.00127
MTRIX1 13 -0.498417 0.767824 -0.402527 0.19670
MTRIX2 13 -0.808132 -0.243400 0.536358 0.26302
MTRIX3 13 0.313853 0.592625 0.741817 -0.11254
MTRIX1 14 0.309355 0.464282 -0.829905 0.18336
MTRIX2 14 -0.437372 0.844397 0.309355 0.04923
MTRIX3 14 0.844397 0.267276 0.464282 -0.09998
MTRIX1 15 0.313853 -0.498417 -0.808132 0.34591
MTRIX2 15 0.592625 0.767824 -0.243400 -0.02032
MTRIX3 15 0.741817 -0.402527 0.536358 0.02159
MTRIX1 16 -0.243400 0.592625 0.767824 -0.02032
MTRIX2 16 0.536358 0.741817 -0.402527 0.02159
MTRIX3 16 -0.808132 0.313853 -0.498417 0.34591
MTRIX1 17 0.592625 0.741817 0.313853 -0.11254
MTRIX2 17 0.767824 -0.402527 -0.498417 0.19670
MTRIX3 17 -0.243400 0.536358 -0.808132 0.26302
MTRIX1 18 0.985418 -0.116620 0.123898 0.00127
MTRIX2 18 -0.116620 -0.993150 -0.007277 0.36750
MTRIX3 18 0.123898 -0.007277 -0.992269 0.32559
MTRIX1 19 0.392154 -0.796357 0.460470 0.16382
MTRIX2 19 -0.894702 -0.213831 0.392154 0.29795
MTRIX3 19 -0.213831 -0.565768 -0.796357 0.44716
MTRIX1 20 -0.367298 -0.358019 0.858438 0.15048
MTRIX2 20 -0.491140 0.858438 0.147876 0.08416
MTRIX3 20 -0.789857 -0.367298 -0.491140 0.45972
(ATOM LINES ARE NOT SHOWN.)
END