HEADER VIRUS 15-FEB-01 1H8T
TITLE ECHOVIRUS 11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECHOVIRUS 11 COAT PROTEIN VP1;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ECHOVIRUS 11 COAT PROTEIN VP2;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: ECHOVIRUS 11 COAT PROTEIN VP3;
COMPND 9 CHAIN: C;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: ECHOVIRUS 11 COAT PROTEIN VP4;
COMPND 12 CHAIN: D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECHOVIRUS 11;
SOURCE 3 ORGANISM_TAXID: 12078;
SOURCE 4 STRAIN: 207;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ECHOVIRUS 11;
SOURCE 7 ORGANISM_TAXID: 12078;
SOURCE 8 STRAIN: 207;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ECHOVIRUS 11;
SOURCE 11 ORGANISM_TAXID: 12078;
SOURCE 12 STRAIN: 207;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: ECHOVIRUS 11;
SOURCE 15 ORGANISM_TAXID: 12078;
SOURCE 16 STRAIN: 207
KEYWDS VIRUS, ECHOVIRUS COAT PROTEIN, ECHOVIRUS, ICOSAHEDRAL VIRUS
EXPDTA X-RAY DIFFRACTION
AUTHOR A.STUART,T.MCKEE,P.A.WILLIAMS,C.HARLEY,D.I.STUART,T.D.K.BROWN,S.M.LEA
REVDAT 5 13-DEC-23 1H8T 1 REMARK
REVDAT 4 15-NOV-23 1H8T 1 REMARK ATOM
REVDAT 3 11-JAN-12 1H8T 1 REMARK VERSN MTRIX3 MTRIX1
REVDAT 3 2 1 MTRIX2
REVDAT 2 24-FEB-09 1H8T 1 VERSN
REVDAT 1 11-JUL-02 1H8T 0
JRNL AUTH A.STUART,T.MCKEE,P.A.WILLIAMS,C.HARLEY,S.SHEN,D.I.STUART,
JRNL AUTH 2 T.D.K.BROWN,S.M.LEA
JRNL TITL DETERMINATION OF THE STRUCTURE OF A DECAY ACCELERATING
JRNL TITL 2 FACTOR-BINDING CLINICAL ISOLATE OF ECHOVIRUS 11 ALLOWS
JRNL TITL 3 MAPPING OF MUTANTS WITH ALTERED RECEPTOR REQUIREMENTS FOR
JRNL TITL 4 INFECTION
JRNL REF J.VIROL. V. 76 7694 2002
JRNL REFN ISSN 0022-538X
JRNL PMID 12097583
JRNL DOI 10.1128/JVI.76.15.7694-7704.2002
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 71.3
REMARK 3 NUMBER OF REFLECTIONS : 402349
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2029
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 34536
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE : 0.3883
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
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 : 6534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.17800
REMARK 3 B22 (A**2) : 1.17800
REMARK 3 B33 (A**2) : -2.35700
REMARK 3 B12 (A**2) : -1.50900
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 2.165
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 3.858 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.447 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.667 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.153 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 30.53
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MYR.PAR
REMARK 3 PARAMETER FILE 4 : PLM-MOD.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED WITH STRICT NCS DISORDERED
REMARK 3 REGIONS ARE NOT MODELLED
REMARK 4
REMARK 4 1H8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1290005893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 287.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 75
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 411040
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.22000
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) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1D4M
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED AT TWO SYNCHROTRONS FOR FINAL NATIVE
REMARK 200 SET AS ABOVE AND ALSO SRS STAION 7.2
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: 2.0M AMMONIUM SULPHATE, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 150.42500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.84791
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 492.20667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 150.42500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 86.84791
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 492.20667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 150.42500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 86.84791
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 492.20667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 150.42500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 86.84791
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 492.20667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 150.42500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 86.84791
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 492.20667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 150.42500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 86.84791
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 492.20667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 173.69583
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 984.41333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 173.69583
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 984.41333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 173.69583
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 984.41333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 173.69583
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 984.41333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 173.69583
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 984.41333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 173.69583
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 984.41333
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: A, B, C, D
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 0.507091 -0.649919 0.566095 -208.96134
REMARK 350 BIOMT2 2 0.861614 0.365580 -0.352096 129.96817
REMARK 350 BIOMT3 2 0.021880 0.666301 0.745362 93.99385
REMARK 350 BIOMT1 3 -0.290451 -0.189976 0.937842 -346.18311
REMARK 350 BIOMT2 3 0.744203 -0.660932 0.096598 -35.65695
REMARK 350 BIOMT3 3 0.601498 0.726001 0.333349 246.07907
REMARK 350 BIOMT1 4 -0.290451 0.744203 0.601498 -222.02949
REMARK 350 BIOMT2 4 -0.189976 -0.660932 0.726001 -267.98708
REMARK 350 BIOMT3 4 0.937842 0.096598 0.333349 246.07905
REMARK 350 BIOMT1 5 0.507091 0.861614 0.021880 -8.07656
REMARK 350 BIOMT2 5 -0.649919 0.365580 0.666301 -245.94988
REMARK 350 BIOMT3 5 0.566095 -0.352096 0.745362 93.99383
REMARK 350 BIOMT1 6 -0.816394 -0.114204 0.566090 -208.95555
REMARK 350 BIOMT2 6 -0.114204 -0.928965 -0.352111 129.97974
REMARK 350 BIOMT3 6 0.566090 -0.352111 0.745359 93.99491
REMARK 350 BIOMT1 7 -0.500000 0.866025 -0.000005 0.00545
REMARK 350 BIOMT2 7 -0.866025 -0.500000 -0.000016 0.01179
REMARK 350 BIOMT3 7 -0.000016 -0.000004 1.000000 0.00000
REMARK 350 BIOMT1 8 0.492634 0.641558 -0.587975 217.04142
REMARK 350 BIOMT2 8 -0.869962 0.380045 -0.314217 115.99204
REMARK 350 BIOMT3 8 0.021869 0.666310 0.745354 93.99669
REMARK 350 BIOMT1 9 0.789721 -0.477399 -0.385266 142.21604
REMARK 350 BIOMT2 9 -0.120573 0.494979 -0.860499 317.63974
REMARK 350 BIOMT3 9 0.601500 0.726007 0.333334 246.08475
REMARK 350 BIOMT1 10 -0.019303 -0.944486 0.327985 -121.06457
REMARK 350 BIOMT2 10 0.346511 -0.314034 -0.883919 326.28462
REMARK 350 BIOMT3 10 0.937847 0.096588 0.333337 246.08365
REMARK 350 BIOMT1 11 -0.442118 0.896957 0.000010 -0.00012
REMARK 350 BIOMT2 11 0.896957 0.442118 0.000016 -0.00794
REMARK 350 BIOMT3 11 0.000010 0.000016 -1.000000 738.26552
REMARK 350 BIOMT1 12 0.548637 0.615257 -0.566088 208.96219
REMARK 350 BIOMT2 12 0.835775 -0.421309 0.352107 -129.97455
REMARK 350 BIOMT3 12 -0.021862 -0.666301 -0.745362 644.27167
REMARK 350 BIOMT1 13 0.795938 -0.508829 -0.327989 121.07326
REMARK 350 BIOMT2 13 0.068512 -0.462599 0.883917 -326.28002
REMARK 350 BIOMT3 13 -0.601489 -0.726014 -0.333339 492.18252
REMARK 350 BIOMT1 14 -0.041977 -0.921852 0.385262 -142.20740
REMARK 350 BIOMT2 14 -0.344500 0.375310 0.860501 -317.63686
REMARK 350 BIOMT3 14 -0.937848 -0.096601 -0.333332 492.18011
REMARK 350 BIOMT1 15 -0.807138 -0.053029 0.587977 -217.03487
REMARK 350 BIOMT2 15 0.167507 0.934455 0.314221 -115.98963
REMARK 350 BIOMT3 15 -0.566101 0.352110 -0.745351 644.26777
REMARK 350 BIOMT1 16 0.258512 -0.782753 -0.566099 208.97001
REMARK 350 BIOMT2 16 -0.782753 -0.513153 0.352095 -129.96423
REMARK 350 BIOMT3 16 -0.566099 0.352095 -0.745359 644.27061
REMARK 350 BIOMT1 17 -0.555729 -0.831364 -0.000002 0.00804
REMARK 350 BIOMT2 17 -0.831364 0.555729 0.000005 0.00216
REMARK 350 BIOMT3 17 -0.000002 0.000005 -1.000000 738.26552
REMARK 350 BIOMT1 18 -0.998120 0.057246 -0.021878 8.08277
REMARK 350 BIOMT2 18 0.057246 0.743485 -0.666297 245.95250
REMARK 350 BIOMT3 18 -0.021878 -0.666297 -0.745365 644.27276
REMARK 350 BIOMT1 19 -0.457293 0.655048 -0.601494 222.03520
REMARK 350 BIOMT2 19 0.655048 -0.209356 -0.726004 267.99178
REMARK 350 BIOMT3 19 -0.601494 -0.726004 -0.333351 492.18713
REMARK 350 BIOMT1 20 0.319349 0.135900 -0.937842 346.19034
REMARK 350 BIOMT2 20 0.135900 -0.986002 -0.096603 35.66246
REMARK 350 BIOMT3 20 -0.937842 -0.096603 -0.333348 492.18580
REMARK 350 BIOMT1 21 0.819330 -0.152792 0.552588 -203.97739
REMARK 350 BIOMT2 21 0.424571 -0.486004 -0.763898 281.98107
REMARK 350 BIOMT3 21 0.385277 0.860497 -0.333326 492.17138
REMARK 350 BIOMT1 22 0.295918 -0.220166 0.929494 -343.10381
REMARK 350 BIOMT2 22 -0.220166 -0.962596 -0.157913 58.29547
REMARK 350 BIOMT3 22 0.929494 -0.157913 -0.333323 492.17002
REMARK 350 BIOMT1 23 -0.019303 0.346511 0.937847 -346.18709
REMARK 350 BIOMT2 23 -0.944486 -0.314034 0.096588 -35.64811
REMARK 350 BIOMT3 23 0.327985 -0.883919 0.333337 246.08770
REMARK 350 BIOMT1 24 0.309291 0.764111 0.566103 -208.96624
REMARK 350 BIOMT2 24 -0.747404 0.563391 -0.352105 129.97718
REMARK 350 BIOMT3 24 -0.587985 -0.314204 0.745351 94.00182
REMARK 350 BIOMT1 25 0.827595 0.455525 0.328000 -121.07581
REMARK 350 BIOMT2 25 0.098720 0.457108 -0.883915 326.28280
REMARK 350 BIOMT3 25 -0.552577 0.763904 0.333331 246.08990
REMARK 350 BIOMT1 26 -0.338633 -0.146205 0.929490 -343.10025
REMARK 350 BIOMT2 26 -0.723549 0.671969 -0.157906 58.29149
REMARK 350 BIOMT3 26 -0.601502 -0.726004 -0.333337 492.18186
REMARK 350 BIOMT1 27 -0.277352 0.785954 0.552587 -203.97472
REMARK 350 BIOMT2 27 0.208618 0.610694 -0.763892 281.97765
REMARK 350 BIOMT3 27 -0.937845 -0.096588 -0.333342 492.18363
REMARK 350 BIOMT1 28 0.548637 0.835775 -0.021862 8.06993
REMARK 350 BIOMT2 28 0.615257 -0.421309 -0.666301 245.95412
REMARK 350 BIOMT3 28 -0.566088 0.352107 -0.745362 644.27170
REMARK 350 BIOMT1 29 0.997846 -0.065593 0.000013 -0.00479
REMARK 350 BIOMT2 29 -0.065593 -0.997846 0.000000 0.00418
REMARK 350 BIOMT3 29 0.000013 0.000000 -1.000000 738.26552
REMARK 350 BIOMT1 30 0.449484 -0.672490 0.587981 -217.03989
REMARK 350 BIOMT2 30 -0.893021 -0.322163 0.314205 -115.97770
REMARK 350 BIOMT3 30 -0.021874 -0.666309 -0.745354 644.26883
REMARK 350 BIOMT1 31 -0.499282 0.667360 -0.552582 203.98037
REMARK 350 BIOMT2 31 -0.623642 0.165939 0.763895 -281.97468
REMARK 350 BIOMT3 31 0.601488 0.726013 0.333343 246.08124
REMARK 350 BIOMT1 32 0.309735 0.200281 -0.929490 343.10736
REMARK 350 BIOMT2 32 -0.156554 0.974964 0.157911 -58.28942
REMARK 350 BIOMT3 32 0.937846 0.096605 0.333335 246.08432
REMARK 350 BIOMT1 33 0.309291 -0.747404 -0.587985 217.04855
REMARK 350 BIOMT2 33 0.764111 0.563391 -0.314204 115.98124
REMARK 350 BIOMT3 33 0.566103 -0.352105 0.745351 93.99776
REMARK 350 BIOMT1 34 -0.500000 -0.866025 -0.000016 0.01293
REMARK 350 BIOMT2 34 0.866025 -0.500000 -0.000004 0.00117
REMARK 350 BIOMT3 34 -0.000005 -0.000016 1.000000 0.00000
REMARK 350 BIOMT1 35 -0.999726 0.008347 0.021864 -8.06364
REMARK 350 BIOMT2 35 0.008347 -0.745639 0.666298 -245.94911
REMARK 350 BIOMT3 35 0.021864 0.666298 0.745365 93.99276
REMARK 350 BIOMT1 36 0.018585 -0.368364 -0.929496 343.11160
REMARK 350 BIOMT2 36 0.922620 -0.351905 0.157909 -58.29030
REMARK 350 BIOMT3 36 -0.385262 -0.860506 0.333320 246.09657
REMARK 350 BIOMT1 37 -0.328301 -0.766069 -0.552591 203.98552
REMARK 350 BIOMT2 37 0.168101 -0.623062 0.763895 -281.97612
REMARK 350 BIOMT3 37 -0.929495 0.157896 0.333329 246.09307
REMARK 350 BIOMT1 38 -0.838626 -0.434883 -0.328000 121.08295
REMARK 350 BIOMT2 38 -0.434883 0.171952 0.883917 -326.27967
REMARK 350 BIOMT3 38 -0.328000 0.883917 -0.333326 492.17389
REMARK 350 BIOMT1 39 -0.807138 0.167507 -0.566101 208.97243
REMARK 350 BIOMT2 39 -0.053029 0.934455 0.352110 -129.97496
REMARK 350 BIOMT3 39 0.587977 0.314221 -0.745351 644.26370
REMARK 350 BIOMT1 40 -0.277352 0.208618 -0.937845 346.19368
REMARK 350 BIOMT2 40 0.785954 0.610694 -0.096588 35.65158
REMARK 350 BIOMT3 40 0.552587 -0.763892 -0.333342 492.17955
REMARK 350 BIOMT1 41 0.819330 0.424571 0.385277 -142.21850
REMARK 350 BIOMT2 41 -0.152792 -0.486004 0.860497 -317.63432
REMARK 350 BIOMT3 41 0.552588 -0.763898 -0.333326 492.17386
REMARK 350 BIOMT1 42 0.789721 -0.120573 0.601500 -222.03238
REMARK 350 BIOMT2 42 -0.477399 0.494979 0.726007 -267.99032
REMARK 350 BIOMT3 42 -0.385266 -0.860499 0.333334 246.09129
REMARK 350 BIOMT1 43 0.309735 -0.156554 0.937846 -346.18694
REMARK 350 BIOMT2 43 0.200281 0.974964 0.096605 -35.66069
REMARK 350 BIOMT3 43 -0.929490 0.157911 0.333335 246.09090
REMARK 350 BIOMT1 44 0.042695 0.366352 0.929496 -343.10480
REMARK 350 BIOMT2 44 0.943718 0.290629 -0.157897 58.28292
REMARK 350 BIOMT3 44 -0.327985 0.883924 -0.333324 492.17322
REMARK 350 BIOMT1 45 0.357642 0.725507 0.587990 -217.04537
REMARK 350 BIOMT2 45 0.725507 -0.612298 0.314214 -115.98637
REMARK 350 BIOMT3 45 0.587990 0.314214 -0.745344 644.26086
REMARK 350 BIOMT1 46 -0.499282 -0.623642 0.601488 -222.02230
REMARK 350 BIOMT2 46 0.667360 0.165939 0.726013 -267.99591
REMARK 350 BIOMT3 46 -0.552582 0.763895 0.333343 246.08530
REMARK 350 BIOMT1 47 -0.777360 0.497273 0.385266 -142.20903
REMARK 350 BIOMT2 47 0.497273 0.110677 0.860506 -317.64088
REMARK 350 BIOMT3 47 0.385266 0.860506 -0.333317 492.16787
REMARK 350 BIOMT1 48 0.042695 0.943718 -0.327985 121.07160
REMARK 350 BIOMT2 48 0.366352 0.290629 0.883924 -326.28510
REMARK 350 BIOMT3 48 0.929496 -0.157897 -0.333324 492.17069
REMARK 350 BIOMT1 49 0.827595 0.098720 -0.552577 203.97470
REMARK 350 BIOMT2 49 0.455525 0.457108 0.763904 -281.98255
REMARK 350 BIOMT3 49 0.328000 -0.883915 0.333331 246.08987
REMARK 350 BIOMT1 50 0.492634 -0.869962 0.021869 -8.06899
REMARK 350 BIOMT2 50 0.641558 0.380045 0.666310 -245.95785
REMARK 350 BIOMT3 50 -0.587975 -0.314217 0.745354 94.00073
REMARK 350 BIOMT1 51 0.018585 0.922620 -0.385262 142.21471
REMARK 350 BIOMT2 51 -0.368364 -0.351905 -0.860506 317.64492
REMARK 350 BIOMT3 51 -0.929496 0.157909 0.333320 246.09659
REMARK 350 BIOMT1 52 0.795938 0.068512 -0.601489 222.03005
REMARK 350 BIOMT2 52 -0.508829 -0.462599 -0.726014 268.00001
REMARK 350 BIOMT3 52 -0.327989 0.883917 -0.333339 492.17850
REMARK 350 BIOMT1 53 0.449484 -0.893021 -0.021874 8.07801
REMARK 350 BIOMT2 53 -0.672490 -0.322163 -0.666309 245.96158
REMARK 350 BIOMT3 53 0.587981 0.314205 -0.745354 644.26479
REMARK 350 BIOMT1 54 -0.541989 -0.633173 0.552575 -203.96697
REMARK 350 BIOMT2 54 -0.633173 -0.124675 -0.763903 281.98599
REMARK 350 BIOMT3 54 0.552575 -0.763903 -0.333336 492.17738
REMARK 350 BIOMT1 55 -0.808299 0.488954 0.327989 -121.06593
REMARK 350 BIOMT2 55 -0.445213 -0.143057 -0.883923 326.28873
REMARK 350 BIOMT3 55 -0.385277 -0.860499 0.333321 246.09590
REMARK 350 BIOMT1 56 -0.338633 -0.723549 -0.601502 222.04043
REMARK 350 BIOMT2 56 -0.146205 0.671969 -0.726004 267.99288
REMARK 350 BIOMT3 56 0.929490 -0.157906 -0.333337 492.17529
REMARK 350 BIOMT1 57 -0.808299 -0.445213 -0.385277 142.22569
REMARK 350 BIOMT2 57 0.488954 -0.143057 -0.860499 317.63876
REMARK 350 BIOMT3 57 0.327989 -0.883923 0.333321 246.09338
REMARK 350 BIOMT1 58 -0.801913 0.105857 -0.587987 217.05167
REMARK 350 BIOMT2 58 0.105857 -0.943430 -0.314219 115.99178
REMARK 350 BIOMT3 58 -0.587987 -0.314219 0.745344 94.00466
REMARK 350 BIOMT1 59 -0.328301 0.168101 -0.929495 343.11141
REMARK 350 BIOMT2 59 -0.766069 -0.623062 0.157896 -58.27879
REMARK 350 BIOMT3 59 -0.552591 0.763895 0.333329 246.09057
REMARK 350 BIOMT1 60 -0.041977 -0.344500 -0.937848 346.19463
REMARK 350 BIOMT2 60 -0.921852 0.375310 -0.096601 35.66306
REMARK 350 BIOMT3 60 0.385262 0.860501 -0.333332 492.17356
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 ASN A 291
REMARK 465 HIS A 292
REMARK 465 SER B 1001
REMARK 465 PRO B 1002
REMARK 465 SER B 1003
REMARK 465 ALA B 1004
REMARK 465 GLU B 1005
REMARK 465 GLU B 1006
REMARK 465 CYS B 1007
REMARK 465 GLY B 1008
REMARK 465 TYR B 1009
REMARK 465 GLY D 3016
REMARK 465 LEU D 3017
REMARK 465 ARG D 3018
REMARK 465 ALA D 3019
REMARK 465 SER D 3020
REMARK 465 GLY D 3021
REMARK 465 ASN D 3022
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 290 CA C O CB OG
REMARK 470 GLN B1262 CA C O CB CG CD OE1
REMARK 470 GLN B1262 NE2
REMARK 470 THR D3015 CA C O CB OG1 CG2
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 O ASP B 1234 N SER B 1236 1.92
REMARK 500 N GLY D 3002 O1 MYR D 3500 2.13
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 MET A 76 SD MET A 76 CE 0.366
REMARK 500 GLY C2001 N GLY C2001 CA 0.091
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 ARG A 237 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B1014 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO B1056 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PHE B1082 N - CA - C ANGL. DEV. = 23.2 DEGREES
REMARK 500 PRO B1083 C - N - CA ANGL. DEV. = -20.7 DEGREES
REMARK 500 ASN B1195 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO C2071 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 GLY C2197 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU C2237 CB - CG - CD1 ANGL. DEV. = -13.5 DEGREES
REMARK 500 LEU C2237 CB - CG - CD2 ANGL. DEV. = 11.5 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 VAL A 4 -14.17 -148.76
REMARK 500 ALA A 6 45.17 -86.42
REMARK 500 VAL A 7 142.30 -179.29
REMARK 500 GLU A 8 92.22 171.94
REMARK 500 ASN A 9 -172.72 -43.70
REMARK 500 ALA A 10 122.43 95.70
REMARK 500 GLN A 86 -51.06 58.24
REMARK 500 GLU A 108 6.26 -65.80
REMARK 500 THR A 164 42.95 35.01
REMARK 500 THR A 166 -31.79 -135.14
REMARK 500 ASN A 214 -123.86 -57.13
REMARK 500 HIS A 215 68.57 64.36
REMARK 500 SER A 227 -82.32 -173.39
REMARK 500 SER A 228 118.08 42.67
REMARK 500 HIS A 244 53.08 70.55
REMARK 500 VAL A 249 87.41 41.60
REMARK 500 THR A 272 -169.99 -167.31
REMARK 500 PRO A 287 28.72 -65.04
REMARK 500 ASP A 288 86.83 75.39
REMARK 500 ARG B1014 141.93 -172.65
REMARK 500 ALA B1029 -109.79 -95.67
REMARK 500 ASN B1030 -134.43 -113.90
REMARK 500 TYR B1035 51.02 -109.49
REMARK 500 ASP B1057 -116.86 57.83
REMARK 500 PHE B1082 -65.59 -102.54
REMARK 500 ALA B1085 -25.10 124.90
REMARK 500 ALA B1114 -130.49 -140.30
REMARK 500 GLU B1150 -135.00 -81.18
REMARK 500 THR B1151 -112.34 55.37
REMARK 500 ALA B1152 138.68 141.57
REMARK 500 ASN B1164 -24.85 78.85
REMARK 500 GLN B1167 92.15 -67.48
REMARK 500 SER B1168 40.23 -98.69
REMARK 500 ALA B1173 22.94 46.28
REMARK 500 TYR B1231 -177.66 -170.96
REMARK 500 SER B1232 -123.88 -118.74
REMARK 500 ASP B1234 65.25 -50.19
REMARK 500 PHE B1235 38.13 -27.17
REMARK 500 ARG B1256 -164.49 -165.87
REMARK 500 LEU B1261 -170.36 -51.61
REMARK 500 ASP C2018 79.37 -159.27
REMARK 500 ASN C2056 47.37 -94.09
REMARK 500 PRO C2137 170.36 -55.24
REMARK 500 THR C2196 68.51 -169.74
REMARK 500 LEU C2224 82.77 60.89
REMARK 500 LEU C2236 -156.66 -64.88
REMARK 500 LEU C2237 28.07 41.94
REMARK 500 ALA D3012 32.63 -20.79
REMARK 500 ILE D3025 38.73 -98.56
REMARK 500 GLN D3048 140.89 -175.94
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MYR D 3500
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DOA A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR D 3500
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DBREF IS TO STRAIN GREGORY, NOT SEQUENCE DETAILS
REMARK 999 ARE AVAILABLE FOR STRAIN 207
DBREF 1H8T A 1 292 UNP P29813 POLG_EC11G 570 861
DBREF 1H8T B 1001 1262 UNP P29813 POLG_EC11G 70 331
DBREF 1H8T C 2001 2238 UNP P29813 POLG_EC11G 332 569
DBREF 1H8T D 3002 3069 UNP P29813 POLG_EC11G 2 69
SEQADV 1H8T VAL A 48 UNP P29813 MET 617 CONFLICT
SEQADV 1H8T GLU A 78 UNP P29813 GLY 648 CONFLICT
SEQADV 1H8T SER A 84 UNP P29813 THR 653 CONFLICT
SEQADV 1H8T THR A 131 UNP P29813 SER 700 CONFLICT
SEQADV 1H8T GLN A 132 UNP P29813 ARG 701 CONFLICT
SEQADV 1H8T THR A 161 UNP P29813 ALA 730 CONFLICT
SEQADV 1H8T SER A 267 UNP P29813 THR 836 CONFLICT
SEQADV 1H8T ASP A 270 UNP P29813 ASN 839 CONFLICT
SEQADV 1H8T ILE A 271 UNP P29813 VAL 840 CONFLICT
SEQADV 1H8T ASN A 276 UNP P29813 THR 845 CONFLICT
SEQADV 1H8T THR A 279 UNP P29813 ASN 848 CONFLICT
SEQADV 1H8T ASP A 283 UNP P29813 GLU 852 CONFLICT
SEQADV 1H8T VAL A 289 UNP P29813 LEU 858 CONFLICT
SEQADV 1H8T HIS A 292 UNP P29813 TYR 861 CONFLICT
SEQADV 1H8T ARG B 1043 UNP P29813 LYS 112 CONFLICT
SEQADV 1H8T ASP B 1045 UNP P29813 ASN 114 CONFLICT
SEQADV 1H8T LYS B 1073 UNP P29813 ARG 142 CONFLICT
SEQADV 1H8T ILE B 1108 UNP P29813 LEU 177 CONFLICT
SEQADV 1H8T THR B 1136 UNP P29813 GLN 205 CONFLICT
SEQADV 1H8T ALA B 1157 UNP P29813 SER 226 CONFLICT
SEQADV 1H8T GLY B 1159 UNP P29813 SER 228 CONFLICT
SEQADV 1H8T SER B 1168 UNP P29813 THR 237 CONFLICT
SEQADV 1H8T PHE B 1185 UNP P29813 TYR 254 CONFLICT
SEQADV 1H8T ASN B 1230 UNP P29813 ASP 299 CONFLICT
SEQADV 1H8T PHE B 1235 UNP P29813 SER 304 CONFLICT
SEQADV 1H8T ALA B 1260 UNP P29813 SER 329 CONFLICT
SEQADV 1H8T ILE C 2005 UNP P29813 MET 336 CONFLICT
SEQADV 1H8T ALA C 2059 UNP P29813 GLU 390 CONFLICT
SEQADV 1H8T ASN C 2061 UNP P29813 LYS 392 CONFLICT
SEQADV 1H8T GLU C 2063 UNP P29813 ASP 394 CONFLICT
SEQADV 1H8T ASP C 2066 UNP P29813 GLU 397 CONFLICT
SEQADV 1H8T ILE C 2067 UNP P29813 VAL 398 CONFLICT
SEQADV 1H8T SER C 2080 UNP P29813 ASP 411 CONFLICT
SEQADV 1H8T GLY C 2093 UNP P29813 SER 424 CONFLICT
SEQADV 1H8T TYR C 2107 UNP P29813 PHE 438 CONFLICT
SEQADV 1H8T SER C 2144 UNP P29813 ASN 475 CONFLICT
SEQADV 1H8T ILE C 2168 UNP P29813 VAL 499 CONFLICT
SEQADV 1H8T GLN C 2232 UNP P29813 GLU 563 CONFLICT
SEQADV 1H8T ALA C 2234 UNP P29813 THR 565 CONFLICT
SEQADV 1H8T ARG D 3018 UNP P29813 ASN 18 CONFLICT
SEQADV 1H8T ASN D 3022 UNP P29813 SER 22 CONFLICT
SEQADV 1H8T ASP D 3045 UNP P29813 GLU 45 CONFLICT
SEQADV 1H8T THR D 3047 UNP P29813 SER 47 CONFLICT
SEQRES 1 A 292 GLY ASP VAL VAL GLU ALA VAL GLU ASN ALA VAL ALA ARG
SEQRES 2 A 292 VAL ALA ASP THR ILE GLY SER GLY PRO SER ASN SER GLN
SEQRES 3 A 292 ALA VAL PRO ALA LEU THR ALA VAL GLU THR GLY HIS THR
SEQRES 4 A 292 SER GLN VAL THR PRO SER ASP THR VAL GLN THR ARG HIS
SEQRES 5 A 292 VAL LYS ASN TYR HIS SER ARG SER GLU SER SER ILE GLU
SEQRES 6 A 292 ASN PHE LEU SER ARG SER ALA CYS VAL TYR MET GLY GLU
SEQRES 7 A 292 TYR HIS THR THR ASN SER ASP GLN THR LYS LEU PHE ALA
SEQRES 8 A 292 SER TRP THR ILE SER ALA ARG ARG MET VAL GLN MET ARG
SEQRES 9 A 292 ARG LYS LEU GLU ILE PHE THR TYR VAL ARG PHE ASP VAL
SEQRES 10 A 292 GLU VAL THR PHE VAL ILE THR SER LYS GLN ASP GLN GLY
SEQRES 11 A 292 THR GLN LEU GLY GLN ASP MET PRO PRO LEU THR HIS GLN
SEQRES 12 A 292 ILE MET TYR ILE PRO PRO GLY GLY PRO ILE PRO LYS SER
SEQRES 13 A 292 VAL THR ASP TYR THR TRP GLN THR SER THR ASN PRO SER
SEQRES 14 A 292 ILE PHE TRP THR GLU GLY ASN ALA PRO PRO ARG MET SER
SEQRES 15 A 292 ILE PRO PHE ILE SER ILE GLY ASN ALA TYR SER ASN PHE
SEQRES 16 A 292 TYR ASP GLY TRP SER HIS PHE SER GLN ASN GLY VAL TYR
SEQRES 17 A 292 GLY TYR ASN THR LEU ASN HIS MET GLY GLN ILE TYR VAL
SEQRES 18 A 292 ARG HIS VAL ASN GLY SER SER PRO LEU PRO MET THR SER
SEQRES 19 A 292 THR VAL ARG MET TYR PHE LYS PRO LYS HIS VAL LYS ALA
SEQRES 20 A 292 TRP VAL PRO ARG PRO PRO ARG LEU CYS GLN TYR LYS ASN
SEQRES 21 A 292 ALA SER THR VAL ASN PHE SER PRO THR ASP ILE THR ASP
SEQRES 22 A 292 LYS ARG ASN SER ILE THR TYR ILE PRO ASP THR VAL LYS
SEQRES 23 A 292 PRO ASP VAL SER ASN HIS
SEQRES 1 B 262 SER PRO SER ALA GLU GLU CYS GLY TYR SER ASP ARG VAL
SEQRES 2 B 262 ARG SER ILE THR LEU GLY ASN SER THR ILE THR THR GLN
SEQRES 3 B 262 GLU SER ALA ASN VAL VAL VAL GLY TYR GLY ARG TRP PRO
SEQRES 4 B 262 GLU TYR LEU ARG ASP ASP GLU ALA THR ALA GLU ASP GLN
SEQRES 5 B 262 PRO THR GLN PRO ASP VAL ALA THR CYS ARG PHE TYR THR
SEQRES 6 B 262 LEU GLU SER VAL THR TRP GLU LYS ASP SER PRO GLY TRP
SEQRES 7 B 262 TRP TRP LYS PHE PRO ASP ALA LEU LYS ASP MET GLY LEU
SEQRES 8 B 262 PHE GLY GLN ASN MET TYR TYR HIS TYR LEU GLY ARG ALA
SEQRES 9 B 262 GLY TYR THR ILE HIS VAL GLN CYS ASN ALA SER LYS PHE
SEQRES 10 B 262 HIS GLN GLY CYS LEU LEU VAL VAL CYS VAL PRO GLU ALA
SEQRES 11 B 262 GLU MET GLY CYS SER THR VAL ASP GLY THR VAL ASN GLU
SEQRES 12 B 262 HIS GLY LEU SER GLU GLY GLU THR ALA LYS LYS PHE SER
SEQRES 13 B 262 ALA THR GLY THR ASN GLY THR ASN THR VAL GLN SER ILE
SEQRES 14 B 262 VAL THR ASN ALA GLY MET GLY VAL GLY VAL GLY ASN LEU
SEQRES 15 B 262 THR ILE PHE PRO HIS GLN TRP ILE ASN LEU ARG THR ASN
SEQRES 16 B 262 ASN CYS ALA THR ILE VAL MET PRO TYR ILE ASN ASN VAL
SEQRES 17 B 262 PRO MET ASP ASN MET PHE ARG HIS HIS ASN PHE THR LEU
SEQRES 18 B 262 MET ILE ILE PRO PHE VAL PRO LEU ASN TYR SER SER ASP
SEQRES 19 B 262 PHE SER THR TYR VAL PRO ILE THR VAL THR VAL ALA PRO
SEQRES 20 B 262 MET CYS ALA GLU TYR ASN GLY LEU ARG LEU SER THR ALA
SEQRES 21 B 262 LEU GLN
SEQRES 1 C 238 GLY LEU PRO VAL ILE ASN THR PRO GLY SER ASN GLN PHE
SEQRES 2 C 238 LEU THR SER ASP ASP PHE GLN SER PRO SER ALA MET PRO
SEQRES 3 C 238 GLN PHE ASP VAL THR PRO GLU LEU ASN ILE PRO GLY GLU
SEQRES 4 C 238 VAL GLN ASN LEU MET GLU ILE ALA GLU VAL ASP SER VAL
SEQRES 5 C 238 VAL PRO VAL ASN ASN VAL ALA GLY ASN LEU GLU THR MET
SEQRES 6 C 238 ASP ILE TYR ARG ILE PRO VAL GLN SER GLY ASN HIS GLN
SEQRES 7 C 238 SER SER GLN VAL PHE GLY PHE GLN VAL GLN PRO GLY LEU
SEQRES 8 C 238 ASP GLY VAL PHE LYS HIS THR LEU LEU GLY GLU ILE LEU
SEQRES 9 C 238 ASN TYR TYR ALA HIS TRP SER GLY SER ILE LYS LEU THR
SEQRES 10 C 238 PHE VAL PHE CYS GLY SER ALA MET ALA THR GLY LYS PHE
SEQRES 11 C 238 LEU LEU ALA TYR ALA PRO PRO GLY ALA ASN ALA PRO LYS
SEQRES 12 C 238 SER ARG LYS ASP ALA MET LEU GLY THR HIS ILE ILE TRP
SEQRES 13 C 238 ASP VAL GLY LEU GLN SER SER CYS VAL LEU CYS ILE PRO
SEQRES 14 C 238 TRP ILE SER GLN THR HIS TYR ARG LEU VAL GLN GLN ASP
SEQRES 15 C 238 GLU TYR THR SER ALA GLY ASN VAL THR CYS TRP TYR GLN
SEQRES 16 C 238 THR GLY ILE VAL VAL PRO ALA GLY THR PRO THR SER CYS
SEQRES 17 C 238 SER ILE MET CYS PHE VAL SER ALA CYS ASN ASP PHE SER
SEQRES 18 C 238 VAL ARG LEU LEU LYS ASP THR PRO PHE ILE GLN GLN ALA
SEQRES 19 C 238 ALA LEU LEU GLN
SEQRES 1 D 68 GLY ALA GLN VAL SER THR GLN LYS THR GLY ALA HIS GLU
SEQRES 2 D 68 THR GLY LEU ARG ALA SER GLY ASN SER ILE ILE HIS TYR
SEQRES 3 D 68 THR ASN ILE ASN TYR TYR LYS ASP ALA ALA SER ASN SER
SEQRES 4 D 68 ALA ASN ARG GLN ASP PHE THR GLN ASP PRO GLY LYS PHE
SEQRES 5 D 68 THR GLU PRO VAL LYS ASP ILE MET VAL LYS SER LEU PRO
SEQRES 6 D 68 ALA LEU ASN
HET DOA A1000 15
HET MYR D3500 15
HETNAM DOA 12-AMINO-DODECANOIC ACID
HETNAM MYR MYRISTIC ACID
FORMUL 5 DOA C12 H25 N O2
FORMUL 6 MYR C14 H28 O2
FORMUL 7 HOH *11(H2 O)
HELIX 1 1 THR A 43 VAL A 48 1 6
HELIX 2 2 ARG A 59 SER A 62 5 4
HELIX 3 3 SER A 63 SER A 69 1 7
HELIX 4 4 GLN A 86 LYS A 88 5 3
HELIX 5 5 MET A 100 GLU A 108 1 9
HELIX 6 6 ASP A 159 THR A 164 5 6
HELIX 7 7 TYR A 210 ASN A 214 5 5
HELIX 8 8 PRO B 1056 THR B 1060 5 5
HELIX 9 9 GLN B 1094 TYR B 1098 1 5
HELIX 10 10 VAL B 1170 ALA B 1173 5 4
HELIX 11 11 ASN B 1181 PHE B 1185 5 5
HELIX 12 12 ASN C 2042 GLU C 2048 1 7
HELIX 13 13 THR C 2064 ARG C 2069 5 6
HELIX 14 14 ILE C 2103 ASN C 2105 5 3
HELIX 15 15 SER C 2144 MET C 2149 1 6
HELIX 16 16 ASP D 3035 ASN D 3039 5 5
SHEET 1 AA 4 LEU A 31 THR A 32 0
SHEET 2 AA 4 SER C2163 ILE C2168 -1 O SER C2163 N THR A 32
SHEET 3 AA 4 TYR C2107 PHE C2120 -1 O ILE C2114 N ILE C2168
SHEET 4 AA 4 SER C2207 LEU C2225 -1 O MET C2211 N VAL C2119
SHEET 1 AB 4 LEU A 31 THR A 32 0
SHEET 2 AB 4 SER C2163 ILE C2168 -1 O SER C2163 N THR A 32
SHEET 3 AB 4 TYR C2107 PHE C2120 -1 O ILE C2114 N ILE C2168
SHEET 4 AB 4 ARG C2177 LEU C2178 -1 O ARG C2177 N TRP C2110
SHEET 1 AC 3 ALA A 72 TYR A 75 0
SHEET 2 AC 3 MET A 232 PRO A 250 -1 O MET A 238 N VAL A 74
SHEET 3 AC 3 TYR A 79 HIS A 80 -1 O TYR A 79 N SER A 234
SHEET 1 AD 2 ALA A 72 TYR A 75 0
SHEET 2 AD 2 MET A 232 PRO A 250 -1 O MET A 238 N VAL A 74
SHEET 1 AE 4 PHE A 90 TRP A 93 0
SHEET 2 AE 4 ILE A 219 HIS A 223 -1 O ILE A 219 N TRP A 93
SHEET 3 AE 4 THR A 141 TYR A 146 -1 O GLN A 143 N ARG A 222
SHEET 4 AE 4 SER A 169 THR A 173 -1 O ILE A 170 N ILE A 144
SHEET 1 BA 2 ARG B1014 THR B1017 0
SHEET 2 BA 2 THR B1022 THR B1025 -1 O ILE B1023 N ILE B1016
SHEET 1 BB 2 VAL B1031 VAL B1032 0
SHEET 2 BB 2 VAL D3057 LYS D3058 -1 O LYS D3058 N VAL B1031
SHEET 1 BC 3 TYR B1064 THR B1065 0
SHEET 2 BC 3 VAL B1239 ALA B1246 -1 O VAL B1245 N TYR B1064
SHEET 3 BC 3 VAL B1069 TRP B1071 -1 O VAL B1069 N ILE B1241
SHEET 1 BD 2 TYR B1064 THR B1065 0
SHEET 2 BD 2 VAL B1239 ALA B1246 -1 O VAL B1245 N TYR B1064
SHEET 1 BE 4 TRP B1079 LYS B1081 0
SHEET 2 BE 4 PHE B1219 ASN B1230 -1 O LEU B1221 N TRP B1080
SHEET 3 BE 4 GLN B1119 PRO B1128 -1 O GLN B1119 N ASN B1230
SHEET 4 BE 4 HIS B1187 ILE B1190 -1 O GLN B1188 N VAL B1124
SHEET 1 BF 2 HIS B1099 LEU B1101 0
SHEET 2 BF 2 ASN B1253 LEU B1255 -1 O ASN B1253 N LEU B1101
SHEET 1 CA 3 HIS C2153 TRP C2156 0
SHEET 2 CA 3 THR C2127 TYR C2134 -1 O PHE C2130 N TRP C2156
SHEET 3 CA 3 VAL C2190 VAL C2199 -1 O THR C2191 N ALA C2133
SHEET 1 DA 2 GLN D3004 THR D3007 0
SHEET 2 DA 2 HIS D3026 ASN D3029 -1 O TYR D3027 N SER D3006
SITE 1 AC1 4 TYR A 192 ASN A 194 TYR A 210 MET A 216
SITE 1 AC2 2 GLY D3002 TYR D3032
CRYST1 300.850 300.850 1476.620 90.00 90.00 120.00 H 3 2 1080
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 0.003324 0.001919 0.000000 0.00000
SCALE2 0.000000 0.003838 0.000000 0.00000
SCALE3 0.000000 0.000000 0.000677 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 0.507091 -0.649919 0.566095 -208.96134
MTRIX2 2 0.861614 0.365580 -0.352096 129.96817
MTRIX3 2 0.021880 0.666301 0.745362 93.99385
MTRIX1 3 -0.290451 -0.189976 0.937842 -346.18311
MTRIX2 3 0.744203 -0.660932 0.096598 -35.65695
MTRIX3 3 0.601498 0.726001 0.333349 246.07907
MTRIX1 4 -0.290451 0.744203 0.601498 -222.02949
MTRIX2 4 -0.189976 -0.660932 0.726001 -267.98708
MTRIX3 4 0.937842 0.096598 0.333349 246.07905
MTRIX1 5 0.507091 0.861614 0.021880 -8.07656
MTRIX2 5 -0.649919 0.365580 0.666301 -245.94988
MTRIX3 5 0.566095 -0.352096 0.745362 93.99383
MTRIX1 6 -0.816394 -0.114204 0.566090 -208.95555
MTRIX2 6 -0.114204 -0.928965 -0.352111 129.97974
MTRIX3 6 0.566090 -0.352111 0.745359 93.99491
MTRIX1 7 -0.500000 0.866025 -0.000005 0.00545
MTRIX2 7 -0.866025 -0.500000 -0.000016 0.01179
MTRIX3 7 -0.000016 -0.000004 1.000000 0.00000
MTRIX1 8 0.492634 0.641558 -0.587975 217.04142
MTRIX2 8 -0.869962 0.380045 -0.314217 115.99204
MTRIX3 8 0.021869 0.666310 0.745354 93.99669
MTRIX1 9 0.789721 -0.477399 -0.385266 142.21604
MTRIX2 9 -0.120573 0.494979 -0.860499 317.63974
MTRIX3 9 0.601500 0.726007 0.333334 246.08475
MTRIX1 10 -0.019303 -0.944486 0.327985 -121.06457
MTRIX2 10 0.346511 -0.314034 -0.883919 326.28462
MTRIX3 10 0.937847 0.096588 0.333337 246.08365
MTRIX1 11 -0.442118 0.896957 0.000010 -0.00012
MTRIX2 11 0.896957 0.442118 0.000016 -0.00794
MTRIX3 11 0.000010 0.000016 -1.000000 738.26552
MTRIX1 12 0.548637 0.615257 -0.566088 208.96219
MTRIX2 12 0.835775 -0.421309 0.352107 -129.97455
MTRIX3 12 -0.021862 -0.666301 -0.745362 644.27167
MTRIX1 13 0.795938 -0.508829 -0.327989 121.07326
MTRIX2 13 0.068512 -0.462599 0.883917 -326.28002
MTRIX3 13 -0.601489 -0.726014 -0.333339 492.18252
MTRIX1 14 -0.041977 -0.921852 0.385262 -142.20740
MTRIX2 14 -0.344500 0.375310 0.860501 -317.63686
MTRIX3 14 -0.937848 -0.096601 -0.333332 492.18011
MTRIX1 15 -0.807138 -0.053029 0.587977 -217.03487
MTRIX2 15 0.167507 0.934455 0.314221 -115.98963
MTRIX3 15 -0.566101 0.352110 -0.745351 644.26777
MTRIX1 16 0.258512 -0.782753 -0.566099 208.97001
MTRIX2 16 -0.782753 -0.513153 0.352095 -129.96423
MTRIX3 16 -0.566099 0.352095 -0.745359 644.27061
MTRIX1 17 -0.555729 -0.831364 -0.000002 0.00804
MTRIX2 17 -0.831364 0.555729 0.000005 0.00216
MTRIX3 17 -0.000002 0.000005 -1.000000 738.26552
MTRIX1 18 -0.998120 0.057246 -0.021878 8.08277
MTRIX2 18 0.057246 0.743485 -0.666297 245.95250
MTRIX3 18 -0.021878 -0.666297 -0.745365 644.27276
MTRIX1 19 -0.457293 0.655048 -0.601494 222.03520
MTRIX2 19 0.655048 -0.209356 -0.726004 267.99178
MTRIX3 19 -0.601494 -0.726004 -0.333351 492.18713
MTRIX1 20 0.319349 0.135900 -0.937842 346.19034
MTRIX2 20 0.135900 -0.986002 -0.096603 35.66246
MTRIX3 20 -0.937842 -0.096603 -0.333348 492.18580
MTRIX1 21 0.819330 -0.152792 0.552588 -203.97739
MTRIX2 21 0.424571 -0.486004 -0.763898 281.98107
MTRIX3 21 0.385277 0.860497 -0.333326 492.17138
MTRIX1 22 0.295918 -0.220166 0.929494 -343.10381
MTRIX2 22 -0.220166 -0.962596 -0.157913 58.29547
MTRIX3 22 0.929494 -0.157913 -0.333323 492.17002
MTRIX1 23 -0.019303 0.346511 0.937847 -346.18709
MTRIX2 23 -0.944486 -0.314034 0.096588 -35.64811
MTRIX3 23 0.327985 -0.883919 0.333337 246.08770
MTRIX1 24 0.309291 0.764111 0.566103 -208.96624
MTRIX2 24 -0.747404 0.563391 -0.352105 129.97718
MTRIX3 24 -0.587985 -0.314204 0.745351 94.00182
MTRIX1 25 0.827595 0.455525 0.328000 -121.07581
MTRIX2 25 0.098720 0.457108 -0.883915 326.28280
MTRIX3 25 -0.552577 0.763904 0.333331 246.08990
MTRIX1 26 -0.338633 -0.146205 0.929490 -343.10025
MTRIX2 26 -0.723549 0.671969 -0.157906 58.29149
MTRIX3 26 -0.601502 -0.726004 -0.333337 492.18186
MTRIX1 27 -0.277352 0.785954 0.552587 -203.97472
MTRIX2 27 0.208618 0.610694 -0.763892 281.97765
MTRIX3 27 -0.937845 -0.096588 -0.333342 492.18363
MTRIX1 28 0.548637 0.835775 -0.021862 8.06993
MTRIX2 28 0.615257 -0.421309 -0.666301 245.95412
MTRIX3 28 -0.566088 0.352107 -0.745362 644.27170
MTRIX1 29 0.997846 -0.065593 0.000013 -0.00479
MTRIX2 29 -0.065593 -0.997846 0.000000 0.00418
MTRIX3 29 0.000013 0.000000 -1.000000 738.26552
MTRIX1 30 0.449484 -0.672490 0.587981 -217.03989
MTRIX2 30 -0.893021 -0.322163 0.314205 -115.97770
MTRIX3 30 -0.021874 -0.666309 -0.745354 644.26883
MTRIX1 31 -0.499282 0.667360 -0.552582 203.98037
MTRIX2 31 -0.623642 0.165939 0.763895 -281.97468
MTRIX3 31 0.601488 0.726013 0.333343 246.08124
MTRIX1 32 0.309735 0.200281 -0.929490 343.10736
MTRIX2 32 -0.156554 0.974964 0.157911 -58.28942
MTRIX3 32 0.937846 0.096605 0.333335 246.08432
MTRIX1 33 0.309291 -0.747404 -0.587985 217.04855
MTRIX2 33 0.764111 0.563391 -0.314204 115.98124
MTRIX3 33 0.566103 -0.352105 0.745351 93.99776
MTRIX1 34 -0.500000 -0.866025 -0.000016 0.01293
MTRIX2 34 0.866025 -0.500000 -0.000004 0.00117
MTRIX3 34 -0.000005 -0.000016 1.000000 0.00000
MTRIX1 35 -0.999726 0.008347 0.021864 -8.06364
MTRIX2 35 0.008347 -0.745639 0.666298 -245.94911
MTRIX3 35 0.021864 0.666298 0.745365 93.99276
MTRIX1 36 0.018585 -0.368364 -0.929496 343.11160
MTRIX2 36 0.922620 -0.351905 0.157909 -58.29030
MTRIX3 36 -0.385262 -0.860506 0.333320 246.09657
MTRIX1 37 -0.328301 -0.766069 -0.552591 203.98552
MTRIX2 37 0.168101 -0.623062 0.763895 -281.97612
MTRIX3 37 -0.929495 0.157896 0.333329 246.09307
MTRIX1 38 -0.838626 -0.434883 -0.328000 121.08295
MTRIX2 38 -0.434883 0.171952 0.883917 -326.27967
MTRIX3 38 -0.328000 0.883917 -0.333326 492.17389
MTRIX1 39 -0.807138 0.167507 -0.566101 208.97243
MTRIX2 39 -0.053029 0.934455 0.352110 -129.97496
MTRIX3 39 0.587977 0.314221 -0.745351 644.26370
MTRIX1 40 -0.277352 0.208618 -0.937845 346.19368
MTRIX2 40 0.785954 0.610694 -0.096588 35.65158
MTRIX3 40 0.552587 -0.763892 -0.333342 492.17955
MTRIX1 41 0.819330 0.424571 0.385277 -142.21850
MTRIX2 41 -0.152792 -0.486004 0.860497 -317.63432
MTRIX3 41 0.552588 -0.763898 -0.333326 492.17386
MTRIX1 42 0.789721 -0.120573 0.601500 -222.03238
MTRIX2 42 -0.477399 0.494979 0.726007 -267.99032
MTRIX3 42 -0.385266 -0.860499 0.333334 246.09129
MTRIX1 43 0.309735 -0.156554 0.937846 -346.18694
MTRIX2 43 0.200281 0.974964 0.096605 -35.66069
MTRIX3 43 -0.929490 0.157911 0.333335 246.09090
MTRIX1 44 0.042695 0.366352 0.929496 -343.10480
MTRIX2 44 0.943718 0.290629 -0.157897 58.28292
MTRIX3 44 -0.327985 0.883924 -0.333324 492.17322
MTRIX1 45 0.357642 0.725507 0.587990 -217.04537
MTRIX2 45 0.725507 -0.612298 0.314214 -115.98637
MTRIX3 45 0.587990 0.314214 -0.745344 644.26086
MTRIX1 46 -0.499282 -0.623642 0.601488 -222.02230
MTRIX2 46 0.667360 0.165939 0.726013 -267.99591
MTRIX3 46 -0.552582 0.763895 0.333343 246.08530
MTRIX1 47 -0.777360 0.497273 0.385266 -142.20903
MTRIX2 47 0.497273 0.110677 0.860506 -317.64088
MTRIX3 47 0.385266 0.860506 -0.333317 492.16787
MTRIX1 48 0.042695 0.943718 -0.327985 121.07160
MTRIX2 48 0.366352 0.290629 0.883924 -326.28510
MTRIX3 48 0.929496 -0.157897 -0.333324 492.17069
MTRIX1 49 0.827595 0.098720 -0.552577 203.97470
MTRIX2 49 0.455525 0.457108 0.763904 -281.98255
MTRIX3 49 0.328000 -0.883915 0.333331 246.08987
MTRIX1 50 0.492634 -0.869962 0.021869 -8.06899
MTRIX2 50 0.641558 0.380045 0.666310 -245.95785
MTRIX3 50 -0.587975 -0.314217 0.745354 94.00073
MTRIX1 51 0.018585 0.922620 -0.385262 142.21471
MTRIX2 51 -0.368364 -0.351905 -0.860506 317.64492
MTRIX3 51 -0.929496 0.157909 0.333320 246.09659
MTRIX1 52 0.795938 0.068512 -0.601489 222.03005
MTRIX2 52 -0.508829 -0.462599 -0.726014 268.00001
MTRIX3 52 -0.327989 0.883917 -0.333339 492.17850
MTRIX1 53 0.449484 -0.893021 -0.021874 8.07801
MTRIX2 53 -0.672490 -0.322163 -0.666309 245.96158
MTRIX3 53 0.587981 0.314205 -0.745354 644.26479
MTRIX1 54 -0.541989 -0.633173 0.552575 -203.96697
MTRIX2 54 -0.633173 -0.124675 -0.763903 281.98599
MTRIX3 54 0.552575 -0.763903 -0.333336 492.17738
MTRIX1 55 -0.808299 0.488954 0.327989 -121.06593
MTRIX2 55 -0.445213 -0.143057 -0.883923 326.28873
MTRIX3 55 -0.385277 -0.860499 0.333321 246.09590
MTRIX1 56 -0.338633 -0.723549 -0.601502 222.04043
MTRIX2 56 -0.146205 0.671969 -0.726004 267.99288
MTRIX3 56 0.929490 -0.157906 -0.333337 492.17529
MTRIX1 57 -0.808299 -0.445213 -0.385277 142.22569
MTRIX2 57 0.488954 -0.143057 -0.860499 317.63876
MTRIX3 57 0.327989 -0.883923 0.333321 246.09338
MTRIX1 58 -0.801913 0.105857 -0.587987 217.05167
MTRIX2 58 0.105857 -0.943430 -0.314219 115.99178
MTRIX3 58 -0.587987 -0.314219 0.745344 94.00466
MTRIX1 59 -0.328301 0.168101 -0.929495 343.11141
MTRIX2 59 -0.766069 -0.623062 0.157896 -58.27879
MTRIX3 59 -0.552591 0.763895 0.333329 246.09057
MTRIX1 60 -0.041977 -0.344500 -0.937848 346.19463
MTRIX2 60 -0.921852 0.375310 -0.096601 35.66306
MTRIX3 60 0.385262 0.860501 -0.333332 492.17356
(ATOM LINES ARE NOT SHOWN.)
END
