HEADER RNA POLYMERASE 31-DEC-00 1HI0
TITLE RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6
TITLE 2 PLUS INITIATION COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P2 PROTEIN;
COMPND 3 CHAIN: P, Q, R;
COMPND 4 SYNONYM: RNA-DIRECTED RNA POLYMERASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-(*TP*TP*TP*CP*C)-3');
COMPND 8 CHAIN: D, E, F;
COMPND 9 OTHER_DETAILS: 5 NUCLEOTIDE DNA VERSION OF OPTIMUM RNA
COMPND 10 TEMPLATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE PHI-6;
SOURCE 3 ORGANISM_COMMON: PHAGE PHI 6;
SOURCE 4 ORGANISM_TAXID: 10879;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES
KEYWDS RNA POLYMERASE, VIRAL POLYMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.GRIMES,S.J.BUTCHER,E.V.MAKEYEV,D.H.BAMFORD,D.I.STUART
REVDAT 2 24-FEB-09 1HI0 1 VERSN
REVDAT 1 27-MAR-01 1HI0 0
JRNL AUTH S.J.BUTCHER,J.M.GRIMES,E.V.MAKEYEV,D.H.BAMFORD,
JRNL AUTH 2 D.I.STUART
JRNL TITL A MECHANISM FOR INITIATING RNA-DEPENDENT RNA
JRNL TITL 2 POLYMERIZATION
JRNL REF NATURE V. 410 235 2001
JRNL REFN ISSN 0028-0836
JRNL PMID 11242087
JRNL DOI 10.1038/35065653
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.BUTCHER,E.V.MAKEYEV,J.M.GRIMES,D.I.STUART,
REMARK 1 AUTH 2 D.H.BAMFORD
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDIES ON THE BACTERIOPHAGE PHI6
REMARK 1 TITL 3 RNA-DEPENDENT RNA POLYMERASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1473 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 11053857
REMARK 1 DOI 10.1107/S0907444900010702
REMARK 2
REMARK 2 RESOLUTION. 3.0 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) : 3.0
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 0.0
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 53533
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) : 0.214
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2711
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 : 15795
REMARK 3 NUCLEIC ACID ATOMS : 225
REMARK 3 HETEROGEN ATOMS : 201
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) : 52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.811
REMARK 3 B22 (A**2) : -21.031
REMARK 3 B33 (A**2) : 18.222
REMARK 3 B12 (A**2) : 0.0
REMARK 3 B13 (A**2) : 1.647
REMARK 3 B23 (A**2) : 0.0
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) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010659
REMARK 3 BOND ANGLES (DEGREES) : 1.51056
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) : 4.061 ; 3
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.878 ; 4
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.308 ; 4
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.947 ; 5
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.322
REMARK 3 BSOL : 23
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : GTP_XPLOR_PAR.TXT
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: NULL
REMARK 4
REMARK 4 1HI0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JAN-01.
REMARK 100 THE PDBE ID CODE IS EBI-5741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9724
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 56000
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
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) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.96000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY TBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 PROTEIN(5MG/ML)+TEMPLATE
REMARK 280 WELL SOLUTION: 10% PEG 8000, 0.1M MES, 2 MM MNCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.35000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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
REMARK 300 DETAILS:THE PROTEIN IS ACTIVE AS A MONOMER
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, E
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 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, F
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 400
REMARK 400 COMPOUND
REMARK 400 P2 IS ONE OF THE 4 STRUCTURAL PROTEINS OF THE POLYHEDRAL
REMARK 400 PROCAPSID. IT IS RESPONSIBLE FOR GENOMIC REPLICATION AND
REMARK 400 TRANSCRIPTION.
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 T D 2
REMARK 465 T E 2
REMARK 465 T F 2
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 NE2 GLN P 608 - NH1 ARG Q 593 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 OE2 GLU P 569 CB PRO R 1 1555 2.16
REMARK 500 NH2 ARG Q 537 N SER R 582 1655 2.03
REMARK 500 CB PRO R 1 OE2 GLU P 569 1545 2.16
REMARK 500 CD LYS R 479 CA GLN R 608 1445 2.19
REMARK 500 CD LYS R 479 CB GLN R 608 1445 1.58
REMARK 500 CD LYS R 479 C GLN R 608 1445 2.19
REMARK 500 CE LYS R 479 N GLN R 608 1445 1.70
REMARK 500 CE LYS R 479 CA GLN R 608 1445 1.55
REMARK 500 CE LYS R 479 CB GLN R 608 1445 2.02
REMARK 500 CE LYS R 479 C GLN R 608 1445 1.71
REMARK 500 CE LYS R 479 N ALA R 609 1445 2.10
REMARK 500 NZ LYS R 479 C ARG R 607 1445 1.27
REMARK 500 NZ LYS R 479 O ARG R 607 1445 1.91
REMARK 500 NZ LYS R 479 N GLN R 608 1445 0.78
REMARK 500 NZ LYS R 479 CA GLN R 608 1445 1.50
REMARK 500 NZ LYS R 479 CB GLN R 608 1445 1.99
REMARK 500 N SER R 582 NH2 ARG Q 537 1455 2.03
REMARK 500 C ARG R 607 NZ LYS R 479 1455 1.27
REMARK 500 O ARG R 607 NZ LYS R 479 1455 1.91
REMARK 500 N GLN R 608 CE LYS R 479 1455 1.70
REMARK 500 N GLN R 608 NZ LYS R 479 1455 0.78
REMARK 500 CA GLN R 608 CD LYS R 479 1455 2.19
REMARK 500 CA GLN R 608 CE LYS R 479 1455 1.55
REMARK 500 CA GLN R 608 NZ LYS R 479 1455 1.50
REMARK 500 C GLN R 608 CD LYS R 479 1455 2.19
REMARK 500 C GLN R 608 CE LYS R 479 1455 1.71
REMARK 500 CB GLN R 608 CD LYS R 479 1455 1.58
REMARK 500 CB GLN R 608 CE LYS R 479 1455 2.02
REMARK 500 CB GLN R 608 NZ LYS R 479 1455 1.99
REMARK 500 N ALA R 609 CE LYS R 479 1455 2.10
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 GLY P 493 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLY Q 493 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLY R 493 N - CA - C ANGL. DEV. = -15.5 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 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 ARG P 2 104.75 78.40
REMARK 500 ARG P 30 119.92 -34.64
REMARK 500 ARG P 88 42.39 -70.39
REMARK 500 SER P 136 -82.82 -90.57
REMARK 500 CYS P 152 -157.73 58.43
REMARK 500 LYS P 185 63.95 -100.55
REMARK 500 GLN P 206 71.75 -116.19
REMARK 500 SER P 207 -8.33 -45.83
REMARK 500 SER P 296 -86.50 -90.00
REMARK 500 THR P 305 -60.07 -138.70
REMARK 500 TRP P 332 118.01 -39.97
REMARK 500 LYS P 362 19.00 -146.00
REMARK 500 ALA P 369 80.02 -150.84
REMARK 500 ASP P 386 35.68 -146.87
REMARK 500 THR P 418 -15.47 -147.75
REMARK 500 LYS P 451 101.70 -160.38
REMARK 500 SER P 452 -123.83 56.29
REMARK 500 ASP P 504 -154.97 -110.04
REMARK 500 GLN P 533 48.12 36.69
REMARK 500 TYR P 564 -74.44 -46.43
REMARK 500 ALA P 603 -74.10 -59.37
REMARK 500 SER P 604 -16.74 -43.59
REMARK 500 ARG P 607 38.31 -59.64
REMARK 500 GLN P 608 12.24 165.51
REMARK 500 TYR P 630 -45.94 -175.36
REMARK 500 ARG Q 2 104.76 78.34
REMARK 500 ARG Q 30 119.86 -34.60
REMARK 500 ARG Q 88 42.42 -70.43
REMARK 500 SER Q 136 -82.83 -90.50
REMARK 500 CYS Q 152 -157.72 58.32
REMARK 500 LYS Q 185 63.97 -100.53
REMARK 500 GLN Q 206 71.68 -116.22
REMARK 500 SER Q 207 -8.31 -45.81
REMARK 500 SER Q 296 -86.44 -90.02
REMARK 500 THR Q 305 -60.05 -138.66
REMARK 500 TRP Q 332 117.97 -39.94
REMARK 500 LYS Q 362 19.01 -146.00
REMARK 500 ALA Q 369 80.02 -150.88
REMARK 500 ASP Q 386 35.69 -146.85
REMARK 500 THR Q 418 -15.49 -147.73
REMARK 500 LYS Q 451 101.68 -160.45
REMARK 500 SER Q 452 -123.80 56.25
REMARK 500 ASP Q 504 -154.94 -110.08
REMARK 500 GLN Q 533 48.21 36.60
REMARK 500 TYR Q 564 -74.44 -46.37
REMARK 500 ALA Q 603 -74.02 -59.40
REMARK 500 SER Q 604 -16.73 -43.58
REMARK 500 ARG Q 607 38.33 -59.62
REMARK 500 GLN Q 608 12.14 165.51
REMARK 500 TYR Q 630 -46.01 -175.29
REMARK 500 ARG R 2 104.76 78.36
REMARK 500 ARG R 30 119.86 -34.54
REMARK 500 ARG R 88 42.38 -70.40
REMARK 500 SER R 136 -82.87 -90.57
REMARK 500 CYS R 152 -157.71 58.37
REMARK 500 LYS R 185 63.99 -100.56
REMARK 500 GLN R 206 71.73 -116.18
REMARK 500 SER R 207 -8.31 -45.84
REMARK 500 SER R 296 -86.51 -89.99
REMARK 500 THR R 305 -60.03 -138.73
REMARK 500 TRP R 332 118.01 -39.95
REMARK 500 LYS R 362 19.02 -146.00
REMARK 500 ALA R 369 80.00 -150.84
REMARK 500 ASP R 386 35.70 -146.87
REMARK 500 THR R 418 -15.42 -147.78
REMARK 500 LYS R 451 101.78 -160.33
REMARK 500 SER R 452 -123.81 56.20
REMARK 500 ASP R 504 -154.96 -110.05
REMARK 500 GLN R 533 48.17 36.63
REMARK 500 TYR R 564 -74.43 -46.41
REMARK 500 ALA R 603 -74.10 -59.38
REMARK 500 SER R 604 -16.73 -43.64
REMARK 500 ARG R 607 38.30 -59.68
REMARK 500 GLN R 608 12.22 165.53
REMARK 500 TYR R 630 -45.96 -175.38
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 DC D 5 0.08 SIDE CHAIN
REMARK 500 DC E 5 0.08 SIDE CHAIN
REMARK 500 DC F 5 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN P 665 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP P 454 OD1
REMARK 620 2 GLU P 491 OE1 171.4
REMARK 620 3 ALA P 495 O 103.6 83.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN Q 665 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU Q 491 OE1
REMARK 620 2 ALA Q 495 O 83.6
REMARK 620 3 ASP Q 454 OD1 171.4 103.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN R 665 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 454 OD1
REMARK 620 2 GLU R 491 OE1 171.4
REMARK 620 3 ALA R 495 O 103.7 83.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG P 668 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL P 325 O
REMARK 620 2 ASP P 453 OD1 81.5
REMARK 620 3 GTP P 667 O2B 84.3 57.8
REMARK 620 4 GTP P 667 O2G 128.8 128.9 82.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG P 669 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP P 667 O1A
REMARK 620 2 GTP P 667 O2G 66.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Q 668 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP Q 667 O2G
REMARK 620 2 VAL Q 325 O 128.8
REMARK 620 3 ASP Q 453 OD1 128.9 81.5
REMARK 620 4 GTP Q 667 O2B 82.6 84.3 57.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Q 669 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP Q 667 O1A
REMARK 620 2 GTP Q 667 O2G 66.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG R 668 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL R 325 O
REMARK 620 2 ASP R 453 OD1 81.5
REMARK 620 3 GTP R 667 O2G 128.8 128.9
REMARK 620 4 GTP R 667 O2B 84.3 57.8 82.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG R 669 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP R 667 O2G
REMARK 620 2 GTP R 667 O1A 66.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN P 665
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 669
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN Q 665
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 669
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN R 665
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 669
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP P 666
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP P 667
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP Q 666
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP Q 667
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP R 666
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP R 667
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HHS RELATED DB: PDB
REMARK 900 RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE
REMARK 900 PHI6
REMARK 900 RELATED ID: 1HHT RELATED DB: PDB
REMARK 900 RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE
REMARK 900 PHI6 PLUS TEMPLATE
REMARK 900 RELATED ID: 1HI1 RELATED DB: PDB
REMARK 900 RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE
REMARK 900 PHI6 PLUS BOUND NTP
REMARK 900 RELATED ID: 1HI8 RELATED DB: PDB
REMARK 900 RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE
REMARK 900 PHI6
DBREF 1HI0 P 1 664 UNP P11124 VP2_BPPH6 1 664
DBREF 1HI0 Q 1 664 UNP P11124 VP2_BPPH6 1 664
DBREF 1HI0 R 1 664 UNP P11124 VP2_BPPH6 1 664
DBREF 1HI0 D 2 6 PDB 1HI0 1HI0 2 6
DBREF 1HI0 E 2 6 PDB 1HI0 1HI0 2 6
DBREF 1HI0 F 2 6 PDB 1HI0 1HI0 2 6
SEQADV 1HI0 MET P 456 UNP P11124 ILE 456 CONFLICT
SEQADV 1HI0 MET Q 456 UNP P11124 ILE 456 CONFLICT
SEQADV 1HI0 MET R 456 UNP P11124 ILE 456 CONFLICT
SEQRES 1 D 5 DT DT DT DC DC
SEQRES 1 E 5 DT DT DT DC DC
SEQRES 1 F 5 DT DT DT DC DC
SEQRES 1 P 664 PRO ARG ARG ALA PRO ALA PHE PRO LEU SER ASP ILE LYS
SEQRES 2 P 664 ALA GLN MET LEU PHE ALA ASN ASN ILE LYS ALA GLN GLN
SEQRES 3 P 664 ALA SER LYS ARG SER PHE LYS GLU GLY ALA ILE GLU THR
SEQRES 4 P 664 TYR GLU GLY LEU LEU SER VAL ASP PRO ARG PHE LEU SER
SEQRES 5 P 664 PHE LYS ASN GLU LEU SER ARG TYR LEU THR ASP HIS PHE
SEQRES 6 P 664 PRO ALA ASN VAL ASP GLU TYR GLY ARG VAL TYR GLY ASN
SEQRES 7 P 664 GLY VAL ARG THR ASN PHE PHE GLY MET ARG HIS MET ASN
SEQRES 8 P 664 GLY PHE PRO MET ILE PRO ALA THR TRP PRO LEU ALA SER
SEQRES 9 P 664 ASN LEU LYS LYS ARG ALA ASP ALA ASP LEU ALA ASP GLY
SEQRES 10 P 664 PRO VAL SER GLU ARG ASP ASN LEU LEU PHE ARG ALA ALA
SEQRES 11 P 664 VAL ARG LEU MET PHE SER ASP LEU GLU PRO VAL PRO LEU
SEQRES 12 P 664 LYS ILE ARG LYS GLY SER SER THR CYS ILE PRO TYR PHE
SEQRES 13 P 664 SER ASN ASP MET GLY THR LYS ILE GLU ILE ALA GLU ARG
SEQRES 14 P 664 ALA LEU GLU LYS ALA GLU GLU ALA GLY ASN LEU MET LEU
SEQRES 15 P 664 GLN GLY LYS PHE ASP ASP ALA TYR GLN LEU HIS GLN MET
SEQRES 16 P 664 GLY GLY ALA TYR TYR VAL VAL TYR ARG ALA GLN SER THR
SEQRES 17 P 664 ASP ALA ILE THR LEU ASP PRO LYS THR GLY LYS PHE VAL
SEQRES 18 P 664 SER LYS ASP ARG MET VAL ALA ASP PHE GLU TYR ALA VAL
SEQRES 19 P 664 THR GLY GLY GLU GLN GLY SER LEU PHE ALA ALA SER LYS
SEQRES 20 P 664 ASP ALA SER ARG LEU LYS GLU GLN TYR GLY ILE ASP VAL
SEQRES 21 P 664 PRO ASP GLY PHE PHE CYS GLU ARG ARG ARG THR ALA MET
SEQRES 22 P 664 GLY GLY PRO PHE ALA LEU ASN ALA PRO ILE MET ALA VAL
SEQRES 23 P 664 ALA GLN PRO VAL ARG ASN LYS ILE TYR SER LYS TYR ALA
SEQRES 24 P 664 TYR THR PHE HIS HIS THR THR ARG LEU ASN LYS GLU GLU
SEQRES 25 P 664 LYS VAL LYS GLU TRP SER LEU CYS VAL ALA THR ASP VAL
SEQRES 26 P 664 SER ASP HIS ASP THR PHE TRP PRO GLY TRP LEU ARG ASP
SEQRES 27 P 664 LEU ILE CYS ASP GLU LEU LEU ASN MET GLY TYR ALA PRO
SEQRES 28 P 664 TRP TRP VAL LYS LEU PHE GLU THR SER LEU LYS LEU PRO
SEQRES 29 P 664 VAL TYR VAL GLY ALA PRO ALA PRO GLU GLN GLY HIS THR
SEQRES 30 P 664 LEU LEU GLY ASP PRO SER ASN PRO ASP LEU GLU VAL GLY
SEQRES 31 P 664 LEU SER SER GLY GLN GLY ALA THR ASP LEU MET GLY THR
SEQRES 32 P 664 LEU LEU MET SER ILE THR TYR LEU VAL MET GLN LEU ASP
SEQRES 33 P 664 HIS THR ALA PRO HIS LEU ASN SER ARG ILE LYS ASP MET
SEQRES 34 P 664 PRO SER ALA CYS ARG PHE LEU ASP SER TYR TRP GLN GLY
SEQRES 35 P 664 HIS GLU GLU ILE ARG GLN ILE SER LYS SER ASP ASP ALA
SEQRES 36 P 664 MET LEU GLY TRP THR LYS GLY ARG ALA LEU VAL GLY GLY
SEQRES 37 P 664 HIS ARG LEU PHE GLU MET LEU LYS GLU GLY LYS VAL ASN
SEQRES 38 P 664 PRO SER PRO TYR MET LYS ILE SER TYR GLU HIS GLY GLY
SEQRES 39 P 664 ALA PHE LEU GLY ASP ILE LEU LEU TYR ASP SER ARG ARG
SEQRES 40 P 664 GLU PRO GLY SER ALA ILE PHE VAL GLY ASN ILE ASN SER
SEQRES 41 P 664 MET LEU ASN ASN GLN PHE SER PRO GLU TYR GLY VAL GLN
SEQRES 42 P 664 SER GLY VAL ARG ASP ARG SER LYS ARG LYS ARG PRO PHE
SEQRES 43 P 664 PRO GLY LEU ALA TRP ALA SER MET LYS ASP THR TYR GLY
SEQRES 44 P 664 ALA CYS PRO ILE TYR SER ASP VAL LEU GLU ALA ILE GLU
SEQRES 45 P 664 ARG CYS TRP TRP ASN ALA PHE GLY GLU SER TYR ARG ALA
SEQRES 46 P 664 TYR ARG GLU ASP MET LEU LYS ARG ASP THR LEU GLU LEU
SEQRES 47 P 664 SER ARG TYR VAL ALA SER MET ALA ARG GLN ALA GLY LEU
SEQRES 48 P 664 ALA GLU LEU THR PRO ILE ASP LEU GLU VAL LEU ALA ASP
SEQRES 49 P 664 PRO ASN LYS LEU GLN TYR LYS TRP THR GLU ALA ASP VAL
SEQRES 50 P 664 SER ALA ASN ILE HIS GLU VAL LEU MET HIS GLY VAL SER
SEQRES 51 P 664 VAL GLU LYS THR GLU ARG PHE LEU ARG SER VAL MET PRO
SEQRES 52 P 664 ARG
SEQRES 1 Q 664 PRO ARG ARG ALA PRO ALA PHE PRO LEU SER ASP ILE LYS
SEQRES 2 Q 664 ALA GLN MET LEU PHE ALA ASN ASN ILE LYS ALA GLN GLN
SEQRES 3 Q 664 ALA SER LYS ARG SER PHE LYS GLU GLY ALA ILE GLU THR
SEQRES 4 Q 664 TYR GLU GLY LEU LEU SER VAL ASP PRO ARG PHE LEU SER
SEQRES 5 Q 664 PHE LYS ASN GLU LEU SER ARG TYR LEU THR ASP HIS PHE
SEQRES 6 Q 664 PRO ALA ASN VAL ASP GLU TYR GLY ARG VAL TYR GLY ASN
SEQRES 7 Q 664 GLY VAL ARG THR ASN PHE PHE GLY MET ARG HIS MET ASN
SEQRES 8 Q 664 GLY PHE PRO MET ILE PRO ALA THR TRP PRO LEU ALA SER
SEQRES 9 Q 664 ASN LEU LYS LYS ARG ALA ASP ALA ASP LEU ALA ASP GLY
SEQRES 10 Q 664 PRO VAL SER GLU ARG ASP ASN LEU LEU PHE ARG ALA ALA
SEQRES 11 Q 664 VAL ARG LEU MET PHE SER ASP LEU GLU PRO VAL PRO LEU
SEQRES 12 Q 664 LYS ILE ARG LYS GLY SER SER THR CYS ILE PRO TYR PHE
SEQRES 13 Q 664 SER ASN ASP MET GLY THR LYS ILE GLU ILE ALA GLU ARG
SEQRES 14 Q 664 ALA LEU GLU LYS ALA GLU GLU ALA GLY ASN LEU MET LEU
SEQRES 15 Q 664 GLN GLY LYS PHE ASP ASP ALA TYR GLN LEU HIS GLN MET
SEQRES 16 Q 664 GLY GLY ALA TYR TYR VAL VAL TYR ARG ALA GLN SER THR
SEQRES 17 Q 664 ASP ALA ILE THR LEU ASP PRO LYS THR GLY LYS PHE VAL
SEQRES 18 Q 664 SER LYS ASP ARG MET VAL ALA ASP PHE GLU TYR ALA VAL
SEQRES 19 Q 664 THR GLY GLY GLU GLN GLY SER LEU PHE ALA ALA SER LYS
SEQRES 20 Q 664 ASP ALA SER ARG LEU LYS GLU GLN TYR GLY ILE ASP VAL
SEQRES 21 Q 664 PRO ASP GLY PHE PHE CYS GLU ARG ARG ARG THR ALA MET
SEQRES 22 Q 664 GLY GLY PRO PHE ALA LEU ASN ALA PRO ILE MET ALA VAL
SEQRES 23 Q 664 ALA GLN PRO VAL ARG ASN LYS ILE TYR SER LYS TYR ALA
SEQRES 24 Q 664 TYR THR PHE HIS HIS THR THR ARG LEU ASN LYS GLU GLU
SEQRES 25 Q 664 LYS VAL LYS GLU TRP SER LEU CYS VAL ALA THR ASP VAL
SEQRES 26 Q 664 SER ASP HIS ASP THR PHE TRP PRO GLY TRP LEU ARG ASP
SEQRES 27 Q 664 LEU ILE CYS ASP GLU LEU LEU ASN MET GLY TYR ALA PRO
SEQRES 28 Q 664 TRP TRP VAL LYS LEU PHE GLU THR SER LEU LYS LEU PRO
SEQRES 29 Q 664 VAL TYR VAL GLY ALA PRO ALA PRO GLU GLN GLY HIS THR
SEQRES 30 Q 664 LEU LEU GLY ASP PRO SER ASN PRO ASP LEU GLU VAL GLY
SEQRES 31 Q 664 LEU SER SER GLY GLN GLY ALA THR ASP LEU MET GLY THR
SEQRES 32 Q 664 LEU LEU MET SER ILE THR TYR LEU VAL MET GLN LEU ASP
SEQRES 33 Q 664 HIS THR ALA PRO HIS LEU ASN SER ARG ILE LYS ASP MET
SEQRES 34 Q 664 PRO SER ALA CYS ARG PHE LEU ASP SER TYR TRP GLN GLY
SEQRES 35 Q 664 HIS GLU GLU ILE ARG GLN ILE SER LYS SER ASP ASP ALA
SEQRES 36 Q 664 MET LEU GLY TRP THR LYS GLY ARG ALA LEU VAL GLY GLY
SEQRES 37 Q 664 HIS ARG LEU PHE GLU MET LEU LYS GLU GLY LYS VAL ASN
SEQRES 38 Q 664 PRO SER PRO TYR MET LYS ILE SER TYR GLU HIS GLY GLY
SEQRES 39 Q 664 ALA PHE LEU GLY ASP ILE LEU LEU TYR ASP SER ARG ARG
SEQRES 40 Q 664 GLU PRO GLY SER ALA ILE PHE VAL GLY ASN ILE ASN SER
SEQRES 41 Q 664 MET LEU ASN ASN GLN PHE SER PRO GLU TYR GLY VAL GLN
SEQRES 42 Q 664 SER GLY VAL ARG ASP ARG SER LYS ARG LYS ARG PRO PHE
SEQRES 43 Q 664 PRO GLY LEU ALA TRP ALA SER MET LYS ASP THR TYR GLY
SEQRES 44 Q 664 ALA CYS PRO ILE TYR SER ASP VAL LEU GLU ALA ILE GLU
SEQRES 45 Q 664 ARG CYS TRP TRP ASN ALA PHE GLY GLU SER TYR ARG ALA
SEQRES 46 Q 664 TYR ARG GLU ASP MET LEU LYS ARG ASP THR LEU GLU LEU
SEQRES 47 Q 664 SER ARG TYR VAL ALA SER MET ALA ARG GLN ALA GLY LEU
SEQRES 48 Q 664 ALA GLU LEU THR PRO ILE ASP LEU GLU VAL LEU ALA ASP
SEQRES 49 Q 664 PRO ASN LYS LEU GLN TYR LYS TRP THR GLU ALA ASP VAL
SEQRES 50 Q 664 SER ALA ASN ILE HIS GLU VAL LEU MET HIS GLY VAL SER
SEQRES 51 Q 664 VAL GLU LYS THR GLU ARG PHE LEU ARG SER VAL MET PRO
SEQRES 52 Q 664 ARG
SEQRES 1 R 664 PRO ARG ARG ALA PRO ALA PHE PRO LEU SER ASP ILE LYS
SEQRES 2 R 664 ALA GLN MET LEU PHE ALA ASN ASN ILE LYS ALA GLN GLN
SEQRES 3 R 664 ALA SER LYS ARG SER PHE LYS GLU GLY ALA ILE GLU THR
SEQRES 4 R 664 TYR GLU GLY LEU LEU SER VAL ASP PRO ARG PHE LEU SER
SEQRES 5 R 664 PHE LYS ASN GLU LEU SER ARG TYR LEU THR ASP HIS PHE
SEQRES 6 R 664 PRO ALA ASN VAL ASP GLU TYR GLY ARG VAL TYR GLY ASN
SEQRES 7 R 664 GLY VAL ARG THR ASN PHE PHE GLY MET ARG HIS MET ASN
SEQRES 8 R 664 GLY PHE PRO MET ILE PRO ALA THR TRP PRO LEU ALA SER
SEQRES 9 R 664 ASN LEU LYS LYS ARG ALA ASP ALA ASP LEU ALA ASP GLY
SEQRES 10 R 664 PRO VAL SER GLU ARG ASP ASN LEU LEU PHE ARG ALA ALA
SEQRES 11 R 664 VAL ARG LEU MET PHE SER ASP LEU GLU PRO VAL PRO LEU
SEQRES 12 R 664 LYS ILE ARG LYS GLY SER SER THR CYS ILE PRO TYR PHE
SEQRES 13 R 664 SER ASN ASP MET GLY THR LYS ILE GLU ILE ALA GLU ARG
SEQRES 14 R 664 ALA LEU GLU LYS ALA GLU GLU ALA GLY ASN LEU MET LEU
SEQRES 15 R 664 GLN GLY LYS PHE ASP ASP ALA TYR GLN LEU HIS GLN MET
SEQRES 16 R 664 GLY GLY ALA TYR TYR VAL VAL TYR ARG ALA GLN SER THR
SEQRES 17 R 664 ASP ALA ILE THR LEU ASP PRO LYS THR GLY LYS PHE VAL
SEQRES 18 R 664 SER LYS ASP ARG MET VAL ALA ASP PHE GLU TYR ALA VAL
SEQRES 19 R 664 THR GLY GLY GLU GLN GLY SER LEU PHE ALA ALA SER LYS
SEQRES 20 R 664 ASP ALA SER ARG LEU LYS GLU GLN TYR GLY ILE ASP VAL
SEQRES 21 R 664 PRO ASP GLY PHE PHE CYS GLU ARG ARG ARG THR ALA MET
SEQRES 22 R 664 GLY GLY PRO PHE ALA LEU ASN ALA PRO ILE MET ALA VAL
SEQRES 23 R 664 ALA GLN PRO VAL ARG ASN LYS ILE TYR SER LYS TYR ALA
SEQRES 24 R 664 TYR THR PHE HIS HIS THR THR ARG LEU ASN LYS GLU GLU
SEQRES 25 R 664 LYS VAL LYS GLU TRP SER LEU CYS VAL ALA THR ASP VAL
SEQRES 26 R 664 SER ASP HIS ASP THR PHE TRP PRO GLY TRP LEU ARG ASP
SEQRES 27 R 664 LEU ILE CYS ASP GLU LEU LEU ASN MET GLY TYR ALA PRO
SEQRES 28 R 664 TRP TRP VAL LYS LEU PHE GLU THR SER LEU LYS LEU PRO
SEQRES 29 R 664 VAL TYR VAL GLY ALA PRO ALA PRO GLU GLN GLY HIS THR
SEQRES 30 R 664 LEU LEU GLY ASP PRO SER ASN PRO ASP LEU GLU VAL GLY
SEQRES 31 R 664 LEU SER SER GLY GLN GLY ALA THR ASP LEU MET GLY THR
SEQRES 32 R 664 LEU LEU MET SER ILE THR TYR LEU VAL MET GLN LEU ASP
SEQRES 33 R 664 HIS THR ALA PRO HIS LEU ASN SER ARG ILE LYS ASP MET
SEQRES 34 R 664 PRO SER ALA CYS ARG PHE LEU ASP SER TYR TRP GLN GLY
SEQRES 35 R 664 HIS GLU GLU ILE ARG GLN ILE SER LYS SER ASP ASP ALA
SEQRES 36 R 664 MET LEU GLY TRP THR LYS GLY ARG ALA LEU VAL GLY GLY
SEQRES 37 R 664 HIS ARG LEU PHE GLU MET LEU LYS GLU GLY LYS VAL ASN
SEQRES 38 R 664 PRO SER PRO TYR MET LYS ILE SER TYR GLU HIS GLY GLY
SEQRES 39 R 664 ALA PHE LEU GLY ASP ILE LEU LEU TYR ASP SER ARG ARG
SEQRES 40 R 664 GLU PRO GLY SER ALA ILE PHE VAL GLY ASN ILE ASN SER
SEQRES 41 R 664 MET LEU ASN ASN GLN PHE SER PRO GLU TYR GLY VAL GLN
SEQRES 42 R 664 SER GLY VAL ARG ASP ARG SER LYS ARG LYS ARG PRO PHE
SEQRES 43 R 664 PRO GLY LEU ALA TRP ALA SER MET LYS ASP THR TYR GLY
SEQRES 44 R 664 ALA CYS PRO ILE TYR SER ASP VAL LEU GLU ALA ILE GLU
SEQRES 45 R 664 ARG CYS TRP TRP ASN ALA PHE GLY GLU SER TYR ARG ALA
SEQRES 46 R 664 TYR ARG GLU ASP MET LEU LYS ARG ASP THR LEU GLU LEU
SEQRES 47 R 664 SER ARG TYR VAL ALA SER MET ALA ARG GLN ALA GLY LEU
SEQRES 48 R 664 ALA GLU LEU THR PRO ILE ASP LEU GLU VAL LEU ALA ASP
SEQRES 49 R 664 PRO ASN LYS LEU GLN TYR LYS TRP THR GLU ALA ASP VAL
SEQRES 50 R 664 SER ALA ASN ILE HIS GLU VAL LEU MET HIS GLY VAL SER
SEQRES 51 R 664 VAL GLU LYS THR GLU ARG PHE LEU ARG SER VAL MET PRO
SEQRES 52 R 664 ARG
HET MN P 665 1
HET MG P 668 1
HET MG P 669 1
HET MN Q 665 1
HET MG Q 668 1
HET MG Q 669 1
HET MN R 665 1
HET MG R 668 1
HET MG R 669 1
HET GTP P 666 32
HET GTP P 667 32
HET GTP Q 666 32
HET GTP Q 667 32
HET GTP R 666 32
HET GTP R 667 32
HETNAM MN MANGANESE (II) ION
HETNAM MG MAGNESIUM ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 7 MN 3(MN 2+)
FORMUL 8 MG 6(MG 2+)
FORMUL 16 GTP 6(C10 H16 N5 O14 P3)
HELIX 1 1 ASP P 11 MET P 16 1 6
HELIX 2 2 ASN P 21 ARG P 30 1 10
HELIX 3 3 ASP P 47 PHE P 65 1 19
HELIX 4 4 PHE P 84 MET P 87 5 4
HELIX 5 5 ASN P 105 ALA P 112 1 8
HELIX 6 6 SER P 120 PHE P 135 1 16
HELIX 7 7 ASP P 159 GLN P 183 1 25
HELIX 8 8 LYS P 185 GLN P 194 1 10
HELIX 9 9 ASP P 229 THR P 235 1 7
HELIX 10 10 SER P 250 GLY P 257 1 8
HELIX 11 11 PRO P 276 TYR P 298 1 23
HELIX 12 12 TYR P 298 HIS P 303 1 6
HELIX 13 13 THR P 306 GLU P 316 1 11
HELIX 14 14 ASP P 327 TRP P 332 1 6
HELIX 15 15 PRO P 333 MET P 347 1 15
HELIX 16 16 ALA P 350 LEU P 361 1 12
HELIX 17 17 ALA P 397 ALA P 419 1 23
HELIX 18 18 PRO P 420 ILE P 426 5 7
HELIX 19 19 ASP P 428 GLN P 441 1 14
HELIX 20 20 GLY P 462 GLY P 478 1 17
HELIX 21 21 GLU P 508 ALA P 512 5 5
HELIX 22 22 ASN P 517 SER P 527 1 11
HELIX 23 23 ASP P 538 ARG P 542 5 5
HELIX 24 24 PHE P 546 GLY P 548 5 3
HELIX 25 25 LEU P 549 GLY P 559 1 11
HELIX 26 26 ILE P 563 GLY P 580 1 18
HELIX 27 27 SER P 582 ARG P 600 1 19
HELIX 28 28 THR P 615 ASP P 624 1 10
HELIX 29 29 PRO P 625 GLN P 629 5 5
HELIX 30 30 THR P 633 VAL P 637 5 5
HELIX 31 31 SER P 638 LEU P 645 1 8
HELIX 32 32 SER P 650 MET P 662 1 13
HELIX 33 33 ASP Q 11 MET Q 16 1 6
HELIX 34 34 ASN Q 21 ARG Q 30 1 10
HELIX 35 35 ASP Q 47 PHE Q 65 1 19
HELIX 36 36 PHE Q 84 MET Q 87 5 4
HELIX 37 37 ASN Q 105 ALA Q 112 1 8
HELIX 38 38 SER Q 120 PHE Q 135 1 16
HELIX 39 39 ASP Q 159 GLN Q 183 1 25
HELIX 40 40 LYS Q 185 GLN Q 194 1 10
HELIX 41 41 ASP Q 229 THR Q 235 1 7
HELIX 42 42 SER Q 250 GLY Q 257 1 8
HELIX 43 43 PRO Q 276 TYR Q 298 1 23
HELIX 44 44 TYR Q 298 HIS Q 303 1 6
HELIX 45 45 THR Q 306 GLU Q 316 1 11
HELIX 46 46 ASP Q 327 TRP Q 332 1 6
HELIX 47 47 PRO Q 333 MET Q 347 1 15
HELIX 48 48 ALA Q 350 LEU Q 361 1 12
HELIX 49 49 ALA Q 397 ALA Q 419 1 23
HELIX 50 50 PRO Q 420 ILE Q 426 5 7
HELIX 51 51 ASP Q 428 GLN Q 441 1 14
HELIX 52 52 GLY Q 462 GLY Q 478 1 17
HELIX 53 53 GLU Q 508 ALA Q 512 5 5
HELIX 54 54 ASN Q 517 SER Q 527 1 11
HELIX 55 55 ASP Q 538 ARG Q 542 5 5
HELIX 56 56 PHE Q 546 GLY Q 548 5 3
HELIX 57 57 LEU Q 549 GLY Q 559 1 11
HELIX 58 58 ILE Q 563 GLY Q 580 1 18
HELIX 59 59 SER Q 582 ARG Q 600 1 19
HELIX 60 60 THR Q 615 ASP Q 624 1 10
HELIX 61 61 PRO Q 625 GLN Q 629 5 5
HELIX 62 62 THR Q 633 VAL Q 637 5 5
HELIX 63 63 SER Q 638 LEU Q 645 1 8
HELIX 64 64 SER Q 650 MET Q 662 1 13
HELIX 65 65 ASP R 11 MET R 16 1 6
HELIX 66 66 ASN R 21 ARG R 30 1 10
HELIX 67 67 ASP R 47 PHE R 65 1 19
HELIX 68 68 PHE R 84 MET R 87 5 4
HELIX 69 69 ASN R 105 ALA R 112 1 8
HELIX 70 70 SER R 120 PHE R 135 1 16
HELIX 71 71 ASP R 159 GLN R 183 1 25
HELIX 72 72 LYS R 185 GLN R 194 1 10
HELIX 73 73 ASP R 229 THR R 235 1 7
HELIX 74 74 SER R 250 GLY R 257 1 8
HELIX 75 75 PRO R 276 TYR R 298 1 23
HELIX 76 76 TYR R 298 HIS R 303 1 6
HELIX 77 77 THR R 306 GLU R 316 1 11
HELIX 78 78 ASP R 327 TRP R 332 1 6
HELIX 79 79 PRO R 333 MET R 347 1 15
HELIX 80 80 ALA R 350 LEU R 361 1 12
HELIX 81 81 ALA R 397 ALA R 419 1 23
HELIX 82 82 PRO R 420 ILE R 426 5 7
HELIX 83 83 ASP R 428 GLN R 441 1 14
HELIX 84 84 GLY R 462 GLY R 478 1 17
HELIX 85 85 GLU R 508 ALA R 512 5 5
HELIX 86 86 ASN R 517 SER R 527 1 11
HELIX 87 87 ASP R 538 ARG R 542 5 5
HELIX 88 88 PHE R 546 GLY R 548 5 3
HELIX 89 89 LEU R 549 GLY R 559 1 11
HELIX 90 90 ILE R 563 GLY R 580 1 18
HELIX 91 91 SER R 582 ARG R 600 1 19
HELIX 92 92 THR R 615 ASP R 624 1 10
HELIX 93 93 PRO R 625 GLN R 629 5 5
HELIX 94 94 THR R 633 VAL R 637 5 5
HELIX 95 95 SER R 638 LEU R 645 1 8
HELIX 96 96 SER R 650 MET R 662 1 13
SHEET 1 PA 5 ALA P 6 PRO P 8 0
SHEET 2 PA 5 THR P 377 LEU P 379 -1 O LEU P 378 N PHE P 7
SHEET 3 PA 5 VAL P 365 VAL P 367 -1 O VAL P 365 N LEU P 379
SHEET 4 PA 5 TYR P 199 VAL P 202 1 O TYR P 199 N TYR P 366
SHEET 5 PA 5 ALA P 272 GLY P 274 -1 O ALA P 272 N VAL P 202
SHEET 1 PB 2 GLU P 38 TYR P 40 0
SHEET 2 PB 2 LEU P 43 LEU P 44 -1 O LEU P 43 N TYR P 40
SHEET 1 PC 3 HIS P 89 PRO P 94 0
SHEET 2 PC 3 PHE P 265 ARG P 269 1 O PHE P 265 N MET P 90
SHEET 3 PC 3 ALA P 205 GLN P 206 -1 O GLN P 206 N ARG P 268
SHEET 1 PD 2 ILE P 145 ARG P 146 0
SHEET 2 PD 2 MET P 646 HIS P 647 -1 O HIS P 647 N ILE P 145
SHEET 1 PE 2 ILE P 211 LEU P 213 0
SHEET 2 PE 2 PHE P 220 SER P 222 -1 O VAL P 221 N THR P 212
SHEET 1 PF 2 MET P 226 ALA P 228 0
SHEET 2 PF 2 LEU P 242 ALA P 244 -1 O PHE P 243 N VAL P 227
SHEET 1 PG 4 ILE P 446 LYS P 451 0
SHEET 2 PG 4 ASP P 454 TRP P 459 -1 O ASP P 454 N LYS P 451
SHEET 3 PG 4 LEU P 319 VAL P 325 -1 O LEU P 319 N TRP P 459
SHEET 4 PG 4 ILE P 488 TYR P 490 -1 O SER P 489 N ASP P 324
SHEET 1 PH 3 ALA P 495 PHE P 496 0
SHEET 2 PH 3 ASP P 499 LEU P 502 -1 O ASP P 499 N PHE P 496
SHEET 3 PH 3 ILE P 513 GLY P 516 -1 O ILE P 513 N LEU P 502
SHEET 1 QA 5 ALA Q 6 PRO Q 8 0
SHEET 2 QA 5 THR Q 377 LEU Q 379 -1 O LEU Q 378 N PHE Q 7
SHEET 3 QA 5 VAL Q 365 VAL Q 367 -1 O VAL Q 365 N LEU Q 379
SHEET 4 QA 5 TYR Q 199 VAL Q 202 1 O TYR Q 199 N TYR Q 366
SHEET 5 QA 5 ALA Q 272 GLY Q 274 -1 O ALA Q 272 N VAL Q 202
SHEET 1 QB 2 GLU Q 38 TYR Q 40 0
SHEET 2 QB 2 LEU Q 43 LEU Q 44 -1 O LEU Q 43 N TYR Q 40
SHEET 1 QC 3 HIS Q 89 PRO Q 94 0
SHEET 2 QC 3 PHE Q 265 ARG Q 269 1 O PHE Q 265 N MET Q 90
SHEET 3 QC 3 ALA Q 205 GLN Q 206 -1 O GLN Q 206 N ARG Q 268
SHEET 1 QD 2 ILE Q 145 ARG Q 146 0
SHEET 2 QD 2 MET Q 646 HIS Q 647 -1 O HIS Q 647 N ILE Q 145
SHEET 1 QE 2 ILE Q 211 LEU Q 213 0
SHEET 2 QE 2 PHE Q 220 SER Q 222 -1 O VAL Q 221 N THR Q 212
SHEET 1 QF 2 MET Q 226 ALA Q 228 0
SHEET 2 QF 2 LEU Q 242 ALA Q 244 -1 O PHE Q 243 N VAL Q 227
SHEET 1 QG 4 ILE Q 446 LYS Q 451 0
SHEET 2 QG 4 ASP Q 454 TRP Q 459 -1 O ASP Q 454 N LYS Q 451
SHEET 3 QG 4 LEU Q 319 VAL Q 325 -1 O LEU Q 319 N TRP Q 459
SHEET 4 QG 4 ILE Q 488 TYR Q 490 -1 O SER Q 489 N ASP Q 324
SHEET 1 QH 3 ALA Q 495 PHE Q 496 0
SHEET 2 QH 3 ASP Q 499 LEU Q 502 -1 O ASP Q 499 N PHE Q 496
SHEET 3 QH 3 ILE Q 513 GLY Q 516 -1 O ILE Q 513 N LEU Q 502
SHEET 1 RA 5 ALA R 6 PRO R 8 0
SHEET 2 RA 5 THR R 377 LEU R 379 -1 O LEU R 378 N PHE R 7
SHEET 3 RA 5 VAL R 365 VAL R 367 -1 O VAL R 365 N LEU R 379
SHEET 4 RA 5 TYR R 199 VAL R 202 1 O TYR R 199 N TYR R 366
SHEET 5 RA 5 ALA R 272 GLY R 274 -1 O ALA R 272 N VAL R 202
SHEET 1 RB 2 GLU R 38 TYR R 40 0
SHEET 2 RB 2 LEU R 43 LEU R 44 -1 O LEU R 43 N TYR R 40
SHEET 1 RC 3 HIS R 89 PRO R 94 0
SHEET 2 RC 3 PHE R 265 ARG R 269 1 O PHE R 265 N MET R 90
SHEET 3 RC 3 ALA R 205 GLN R 206 -1 O GLN R 206 N ARG R 268
SHEET 1 RD 2 ILE R 145 ARG R 146 0
SHEET 2 RD 2 MET R 646 HIS R 647 -1 O HIS R 647 N ILE R 145
SHEET 1 RE 2 ILE R 211 LEU R 213 0
SHEET 2 RE 2 PHE R 220 SER R 222 -1 O VAL R 221 N THR R 212
SHEET 1 RF 2 MET R 226 ALA R 228 0
SHEET 2 RF 2 LEU R 242 ALA R 244 -1 O PHE R 243 N VAL R 227
SHEET 1 RG 4 ILE R 446 LYS R 451 0
SHEET 2 RG 4 ASP R 454 TRP R 459 -1 O ASP R 454 N LYS R 451
SHEET 3 RG 4 LEU R 319 VAL R 325 -1 O LEU R 319 N TRP R 459
SHEET 4 RG 4 ILE R 488 TYR R 490 -1 O SER R 489 N ASP R 324
SHEET 1 RH 3 ALA R 495 PHE R 496 0
SHEET 2 RH 3 ASP R 499 LEU R 502 -1 O ASP R 499 N PHE R 496
SHEET 3 RH 3 ILE R 513 GLY R 516 -1 O ILE R 513 N LEU R 502
LINK MN MN P 665 OD1 ASP P 454 1555 1555 1.93
LINK MN MN P 665 OE1 GLU P 491 1555 1555 1.90
LINK MN MN P 665 O ALA P 495 1555 1555 2.20
LINK MG MG P 668 O VAL P 325 1555 1555 2.87
LINK MG MG P 668 OD1 ASP P 453 1555 1555 2.69
LINK MG MG P 668 O2B GTP P 667 1555 1555 3.04
LINK MG MG P 668 O2G GTP P 667 1555 1555 3.14
LINK MG MG P 669 O1A GTP P 667 1555 1555 2.55
LINK MG MG P 669 O2G GTP P 667 1555 1555 2.94
LINK MN MN Q 665 OE1 GLU Q 491 1555 1555 1.90
LINK MN MN Q 665 O ALA Q 495 1555 1555 2.20
LINK MN MN Q 665 OD1 ASP Q 454 1555 1555 1.93
LINK MG MG Q 668 O2G GTP Q 667 1555 1555 3.14
LINK MG MG Q 668 O VAL Q 325 1555 1555 2.87
LINK MG MG Q 668 O2B GTP Q 667 1555 1555 3.04
LINK MG MG Q 668 OD1 ASP Q 453 1555 1555 2.69
LINK MG MG Q 669 O1A GTP Q 667 1555 1555 2.55
LINK MG MG Q 669 O2G GTP Q 667 1555 1555 2.94
LINK MN MN R 665 O ALA R 495 1555 1555 2.20
LINK MN MN R 665 OE1 GLU R 491 1555 1555 1.90
LINK MN MN R 665 OD1 ASP R 454 1555 1555 1.93
LINK MG MG R 668 OD1 ASP R 453 1555 1555 2.69
LINK MG MG R 668 O2G GTP R 667 1555 1555 3.14
LINK MG MG R 668 O2B GTP R 667 1555 1555 3.04
LINK MG MG R 668 O VAL R 325 1555 1555 2.87
LINK MG MG R 669 O1A GTP R 667 1555 1555 2.55
LINK MG MG R 669 O2G GTP R 667 1555 1555 2.94
CISPEP 1 ILE P 96 PRO P 97 0 -0.32
CISPEP 2 ILE P 153 PRO P 154 0 0.26
CISPEP 3 ILE Q 96 PRO Q 97 0 -0.40
CISPEP 4 ILE Q 153 PRO Q 154 0 0.23
CISPEP 5 ILE R 96 PRO R 97 0 -0.29
CISPEP 6 ILE R 153 PRO R 154 0 0.28
SITE 1 AC1 3 ASP P 454 GLU P 491 ALA P 495
SITE 1 AC2 3 VAL P 325 ASP P 453 GTP P 667
SITE 1 AC3 2 GTP P 666 GTP P 667
SITE 1 AC4 3 ASP Q 454 GLU Q 491 ALA Q 495
SITE 1 AC5 3 VAL Q 325 ASP Q 453 GTP Q 667
SITE 1 AC6 2 GTP Q 666 GTP Q 667
SITE 1 AC7 3 ASP R 454 GLU R 491 ALA R 495
SITE 1 AC8 3 VAL R 325 ASP R 453 GTP R 667
SITE 1 AC9 2 GTP R 666 GTP R 667
SITE 1 BC1 9 DC D 6 ARG P 204 GLN P 206 GLU P 529
SITE 2 BC1 9 ASN P 626 GLN P 629 TYR P 630 GTP P 667
SITE 3 BC1 9 MG P 669
SITE 1 BC2 14 DC D 5 DC D 6 ARG P 204 ARG P 268
SITE 2 BC2 14 ARG P 270 ASP P 327 HIS P 328 ASP P 329
SITE 3 BC2 14 SER P 393 SER P 452 ASP P 453 GTP P 666
SITE 4 BC2 14 MG P 668 MG P 669
SITE 1 BC3 9 DC E 6 ARG Q 204 GLN Q 206 GLU Q 529
SITE 2 BC3 9 ASN Q 626 GLN Q 629 TYR Q 630 GTP Q 667
SITE 3 BC3 9 MG Q 669
SITE 1 BC4 14 DC E 5 DC E 6 ARG Q 204 ARG Q 268
SITE 2 BC4 14 ARG Q 270 ASP Q 327 HIS Q 328 ASP Q 329
SITE 3 BC4 14 SER Q 393 SER Q 452 ASP Q 453 GTP Q 666
SITE 4 BC4 14 MG Q 668 MG Q 669
SITE 1 BC5 9 DC F 6 ARG R 204 GLN R 206 GLU R 529
SITE 2 BC5 9 ASN R 626 GLN R 629 TYR R 630 GTP R 667
SITE 3 BC5 9 MG R 669
SITE 1 BC6 14 DC F 5 DC F 6 ARG R 204 ARG R 268
SITE 2 BC6 14 ARG R 270 ASP R 327 HIS R 328 ASP R 329
SITE 3 BC6 14 SER R 393 SER R 452 ASP R 453 GTP R 666
SITE 4 BC6 14 MG R 668 MG R 669
CRYST1 105.650 92.700 140.790 90.00 101.09 90.00 P 1 21 1 6
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 0.009465 0.000000 0.001855 0.00000
SCALE2 0.000000 0.010787 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007238 0.00000
MTRIX1 1 0.130680 -0.715960 -0.685800 77.14216 1
MTRIX2 1 -0.788650 -0.494250 0.365710 17.38792 1
MTRIX3 1 -0.600790 0.493070 -0.629240 79.71372 1
MTRIX1 2 -0.166000 -0.755310 0.634000 -59.16780 1
MTRIX2 2 0.780190 -0.493800 -0.384010 6.30318 1
MTRIX3 2 0.603120 0.430890 0.671250 -28.45492 1
(ATOM LINES ARE NOT SHOWN.)
END
