HEADER TRANSFERASE 17-SEP-10 3OWG
TITLE CRYSTAL STRUCTURE OF VACCINIA VIRUS POLYADENYLATE POLYMERASE(VP55)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(A) POLYMERASE CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POLY(A) POLYMERASE LARGE SUBUNIT, PAP-L, VP55;
COMPND 5 EC: 2.7.7.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS WR;
SOURCE 3 ORGANISM_COMMON: VACV;
SOURCE 4 ORGANISM_TAXID: 10254;
SOURCE 5 STRAIN: WESTERN RESERVE;
SOURCE 6 GENE: PAPL, VACWR057, E1L;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-15B;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPG198
KEYWDS RNA POLYADENYLATE POLYMERASE COMPLEX, TRANSLOCATION, POLYADENYLATE
KEYWDS 2 POLYMERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.LI,H.LI,S.ZHOU,P.D.GERSHON,T.L.POULOS
REVDAT 5 06-SEP-23 3OWG 1 SEQADV
REVDAT 4 08-NOV-17 3OWG 1 REMARK
REVDAT 3 03-APR-13 3OWG 1 JRNL
REVDAT 2 27-MAR-13 3OWG 1
REVDAT 1 21-SEP-11 3OWG 0
JRNL AUTH H.LI,C.LI,S.ZHOU,T.L.POULOS,P.D.GERSHON
JRNL TITL DOMAIN-LEVEL ROCKING MOTION WITHIN A POLYMERASE THAT
JRNL TITL 2 TRANSLOCATES ON SINGLE-STRANDED NUCLEIC ACID.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 617 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 23519670
JRNL DOI 10.1107/S0907444913000346
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.M.MOURE,B.R.BOWMAN,P.D.GERSHON,F.A.QUIOCHO
REMARK 1 TITL CRYSTAL STRUCTURES OF THE VACCINIA VIRUS POLYADENYLATE
REMARK 1 TITL 2 POLYMERASE HETERODIMER: INSIGHTS INTO ATP SELECTIVITY AND
REMARK 1 TITL 3 PROCESSIVITY.
REMARK 1 REF MOL.CELL V. 22 339 2006
REMARK 1 REFN ISSN 1097-2765
REMARK 1 PMID 16678106
REMARK 1 DOI 10.1016/J.MOLCEL.2006.03.015
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.LI,H.LI,S.ZHOU,E.SUN,J.YOSHIZAWA,T.L.POULOS,P.D.GERSHON
REMARK 1 TITL POLYMERASE TRANSLOCATION WITH RESPECT TO SINGLE-STRANDED
REMARK 1 TITL 2 NUCLEIC ACID: LOOPING OR WRAPPING OF PRIMER AROUND A POLY(A)
REMARK 1 TITL 3 POLYMERASE.
REMARK 1 REF STRUCTURE V. 17 680 2009
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 19446524
REMARK 1 DOI 10.1016/J.STR.2009.03.012
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1227549.900
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 29693
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) : 0.253
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1465
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4153
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 222
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7436
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 14.93000
REMARK 3 B22 (A**2) : -12.17000
REMARK 3 B33 (A**2) : -2.76000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.46
REMARK 3 ESD FROM SIGMAA (A) : 0.57
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.59
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.67
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 67.83
REMARK 3
REMARK 3 NCS MODEL : RESTRAINT
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 3 THE NCS RESTRAINTS (WEIGHT=100)WAS IMPOSED DURING REFINEMENTS
REMARK 4
REMARK 4 3OWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9760
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29731
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.57700
REMARK 200 R SYM FOR SHELL (I) : 0.57700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 2GA9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-16%PEG 3350,200MM NA-CITATE, 5%
REMARK 280 GLYCERO, 1MM DTT, PH ~9, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.06400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.06400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 80.64500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ARG A 3
REMARK 465 ASN A 4
REMARK 465 PRO A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 ASN A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 ILE A 150
REMARK 465 ASP A 151
REMARK 465 LYS A 152
REMARK 465 ALA A 153
REMARK 465 LYS A 154
REMARK 465 VAL A 155
REMARK 465 MET A 156
REMARK 465 GLY A 157
REMARK 465 ARG A 158
REMARK 465 HIS A 159
REMARK 465 ASN A 160
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ARG B 3
REMARK 465 ASN B 4
REMARK 465 PRO B 5
REMARK 465 ASP B 6
REMARK 465 GLN B 7
REMARK 465 ASN B 8
REMARK 465 THR B 9
REMARK 465 LEU B 10
REMARK 465 PRO B 11
REMARK 465 ILE B 150
REMARK 465 ASP B 151
REMARK 465 LYS B 152
REMARK 465 ALA B 153
REMARK 465 LYS B 154
REMARK 465 VAL B 155
REMARK 465 MET B 156
REMARK 465 GLY B 157
REMARK 465 ARG B 158
REMARK 465 HIS B 159
REMARK 465 ASN B 160
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 SER A 124 CB SER A 124 OG 0.115
REMARK 500 SER B 124 CB SER B 124 OG 0.143
REMARK 500 SER B 125 CB SER B 125 OG 0.078
REMARK 500 CYS B 185 CB CYS B 185 SG -0.110
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 PRO B 235 C - N - CA ANGL. DEV. = 9.1 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 SER A 65 -17.50 -48.26
REMARK 500 ASP A 66 35.97 -88.58
REMARK 500 ASN A 68 92.07 -68.99
REMARK 500 ALA A 71 10.15 -65.67
REMARK 500 GLN A 87 30.67 -84.70
REMARK 500 LYS A 126 168.15 56.41
REMARK 500 VAL A 131 44.66 -68.07
REMARK 500 ASN A 146 85.94 -61.83
REMARK 500 ILE A 224 -75.89 -66.79
REMARK 500 SER A 254 144.94 -178.74
REMARK 500 ASP A 271 65.93 28.52
REMARK 500 GLN A 291 105.05 -58.55
REMARK 500 ILE A 292 -29.91 -39.83
REMARK 500 ARG A 328 -141.05 43.15
REMARK 500 ASN A 329 -127.76 -141.96
REMARK 500 ASN A 330 -0.51 70.28
REMARK 500 MET A 333 -159.33 -78.52
REMARK 500 ARG A 342 73.86 39.02
REMARK 500 VAL A 344 79.40 -158.32
REMARK 500 LYS A 349 -35.67 -35.12
REMARK 500 ASP A 350 -73.83 -66.44
REMARK 500 LYS A 355 -79.71 -40.13
REMARK 500 ASN A 374 -58.11 71.26
REMARK 500 ALA A 375 99.85 -52.09
REMARK 500 THR A 377 59.36 -154.57
REMARK 500 GLU A 382 -130.69 48.09
REMARK 500 SER A 401 32.79 -96.65
REMARK 500 SER A 432 16.03 80.69
REMARK 500 TYR A 435 -12.41 -159.02
REMARK 500 HIS A 467 32.73 -65.91
REMARK 500 SER B 27 178.72 -54.74
REMARK 500 ASP B 66 31.81 -82.23
REMARK 500 ASN B 68 91.69 -69.30
REMARK 500 ALA B 71 10.65 -63.40
REMARK 500 GLN B 87 32.40 -83.01
REMARK 500 ASN B 121 109.83 -24.89
REMARK 500 SER B 124 108.20 -30.43
REMARK 500 LYS B 126 -0.47 -151.21
REMARK 500 VAL B 131 39.66 -72.24
REMARK 500 ASN B 146 83.02 -67.52
REMARK 500 ALA B 148 -167.18 -78.85
REMARK 500 SER B 188 -67.34 -29.71
REMARK 500 ILE B 224 -74.98 -63.48
REMARK 500 ILE B 251 -62.99 -109.35
REMARK 500 SER B 254 144.67 179.13
REMARK 500 ASP B 271 67.22 22.24
REMARK 500 GLN B 291 108.79 -59.83
REMARK 500 LYS B 327 73.16 -59.57
REMARK 500 ARG B 328 -135.07 39.81
REMARK 500 ASN B 329 -53.63 -122.79
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 TYR B 89 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GA9 RELATED DB: PDB
REMARK 900 RELATED ID: 3ER9 RELATED DB: PDB
REMARK 900 RELATED ID: 3ER8 RELATED DB: PDB
REMARK 900 RELATED ID: 3ERC RELATED DB: PDB
DBREF 3OWG A 1 479 UNP P23371 PAP1_VACCW 1 479
DBREF 3OWG B 1 479 UNP P23371 PAP1_VACCW 1 479
SEQADV 3OWG HIS A -5 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS A -4 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS A -3 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS A -2 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS A -1 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS A 0 UNP P23371 EXPRESSION TAG
SEQADV 3OWG SER A 36 UNP P23371 LEU 36 ENGINEERED MUTATION
SEQADV 3OWG HIS B -5 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS B -4 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS B -3 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS B -2 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS B -1 UNP P23371 EXPRESSION TAG
SEQADV 3OWG HIS B 0 UNP P23371 EXPRESSION TAG
SEQADV 3OWG SER B 36 UNP P23371 LEU 36 ENGINEERED MUTATION
SEQRES 1 A 485 HIS HIS HIS HIS HIS HIS MET ASN ARG ASN PRO ASP GLN
SEQRES 2 A 485 ASN THR LEU PRO ASN ILE THR LEU LYS ILE ILE GLU THR
SEQRES 3 A 485 TYR LEU GLY ARG VAL PRO SER VAL ASN GLU TYR HIS MET
SEQRES 4 A 485 LEU LYS SER GLN ALA ARG ASN ILE GLN LYS ILE THR VAL
SEQRES 5 A 485 PHE ASN LYS ASP ILE PHE VAL SER LEU VAL LYS LYS ASN
SEQRES 6 A 485 LYS LYS ARG PHE PHE SER ASP VAL ASN THR SER ALA SER
SEQRES 7 A 485 GLU ILE LYS ASP ARG ILE LEU SER TYR PHE SER LYS GLN
SEQRES 8 A 485 THR GLN THR TYR ASN ILE GLY LYS LEU PHE THR ILE ILE
SEQRES 9 A 485 GLU LEU GLN SER VAL LEU VAL THR THR TYR THR ASP ILE
SEQRES 10 A 485 LEU GLY VAL LEU THR ILE LYS ALA PRO ASN VAL ILE SER
SEQRES 11 A 485 SER LYS ILE SER TYR ASN VAL THR SER MET GLU GLU LEU
SEQRES 12 A 485 ALA ARG ASP MET LEU ASN SER MET ASN VAL ALA VAL ILE
SEQRES 13 A 485 ASP LYS ALA LYS VAL MET GLY ARG HIS ASN VAL SER SER
SEQRES 14 A 485 LEU VAL LYS ASN VAL ASN LYS LEU MET GLU GLU TYR LEU
SEQRES 15 A 485 ARG ARG HIS ASN LYS SER CYS ILE CYS TYR GLY SER TYR
SEQRES 16 A 485 SER LEU TYR LEU ILE ASN PRO ASN ILE ARG TYR GLY ASP
SEQRES 17 A 485 ILE ASP ILE LEU GLN THR ASN SER ARG THR PHE LEU ILE
SEQRES 18 A 485 ASP LEU ALA PHE LEU ILE LYS PHE ILE THR GLY ASN ASN
SEQRES 19 A 485 ILE ILE LEU SER LYS ILE PRO TYR LEU ARG ASN TYR MET
SEQRES 20 A 485 VAL ILE LYS ASP GLU ASN ASP ASN HIS ILE ILE ASP SER
SEQRES 21 A 485 PHE ASN ILE ARG GLN ASP THR MET ASN VAL VAL PRO LYS
SEQRES 22 A 485 ILE PHE ILE ASP ASN ILE TYR ILE VAL ASP PRO THR PHE
SEQRES 23 A 485 GLN LEU LEU ASN MET ILE LYS MET PHE SER GLN ILE ASP
SEQRES 24 A 485 ARG LEU GLU ASP LEU SER LYS ASP PRO GLU LYS PHE ASN
SEQRES 25 A 485 ALA ARG MET ALA THR MET LEU GLU TYR VAL ARG TYR THR
SEQRES 26 A 485 HIS GLY ILE VAL PHE ASP GLY LYS ARG ASN ASN MET PRO
SEQRES 27 A 485 MET LYS CYS ILE ILE ASP GLU ASN ASN ARG ILE VAL THR
SEQRES 28 A 485 VAL THR THR LYS ASP TYR PHE SER PHE LYS LYS CYS LEU
SEQRES 29 A 485 VAL TYR LEU ASP GLU ASN VAL LEU SER SER ASP ILE LEU
SEQRES 30 A 485 ASP LEU ASN ALA ASP THR SER CYS ASP PHE GLU SER VAL
SEQRES 31 A 485 THR ASN SER VAL TYR LEU ILE HIS ASP ASN ILE MET TYR
SEQRES 32 A 485 THR TYR PHE SER ASN THR ILE LEU LEU SER ASP LYS GLY
SEQRES 33 A 485 LYS VAL HIS GLU ILE SER ALA ARG GLY LEU CYS ALA HIS
SEQRES 34 A 485 ILE LEU LEU TYR GLN MET LEU THR SER GLY GLU TYR LYS
SEQRES 35 A 485 GLN CYS LEU SER ASP LEU LEU ASN SER MET MET ASN ARG
SEQRES 36 A 485 ASP LYS ILE PRO ILE TYR SER HIS THR GLU ARG ASP LYS
SEQRES 37 A 485 LYS PRO GLY ARG HIS GLY PHE ILE ASN ILE GLU LYS ASP
SEQRES 38 A 485 ILE ILE VAL PHE
SEQRES 1 B 485 HIS HIS HIS HIS HIS HIS MET ASN ARG ASN PRO ASP GLN
SEQRES 2 B 485 ASN THR LEU PRO ASN ILE THR LEU LYS ILE ILE GLU THR
SEQRES 3 B 485 TYR LEU GLY ARG VAL PRO SER VAL ASN GLU TYR HIS MET
SEQRES 4 B 485 LEU LYS SER GLN ALA ARG ASN ILE GLN LYS ILE THR VAL
SEQRES 5 B 485 PHE ASN LYS ASP ILE PHE VAL SER LEU VAL LYS LYS ASN
SEQRES 6 B 485 LYS LYS ARG PHE PHE SER ASP VAL ASN THR SER ALA SER
SEQRES 7 B 485 GLU ILE LYS ASP ARG ILE LEU SER TYR PHE SER LYS GLN
SEQRES 8 B 485 THR GLN THR TYR ASN ILE GLY LYS LEU PHE THR ILE ILE
SEQRES 9 B 485 GLU LEU GLN SER VAL LEU VAL THR THR TYR THR ASP ILE
SEQRES 10 B 485 LEU GLY VAL LEU THR ILE LYS ALA PRO ASN VAL ILE SER
SEQRES 11 B 485 SER LYS ILE SER TYR ASN VAL THR SER MET GLU GLU LEU
SEQRES 12 B 485 ALA ARG ASP MET LEU ASN SER MET ASN VAL ALA VAL ILE
SEQRES 13 B 485 ASP LYS ALA LYS VAL MET GLY ARG HIS ASN VAL SER SER
SEQRES 14 B 485 LEU VAL LYS ASN VAL ASN LYS LEU MET GLU GLU TYR LEU
SEQRES 15 B 485 ARG ARG HIS ASN LYS SER CYS ILE CYS TYR GLY SER TYR
SEQRES 16 B 485 SER LEU TYR LEU ILE ASN PRO ASN ILE ARG TYR GLY ASP
SEQRES 17 B 485 ILE ASP ILE LEU GLN THR ASN SER ARG THR PHE LEU ILE
SEQRES 18 B 485 ASP LEU ALA PHE LEU ILE LYS PHE ILE THR GLY ASN ASN
SEQRES 19 B 485 ILE ILE LEU SER LYS ILE PRO TYR LEU ARG ASN TYR MET
SEQRES 20 B 485 VAL ILE LYS ASP GLU ASN ASP ASN HIS ILE ILE ASP SER
SEQRES 21 B 485 PHE ASN ILE ARG GLN ASP THR MET ASN VAL VAL PRO LYS
SEQRES 22 B 485 ILE PHE ILE ASP ASN ILE TYR ILE VAL ASP PRO THR PHE
SEQRES 23 B 485 GLN LEU LEU ASN MET ILE LYS MET PHE SER GLN ILE ASP
SEQRES 24 B 485 ARG LEU GLU ASP LEU SER LYS ASP PRO GLU LYS PHE ASN
SEQRES 25 B 485 ALA ARG MET ALA THR MET LEU GLU TYR VAL ARG TYR THR
SEQRES 26 B 485 HIS GLY ILE VAL PHE ASP GLY LYS ARG ASN ASN MET PRO
SEQRES 27 B 485 MET LYS CYS ILE ILE ASP GLU ASN ASN ARG ILE VAL THR
SEQRES 28 B 485 VAL THR THR LYS ASP TYR PHE SER PHE LYS LYS CYS LEU
SEQRES 29 B 485 VAL TYR LEU ASP GLU ASN VAL LEU SER SER ASP ILE LEU
SEQRES 30 B 485 ASP LEU ASN ALA ASP THR SER CYS ASP PHE GLU SER VAL
SEQRES 31 B 485 THR ASN SER VAL TYR LEU ILE HIS ASP ASN ILE MET TYR
SEQRES 32 B 485 THR TYR PHE SER ASN THR ILE LEU LEU SER ASP LYS GLY
SEQRES 33 B 485 LYS VAL HIS GLU ILE SER ALA ARG GLY LEU CYS ALA HIS
SEQRES 34 B 485 ILE LEU LEU TYR GLN MET LEU THR SER GLY GLU TYR LYS
SEQRES 35 B 485 GLN CYS LEU SER ASP LEU LEU ASN SER MET MET ASN ARG
SEQRES 36 B 485 ASP LYS ILE PRO ILE TYR SER HIS THR GLU ARG ASP LYS
SEQRES 37 B 485 LYS PRO GLY ARG HIS GLY PHE ILE ASN ILE GLU LYS ASP
SEQRES 38 B 485 ILE ILE VAL PHE
HELIX 1 1 ASN A 12 GLY A 23 1 12
HELIX 2 2 SER A 27 LYS A 35 1 9
HELIX 3 3 GLN A 37 PHE A 47 1 11
HELIX 4 4 ASN A 48 PHE A 64 1 17
HELIX 5 5 SER A 72 PHE A 82 1 11
HELIX 6 6 ASN A 90 LEU A 112 1 23
HELIX 7 7 GLY A 113 ILE A 117 5 5
HELIX 8 8 THR A 132 ASN A 146 1 15
HELIX 9 9 LEU A 164 HIS A 179 1 16
HELIX 10 10 GLY A 187 LEU A 193 1 7
HELIX 11 11 ASN A 209 GLY A 226 1 18
HELIX 12 12 ARG A 258 VAL A 265 1 8
HELIX 13 13 ASP A 277 MET A 288 1 12
HELIX 14 14 GLN A 291 ASP A 301 1 11
HELIX 15 15 ASP A 301 GLY A 321 1 21
HELIX 16 16 ASP A 362 LEU A 371 1 10
HELIX 17 17 PHE A 381 ASN A 386 1 6
HELIX 18 18 HIS A 413 SER A 432 1 20
HELIX 19 19 TYR A 435 SER A 445 1 11
HELIX 20 20 ASN B 12 GLY B 23 1 12
HELIX 21 21 SER B 27 LYS B 35 1 9
HELIX 22 22 GLN B 37 PHE B 47 1 11
HELIX 23 23 ASN B 48 PHE B 64 1 17
HELIX 24 24 SER B 72 PHE B 82 1 11
HELIX 25 25 ASN B 90 LEU B 112 1 23
HELIX 26 26 GLY B 113 ILE B 117 5 5
HELIX 27 27 THR B 132 ASN B 146 1 15
HELIX 28 28 LEU B 164 HIS B 179 1 16
HELIX 29 29 GLY B 187 LEU B 193 1 7
HELIX 30 30 ASN B 209 GLY B 226 1 18
HELIX 31 31 ARG B 258 VAL B 265 1 8
HELIX 32 32 ASP B 277 PHE B 289 1 13
HELIX 33 33 GLN B 291 ASP B 301 1 11
HELIX 34 34 ASP B 301 GLY B 321 1 21
HELIX 35 35 GLU B 363 LEU B 371 1 9
HELIX 36 36 PHE B 381 ASN B 386 1 6
HELIX 37 37 HIS B 413 SER B 432 1 20
HELIX 38 38 TYR B 435 SER B 445 1 11
SHEET 1 A 6 CYS A 183 TYR A 186 0
SHEET 2 A 6 ASP A 204 GLN A 207 -1 O LEU A 206 N ILE A 184
SHEET 3 A 6 HIS A 250 ASN A 256 1 O PHE A 255 N GLN A 207
SHEET 4 A 6 TYR A 240 ASP A 245 -1 N ILE A 243 O ILE A 252
SHEET 5 A 6 ILE A 229 ILE A 234 -1 N SER A 232 O VAL A 242
SHEET 6 A 6 PHE A 469 ASN A 471 -1 O ILE A 470 N LEU A 231
SHEET 1 B 2 LYS A 267 ILE A 270 0
SHEET 2 B 2 ILE A 273 VAL A 276 -1 O ILE A 275 N ILE A 268
SHEET 1 C 6 ILE A 336 ILE A 337 0
SHEET 2 C 6 VAL A 344 THR A 347 -1 O THR A 345 N ILE A 336
SHEET 3 C 6 LYS A 356 TYR A 360 -1 O CYS A 357 N VAL A 346
SHEET 4 C 6 ILE A 395 TYR A 399 1 O MET A 396 N LEU A 358
SHEET 5 C 6 VAL A 388 HIS A 392 -1 N HIS A 392 O ILE A 395
SHEET 6 C 6 CYS A 379 ASP A 380 -1 N CYS A 379 O TYR A 389
SHEET 1 D 3 LYS A 411 VAL A 412 0
SHEET 2 D 3 LEU A 405 ASP A 408 -1 N ASP A 408 O LYS A 411
SHEET 3 D 3 SER A 456 HIS A 457 -1 O SER A 456 N LEU A 406
SHEET 1 E 7 CYS B 183 TYR B 186 0
SHEET 2 E 7 ASP B 204 GLN B 207 -1 O LEU B 206 N ILE B 184
SHEET 3 E 7 HIS B 250 ASN B 256 1 O PHE B 255 N GLN B 207
SHEET 4 E 7 TYR B 240 ASP B 245 -1 N ILE B 243 O ILE B 252
SHEET 5 E 7 ILE B 229 SER B 232 -1 N SER B 232 O VAL B 242
SHEET 6 E 7 PHE B 469 ASN B 471 -1 O ILE B 470 N LEU B 231
SHEET 7 E 7 ILE B 476 ILE B 477 -1 O ILE B 476 N ASN B 471
SHEET 1 F 2 LYS B 267 ILE B 270 0
SHEET 2 F 2 ILE B 273 VAL B 276 -1 O ILE B 275 N ILE B 268
SHEET 1 G 6 CYS B 335 ASP B 338 0
SHEET 2 G 6 ILE B 343 THR B 347 -1 O THR B 345 N ILE B 336
SHEET 3 G 6 LYS B 356 TYR B 360 -1 O CYS B 357 N VAL B 346
SHEET 4 G 6 ILE B 395 TYR B 399 1 O MET B 396 N LEU B 358
SHEET 5 G 6 VAL B 388 HIS B 392 -1 N LEU B 390 O TYR B 397
SHEET 6 G 6 CYS B 379 ASP B 380 -1 N CYS B 379 O TYR B 389
SHEET 1 H 3 LYS B 411 VAL B 412 0
SHEET 2 H 3 LEU B 405 ASP B 408 -1 N ASP B 408 O LYS B 411
SHEET 3 H 3 SER B 456 HIS B 457 -1 O SER B 456 N LEU B 406
CISPEP 1 MET A 331 PRO A 332 0 -0.25
CISPEP 2 MET B 331 PRO B 332 0 0.61
CRYST1 80.128 161.290 97.672 90.00 90.00 90.00 P 21 21 2 8
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 0.012480 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010238 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
