HEADER COMPLEX (ANTIBODY/PV-1 FRAGMENT) 26-JAN-95 1FPT
TITLE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN THE FAB FRAGMENT OF
TITLE 2 AN NEUTRALIZING ANTIBODY FOR TYPE 1 POLIOVIRUS AND ITS VIRAL EPITOPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB FRAGMENT OF AN NEUTRALIZING ANTIBODY FOR TYPE 1
COMPND 3 POLIOVIRUS;
COMPND 4 CHAIN: P;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IGG2A-KAPPA C3 FAB (LIGHT CHAIN);
COMPND 8 CHAIN: L;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: IGG2A-KAPPA C3 FAB (HEAVY CHAIN);
COMPND 12 CHAIN: H;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN POLIOVIRUS 1;
SOURCE 3 ORGANISM_TAXID: 12081;
SOURCE 4 STRAIN: MAHONEY;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090
KEYWDS COMPLEX (ANTIBODY-PV-1 FRAGMENT), COMPLEX (ANTIBODY-PV-1 FRAGMENT)
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.WIEN,J.M.HOGLE
REVDAT 4 13-JUL-11 1FPT 1 VERSN
REVDAT 3 24-FEB-09 1FPT 1 VERSN
REVDAT 2 01-APR-03 1FPT 1 JRNL
REVDAT 1 31-MAR-95 1FPT 0
JRNL AUTH M.W.WIEN,D.J.FILMAN,E.A.STURA,S.GUILLOT,F.DELPEYROUX,
JRNL AUTH 2 R.CRAINIC,J.M.HOGLE
JRNL TITL STRUCTURE OF THE COMPLEX BETWEEN THE FAB FRAGMENT OF A
JRNL TITL 2 NEUTRALIZING ANTIBODY FOR TYPE 1 POLIOVIRUS AND ITS VIRAL
JRNL TITL 3 EPITOPE.
JRNL REF NAT.STRUCT.BIOL. V. 2 232 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7539711
JRNL DOI 10.1038/NSB0395-232
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13342
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3426
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 3.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.91450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.91450
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 71.91450
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 71.91450
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 71.91450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 71.91450
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 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, L, H
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 CYS P 86
REMARK 465 VAL P 87
REMARK 465 THR P 88
REMARK 465 ILE P 89
REMARK 465 MET P 90
REMARK 465 THR P 91
REMARK 465 VAL P 92
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 CYS L 213A SG
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 HIS L 27D NE2 HIS L 27D CD2 -0.076
REMARK 500 HIS L 34 NE2 HIS L 34 CD2 -0.090
REMARK 500 HIS H 172 NE2 HIS H 172 CD2 -0.080
REMARK 500 HIS H 212 NE2 HIS H 212 CD2 -0.082
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 P 95 N - CD - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASN P 94 O - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 THR P 98 CA - CB - OG1 ANGL. DEV. = -12.6 DEGREES
REMARK 500 THR P 98 CA - CB - CG2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 LYS P 103 CB - CG - CD ANGL. DEV. = -16.7 DEGREES
REMARK 500 CYS L 23 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 GLN L 27 CA - CB - CG ANGL. DEV. = -14.5 DEGREES
REMARK 500 LEU L 33 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 TRP L 35 CD1 - CG - CD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TRP L 35 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR L 49 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR L 49 CA - C - N ANGL. DEV. = 19.1 DEGREES
REMARK 500 VAL L 51 CG1 - CB - CG2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG L 61 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG L 61 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 THR L 114 CA - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 LEU L 136 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 TRP L 148 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP L 148 CB - CG - CD1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 TRP L 148 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP L 148 CG - CD2 - CE3 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP L 163 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP L 163 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP L 163 CG - CD2 - CE3 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG L 188 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TYR L 192 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG L 211 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG L 211 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLN H 3 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 VAL H 18 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 TRP H 36 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP H 36 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 GLN H 43 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 TRP H 47 CD1 - CG - CD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP H 47 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP H 47 CE2 - CD2 - CG ANGL. DEV. = -6.5 DEGREES
REMARK 500 ILE H 48 CA - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 VAL H 50 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 GLN H 81 CA - CB - CG ANGL. DEV. = -14.4 DEGREES
REMARK 500 TYR H 99 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TYR H 99 CB - CG - CD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP H 103 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP H 103 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TYR H 122 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 GLY H 135 CA - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 CYS H 142 CA - CB - SG ANGL. DEV. = -21.4 DEGREES
REMARK 500 VAL H 144 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 PRO H 151 N - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 THR H 156 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 TRP H 157 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 57 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL L 2 79.54 89.46
REMARK 500 LEU L 15 135.44 -37.50
REMARK 500 SER L 27E -39.98 -15.66
REMARK 500 TYR L 32 71.48 -101.20
REMARK 500 GLN L 42 175.94 -55.01
REMARK 500 VAL L 51 -43.04 -161.60
REMARK 500 LYS L 107 59.12 -113.80
REMARK 500 ASN L 138 43.45 32.85
REMARK 500 TYR L 140 125.94 -176.05
REMARK 500 SER L 171 11.03 56.58
REMARK 500 ARG L 188 51.15 -97.07
REMARK 500 HIS L 198 -124.21 -150.39
REMARK 500 LYS L 199 -16.68 -145.88
REMARK 500 ARG L 211 -32.73 -27.75
REMARK 500 PHE H 29 -46.29 -28.67
REMARK 500 LYS H 66 -70.43 -89.70
REMARK 500 SER H 75 53.82 -158.57
REMARK 500 SER H 76 51.15 21.82
REMARK 500 SER H 82B 71.13 48.60
REMARK 500 SER H 84 -37.81 -29.39
REMARK 500 VAL H 100I 33.59 -142.29
REMARK 500 ASP H 101 -79.60 -21.23
REMARK 500 SER H 112 147.94 -170.37
REMARK 500 CYS H 128 -70.77 -32.17
REMARK 500 ASP H 130 -140.37 -135.88
REMARK 500 THR H 134 -127.16 -156.81
REMARK 500 SER H 136 -98.86 -140.73
REMARK 500 LEU H 140 -179.37 -173.79
REMARK 500 GLN H 179 -109.84 -82.16
REMARK 500 ASP H 181 -1.24 59.85
REMARK 500 SER H 193 -30.13 -28.33
REMARK 500 GLN H 203 -71.77 -125.94
REMARK 500 SER H 204 132.45 178.58
REMARK 500 ALA H 214 10.70 -63.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG H 40 PRO H 41 -112.67
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 L 32 0.07 SIDE CHAIN
REMARK 500 TYR H 59 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN P 94 10.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP L 110 23.7 L L OUTSIDE RANGE
REMARK 500 SER H 194 24.6 L L OUTSIDE RANGE
REMARK 500 SER H 204 24.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FAB FRAGMENT IS NUMBERED ACCORDING TO THE CONVENTION OF
REMARK 999 E. KABAT (E.A. KABAT, T.T. WU, M. REID-MILLER, H.M. PERRY,
REMARK 999 K.S. GOTTESMAN, SEQUENCES OF PROTEINS OF IMMUNOLOGICAL
REMARK 999 INTEREST, 4TH ED., (1987), NATIONAL INSTITUTE OF HEALTH,
REMARK 999 BETHESDA, MD.
REMARK 999
REMARK 999 THE PEPTIDE IS NUMBERED ACCORDING TO THE POLIOVIRUS TYPE 1
REMARK 999 SEQUENCE (MAHONEY STRAIN) (V.R. RANCANIELLO AND D.
REMARK 999 BALTIMORE (1981) PROCEEDINGS OF THE NATIONAL ACADEMY
REMARK 999 OF SCIENCES, USA V. 78, 4887-4891). THE PEPTIDE USED WAS A
REMARK 999 SYNTHETIC HOMOLOGUE OF RESIDUES 86 - 103 OF PV-1 VP1
REMARK 999 (MAHONEY STRAIN). PV-1 VP1 RESIDUES ARE
REMARK 999 (CVTIMYVDNPASTTNKDK). DUE TO DISORDER, RESIDUES 86 - 92
REMARK 999 ARE NOT PRESENTED IN THE RECORDS BELOW.
DBREF 1FPT P 86 103 UNP P03299 POLG_POL1M 663 680
DBREF 1FPT H 114 228 UNP P01865 GCAM_MOUSE 1 100
DBREF 1FPT L 1 213A PDB 1FPT 1FPT 1 213
SEQRES 1 P 18 CYS VAL THR ILE MET THR VAL ASP ASN PRO ALA SER THR
SEQRES 2 P 18 THR ASN LYS ASP LYS
SEQRES 1 L 219 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS SER SER SER
SEQRES 3 L 219 GLN SER LEU VAL HIS SER ASN GLY LYS THR TYR LEU HIS
SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU
SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR TYR PHE THR LEU
SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 219 PHE CYS SER GLN SER THR HIS VAL PRO TYR THR PHE GLY
SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA
SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 L 219 GLY SER GLU VAL GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS
SEQRES 1 H 220 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG
SEQRES 2 H 220 PRO GLY THR SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 220 TYR ALA PHE THR ASN TYR LEU ILE GLN TRP ILE LYS GLN
SEQRES 4 H 220 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY VAL ILE ASN
SEQRES 5 H 220 PRO GLY SER GLY GLY THR ASP TYR ASN ALA ASN PHE LYS
SEQRES 6 H 220 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER ILE
SEQRES 7 H 220 VAL TYR MET GLN LEU SER SER LEU THR SER ASP ASP SER
SEQRES 8 H 220 ALA VAL TYR PHE CYS ALA ARG ASP PHE TYR ASP TYR ASP
SEQRES 9 H 220 VAL GLY PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 H 220 VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO
SEQRES 11 H 220 LEU ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL
SEQRES 12 H 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 H 220 VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES 14 H 220 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES 15 H 220 THR LEU SER SER SER VAL THR VAL THR SER SER THR TRP
SEQRES 16 H 220 PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 H 220 SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG
FORMUL 4 HOH *39(H2 O)
HELIX 1 1 ALA L 80 ASP L 82 5 3
HELIX 2 2 SER L 122 THR L 126 1 5
HELIX 3 3 LYS L 183 GLU L 187 1 5
HELIX 4 4 PHE H 29 ASN H 31 5 3
HELIX 5 5 LYS H 73 SER H 75 5 3
HELIX 6 6 SER H 84 ASP H 86 5 3
HELIX 7 7 ASN H 162 GLY H 164 5 3
HELIX 8 8 PRO H 213 SER H 215 5 3
SHEET 1 A 4 MET L 4 THR L 7 0
SHEET 2 A 4 ALA L 19 SER L 25 -1 N SER L 24 O THR L 5
SHEET 3 A 4 TYR L 70 ILE L 75 -1 N ILE L 75 O ALA L 19
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 67 O TYR L 70
SHEET 1 B 5 SER L 10 VAL L 13 0
SHEET 2 B 5 THR L 102 ILE L 106 1 N LYS L 103 O LEU L 11
SHEET 3 B 5 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 B 5 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85
SHEET 5 B 5 LYS L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 C 3 GLY L 129 LEU L 136 0
SHEET 2 C 3 MET L 175 THR L 182 -1 N LEU L 181 O ALA L 130
SHEET 3 C 3 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 D 3 ASN L 145 ILE L 150 0
SHEET 2 D 3 SER L 191 THR L 197 -1 N THR L 197 O ASN L 145
SHEET 3 D 3 LYS L 207 ASN L 210 -1 N PHE L 209 O TYR L 192
SHEET 1 E 4 GLN H 3 GLN H 6 0
SHEET 2 E 4 VAL H 18 SER H 25 -1 N SER H 25 O GLN H 3
SHEET 3 E 4 ILE H 77 LEU H 82 -1 N LEU H 82 O VAL H 18
SHEET 4 E 4 ALA H 67 ASP H 72 -1 N ASP H 72 O ILE H 77
SHEET 1 F 3 ALA H 9 VAL H 12 0
SHEET 2 F 3 THR H 107 VAL H 111 1 N THR H 108 O GLU H 10
SHEET 3 F 3 ALA H 88 TYR H 90 -1 N TYR H 90 O THR H 107
SHEET 1 G 4 ALA H 93 PHE H 96 0
SHEET 2 G 4 TYR H 32 GLN H 39 -1 N GLN H 35 O ALA H 93
SHEET 3 G 4 LEU H 45 ILE H 51 -1 N ILE H 51 O ILE H 34
SHEET 4 G 4 THR H 57 TYR H 59 -1 N ASP H 58 O VAL H 50
SHEET 1 H 4 SER H 120 LEU H 124 0
SHEET 2 H 4 SER H 137 LYS H 145 -1 N LYS H 145 O SER H 120
SHEET 3 H 4 LEU H 185 THR H 192 -1 N VAL H 191 O VAL H 138
SHEET 4 H 4 VAL H 171 THR H 173 -1 N HIS H 172 O SER H 188
SHEET 1 I 3 VAL H 152 TRP H 157 0
SHEET 2 I 3 THR H 206 HIS H 212 -1 N ALA H 211 O THR H 153
SHEET 3 I 3 THR H 217 LYS H 222 -1 N LYS H 221 O CYS H 208
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.39
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.64
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.41
SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.59
CISPEP 1 THR L 7 PRO L 8 0 0.30
CISPEP 2 VAL L 94 PRO L 95 0 -0.45
CISPEP 3 TYR L 140 PRO L 141 0 -1.23
CISPEP 4 PHE H 148 PRO H 149 0 -1.08
CISPEP 5 GLU H 150 PRO H 151 0 2.98
CRYST1 129.785 129.785 143.829 90.00 90.00 120.00 P 63 2 2 12
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 0.007705 0.004449 0.000000 0.00000
SCALE2 0.000000 0.008897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006953 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
