HEADER IMMUNE SYSTEM/VIRAL PROTEIN 02-APR-14 4Q0X
TITLE CRYSTAL STRUCTURE OF NON-NEUTRALIZING ANTIBODY IN COMPLEX WITH EPITOPE
TITLE 2 II OF HCV E2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAB 12 HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 FRAGMENT: FAB;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MAB 12 LIGHT CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 FRAGMENT: FAB;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN E2;
COMPND 11 CHAIN: E;
COMPND 12 FRAGMENT: EPITOPE II (UNP RESIDUES 421-446);
COMPND 13 SYNONYM: NS1, GP68, GP70
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 11 ORGANISM_COMMON: HCV;
SOURCE 12 ORGANISM_TAXID: 11103
KEYWDS ANTIBODY, ANTI-HCV E2, HCV E2, IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.DENG,P.ZHANG
REVDAT 3 06-AUG-14 4Q0X 1 JRNL
REVDAT 2 23-JUL-14 4Q0X 1 JRNL
REVDAT 1 09-JUL-14 4Q0X 0
JRNL AUTH L.DENG,L.MA,M.L.VIRATA-THEIMER,L.ZHONG,H.YAN,Z.ZHAO,
JRNL AUTH 2 E.STRUBLE,S.FEINSTONE,H.ALTER,P.ZHANG
JRNL TITL DISCRETE CONFORMATIONS OF EPITOPE II ON THE HEPATITIS C
JRNL TITL 2 VIRUS E2 PROTEIN FOR ANTIBODY-MEDIATED NEUTRALIZATION AND
JRNL TITL 3 NONNEUTRALIZATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 10690 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25002515
JRNL DOI 10.1073/PNAS.1411317111
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11454
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 + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 606
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 826
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 38
REMARK 3 BIN FREE R VALUE : 0.4360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3398
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.45000
REMARK 3 B22 (A**2) : 1.45000
REMARK 3 B33 (A**2) : -2.90000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.459
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.379
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.623
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3489 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4756 ; 1.222 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 439 ;12.255 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;34.695 ;24.161
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 546 ;16.759 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;21.435 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 530 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2633 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1768 ; 0.981 ; 5.011
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2203 ; 1.797 ; 7.502
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1717 ; 0.657 ; 5.008
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5049 ; 5.019 ;42.177
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 117
REMARK 3 RESIDUE RANGE : L 1 L 112
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9876 13.4151 17.0542
REMARK 3 T TENSOR
REMARK 3 T11: 0.4646 T22: 0.0564
REMARK 3 T33: 0.0303 T12: -0.0363
REMARK 3 T13: -0.0149 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.8667 L22: 4.0824
REMARK 3 L33: 2.7444 L12: 0.4699
REMARK 3 L13: 0.8429 L23: -0.5057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0658 S12: 0.1221 S13: 0.0434
REMARK 3 S21: -0.6257 S22: 0.1024 S23: 0.2112
REMARK 3 S31: -0.2303 S32: -0.1706 S33: -0.0366
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 123 H 218
REMARK 3 RESIDUE RANGE : L 115 L 217
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9172 -5.9579 44.7724
REMARK 3 T TENSOR
REMARK 3 T11: 0.0727 T22: 0.0715
REMARK 3 T33: 0.1716 T12: -0.0320
REMARK 3 T13: 0.0425 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 3.4601 L22: 2.7127
REMARK 3 L33: 2.5446 L12: 0.9980
REMARK 3 L13: 1.1802 L23: 0.4889
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.2810 S13: -0.1696
REMARK 3 S21: -0.3743 S22: 0.0804 S23: -0.1808
REMARK 3 S31: -0.0786 S32: 0.1346 S33: -0.0880
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Q0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12050
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 97.646
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 14% W/V PEG550 MME,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 195.29250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 292.93875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 97.64625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.29250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 97.64625
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 292.93875
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, L
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 GLN H 137
REMARK 465 THR H 138
REMARK 465 ASN H 139
REMARK 465 HIS E 421
REMARK 465 ILE E 422
REMARK 465 ASN E 423
REMARK 465 SER E 424
REMARK 465 THR E 425
REMARK 465 ALA E 426
REMARK 465 LEU E 427
REMARK 465 ASN E 428
REMARK 465 CYS E 429
REMARK 465 ASN E 430
REMARK 465 GLU E 431
REMARK 465 SER E 432
REMARK 465 LEU E 433
REMARK 465 TYR E 443
REMARK 465 GLN E 444
REMARK 465 HIS E 445
REMARK 465 LYS E 446
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 PHE H 152 C PRO H 153 N 0.203
REMARK 500 GLU H 154 C PRO H 155 N 0.124
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 H 153 C - N - CA ANGL. DEV. = -15.7 DEGREES
REMARK 500 PRO H 155 C - N - CA ANGL. DEV. = -19.6 DEGREES
REMARK 500 PRO H 195 C - N - CD ANGL. DEV. = 19.5 DEGREES
REMARK 500 PRO L 146 C - N - CD ANGL. DEV. = 18.1 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 VAL H 56 7.18 54.50
REMARK 500 SER H 84 -83.28 -104.01
REMARK 500 ASP H 102 18.18 58.67
REMARK 500 ALA H 135 -132.80 -102.55
REMARK 500 SER H 162 10.23 59.61
REMARK 500 SER H 178 67.34 61.68
REMARK 500 VAL L 56 -58.28 70.41
REMARK 500 ALA L 85 -51.12 66.44
REMARK 500 LYS L 174 -61.76 -107.30
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 PHE H 152 PRO H 153 -67.15
REMARK 500 GLU H 154 PRO H 155 62.88
REMARK 500 TRP H 194 PRO H 195 32.72
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 PHE H 152 -15.10
REMARK 500 GLU H 154 10.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HZL RELATED DB: PDB
REMARK 900 STRUCTURAL EVIDENCE FOR A BIFURCATED MODE OF ACTION IN THE
REMARK 900 ANTIBODY-MEDIATED NEUTRALIZATION OF HEPATITIS C VIRUS
DBREF 4Q0X E 421 446 UNP P27958 POLG_HCVH 421 446
DBREF 4Q0X H 1 219 PDB 4Q0X 4Q0X 1 219
DBREF 4Q0X L 1 218 PDB 4Q0X 4Q0X 1 218
SEQRES 1 H 219 GLN VAL GLN LEU ARG GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 219 PRO GLY ALA SER VAL ARG ILE SER CYS LYS ALA SER GLY
SEQRES 3 H 219 TYR THR PHE THR SER TYR TYR ILE HIS TRP VAL LYS GLN
SEQRES 4 H 219 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR
SEQRES 5 H 219 PRO GLY ASN VAL ASN THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 H 219 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 H 219 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 H 219 ALA VAL TYR PHE CYS ALA ARG ASP ASP TYR ASP GLY ALA
SEQRES 9 H 219 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 H 219 SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU
SEQRES 11 H 219 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR
SEQRES 12 H 219 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 H 219 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 H 219 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 H 219 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO
SEQRES 16 H 219 SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 H 219 SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG
SEQRES 1 L 218 ASP VAL LEU MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 218 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 L 218 GLN SER ILE VAL HIS ASN ASN GLY ASN THR TYR LEU ASP
SEQRES 4 L 218 TRP SER LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU
SEQRES 5 L 218 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 L 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 218 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 218 TYR CYS PHE GLN GLY SER HIS VAL PRO PRO THR PHE GLY
SEQRES 9 L 218 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA
SEQRES 10 L 218 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 L 218 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 L 218 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 L 218 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 L 218 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 L 218 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 L 218 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 L 218 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU
SEQRES 1 E 26 HIS ILE ASN SER THR ALA LEU ASN CYS ASN GLU SER LEU
SEQRES 2 E 26 ASN THR GLY TRP LEU ALA GLY LEU PHE TYR GLN HIS LYS
FORMUL 4 HOH *23(H2 O)
HELIX 1 1 THR H 28 TYR H 32 5 5
HELIX 2 2 GLU H 62 LYS H 65 5 4
HELIX 3 3 THR H 87 SER H 91 5 5
HELIX 4 4 SER H 162 SER H 164 5 3
HELIX 5 5 SER L 126 THR L 131 1 6
HELIX 6 6 LYS L 188 GLU L 192 1 5
HELIX 7 7 GLY E 436 PHE E 442 1 7
SHEET 1 A 4 GLN H 3 GLN H 6 0
SHEET 2 A 4 VAL H 18 SER H 25 -1 O LYS H 23 N ARG H 5
SHEET 3 A 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22
SHEET 4 A 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80
SHEET 1 B 6 GLU H 10 VAL H 12 0
SHEET 2 B 6 THR H 113 VAL H 117 1 O LEU H 114 N GLU H 10
SHEET 3 B 6 ALA H 92 ASP H 100 -1 N ALA H 92 O VAL H 115
SHEET 4 B 6 ILE H 34 ARG H 40 -1 N HIS H 35 O ALA H 97
SHEET 5 B 6 GLY H 44 TYR H 52 -1 O GLU H 46 N LYS H 38
SHEET 6 B 6 ASN H 57 TYR H 60 -1 O ASN H 57 N TYR H 52
SHEET 1 C 4 GLU H 10 VAL H 12 0
SHEET 2 C 4 THR H 113 VAL H 117 1 O LEU H 114 N GLU H 10
SHEET 3 C 4 ALA H 92 ASP H 100 -1 N ALA H 92 O VAL H 115
SHEET 4 C 4 ALA H 104 TRP H 109 -1 O ALA H 107 N ARG H 98
SHEET 1 D 4 SER H 126 LEU H 130 0
SHEET 2 D 4 MET H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 D 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 148
SHEET 4 D 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186
SHEET 1 E 4 SER H 126 LEU H 130 0
SHEET 2 E 4 MET H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 E 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 148
SHEET 4 E 4 VAL H 175 LEU H 176 -1 N VAL H 175 O THR H 182
SHEET 1 F 3 THR H 157 TRP H 160 0
SHEET 2 F 3 THR H 200 HIS H 205 -1 O ALA H 204 N THR H 157
SHEET 3 F 3 THR H 210 LYS H 215 -1 O VAL H 212 N VAL H 203
SHEET 1 G 4 MET L 4 THR L 5 0
SHEET 2 G 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5
SHEET 3 G 4 ASP L 75 ILE L 80 -1 O LEU L 78 N ILE L 21
SHEET 4 G 4 PHE L 67 SER L 72 -1 N SER L 68 O LYS L 79
SHEET 1 H 6 SER L 10 VAL L 13 0
SHEET 2 H 6 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11
SHEET 3 H 6 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107
SHEET 4 H 6 LEU L 38 GLN L 43 -1 N GLN L 43 O VAL L 90
SHEET 5 H 6 PRO L 49 TYR L 54 -1 O LEU L 52 N TRP L 40
SHEET 6 H 6 ASN L 58 ARG L 59 -1 O ASN L 58 N TYR L 54
SHEET 1 I 4 SER L 10 VAL L 13 0
SHEET 2 I 4 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11
SHEET 3 I 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107
SHEET 4 I 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95
SHEET 1 J 4 THR L 119 PHE L 123 0
SHEET 2 J 4 GLY L 134 PHE L 144 -1 O VAL L 138 N PHE L 123
SHEET 3 J 4 TYR L 178 THR L 187 -1 O MET L 180 N LEU L 141
SHEET 4 J 4 VAL L 164 TRP L 168 -1 N SER L 167 O SER L 181
SHEET 1 K 4 SER L 158 ARG L 160 0
SHEET 2 K 4 ASN L 150 ILE L 155 -1 N ILE L 155 O SER L 158
SHEET 3 K 4 SER L 196 THR L 202 -1 O THR L 198 N LYS L 154
SHEET 4 K 4 ILE L 210 ASN L 215 -1 O LYS L 212 N CYS L 199
SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 2 CYS H 146 CYS H 201 1555 1555 2.03
SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.04
SSBOND 4 CYS L 139 CYS L 199 1555 1555 2.03
CISPEP 1 TYR L 145 PRO L 146 0 -9.91
CRYST1 49.991 49.991 390.585 90.00 90.00 90.00 P 43 2 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 0.020004 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
