[English] 日本語
Yorodumi
- PDB-4hs6: Hepatitus C envelope glycoprotein E2 fragment 412-423 with humani... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4hs6
TitleHepatitus C envelope glycoprotein E2 fragment 412-423 with humanized and affinity-matured antibody MRCT10.v362
Components
  • E2-peptide
  • MRCT10.v362 Fab heavy chain
  • MRCT10.v362 Fab light chain
KeywordsIMMUNE SYSTEM
Function / homology
Function and homology information


host cell lipid droplet / lipid droplet / host cell endoplasmic reticulum membrane / viral envelope / virion membrane / membrane
Similarity search - Function
Hepatitis C virus, Non-structural protein E2/NS1 / Hepatitis C virus non-structural protein E2/NS1 / Hepatitis C virus, Envelope glycoprotein E1 / Hepatitis C virus envelope glycoprotein E1 / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Hepatitis C virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.53 Å
AuthorsEigenbrot, C. / Ultsch, M.
CitationJournal: J.Mol.Biol. / Year: 2013
Title: Glycan shifting on hepatitis C virus (HCV) e2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies.
Authors: Pantua, H. / Diao, J. / Ultsch, M. / Hazen, M. / Mathieu, M. / McCutcheon, K. / Takeda, K. / Date, S. / Cheung, T.K. / Phung, Q. / Hass, P. / Arnott, D. / Hongo, J.A. / Matthews, D.J. / ...Authors: Pantua, H. / Diao, J. / Ultsch, M. / Hazen, M. / Mathieu, M. / McCutcheon, K. / Takeda, K. / Date, S. / Cheung, T.K. / Phung, Q. / Hass, P. / Arnott, D. / Hongo, J.A. / Matthews, D.J. / Brown, A. / Patel, A.H. / Kelley, R.F. / Eigenbrot, C. / Kapadia, S.B.
History
DepositionOct 29, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 3, 2013Provider: repository / Type: Initial release
Revision 1.1May 29, 2013Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
Z: E2-peptide
Y: E2-peptide
A: MRCT10.v362 Fab light chain
L: MRCT10.v362 Fab light chain
B: MRCT10.v362 Fab heavy chain
H: MRCT10.v362 Fab heavy chain


Theoretical massNumber of molelcules
Total (without water)99,5216
Polymers99,5216
Non-polymers00
Water19,0781059
1
Z: E2-peptide
A: MRCT10.v362 Fab light chain
B: MRCT10.v362 Fab heavy chain


Theoretical massNumber of molelcules
Total (without water)49,7603
Polymers49,7603
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4780 Å2
ΔGint-35 kcal/mol
Surface area19170 Å2
MethodPISA
2
Y: E2-peptide
L: MRCT10.v362 Fab light chain
H: MRCT10.v362 Fab heavy chain


Theoretical massNumber of molelcules
Total (without water)49,7603
Polymers49,7603
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4670 Å2
ΔGint-36 kcal/mol
Surface area19600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.091, 90.821, 72.681
Angle α, β, γ (deg.)90.00, 109.35, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21L
12B
22H
13Z
23Y

NCS domain segments:

Component-ID: 1 / Ens-ID: 3 / Beg auth comp-ID: GLN / Beg label comp-ID: GLN / End auth comp-ID: ASN / End label comp-ID: ASN / Refine code: 4 / Auth seq-ID: 412 - 423 / Label seq-ID: 1 - 12

Dom-IDAuth asym-IDLabel asym-ID
1ZA
2YB

NCS ensembles :
ID
3
1
2

-
Components

#1: Protein/peptide E2-peptide


Mass: 1727.877 Da / Num. of mol.: 2 / Fragment: UNP residues 50-62 / Source method: obtained synthetically
Details: This sequence occurs naturally in hepatitus C virus
Source: (synth.) Hepatitis C virus / References: UniProt: Q9YK84
#2: Antibody MRCT10.v362 Fab light chain


Mass: 23846.387 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#3: Antibody MRCT10.v362 Fab heavy chain


Mass: 24186.021 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1059 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer detailsE2-PEPTIDE IS BIOTINYLATED, WITH BIOTIN (BTN) ATTACHED TO THE SIDE CHAIN OF THE C-TERMINAL LYS ...E2-PEPTIDE IS BIOTINYLATED, WITH BIOTIN (BTN) ATTACHED TO THE SIDE CHAIN OF THE C-TERMINAL LYS RESIDUE. HOWEVER, SOME RESIDUES AT THE C-TERMINUS, INCLUDING BTN, ARE MISSING DUE TO DISORDER.

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.22 Å3/Da / Density % sol: 44.71 %
Crystal growTemperature: 291 K / pH: 8.5
Details: LiCl, PEG6000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K

-
Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.98
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Sep 23, 2011
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.53→50 Å / Num. obs: 131070 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 21 Å2 / Rsym value: 0.052 / Net I/σ(I): 23

-
Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1FVC
Resolution: 1.53→50 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.957 / SU B: 3.029 / SU ML: 0.05 / Isotropic thermal model: TLS in 23 groups / Cross valid method: THROUGHOUT / ESU R: 0.077 / ESU R Free: 0.076 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2 1318 1 %RANDOM
Rwork0.175 ---
obs0.175 129605 99.9 %-
all-130923 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.1 Å2
Baniso -1Baniso -2Baniso -3
1-0.32 Å20 Å20.1 Å2
2--0.06 Å2-0 Å2
3----0.31 Å2
Refine analyzeLuzzati coordinate error free: 0.076 Å
Refinement stepCycle: LAST / Resolution: 1.53→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6784 0 0 1059 7843
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0227063
X-RAY DIFFRACTIONr_bond_other_d0.0060.024659
X-RAY DIFFRACTIONr_angle_refined_deg1.2321.9529669
X-RAY DIFFRACTIONr_angle_other_deg0.9193.00111456
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.8435920
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.26924.384276
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.506151134
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.7471527
X-RAY DIFFRACTIONr_chiral_restr0.0740.21109
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0217872
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021381
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.5232.54472
X-RAY DIFFRACTIONr_mcbond_other0.5872.51797
X-RAY DIFFRACTIONr_mcangle_it3.91957295
X-RAY DIFFRACTIONr_scbond_it3.762.52591
X-RAY DIFFRACTIONr_scangle_it5.40552353
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A2715medium positional0.730.5
2B2598medium positional0.810.5
3Z144medium positional0.490.5
1A2715medium thermal2.5430
2B2598medium thermal2.5830
3Z144medium thermal2.4430
LS refinement shellResolution: 1.53→1.61 Å / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.253 183 -
Rwork0.254 18802 -
obs--99.41 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.9948-0.1034-0.38360.50280.37630.4754-0.0598-0.03990.08350.08730.0477-0.05350.04580.00260.0120.05110.0289-0.03110.0217-0.03210.061634.061822.52965.076
21.89960.7373-1.54930.3731-0.64321.28660.0259-0.15530.05920.0429-0.0025-0.0054-0.02090.0969-0.02340.09460.02110.01130.075-0.04410.033814.695718.80915.1505
30.69560.24030.02160.67320.64131.0491-0.0718-0.0871-0.07880.10880.04930.03220.1117-0.06070.02250.04530.03380.03230.08040.02590.03050.88212.204210.1219
40.472-0.08190.03660.49260.08910.22420.02180.0401-0.04310.0117-0.0309-0.0221-0.01420.01140.00910.02410.00410.0050.0065-0.00140.043134.74939.3547-12.1456
52.4601-1.0515-0.27891.05810.19740.32190.02810.0729-0.2332-0.0011-0.06030.06710.0086-0.10230.03220.0046-0.0019-0.01110.033-0.01120.04729.0057-2.2828-6.236
61.3375-0.8219-0.62851.2240.99911.4140.0081-0.0166-0.0732-0.11860.04780.0473-0.1952-0.0042-0.05590.03730.00630.00850.01210.00140.02455.29886.0857-5.1482
71.4135-0.2231-0.71920.38210.04890.72960.03820.1697-0.1757-0.0361-0.11010.0438-0.0619-0.12430.07190.01410.01060.00150.0669-0.03520.0315-15.5694-11.6525-51.4717
80.7832-0.2537-0.46740.46510.18270.30850.09410.13910.0297-0.0587-0.0709-0.0191-0.0721-0.0933-0.02320.03670.04610.00530.0620.00560.0022-18.5194-0.4781-48.6101
91.5631-0.2928-0.8830.1440.22050.76240.02550.0934-0.0647-0.038-0.0518-0.0032-0.0448-0.08920.02630.02190.01960.01040.0392-0.00650.0172-15.8811-5.2593-44.6397
102.0476-0.79380.26680.81080.19060.47210.10670.10880.0144-0.0776-0.02910.01110.01680.0779-0.07770.04350.00470.00770.047-0.02590.03912.0214-13.6029-50.7976
110.2097-0.11880.09870.68110.05813.18020.07270.03210.01320.08810.0843-0.1817-0.02890.2323-0.1570.05350.0164-0.02690.0883-0.04150.056919.2855-16.0386-26.2242
120.35940.04980.64440.7709-0.19591.60270.06990.038-0.0828-0.0310.0269-0.06680.12460.0683-0.09680.01840.0118-0.01650.0451-0.03420.041910.6506-21.0356-38.7052
130.1959-0.31780.07812.187-0.3981.57550.05110.0537-0.0640.0912-0.06370.02040.2005-0.04630.01260.06030.0055-0.01970.022-0.02240.049810.059-26.5695-31.3262
140.7991-0.94451.2121.8383-2.62653.8219-0.1154-0.07540.06890.17450.0006-0.0938-0.24550.05930.11480.0495-0.00580.00370.0584-0.03790.03465.1076-8.2546-45.5734
150.26890.07680.30431.1058-0.03332.55440.10170.0346-0.08530.06710.0017-0.17810.30590.1622-0.10340.05870.0331-0.04540.0553-0.03790.065517.917-25.046-32.6025
160.5985-0.16420.11561.185-0.42930.8980.0047-0.01780.02080.0471-0.0461-0.1341-0.06330.06130.04150.0265-0.00470.01720.02150.00690.0381-12.02560.3315-21.5018
170.4323-0.235-0.14580.28440.15560.81330.06640.0616-0.0074-0.0199-0.07270.0073-0.0127-0.05080.00630.02450.01290.01930.03250.00770.0332-21.14192.2801-30.4226
181.4262-0.97451.23672.2248-2.24332.35960.1208-0.1032-0.1558-0.0460.08330.24340.1032-0.1031-0.20420.0431-0.01980.03580.04110.00930.0968-27.1144-7.8148-23.5302
190.3454-0.2203-0.19450.26140.10820.41270.0510.00430.0266-0.0204-0.04510.0028-0.02180.0076-0.00590.02380.00880.02310.02560.00980.0349-18.19783.5455-28.476
201.3229-0.0843-0.33120.37930.00950.51530.0291-0.1438-0.0010.06820.048-0.0251-0.00830.1044-0.07710.02240.0009-0.00330.0425-0.01150.01787.8708-10.0686-21.3521
210.73570.0782-0.38240.3857-0.15530.84570.0077-0.0047-0.00830.00160.0128-0.0161-0.0020.0655-0.02050.0132-0.01320.00890.0457-0.01710.009211.5283-5.357-28.2685
220.353-0.34130.00534.3005-0.49761.4256-0.02540.13390.0817-0.0245-0.0216-0.1779-0.08550.19350.0470.0086-0.0248-0.0070.08770.01690.104250.05222.2805-10.3433
230.67170.3402-0.40452.07-2.27123.06040.03840.05110.0211-0.03-0.01580.0948-0.0454-0.159-0.02260.02040.046-0.00660.1097-0.01040.0204-34.73446.6044-39.1739
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 101
2X-RAY DIFFRACTION2A102 - 113
3X-RAY DIFFRACTION3A114 - 214
4X-RAY DIFFRACTION4B1 - 109
5X-RAY DIFFRACTION5B110 - 134
6X-RAY DIFFRACTION6B135 - 216
7X-RAY DIFFRACTION7L1 - 25
8X-RAY DIFFRACTION8L26 - 75
9X-RAY DIFFRACTION9L76 - 101
10X-RAY DIFFRACTION10L102 - 113
11X-RAY DIFFRACTION11L114 - 128
12X-RAY DIFFRACTION12L129 - 150
13X-RAY DIFFRACTION13L151 - 163
14X-RAY DIFFRACTION14L164 - 174
15X-RAY DIFFRACTION15L175 - 214
16X-RAY DIFFRACTION16H1 - 17
17X-RAY DIFFRACTION17H18 - 60
18X-RAY DIFFRACTION18H61 - 66
19X-RAY DIFFRACTION19H67 - 109
20X-RAY DIFFRACTION20H110 - 134
21X-RAY DIFFRACTION21H135 - 216
22X-RAY DIFFRACTION22Z412 - 423
23X-RAY DIFFRACTION23Y412 - 423

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more