[English] 日本語
Yorodumi
- PDB-1hcv: LLAMA HEAVY CHAIN VARIABLE DOMAIN AGAINST ALPHA SUBUNIT OF HCG (H... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1hcv
TitleLLAMA HEAVY CHAIN VARIABLE DOMAIN AGAINST ALPHA SUBUNIT OF HCG (HUMAN CHORIONIC GONADOTROPIN)
ComponentsIMMUNOGLOBULIN G
KeywordsIMMUNOGLOBULIN / CAMELIDS
Function / homologyImmunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / :
Function and homology information
Biological speciesLama glama (llama)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.85 Å
AuthorsSpinelli, S. / Cambillau, C. / Tegoni, M.
Citation
Journal: Nat.Struct.Biol. / Year: 1996
Title: The crystal structure of a llama heavy chain variable domain.
Authors: Spinelli, S. / Frenken, L. / Bourgeois, D. / de Ron, L. / Bos, W. / Verrips, T. / Anguille, C. / Cambillau, C. / Tegoni, M.
#1: Journal: Nat.Struct.Biol. / Year: 1996
Title: Crystal Structure of a Camel Single-Domain Vh Antibody Fragment in Complex with Lysozyme
Authors: Desmyter, A. / Transue, T.R. / Ghahroudi, M.A. / Thi, M.H. / Poortmans, F. / Hamers, R. / Muyldermans, S. / Wyns, L.
#2: Journal: Nat.Struct.Biol. / Year: 1996
Title: Redefining the Minimal Antigen-Binding Fragment
Authors: Sheriff, S. / Constantine, K.L.
#3: Journal: Protein Eng. / Year: 1994
Title: Sequence and Structure of Vh Domain from Naturally Occurring Camel Heavy Chain Immunoglobulins Lacking Light Chains
Authors: Muyldermans, S. / Atarhouch, T. / Saldanha, J. / Barbosa, J.A. / Hamers, R.
#4: Journal: Nature / Year: 1993
Title: Naturally Occurring Antibodies Devoid of Light Chains
Authors: Hamers-Casterman, C. / Atarhouch, T. / Muyldermans, S. / Robinson, G. / Hamers, C. / Songa, E.B. / Bendahman, N. / Hamers, R.
History
DepositionJul 13, 1996Processing site: BNL
Revision 1.0Jul 23, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Apr 3, 2024Group: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: IMMUNOGLOBULIN G


Theoretical massNumber of molelcules
Total (without water)12,5091
Polymers12,5091
Non-polymers00
Water1,856103
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)29.620, 41.830, 38.520
Angle α, β, γ (deg.)90.00, 95.45, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Antibody IMMUNOGLOBULIN G / HC-V LLAMA


Mass: 12508.674 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN VARIABLE DOMAIN FROM LLAMA
Source method: isolated from a genetically manipulated source
Details: FROM IMMUNIZED LLAMA / Source: (gene. exp.) Lama glama (llama) / Tissue: BLOOD / Cell: LYMPHOCYTE / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: EMBL: AJ236094
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 103 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

-
Sample preparation

CrystalDensity Matthews: 1.72 Å3/Da / Density % sol: 32 %
Crystal growMethod: vapor diffusion / pH: 8
Details: VAPOR DIFFUSION, PEG 8K 25%, TRIS 0.1M, PH 8.0, vapor diffusion
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
15 mg/mlprotein1drop
225 %PEG80001reservoir
30.1 MTris-HCl1reservoir

-
Data collection

DiffractionMean temperature: 290 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-D / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 19, 1996
RadiationMonochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.5→30 Å / Num. obs: 4270 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 1.6 % / Rmerge(I) obs: 0.109 / Net I/σ(I): 9.03
Reflection shellResolution: 2.5→2.59 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 3.4 / % possible all: 98.7
Reflection
*PLUS
Num. obs: 8077 / % possible obs: 99.8 % / Num. measured all: 92439 / Rmerge(I) obs: 0.089
Reflection shell
*PLUS
Highest resolution: 1.85 Å / Lowest resolution: 1.88 Å / % possible obs: 100 % / Rmerge(I) obs: 0.191 / Mean I/σ(I) obs: 10.4

-
Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLOR3.1refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: VH OF FAB FRAGMENT OF ANTIBODY AGAINST 2-PHENYL-OXAZOLONE

Resolution: 1.85→6 Å / Cross valid method: YES / σ(F): 1
RfactorNum. reflection% reflectionSelection details
Rfree0.218 844 10 %0.243
Rwork0.171 ---
obs0.171 7950 99 %-
Displacement parametersBiso mean: 16 Å2
Refinement stepCycle: LAST / Resolution: 1.85→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1386 0 0 99 1485
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.7
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d26
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.2
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg26
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.2

+
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://pdbjlvh1.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