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- PDB-5xf1: Structure of the Full-length glucagon class B G protein-coupled r... -

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Basic information

Entry
Database: PDB / ID: 5xf1
TitleStructure of the Full-length glucagon class B G protein-coupled receptor
Components
  • (Antibody mAb1 ...) x 2
  • Glucagon receptor,Endolysin,Glucagon receptor
KeywordsSIGNALING PROTEIN / Human GCGR receptor / Class B / 7TM domain / membrane / LCP / XFEL
Function / homology
Function and homology information


regulation of glycogen metabolic process / glucagon receptor activity / response to starvation / peptide hormone binding / viral release from host cell by cytolysis / peptidoglycan catabolic process / response to nutrient / cellular response to glucagon stimulus / guanyl-nucleotide exchange factor activity / cellular response to starvation ...regulation of glycogen metabolic process / glucagon receptor activity / response to starvation / peptide hormone binding / viral release from host cell by cytolysis / peptidoglycan catabolic process / response to nutrient / cellular response to glucagon stimulus / guanyl-nucleotide exchange factor activity / cellular response to starvation / generation of precursor metabolites and energy / regulation of blood pressure / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cell wall macromolecule catabolic process / Glucagon signaling in metabolic regulation / Glucagon-type ligand receptors / lysozyme / lysozyme activity / glucose homeostasis / G alpha (s) signalling events / G alpha (q) signalling events / host cell cytoplasm / cell surface receptor signaling pathway / defense response to bacterium / positive regulation of gene expression / membrane / plasma membrane
Similarity search - Function
GPCR, family 2, glucagon receptor / GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / GPCR, family 2, glucagon-like peptide-1/glucagon receptor / G-protein coupled receptors family 2 signature 1. / : / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / Hormone receptor domain ...GPCR, family 2, glucagon receptor / GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / GPCR, family 2, glucagon-like peptide-1/glucagon receptor / G-protein coupled receptors family 2 signature 1. / : / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / Hormone receptor domain / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. / GPCR, family 2, secretin-like, conserved site / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Lysozyme - #40 / Endolysin T4 type / T4-type lysozyme / : / Glycoside hydrolase, family 24 / Phage lysozyme / Lysozyme domain superfamily / Lysozyme / Few Secondary Structures / Irregular / Lysozyme-like domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
triacetyl-beta-chitotriose / Chem-97V / Endolysin / Glucagon receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
Enterobacteria phage T4 (virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.19 Å
AuthorsZhang, H. / Qiao, A. / Yang, D. / Yang, L. / Dai, A. / de Graaf, C. / Reedtz-Runge, S. / Dharmarajan, V. / Zhang, H. / Han, G.W. ...Zhang, H. / Qiao, A. / Yang, D. / Yang, L. / Dai, A. / de Graaf, C. / Reedtz-Runge, S. / Dharmarajan, V. / Zhang, H. / Han, G.W. / Grant, T. / Sierra, R. / Weierstall, U. / Nelson, G. / Liu, W. / Wu, Y. / Ma, L. / Cai, X. / Lin, G. / Wu, X. / Geng, Z. / Dong, Y. / Song, G. / Griffin, P. / Lau, J. / Cherezov, V. / Yang, H. / Hanson, M. / Stevens, R. / Jiang, H. / Wang, M. / Zhao, Q. / Wu, B.
CitationJournal: Nature / Year: 2017
Title: Structure of the full-length glucagon class B G-protein-coupled receptor.
Authors: Zhang, H. / Qiao, A. / Yang, D. / Yang, L. / Dai, A. / de Graaf, C. / Reedtz-Runge, S. / Dharmarajan, V. / Zhang, H. / Han, G.W. / Grant, T.D. / Sierra, R.G. / Weierstall, U. / Nelson, G. / ...Authors: Zhang, H. / Qiao, A. / Yang, D. / Yang, L. / Dai, A. / de Graaf, C. / Reedtz-Runge, S. / Dharmarajan, V. / Zhang, H. / Han, G.W. / Grant, T.D. / Sierra, R.G. / Weierstall, U. / Nelson, G. / Liu, W. / Wu, Y. / Ma, L. / Cai, X. / Lin, G. / Wu, X. / Geng, Z. / Dong, Y. / Song, G. / Griffin, P.R. / Lau, J. / Cherezov, V. / Yang, H. / Hanson, M.A. / Stevens, R.C. / Zhao, Q. / Jiang, H. / Wang, M.W. / Wu, B.
History
DepositionApr 6, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 24, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 7, 2017Group: Database references
Revision 1.2Jun 14, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_id_ASTM ..._citation.country / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glucagon receptor,Endolysin,Glucagon receptor
B: Glucagon receptor,Endolysin,Glucagon receptor
C: Antibody mAb1 Heavy chain
D: Antibody mAb1 Light chain
H: Antibody mAb1 Heavy chain
L: Antibody mAb1 Light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)232,17015
Polymers228,0526
Non-polymers4,1189
Water181
1
A: Glucagon receptor,Endolysin,Glucagon receptor
C: Antibody mAb1 Heavy chain
D: Antibody mAb1 Light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)115,8737
Polymers114,0263
Non-polymers1,8474
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7040 Å2
ΔGint-13 kcal/mol
Surface area50200 Å2
MethodPISA
2
B: Glucagon receptor,Endolysin,Glucagon receptor
H: Antibody mAb1 Heavy chain
L: Antibody mAb1 Light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,2978
Polymers114,0263
Non-polymers2,2715
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7430 Å2
ΔGint-9 kcal/mol
Surface area47670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.460, 248.790, 93.330
Angle α, β, γ (deg.)90.00, 90.16, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22H
13D
23L

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1010A27 - 573
2010B27 - 573
1020C215 - 445
2020H215 - 445
1030D1 - 214
2030L1 - 214

NCS ensembles :
ID
1
2
3

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Glucagon receptor,Endolysin,Glucagon receptor / GL-R / Lysis protein / Lysozyme / Muramidase / GL-R


Mass: 65784.070 Da / Num. of mol.: 2
Fragment: UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Mutation: C54T, C97A
Source method: isolated from a genetically manipulated source
Details: The fusion protein of Glucagon receptor (UNP RESIDUES 27-256), Endolysin (UNP RESIDUES 2-161) and Glucagon receptor (UNP RESIDUES 260-432)
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Enterobacteria phage T4 (virus)
Gene: GCGR, e, T4Tp126 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P47871, UniProt: D9IEF7, lysozyme

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Antibody , 2 types, 4 molecules CHDL

#2: Antibody Antibody mAb1 Heavy chain


Mass: 24977.961 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
#3: Antibody Antibody mAb1 Light chain


Mass: 23263.811 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 / Production host: Homo sapiens (human)

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Sugars , 3 types, 7 molecules

#4: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / triacetyl-beta-chitotriose


Type: oligosaccharide, Oligosaccharide / Class: Inhibitor / Mass: 627.594 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: triacetyl-beta-chitotriose
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,3,2/[a2122h-1b_1-5_2*NCC/3=O]/1-1-1/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}}LINUCSPDB-CARE
#7: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 3 molecules

#6: Chemical ChemComp-97V / 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide


Mass: 573.666 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C29H31N7O4S
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.68 Å3/Da / Density % sol: 66.56 %
Crystal growTemperature: 293 K / Method: lipidic cubic phase
Details: 100mM HEPES, pH7.0, 200mM potassium phospphate monobasic, 20% PEG500DME, 10 mM gly-gly-glysine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 20, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.555
11-h,-k,l20.445
ReflectionResolution: 3.19→50 Å / Num. obs: 49677 / % possible obs: 92.8 % / Redundancy: 2.8 % / Net I/σ(I): 3.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0103refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4L6R

4l6r


Resolution: 3.19→46.92 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.879 / SU B: 19.837 / SU ML: 0.165 / Cross valid method: THROUGHOUT / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23148 2547 5 %RANDOM
Rwork0.20526 ---
obs0.2066 48212 94.08 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 116.895 Å2
Baniso -1Baniso -2Baniso -3
1--13.93 Å2-0 Å23.56 Å2
2---5.66 Å20 Å2
3---19.59 Å2
Refinement stepCycle: 1 / Resolution: 3.19→46.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14762 0 278 1 15041
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01915432
X-RAY DIFFRACTIONr_bond_other_d0.0050.0214181
X-RAY DIFFRACTIONr_angle_refined_deg1.3971.96221020
X-RAY DIFFRACTIONr_angle_other_deg1.2083.00132538
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.78151922
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.18723.573627
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.332152354
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.4291582
X-RAY DIFFRACTIONr_chiral_restr0.0750.22375
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0217453
X-RAY DIFFRACTIONr_gen_planes_other0.0040.023637
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_it4.76410.7297712
X-RAY DIFFRACTIONr_mcbond_other4.76410.7287711
X-RAY DIFFRACTIONr_mcangle_it7.67616.0789626
X-RAY DIFFRACTIONr_mcangle_other7.67516.0799627
X-RAY DIFFRACTIONr_scbond_it4.25911.0267720
X-RAY DIFFRACTIONr_scbond_other4.25811.0267720
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.9816.44211395
X-RAY DIFFRACTIONr_long_range_B_refined13.42259786
X-RAY DIFFRACTIONr_long_range_B_other13.42259786
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A466140.13
12B466140.13
21C247120.1
22H247120.1
31D238260.07
32L238260.07
LS refinement shellResolution: 3.192→3.275 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.36 162 -
Rwork0.28 3243 -
obs--84.47 %
Refinement TLS params.Method: refined / Origin x: 168.104 Å / Origin y: -1.936 Å / Origin z: 48.911 Å
111213212223313233
T0.0806 Å20.0471 Å20.0157 Å2-0.1783 Å2-0.001 Å2--0.1302 Å2
L0.0018 °20.0018 °20.0026 °2-0.0243 °2-0.0091 °2--0.0413 °2
S0.0033 Å °0.014 Å °-0.0027 Å °0.0077 Å °-0.0035 Å °0.0234 Å °-0.0027 Å °0.0084 Å °0.0002 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A27 - 1161
2X-RAY DIFFRACTION1A1201 - 1207

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