[English] 日本語
Yorodumi
- PDB-7lk4: Crystal structure of BAK L100A in complex with activating antibod... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7lk4
TitleCrystal structure of BAK L100A in complex with activating antibody fragments
Components
  • 7D10 antibody VH fragment
  • 7D10 antibody VL fragment
  • Bcl-2 homologous antagonist/killer
KeywordsAPOPTOSIS / swap dimer / antibody fragments
Function / homology
Function and homology information


Activation and oligomerization of BAK protein / response to mycotoxin / B cell negative selection / BAK complex / BH domain binding / apoptotic process involved in blood vessel morphogenesis / response to fungus / negative regulation of endoplasmic reticulum calcium ion concentration / limb morphogenesis / Release of apoptotic factors from the mitochondria ...Activation and oligomerization of BAK protein / response to mycotoxin / B cell negative selection / BAK complex / BH domain binding / apoptotic process involved in blood vessel morphogenesis / response to fungus / negative regulation of endoplasmic reticulum calcium ion concentration / limb morphogenesis / Release of apoptotic factors from the mitochondria / post-embryonic camera-type eye morphogenesis / endocrine pancreas development / establishment or maintenance of transmembrane electrochemical gradient / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / B cell apoptotic process / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / activation of cysteine-type endopeptidase activity / endoplasmic reticulum calcium ion homeostasis / positive regulation of endoplasmic reticulum unfolded protein response / regulation of mitochondrial membrane permeability / calcium ion transport into cytosol / response to UV-C / fibroblast apoptotic process / mitochondrial fusion / Bcl-2 family protein complex / myeloid cell homeostasis / positive regulation of calcium ion transport into cytosol / porin activity / pore complex / thymocyte apoptotic process / negative regulation of release of cytochrome c from mitochondria / negative regulation of peptidyl-serine phosphorylation / positive regulation of IRE1-mediated unfolded protein response / positive regulation of release of cytochrome c from mitochondria / vagina development / positive regulation of proteolysis / B cell homeostasis / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / cellular response to unfolded protein / blood vessel remodeling / Pyroptosis / animal organ regeneration / extrinsic apoptotic signaling pathway in absence of ligand / heat shock protein binding / intrinsic apoptotic signaling pathway / release of cytochrome c from mitochondria / regulation of mitochondrial membrane potential / epithelial cell proliferation / establishment of localization in cell / response to gamma radiation / apoptotic signaling pathway / positive regulation of protein-containing complex assembly / response to hydrogen peroxide / response to organic cyclic compound / cellular response to mechanical stimulus / intrinsic apoptotic signaling pathway in response to DNA damage / cellular response to UV / protein-folding chaperone binding / response to ethanol / mitochondrial outer membrane / transmembrane transporter binding / regulation of cell cycle / response to xenobiotic stimulus / positive regulation of apoptotic process / protein heterodimerization activity / negative regulation of cell population proliferation / negative regulation of gene expression / apoptotic process / protein-containing complex binding / endoplasmic reticulum / protein homodimerization activity / mitochondrion / identical protein binding / metal ion binding / cytosol
Similarity search - Function
Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family / Bcl-2, Bcl-2 homology region 1-3 / Bcl2-like ...Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family / Bcl-2, Bcl-2 homology region 1-3 / Bcl2-like / Apoptosis regulator proteins, Bcl-2 family / BCL2-like apoptosis inhibitors family profile. / Bcl-2-like superfamily
Similarity search - Domain/homology
Bcl-2 homologous antagonist/killer
Similarity search - Component
Biological speciesHomo sapiens (human)
Rattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.1 Å
AuthorsRobin, Y.A. / Colman, P.M.
CitationJournal: Cell Death Differ. / Year: 2022
Title: Structure of the BAK-activating antibody 7D10 bound to BAK reveals an unexpected role for the alpha 1-alpha 2 loop in BAK activation.
Authors: Robin, A.Y. / Miller, M.S. / Iyer, S. / Shi, M.X. / Wardak, A.Z. / Lio, D. / Smith, N.A. / Smith, B.J. / Birkinshaw, R.W. / Czabotar, P.E. / Kluck, R.M. / Colman, P.M.
History
DepositionFeb 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 9, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Sep 14, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
P: Bcl-2 homologous antagonist/killer
Q: Bcl-2 homologous antagonist/killer
R: Bcl-2 homologous antagonist/killer
S: Bcl-2 homologous antagonist/killer
A: 7D10 antibody VL fragment
B: 7D10 antibody VH fragment
C: 7D10 antibody VL fragment
D: 7D10 antibody VH fragment
E: 7D10 antibody VL fragment
F: 7D10 antibody VH fragment
G: 7D10 antibody VL fragment
H: 7D10 antibody VH fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)178,60419
Polymers177,77712
Non-polymers8277
Water32418
1
P: Bcl-2 homologous antagonist/killer
R: Bcl-2 homologous antagonist/killer
A: 7D10 antibody VL fragment
B: 7D10 antibody VH fragment
E: 7D10 antibody VL fragment
F: 7D10 antibody VH fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,2439
Polymers88,8896
Non-polymers3553
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
Q: Bcl-2 homologous antagonist/killer
S: Bcl-2 homologous antagonist/killer
C: 7D10 antibody VL fragment
D: 7D10 antibody VH fragment
G: 7D10 antibody VL fragment
H: 7D10 antibody VH fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,36110
Polymers88,8896
Non-polymers4734
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)57.170, 271.800, 74.040
Angle α, β, γ (deg.)90.000, 91.790, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain B and (resid 1 through 88 or resid 90 through 120))
21(chain D and (resid 1 through 88 or resid 90 through 120))
31(chain F and (resid 1 through 88 or resid 90 through 120))
41(chain H and (resid 1 through 88 or resid 90 through 120))
12chain A
22chain C
32chain E
42chain G
13(chain P and (resid 23 through 31 or (resid 32...
23(chain Q and (resid 23 through 31 or (resid 32...
33(chain R and (resid 23 through 36 or resid 38...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLUGLUSERSER(chain B and (resid 1 through 88 or resid 90 through 120))BF1 - 883 - 90
121ASPASPGLYGLY(chain B and (resid 1 through 88 or resid 90 through 120))BF90 - 12092 - 122
211GLUGLUSERSER(chain D and (resid 1 through 88 or resid 90 through 120))DH1 - 883 - 90
221ASPASPGLYGLY(chain D and (resid 1 through 88 or resid 90 through 120))DH90 - 12092 - 122
311GLUGLUSERSER(chain F and (resid 1 through 88 or resid 90 through 120))FJ1 - 883 - 90
321ASPASPGLYGLY(chain F and (resid 1 through 88 or resid 90 through 120))FJ90 - 12092 - 122
411GLUGLUSERSER(chain H and (resid 1 through 88 or resid 90 through 120))HL1 - 883 - 90
421ASPASPGLYGLY(chain H and (resid 1 through 88 or resid 90 through 120))HL90 - 12092 - 122
112GLYGLYLYSLYSchain AAE-1 - 1071 - 109
212GLYGLYLYSLYSchain CCG-1 - 1071 - 109
312GLYGLYLYSLYSchain EEI-1 - 1071 - 109
412GLYGLYLYSLYSchain GGK-1 - 1071 - 109
113SERSERTHRTHR(chain P and (resid 23 through 31 or (resid 32...PA23 - 311 - 9
123GLUGLUGLUGLU(chain P and (resid 23 through 31 or (resid 32...PA3210
133SERSERASNASN(chain P and (resid 23 through 31 or (resid 32...PA23 - 1821 - 160
143SERSERASNASN(chain P and (resid 23 through 31 or (resid 32...PA23 - 1821 - 160
153SERSERASNASN(chain P and (resid 23 through 31 or (resid 32...PA23 - 1821 - 160
163SERSERASNASN(chain P and (resid 23 through 31 or (resid 32...PA23 - 1821 - 160
213SERSERTHRTHR(chain Q and (resid 23 through 31 or (resid 32...QB23 - 311 - 9
223GLUGLUGLUGLU(chain Q and (resid 23 through 31 or (resid 32...QB3210
233SERSERASNASN(chain Q and (resid 23 through 31 or (resid 32...QB23 - 1821 - 160
243SERSERASNASN(chain Q and (resid 23 through 31 or (resid 32...QB23 - 1821 - 160
253SERSERASNASN(chain Q and (resid 23 through 31 or (resid 32...QB23 - 1821 - 160
263SERSERASNASN(chain Q and (resid 23 through 31 or (resid 32...QB23 - 1821 - 160
313SERSERARGARG(chain R and (resid 23 through 36 or resid 38...RC23 - 361 - 14
323TYRTYRPROPRO(chain R and (resid 23 through 36 or resid 38...RC38 - 5816 - 36
333SERSERILEILE(chain R and (resid 23 through 36 or resid 38...RC69 - 8047 - 58
343HISHISALAALA(chain R and (resid 23 through 36 or resid 38...RC99 - 10077 - 78
353GLNGLNGLNGLN(chain R and (resid 23 through 36 or resid 38...RC10179
363SERSERALAALA(chain R and (resid 23 through 36 or resid 38...RC23 - 1791 - 157
373SERSERALAALA(chain R and (resid 23 through 36 or resid 38...RC23 - 1791 - 157
383SERSERALAALA(chain R and (resid 23 through 36 or resid 38...RC23 - 1791 - 157
393SERSERALAALA(chain R and (resid 23 through 36 or resid 38...RC23 - 1791 - 157

NCS ensembles :
ID
1
2
3

-
Components

#1: Protein
Bcl-2 homologous antagonist/killer / Apoptosis regulator BAK / Bcl-2-like protein 7 / Bcl2-L-7


Mass: 18452.590 Da / Num. of mol.: 4 / Mutation: L100A, C166S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BAK1, BAK, BCL2L7, CDN1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q16611
#2: Antibody
7D10 antibody VL fragment


Mass: 11728.907 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Production host: Brevibacillus brevis (bacteria)
#3: Antibody
7D10 antibody VH fragment


Mass: 14262.789 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Production host: Brevibacillus brevis (bacteria)
#4: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.23 Å3/Da / Density % sol: 61.97 %
Crystal growTemperature: 281 K / Method: vapor diffusion, sitting drop
Details: 38.9 % 2-methyl-2,4-pentanediol, 0.1 M Sodium cacodylate pH 6.44, 4 % Polyethylene glycol 8000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER2 X 9M / Detector: PIXEL / Date: Feb 28, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 3.1→39.385 Å / Num. obs: 40131 / % possible obs: 98.5 % / Redundancy: 3.5 % / Biso Wilson estimate: 66.95 Å2 / CC1/2: 0.98 / Net I/σ(I): 6.8
Reflection shellResolution: 3.1→3.21 Å / Mean I/σ(I) obs: 1.2 / Num. unique obs: 3207 / CC1/2: 0.43 / % possible all: 98.1

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
XDSdata reduction
PHASERphasing
PDB_EXTRACT3.27data extraction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5W5X

5w5x


Resolution: 3.1→39.385 Å / SU ML: 0.49 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 26.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2621 1711 4.26 %
Rwork0.2144 38420 -
obs0.2164 40131 98.46 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 301.22 Å2 / Biso mean: 85.1927 Å2 / Biso min: 16.56 Å2
Refinement stepCycle: final / Resolution: 3.1→39.385 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11533 0 56 18 11607
Biso mean--73.41 30.05 -
Num. residues----1500
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00211896
X-RAY DIFFRACTIONf_angle_d0.50216160
X-RAY DIFFRACTIONf_dihedral_angle_d16.0226915
X-RAY DIFFRACTIONf_chiral_restr0.0381763
X-RAY DIFFRACTIONf_plane_restr0.0032077
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11B1987X-RAY DIFFRACTION11.047TORSIONAL
12D1987X-RAY DIFFRACTION11.047TORSIONAL
13F1987X-RAY DIFFRACTION11.047TORSIONAL
14H1987X-RAY DIFFRACTION11.047TORSIONAL
21A2195X-RAY DIFFRACTION11.047TORSIONAL
22C2195X-RAY DIFFRACTION11.047TORSIONAL
23E2195X-RAY DIFFRACTION11.047TORSIONAL
24G2195X-RAY DIFFRACTION11.047TORSIONAL
31P1693X-RAY DIFFRACTION11.047TORSIONAL
32Q1693X-RAY DIFFRACTION11.047TORSIONAL
33R1693X-RAY DIFFRACTION11.047TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.1001-3.19120.35681480.3257320798
3.1912-3.29420.35571390.3049313598
3.2942-3.41190.36091420.2862320098
3.4119-3.54840.28321390.2476321198
3.5484-3.70980.29381470.2358315799
3.7098-3.90520.27431330.2241321699
3.9052-4.14960.24851470.2142318298
4.1496-4.46960.21991480.1794320199
4.4696-4.91870.22811460.1669320098
4.9187-5.62860.22571300.1936323899
5.6286-7.08470.27881460.2247322199
7.0847-39.3850.22851460.1825325299
Refinement TLS params.

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

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.58440.267-0.13284.2256-1.94351.92330.03540.02040.31680.04920.0380.154-0.41330.097-0.03460.6848-0.05920.03850.4554-0.080.3227-8.726854.650745.0183
21.876-0.58950.29411.57650.25130.6995-0.003-0.16480.5705-0.0149-0.085-0.1582-0.2401-0.01460.0470.6483-0.0370.11750.44470.02420.473-1.845954.853320.3446
31.83321.32090.51843.92190.59821.42890.08270.0119-0.436-0.0170.074-0.37340.2307-0.0782-0.09550.4255-0.01430.06060.4610.06630.3692-22.4172130.899736.7757
43.2123-0.8657-1.07971.2665-0.31531.59390.0729-0.0249-0.2045-0.0212-0.1070.00830.0256-0.00510.05430.5187-0.0356-0.06110.3664-0.04810.2693-28.8944143.9114.9957
50.5968-1.0884-1.18456.11810.25043.2371-0.5653-0.22040.8605-0.57880.609-0.03950.49530.07-0.07850.7410.0452-0.2080.4060.02371.0486-11.313871.756831.6178
65.5304-2.3838-0.09776.6273-0.23832.8848-0.0244-0.6118-0.1617-0.50480.19760.23360.0887-0.3155-0.15620.6651-0.00820.06010.51360.06431.2083-24.0076108.270624.3385
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'P' and (resid 49 through 58 ) or chain 'E' or chain 'F'P0
2X-RAY DIFFRACTION2chain 'R' and (resid 49 through 60) or chain 'A' or chain 'B'R0
3X-RAY DIFFRACTION3chain 'Q' and (resid 49 through 60) or chain 'G' or chain 'H'Q0
4X-RAY DIFFRACTION4chain 'S' and (resid 49 through 61) or chain 'C' or chain 'D'S0
5X-RAY DIFFRACTION5chain 'P' and (not (resid 49 through 61)) or chain 'R' and (not (resid 49 through 61))P0
6X-RAY DIFFRACTION6chain 'Q' and (not (resid 49 through 61)) or chain 'S' and (not (resid 49 through 61))Q0

+
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