[English] 日本語
Yorodumi
- PDB-6f5d: Trypanosoma brucei F1-ATPase -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6f5d
TitleTrypanosoma brucei F1-ATPase
Components
  • (ATP synthase subunit ...) x 5
  • ATP synthase gamma subunit
KeywordsHYDROLASE / ATP synthase / mitochondria / trypanosoma brucei / p18
Function / homology
Function and homology information


proton-transporting two-sector ATPase complex / H+-transporting two-sector ATPase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / kinetoplast / ATP biosynthetic process / : / : / : / : / proton motive force-driven ATP synthesis ...proton-transporting two-sector ATPase complex / H+-transporting two-sector ATPase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / kinetoplast / ATP biosynthetic process / : / : / : / : / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / chloroplast thylakoid membrane / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton transmembrane transport / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / mitochondrial inner membrane / hydrolase activity / GTP binding / ATP hydrolysis activity / mitochondrion / ATP binding / plasma membrane / cytoplasm
Similarity search - Function
Thrombin, subunit H - #170 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain ...Thrombin, subunit H - #170 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Tetratricopeptide-like helical domain superfamily / Thrombin, subunit H / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit delta, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase subunit p18, mitochondrial / Uncharacterized protein / ATP synthase F1 subunit gamma protein, putative / ATP synthase alpha chain, mitochondrial / ATP synthase subunit beta / Ribonucleoprotein p18, mitochondrial, putative ...ADENOSINE-5'-DIPHOSPHATE / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit delta, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase subunit p18, mitochondrial / Uncharacterized protein / ATP synthase F1 subunit gamma protein, putative / ATP synthase alpha chain, mitochondrial / ATP synthase subunit beta / Ribonucleoprotein p18, mitochondrial, putative / ATP synthase, epsilon chain, putative / ATP synthase subunit beta, mitochondrial / ATP synthase subunit alpha, mitochondrial
Similarity search - Component
Biological speciesTrypanosoma brucei brucei (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.2 Å
AuthorsMontgomery, M.G. / Gahura, O. / Leslie, A.G.W. / Zikova, A. / Walker, J.E.
Funding support United Kingdom, Czech Republic, 6items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)MR/M009858/1 United Kingdom
Medical Research Council (United Kingdom)MC_U105663150 United Kingdom
Medical Research Council (United Kingdom)MC_U105184325 United Kingdom
Ministry of Education ERC CZLL1205 Czech Republic
Postdok_BIOGLOBECZ.1.07/2.3.00/30.0032 Czech Republic
European Molecular Biology OrganizationASTF 81-2016
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018
Title: ATP synthase fromTrypanosoma bruceihas an elaborated canonical F1-domain and conventional catalytic sites.
Authors: Montgomery, M.G. / Gahura, O. / Leslie, A.G.W. / Zikova, A. / Walker, J.E.
History
DepositionDec 1, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 21, 2018Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 2.0Aug 15, 2018Group: Data collection / Database references ...Data collection / Database references / Non-polymer description / Structure summary
Category: chem_comp / entity ...chem_comp / entity / entity_name_com / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _chem_comp.formula / _chem_comp.formula_weight ..._chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _entity.pdbx_description / _entity.pdbx_ec / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession
Revision 2.1Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_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
A: ATP synthase subunit alpha, mitochondrial
B: ATP synthase subunit alpha, mitochondrial
C: ATP synthase subunit alpha, mitochondrial
D: ATP synthase subunit beta, mitochondrial
E: ATP synthase subunit beta, mitochondrial
F: ATP synthase subunit beta, mitochondrial
G: ATP synthase gamma subunit
H: ATP synthase subunit delta, mitochondrial
I: ATP synthase subunit epsilon, mitochondrial
J: ATP synthase subunit p18, mitochondrial
K: ATP synthase subunit p18, mitochondrial
L: ATP synthase subunit p18, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)464,52523
Polymers461,84012
Non-polymers2,68511
Water36020
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, mass spectrometry, native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area62560 Å2
ΔGint-388 kcal/mol
Surface area143640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)124.218, 206.350, 130.210
Angle α, β, γ (deg.)90.00, 104.85, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13B
23C
14D
24E
15D
25F
16E
26F
17J
27K
18J
28L
19K
29L

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PHEPHEVALVALAA22 - 56022 - 560
21PHEPHEVALVALBB22 - 56022 - 560
12PHEPHEALAALAAA22 - 55922 - 559
22PHEPHEALAALACC22 - 55922 - 559
13PHEPHEVALVALBB22 - 56022 - 560
23PHEPHEVALVALCC22 - 56022 - 560
14ASPASPLYSLYSDD8 - 4878 - 487
24ASPASPLYSLYSEE8 - 4878 - 487
15ASPASPLYSLYSDD8 - 4878 - 487
25ASPASPLYSLYSFF8 - 4878 - 487
16ALAALAALAALAEE7 - 4917 - 491
26ALAALAALAALAFF7 - 4917 - 491
17ALAALAASPASPJJ6 - 1666 - 166
27ALAALAASPASPKK6 - 1666 - 166
18ALAALALYSLYSJJ6 - 1686 - 168
28ALAALALYSLYSLL6 - 1686 - 168
19ALAALAASPASPKK6 - 1666 - 166
29ALAALAASPASPLL6 - 1666 - 166

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9

-
Components

-
ATP synthase subunit ... , 5 types, 11 molecules ABCDEFHIJKL

#1: Protein ATP synthase subunit alpha, mitochondrial / ATP synthase F1 subunit alpha


Mass: 61087.488 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427 / References: UniProt: Q9GS23, UniProt: Q57TX9*PLUS
#2: Protein ATP synthase subunit beta, mitochondrial / ATP synthase F1 subunit beta


Mass: 53617.234 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427
References: UniProt: Q9GPE9, UniProt: Q57XX1*PLUS, H+-transporting two-sector ATPase
#4: Protein ATP synthase subunit delta, mitochondrial / ATP synthase F1 subunit delta


Mass: 18177.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427 / References: UniProt: P0DPG2, UniProt: Q586H1*PLUS
#5: Protein ATP synthase subunit epsilon, mitochondrial / ATP synthase F1 subunit epsilon


Mass: 7660.534 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427 / References: UniProt: P0DPG3, UniProt: Q38B96*PLUS
#6: Protein ATP synthase subunit p18, mitochondrial / ATP synthase F1 subunit p18


Mass: 19191.742 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427 / References: UniProt: P0DPG4, UniProt: Q57ZP0*PLUS

-
Protein , 1 types, 1 molecules G

#3: Protein ATP synthase gamma subunit / F1F0-ATPase gamma subunit


Mass: 34313.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Variant: 427
References: UniProt: A0A161CFW5, UniProt: Q38CM0*PLUS, H+-transporting two-sector ATPase

-
Non-polymers , 3 types, 31 molecules

#7: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.48 Å3/Da / Density % sol: 64.61 %
Crystal growTemperature: 277 K / Method: microbatch
Details: 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgSO4 and 1 mM ADP, 7.7% (w/v) polyethyleneglycol 10000 dissolved in a buffer containing 100 mM 2-(N-morpholino)-ethanesulfonic acid, pH 6.0

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.966 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Jun 19, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.966 Å / Relative weight: 1
ReflectionResolution: 3.2→90.51 Å / Num. obs: 102391 / % possible obs: 98.2 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.123 / Net I/σ(I): 8.1
Reflection shellResolution: 3.2→3.25 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.565 / % possible all: 97.6

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
REFMAC5.8.0190refinement
Aimless0.5.32data scaling
PHASER2.7.17phasing
PDB_EXTRACT3.24data extraction
MOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2JDI

2jdi


Resolution: 3.2→90.51 Å / Cor.coef. Fo:Fc: 0.879 / Cor.coef. Fo:Fc free: 0.849 / SU B: 39.307 / SU ML: 0.605 / Cross valid method: THROUGHOUT / ESU R Free: 0.562 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.29712 4968 5 %RANDOM
Rwork0.27169 ---
obs0.27297 94768 95.59 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 89.235 Å2
Baniso -1Baniso -2Baniso -3
1-0.05 Å2-0 Å26.82 Å2
2---0.84 Å2-0 Å2
3----2.48 Å2
Refinement stepCycle: 1 / Resolution: 3.2→90.51 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms30905 0 167 20 31092
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01931650
X-RAY DIFFRACTIONr_bond_other_d0.0010.0229909
X-RAY DIFFRACTIONr_angle_refined_deg1.0661.97642896
X-RAY DIFFRACTIONr_angle_other_deg0.869369355
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.38353985
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.76424.4351344
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.725155513
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.09415181
X-RAY DIFFRACTIONr_chiral_restr0.060.24930
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02134943
X-RAY DIFFRACTIONr_gen_planes_other0.0010.026112
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_it1.5549.09116000
X-RAY DIFFRACTIONr_mcbond_other1.5549.09115999
X-RAY DIFFRACTIONr_mcangle_it2.7613.62619990
X-RAY DIFFRACTIONr_mcangle_other2.75913.62719991
X-RAY DIFFRACTIONr_scbond_it1.1019.18815650
X-RAY DIFFRACTIONr_scbond_other1.1019.18715648
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.03213.71122906
X-RAY DIFFRACTIONr_long_range_B_refined4.54834736
X-RAY DIFFRACTIONr_long_range_B_other4.54834737
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)
11A310600.09
12B310600.09
21A311720.08
22C311720.08
31B309840.09
32C309840.09
41D274900.1
42E274900.1
51D283320.08
52F283320.08
61E275660.1
62F275660.1
71J89400.12
72K89400.12
81J90000.12
82L90000.12
91K88580.13
92L88580.13
LS refinement shellResolution: 3.2→3.283 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.433 302 -
Rwork0.397 5503 -
obs--75.68 %

+
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