[English] 日本語
Yorodumi
- PDB-4pjf: Structure of human MR1-Ac-6-FP in complex with human MAIT B-C10 TCR -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4pjf
TitleStructure of human MR1-Ac-6-FP in complex with human MAIT B-C10 TCR
Components
  • Beta-2-microglobulinBeta-2 microglobulin
  • Major histocompatibility complex class I-related gene protein
  • TCR-alpha
  • TCR-beta
KeywordsIMMUNE SYSTEM / MR1 / TCR / Immune complex / Ac-6-FP
Function / homology
Function and homology information


positive regulation of T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of exogenous antigen / MHC class I receptor activity / antigen processing and presentation of peptide antigen via MHC class I / beta-2-microglobulin binding / T cell receptor binding / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / early endosome lumen / positive regulation of receptor binding ...positive regulation of T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of exogenous antigen / MHC class I receptor activity / antigen processing and presentation of peptide antigen via MHC class I / beta-2-microglobulin binding / T cell receptor binding / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / early endosome lumen / positive regulation of receptor binding / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / negative regulation of receptor binding / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / response to molecule of bacterial origin / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / cellular response to iron ion / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / recycling endosome membrane / specific granule lumen / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon gamma signaling / positive regulation of immune response / negative regulation of epithelial cell proliferation / Modulation by Mtb of host immune system / positive regulation of T cell activation / sensory perception of smell / negative regulation of neuron projection development / tertiary granule lumen / DAP12 signaling / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / positive regulation of protein binding / ER-Phagosome pathway / iron ion transport / protein refolding / early endosome membrane / protein homotetramerization / intracellular iron ion homeostasis / defense response to Gram-negative bacterium / amyloid fibril formation / learning or memory / defense response to Gram-positive bacterium / immune response / Amyloid fiber formation / lysosomal membrane / endoplasmic reticulum lumen / external side of plasma membrane / Golgi membrane / focal adhesion / innate immune response / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / Golgi apparatus / endoplasmic reticulum / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / membrane / identical protein binding / plasma membrane / cytosol
Similarity search - Function
MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. ...MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-30W / Beta-2-microglobulin / Major histocompatibility complex class I-related gene protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.45 Å
AuthorsBirkinshaw, R.W. / Rossjohn, J.
CitationJournal: J.Exp.Med. / Year: 2014
Title: A molecular basis underpinning the T cell receptor heterogeneity of mucosal-associated invariant T cells.
Authors: Eckle, S.B. / Birkinshaw, R.W. / Kostenko, L. / Corbett, A.J. / McWilliam, H.E. / Reantragoon, R. / Chen, Z. / Gherardin, N.A. / Beddoe, T. / Liu, L. / Patel, O. / Meehan, B. / Fairlie, D.P. ...Authors: Eckle, S.B. / Birkinshaw, R.W. / Kostenko, L. / Corbett, A.J. / McWilliam, H.E. / Reantragoon, R. / Chen, Z. / Gherardin, N.A. / Beddoe, T. / Liu, L. / Patel, O. / Meehan, B. / Fairlie, D.P. / Villadangos, J.A. / Godfrey, D.I. / Kjer-Nielsen, L. / McCluskey, J. / Rossjohn, J.
History
DepositionMay 12, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 9, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 6, 2014Group: Database references
Revision 1.2Sep 3, 2014Group: Refinement description
Revision 1.3Oct 1, 2014Group: Database references
Revision 1.4Dec 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description / Source and taxonomy
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / diffrn_source / entity_src_gen / pdbx_database_status / pdbx_struct_oper_list / refine_hist
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_oper_list.symmetry_operation / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_nucleic_acid
Remark 0 : statistics at the very beginning when nothing is done yet

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Major histocompatibility complex class I-related gene protein
B: Beta-2-microglobulin
C: Major histocompatibility complex class I-related gene protein
D: Beta-2-microglobulin
E: TCR-alpha
F: TCR-beta
G: TCR-alpha
H: TCR-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)188,98912
Polymers188,3388
Non-polymers6514
Water15,025834
1
A: Major histocompatibility complex class I-related gene protein
B: Beta-2-microglobulin
G: TCR-alpha
H: TCR-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,5867
Polymers94,1694
Non-polymers4173
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Major histocompatibility complex class I-related gene protein
D: Beta-2-microglobulin
E: TCR-alpha
F: TCR-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,4025
Polymers94,1694
Non-polymers2331
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)218.987, 71.698, 144.031
Angle α, β, γ (deg.)90.00, 104.85, 90.00
Int Tables number5
Space group name H-MC121

-
Components

-
Protein , 4 types, 8 molecules ACBDEGFH

#1: Protein Major histocompatibility complex class I-related gene protein / MHC class I-related gene protein / Class I histocompatibility antigen-like protein


Mass: 31711.670 Da / Num. of mol.: 2 / Fragment: UNP residues 23-292 / Mutation: C262S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MR1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q95460
#2: Protein Beta-2-microglobulin / Beta-2 microglobulin


Mass: 11879.356 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / References: UniProt: P61769
#3: Protein TCR-alpha


Mass: 22891.295 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: Protein TCR-beta


Mass: 27686.791 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)

-
Non-polymers , 3 types, 838 molecules

#5: Chemical ChemComp-30W / N-(6-formyl-4-oxo-3,4-dihydropteridin-2-yl)acetamide / Acetyl 6-formylpterin


Mass: 233.184 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H7N5O3
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 834 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.9 Å3/Da / Density % sol: 57.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, Bis-tris propane, sodium acetate

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.95 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 12, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.95 Å / Relative weight: 1
ReflectionResolution: 2.45→69.6 Å / Num. obs: 79322 / % possible obs: 98.8 % / Redundancy: 3.4 % / Biso Wilson estimate: 57.44 Å2 / Net I/σ(I): 12.7

-
Processing

SoftwareName: BUSTER / Version: 2.10.0 / Classification: refinement
RefinementResolution: 2.45→35.87 Å / Cor.coef. Fo:Fc: 0.9414 / Cor.coef. Fo:Fc free: 0.9248 / SU R Cruickshank DPI: 0.31 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.319 / SU Rfree Blow DPI: 0.212 / SU Rfree Cruickshank DPI: 0.212
RfactorNum. reflection% reflectionSelection details
Rfree0.2118 3969 5.02 %RANDOM
Rwork0.1781 ---
obs0.1798 78987 98.99 %-
Displacement parametersBiso mean: 48.89 Å2
Baniso -1Baniso -2Baniso -3
1-3.8398 Å20 Å22.9713 Å2
2---8.7426 Å20 Å2
3---4.9029 Å2
Refine analyzeLuzzati coordinate error obs: 0.303 Å
Refinement stepCycle: 1 / Resolution: 2.45→35.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12331 0 44 834 13209
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00912726HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.0817353HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d4109SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes298HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1903HARMONIC5
X-RAY DIFFRACTIONt_it12726HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.26
X-RAY DIFFRACTIONt_other_torsion17.82
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1639SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact13931SEMIHARMONIC4
LS refinement shellResolution: 2.45→2.51 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2781 304 5.19 %
Rwork0.2219 5556 -
all0.2248 5860 -
obs--98.99 %
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)
11.20120.4188-0.3111.6904-0.22472.11040.03550.17570.0692-0.0065-0.05440.315-0.1925-0.10630.019-0.0755-0.00660.0204-0.0023-0.033-0.0254-6.239861.6531161.0819
22.13480.3715-0.37612.8489-0.38291.20240.0992-0.1025-0.16810.3035-0.187-0.00060.05570.16250.0878-0.0272-0.04010.0112-0.0277-0.023-0.14892.026455.0676171.5377
33.10691.1212-0.692.94090.61040.95030.0178-0.3323-0.14140.1332-0.0540.09910.1122-0.02470.0362-0.04520.04820.0122-0.05220.0016-0.0499-22.199371.1092191.7997
44.5228-1.3395-0.80393.06350.89981.79560.00180.59360.1639-0.3198-0.05030.4193-0.2168-0.38950.0485-0.12190.0101-0.0182-0.0282-0.0101-0.0651-29.033263.3331171.7164
51.54820.3-0.45741.7543-0.43351.71830.0131-0.25310.22850.05280.10430.17640.0143-0.2455-0.1174-0.13090.0578-0.03870.067-0.0056-0.0766-50.354240.098193.3372
62.19230.143-0.26543.18660.19020.8530.03440.08620.1711-0.16890.039-0.2434-0.04650.0055-0.0734-0.070.0116-0.0221-0.02650.0008-0.0832-37.862143.6742182.6943
72.4346-0.63531.9170.8514-0.0782.176-0.19170.07650.3856-0.1255-0.0052-0.0594-0.1035-0.1170.1969-0.078-0.0693-0.07290.04380.1014-0.0334-65.943139.1128167.1368
88.8097-0.25630.27661.6485-0.00812.3614-0.1533-0.29320.9967-0.05610.15120.5946-0.4278-0.62870.0021-0.24880.1524-0.0728-0.0353-0.00130.0155-69.074553.2067183.1553
90.6796-2.01822.01161.20310.58551.01890.08280.0521-0.0374-0.07990.07390.0724-0.03280.0983-0.15680.02040.03850.0055-0.0274-0.0154-0.0005-20.365812.896196.7519
104.0056-1.02840.69921.6312-0.74852.70650.0066-0.0023-0.2045-0.05620.09230.14570.11280.0677-0.0989-0.05490.0749-0.0289-0.1022-0.038-0.1414-25.969322.6421194.7086
112.0069-2.21343.12854.5675-2.47065.36050.03290.15670.0884-0.41740.0158-0.09690.0430.0112-0.04870.02090.05630.0408-0.015-0.0372-0.069-21.366521.3838187.1094
121.2852-1.49351.44161.1344-1.10420.6741-0.03040.1357-0.1611-0.02320.0550.0667-0.063-0.0093-0.02460.04140.06850.01070.1473-0.0866-0.0398-15.122717.1146201.2148
134.0157-1.3357-2.3730.15392.27425.2774-0.10.2531-0.46820.05260.0515-0.00840.6225-0.43680.04850.0615-0.0730.0353-0.1715-0.0435-0.0733-3.36625.7813219.2347
143.7683-0.008-1.49514.1551-1.09416.5345-0.19740.278-0.43810.07640.0672-0.02590.49140.03830.13020-0.06440.0608-0.0489-0.1192-0.06951.04996.5603214.6152
150.8889-0.77291.14951.0032-0.91511.8748-0.1242-0.27510.06670.05450.06520.0635-0.1796-0.36550.059-0.09270.09170.00020.1254-0.0429-0.1454-32.898528.3625214.3745
164.5873-0.4029-2.99820.58730.87823.00460.07620.4124-0.0306-0.0759-0.0141-0.1305-0.0938-0.2418-0.0622-0.04070.0506-0.0271-0.0238-0.0291-0.1215-6.182419.0248225.1392
172.5160.2767-0.12360.6979-0.24310.8680.0492-0.02450.0320.0569-0.0754-0.07690.05670.19390.0261-0.067-0.0311-0.0360.04730.0405-0.12527.740362.1488160.1816
187.78170.4542-1.41764.62730.04812.1656-0.013-0.13720.12430.0599-0.0364-0.212-0.02240.30930.0493-0.31280.0721-0.0203-0.0140.0645-0.032455.875760.6354142.3933
1910.2053.38420.464500.75626.4796-0.0962-0.27540.33160.21580.0719-0.03060.12520.08430.0243-0.04060.0367-0.0656-0.01630.08110.036649.021460.0806140.4073
204.59471.57531.35910.52672.49920.9237-0.07930.25950.43710.10030.2355-0.31180.09550.3435-0.1562-0.18570.0649-0.08410.03640.07690.215757.29264.3738139.0847
211.7383-0.0776-1.26520.6787-0.15531.5275-0.00080.19490.0217-0.1239-0.0385-0.04210.0804-0.07140.0393-0.0402-0.0241-0.0257-0.03560.0168-0.148815.069961.7765140.0799
225.3973-0.89253.03373.0008-0.85374.27630.29590.3794-0.6480.02920.043-0.2490.49690.554-0.3389-0.04580.08640.0479-0.1234-0.0374-0.138142.455555.3661129.5695
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{A|1 - 84}
2X-RAY DIFFRACTION2{A|85 - 171}
3X-RAY DIFFRACTION3{A|172 - 269}
4X-RAY DIFFRACTION4{B|0 - 98}
5X-RAY DIFFRACTION5{C|1 - 83}
6X-RAY DIFFRACTION6{C|84 - 158}
7X-RAY DIFFRACTION7{C|159 - 269}
8X-RAY DIFFRACTION8{D|1 - 97}
9X-RAY DIFFRACTION9{E|1 - 17}
10X-RAY DIFFRACTION10{E|18 - 52}
11X-RAY DIFFRACTION11{E|53 - 75}
12X-RAY DIFFRACTION12{E|76 - 120}
13X-RAY DIFFRACTION13{E|121 - 156}
14X-RAY DIFFRACTION14{E|157 - 198}
15X-RAY DIFFRACTION15{F|3 - 123}
16X-RAY DIFFRACTION16{F|124 - 242}
17X-RAY DIFFRACTION17{G|1 - 108}
18X-RAY DIFFRACTION18{G|109 - 145}
19X-RAY DIFFRACTION19{G|146 - 165}
20X-RAY DIFFRACTION20{G|166 - 198}
21X-RAY DIFFRACTION21{H|3 - 123}
22X-RAY DIFFRACTION22{H|124 - 242}

+
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