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- PDB-3utt: 1E6-A*0201-ALWGPDPAAA Complex, Triclinic -

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Open data


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Basic information

Entry
Database: PDB / ID: 3utt
Title1E6-A*0201-ALWGPDPAAA Complex, Triclinic
Components
  • 1E6 TCR Alpha Chain
  • 1E6 TCR Beta Chain
  • Beta-2-microglobulinBeta-2 microglobulin
  • HLA class I histocompatibility antigen, A-2 alpha chain
  • Insulin
KeywordsIMMUNE SYSTEM / Major Histocompatibility Complex / Human Leukocyte antigen / Type I Diabetes / T cell Receptor
Function / homology
Function and homology information


negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / Signaling by Insulin receptor / IRS activation / nitric oxide-cGMP-mediated signaling / negative regulation of fatty acid metabolic process / Insulin processing / negative regulation of feeding behavior / regulation of protein secretion ...negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / Signaling by Insulin receptor / IRS activation / nitric oxide-cGMP-mediated signaling / negative regulation of fatty acid metabolic process / Insulin processing / negative regulation of feeding behavior / regulation of protein secretion / positive regulation of peptide hormone secretion / Regulation of gene expression in beta cells / positive regulation of respiratory burst / T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / positive regulation of dendritic spine maintenance / alpha-beta T cell activation / positive regulation of memory T cell activation / TAP complex binding / negative regulation of acute inflammatory response / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / negative regulation of respiratory burst involved in inflammatory response / negative regulation of protein secretion / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / CD8 receptor binding / fatty acid homeostasis / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of glycogen biosynthetic process / positive regulation of lipid biosynthetic process / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of gluconeogenesis / positive regulation of nitric oxide mediated signal transduction / endoplasmic reticulum exit site / regulation of protein localization to plasma membrane / beta-2-microglobulin binding / COPI-mediated anterograde transport / negative regulation of lipid catabolic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of insulin receptor signaling pathway / TAP binding / negative regulation of reactive oxygen species biosynthetic process / transport vesicle / positive regulation of protein autophosphorylation / protection from natural killer cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / Insulin receptor recycling / insulin-like growth factor receptor binding / NPAS4 regulates expression of target genes / positive regulation of protein metabolic process / neuron projection maintenance / detection of bacterium / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of brown fat cell differentiation / activation of protein kinase B activity / T cell receptor binding / positive regulation of glycolytic process / Insulin receptor signalling cascade / positive regulation of mitotic nuclear division / 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 / Regulation of insulin secretion / positive regulation of nitric-oxide synthase activity / positive regulation of long-term synaptic potentiation / endosome lumen / positive regulation of cytokine production / acute-phase response / positive regulation of protein secretion / lumenal side of endoplasmic reticulum membrane / regulation of transmembrane transporter activity / positive regulation of cell differentiation / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / positive regulation of glucose import / negative regulation of proteolysis / regulation of synaptic plasticity / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / wound healing / negative regulation of forebrain neuron differentiation / insulin receptor binding / ER to Golgi transport vesicle membrane / response to molecule of bacterial origin / regulation of erythrocyte differentiation / regulation of iron ion transport / negative regulation of protein catabolic process / MHC class I peptide loading complex / positive regulation of neuron projection development / hormone activity / HFE-transferrin receptor complex / T cell mediated cytotoxicity
Similarity search - Function
Insulin / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily / MHC class I, alpha chain, C-terminal / MHC_I C-terminus ...Insulin / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / 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
Insulin / HLA class I histocompatibility antigen, A alpha chain / HLA class I histocompatibility antigen, A alpha chain / Beta-2-microglobulin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsRizkallah, P.J. / Cole, D.K. / Sewell, A.K. / Bulek, A.M. / Rossjohn, J. / Gras, S.
CitationJournal: Nat.Immunol. / Year: 2012
Title: Structural basis for the killing of human beta cells by CD8(+) T cells in type 1 diabetes.
Authors: Bulek, A.M. / Cole, D.K. / Skowera, A. / Dolton, G. / Gras, S. / Madura, F. / Fuller, A. / Miles, J.J. / Gostick, E. / Price, D.A. / Drijfhout, J.W. / Knight, R.R. / Huang, G.C. / Lissin, N. ...Authors: Bulek, A.M. / Cole, D.K. / Skowera, A. / Dolton, G. / Gras, S. / Madura, F. / Fuller, A. / Miles, J.J. / Gostick, E. / Price, D.A. / Drijfhout, J.W. / Knight, R.R. / Huang, G.C. / Lissin, N. / Molloy, P.E. / Wooldridge, L. / Jakobsen, B.K. / Rossjohn, J. / Peakman, M. / Rizkallah, P.J. / Sewell, A.K.
History
DepositionNov 26, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 7, 2012Group: Database references
Revision 1.2Jul 17, 2019Group: Data collection / Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: Insulin
D: 1E6 TCR Alpha Chain
E: 1E6 TCR Beta Chain
F: HLA class I histocompatibility antigen, A-2 alpha chain
G: Beta-2-microglobulin
H: Insulin
I: 1E6 TCR Alpha Chain
J: 1E6 TCR Beta Chain


Theoretical massNumber of molelcules
Total (without water)189,99910
Polymers189,99910
Non-polymers00
Water2,720151
1
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: Insulin
D: 1E6 TCR Alpha Chain
E: 1E6 TCR Beta Chain


Theoretical massNumber of molelcules
Total (without water)95,0005
Polymers95,0005
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: HLA class I histocompatibility antigen, A-2 alpha chain
G: Beta-2-microglobulin
H: Insulin
I: 1E6 TCR Alpha Chain
J: 1E6 TCR Beta Chain


Theoretical massNumber of molelcules
Total (without water)95,0005
Polymers95,0005
Non-polymers00
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)41.480, 98.440, 121.300
Angle α, β, γ (deg.)97.270, 98.160, 93.380
Int Tables number1
Space group name H-MP1

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Components

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Protein , 4 types, 8 molecules AFBGDIEJ

#1: Protein HLA class I histocompatibility antigen, A-2 alpha chain / MHC Class I Heavy Chain / MHC class I antigen A*2


Mass: 31854.203 Da / Num. of mol.: 2 / Fragment: UNP residues 25-299
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta DE3 / References: UniProt: P01892, UniProt: P04439*PLUS
#2: Protein Beta-2-microglobulin / Beta-2 microglobulin


Mass: 11879.356 Da / Num. of mol.: 2 / Fragment: UNP residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta DE3 / References: UniProt: P61769
#4: Protein 1E6 TCR Alpha Chain


Mass: 22386.768 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) / Strain (production host): Rosetta DE3
#5: Protein 1E6 TCR Beta Chain


Mass: 27911.346 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) / Strain (production host): Rosetta DE3

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Protein/peptide / Non-polymers , 2 types, 153 molecules CH

#3: Protein/peptide Insulin /


Mass: 968.063 Da / Num. of mol.: 2
Fragment: Pre-pro-insulin Derived Peptide (UNP residues 15-24)
Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P01308
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 151 / Source method: isolated from a natural source / Formula: H2O

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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: 2.55 Å3/Da / Density % sol: 51.8 %
Crystal growTemperature: 291 K / Method: vapor diffusion / pH: 6.5
Details: 20% w/v PEG3350, 0.2 M sodium citrate, 0.1 M Bis-tris propane, pH 6.5, VAPOR DIFFUSION, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9778 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 25, 2011 / Details: mirrors
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9778 Å / Relative weight: 1
ReflectionResolution: 2.579→47.925 Å / Num. all: 61204 / Num. obs: 61204 / % possible obs: 97.2 % / Redundancy: 2.2 % / Rsym value: 0.106 / Net I/σ(I): 6.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRsym value% possible all
2.579-2.652.20.7361984344600.73696.7
2.65-2.722.20.6251.2968344300.62596.8
2.72-2.82.20.51.5930242240.596.8
2.8-2.882.20.382919241970.3896.8
2.88-2.982.20.3042.5883840110.30497.2
2.98-3.082.20.2523.1862639320.25297
3.08-3.22.20.1824.2820437410.18297.1
3.2-3.332.20.155805736840.1597
3.33-3.482.20.1315.6746934120.13197.5
3.48-3.652.20.1066.4741534020.10697.1
3.65-3.842.20.0897.1685431240.08997.4
3.84-4.082.20.0818.2646529880.08197.1
4.08-4.362.20.0749617728560.07497.7
4.36-4.712.20.0689.6563926120.06897.4
4.71-5.162.10.06310514724130.06397.4
5.16-5.772.10.0689459221800.06898.3
5.77-6.662.20.06410430219640.06498.4
6.66-8.152.20.0669.5357116440.06698.6
8.15-11.532.20.05111.6275112640.05197.8
11.53-47.9252.10.0729.413956660.07294.7

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Processing

Software
NameVersionClassificationNB
PHENIX1.6.1_357refinement
REFMACrefinement
PDB_EXTRACT3.1data extraction
GDAdata collection
xia2data reduction
PHASERphasing
SCALA3.3.15data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→29.336 Å / Occupancy max: 1 / Occupancy min: 0.44 / SU ML: 0.39 / σ(F): 0.01 / Phase error: 31.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2738 2634 5.08 %
Rwork0.1946 --
obs0.1986 51877 89.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 30.396 Å2 / ksol: 0.329 e/Å3
Displacement parametersBiso max: 271.66 Å2 / Biso mean: 61.3677 Å2 / Biso min: 6.6 Å2
Baniso -1Baniso -2Baniso -3
1-12.3058 Å24.8857 Å23.9699 Å2
2--0.796 Å2-1.5035 Å2
3----13.1017 Å2
Refinement stepCycle: LAST / Resolution: 2.6→29.336 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13369 0 0 151 13520
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00313795
X-RAY DIFFRACTIONf_angle_d0.67118707
X-RAY DIFFRACTIONf_chiral_restr0.0481937
X-RAY DIFFRACTIONf_plane_restr0.0042457
X-RAY DIFFRACTIONf_dihedral_angle_d11.9565051
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5999-2.69270.37882170.28454146436377
2.6927-2.80050.34712200.2724469468980
2.8005-2.92780.37732310.2744625485685
2.9278-3.0820.34992470.23874810505788
3.082-3.27490.30572910.22745013530491
3.2749-3.52740.31472980.20495080537894
3.5274-3.88160.2662870.17815190547795
3.8816-4.44160.22552870.14475260554796
4.4416-5.58960.2083000.13985286558697
5.5896-29.33820.22932560.17525364562097
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)
11.0618-0.74120.65151.1514-0.93231.6051-0.1907-0.06870.06650.56480.12620.1061-0.27730.23610.0485-0.0566-0.0382-0.0890.2798-0.04020.149513.08017.3159-7.9497
20.56080.47570.11870.57650.18240.6940.2720.0855-0.01540.5759-0.1330.04040.2227-0.03180.01230.3956-0.1054-0.07720.3344-0.04220.07227.86670.741826.4945
30.6182-0.0594-0.09030.58230.27571.6839-0.0522-0.09250.05080.3960.12080.051.0366-0.1656-0.01110.1635-0.09220.04680.24630.08570.0963.914-10.8068.1687
40.4458-0.055-0.14230.43190.29331.2205-0.1409-0.232-0.11030.3895-0.0573-0.0390.94670.1787-0.00310.2375-0.03380.0620.27460.0280.09972.8067-13.01387.4028
50.061-0.14070.00190.5678-0.32840.4867-0.18080.0030.07530.1263-0.4469-0.2693-0.06280.7529-0.0999-0.12250.0873-0.0970.41480.08310.279514.775610.2431-15.1681
60.1640.10050.29130.9805-0.06340.3704-0.13410.0313-0.1326-0.05880.1697-0.0584-0.7797-0.23110.05190.571-0.02580.1192-0.00990.00920.289213.6430.7149-31.7865
70.0783-0.1946-0.24560.44680.47971.4059-0.12940.12090.0244-0.990.2288-0.043-0.27830.5057-0.05142.1692-0.3140.06630.06-0.07130.299714.477538.1922-62.8503
81.49250.0721-0.29810.30090.24280.61650.3723-0.36080.4321-0.09190.33760.1673-0.1512-0.17590.00371.8903-0.3032-0.28940.11240.0740.62518.464346.0918-67.2639
90.82880.0341-0.25050.1490.19071.76310.18080.3369-0.1623-0.18230.00070.1027-0.6607-0.20790.041-0.1622-0.1711-0.03730.00790.02760.1966.8349.5917-38.954
100.54260.39720.20770.4590.35140.73720.36230.17940.1492-0.19770.19840.0178-1.40410.14720.04451.2401-0.1230.27870.14210.02650.146113.790226.9079-64.1769
110.6312-0.44680.05190.71880.24181.26660.13090.3413-0.3321-0.39260.4428-0.2556-1.3460.03140.05390.614-0.14940.250.1722-0.13460.251812.507715.532-68.2193
120.66540.6909-0.27921.0649-0.47731.0244-0.4104-0.0261-0.0858-0.67320.1475-0.23110.9677-0.0235-0.3315-0.33370.1703-0.06160.03620.01920.132121.1665-20.5905-54.7557
130.2497-0.05370.04670.23790.25160.7364-0.1701-0.10730.2164-0.30840.1998-0.13520.35380.26730.00010.23880.04090.10020.34480.01990.149625.9-13.6209-89.3465
140.6670.0845-0.06850.44260.19111.71170.21510.1451-0.2115-0.04930.11450.003-0.2072-0.13270.02120.01850.0103-0.02310.16890.05990.172516.493-5.3309-73.2019
150.6216-0.00350.04880.5633-0.15730.7491-0.11550.176-0.0272-0.0125-0.03520.0049-0.325-0.0544-0.00040.15390.0430.00440.1430.04580.11613.5223-1.9976-73.4476
160.20790.7297-0.16144.72660.04550.27990.0175-0.290.1763-0.1837-0.7717-0.05940.0504-0.2666-0.265-0.0041-0.2313-0.15320.1639-0.12910.185421.1179-23.3691-47.4896
170.3751-0.4037-0.07330.9778-0.38921.4216-0.5454-0.41470.09210.13450.4009-0.05490.9771-0.7028-0.01320.4997-0.115-0.0192-0.2552-0.01740.139417.7804-44.25-31.3694
180.1352-0.14090.05990.1705-0.02920.1127-0.1648-0.146-0.04350.46650.36490.3719-0.20030.3076-0.00011.38890.14940.23840.4618-0.10250.504412.0275-52.3791-1.6814
190.0570.034-0.03610.0442-0.04240.0249-0.28890.3058-0.3515-0.18840.5554-0.13080.42060.1198-0.00031.13790.10980.22030.37040.05150.72314.7858-59.20960.883
200.61410.3274-0.09540.35940.36461.6145-0.0161-0.37020.2004-0.0609-0.17220.1113-0.2053-0.46890.00080.05880.088-0.030.3465-0.02370.14277.5508-25.011-27.9148
210.5759-0.6092-0.35620.74430.25920.57640.06490.1115-0.0510.17830.03590.01451.0740.18960.00110.6570.17050.04440.3705-0.06310.16948.2241-41.0261-0.5981
220.5126-0.30670.10060.93460.30591.4666-0.3632-0.25050.25380.43290.4941-0.17740.9278-0.06220.04430.30690.11690.05960.4838-0.05340.07413.3728-30.05511.4428
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:181)A1 - 181
2X-RAY DIFFRACTION2(chain A and resid 182:275)A182 - 275
3X-RAY DIFFRACTION3(chain B and resid 0:42)B0 - 42
4X-RAY DIFFRACTION4(chain B and resid 43:99)B43 - 99
5X-RAY DIFFRACTION5(chain C and resid 1:10)C1 - 10
6X-RAY DIFFRACTION6(chain D and resid 3:109)D3 - 109
7X-RAY DIFFRACTION7(chain D and resid 110:176)D110 - 176
8X-RAY DIFFRACTION8(chain D and resid 177:199)D177 - 199
9X-RAY DIFFRACTION9(chain E and resid 3:118)E3 - 118
10X-RAY DIFFRACTION10(chain E and resid 119:201)E119 - 201
11X-RAY DIFFRACTION11(chain E and resid 202:244)E202 - 244
12X-RAY DIFFRACTION12(chain F and resid 1:181)F1 - 181
13X-RAY DIFFRACTION13(chain F and resid 182:275)F182 - 275
14X-RAY DIFFRACTION14(chain G and resid 0:37)G0 - 37
15X-RAY DIFFRACTION15(chain G and resid 38:99)G38 - 99
16X-RAY DIFFRACTION16(chain H and resid 1:10)H1 - 10
17X-RAY DIFFRACTION17(chain I and resid 3:109)I3 - 109
18X-RAY DIFFRACTION18(chain I and resid 110:170)I110 - 170
19X-RAY DIFFRACTION19(chain I and resid 171:199)I171 - 199
20X-RAY DIFFRACTION20(chain J and resid 2:115)J2 - 115
21X-RAY DIFFRACTION21(chain J and resid 116:204)J116 - 204
22X-RAY DIFFRACTION22(chain J and resid 205:244)J205 - 244

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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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

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