[English] 日本語
Yorodumi
- PDB-4n0i: Crystal structure of S. cerevisiae mitochondrial GatFAB in comple... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4n0i
TitleCrystal structure of S. cerevisiae mitochondrial GatFAB in complex with glutamine
Components(Glutamyl-tRNA(Gln) amidotransferase subunit ...) x 3
KeywordsLIGASE / amidotransferase
Function / homology
Function and homology information


glutaminyl-tRNA synthase (glutamine-hydrolysing) / glutamyl-tRNA(Gln) amidotransferase complex / Ligases; Forming carbon-nitrogen bonds; Carbon-nitrogen ligases with glutamine as amido-N-donor / glutaminyl-tRNAGln biosynthesis via transamidation / glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity / endoplasmic reticulum organization / mitochondrial translation / mitochondrial inner membrane / mitochondrion / ATP binding
Similarity search - Function
Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial / Glutamyl-tRNA(Gln) amidotransferase subunit F / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit / Glutamyl-tRNA(Gln) amidotransferase A subunit / Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic / Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E / GatB/GatE catalytic domain / Glutamyl-tRNA(Gln) amidotransferase subunit B signature. / Asn/Gln amidotransferase ...Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial / Glutamyl-tRNA(Gln) amidotransferase subunit F / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit / Glutamyl-tRNA(Gln) amidotransferase A subunit / Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic / Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E / GatB/GatE catalytic domain / Glutamyl-tRNA(Gln) amidotransferase subunit B signature. / Asn/Gln amidotransferase / GatB domain / GatB domain / Aspartyl/glutamyl-tRNA amidotransferase subunit B-like / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 2 / Amidase / Amidase, conserved site / Amidases signature. / Amidase signature (AS) enzymes / Amidase signature (AS) domain / Amidase signature domain / Amidase signature (AS) superfamily / Amidase / Glutamine synthetase/guanido kinase, catalytic domain / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
GLUTAMINE / NITRATE ION / Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial / Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial / Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.001 Å
AuthorsAraiso, Y. / Ishitani, R. / Nureki, O.
CitationJournal: Nucleic Acids Res. / Year: 2014
Title: Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases
Authors: Araiso, Y. / Huot, J.L. / Sekiguchi, T. / Frechin, M. / Fischer, F. / Enkler, L. / Senger, B. / Ishitani, R. / Becker, H.D. / Nureki, O.
History
DepositionOct 2, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Apr 16, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 17, 2014Group: Database references
Revision 1.2Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
B: Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
F: Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,0155
Polymers105,8063
Non-polymers2082
Water5,891327
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12560 Å2
ΔGint-86 kcal/mol
Surface area32310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.438, 85.426, 194.784
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

-
Glutamyl-tRNA(Gln) amidotransferase subunit ... , 3 types, 3 molecules ABF

#1: Protein Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial / Glu-AdT subunit A / HMG2-induced ER-remodeling protein 2 / Loss of respiratory capacity protein 6


Mass: 50981.410 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: GatA, GEP6, HER2, LRC6, YMR293C / Plasmid: pCGFP-BC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Star2 CodonPlus
References: UniProt: Q03557, Ligases; Forming carbon-nitrogen bonds; Carbon-nitrogen ligases with glutamine as amido-N-donor
#2: Protein Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial / Glu-AdT subunit B / Cytochrome c oxidase assembly factor PET112


Mass: 36704.215 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: GatB, PET112, YBL0724, YBL080C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Star2 CodonPlus
References: UniProt: P33893, Ligases; Forming carbon-nitrogen bonds; Carbon-nitrogen ligases with glutamine as amido-N-donor
#3: Protein Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial / Glu-AdT subunit F


Mass: 18120.826 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: GatF, GTF1, YGR102C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Star2 CodonPlus
References: UniProt: P53260, Ligases; Forming carbon-nitrogen bonds; Carbon-nitrogen ligases with glutamine as amido-N-donor

-
Non-polymers , 3 types, 329 molecules

#4: Chemical ChemComp-GLN / GLUTAMINE


Type: L-peptide linking / Mass: 146.144 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H10N2O3
#5: Chemical ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: NO3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 327 / 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: 2.45 Å3/Da / Density % sol: 49.89 % / Mosaicity: 0.71 °
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 50mM Sodium malonate, 200mM Mg(NO3)2, 10% PEG3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 17, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 68988 / % possible obs: 96.9 % / Redundancy: 5.3 % / Biso Wilson estimate: 30.69 Å2 / Rmerge(I) obs: 0.071 / Χ2: 2.257 / Net I/σ(I): 15.7
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2-2.034.20.33234501.435197.5
2.03-2.074.40.30834501.54198.3
2.07-2.114.50.27334121.508198
2.11-2.154.40.24334351.465197.3
2.15-2.24.40.20833921.459196.9
2.2-2.254.40.18633761.461196.1
2.25-2.314.40.16634181.486196.4
2.31-2.374.50.14633351.547195.4
2.37-2.444.70.13433531.683195.4
2.44-2.524.80.12534191.783196.2
2.52-2.614.90.11333701.798195.5
2.61-2.715.20.10134201.965196.4
2.71-2.845.40.09234272.115196.2
2.84-2.995.70.08334302.364197.7
2.99-3.176.10.07735182.587198.3
3.17-3.426.70.0735532.799199.1
3.42-3.766.90.06435553.116199.6
3.76-4.316.70.05835703.302198.7
4.31-5.436.60.05436233.347199
5.43-5060.0534823.218190.2

-
Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHENIX1.7.2_869refinement
PDB_EXTRACT3.11data extraction
uguisdata collection
HKL-2000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Yeast GatFAB, free form

Resolution: 2.001→26.458 Å / Occupancy max: 1 / Occupancy min: 0.5 / SU ML: 0.5 / σ(F): 1.49 / Phase error: 19.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2192 3447 5 %RANDOM
Rwork0.189 ---
obs0.1906 68955 96.93 %-
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 49.306 Å2 / ksol: 0.338 e/Å3
Displacement parametersBiso max: 190.49 Å2 / Biso mean: 50.9464 Å2 / Biso min: 16.02 Å2
Baniso -1Baniso -2Baniso -3
1-0.861 Å2-0 Å20 Å2
2---3.4658 Å20 Å2
3---2.6049 Å2
Refinement stepCycle: LAST / Resolution: 2.001→26.458 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6565 0 13 327 6905
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0066742
X-RAY DIFFRACTIONf_angle_d1.069150
X-RAY DIFFRACTIONf_chiral_restr0.0681060
X-RAY DIFFRACTIONf_plane_restr0.0051176
X-RAY DIFFRACTIONf_dihedral_angle_d13.8832473
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 25

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.001-2.02860.3031340.27352551268596
2.0286-2.05760.27331370.24932595273298
2.0576-2.08830.27341400.24042664280498
2.0883-2.12090.25361360.22242576271298
2.1209-2.15570.24031370.22012612274997
2.1557-2.19280.23571370.20072594273197
2.1928-2.23270.25711350.19692569270496
2.2327-2.27560.21621340.19052549268396
2.2756-2.3220.24641360.18822580271696
2.322-2.37250.18061330.1812560269396
2.3725-2.42760.22311340.18342533266795
2.4276-2.48830.2421370.19132611274896
2.4883-2.55550.23561350.19932559269497
2.5555-2.63070.23771360.19982574271095
2.6307-2.71550.26741370.20332613275096
2.7155-2.81240.25521340.2052560269496
2.8124-2.92490.25941390.19932634277397
2.9249-3.05780.20921400.19172653279398
3.0578-3.21880.22911410.18812671281298
3.2188-3.42010.21271430.18952714285799
3.4201-3.68350.19081420.180827112853100
3.6835-4.0530.19091430.16722717286099
4.053-4.63680.17241430.15372711285499
4.6368-5.83150.18221460.16762769291599
5.8315-26.46030.25131380.20992628276690
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)
10.65210.1872-0.70851.479-0.07571.3072-0.2497-0.4477-0.37350.65370.0283-0.22660.77870.44890.31640.81130.24140.22720.39960.17290.336523.0019-15.58971.4721
20.6437-0.3416-0.43671.23370.85951.6369-0.3119-0.2267-0.43720.32350.08240.09650.86680.12560.22220.54280.22930.25340.20180.01380.285423.9967-14.621-15.1839
31.1655-0.2465-0.79310.420.44291.7349-0.2815-0.252-0.44140.4935-0.07030.3580.6767-0.25690.37490.62360.03050.27620.30220.03850.458611.8018-12.5304-4.6143
41.0187-0.2709-0.82941.13920.34131.7531-0.2891-0.3191-0.15390.36720.08090.05560.63350.21180.2170.31090.09850.09270.2920.00440.225418.9082-1.6778-7.3172
50.592-0.1139-0.65541.31350.98671.614-0.0355-0.15030.1411-0.11990.1493-0.2392-0.03030.2945-0.0590.165-0.0040.01660.2995-0.06540.253124.679913.3849-14.8463
60.7616-0.4242-0.53310.99350.54491.1088-0.3174-0.1232-0.32080.1431-0.06860.28630.3976-0.2810.18890.2339-0.08720.16270.1889-0.16020.33627.5452-0.8938-14.9473
71.07890.85080.14312.44410.9351.2194-0.28710.2876-0.2196-0.1301-0.180.53350.0598-0.34060.11630.1847-0.02710.0480.3777-0.1870.37724.34433.8843-25.953
81.5377-0.2101-0.72141.5670.27042.1795-0.2238-0.2183-0.15290.21710.0010.21730.2288-0.06960.1330.17090.03150.05580.2443-0.08650.238311.71768.6694-7.3968
90.60540.2755-0.53142.52310.54471.4244-0.13080.2208-0.2899-0.5676-0.07380.14090.32050.1435-0.02160.53140.07080.30170.2419-0.11830.215326.3762-12.0452-45.5111
101.04140.2596-0.69782.06360.13631.3422-0.19570.10270.0219-0.452-0.0250.16770.0204-0.22150.12510.3527-0.00770.09870.2322-0.06540.264320.6479-2.6579-40.3915
110.9153-0.71930.10221.0773-0.44061.7953-0.02440.4558-0.1276-1.288-0.24210.170.0732-0.33850.19951.12940.0613-0.04850.4655-0.08140.334619.6204-3.4665-58.774
121.4555-0.2404-0.01062.11330.19971.2367-0.1560.6006-0.1163-1.1217-0.23930.53840.0407-0.1608-0.05140.8862-0.0003-0.00160.3753-0.17290.329220.9517-8.2618-55.7519
134.30611.4648-0.20965.5440.96942.7223-0.07520.2172-0.1253-1.0598-0.17630.56090.1083-0.11610.26350.84130.00450.0130.2841-0.05350.425123.7538-9.227-56.3653
140.0758-0.06730.15480.0582-0.13340.309-0.11890.22170.0951-0.91-0.03910.9622-0.3464-0.46010.38921.1335-0.0737-0.73460.7644-0.24081.64034.4776-10.8381-64.0764
150.0587-0.0893-0.12141.21272.28354.3373-0.04390.5437-0.5608-1.1134-0.08150.25930.1152-0.13050.14860.8404-0.0889-0.06380.6264-0.37650.66276.2795-12.3652-50.2164
161.09130.4319-1.04430.9835-0.42392.6099-0.1560.0475-0.0553-0.6487-0.1267-0.2227-0.33520.0972-0.0190.6014-0.04490.18860.23790.0340.31929.2547.6652-45.5853
171.03740.0636-1.11681.0861-0.50633.14470.0258-0.0640.1078-0.0508-0.09380.1703-0.176-0.2250.20360.24570.0274-0.0050.2808-0.13180.34394.985225.70260.2352
185.155-3.7196-2.42425.80350.32361.7915-0.07920.4452-0.2168-0.3156-0.29290.489-0.0955-0.40470.25190.12720.0967-0.02470.49-0.20870.3894-6.021619.244-5.3587
190.2621-0.3485-0.29830.47890.45460.5538-0.03330.0407-0.21150.0797-0.28470.38590.1489-0.40910.53020.2605-0.03320.08610.6534-0.38550.5308-7.89375.2243-16.4184
201.08290.1869-0.19960.32380.29850.6294-0.14050.0287-0.13970.0873-0.18310.37370.2838-0.3881-0.02320.4487-0.29170.21430.5887-0.42920.7273-4.0553-15.6625-31.1253
211.256-0.1662-0.32360.19430.1770.3469-0.19270.17460.0381-0.2056-0.070.49710.1304-0.44960.14860.2313-0.103-0.00590.4989-0.31490.5926-0.43983.0371-26.0082
220.16980.175-0.09194.1395-2.43941.4458-0.0966-0.34350.29880.2596-0.261-0.3763-0.10450.34810.45550.3279-0.05690.06790.29640.03530.431437.4673-0.1851-35
230.03130.1848-0.00311.15710.26640.8927-0.14130.1405-0.39910.1274-0.15760.11980.663-0.10530.13210.58210.03670.2890.2239-0.09180.430224.7257-25.0428-32.225
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resseq 6:52)A6 - 52
2X-RAY DIFFRACTION2chain 'A' and (resseq 53:87)A53 - 87
3X-RAY DIFFRACTION3chain 'A' and (resseq 88:123)A88 - 123
4X-RAY DIFFRACTION4chain 'A' and (resseq 124:206)A124 - 206
5X-RAY DIFFRACTION5chain 'A' and (resseq 207:243)A207 - 243
6X-RAY DIFFRACTION6chain 'A' and (resseq 244:328)A244 - 328
7X-RAY DIFFRACTION7chain 'A' and (resseq 329:368)A329 - 368
8X-RAY DIFFRACTION8chain 'A' and (resseq 369:464)A369 - 464
9X-RAY DIFFRACTION9chain 'B' and (resseq 27:66)B27 - 66
10X-RAY DIFFRACTION10chain 'B' and (resseq 67:126)B67 - 126
11X-RAY DIFFRACTION11chain 'B' and (resseq 127:171)B127 - 171
12X-RAY DIFFRACTION12chain 'B' and (resseq 172:211)B172 - 211
13X-RAY DIFFRACTION13chain 'B' and (resseq 212:231)B212 - 231
14X-RAY DIFFRACTION14chain 'B' and (resseq 232:276)B232 - 276
15X-RAY DIFFRACTION15chain 'B' and (resseq 277:302)B277 - 302
16X-RAY DIFFRACTION16chain 'B' and (resseq 303:327)B303 - 327
17X-RAY DIFFRACTION17chain 'F' and (resseq 29:46)F29 - 46
18X-RAY DIFFRACTION18chain 'F' and (resseq 47:52)F47 - 52
19X-RAY DIFFRACTION19chain 'F' and (resseq 53:70)F53 - 70
20X-RAY DIFFRACTION20chain 'F' and (resseq 71:89)F71 - 89
21X-RAY DIFFRACTION21chain 'F' and (resseq 90:134)F90 - 134
22X-RAY DIFFRACTION22chain 'F' and (resseq 135:151)F135 - 151
23X-RAY DIFFRACTION23chain 'F' and (resseq 152:176)F152 - 176

+
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