[English] 日本語
Yorodumi
- PDB-4odi: 2.6 Angstrom Crystal Structure of Putative Phosphoglycerate Mutas... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4odi
Title2.6 Angstrom Crystal Structure of Putative Phosphoglycerate Mutase 1 from Toxoplasma gondii
ComponentsPhosphoglycerate mutase PGMII
KeywordsISOMERASE / Structural Genomics / NIAID / National Institute of Allergy and Infectious Diseases / Center for Structural Genomics of Infectious Diseases / CSGID / Phosphoglycerate mutase-like
Function / homology
Function and homology information


phosphoglycerate mutase activity / phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) / glycolytic process
Similarity search - Function
Phosphoglycerate mutase 1 / Phosphoglycerate/bisphosphoglycerate mutase, active site / Phosphoglycerate mutase family phosphohistidine signature. / Phosphoglycerate mutase family / Phosphoglycerate mutase-like / Histidine phosphatase superfamily, clade-1 / Histidine phosphatase superfamily (branch 1) / Histidine phosphatase superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphoglycerate mutase
Similarity search - Component
Biological speciesToxoplasma gondii (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsMinasov, G. / Ruan, J. / Ngo, H. / Shuvalova, L. / Dubrovska, I. / Flores, K. / Shanmugam, D. / Roos, D. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID)
CitationJournal: Front Cell Infect Microbiol / Year: 2018
Title: CSGID Solves Structures and Identifies Phenotypes for Five Enzymes in Toxoplasma gondii .
Authors: Lykins, J.D. / Filippova, E.V. / Halavaty, A.S. / Minasov, G. / Zhou, Y. / Dubrovska, I. / Flores, K.J. / Shuvalova, L.A. / Ruan, J. / El Bissati, K. / Dovgin, S. / Roberts, C.W. / Woods, S. ...Authors: Lykins, J.D. / Filippova, E.V. / Halavaty, A.S. / Minasov, G. / Zhou, Y. / Dubrovska, I. / Flores, K.J. / Shuvalova, L.A. / Ruan, J. / El Bissati, K. / Dovgin, S. / Roberts, C.W. / Woods, S. / Moulton, J.D. / Moulton, H. / McPhillie, M.J. / Muench, S.P. / Fishwick, C.W.G. / Sabini, E. / Shanmugam, D. / Roos, D.S. / McLeod, R. / Anderson, W.F. / Ngo, H.M.
History
DepositionJan 10, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 22, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.2Jan 27, 2021Group: Database references / Derived calculations
Category: citation / citation_author ...citation / citation_author / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Sep 20, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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: Phosphoglycerate mutase PGMII
B: Phosphoglycerate mutase PGMII
C: Phosphoglycerate mutase PGMII
D: Phosphoglycerate mutase PGMII
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,0388
Polymers127,9464
Non-polymers924
Water2,954164
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6810 Å2
ΔGint-90 kcal/mol
Surface area41210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.182, 149.474, 72.120
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / Refine code: _

Dom-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUAA15 - 25615 - 256
21GLUGLUBB15 - 25615 - 256
12GLUGLUAA15 - 25615 - 256
22GLUGLUCC15 - 25615 - 256
13ASPASPAA17 - 24717 - 247
23ASPASPDD17 - 24717 - 247
14GLUGLUBB15 - 25615 - 256
24GLUGLUCC15 - 25615 - 256
15ASPASPBB17 - 24717 - 247
25ASPASPDD17 - 24717 - 247
16ASPASPCC17 - 24717 - 247
26ASPASPDD17 - 24717 - 247

NCS ensembles :
ID
1
2
3
4
5
6

-
Components

#1: Protein
Phosphoglycerate mutase PGMII


Mass: 31986.537 Da / Num. of mol.: 4 / Fragment: UNP residues 75-339
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Toxoplasma gondii (eukaryote) / Strain: ME49 / Gene: PGMII, TGME49_297060 / Plasmid: pMCSG28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)/pMagic / References: UniProt: S8GJT7, bisphosphoglycerate mutase
#2: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 164 / 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: 2.05 Å3/Da / Density % sol: 39.91 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: Protein - 7.5 mG/mL, 0.5 M Sodium chloride, 0.01 M Tris-HCL buffer pH 8.3, Screen - Classics II (G12), 0.2M Magnesium chloride, 0.1M HEPES pH 7.5, 25% (w/v) PEG 3350, VAPOR DIFFUSION, ...Details: Protein - 7.5 mG/mL, 0.5 M Sodium chloride, 0.01 M Tris-HCL buffer pH 8.3, Screen - Classics II (G12), 0.2M Magnesium chloride, 0.1M HEPES pH 7.5, 25% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 18, 2013 / Details: Beryllium lenses
RadiationMonochromator: Diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.6→30 Å / Num. all: 33033 / Num. obs: 33033 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 7.3 % / Biso Wilson estimate: 52 Å2 / Rmerge(I) obs: 0.106 / Rsym value: 0.106 / Net I/σ(I): 18.3
Reflection shellResolution: 2.6→2.64 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.645 / Mean I/σ(I) obs: 3.3 / Num. unique all: 1604 / Rsym value: 0.645 / % possible all: 100

-
Processing

Software
NameVersionClassification
Blu-IceMaxdata collection
PHASERphasing
REFMAC5.7.0032refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1XQ9
Resolution: 2.6→29.72 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.911 / SU B: 21.851 / SU ML: 0.232
Isotropic thermal model: Thermal Factors Individually Isotropically Refined
Cross valid method: THROUGHOUT / ESU R Free: 0.318 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23881 1671 5.1 %RANDOM
Rwork0.19717 ---
all0.19925 31317 --
obs0.19925 31317 99.77 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 56.296 Å2
Baniso -1Baniso -2Baniso -3
1--1.48 Å20 Å20 Å2
2--2.24 Å20 Å2
3----0.76 Å2
Refinement stepCycle: LAST / Resolution: 2.6→29.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7719 0 4 164 7887
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0197937
X-RAY DIFFRACTIONr_bond_other_d0.0060.027631
X-RAY DIFFRACTIONr_angle_refined_deg1.6261.96210788
X-RAY DIFFRACTIONr_angle_other_deg1.217317624
X-RAY DIFFRACTIONr_dihedral_angle_1_deg2.3825966
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.11224.101356
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.868151383
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.5541549
X-RAY DIFFRACTIONr_chiral_restr0.0920.21183
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0218821
X-RAY DIFFRACTIONr_gen_planes_other0.0050.021732
X-RAY DIFFRACTIONr_mcbond_it2.2682.4863870
X-RAY DIFFRACTIONr_mcbond_other2.2552.4853869
X-RAY DIFFRACTIONr_mcangle_it3.5413.7254834
X-RAY DIFFRACTIONr_mcangle_other3.5423.7264835
X-RAY DIFFRACTIONr_scbond_it3.0032.7784067
X-RAY DIFFRACTIONr_scbond_other3.0032.7764065
X-RAY DIFFRACTIONr_scangle_other4.754.0215954
X-RAY DIFFRACTIONr_long_range_B_refined6.81520.259103
X-RAY DIFFRACTIONr_long_range_B_other6.81520.2119080
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A146320.13
12B146320.13
21A143910.14
22C143910.14
31A137520.13
32D137520.13
41B143610.13
42C143610.13
51B137660.12
52D137660.12
61C137820.12
62D137820.12
LS refinement shellResolution: 2.6→2.667 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.277 94 -
Rwork0.259 2253 -
obs--98.24 %
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.590.487-0.49531.5547-0.38210.23650.1379-0.08870.23920.2607-0.08930.0137-0.01370.094-0.04870.1009-0.005-0.02490.1965-0.03790.146336.746327.48135.4492
210.42935.5866-9.09117.1207-3.158.6426-0.3473-0.5687-0.11930.1574-0.08570.64760.47890.570.4330.2101-0.00350.01710.26320.02570.277221.066414.577.8608
317.2411-11.7723-15.114426.439611.479421.53690.5447-0.88530.05681.5713-0.8772-0.23731.2471-0.37950.33250.6506-0.26950.08140.4307-0.02820.396420.34435.457616.03
43.0823-0.2076-0.81141.4706-0.5381.6158-0.02470.0173-0.36590.11420.02440.20670.0537-0.09270.00030.0403-0.0368-0.01230.0968-0.03040.203323.558415.526-2.1968
52.64730.0046-0.82471.9884-0.23741.2709-0.0632-0.2724-0.15980.27550.1284-0.11290.10160.0651-0.06520.05990.0256-0.05470.187-0.02760.153543.323217.34690.8005
631.2095-1.19698.58141.273-3.21739.7116-0.7336-1.6108-1.5367-0.0098-0.1118-0.4620.19170.58710.84540.55120.14790.06710.72180.13150.375445.08917.04318.296
71.84011.1907-0.21592.4993-0.17641.10890.1866-0.2056-0.09270.3526-0.22020.0758-0.071-0.00440.03360.0757-0.0088-0.00390.1272-0.04040.102427.434246.97332.7135
87.93356.43391.850411.08934.64553.83170.17230.07510.29110.2772-0.229-0.3354-0.06830.24150.05670.0368-0.0311-0.04410.15260.05110.160739.794354.6505-5.2798
97.0153-5.456.528512.97162.463723.0624-0.3605-0.02160.68020.5665-0.36870.3254-1.27020.73680.72920.3778-0.12360.03220.4314-0.07590.430144.454471.45111.1361
104.12860.35020.77571.98160.11311.5228-0.05530.08950.3107-0.0431-0.0111-0.1595-0.18840.10680.06640.03720.0009-0.00620.1106-0.02230.113236.160753.442-10.0909
112.03670.15360.21063.37961.01574.5076-0.04330.01330.2874-0.05370.02970.2909-0.269-0.21550.01350.03340.04270.01590.1439-0.05320.213218.833757.0156-6.757
1226.1805-5.7046-4.840313.4166-0.00754.3169-1.0716-1.14031.6693-0.08661.05350.6907-0.4992-0.14730.01810.2849-0.0305-0.08140.3361-0.23950.453119.433561.92568.4957
134.8369-0.9839-0.72185.19330.57145.0711-0.15520.3976-0.0182-1.7468-0.01010.80570.39880.02770.16530.7021-0.0346-0.25770.0380.00120.168326.733114.0261-33.4001
142.9929-0.5910.85743.6131-0.61912.6875-0.20320.23710.171-1.19220.16480.4280.18070.03470.03840.5017-0.0783-0.22040.14130.03430.116826.166121.7083-33.6074
153.39020.1934-3.544313.61724.734311.82820.18520.5408-0.7498-1.04490.08070.01491.27160.0891-0.26590.96520.1871-0.23820.3756-0.13970.431336.6884-5.2475-34.1124
163.0116-0.3792-0.64673.9537-0.20291.7177-0.06160.0131-0.2041-0.66550.13290.32010.35660.0876-0.07130.22930.021-0.11980.0681-0.04780.111230.389111.6292-21.8954
174.94492.98272.40724.96580.38766.7297-0.09420.04890.1185-0.9425-0.20141.61540.5284-0.61930.29560.3931-0.0538-0.48890.265-0.05511.038113.641813.539-26.9161
1821.8627-13.5707-0.454917.94749.18298.3592-0.2668-0.0657-1.74130.4460.25480.93470.281-0.02770.0120.923-0.2816-0.22210.9317-0.08660.550913.26319.4517-41.2149
194.2922-0.84740.78654.0095-0.27684.6755-0.25190.55190.0291-1.92480.1272-0.4811-0.02760.35750.12471.133-0.28430.24960.2556-0.02950.062237.880739.4074-42.1474
202.5566-0.59161.12625.29060.64530.727-0.20.2829-0.1972-1.42670.2801-0.1536-0.24530.1917-0.08010.7377-0.10660.06390.1943-0.01370.074234.065138.5906-34.4846
215.4409-0.5692-0.40266.81211.24816.46220.18310.94420.4055-0.2653-0.1341-0.4326-1.58070.08-0.0491.37150.0077-0.32080.23890.18150.34627.254260.9013-41.5514
223.62650.56841.58873.6521.11662.4333-0.37860.12880.1886-1.28090.36-0.247-0.68190.17760.01860.544-0.10240.06250.13090.03580.087733.696446.516-27.8788
237.44030.48816.44668.7306-1.22477.0853-1.04821.295-0.0259-2.53491.1665-1.6596-1.28381.597-0.11831.4671-0.88620.8530.9093-0.26620.668147.449649.5637-34.4399
244.7143-2.81989.02277.21934.623235.4170.17440.25140.3872-0.67340.5601-1.0639-0.71641.7631-0.73450.3131-0.24950.29620.4919-0.00420.51953.423242.3337-33.9318
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A12 - 102
2X-RAY DIFFRACTION2A103 - 114
3X-RAY DIFFRACTION3A115 - 129
4X-RAY DIFFRACTION4A130 - 187
5X-RAY DIFFRACTION5A188 - 247
6X-RAY DIFFRACTION6A248 - 257
7X-RAY DIFFRACTION7B15 - 96
8X-RAY DIFFRACTION8B97 - 114
9X-RAY DIFFRACTION9B115 - 129
10X-RAY DIFFRACTION10B130 - 208
11X-RAY DIFFRACTION11B209 - 246
12X-RAY DIFFRACTION12B247 - 259
13X-RAY DIFFRACTION13C15 - 45
14X-RAY DIFFRACTION14C46 - 110
15X-RAY DIFFRACTION15C111 - 129
16X-RAY DIFFRACTION16C130 - 217
17X-RAY DIFFRACTION17C218 - 244
18X-RAY DIFFRACTION18C245 - 257
19X-RAY DIFFRACTION19D17 - 64
20X-RAY DIFFRACTION20D65 - 114
21X-RAY DIFFRACTION21D115 - 146
22X-RAY DIFFRACTION22D147 - 208
23X-RAY DIFFRACTION23D209 - 234
24X-RAY DIFFRACTION24D235 - 248

+
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