[English] 日本語
Yorodumi
- PDB-5td3: Crystal structure of Catechol 1,2-dioxygenase from Burkholderia v... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5td3
TitleCrystal structure of Catechol 1,2-dioxygenase from Burkholderia vietnamiensis
ComponentsCatechol 1,2-dioxygenase
KeywordsOXIDOREDUCTASE / SSGCID / catechol 1 / 2-dioxygenase / Burkholderia vietnamiensis / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


catechol-containing compound catabolic process / catechol 1,2-dioxygenase / catechol 1,2-dioxygenase activity / beta-ketoadipate pathway / ferric iron binding
Similarity search - Function
Catechol 1,2-dioxygenase, proteobacteria / Catechol dioxygenase, N-terminal / Catechol dioxygenase N terminus / Protocatechuate 3,4-Dioxygenase, subunit A / Aromatic compound dioxygenase / Intradiol ring-cleavage dioxygenases signature. / : / Intradiol ring-cleavage dioxygenase, C-terminal / Intradiol ring-cleavage dioxygenase, core / Dioxygenase ...Catechol 1,2-dioxygenase, proteobacteria / Catechol dioxygenase, N-terminal / Catechol dioxygenase N terminus / Protocatechuate 3,4-Dioxygenase, subunit A / Aromatic compound dioxygenase / Intradiol ring-cleavage dioxygenases signature. / : / Intradiol ring-cleavage dioxygenase, C-terminal / Intradiol ring-cleavage dioxygenase, core / Dioxygenase / Sandwich / Mainly Beta
Similarity search - Domain/homology
PHOSPHATIDYLETHANOLAMINE / catechol 1,2-dioxygenase
Similarity search - Component
Biological speciesBurkholderia vietnamiensis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: to be published
Title: Crystal structure of Catechol 1,2-dioxygenase from Burkholderia vietnamiensis
Authors: Conrady, D.G. / Dranow, D.M. / Lorimer, D. / Edwards, T.E.
History
DepositionSep 16, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 2, 2016Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2023Group: 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_prerelease_seq / pdbx_struct_conn_angle / pdbx_struct_oper_list / 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_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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _pdbx_struct_oper_list.symmetry_operation / _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_conn.ptnr2_symmetry / _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: Catechol 1,2-dioxygenase
B: Catechol 1,2-dioxygenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,73711
Polymers68,9192
Non-polymers1,8189
Water12,214678
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11570 Å2
ΔGint-163 kcal/mol
Surface area23950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)169.410, 55.860, 85.690
Angle α, β, γ (deg.)90.000, 116.300, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 11:26 or resid 29:30 or resid...
21(chain B and ((resid 11 and (name N or name...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ILEILEALAALA(chain A and (resid 11:26 or resid 29:30 or resid...AA11 - 2611 - 26
12ALAALAASNASN(chain A and (resid 11:26 or resid 29:30 or resid...AA29 - 3029 - 30
13SERSERGLYGLY(chain A and (resid 11:26 or resid 29:30 or resid...AA35 - 7735 - 77
14ASPASPGLYGLY(chain A and (resid 11:26 or resid 29:30 or resid...AA79 - 13079 - 130
15ALAALAGLYGLY(chain A and (resid 11:26 or resid 29:30 or resid...AA132 - 149132 - 149
16VALVALVALVAL(chain A and (resid 11:26 or resid 29:30 or resid...AA151 - 193151 - 193
17THRTHRVALVAL(chain A and (resid 11:26 or resid 29:30 or resid...AA195 - 240195 - 240
18SERSERTHRTHR(chain A and (resid 11:26 or resid 29:30 or resid...AA242 - 250242 - 250
19PHEPHELYSLYS(chain A and (resid 11:26 or resid 29:30 or resid...AA252 - 279252 - 279
110THRTHRTHRTHR(chain A and (resid 11:26 or resid 29:30 or resid...AA280280
111ILEILEHOHHOH(chain A and (resid 11:26 or resid 29:30 or resid...AA - L11 - 50111
112ILEILEHOHHOH(chain A and (resid 11:26 or resid 29:30 or resid...AA - L11 - 50111
113ILEILEHOHHOH(chain A and (resid 11:26 or resid 29:30 or resid...AA - L11 - 50111
114ILEILEHOHHOH(chain A and (resid 11:26 or resid 29:30 or resid...AA - L11 - 50111
21ILEILEILEILE(chain B and ((resid 11 and (name N or name...BB1111
22ILEILEPTYPTY(chain B and ((resid 11 and (name N or name...BB - J11 - 40111
23ILEILEPTYPTY(chain B and ((resid 11 and (name N or name...BB - J11 - 40111
24ILEILEPTYPTY(chain B and ((resid 11 and (name N or name...BB - J11 - 40111
25ILEILEPTYPTY(chain B and ((resid 11 and (name N or name...BB - J11 - 40111

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein Catechol 1,2-dioxygenase


Mass: 34459.559 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia vietnamiensis (strain G4 / LMG 22486) (bacteria)
Strain: G4 / LMG 22486 / Gene: Bcep1808_5824 / Plasmid: BuviA.00117.a.B1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A4JR51, catechol 1,2-dioxygenase

-
Non-polymers , 6 types, 687 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Cl
#6: Chemical ChemComp-PTY / PHOSPHATIDYLETHANOLAMINE


Mass: 734.039 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C40H80NO8P / Comment: phospholipid*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 678 / 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: 2.78 Å3/Da / Density % sol: 55.85 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop
Details: Rigaku Reagents Screen JCSG+ well D6: 0.2 M Magnesium Chloride, 20% PEG 8000, 0.1 M Tris pH 8.5; 0.4 uL screen : 0.4 uL BuviA.00117.a.B1.PS02511 at 21.4 mg/ml

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 3, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.75→40.513 Å / Num. obs: 72445 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4.15 % / Biso Wilson estimate: 22.21 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.052 / Net I/σ(I): 16.72
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsCC1/2Diffraction-ID% possible all
1.75-1.80.5772.480.759199.8
1.8-1.840.4653.080.828199.8
1.84-1.90.3564.030.897199.7
1.9-1.960.2665.360.939199.8
1.96-2.020.2016.970.96199.9
2.02-2.090.1539.210.976199.6
2.09-2.170.13110.540.982199.6
2.17-2.260.1112.630.988199.6
2.26-2.360.08915.410.99199.5
2.36-2.470.07817.370.993199.5
2.47-2.610.06519.940.995199.4
2.61-2.770.05323.610.996199.6
2.77-2.960.04527.530.997199.3
2.96-3.20.03830.980.998199.5
3.2-3.50.03235.860.998199.4
3.5-3.910.03139.090.998199.2
3.91-4.520.02741.350.999199.3
4.52-5.530.02542.150.999199.3
5.53-7.830.025420.999198.6
7.830.02242.610.999193.9

-
Processing

Software
NameVersionClassification
PHENIXrefinement
XSCALEdata scaling
PDB_EXTRACT3.2data extraction
MOLREPphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1DMH

1dmh


Resolution: 1.75→40.513 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.71 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2101 1995 2.75 %
Rwork0.177 70446 -
obs0.1779 72441 99.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 113.58 Å2 / Biso mean: 32.0597 Å2 / Biso min: 11.22 Å2
Refinement stepCycle: final / Resolution: 1.75→40.513 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4577 0 113 686 5376
Biso mean--52.5 35.98 -
Num. residues----611
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0064851
X-RAY DIFFRACTIONf_angle_d0.8186591
X-RAY DIFFRACTIONf_chiral_restr0.053728
X-RAY DIFFRACTIONf_plane_restr0.006875
X-RAY DIFFRACTIONf_dihedral_angle_d10.4172910
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2643X-RAY DIFFRACTION4.292TORSIONAL
12B2643X-RAY DIFFRACTION4.292TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.75-1.79370.26461340.246249835117100
1.7937-1.84220.26151460.244950085154100
1.8422-1.89650.30431510.237650155166100
1.8965-1.95770.23811350.223950165151100
1.9577-2.02760.26341430.212350045147100
2.0276-2.10880.23781460.195649915137100
2.1088-2.20480.22911370.194350365173100
2.2048-2.3210.23541340.18550455179100
2.321-2.46640.24131510.184850095160100
2.4664-2.65680.19651410.184750385179100
2.6568-2.92410.2371480.178950335181100
2.9241-3.34710.21221450.174150345179100
3.3471-4.21620.18981390.14545077521699
4.2162-40.52410.14811450.14945157530299
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)
14.4550.4952-1.64414.7627-1.98135.8151-0.2945-0.80060.23790.85290.08370.32430.0131-0.0250.18510.36030.1350.04770.3431-0.0850.202144.7431-16.36267.2808
21.3183-0.7176-0.15440.8314-0.30681.5388-0.0642-0.01560.0980.09870.07940.14370.0606-0.1366-0.01880.1311-0.044-0.01080.1012-0.01790.181841.1077-12.790947.5113
30.6746-0.2188-0.36491.7130.21920.53240.31440.37070.4049-0.2525-0.133-0.1346-0.2115-0.1989-0.11940.19780.07160.04720.25710.12310.340745.53873.062422.9097
40.9149-1.15480.32545.96320.19471.04830.34530.21620.6221-0.189-0.0111-0.6042-0.293-0.0417-0.21450.23110.04870.12260.20650.11570.422351.28663.257822.4048
51.252-0.4564-0.59211.1751-0.35771.79160.09330.30880.1981-0.1616-0.0046-0.05120.1138-0.2311-0.0880.143-0.003-0.03840.23240.02740.200343.2882-9.973827.5036
61.7537-1.2596-0.62271.3225-0.19712.19170.12710.37580.1903-0.2575-0.01650.22050.046-0.3493-0.08550.1331-0.0115-0.03530.29280.06930.269735.22-3.36428.8815
71.3982-0.4788-1.38130.6201-0.42833.22850.42310.56170.5618-0.4412-0.04560.0159-0.3969-0.4113-0.2640.28430.1310.00280.48130.18790.405937.21725.145217.9836
87.3026-3.5336-1.02976.37061.07455.99990.0957-0.22610.79940.07740.1534-0.2408-0.31550.2167-0.28370.146-0.0482-0.02880.09070.03920.343646.92653.457539.9438
95.1864-3.6871-0.99875.42860.73282.3569-0.14180.3069-0.1527-0.06740.04450.41050.2451-0.26490.1020.1676-0.12790.00580.23890.00490.260429.9256-16.428741.7281
101.9893-0.643-0.00320.7936-0.26140.7007-0.1349-0.03130.11590.13470.08530.06450.0994-0.07610.04490.1588-0.0297-0.01250.1068-0.02210.132244.5855-14.123649.5114
112.95390.50710.84152.9591-1.43072.1002-0.2668-0.731-0.67870.20970.08040.35730.50470.0150.13960.42910.06950.17250.28480.07550.305446.7288-33.756466.1334
121.4985-0.58420.0970.7860.04850.3721-0.4063-0.7016-0.61080.12710.1999-0.05790.25230.08860.2070.39320.1130.1270.31530.14720.315368.5495-36.459963.0973
131.26781.81480.17898.9043-2.59791.3959-0.3601-0.2761-0.6478-0.31940.1679-0.19290.35610.1330.21170.36590.09540.13240.20970.08140.375971.7281-36.649158.3655
142.8439-0.6852-0.15021.6564-0.50820.8801-0.3536-0.462-0.03450.1920.1951-0.0840.13680.21320.16490.29460.0706-0.00170.2588-0.00650.135563.4941-23.113263.1286
152.281-0.25560.70074.17010.74331.4091-0.3687-0.9035-0.29590.53330.11640.35830.21070.02250.15060.43350.13690.13260.46410.09110.212459.2256-31.573469.0478
160.3328-0.26960.19840.342-0.17890.1304-0.5459-0.9067-0.26430.48280.109-0.09370.28160.3958-0.08790.54680.32820.12250.83820.30670.236768.2902-33.812773.948
173.56583.17730.46647.7159-4.86315.7812-0.39880.0749-0.6343-0.07930.38580.260.724-0.35380.03360.44050.03470.13370.11050.00060.328553.1817-38.791655.8831
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 11 through 38 )A11 - 38
2X-RAY DIFFRACTION2chain 'A' and (resid 39 through 115 )A39 - 115
3X-RAY DIFFRACTION3chain 'A' and (resid 116 through 178 )A116 - 178
4X-RAY DIFFRACTION4chain 'A' and (resid 179 through 199 )A179 - 199
5X-RAY DIFFRACTION5chain 'A' and (resid 200 through 241 )A200 - 241
6X-RAY DIFFRACTION6chain 'A' and (resid 242 through 272 )A242 - 272
7X-RAY DIFFRACTION7chain 'A' and (resid 273 through 307 )A273 - 307
8X-RAY DIFFRACTION8chain 'A' and (resid 308 through 320 )A308 - 320
9X-RAY DIFFRACTION9chain 'B' and (resid 11 through 38 )B11 - 38
10X-RAY DIFFRACTION10chain 'B' and (resid 39 through 90 )B39 - 90
11X-RAY DIFFRACTION11chain 'B' and (resid 91 through 115 )B91 - 115
12X-RAY DIFFRACTION12chain 'B' and (resid 116 through 178 )B116 - 178
13X-RAY DIFFRACTION13chain 'B' and (resid 179 through 199 )B179 - 199
14X-RAY DIFFRACTION14chain 'B' and (resid 200 through 241 )B200 - 241
15X-RAY DIFFRACTION15chain 'B' and (resid 242 through 263 )B242 - 263
16X-RAY DIFFRACTION16chain 'B' and (resid 264 through 301 )B264 - 301
17X-RAY DIFFRACTION17chain 'B' and (resid 302 through 320 )B302 - 320

+
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