[English] 日本語
Yorodumi
- PDB-7kkt: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant w... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7kkt
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site
Components4-hydroxy-tetrahydrodipicolinate synthase
KeywordsLYASE / DIHYDRODIPICOLINATE SYNTHASE
Function / homology
Function and homology information


(R,S)-4-hydroxy-2-oxoglutarate aldolase activity / 4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / glyoxylate catabolic process / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / cytosol
Similarity search - Function
4-hydroxy-tetrahydrodipicolinate synthase, DapA / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase-type TIM barrel
Similarity search - Domain/homology
Chem-3VN / ACETATE ION / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / 4-hydroxy-tetrahydrodipicolinate synthase
Similarity search - Component
Biological speciesCampylobacter jejuni subsp. jejuni serotype O:2 (Campylobacter)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.71 Å
AuthorsSaran, S. / Majdi Yazdi, M. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: To Be Published
Title: A TIGHT DIMER INTERFACE N84 RESIDUE, PLAYS A CRITICAL ROLE IN THE TRANSMISSION OF THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS
Authors: Saran, S. / Majdi Yazdi, M. / Palmer, D.R.J. / Sanders, D.A.R.
History
DepositionOct 28, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 3, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.2Nov 29, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)209,29361
Polymers205,1176
Non-polymers4,17655
Water26,6621480
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,36114
Polymers68,3722
Non-polymers98912
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5420 Å2
ΔGint-39 kcal/mol
Surface area21900 Å2
MethodPISA
2
B: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,86624
Polymers68,3722
Non-polymers1,49322
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6290 Å2
ΔGint-68 kcal/mol
Surface area22020 Å2
MethodPISA
3
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,06623
Polymers68,3722
Non-polymers1,69421
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7200 Å2
ΔGint-19 kcal/mol
Surface area22160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.020, 225.470, 200.420
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 or resid 5:20 or resid...
21(chain B and (resid 3 or resid 5:20 or resid...
31(chain C and (resid 3 or resid 5:20 or resid...
41(chain D and (resid 3 or resid 5:20 or resid...
51(chain E and (resid 3 or resid 5:20 or resid...
61(chain F and (resid 3 or resid 5:20 or resid...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 3 or resid 5:20 or resid...A3
121(chain A and (resid 3 or resid 5:20 or resid...A5 - 20
131(chain A and (resid 3 or resid 5:20 or resid...A22 - 24
141(chain A and (resid 3 or resid 5:20 or resid...A26 - 31
151(chain A and (resid 3 or resid 5:20 or resid...A0
161(chain A and (resid 3 or resid 5:20 or resid...A52 - 56
171(chain A and (resid 3 or resid 5:20 or resid...A3 - 298
181(chain A and (resid 3 or resid 5:20 or resid...A75 - 97
191(chain A and (resid 3 or resid 5:20 or resid...A3 - 298
1101(chain A and (resid 3 or resid 5:20 or resid...A3 - 298
1111(chain A and (resid 3 or resid 5:20 or resid...A162 - 165
1121(chain A and (resid 3 or resid 5:20 or resid...A233 - 231
1131(chain A and (resid 3 or resid 5:20 or resid...A233 - 234
1141(chain A and (resid 3 or resid 5:20 or resid...A236 - 238
1151(chain A and (resid 3 or resid 5:20 or resid...A240 - 266
1161(chain A and (resid 3 or resid 5:20 or resid...A282 - 289
1171(chain A and (resid 3 or resid 5:20 or resid...A289 - 296
1181(chain A and (resid 3 or resid 5:20 or resid...A289 - 291
1191(chain A and (resid 3 or resid 5:20 or resid...A293
1201(chain A and (resid 3 or resid 5:20 or resid...A295 - 298
211(chain B and (resid 3 or resid 5:20 or resid...B3
221(chain B and (resid 3 or resid 5:20 or resid...B5 - 20
231(chain B and (resid 3 or resid 5:20 or resid...B22 - 24
241(chain B and (resid 3 or resid 5:20 or resid...B26 - 31
251(chain B and (resid 3 or resid 5:20 or resid...B0
261(chain B and (resid 3 or resid 5:20 or resid...B52 - 56
271(chain B and (resid 3 or resid 5:20 or resid...B-7 - 298
281(chain B and (resid 3 or resid 5:20 or resid...B75 - 97
291(chain B and (resid 3 or resid 5:20 or resid...B-7 - 298
2101(chain B and (resid 3 or resid 5:20 or resid...B-7 - 298
2111(chain B and (resid 3 or resid 5:20 or resid...B162 - 165
2121(chain B and (resid 3 or resid 5:20 or resid...B233 - 231
2131(chain B and (resid 3 or resid 5:20 or resid...B233 - 234
2141(chain B and (resid 3 or resid 5:20 or resid...B236 - 238
2151(chain B and (resid 3 or resid 5:20 or resid...B240 - 266
2161(chain B and (resid 3 or resid 5:20 or resid...B282 - 289
2171(chain B and (resid 3 or resid 5:20 or resid...B289 - 296
2181(chain B and (resid 3 or resid 5:20 or resid...B289 - 291
2191(chain B and (resid 3 or resid 5:20 or resid...B293
2201(chain B and (resid 3 or resid 5:20 or resid...B295 - 298
311(chain C and (resid 3 or resid 5:20 or resid...C3
321(chain C and (resid 3 or resid 5:20 or resid...C5 - 20
331(chain C and (resid 3 or resid 5:20 or resid...C22 - 24
341(chain C and (resid 3 or resid 5:20 or resid...C26 - 31
351(chain C and (resid 3 or resid 5:20 or resid...C0
361(chain C and (resid 3 or resid 5:20 or resid...C52 - 56
371(chain C and (resid 3 or resid 5:20 or resid...C-7 - 298
381(chain C and (resid 3 or resid 5:20 or resid...C75 - 97
391(chain C and (resid 3 or resid 5:20 or resid...C-7 - 298
3101(chain C and (resid 3 or resid 5:20 or resid...C-7 - 298
3111(chain C and (resid 3 or resid 5:20 or resid...C162 - 165
3121(chain C and (resid 3 or resid 5:20 or resid...C233 - 231
3131(chain C and (resid 3 or resid 5:20 or resid...C233 - 234
3141(chain C and (resid 3 or resid 5:20 or resid...C236 - 238
3151(chain C and (resid 3 or resid 5:20 or resid...C240 - 266
3161(chain C and (resid 3 or resid 5:20 or resid...C282 - 289
3171(chain C and (resid 3 or resid 5:20 or resid...C289 - 296
3181(chain C and (resid 3 or resid 5:20 or resid...C289 - 291
3191(chain C and (resid 3 or resid 5:20 or resid...C293
3201(chain C and (resid 3 or resid 5:20 or resid...C295 - 298
411(chain D and (resid 3 or resid 5:20 or resid...D3
421(chain D and (resid 3 or resid 5:20 or resid...D5 - 20
431(chain D and (resid 3 or resid 5:20 or resid...D22 - 24
441(chain D and (resid 3 or resid 5:20 or resid...D26 - 31
451(chain D and (resid 3 or resid 5:20 or resid...D0
461(chain D and (resid 3 or resid 5:20 or resid...D52 - 56
471(chain D and (resid 3 or resid 5:20 or resid...D3 - 298
481(chain D and (resid 3 or resid 5:20 or resid...D75 - 97
491(chain D and (resid 3 or resid 5:20 or resid...D3 - 298
4101(chain D and (resid 3 or resid 5:20 or resid...D3 - 298
4111(chain D and (resid 3 or resid 5:20 or resid...D162 - 165
4121(chain D and (resid 3 or resid 5:20 or resid...D233 - 231
4131(chain D and (resid 3 or resid 5:20 or resid...D233 - 234
4141(chain D and (resid 3 or resid 5:20 or resid...D236 - 238
4151(chain D and (resid 3 or resid 5:20 or resid...D240 - 266
4161(chain D and (resid 3 or resid 5:20 or resid...D282 - 289
4171(chain D and (resid 3 or resid 5:20 or resid...D289 - 296
4181(chain D and (resid 3 or resid 5:20 or resid...D289 - 291
4191(chain D and (resid 3 or resid 5:20 or resid...D293
4201(chain D and (resid 3 or resid 5:20 or resid...D295 - 298
511(chain E and (resid 3 or resid 5:20 or resid...E3
521(chain E and (resid 3 or resid 5:20 or resid...E5 - 20
531(chain E and (resid 3 or resid 5:20 or resid...E22 - 24
541(chain E and (resid 3 or resid 5:20 or resid...E26 - 31
551(chain E and (resid 3 or resid 5:20 or resid...E0
561(chain E and (resid 3 or resid 5:20 or resid...E52 - 56
571(chain E and (resid 3 or resid 5:20 or resid...E2 - 298
581(chain E and (resid 3 or resid 5:20 or resid...E75 - 97
591(chain E and (resid 3 or resid 5:20 or resid...E2 - 298
5101(chain E and (resid 3 or resid 5:20 or resid...E2 - 298
5111(chain E and (resid 3 or resid 5:20 or resid...E162 - 165
5121(chain E and (resid 3 or resid 5:20 or resid...E233 - 231
5131(chain E and (resid 3 or resid 5:20 or resid...E233 - 234
5141(chain E and (resid 3 or resid 5:20 or resid...E236 - 238
5151(chain E and (resid 3 or resid 5:20 or resid...E240 - 266
5161(chain E and (resid 3 or resid 5:20 or resid...E282 - 289
5171(chain E and (resid 3 or resid 5:20 or resid...E289 - 296
5181(chain E and (resid 3 or resid 5:20 or resid...E289 - 291
5191(chain E and (resid 3 or resid 5:20 or resid...E293
5201(chain E and (resid 3 or resid 5:20 or resid...E295 - 298
611(chain F and (resid 3 or resid 5:20 or resid...F3
621(chain F and (resid 3 or resid 5:20 or resid...F5 - 20
631(chain F and (resid 3 or resid 5:20 or resid...F22 - 24
641(chain F and (resid 3 or resid 5:20 or resid...F26 - 31
651(chain F and (resid 3 or resid 5:20 or resid...F0
661(chain F and (resid 3 or resid 5:20 or resid...F52 - 56
671(chain F and (resid 3 or resid 5:20 or resid...F3 - 298
681(chain F and (resid 3 or resid 5:20 or resid...F75 - 97
691(chain F and (resid 3 or resid 5:20 or resid...F3 - 298
6101(chain F and (resid 3 or resid 5:20 or resid...F3 - 298
6111(chain F and (resid 3 or resid 5:20 or resid...F162 - 165
6121(chain F and (resid 3 or resid 5:20 or resid...F233 - 231
6131(chain F and (resid 3 or resid 5:20 or resid...F233 - 234
6141(chain F and (resid 3 or resid 5:20 or resid...F236 - 238
6151(chain F and (resid 3 or resid 5:20 or resid...F240 - 266
6161(chain F and (resid 3 or resid 5:20 or resid...F282 - 289
6171(chain F and (resid 3 or resid 5:20 or resid...F289 - 296
6181(chain F and (resid 3 or resid 5:20 or resid...F289 - 291
6191(chain F and (resid 3 or resid 5:20 or resid...F293
6201(chain F and (resid 3 or resid 5:20 or resid...F295 - 298

-
Components

-
Protein , 1 types, 6 molecules ABCDEF

#1: Protein
4-hydroxy-tetrahydrodipicolinate synthase / HTPA synthase


Mass: 34186.246 Da / Num. of mol.: 6 / Mutation: N84D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase

-
Non-polymers , 9 types, 1535 molecules

#2: Chemical ChemComp-3VN / (2R,5R)-2,5-diamino-2,5-bis(4-aminobutyl)hexanedioic acid / bis-Lysine


Mass: 318.412 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C14H30N4O4
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H14O4
#5: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#6: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H3O2
#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C4H10O3
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1480 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49.35 %
Crystal growTemperature: 288.15 K / Method: microbatch / pH: 7.4
Details: 0.7 M Magnesium acetate, 10 % PEG8000, 0.1 M Sodium acetate (pH 7.4), 120 mMR,R-BisLysine

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Sep 5, 2017
RadiationMonochromator: Double beam monochromater / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.71→49.129 Å / Num. obs: 203207 / % possible obs: 98.3 % / Redundancy: 15 % / Biso Wilson estimate: 19.48 Å2 / CC1/2: 0.99 / Net I/σ(I): 15.43
Reflection shellResolution: 1.71→1.771 Å / Rmerge(I) obs: 0.3301 / Num. unique obs: 17773 / % possible all: 86.34

-
Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIXdev_2398refinement
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LY8
Resolution: 1.71→49.129 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.3 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1951 10156 5 %
Rwork0.1636 192999 -
obs0.1652 203155 98.32 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 79.76 Å2 / Biso mean: 21.9434 Å2 / Biso min: 8.52 Å2
Refinement stepCycle: final / Resolution: 1.71→49.129 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13852 0 267 1480 15599
Biso mean--34.53 30.98 -
Num. residues----1797
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00914340
X-RAY DIFFRACTIONf_angle_d1.03619305
X-RAY DIFFRACTIONf_chiral_restr0.0662204
X-RAY DIFFRACTIONf_plane_restr0.0072461
X-RAY DIFFRACTIONf_dihedral_angle_d15.558710
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A7381X-RAY DIFFRACTION4.586TORSIONAL
12B7381X-RAY DIFFRACTION4.586TORSIONAL
13C7381X-RAY DIFFRACTION4.586TORSIONAL
14D7381X-RAY DIFFRACTION4.586TORSIONAL
15E7381X-RAY DIFFRACTION4.586TORSIONAL
16F7381X-RAY DIFFRACTION4.586TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.71-1.72950.3913000.3894572788
1.7295-1.74980.37392840.3807538283
1.7498-1.77110.39143030.3124575888
1.7711-1.79360.24213380.19216429100
1.7936-1.81720.22613410.1716469100
1.8172-1.84210.2223430.1796517100
1.8421-1.86840.22093410.18166483100
1.8684-1.89630.2843410.23176484100
1.8963-1.92590.43293310.3479629197
1.9259-1.95750.23863410.206647599
1.9575-1.99120.21263390.16376479100
1.9912-2.02740.20573440.15426535100
2.0274-2.06640.22013400.1991645299
2.0664-2.10860.23583400.18226476100
2.1086-2.15450.18513440.14416529100
2.1545-2.20460.19943420.14846495100
2.2046-2.25970.26143350.2182636598
2.2597-2.32080.19653440.15196527100
2.3208-2.38910.19533420.14766516100
2.3891-2.46620.17913440.14846521100
2.4662-2.55430.15913440.13926545100
2.5543-2.65660.18093470.14296586100
2.6566-2.77750.18023400.1476465100
2.7775-2.92390.19263470.15386588100
2.9239-3.10710.19493450.1546568100
3.1071-3.34690.18853480.15796604100
3.3469-3.68370.16553450.1527655999
3.6837-4.21640.15133470.13426595100
4.2164-5.31130.15133530.12956709100
5.3113-7.650.15143630.14576870100

+
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