[English] 日本語
Yorodumi
- PDB-5ue8: The crystal structure of Munc13-1 C1C2BMUN domain -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5ue8
TitleThe crystal structure of Munc13-1 C1C2BMUN domain
ComponentsProtein unc-13 homolog A
KeywordsEXOCYTOSIS / ALPHA HELICAL / NEUROTRANSMITTER RELEASE / SNARE MOTIF / C1 DOMAIN / C2 DOMAIN
Function / homology
Function and homology information


dense core granule priming / neuronal dense core vesicle exocytosis / diacylglycerol binding / synaptic vesicle maturation / synaptic vesicle docking / regulation of synaptic vesicle priming / positive regulation of synaptic plasticity / positive regulation of dendrite extension / positive regulation of glutamate receptor signaling pathway / regulation of short-term neuronal synaptic plasticity ...dense core granule priming / neuronal dense core vesicle exocytosis / diacylglycerol binding / synaptic vesicle maturation / synaptic vesicle docking / regulation of synaptic vesicle priming / positive regulation of synaptic plasticity / positive regulation of dendrite extension / positive regulation of glutamate receptor signaling pathway / regulation of short-term neuronal synaptic plasticity / neurotransmitter secretion / innervation / regulation of amyloid precursor protein catabolic process / syntaxin binding / presynaptic active zone / syntaxin-1 binding / Golgi-associated vesicle / spectrin binding / positive regulation of neurotransmitter secretion / neuromuscular junction development / synaptic vesicle priming / excitatory synapse / synaptic vesicle exocytosis / amyloid-beta metabolic process / synaptic membrane / calyx of Held / SNARE binding / synaptic transmission, glutamatergic / neuromuscular junction / phospholipid binding / long-term synaptic potentiation / terminal bouton / synaptic vesicle membrane / presynapse / presynaptic membrane / cell differentiation / calmodulin binding / protein domain specific binding / axon / calcium ion binding / synapse / protein-containing complex binding / glutamatergic synapse / protein-containing complex / zinc ion binding / identical protein binding / plasma membrane
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #1100 / Tetracycline Repressor; domain 2 - #50 / Protein Unc-13 / Protein Unc-13, C2B domain / Mammalian uncoordinated homology 13, domain 2 / Munc13-homology domain 2 (MHD2) profile. / Domain of Unknown Function (DUF1041) / MUN domain / Munc13 homology 1 / MUN domain ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #1100 / Tetracycline Repressor; domain 2 - #50 / Protein Unc-13 / Protein Unc-13, C2B domain / Mammalian uncoordinated homology 13, domain 2 / Munc13-homology domain 2 (MHD2) profile. / Domain of Unknown Function (DUF1041) / MUN domain / Munc13 homology 1 / MUN domain / Munc13-homology domain 1 (MHD1) profile. / Phorbol esters/diacylglycerol binding domain (C1 domain) / C2 domain / Tetracycline Repressor; domain 2 / Zinc finger phorbol-ester/DAG-type signature. / Protein kinase C conserved region 2 (CalB) / C2 domain / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C2 domain / C2 domain profile. / C1-like domain superfamily / C2 domain superfamily / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Up-down Bundle / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Protein unc-13 homolog A
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / MAD / molecular replacement / Resolution: 3.35 Å
Model detailsAlternatively spliced loop between residues 1407 and 1453 has been removed.
AuthorsTomchick, D.R. / Rizo, J. / Xu, J.
Citation
Journal: Elife / Year: 2017
Title: Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN.
Authors: Xu, J. / Camacho, M. / Xu, Y. / Esser, V. / Liu, X. / Trimbuch, T. / Pan, Y.Z. / Ma, C. / Tomchick, D.R. / Rosenmund, C. / Rizo, J.
#1: Journal: Elife / Year: 2016
Title: Functional synergy between the Munc13 C-terminal C1 and C2 domains.
Authors: Liu, X. / Seven, A.B. / Camacho, M. / Esser, V. / Xu, J. / Trimbuch, T. / Quade, B. / Su, L. / Ma, C. / Rosenmund, C. / Rizo, J.
#2: Journal: Nat Struct Mol Biol / Year: 2015
Title: Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming.
Authors: Yang, X. / Wang, S. / Sheng, Y. / Zhang, M. / Zou, W. / Wu, L. / Kang, L. / Rizo, J. / Zhang, R. / Xu, T. / Ma, C.
#3: Journal: Structure / Year: 2011
Title: The Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering Factors
Authors: Li, W. / Ma, C. / Guan, R. / Xu, Y. / Tomchick, D.R. / Rizo, J.
History
DepositionDec 29, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 15, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Refinement description / Category: software
Revision 2.0Feb 21, 2018Group: Database references / Polymer sequence / Category: citation / entity_poly / Item: _citation.title / _entity_poly.pdbx_target_identifier
Revision 2.1Mar 28, 2018Group: Data collection / Database references / Category: citation / Item: _citation.title
Revision 2.2Oct 30, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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: Protein unc-13 homolog A
B: Protein unc-13 homolog A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)219,7378
Polymers219,4042
Non-polymers3336
Water00
1
A: Protein unc-13 homolog A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)109,8684
Polymers109,7021
Non-polymers1663
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Protein unc-13 homolog A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)109,8684
Polymers109,7021
Non-polymers1663
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)176.145, 86.351, 202.142
Angle α, β, γ (deg.)90.000, 115.540, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 542 through 625 or resid 631...
21(chain B and (resid 542 through 800 or resid 808...

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
11ASNASNSERSER(chain A and (resid 542 through 625 or resid 631...AA542 - 62514 - 97
12ASPASPGLNGLN(chain A and (resid 542 through 625 or resid 631...AA631 - 702103 - 174
13SERSERPHEPHE(chain A and (resid 542 through 625 or resid 631...AA709 - 742181 - 214
14ASNASNGLUGLU(chain A and (resid 542 through 625 or resid 631...AA746 - 758218 - 230
15ASPASPILEILE(chain A and (resid 542 through 625 or resid 631...AA775 - 819247 - 291
16VALVALALAALA(chain A and (resid 542 through 625 or resid 631...AA825 - 922297 - 394
17VALVALSERSER(chain A and (resid 542 through 625 or resid 631...AA930 - 1337402 - 809
18VALVALLYSLYS(chain A and (resid 542 through 625 or resid 631...AA1353 - 1470825 - 900
19CYSCYSTHRTHR(chain A and (resid 542 through 625 or resid 631...AA1472 - 1515902 - 945
21ASNASNLYSLYS(chain B and (resid 542 through 800 or resid 808...BB542 - 80014 - 272
22SERSERALAALA(chain B and (resid 542 through 800 or resid 808...BB808 - 922280 - 394
23VALVALGLNGLN(chain B and (resid 542 through 800 or resid 808...BB930 - 1037402 - 509
24PROPROGLNGLN(chain B and (resid 542 through 800 or resid 808...BB1053 - 1190525 - 662
25LEULEUILEILE(chain B and (resid 542 through 800 or resid 808...BB1197 - 1403669 - 875
26LYSLYSLYSLYS(chain B and (resid 542 through 800 or resid 808...BB1470900
27CYSCYSTHRTHR(chain B and (resid 542 through 800 or resid 808...BB1472 - 1515902 - 945

-
Components

#1: Protein Protein unc-13 homolog A / Munc13-1


Mass: 109702.156 Da / Num. of mol.: 2
Fragment: C1C2BMUN domain (UNP residues 529-1407 and 1452-1531)
Mutation: L756W mutation. Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact.
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Unc13a, Unc13h1 / Plasmid: pFASTBac / Cell line (production host): sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q62768
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.14 Å3/Da / Density % sol: 60.84 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.2 M LiCl, 0.1 M Tris-HCl pH 8.0, 0.15 M NaCl, 12% PEG 10,000, 10% glycerol, 5 mM TCEP, 25% ethylene glycol
PH range: 8.0 - 8.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97931 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 17, 2012 / Details: MONOCHROMATOR
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97931 Å / Relative weight: 1
ReflectionResolution: 3.35→50 Å / Num. obs: 37636 / % possible obs: 93.9 % / Redundancy: 3.9 % / Biso Wilson estimate: 37.65 Å2 / Rmerge(I) obs: 0.056 / Rpim(I) all: 0.031 / Rrim(I) all: 0.064 / Χ2: 0.851 / Net I/σ(I): 9.9 / Num. measured all: 147746
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.35-3.413.30.69213630.8090.3880.7980.93868.9
3.41-3.473.40.62414600.850.3550.7220.96474
3.47-3.543.50.55116020.8660.3150.6380.92480.9
3.54-3.613.70.48116860.9010.2750.5560.92784.5
3.61-3.693.70.41617540.9230.2390.4810.96888.4
3.69-3.773.80.32818400.9590.1870.3790.93191.5
3.77-3.873.90.28318780.9640.1610.3270.93495.6
3.87-3.973.90.25519670.9710.1480.2960.96998.1
3.97-4.0940.19220040.9840.110.2220.90699.8
4.09-4.224.10.14219780.9930.080.1630.91899.9
4.22-4.374.10.10719840.9950.060.1230.90399.9
4.37-4.554.20.0820030.9970.0450.0920.875100
4.55-4.754.20.06619940.9970.0370.0760.805100
4.75-54.20.0520090.9980.0280.0580.761100
5-5.324.10.04919930.9980.0270.0560.797100
5.32-5.734.10.05420290.9950.030.0620.798100
5.73-6.34.10.0520290.9940.0280.0580.784100
6.3-7.2140.04120160.9950.0230.0470.847100
7.21-9.083.90.02320270.9980.0130.0270.727100
9.08-503.80.01620200.9980.0090.0190.51995.6

-
Phasing

Phasing
Method
MAD
molecular replacement

-
Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
HKL-3000data scaling
PHASERphasing
PDB_EXTRACT3.22data extraction
HKL-3000data reduction
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: SAD / Resolution: 3.35→45.598 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.53 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.29 1490 4.98 %random
Rwork0.2524 28445 --
obs0.2542 29935 75.29 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 249.88 Å2 / Biso mean: 66.067 Å2 / Biso min: 8.21 Å2
Refinement stepCycle: final / Resolution: 3.35→45.598 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13597 0 6 0 13603
Biso mean--32.34 --
Num. residues----1685
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00313884
X-RAY DIFFRACTIONf_angle_d0.6118728
X-RAY DIFFRACTIONf_chiral_restr0.042088
X-RAY DIFFRACTIONf_plane_restr0.0042383
X-RAY DIFFRACTIONf_dihedral_angle_d11.4978409
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9780X-RAY DIFFRACTION8.508TORSIONAL
12B9780X-RAY DIFFRACTION8.508TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 11

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.35-3.45810.4435340.326575278622
3.4581-3.58170.3302610.30951017107830
3.5817-3.7250.2984820.30241520160245
3.725-3.89450.3079990.29152068216760
3.8945-4.09970.34561460.27362655280177
4.0997-4.35630.27851550.25313211336694
4.3563-4.69240.25231840.23534483632100
4.6924-5.1640.24211820.21734243606100
5.164-5.90990.27461800.256734193599100
5.9099-7.44060.34651820.290234823664100
7.4406-45.60240.28411850.21323449363497
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)
12.44110.28371.41230.17830.0530.898-0.02480.04430.1467-0.0738-0.1009-0.0732-0.09860.10860.08210.08040.0420.01390.4197-0.06310.26586.2233-28.8978164.3539
21.44160.59680.77780.53590.40010.91620.0052-0.36460.09830.14180.0143-0.0302-0.04940.02280.06660.27580.2351-0.08380.6602-0.04990.3009-11.7445-29.4582163.0982
31.1884-0.39310.38050.608-0.31780.65170.0321-0.0058-0.14640.0504-0.0225-0.24830.10930.15990.09250.18640.4083-0.19070.5047-0.01230.30845.1038-40.8834150.3957
40.64610.40220.93850.65550.18251.7802-0.10210.0960.0859-0.08710.2362-0.10390.19750.2509-0.0620.21750.10060.01750.74810.05570.2528-1.0295-40.3723120.4295
51.29240.40680.67541.36770.84012.5294-0.10020.0877-0.0535-0.2842-0.0161-0.0926-0.0513-0.01960.07690.5991-0.1736-0.00760.72770.19390.2894-8.0964-40.608288.5903
60.3786-0.03180.39360.0204-0.04380.8103-0.00230.09570.1022-0.2429-0.0309-0.0067-0.12070.01870.04641.35-0.32780.10780.96410.13860.4599-7.6746-37.936957.3435
70.94710.0843-0.47271.07490.31250.35420.04640.1589-0.012-0.1349-0.00980.0002-0.00870.0686-0.01061.7061-0.24040.22171.41070.23330.5624-0.8785-36.212441.2077
80.0273-0.0191-0.04630.02320.03740.08190.05570.21010.0647-0.09910.022-0.0421-0.05540.064-0.02992.0165-0.31080.43671.93980.13731.157210.3305-29.655217.025
90.06580.3453-0.12552.6262-0.2273.26340.03220.1003-0.0136-0.0108-0.04320.0867-0.0264-0.18870.01060.6924-0.1031-0.00970.3726-0.05430.2086-42.8293-36.5293-69.3063
100.67621.06570.22531.6870.36010.0788-0.0054-0.1603-0.21870.2642-0.0801-0.04230.18810.01380.05680.9643-0.21570.16030.91410.08170.7465-21.5776-21.96-84.5741
110.73010.0387-0.09080.7865-0.11790.79290.07780.3077-0.0253-0.17860.0798-0.0172-0.1144-0.1032-0.03611.0391-0.02220.16490.46290.09660.3527-40.092-24.6917-69.8101
120.34640.1706-0.19560.4195-0.25081.65520.00290.10910.0386-0.26250.1407-0.1223-0.11680.03140.00530.4255-0.02470.08890.1250.04470.2003-39.7933-26.2514-44.1622
130.73390.0198-0.51160.2755-0.02651.03190.0552-0.0447-0.0122-0.08630.0003-0.1038-0.09010.0724-0.00910.0286-0.25060.03120.16880.14140.1259-48.7522-28.5344-6.142
140.95750.16950.3990.76660.41731.12530.0549-0.187-0.11790.18380.0131-0.22860.05050.04610.00710.3212-0.242-0.08540.29610.01750.206-42.5081-28.218534.9698
150.15-0.1251-0.46830.12410.31941.76320.0519-0.1533-0.08870.19740.0441-0.1278-0.01260.21580.02760.94260.2626-0.39240.7168-0.01970.554-27.7398-22.58766.7737
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 541:611)A541 - 611
2X-RAY DIFFRACTION2(chain A and resid 612:687)A612 - 687
3X-RAY DIFFRACTION3(chain A and resid 688:892)A688 - 892
4X-RAY DIFFRACTION4(chain A and resid 893:1027)A893 - 1027
5X-RAY DIFFRACTION5(chain A and resid 1028:1160)A1028 - 1160
6X-RAY DIFFRACTION6(chain A and resid 1161:1244)A1161 - 1244
7X-RAY DIFFRACTION7(chain A and resid 1245:1324)A1245 - 1324
8X-RAY DIFFRACTION8(chain A and resid 1325:1517)A1325 - 1517
9X-RAY DIFFRACTION9(chain B and resid 542:566)B542 - 566
10X-RAY DIFFRACTION10(chain B and resid 567:624)B567 - 624
11X-RAY DIFFRACTION11(chain B and resid 625:856)B625 - 856
12X-RAY DIFFRACTION12(chain B and resid 857:1002)B857 - 1002
13X-RAY DIFFRACTION13(chain B and resid 1003:1161)B1003 - 1161
14X-RAY DIFFRACTION14(chain B and resid 1162:1322)B1162 - 1322
15X-RAY DIFFRACTION15(chain B and resid 1323:1515)B1323 - 1515

+
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