[English] 日本語
Yorodumi
- PDB-6wmo: Human poly-N-acetyl-lactosamine synthase structure demonstrates a... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6wmo
TitleHuman poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases
ComponentsN-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
KeywordsTRANSFERASE / Glycosyltransferase / GT-A fold / poly LacNAc synthesis
Function / homology
Function and homology information


N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity / keratan sulfate proteoglycan biosynthetic process / poly-N-acetyllactosamine biosynthetic process / N-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase activity / Keratan sulfate biosynthesis / protein O-linked GalNAcylation / O-linked glycosylation of mucins / protein O-linked glycosylation / axon guidance ...N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity / keratan sulfate proteoglycan biosynthetic process / poly-N-acetyllactosamine biosynthetic process / N-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase activity / Keratan sulfate biosynthesis / protein O-linked GalNAcylation / O-linked glycosylation of mucins / protein O-linked glycosylation / axon guidance / cellular response to leukemia inhibitory factor / sensory perception of smell / Golgi membrane
Similarity search - Function
Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A - #50 / Glycosyl transferase, family 31 / Galactosyltransferase / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
URIDINE-5'-DIPHOSPHATE / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å
AuthorsKadirvelraj, R. / Wood, Z.A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)1P01GM107012-02 United States
CitationJournal: J.Biol.Chem. / Year: 2020
Title: Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites.
Authors: Kadirvelraj, R. / Yang, J.Y. / Kim, H.W. / Sanders, J.H. / Moremen, K.W. / Wood, Z.A.
History
DepositionApr 21, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 2, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 9, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Apr 28, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 18, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
B: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,95219
Polymers84,4402
Non-polymers4,51117
Water4,143230
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: assay for oligomerization, Ultracentrifugation: Velocity
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10510 Å2
ΔGint24 kcal/mol
Surface area28110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)48.190, 109.280, 147.550
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 56 through 147 or resid 149...
21(chain B and (resid 56 through 147 or resid 149...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 56 through 147 or resid 149...A56 - 147
121(chain A and (resid 56 through 147 or resid 149...A149
131(chain A and (resid 56 through 147 or resid 149...A151 - 211
141(chain A and (resid 56 through 147 or resid 149...A308 - 332
151(chain A and (resid 56 through 147 or resid 149...A334 - 35
161(chain A and (resid 56 through 147 or resid 149...A365 - 392
211(chain B and (resid 56 through 147 or resid 149...B56 - 147
221(chain B and (resid 56 through 147 or resid 149...B149
231(chain B and (resid 56 through 147 or resid 149...B151 - 211
241(chain B and (resid 56 through 147 or resid 149...B213 - 260
251(chain B and (resid 56 through 147 or resid 149...B56 - 392
261(chain B and (resid 56 through 147 or resid 149...B33
271(chain B and (resid 56 through 147 or resid 149...B334 - 392

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 / Beta-1 / 3-N-acetylglucosaminyltransferase 1 / Beta3Gn-T1 / 3-galactosyltransferase 7 / b3Gal-T7 / ...Beta-1 / 3-N-acetylglucosaminyltransferase 1 / Beta3Gn-T1 / 3-galactosyltransferase 7 / b3Gal-T7 / Beta-3-Gx-T7 / UDP-Gal:beta-GlcNAc beta-1 / UDP-GlcNAc:betaGal beta-1 / 3-N-acetylglucosaminyltransferase 2 / Beta3Gn-T2 / UDP-galactose:beta-N-acetylglucosamine beta-1


Mass: 42220.207 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B3GNT2, B3GALT7, B3GNT1 / Production host: Homo sapiens (human)
References: UniProt: Q9NY97, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase

-
Sugars , 3 types, 7 molecules

#2: Polysaccharide beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose


Type: oligosaccharide / Mass: 545.490 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGalpb1-4DGlcpNAcb1-3DGalpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2112h-1b_1-5][a2122h-1b_1-5_2*NCC/3=O]/1-2-1/a3-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][b-D-Galp]{[(3+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

-
Non-polymers , 5 types, 240 molecules

#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: Mg
#5: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C9H14N2O12P2 / Comment: UDP*YM
#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


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


Mass: 18.015 Da / Num. of mol.: 230 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestN
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.3 Å3/Da / Density % sol: 46.5 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 24% PEG3350, 6% Ethylene glycol, 100 mM Hepes pH 8.5

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Mar 21, 2016
RadiationMonochromator: Rosenbaum-Rock double monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.85→37.848 Å / Num. obs: 67358 / % possible obs: 99.7 % / Redundancy: 14.071 % / Biso Wilson estimate: 37 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.061 / Rrim(I) all: 0.063 / Χ2: 1.036 / Net I/σ(I): 24.4 / Num. measured all: 947780 / Scaling rejects: 43
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique obsCC1/2% possible allRrim(I) all
1.85-1.99.8991.0147310.44996.4
1.9-1.9512.6981.8347990.805100
1.95-2.0114.5792.5646920.867100
2.01-2.0714.5613.6745130.94100
2.07-2.1414.3835.1544300.96100
2.14-2.2114.3536.8742820.977100
2.21-2.2914.3279.0341460.987100
2.29-2.3914.44111.7939610.992100
2.39-2.4914.66715.3738070.994100
2.49-2.6214.88520.0936280.997100
2.62-2.7614.92425.2835060.998100
2.76-2.9214.90132.9533140.999100
2.92-3.1314.8341.631080.999100
3.13-3.3814.78751.3129100.999100
3.38-3.714.63264.0327161100
3.7-4.1414.52672.924281100
4.14-4.7714.35578.9121961100
4.77-5.8514.1178.4818471100
5.85-8.2713.67378.7414841100
8.27-37.84812.28582.81860198.70.027

-
Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
XDSdata reduction
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6WMM

6wmm


Resolution: 1.85→37.848 Å / SU ML: 0.23 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 22.71
RfactorNum. reflection% reflection
Rfree0.2115 3367 5 %
Rwork0.1828 --
obs0.1842 67291 99.78 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 118.7 Å2 / Biso mean: 50.3168 Å2 / Biso min: 20.94 Å2
Refinement stepCycle: final / Resolution: 1.85→37.848 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5261 0 294 230 5785
Biso mean--55.13 48.22 -
Num. residues----638
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.015772
X-RAY DIFFRACTIONf_angle_d0.9287843
X-RAY DIFFRACTIONf_chiral_restr0.057877
X-RAY DIFFRACTIONf_plane_restr0.006972
X-RAY DIFFRACTIONf_dihedral_angle_d11.7743427
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2987X-RAY DIFFRACTION7.059TORSIONAL
12B2987X-RAY DIFFRACTION7.059TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.85-1.87640.36361290.3552246796
1.8764-1.90440.39171330.305261899
1.9044-1.93420.31961490.27622664100
1.9342-1.96590.2971320.24442600100
1.9659-1.99980.29471460.23682654100
1.9998-2.03620.23641300.21572608100
2.0362-2.07530.22841430.20312643100
2.0753-2.11770.23431400.20012642100
2.1177-2.16370.22961390.2022655100
2.1637-2.21410.23261450.18642636100
2.2141-2.26940.22271300.1812646100
2.2694-2.33080.24061400.18642653100
2.3308-2.39930.24561410.19012660100
2.3993-2.47680.24591410.19162642100
2.4768-2.56530.23211400.18152659100
2.5653-2.6680.22111340.18542699100
2.668-2.78940.22981420.17462659100
2.7894-2.93640.22451430.1942647100
2.9364-3.12030.24811440.19272696100
3.1203-3.3610.2211390.18992679100
3.361-3.6990.20081460.17042732100
3.699-4.23360.17731420.1492711100
4.2336-5.33160.16051450.15732762100
5.3316-37.8480.19691540.19152892100
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)
13.3212-0.18720.762.72680.26886.0432-0.20690.3504-0.3464-1.01770.0740.21970.7414-0.37140.15730.9301-0.07210.03490.3942-0.0780.419716.4604-24.4401-41.7151
25.3888-5.8296-3.13667.27742.66993.4765-0.36480.0549-0.59640.07870.03760.6440.7119-0.29840.29620.4884-0.13410.00930.2997-0.0590.306811.4157-18.157-32.6431
33.42221.38690.72383.02320.35397.14-0.0405-0.02460.30440.1015-0.12130.3971-0.2999-0.33440.15060.29080.03970.05140.2464-0.02540.275911.8326.9613-26.9056
40.86182.3764-1.63977.0412-5.77535.1152-0.16170.16760.1452-0.22350.36730.46740.2078-0.6907-0.1760.431-0.05330.03730.3773-0.03570.335410.1009-0.9764-24.2154
52.1035-0.9504-0.30735.6465-0.644.8617-0.02670.03760.066-0.10360.08480.3410.3757-0.3863-0.03640.2467-0.08640.0030.331-0.00970.28358.0424-3.3443-28.0389
63.81591.29570.85777.8749-2.93283.2234-0.0510.29780.1981-0.4471-0.03110.0449-0.40360.00870.09130.45590.01840.07760.3062-0.02170.202520.486410.1634-34.4638
72.1656-0.19750.21334.2142-1.39323.3489-0.03750.2854-0.1437-0.5075-0.0781-0.25910.2770.25790.11890.49440.00710.09840.3779-0.02490.213124.0437-6.9335-39.7061
85.6551.89111.60526.68842.36624.153-0.0809-0.16870.0040.04810.0487-0.8694-0.01491.6854-0.01830.3114-0.03450.05910.65920.03030.366734.20095.0185-30.4239
94.2449-3.0838-0.52035.95620.67664.61080.0087-0.21330.7199-0.4850.187-0.6829-0.84520.5186-0.14290.4694-0.15120.04190.437-0.03480.308128.595113.5628-21.8329
104.60350.86971.01763.05950.16954.6956-0.1696-0.47890.6890.38790.0525-1.0083-0.86830.67010.11210.4843-0.0803-0.13350.446-0.12360.704630.554614.635512.1798
110.56650.73290.71035.58080.21555.7078-0.0559-0.085-0.0233-0.0572-0.0040.22060.2579-0.55090.04770.1641-0.02840.00970.3189-0.02320.25338.6738-6.11972.0082
123.97262.7279-1.78116.6334-1.98327.3672-0.006-0.01180.1087-0.2577-0.00870.0644-0.2111-0.3071-0.02420.18080.06470.01860.2699-0.06670.238210.51053.1992-1.5651
132.37240.87020.7323.67051.16923.22930.1696-0.2929-0.47870.56470.066-1.07040.45060.348-0.12420.30090.0624-0.11860.39510.00430.543823.9788-6.676810.8496
145.1347-0.37393.35535.78062.04125.78360.06720.1169-0.52280.3530.0355-0.47371.07290.2848-0.08130.52460.04610.11210.3286-0.10740.498717.5677-18.6298-4.8064
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 54 through 113 )A54 - 113
2X-RAY DIFFRACTION2chain 'A' and (resid 114 through 131 )A114 - 131
3X-RAY DIFFRACTION3chain 'A' and (resid 132 through 170 )A132 - 170
4X-RAY DIFFRACTION4chain 'A' and (resid 171 through 194 )A171 - 194
5X-RAY DIFFRACTION5chain 'A' and (resid 195 through 234 )A195 - 234
6X-RAY DIFFRACTION6chain 'A' and (resid 235 through 261 )A235 - 261
7X-RAY DIFFRACTION7chain 'A' and (resid 262 through 343 )A262 - 343
8X-RAY DIFFRACTION8chain 'A' and (resid 344 through 365 )A344 - 365
9X-RAY DIFFRACTION9chain 'A' and (resid 366 through 397 )A366 - 397
10X-RAY DIFFRACTION10chain 'B' and (resid 56 through 131 )B56 - 131
11X-RAY DIFFRACTION11chain 'B' and (resid 132 through 170 )B132 - 170
12X-RAY DIFFRACTION12chain 'B' and (resid 171 through 216 )B171 - 216
13X-RAY DIFFRACTION13chain 'B' and (resid 217 through 369 )B217 - 369
14X-RAY DIFFRACTION14chain 'B' and (resid 370 through 392 )B370 - 392

+
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