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- PDB-4mj1: unliganded BK Polyomavirus VP1 pentamer -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4mj1
Titleunliganded BK Polyomavirus VP1 pentamer
ComponentsVP1 capsid protein
KeywordsVIRAL PROTEIN / antiparallel beta sandwich / jelly-roll topology / polyomavirus / receptor switch / virus major capsid protein / attachment to host-cell surface receptors
Function / homology
Function and homology information


caveolin-mediated endocytosis of virus by host cell / T=7 icosahedral viral capsid / host cell nucleus / virion attachment to host cell / structural molecule activity
Similarity search - Function
Capsid protein VP1,Polyomavirus / Polyomavirus Vp1; Chain A / Capsid protein VP1,Polyomavirus / Polyomavirus capsid protein VP1 superfamily / Polyomavirus coat protein / Double-stranded DNA virus, group I, capsid / Sandwich / Mainly Beta
Similarity search - Domain/homology
Major capsid protein VP1 / Capsid protein VP1
Similarity search - Component
Biological speciesBK polyomavirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsNeu, U. / Stroh, L.J. / Stehle, T.
CitationJournal: Plos Pathog. / Year: 2013
Title: A Structure-Guided Mutation in the Major Capsid Protein Retargets BK Polyomavirus.
Authors: Neu, U. / Allen, S.A. / Blaum, B.S. / Liu, Y. / Frank, M. / Palma, A.S. / Stroh, L.J. / Feizi, T. / Peters, T. / Atwood, W.J. / Stehle, T.
History
DepositionSep 3, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 6, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 20, 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 / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: VP1 capsid protein
B: VP1 capsid protein
C: VP1 capsid protein
D: VP1 capsid protein
E: VP1 capsid protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,94315
Polymers151,3055
Non-polymers63810
Water15,565864
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24310 Å2
ΔGint-209 kcal/mol
Surface area44850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)144.900, 152.290, 62.720
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
31C
41D
51E

NCS domain segments:

Ens-ID: 1 / Refine code: 4

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNASPASPAA52 - 5927 - 34
21ASNASNASPASPBB52 - 5927 - 34
31ASNASNASPASPCC52 - 5927 - 34
41ASNASNASPASPDD52 - 5927 - 34
51ASNASNASPASPEE52 - 5927 - 34
12ASNASNLEULEUAA61 - 6936 - 44
22ASNASNLEULEUBB61 - 6936 - 44
32ASNASNLEULEUCC61 - 6936 - 44
42ASNASNLEULEUDD61 - 6936 - 44
52ASNASNLEULEUEE61 - 6936 - 44
13SERSERASPASPAA70 - 7845 - 53
23SERSERASPASPBB70 - 7845 - 53
33SERSERASPASPCC70 - 7845 - 53
43SERSERASPASPDD70 - 7845 - 53
53SERSERASPASPEE70 - 7845 - 53
14METMETALAALAAA84 - 9159 - 66
24METMETALAALABB84 - 9159 - 66
34METMETALAALACC84 - 9159 - 66
44METMETALAALADD84 - 9159 - 66
54METMETALAALAEE84 - 9159 - 66
15THRTHRSERSERAA117 - 12492 - 99
25THRTHRSERSERBB117 - 12492 - 99
35THRTHRSERSERCC117 - 12492 - 99
45THRTHRSERSERDD117 - 12492 - 99
55THRTHRSERSEREE117 - 12492 - 99
16LEULEUGLNGLNAA126 - 133101 - 108
26LEULEUGLNGLNBB126 - 133101 - 108
36LEULEUGLNGLNCC126 - 133101 - 108
46LEULEUGLNGLNDD126 - 133101 - 108
56LEULEUGLNGLNEE126 - 133101 - 108
17VALVALHISHISAA135 - 136110 - 111
27VALVALHISHISBB135 - 136110 - 111
37VALVALHISHISCC135 - 136110 - 111
47VALVALHISHISDD135 - 136110 - 111
57VALVALHISHISEE135 - 136110 - 111
18HISHISLEULEUAA138 - 159113 - 134
28HISHISLEULEUBB138 - 159113 - 134
38HISHISLEULEUCC138 - 159113 - 134
48HISHISLEULEUDD138 - 159113 - 134
58HISHISLEULEUEE138 - 159113 - 134
19METMETLEULEUAA161 - 165136 - 140
29METMETLEULEUBB161 - 165136 - 140
39METMETLEULEUCC161 - 165136 - 140
49METMETLEULEUDD161 - 165136 - 140
59METMETLEULEUEE161 - 165136 - 140
110ASNASNTHRTHRAA167 - 170142 - 145
210ASNASNTHRTHRBB167 - 170142 - 145
310ASNASNTHRTHRCC167 - 170142 - 145
410ASNASNTHRTHRDD167 - 170142 - 145
510ASNASNTHRTHREE167 - 170142 - 145
111GLYGLYPROPROAA175 - 179150 - 154
211GLYGLYPROPROBB175 - 179150 - 154
311GLYGLYPROPROCC175 - 179150 - 154
411GLYGLYPROPRODD175 - 179150 - 154
511GLYGLYPROPROEE175 - 179150 - 154
112PROPROALAALAAA182 - 184157 - 159
212PROPROALAALABB182 - 184157 - 159
312PROPROALAALACC182 - 184157 - 159
412PROPROALAALADD182 - 184157 - 159
512PROPROALAALAEE182 - 184157 - 159
113SERSERGLNGLNAA186 - 187161 - 162
213SERSERGLNGLNBB186 - 187161 - 162
313SERSERGLNGLNCC186 - 187161 - 162
413SERSERGLNGLNDD186 - 187161 - 162
513SERSERGLNGLNEE186 - 187161 - 162
114ASNASNALAALAAA190 - 195165 - 170
214ASNASNALAALABB190 - 195165 - 170
314ASNASNALAALACC190 - 195165 - 170
414ASNASNALAALADD190 - 195165 - 170
514ASNASNALAALAEE190 - 195165 - 170
115LEULEUSERSERAA197 - 213172 - 188
215LEULEUSERSERBB197 - 213172 - 188
315LEULEUSERSERCC197 - 213172 - 188
415LEULEUSERSERDD197 - 213172 - 188
515LEULEUSERSEREE197 - 213172 - 188
116GLUGLUGLYGLYAA216 - 227191 - 202
216GLUGLUGLYGLYBB216 - 227191 - 202
316GLUGLUGLYGLYCC216 - 227191 - 202
416GLUGLUGLYGLYDD216 - 227191 - 202
516GLUGLUGLYGLYEE216 - 227191 - 202
117PROPROASNASNAA231 - 238206 - 213
217PROPROASNASNBB231 - 238206 - 213
317PROPROASNASNCC231 - 238206 - 213
417PROPROASNASNDD231 - 238206 - 213
517PROPROASNASNEE231 - 238206 - 213
118LEULEUASPASPAA244 - 246219 - 221
218LEULEUASPASPBB244 - 246219 - 221
318LEULEUASPASPCC244 - 246219 - 221
418LEULEUASPASPDD244 - 246219 - 221
518LEULEUASPASPEE244 - 246219 - 221
119GLYGLYLEULEUAA251 - 253226 - 228
219GLYGLYLEULEUBB251 - 253226 - 228
319GLYGLYLEULEUCC251 - 253226 - 228
419GLYGLYLEULEUDD251 - 253226 - 228
519GLYGLYLEULEUEE251 - 253226 - 228
120SERSERSERSERAA258 - 273233 - 248
220SERSERSERSERBB258 - 273233 - 248
320SERSERSERSERCC258 - 273233 - 248
420SERSERSERSERDD258 - 273233 - 248
520SERSERSERSEREE258 - 273233 - 248
121GLNGLNLYSLYSAA277 - 287252 - 262
221GLNGLNLYSLYSBB277 - 287252 - 262
321GLNGLNLYSLYSCC277 - 287252 - 262
421GLNGLNLYSLYSDD277 - 287252 - 262
521GLNGLNLYSLYSEE277 - 287252 - 262
122PHEPHEASPASPAA75 - 7850 - 53
222PHEPHEASPASPBB75 - 7850 - 53
322PHEPHEASPASPCC75 - 7850 - 53
422PHEPHEASPASPDD75 - 7850 - 53
522PHEPHEASPASPEE75 - 7850 - 53

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Components

#1: Protein
VP1 capsid protein


Mass: 30261.039 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) BK polyomavirus / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q85235, UniProt: P03088*PLUS
#2: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#3: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 864 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 46.21 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 16-18 % PEG 3,350, 0.1 M HEPES pH 7.5, 0.25 M LiCl , VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jan 28, 2009
RadiationMonochromator: Bartels monochromator (DCCM) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. all: 94566 / Num. obs: 94342 / % possible obs: 99.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 4.1 % / Biso Wilson estimate: 27.1 Å2 / Net I/σ(I): 11.01
Reflection shellResolution: 2→2.05 Å / Redundancy: 4.1 % / Mean I/σ(I) obs: 2.4 / Num. unique all: 6939 / % possible all: 98.4

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHASERphasing
REFMAC5.5.0102refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3BWQ
Resolution: 2→47.42 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.941 / SU B: 7.547 / SU ML: 0.094 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / ESU R: 0.156 / ESU R Free: 0.139 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19876 3296 3.5 %RANDOM
Rwork0.16091 ---
all0.16224 94340 --
obs0.16224 91044 99.78 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 18.461 Å2
Refinement stepCycle: LAST / Resolution: 2→47.42 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9843 0 35 864 10742
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02210227
X-RAY DIFFRACTIONr_bond_other_d0.0010.026848
X-RAY DIFFRACTIONr_angle_refined_deg1.2461.95813934
X-RAY DIFFRACTIONr_angle_other_deg0.819316768
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.25451312
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.43524.602465
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.537151640
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.1491558
X-RAY DIFFRACTIONr_chiral_restr0.0750.21550
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02111507
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021984
X-RAY DIFFRACTIONr_mcbond_it1.29346441
X-RAY DIFFRACTIONr_mcbond_other0.58742601
X-RAY DIFFRACTIONr_mcangle_it1.865510448
X-RAY DIFFRACTIONr_scbond_it2.32863786
X-RAY DIFFRACTIONr_scangle_it3.18873465
Refine LS restraints NCS

Dom-ID: 1 / Ens-ID: 1 / Number: 2205 / Refine-ID: X-RAY DIFFRACTION

Auth asym-IDTypeRms dev position (Å)Weight position
Amedium positional0.160.5
Bmedium positional0.130.5
Cmedium positional0.130.5
Dmedium positional0.130.5
Emedium positional0.130.5
Amedium thermal0.62
Bmedium thermal0.62
Cmedium thermal0.622
Dmedium thermal0.72
Emedium thermal0.672
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.251 249 -
Rwork0.22 6567 -
obs-6816 98.45 %
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)
11.14260.0804-0.03911.02070.08091.3260.0414-0.04210.19260.00110.0140.0265-0.27520.0162-0.05550.12340.03970.02380.0406-0.01320.110628.275249.021322.5809
21.8059-0.64241.8961.3485-1.3655.2198-0.0044-0.13960.0534-0.00760.07710.04680.0424-0.121-0.07260.0362-0.01930.04780.0235-0.03250.085238.827946.418419.9992
32.13680.4937-0.47660.9842-0.19161.64430.0116-0.00640.06020.03760.05290.104-0.0758-0.1618-0.06450.070.01940.02150.02580.00070.045622.230540.697519.7682
41.2174-0.38890.46421.4839-1.31744.95740.0380.10090.0732-0.1048-0.00180.0425-0.02030.0227-0.03620.0475-0.00690.02840.0117-0.00620.084932.165446.28912.2484
51.8687-0.4257-0.05121.5466-0.03640.9745-0.0136-0.10520.17410.08490.0384-0.25-0.07390.2381-0.02480.0848-0.0452-0.02630.1049-0.02770.139660.446244.024826.5536
61.21080.3842-0.45892.9232-2.10033.51630.08480.05590.1038-0.00380.073-0.03240.04610.0184-0.15780.0085-0.00180.00640.0957-0.0580.10162.514235.680818.1827
71.3817-0.4345-0.36531.36780.26171.52260.022-0.08370.15780.0830.0244-0.0544-0.14360.0225-0.04640.0558-0.0227-0.00770.07-0.02450.0851.335346.877922.4247
81.55030.0995-0.78181.6091-1.10874.78240.01310.17120.0862-0.1405-0.0124-0.07250.02320.0864-0.00070.0326-0.02150.00450.071-0.02790.102859.332841.74213.0212
91.41280.56140.54682.132-0.31450.71130.1335-0.0963-0.25060.24230.0024-0.35270.16980.1441-0.13590.13450.0659-0.08480.1596-0.01160.230565.758711.129626.4076
102.70441.2191-1.86121.8097-1.19434.50980.032-0.0625-0.2176-0.03910.0145-0.23010.0030.2233-0.04650.06490.0226-0.05890.0281-0.0280.136355.07717.694418.822
111.98711.04630.84081.96440.70531.472-0.02660.0584-0.067-0.09390.0548-0.2559-0.04330.199-0.02820.0510.01220.00620.0628-0.00070.147466.323921.553916.9732
122.3980.2018-1.99011.41580.48746.9981-0.00990.2079-0.1269-0.06790.0124-0.2230.0157-0.1723-0.00260.0396-0.0027-0.0110.0299-0.01620.150759.865711.154315.7712
133.85060.4319-7.91811.4149-0.140831.4213-0.1360.8937-0.0488-0.44720.05150.14140.2151-2.32790.08450.259-0.0253-0.03780.2964-0.01840.173227.9344-0.8335-5.6929
141.4088-0.4187-0.38720.92310.05280.3940.0023-0.078-0.20550.06660.0226-0.06620.1449-0.0719-0.02480.1223-0.035-0.0420.04590.03940.105137.9099-0.93718.859
151.8535-0.36830.54791.1053-0.0391.40180.05720.0906-0.03160.0108-0.0018-0.18480.06820.126-0.05540.0669-0.0186-0.00270.0231-0.0060.106746.41461.924111.7471
161.3132-0.3151-0.13321.91861.58574.99430.01580.0831-0.1029-0.201-0.0281-0.0454-0.1701-0.05760.01230.0407-0.0106-0.0180.01510.01490.073935.68180.96810.1431
170.8307-0.2147-0.38971.01470.34783.59410.00560.03980.0334-0.0287-0.02590.1037-0.1972-0.56130.02030.05620.00770.00870.12150.0310.089613.608822.93114.7725
181.328-0.43110.21071.3459-1.97845.41590.0498-0.0059-0.0867-0.0590.09560.13820.1668-0.6152-0.14540.0357-0.0252-0.00680.0996-0.00190.054311.716916.82810.7903
190.5679-0.1147-0.00381.46120.3591.07540.0279-0.0432-0.07090.06180.0270.020.0941-0.0668-0.05490.0316-0.00210.00230.06760.02870.040420.84216.022118.8721
201.05560.10031.01660.7363-0.20246.37360.00210.0997-0.041-0.05570.0228-0.0105-0.1011-0.0826-0.0250.01710.0150.02130.02910.02070.047417.214622.09839.1764
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A33 - 93
2X-RAY DIFFRACTION2A94 - 144
3X-RAY DIFFRACTION3A145 - 239
4X-RAY DIFFRACTION4A240 - 296
5X-RAY DIFFRACTION5B34 - 91
6X-RAY DIFFRACTION6B92 - 141
7X-RAY DIFFRACTION7B142 - 240
8X-RAY DIFFRACTION8B241 - 297
9X-RAY DIFFRACTION9C43 - 91
10X-RAY DIFFRACTION10C92 - 144
11X-RAY DIFFRACTION11C145 - 262
12X-RAY DIFFRACTION12C263 - 295
13X-RAY DIFFRACTION13D32 - 50
14X-RAY DIFFRACTION14D51 - 178
15X-RAY DIFFRACTION15D179 - 254
16X-RAY DIFFRACTION16D255 - 297
17X-RAY DIFFRACTION17E32 - 73
18X-RAY DIFFRACTION18E74 - 116
19X-RAY DIFFRACTION19E117 - 245
20X-RAY DIFFRACTION20E246 - 297

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