[English] 日本語
Yorodumi
- PDB-7kf3: Crystal structure of GDP-mannose 4,6-dehydratase from Brucella ab... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7kf3
TitleCrystal structure of GDP-mannose 4,6-dehydratase from Brucella abortus (strain 2308) in complex with Guanosine-diphosphate-rhamnose
ComponentsGDP-mannose 4,6-dehydratase
KeywordsLYASE / SSGCID / Structural genomics / GDP-mannose 4 / 6-dehydratase / gmd / Brucella abortus / Guanosine-diphosphate-rhamnose / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


GDP-mannose 4,6-dehydratase / GDP-mannose 4,6-dehydratase activity / GDP-mannose metabolic process / NADP+ binding
Similarity search - Function
GDP-mannose 4,6-dehydratase / GDP-mannose 4,6 dehydratase / NAD(P)-binding domain / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE-RHAMNOSE / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / GDP-mannose 4,6-dehydratase
Similarity search - Component
Biological speciesBrucella abortus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: to be published
Title: Crystal structure of GDP-mannose 4,6-dehydratase from Brucella abortus (strain 2308) in complex with Guanosine-diphosphate-rhamnose
Authors: Abendroth, J. / Lorimer, D.D. / Horanyi, P.S. / Edwards, T.E.
History
DepositionOct 13, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 4, 2020Provider: repository / Type: Initial release
Revision 1.1Oct 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 / 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: GDP-mannose 4,6-dehydratase
B: GDP-mannose 4,6-dehydratase
C: GDP-mannose 4,6-dehydratase
D: GDP-mannose 4,6-dehydratase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)173,33712
Polymers168,0064
Non-polymers5,3318
Water10,251569
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25110 Å2
ΔGint-124 kcal/mol
Surface area45360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.130, 93.300, 93.770
Angle α, β, γ (deg.)89.060, 78.910, 87.510
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 1 through 202 or resid 204...
21(chain B and (resid 1 through 124 or (resid 125...
31(chain C and (resid 1 through 123 or (resid 124...
41(chain D and (resid 1 through 123 or (resid 124...

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
11METMETTHRTHR(chain A and (resid 1 through 202 or resid 204...AA1 - 2021 - 202
12ALAALAGLYGLY(chain A and (resid 1 through 202 or resid 204...AA204 - 254204 - 254
13LYSLYSLYSLYS(chain A and (resid 1 through 202 or resid 204...AA255255
14METMETNAPNAP(chain A and (resid 1 through 202 or resid 204...AA - F1 - 4011
15METMETNAPNAP(chain A and (resid 1 through 202 or resid 204...AA - F1 - 4011
16METMETNAPNAP(chain A and (resid 1 through 202 or resid 204...AA - F1 - 4011
17METMETNAPNAP(chain A and (resid 1 through 202 or resid 204...AA - F1 - 4011
21METMETLYSLYS(chain B and (resid 1 through 124 or (resid 125...BB1 - 1241 - 124
22GLNGLNGLNGLN(chain B and (resid 1 through 124 or (resid 125...BB125125
23METMETNAPNAP(chain B and (resid 1 through 124 or (resid 125...BB - H1 - 4011
24METMETNAPNAP(chain B and (resid 1 through 124 or (resid 125...BB - H1 - 4011
25METMETNAPNAP(chain B and (resid 1 through 124 or (resid 125...BB - H1 - 4011
26METMETNAPNAP(chain B and (resid 1 through 124 or (resid 125...BB - H1 - 4011
31METMETGLUGLU(chain C and (resid 1 through 123 or (resid 124...CC1 - 1231 - 123
32LYSLYSGLNGLN(chain C and (resid 1 through 123 or (resid 124...CC124 - 125124 - 125
33METMETNAPNAP(chain C and (resid 1 through 123 or (resid 124...CC - J1 - 4011
34METMETNAPNAP(chain C and (resid 1 through 123 or (resid 124...CC - J1 - 4011
35METMETNAPNAP(chain C and (resid 1 through 123 or (resid 124...CC - J1 - 4011
36METMETNAPNAP(chain C and (resid 1 through 123 or (resid 124...CC - J1 - 4011
41METMETGLUGLU(chain D and (resid 1 through 123 or (resid 124...DD1 - 1231 - 123
42LYSLYSGLNGLN(chain D and (resid 1 through 123 or (resid 124...DD124 - 125124 - 125
43METMETNAPNAP(chain D and (resid 1 through 123 or (resid 124...DD - L1 - 4011
44METMETNAPNAP(chain D and (resid 1 through 123 or (resid 124...DD - L1 - 4011
45METMETNAPNAP(chain D and (resid 1 through 123 or (resid 124...DD - L1 - 4011
46METMETNAPNAP(chain D and (resid 1 through 123 or (resid 124...DD - L1 - 4011

-
Components

#1: Protein
GDP-mannose 4,6-dehydratase / GDP-D-mannose dehydratase


Mass: 42001.391 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Brucella abortus (strain 2308) (bacteria)
Strain: 2308 / Gene: gmd, BAB1_0545 / Plasmid: Braba.00085.a.AE1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q2YMP3, GDP-mannose 4,6-dehydratase
#2: Chemical
ChemComp-GDR / GUANOSINE-5'-DIPHOSPHATE-RHAMNOSE


Type: RNA linking / Mass: 589.342 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C16H25N5O15P2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE


Mass: 743.405 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H28N7O17P3 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 569 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.2 Å3/Da / Density % sol: 59.3 %
Crystal growTemperature: 287 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: Microlytic Morpheus screen D12: 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD: 20mM of each 1,6-hexanediol, 1-butanol, (RS)-1,2- propanediol, 2-propanol, 1,4-butanediol, 1,3- ...Details: Microlytic Morpheus screen D12: 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD: 20mM of each 1,6-hexanediol, 1-butanol, (RS)-1,2- propanediol, 2-propanol, 1,4-butanediol, 1,3-propanediol: 100mM bicine/Trizma base pH 8.5: Braba.00085.a.AE1.PW38674 at 29.4mg/ml: tray 311690 d12: cryo: direct: puck zdr6-4.

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Dec 12, 2019 / Details: Beryllium Lenses
RadiationMonochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.35→48.35 Å / Num. obs: 78643 / % possible obs: 96.1 % / Redundancy: 2.198 % / Biso Wilson estimate: 49.532 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.047 / Rrim(I) all: 0.064 / Χ2: 0.933 / Net I/σ(I): 12.13 / Num. measured all: 172882 / Scaling rejects: 18
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.35-2.412.2110.4182.0112775601057780.8080.56296.1
2.41-2.482.2130.3592.3312652592157180.8460.48396.6
2.48-2.552.2070.2693.1212031569554510.8920.36295.7
2.55-2.632.2130.2233.7211882558853680.9340.396.1
2.63-2.712.2090.194.411541542752240.9490.25596.3
2.71-2.812.2040.1485.5111108524550390.9660.296.1
2.81-2.912.2090.1166.8710692503148410.9780.15596.2
2.91-3.032.2110.0928.510346485046790.9880.12496.5
3.03-3.172.20.07310.339830464544680.9910.09996.2
3.17-3.322.1990.05613.159383446842670.9940.07695.5
3.32-3.52.1970.04416.68970425240830.9950.0696
3.5-3.722.1860.03718.928451400438660.9970.0596.6
3.72-3.972.1860.03221.977829373035810.9970.04396
3.97-4.292.1820.02825.127380350833820.9970.03796.4
4.29-4.72.1830.02527.096799322431140.9980.03496.6
4.7-5.252.1740.02527.376078290427960.9980.03396.3
5.25-6.072.1750.02726.015343255224560.9970.03696.2
6.07-7.432.170.02628.064550219520970.9970.03595.5
7.43-10.512.1730.02231.533466166815950.9980.02995.6
10.51-48.352.1140.0232.5317769168400.9980.02891.7

-
Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIX1.19.1refinement
PDB_EXTRACT3.25data extraction
MoRDaphasing
PHENIXmodel building
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UZH

5uzh


Resolution: 2.35→48.35 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 23.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2101 1973 2.51 %0
Rwork0.1743 76627 --
obs0.1751 78600 96.1 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 116.43 Å2 / Biso mean: 47.4039 Å2 / Biso min: 22.1 Å2
Refinement stepCycle: final / Resolution: 2.35→48.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11350 0 344 570 12264
Biso mean--36.94 44.89 -
Num. residues----1448
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00512025
X-RAY DIFFRACTIONf_angle_d0.74716412
X-RAY DIFFRACTIONf_dihedral_angle_d14.3314494
X-RAY DIFFRACTIONf_chiral_restr0.0461818
X-RAY DIFFRACTIONf_plane_restr0.0062223
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A7112X-RAY DIFFRACTION5.685TORSIONAL
12B7112X-RAY DIFFRACTION5.685TORSIONAL
13C7112X-RAY DIFFRACTION5.685TORSIONAL
14D7112X-RAY DIFFRACTION5.685TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.35-2.410.33361650.28345387555296
2.41-2.470.27431350.25025553568897
2.47-2.550.26041430.22135405554895
2.55-2.630.26661470.21415463561096
2.63-2.720.26781770.21795463564096
2.72-2.830.25831580.2055493565196
2.83-2.960.2821380.2055501563996
2.96-3.120.25741350.20125493562897
3.12-3.310.23031130.19655454556796
3.31-3.570.22831200.17035489560996
3.57-3.930.16461520.15815506565897
3.93-4.490.17371260.13495486561296
4.49-5.660.16871340.14265494562896
5.66-48.350.17231300.15815440557095
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)
11.8842-0.4752-0.43852.01360.79331.79510.0224-0.0451-0.3750.0726-0.01890.02290.7491-0.06090.05590.7196-0.0493-0.07870.27230.01510.4641-8.9479-42.595258.8978
20.59330.24760.27961.84280.6151.88480.00190.1104-0.2890.11060.1722-0.24660.9640.2149-0.11350.78130.1084-0.09870.31090.02150.5952-0.715-45.489660.2543
31.93380.5156-0.92740.9286-0.44694.3584-0.10150.4405-0.2749-0.42550.2365-0.2520.5844-0.3011-0.08960.9455-0.0159-0.08250.4656-0.10840.6723-9.5427-42.730240.8181
42.9645-1.0063-0.08392.56820.06713.2488-0.1187-0.20410.22420.08060.2324-0.4409-0.73310.7343-0.05950.3078-0.0851-0.02370.3903-0.05440.40189.79822.194277.6132
50.57230.13410.1171.21440.08832.2580.0685-0.1652-0.08090.23720.0144-0.23260.15640.1793-0.07030.27350.0216-0.0540.33960.01620.34971.294-14.551476.5782
63.03030.1603-0.87091.74720.56332.77520.0715-0.18920.2143-0.007-0.06550.1701-0.4721-0.15260.00410.52370.028-0.02380.4961-0.03480.2932-10.7105-0.284296.4376
72.67720.4995-0.38391.83970.58452.12870.0646-0.1181-0.20260.5050.0918-0.48830.27330.5064-0.14550.42090.0908-0.17170.48160.02320.4229.248-15.014188.6276
80.9919-0.8271-0.3751.46130.36294.336-0.0454-0.50680.17230.5492-0.03890.3516-0.3391-0.29170.13630.5816-0.00930.08960.6779-0.06590.4071-16.235-2.253103.7826
92.3959-0.36710.07921.64370.72322.7139-0.2386-0.4553-0.16480.79050.1659-0.27480.28910.10250.06730.63070.0144-0.11890.49540.07520.37411.4626-16.931293.3216
102.4012-1.27510.98395.628-0.92591.9707-0.3827-0.27540.63360.58710.2463-0.4108-0.9415-0.20710.09480.68230.0416-0.02030.51-0.09980.4071-4.236811.040994.8418
112.3831.00470.9122.74990.07211.7314-0.0809-0.48510.45990.328-0.02490.2101-0.4822-0.41320.08590.42530.14970.01720.4306-0.06820.3301-18.436110.456175.8462
120.82850.41810.23611.4660.45731.954-0.1130.00890.3107-0.16470.05190.0285-0.7281-0.01960.05920.54030.0434-0.01260.23820.01390.379-8.339216.20459.7572
132.4989-0.91732.00472.0385-0.61664.5993-0.2583-0.50410.321-0.01910.1753-0.4626-0.1401-0.0740.13550.8818-0.11710.00680.5075-0.13880.64990.898723.857880.5136
142.45981.02380.60671.9136-0.69443.12470.02370.3599-0.4186-0.34480.135-0.37650.45780.3313-0.14030.30640.02440.06260.3349-0.08240.41211.5502-21.897540.0053
150.6197-0.00680.15951.63180.04092.5608-0.06140.14930.0268-0.35850.1303-0.1246-0.23150.0407-0.06920.3186-0.01850.0350.29460.0040.3057-4.695-4.568343.8816
162.33140.54111.05231.46150.76572.0926-0.06630.2726-0.0563-0.31420.04120.1015-0.1124-0.18920.03790.4835-0.0185-0.02440.44180.02680.2679-18.688-10.527328.2566
171.45510.7285-1.05392.8917-1.19422.1839-0.30050.2442-0.3608-0.16210.2780.04990.7611-0.45360.04950.7281-0.0715-0.06710.5582-0.08550.4292-18.6923-29.629829.4669
181.76-0.795-1.20013.51630.20951.9308-0.0310.2836-0.3577-0.3859-0.03510.45910.5232-0.68730.06070.3788-0.1533-0.05030.4951-0.01290.3789-24.6648-27.822952.375
191.03920.02170.89892.67160.38282.85240.0438-0.1505-0.07670.0606-0.00540.10090.2575-0.3201-0.03430.2072-0.0328-0.01030.26710.01570.2547-15.8196-19.482962.7579
200.85440.1779-0.40531.7960.56542.59850.1669-0.1474-0.16630.3272-0.1291-0.04370.5819-0.2704-0.02230.4308-0.0818-0.03580.26650.05320.3814-12.7741-29.430470.84
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'B' and (resid 197 through 270 )B197 - 270
2X-RAY DIFFRACTION2chain 'B' and (resid 271 through 328 )B271 - 328
3X-RAY DIFFRACTION3chain 'B' and (resid 329 through 362 )B329 - 362
4X-RAY DIFFRACTION4chain 'C' and (resid 1 through 67 )C1 - 67
5X-RAY DIFFRACTION5chain 'C' and (resid 68 through 196 )C68 - 196
6X-RAY DIFFRACTION6chain 'C' and (resid 197 through 229 )C197 - 229
7X-RAY DIFFRACTION7chain 'C' and (resid 230 through 258 )C230 - 258
8X-RAY DIFFRACTION8chain 'C' and (resid 259 through 301 )C259 - 301
9X-RAY DIFFRACTION9chain 'C' and (resid 302 through 328 )C302 - 328
10X-RAY DIFFRACTION10chain 'C' and (resid 329 through 362 )C329 - 362
11X-RAY DIFFRACTION11chain 'D' and (resid 1 through 67 )D1 - 67
12X-RAY DIFFRACTION12chain 'D' and (resid 68 through 328 )D68 - 328
13X-RAY DIFFRACTION13chain 'D' and (resid 329 through 362 )D329 - 362
14X-RAY DIFFRACTION14chain 'A' and (resid 1 through 67 )A1 - 67
15X-RAY DIFFRACTION15chain 'A' and (resid 68 through 196 )A68 - 196
16X-RAY DIFFRACTION16chain 'A' and (resid 197 through 328 )A197 - 328
17X-RAY DIFFRACTION17chain 'A' and (resid 329 through 362 )A329 - 362
18X-RAY DIFFRACTION18chain 'B' and (resid 1 through 67 )B1 - 67
19X-RAY DIFFRACTION19chain 'B' and (resid 68 through 119 )B68 - 119
20X-RAY DIFFRACTION20chain 'B' and (resid 120 through 196 )B120 - 196

+
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