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- PDB-6fjf: Tubulin-FcMaytansine complex -

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Basic information

Entry
Database: PDB / ID: 6fjf
TitleTubulin-FcMaytansine complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin tyrosine ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / microtubule cytoskeleton / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / cilium / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / ATP-grasp fold, A domain / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Dna Ligase; domain 1 / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Helix non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / FcMaytansine / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / DI(HYDROXYETHYL)ETHER / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain / Tubulin beta-2B chain
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Gallus gallus (chicken)
Bos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.402 Å
AuthorsMenchon, G. / Prota, A.E. / Lucena Angell, D. / Bucher, P. / Mueller, R. / Paterson, I. / Diaz, J.F. / Altmann, K.-H. / Steinmetz, M.O.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
CitationJournal: Nat Commun / Year: 2018
Title: A fluorescence anisotropy assay to discover and characterize ligands targeting the maytansine site of tubulin.
Authors: Menchon, G. / Prota, A.E. / Lucena-Agell, D. / Bucher, P. / Jansen, R. / Irschik, H. / Muller, R. / Paterson, I. / Diaz, J.F. / Altmann, K.H. / Steinmetz, M.O.
History
DepositionJan 22, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 30, 2018Provider: repository / Type: Initial release
Revision 1.1Jun 13, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Jan 17, 2024Group: 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 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Revision 2.0Apr 23, 2025Group: Data collection / Non-polymer description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / pdbx_entry_details
Item: _chem_comp.formula

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tubulin alpha-1B chain
B: Tubulin beta-2B chain
C: Tubulin alpha-1B chain
D: Tubulin beta-2B chain
E: Stathmin-4
F: Tubulin tyrosine ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,09626
Polymers261,6316
Non-polymers4,46420
Water8,143452
1


  • Idetical with deposited unit
  • defined by software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24590 Å2
ΔGint-111 kcal/mol
Surface area80380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.373, 156.739, 180.956
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein Tubulin alpha-1B chain / Alpha-tubulin ubiquitous / Tubulin K-alpha-1 / Tubulin alpha-ubiquitous chain


Mass: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Organ: Brain / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Organ: Brain / References: UniProt: Q6B856
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63043
#4: Protein Tubulin tyrosine ligase


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 10 types, 472 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#8: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#9: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#10: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#12: Chemical ChemComp-DKE / FcMaytansine


Mass: 1132.624 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C59H63ClN6O15
#13: Chemical ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#14: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 452 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationN

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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: 2.83 Å3/Da / Density % sol: 56.52 %
Crystal growTemperature: 294 K / Method: vapor diffusion / pH: 6.7
Details: 10 % PEG 4k, 16 % glycerol, 30 mM MgCl2, 30 mM CaCl2, and 100 mM 2-(N-morpholino)ethanesulfonic acid/imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00036 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 25, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00036 Å / Relative weight: 1
ReflectionResolution: 2.4→49.6 Å / Num. obs: 116072 / % possible obs: 100 % / Redundancy: 6.8 % / CC1/2: 0.994 / Rmerge(I) obs: 0.216 / Rrim(I) all: 0.234 / Net I/σ(I): 9.96
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 6.5 % / Rmerge(I) obs: 2.586 / Mean I/σ(I) obs: 0.75 / Num. unique obs: 8494 / CC1/2: 0.277 / Rrim(I) all: 2.814 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX(dev_2863: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.402→49.547 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 28.97
RfactorNum. reflection% reflection
Rfree0.2575 5732 4.94 %
Rwork0.2005 --
obs0.2033 116054 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.402→49.547 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17362 0 278 453 18093
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218074
X-RAY DIFFRACTIONf_angle_d0.54524510
X-RAY DIFFRACTIONf_dihedral_angle_d11.72110781
X-RAY DIFFRACTIONf_chiral_restr0.0422654
X-RAY DIFFRACTIONf_plane_restr0.0043170
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.402-2.42930.44361960.37913633X-RAY DIFFRACTION100
2.4293-2.45790.36271950.34393603X-RAY DIFFRACTION100
2.4579-2.48790.37972060.33743657X-RAY DIFFRACTION100
2.4879-2.51930.3762070.32193594X-RAY DIFFRACTION100
2.5193-2.55250.35711850.31493627X-RAY DIFFRACTION100
2.5525-2.58750.3491720.29843646X-RAY DIFFRACTION100
2.5875-2.62440.36962260.30563622X-RAY DIFFRACTION100
2.6244-2.66360.34571890.29243649X-RAY DIFFRACTION100
2.6636-2.70520.32441970.28763617X-RAY DIFFRACTION100
2.7052-2.74960.35051850.28183731X-RAY DIFFRACTION100
2.7496-2.7970.31072050.27363539X-RAY DIFFRACTION100
2.797-2.84780.31971880.26713675X-RAY DIFFRACTION100
2.8478-2.90260.32631830.26173700X-RAY DIFFRACTION100
2.9026-2.96180.30881770.26183618X-RAY DIFFRACTION100
2.9618-3.02620.31011860.25293669X-RAY DIFFRACTION100
3.0262-3.09660.31911740.23963629X-RAY DIFFRACTION100
3.0966-3.1740.33111900.22393707X-RAY DIFFRACTION100
3.174-3.25980.27741680.22083694X-RAY DIFFRACTION100
3.2598-3.35570.26682060.2083643X-RAY DIFFRACTION100
3.3557-3.4640.25641880.20223654X-RAY DIFFRACTION100
3.464-3.58780.26361880.18783719X-RAY DIFFRACTION100
3.5878-3.73140.24262050.18083700X-RAY DIFFRACTION100
3.7314-3.90120.2241720.16263644X-RAY DIFFRACTION100
3.9012-4.10670.20181840.15693686X-RAY DIFFRACTION100
4.1067-4.36390.19531840.1543743X-RAY DIFFRACTION100
4.3639-4.70060.19081820.13783713X-RAY DIFFRACTION100
4.7006-5.17320.22321650.14643757X-RAY DIFFRACTION100
5.1732-5.92070.2382020.1763740X-RAY DIFFRACTION100
5.9207-7.45540.24772020.1853813X-RAY DIFFRACTION100
7.4554-49.55730.18962250.1553900X-RAY DIFFRACTION100
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)
11.415-0.256-0.43613.61111.3832.5310.02620.05290.2108-0.43640.3249-0.4271-0.65140.4815-0.30290.5073-0.14510.09250.5061-0.16310.423831.526885.755652.8666
22.19480.16860.72433.29241.05594.26910.0657-0.12240.13080.3352-0.04740.1631-0.3651-0.0608-0.0320.40270.01070.08440.3438-0.07780.370516.973286.090170.7339
31.21520.1132-0.23992.96083.05944.52210.01920.0744-0.17920.60260.1729-0.35510.52240.5947-0.18270.42150.1115-0.04780.3554-0.07030.461229.553461.693861.6124
42.1651-0.3483-0.47983.19820.82952.67740.09610.19020.2744-0.2580.0188-0.0101-0.44330.0777-0.11690.2989-0.00390.01270.4127-0.06570.350221.410360.778421.1364
52.1054-0.13050.04791.67161.0572.8915-0.1603-0.0738-0.01550.1156-0.03740.2659-0.1036-0.67150.18260.33450.02390.02450.4894-0.12580.40687.403459.656938.5719
60.0416-0.597-0.38464.60184.0433.5742-0.0263-0.0129-0.14170.6516-0.01640.07940.86890.27590.0060.40780.0302-0.02230.4187-0.03240.395222.670837.397330.9985
71.0383-0.3653-0.18542.28610.15991.6093-0.01640.13680.1127-0.17970.0797-0.0618-0.12830.056-0.05510.2413-0.06420.02260.3422-0.0420.294219.901332.3889-11.5582
81.1823-0.38910.59071.20640.77252.42060.0034-0.11970.1320.0672-0.13630.23360.0489-0.39660.12620.2752-0.05290.03350.3754-0.04030.37882.336830.82593.5483
92.3041-2.1006-2.20153.41443.81065.9192-0.1029-0.1085-0.0620.4160.1538-0.05230.53920.2349-0.06890.28830.023-0.01070.2495-0.00130.310922.234610.4822.2586
102.1863-0.3114-0.22873.08520.20321.7066-0.08690.5102-0.0759-0.50180.1297-0.20830.2160.1513-0.03420.5045-0.06670.08250.6016-0.1310.336623.84721.9896-39.7039
111.408-0.2935-0.59711.8250.90152.7019-0.13220.3264-0.1832-0.1680.00870.16950.3614-0.44250.1210.4322-0.08990.01980.4526-0.09160.33727.3837-0.9223-24.6225
122.6724-1.881-3.4792.54133.09015.9198-0.29670.2285-0.59120.02360.1991-0.2631.09120.41860.13370.780.04260.08350.5414-0.20380.648928.3364-18.9899-26.3753
132.7993-1.77650.5148.7757-4.8882.8883-0.1638-0.2429-0.06091.6533-0.1378-0.0956-0.32840.66190.18690.9146-0.03020.04440.6784-0.14410.463725.481294.589584.2024
141.76973.84443.8957.24097.72748.2450.2898-0.20260.11250.50060.3237-0.56020.49790.3324-0.57880.37390.07580.01770.7475-0.28440.752943.447455.039334.188
15-0.0938-1.413-1.65764.61735.61425.7154-0.10330.0034-0.05530.30980.187-0.11280.44410.3464-0.27120.66460.0910.08160.7871-0.26490.720942.58965.5864-19.8226
162.43481.9491-0.35935.67411.7183.5169-0.5450.4441-0.6446-0.59430.2785-0.17241.253-0.53020.20350.9656-0.16540.15880.5898-0.15810.5616.420154.109169.7882
172.104-0.1503-0.19283.1632-0.96033.330.019-0.7483-0.52930.7348-0.4156-0.80140.32161.60150.39250.81760.1748-0.09521.18230.25160.77815.387557.0292105.2674
182.42610.7709-1.96812.0776-0.61312.122-0.48140.0004-0.62330.23110.2085-0.02670.8929-0.10250.07510.8462-0.0040.14170.39040.02550.6055-1.363552.987993.4942
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 205)
2X-RAY DIFFRACTION2chain 'A' and (resid 206 through 381)
3X-RAY DIFFRACTION3chain 'A' and (resid 382 through 436)
4X-RAY DIFFRACTION4chain 'B' and (resid 2 through 205)
5X-RAY DIFFRACTION5chain 'B' and (resid 206 through 381)
6X-RAY DIFFRACTION6chain 'B' and (resid 382 through 436)
7X-RAY DIFFRACTION7chain 'C' and (resid 1 through 205)
8X-RAY DIFFRACTION8chain 'C' and (resid 206 through 381)
9X-RAY DIFFRACTION9chain 'C' and (resid 382 through 440)
10X-RAY DIFFRACTION10chain 'D' and (resid 2 through 205)
11X-RAY DIFFRACTION11chain 'D' and (resid 206 through 381)
12X-RAY DIFFRACTION12chain 'D' and (resid 382 through 436)
13X-RAY DIFFRACTION13chain 'E' and (resid 7 through 28)
14X-RAY DIFFRACTION14chain 'E' and (resid 45 through 89)
15X-RAY DIFFRACTION15chain 'E' and (resid 90 through 144)
16X-RAY DIFFRACTION16chain 'F' and (resid 1 through 66)
17X-RAY DIFFRACTION17chain 'F' and (resid 67 through 198)
18X-RAY DIFFRACTION18chain 'F' and (resid 199 through 384)

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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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

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