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- PDB-4z87: Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP -

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Basic information

Entry
Database: PDB / ID: 4z87
TitleStructure of the IMP dehydrogenase from Ashbya gossypii bound to GDP
ComponentsInosine-5'-monophosphate dehydrogenase
KeywordsOXIDOREDUCTASE / IMP dehydrgoenase / Bateman domain
Function / homology
Function and homology information


IMP dehydrogenase activity / IMP dehydrogenase / GMP biosynthetic process / GTP biosynthetic process / ATP binding / metal ion binding / cytoplasm
Similarity search - Function
IMP dehydrogenase / GMP reductase domain / Inosine-5'-monophosphate dehydrogenase / IMP dehydrogenase / GMP reductase, conserved site / IMP dehydrogenase / GMP reductase signature. / IMP dehydrogenase/GMP reductase / IMP dehydrogenase / GMP reductase domain / CBS domain superfamily / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain ...IMP dehydrogenase / GMP reductase domain / Inosine-5'-monophosphate dehydrogenase / IMP dehydrogenase / GMP reductase, conserved site / IMP dehydrogenase / GMP reductase signature. / IMP dehydrogenase/GMP reductase / IMP dehydrogenase / GMP reductase domain / CBS domain superfamily / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain / CBS domain profile. / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-MONOPHOSPHATE / ACETATE ION / GUANOSINE-5'-DIPHOSPHATE / : / Inosine-5'-monophosphate dehydrogenase
Similarity search - Component
Biological speciesAshbya gossypii (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsBuey, R.M. / de Pereda, J.M. / Revuelta, J.L.
CitationJournal: Nat Commun / Year: 2015
Title: Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
Authors: Buey, R.M. / Ledesma-Amaro, R. / Velazquez-Campoy, A. / Balsera, M. / Chagoyen, M. / de Pereda, J.M. / Revuelta, J.L.
History
DepositionApr 8, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Nov 25, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 10, 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 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Inosine-5'-monophosphate dehydrogenase
B: Inosine-5'-monophosphate dehydrogenase
C: Inosine-5'-monophosphate dehydrogenase
D: Inosine-5'-monophosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)234,39928
Polymers227,2354
Non-polymers7,16424
Water8,053447
1
A: Inosine-5'-monophosphate dehydrogenase
B: Inosine-5'-monophosphate dehydrogenase
hetero molecules

A: Inosine-5'-monophosphate dehydrogenase
B: Inosine-5'-monophosphate dehydrogenase
hetero molecules

A: Inosine-5'-monophosphate dehydrogenase
B: Inosine-5'-monophosphate dehydrogenase
hetero molecules

A: Inosine-5'-monophosphate dehydrogenase
B: Inosine-5'-monophosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)468,79756
Polymers454,4708
Non-polymers14,32848
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
crystal symmetry operation3_555-y,x,z1
crystal symmetry operation4_555y,-x,z1
Buried area76340 Å2
ΔGint-406 kcal/mol
Surface area134650 Å2
MethodPISA
2
C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)468,79756
Polymers454,4708
Non-polymers14,32848
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_645-x+1,-y-1,z1
crystal symmetry operation3_545-y,x-1,z1
crystal symmetry operation4_655y+1,-x,z1
crystal symmetry operation1_554x,y,z-11
crystal symmetry operation2_644-x+1,-y-1,z-11
crystal symmetry operation3_544-y,x-1,z-11
crystal symmetry operation4_654y+1,-x,z-11
Buried area72250 Å2
ΔGint-363 kcal/mol
Surface area132190 Å2
MethodPISA
3
D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

D: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules

C: Inosine-5'-monophosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)468,79756
Polymers454,4708
Non-polymers14,32848
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_655y+1,-x,z1
crystal symmetry operation2_645-x+1,-y-1,z1
crystal symmetry operation3_545-y,x-1,z1
crystal symmetry operation3_546-y,x-1,z+11
crystal symmetry operation1_556x,y,z+11
crystal symmetry operation2_646-x+1,-y-1,z+11
crystal symmetry operation4_656y+1,-x,z+11
Buried area69800 Å2
ΔGint-359.5 kcal/mol
Surface area132290 Å2
MethodPISA
Unit cell
Length a, b, c (Å)122.042, 122.042, 147.613
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number75
Space group name H-MP4

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Inosine-5'-monophosphate dehydrogenase / IMPDH


Mass: 56808.699 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Ashbya gossypii (strain ATCC 10895) (fungus)
Gene: AGOS_AER117W / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q756Z6, IMP dehydrogenase

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Non-polymers , 5 types, 471 molecules

#2: Chemical
ChemComp-5GP / GUANOSINE-5'-MONOPHOSPHATE


Mass: 363.221 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H14N5O8P
#3: Chemical
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: K
#5: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 447 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.42 Å3/Da / Density % sol: 49.15 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop
Details: 40% (v/v) 1,2-propanediol, 0.1 M sodium acetate, pH 4.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00004 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Oct 22, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00004 Å / Relative weight: 1
ReflectionResolution: 2.25→47.05 Å / Num. obs: 102432 / % possible obs: 100 % / Redundancy: 13.84 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 26.04
Reflection shellResolution: 2.25→2.31 Å / Redundancy: 14.15 % / Rmerge(I) obs: 1.65 / Mean I/σ(I) obs: 1.98 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIXdev_1839refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4Z0G
Resolution: 2.25→47.029 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 22.94 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2254 5017 4.91 %
Rwork0.1949 --
obs0.1964 102236 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.25→47.029 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14567 0 452 447 15466
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00815389
X-RAY DIFFRACTIONf_angle_d0.73720857
X-RAY DIFFRACTIONf_dihedral_angle_d11.4975502
X-RAY DIFFRACTIONf_chiral_restr0.0282420
X-RAY DIFFRACTIONf_plane_restr0.0032632
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.25-2.27560.33491700.28053202X-RAY DIFFRACTION100
2.2756-2.30240.2621550.26273280X-RAY DIFFRACTION100
2.3024-2.33040.30741790.26023201X-RAY DIFFRACTION100
2.3304-2.35990.29511980.25543185X-RAY DIFFRACTION100
2.3599-2.3910.28861540.24933269X-RAY DIFFRACTION100
2.391-2.42370.27451760.24763201X-RAY DIFFRACTION100
2.4237-2.45840.26821390.23963280X-RAY DIFFRACTION100
2.4584-2.49510.2891710.23723215X-RAY DIFFRACTION100
2.4951-2.5340.27891500.23453220X-RAY DIFFRACTION100
2.534-2.57560.28141610.23453243X-RAY DIFFRACTION100
2.5756-2.620.23092000.22643199X-RAY DIFFRACTION100
2.62-2.66760.27052030.22493207X-RAY DIFFRACTION100
2.6676-2.71890.27671300.22873287X-RAY DIFFRACTION100
2.7189-2.77440.26631350.21853262X-RAY DIFFRACTION100
2.7744-2.83480.27661480.22273236X-RAY DIFFRACTION100
2.8348-2.90070.27241850.22253231X-RAY DIFFRACTION100
2.9007-2.97320.26371350.21773266X-RAY DIFFRACTION100
2.9732-3.05360.23951720.21833217X-RAY DIFFRACTION100
3.0536-3.14340.24561890.20863227X-RAY DIFFRACTION100
3.1434-3.24490.22241680.20813234X-RAY DIFFRACTION100
3.2449-3.36080.23661610.19733241X-RAY DIFFRACTION100
3.3608-3.49530.20911820.1843246X-RAY DIFFRACTION100
3.4953-3.65430.19811910.17593196X-RAY DIFFRACTION100
3.6543-3.84690.1851490.17033267X-RAY DIFFRACTION100
3.8469-4.08780.18991810.16563232X-RAY DIFFRACTION100
4.0878-4.40320.19191790.15813213X-RAY DIFFRACTION100
4.4032-4.84590.17951690.15113287X-RAY DIFFRACTION100
4.8459-5.54620.19731620.17413266X-RAY DIFFRACTION100
5.5462-6.9840.23221670.20073268X-RAY DIFFRACTION100
6.984-47.03930.23311580.19493341X-RAY DIFFRACTION100
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)
12.42681.79080.01612.88320.84860.60610.0025-0.3229-0.04520.1771-0.0583-0.10250.07860.09140.07430.3131-0.0101-0.00870.28380.0090.280521.3715-4.8048-17.2592
20.8538-1.0309-0.90261.50431.4631.5646-0.00280.139-0.2097-0.1022-0.09430.16880.0204-0.13950.11480.3566-0.0012-0.02130.2399-0.00960.418516.8422-47.3076-44.0476
31.93960.2427-0.61211.39430.51922.06510.00120.2832-0.0865-0.35480.02270.0837-0.1209-0.3581-0.02310.30670.0234-0.01590.20940.00340.28517.6598-24.513-33.6729
42.45250.1017-0.121.52830.09511.3963-0.20950.73240.5128-0.7961-0.2803-0.3218-0.0581-0.29790.37760.70830.02320.06020.49650.01350.547414.8666-5.2945-34.503
54.28111.89460.63082.30060.18392.1809-0.65551.09860.0367-0.71980.6499-0.107-0.02970.11850.10080.4458-0.0092-0.03750.51380.03060.2962-2.6656-19.3187-99.6201
62.5457-1.21831.20540.6704-0.82010.9653-0.0729-0.187-0.09170.150.0831-0.10670.0433-0.0752-0.00680.30720.0536-0.0260.3283-0.03890.334927.1873-23.9121-76.7287
72.2310.48560.27581.9021-0.43742.90970.2042-0.2689-0.11620.0648-0.1946-0.17720.01020.5395-0.00710.29110.0348-0.03580.4513-0.02290.354848.8013-40.762-56.0703
80.6212-1.50321.08843.3476-2.37912.04260.03750.16010.0994-0.1432-0.1223-0.30830.06210.27280.10990.30610.02210.01230.4117-0.05470.378536.9671-23.134-79.7354
91.6496-0.50280.0891.3064-0.39951.9414-0.0419-0.25630.14320.14420.0492-0.0407-0.20650.0619-0.04020.40030.01110.01650.4083-0.09310.378619.5139-12.8434-77.9936
101.5270.2175-0.37440.56360.67881.6579-0.0533-0.36950.453-0.1432-0.1556-0.0493-0.59790.02410.17320.6018-0.0465-0.07180.65120.07760.570918.3739-17.4066-72.325
112.6987-0.1763-0.03981.5096-0.37651.5032-0.0626-0.01830.36990.2146-0.09740.265-0.2756-0.58680.2250.51140.02660.01980.5384-0.0550.47494.5447-19.2797-84.0721
120.99880.73780.01582.7038-1.01330.872-0.07570.07690.2223-0.1495-0.0911-0.065-0.0849-0.04810.16740.44140.0518-0.07760.3273-0.01350.330948.0877-34.177-102.5352
131.9935-0.29581.13061.7227-0.49172.503-0.56820.04750.63530.22830.117-0.3572-1.09120.3740.43070.9874-0.0643-0.23170.50070.10090.762143.75250.2729-127.2752
141.5023-0.28230.82791.7875-1.01572.0082-0.09190.2180.2957-0.1052-0.1344-0.3126-0.17730.250.21480.4697-0.0052-0.04230.39780.02330.422158.963-27.2967-104.7147
150.88830.13880.01740.4921-0.00232.0511-0.24620.4336-0.1395-0.44640.131-0.53110.1360.5092-0.00260.8317-0.0313-0.03490.6883-0.02050.676754.9625-36.807-114.4808
162.52020.5875-0.48862.3398-0.03271.4245-0.13290.1845-0.3444-0.1935-0.1075-0.08770.38670.01970.29990.55490.024-0.0490.4595-0.01560.528245.4041-48.4061-101.6682
172.16070.47340.36072.1456-0.08751.315-0.24810.79660.1346-0.49160.347-0.0984-0.28930.1571-0.08580.4757-0.06760.03260.55820.00170.253367.1614-40.6148-23.8268
182.3906-1.1538-0.62972.00590.9040.8697-0.1239-0.33030.24410.05350.07510.2232-0.04310.06020.08570.34670.0308-0.0130.45360.02190.316537.0791-33.4517-0.656
192.0923-0.7616-0.32272.4040.70552.0798-0.2569-0.1133-0.03570.38990.13290.43470.1225-0.26950.07540.58870.10590.07180.54810.07270.643518.3951-13.592620.0091
200.9381-0.5163-0.6792.47980.78451.82050.06550.21230.4177-0.03890.01830.1316-0.4434-0.3798-0.06290.63360.0711-0.0510.59790.05010.580127.9233-13.52484.2861
212.7-1.5778-0.78283.15861.5221.6635-0.1030.0686-0.14910.0584-0.03450.390.1682-0.09240.10620.4861-0.0243-0.0630.4360.06870.382530.3638-46.6849-9.7256
221.9220.58190.32742.07520.75751.26150.0393-0.7232-0.29970.3186-0.05630.03780.3815-0.00070.12360.45140.019-0.00210.65420.05910.397445.429-40.78943.1334
233.0507-0.31260.06732.73070.63560.4548-0.1311-0.0137-0.32060.42290.0797-0.26590.40190.0281-0.05880.6909-0.00730.04110.56370.05060.484459.3482-41.7413-8.8915
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 0 through 51 )
2X-RAY DIFFRACTION2chain 'A' and (resid 52 through 296 )
3X-RAY DIFFRACTION3chain 'A' and (resid 297 through 491 )
4X-RAY DIFFRACTION4chain 'A' and (resid 492 through 522 )
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 37 )
6X-RAY DIFFRACTION6chain 'B' and (resid 38 through 124 )
7X-RAY DIFFRACTION7chain 'B' and (resid 125 through 195 )
8X-RAY DIFFRACTION8chain 'B' and (resid 196 through 335 )
9X-RAY DIFFRACTION9chain 'B' and (resid 336 through 415 )
10X-RAY DIFFRACTION10chain 'B' and (resid 416 through 478 )
11X-RAY DIFFRACTION11chain 'B' and (resid 479 through 522 )
12X-RAY DIFFRACTION12chain 'C' and (resid 2 through 124 )
13X-RAY DIFFRACTION13chain 'C' and (resid 125 through 219 )
14X-RAY DIFFRACTION14chain 'C' and (resid 220 through 410 )
15X-RAY DIFFRACTION15chain 'C' and (resid 411 through 478 )
16X-RAY DIFFRACTION16chain 'C' and (resid 479 through 522 )
17X-RAY DIFFRACTION17chain 'D' and (resid 2 through 37 )
18X-RAY DIFFRACTION18chain 'D' and (resid 38 through 124 )
19X-RAY DIFFRACTION19chain 'D' and (resid 125 through 195 )
20X-RAY DIFFRACTION20chain 'D' and (resid 196 through 249 )
21X-RAY DIFFRACTION21chain 'D' and (resid 250 through 360 )
22X-RAY DIFFRACTION22chain 'D' and (resid 361 through 478 )
23X-RAY DIFFRACTION23chain 'D' and (resid 479 through 517 )

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