[English] 日本語
Yorodumi
- PDB-9emy: P. falciparum FIKK13 in complex with ATPgammaS -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9emy
TitleP. falciparum FIKK13 in complex with ATPgammaS
Components
  • Nanobody 2G9
  • Nanobody 9F10
  • non-specific serine/threonine protein kinase
KeywordsPEPTIDE BINDING PROTEIN / Malaria / kinase
Function / homology
Function and homology information


non-specific serine/threonine protein kinase / protein serine/threonine kinase activity / ATP binding / membrane
Similarity search - Function
Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / non-specific serine/threonine protein kinase
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.814 Å
AuthorsPurkiss, A.G. / Ogrodowicz, R.W. / Christodoulou, E. / Kjaer, S.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
The Francis Crick Institute United Kingdom
CitationJournal: To Be Published
Title: Evolution and inhibition of the FIKK effector kinase family in P. falciparum
Authors: Purkiss, A.G. / Ogrodowicz, R.W. / Christodoulou, E. / Kjaer, S. / Belda, H. / Bradley, D. / Nofal, S.D. / Broncel, M. / Jones, D.A. / Davies, H. / Bertran, M.T. / Joshi, D. / OReilly, N. / ...Authors: Purkiss, A.G. / Ogrodowicz, R.W. / Christodoulou, E. / Kjaer, S. / Belda, H. / Bradley, D. / Nofal, S.D. / Broncel, M. / Jones, D.A. / Davies, H. / Bertran, M.T. / Joshi, D. / OReilly, N. / Walport, L. / Claessens, A. / Powell, A.J. / House, D. / Landry, C.R.
History
DepositionMar 11, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 26, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: non-specific serine/threonine protein kinase
B: non-specific serine/threonine protein kinase
C: Nanobody 9F10
D: Nanobody 9F10
E: Nanobody 2G9
F: Nanobody 2G9
G: non-specific serine/threonine protein kinase
H: non-specific serine/threonine protein kinase
I: Nanobody 9F10
J: Nanobody 9F10
K: Nanobody 2G9
L: Nanobody 2G9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)318,22617
Polymers315,77812
Non-polymers2,4475
Water32418
1
A: non-specific serine/threonine protein kinase
C: Nanobody 9F10
E: Nanobody 2G9
hetero molecules


  • defined by author
  • Evidence: homology, Apo structure is a pair of trimers. Each trimer comprising one copy each of FIKK13 and the two nanobodies., PISA analysis suggests the interface between FIKK monomers is much ...Evidence: homology, Apo structure is a pair of trimers. Each trimer comprising one copy each of FIKK13 and the two nanobodies., PISA analysis suggests the interface between FIKK monomers is much weaker than between FIKK monomers and each nanobody.
  • 79.8 kDa, 3 polymers
  • Search similar-shape structures of this assembly by Omokage search (details)
Theoretical massNumber of molelcules
Total (without water)79,8225
Polymers78,9453
Non-polymers8782
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4730 Å2
ΔGint-30 kcal/mol
Surface area25650 Å2
MethodPISA
2
B: non-specific serine/threonine protein kinase
D: Nanobody 9F10
F: Nanobody 2G9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,4684
Polymers78,9453
Non-polymers5231
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4570 Å2
ΔGint-28 kcal/mol
Surface area26700 Å2
MethodPISA
3
G: non-specific serine/threonine protein kinase
I: Nanobody 9F10
K: Nanobody 2G9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,4684
Polymers78,9453
Non-polymers5231
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4720 Å2
ΔGint-31 kcal/mol
Surface area25530 Å2
MethodPISA
4
H: non-specific serine/threonine protein kinase
J: Nanobody 9F10
L: Nanobody 2G9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,4684
Polymers78,9453
Non-polymers5231
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4520 Å2
ΔGint-27 kcal/mol
Surface area26000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.397, 121.657, 151.059
Angle α, β, γ (deg.)90, 90.02, 90
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
32A
42G
53A
63H
74B
84G
95B
105H
116C
126D
137C
147I
158C
168J
179D
189I
1910D
2010J
2111E
2211F
2312E
2412K
2513E
2613L
2714F
2814K
2915F
3015L
3116G
3216H
3317I
3417J
3518K
3618L

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111TYRTYRLYSLYSAA158 - 56010 - 412
211TYRTYRLYSLYSBB158 - 56010 - 412
322SERSERSERSERAA157 - 5589 - 410
422SERSERSERSERGG157 - 5589 - 410
533TYRTYRLYSLYSAA158 - 56010 - 412
633TYRTYRLYSLYSHH158 - 56010 - 412
744TYRTYRSERSERBB158 - 55910 - 411
844TYRTYRSERSERGG158 - 55910 - 411
955TYRTYRLYSLYSBB158 - 56010 - 412
1055TYRTYRLYSLYSHH158 - 56010 - 412
1166GLUGLUSERSERCC4 - 1282 - 126
1266GLUGLUSERSERDD4 - 1282 - 126
1377GLUGLUSERSERCC4 - 1282 - 126
1477GLUGLUSERSERII4 - 1282 - 126
1588GLNGLNSERSERCC5 - 1283 - 126
1688GLNGLNSERSERJJ5 - 1283 - 126
1799GLUGLUSERSERDD4 - 1282 - 126
1899GLUGLUSERSERII4 - 1282 - 126
191010GLNGLNSERSERDD5 - 1283 - 126
201010GLNGLNSERSERJJ5 - 1283 - 126
211111GLUGLUSERSEREE8 - 1266 - 124
221111GLUGLUSERSERFF8 - 1266 - 124
231212VALVALSERSEREE4 - 1262 - 124
241212VALVALSERSERKK4 - 1262 - 124
251313GLUGLUSERSEREE8 - 1266 - 124
261313GLUGLUSERSERLL8 - 1266 - 124
271414GLUGLUSERSERFF8 - 1276 - 125
281414GLUGLUSERSERKK8 - 1276 - 125
291515GLUGLUSERSERFF8 - 1276 - 125
301515GLUGLUSERSERLL8 - 1276 - 125
311616TYRTYRSERSERGG158 - 55910 - 411
321616TYRTYRSERSERHH158 - 55910 - 411
331717GLNGLNSERSERII5 - 1283 - 126
341717GLNGLNSERSERJJ5 - 1283 - 126
351818GLUGLUSERSERKK8 - 1266 - 124
361818GLUGLUSERSERLL8 - 1266 - 124

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36

-
Components

-
Protein , 1 types, 4 molecules ABGH

#1: Protein
non-specific serine/threonine protein kinase


Mass: 49764.645 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Gene: CK202_4380, CYL21_5595 / Production host: Escherichia coli BL21 (bacteria)
References: UniProt: A0A2I0BRS6, non-specific serine/threonine protein kinase

-
Antibody , 2 types, 8 molecules CDIJEFKL

#2: Antibody
Nanobody 9F10


Mass: 14703.017 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)
#3: Antibody
Nanobody 2G9


Mass: 14476.922 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli BL21 (bacteria)

-
Non-polymers , 3 types, 23 molecules

#4: Chemical
ChemComp-AGS / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-GAMMA-S / ADENOSINE 5'-(3-THIOTRIPHOSPHATE) / ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE) / ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE


Mass: 523.247 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O12P3S / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
#5: Chemical ChemComp-PE4 / 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / POLYETHYLENE GLYCOL PEG4000


Mass: 354.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H34O8 / Comment: precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.71 Å3/Da / Density % sol: 27.96 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.2 M LiCl, 20% w/v PEG 6,000, 10% v/v Ethylene Glycol, 0.1M HEPES

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 22, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.81→64.17 Å / Num. obs: 72257 / % possible obs: 99.8 % / Redundancy: 7 % / Biso Wilson estimate: 55.6 Å2 / CC1/2: 0.995 / R split: 0.212 / Rmerge(I) obs: 0.196 / Rpim(I) all: 0.079 / Net I/σ(I): 6.8
Reflection shellResolution: 2.81→2.86 Å / Redundancy: 7.3 % / Rmerge(I) obs: 2.123 / Mean I/σ(I) obs: 0.4 / Num. unique obs: 3451 / CC1/2: 0.614 / Rpim(I) all: 0.844 / Rrim(I) all: 2.286 / % possible all: 96.1

-
Processing

Software
NameVersionClassification
REFMAC5.8.0430 (refmacat 0.4.88)refinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.814→64.169 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.869 / WRfactor Rfree: 0.246 / WRfactor Rwork: 0.202 / SU B: 66.896 / SU ML: 0.534 / Average fsc free: 0.9301 / Average fsc work: 0.9516 / Cross valid method: THROUGHOUT / ESU R Free: 0.434 / Details: Hydrogens have not been used
RfactorNum. reflection% reflection
Rfree0.2862 3699 5.126 %
Rwork0.2423 68457 -
all0.245 --
obs-72156 99.686 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 74.501 Å2
Baniso -1Baniso -2Baniso -3
1--0.124 Å2-0 Å2-0.015 Å2
2---0.963 Å20 Å2
3---1.086 Å2
Refinement stepCycle: LAST / Resolution: 2.814→64.169 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19014 0 148 18 19180
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01219651
X-RAY DIFFRACTIONr_angle_refined_deg1.5491.79626740
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.79652436
X-RAY DIFFRACTIONr_dihedral_angle_2_deg23.05564
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.576102966
X-RAY DIFFRACTIONr_dihedral_angle_6_deg14.68910846
X-RAY DIFFRACTIONr_chiral_restr0.0990.22901
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0215316
X-RAY DIFFRACTIONr_nbd_refined0.2350.28248
X-RAY DIFFRACTIONr_nbtor_refined0.3140.213230
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1470.2485
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.320.224
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2380.25
X-RAY DIFFRACTIONr_mcbond_it2.2192.4029840
X-RAY DIFFRACTIONr_mcangle_it3.6944.30412244
X-RAY DIFFRACTIONr_scbond_it2.6322.4889811
X-RAY DIFFRACTIONr_scangle_it4.1894.54114496
X-RAY DIFFRACTIONr_lrange_it7.86328.64280690
X-RAY DIFFRACTIONr_ncsr_local_group_10.0770.0512224
X-RAY DIFFRACTIONr_ncsr_local_group_20.0590.0512587
X-RAY DIFFRACTIONr_ncsr_local_group_30.0770.0512208
X-RAY DIFFRACTIONr_ncsr_local_group_40.0820.0512087
X-RAY DIFFRACTIONr_ncsr_local_group_50.0420.0512739
X-RAY DIFFRACTIONr_ncsr_local_group_60.1160.053207
X-RAY DIFFRACTIONr_ncsr_local_group_70.0490.053626
X-RAY DIFFRACTIONr_ncsr_local_group_80.1210.053154
X-RAY DIFFRACTIONr_ncsr_local_group_90.1060.053233
X-RAY DIFFRACTIONr_ncsr_local_group_100.0840.053332
X-RAY DIFFRACTIONr_ncsr_local_group_110.1190.052932
X-RAY DIFFRACTIONr_ncsr_local_group_120.0910.053539
X-RAY DIFFRACTIONr_ncsr_local_group_130.1320.052964
X-RAY DIFFRACTIONr_ncsr_local_group_140.1150.052992
X-RAY DIFFRACTIONr_ncsr_local_group_150.0750.053046
X-RAY DIFFRACTIONr_ncsr_local_group_160.0820.0512094
X-RAY DIFFRACTIONr_ncsr_local_group_170.1090.053190
X-RAY DIFFRACTIONr_ncsr_local_group_180.1230.053022
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.076540.0501
12BX-RAY DIFFRACTIONLocal ncs0.076540.0501
23AX-RAY DIFFRACTIONLocal ncs0.059110.05011
24GX-RAY DIFFRACTIONLocal ncs0.059110.05011
35AX-RAY DIFFRACTIONLocal ncs0.077220.0501
36HX-RAY DIFFRACTIONLocal ncs0.077220.0501
47BX-RAY DIFFRACTIONLocal ncs0.081860.0501
48GX-RAY DIFFRACTIONLocal ncs0.081860.0501
59BX-RAY DIFFRACTIONLocal ncs0.042180.05011
510HX-RAY DIFFRACTIONLocal ncs0.042180.05011
611CX-RAY DIFFRACTIONLocal ncs0.116430.05011
612DX-RAY DIFFRACTIONLocal ncs0.116430.05011
713CX-RAY DIFFRACTIONLocal ncs0.049320.05013
714IX-RAY DIFFRACTIONLocal ncs0.049320.05013
815CX-RAY DIFFRACTIONLocal ncs0.121160.0501
816JX-RAY DIFFRACTIONLocal ncs0.121160.0501
917DX-RAY DIFFRACTIONLocal ncs0.105910.05011
918IX-RAY DIFFRACTIONLocal ncs0.105910.05011
1019DX-RAY DIFFRACTIONLocal ncs0.083620.05011
1020JX-RAY DIFFRACTIONLocal ncs0.083620.05011
1121EX-RAY DIFFRACTIONLocal ncs0.118770.05009
1122FX-RAY DIFFRACTIONLocal ncs0.118770.05009
1223EX-RAY DIFFRACTIONLocal ncs0.090570.05011
1224KX-RAY DIFFRACTIONLocal ncs0.090570.05011
1325EX-RAY DIFFRACTIONLocal ncs0.132420.05009
1326LX-RAY DIFFRACTIONLocal ncs0.132420.05009
1427FX-RAY DIFFRACTIONLocal ncs0.115470.0501
1428KX-RAY DIFFRACTIONLocal ncs0.115470.0501
1529FX-RAY DIFFRACTIONLocal ncs0.075180.05011
1530LX-RAY DIFFRACTIONLocal ncs0.075180.05011
1631GX-RAY DIFFRACTIONLocal ncs0.082290.0501
1632HX-RAY DIFFRACTIONLocal ncs0.082290.0501
1733IX-RAY DIFFRACTIONLocal ncs0.108980.05011
1734JX-RAY DIFFRACTIONLocal ncs0.108980.05011
1835KX-RAY DIFFRACTIONLocal ncs0.12260.0501
1836LX-RAY DIFFRACTIONLocal ncs0.12260.0501
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.814-2.8870.4172850.39549000.39653340.8730.89397.20660.397
2.887-2.9660.4342410.36849640.37152160.860.91399.78910.364
2.966-3.0520.3662470.35747960.35750510.9140.91799.84160.346
3.052-3.1460.3982700.33146000.33548790.8860.93299.81550.312
3.146-3.2490.3232130.31444840.31447080.9290.93999.76640.287
3.249-3.3620.3392420.27543560.27946070.9320.95499.80460.243
3.362-3.4890.312780.26641610.26844430.9380.95899.910.232
3.489-3.6310.2592120.23940330.2442470.9530.96799.95290.204
3.631-3.7920.2941900.23339310.23641220.9420.96999.97570.197
3.792-3.9760.2741920.20837750.21139680.9490.97599.97480.174
3.976-4.1910.2511790.19735300.237120.9570.97799.91920.161
4.191-4.4440.2312140.18932970.19235130.9690.9899.94310.159
4.444-4.7490.2231650.18131740.18233400.9710.98199.97010.15
4.749-5.1270.2161450.19629510.19730960.970.9771000.161
5.127-5.6130.2661210.2127450.21328670.9430.97499.96510.168
5.613-6.2690.2621540.2324350.23225920.9540.97299.88430.184
6.269-7.2270.2881270.24321610.24522890.9410.96899.95630.198
7.227-8.8240.1921040.19218580.19219620.9770.9771000.164
8.824-12.3620.266750.18314590.18715350.9580.9899.93490.173
12.362-64.1690.527450.4028470.4088950.8540.90299.66480.37
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)
11.52540.0751-0.40221.7357-0.19360.8591-0.0787-0.0412-0.12130.03750.0985-0.17060.09970.1913-0.01980.89720.0493-0.04850.4066-0.05030.035522.9319-6.802822.5341
21.3787-0.2132-0.16981.43410.5641.4718-0.113-0.07840.08560.04670.11350.12620.1374-0.0411-0.00040.99480.08510.0530.45360.05780.029-3.879919.337154.7435
32.25841.28563.12722.32331.79014.9265-0.00210.3414-0.3622-0.05390.11160.1264-0.00960.0915-0.10950.77570.06540.01810.4691-0.19510.4728-2.2749-23.54192.2867
42.268-0.249-0.65031.3435-0.56892.6657-0.0022-0.0372-0.788-0.3538-0.07680.40280.2118-0.53370.0791.1295-0.04030.02220.69060.04370.5346-31.6432-1.705563.6093
53.7465-3.0766-0.09584.03410.9442.1556-0.02020.43040.076-0.1921-0.13930.475-0.2871-0.25760.15950.86190.0277-0.02350.53120.02230.2461-9.968710.52316.573
61.3086-1.1375-0.9454.53970.73222.1606-0.0142-0.3785-0.22360.2196-0.04810.250.1456-0.01440.06230.88860.02270.07570.5190.08630.17882.8845-17.740353.6404
71.283-0.22580.4181.6275-0.25331.0431-0.0676-0.03080.1318-0.03930.1026-0.1761-0.07970.1808-0.03490.8907-0.05430.01640.4042-0.06830.041864.223567.412253.1029
81.27390.17480.21011.58920.56141.1941-0.12480.1046-0.0376-0.06410.11420.128-0.136-0.04760.01060.9839-0.0916-0.0670.45080.05440.022137.110541.722920.6311
92.0858-1.263-2.96182.74641.6864.9737-0.0147-0.30110.35580.07210.08740.19040.01220.0393-0.07270.7784-0.0424-0.02380.4809-0.19360.465438.860184.392673.2982
102.45330.37840.48541.5335-0.78871.53740.0941-0.00130.84590.4041-0.14630.3553-0.1825-0.55960.05211.13840.026-0.04460.71560.04380.5039.477962.320711.9507
114.13133.17440.08254.44740.85061.9759-0.0521-0.3116-0.0980.22-0.0870.45830.2948-0.19880.13910.853-0.03120.0090.5290.00760.197331.350250.089358.8446
120.80751.3221.10675.41951.47112.71070.02890.32320.1458-0.2389-0.05690.21-0.149-0.05830.02810.8663-0.0083-0.06580.5740.11390.194943.887378.542521.7848
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1ALLAp157 - 601
2X-RAY DIFFRACTION2ALLBp158 - 602
3X-RAY DIFFRACTION3ALLCp4 - 128
4X-RAY DIFFRACTION4ALLDp4 - 129
5X-RAY DIFFRACTION5ALLEp3 - 127
6X-RAY DIFFRACTION6ALLFp8 - 127
7X-RAY DIFFRACTION7ALLGp157 - 601
8X-RAY DIFFRACTION8ALLHp158 - 601
9X-RAY DIFFRACTION9ALLIp4 - 128
10X-RAY DIFFRACTION10ALLJp5 - 129
11X-RAY DIFFRACTION11ALLKp4 - 127
12X-RAY DIFFRACTION12ALLLp8 - 127

+
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