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- PDB-8p2l: A CHIMERA construct containing human SARM1 ARM and SAM domains an... -

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Basic information

Entry
Database: PDB / ID: 8p2l
TitleA CHIMERA construct containing human SARM1 ARM and SAM domains and C. elegans TIR domain.
ComponentsNAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
KeywordsHYDROLASE / SARM1 / TIR-1 / C. elegans / neurodegeneration / cryo-EM / structural biology / NAD+ metabolism / axon Wallerian degeneration
Function / homology
Function and homology information


serotonin biosynthetic process / negative regulation of MyD88-independent toll-like receptor signaling pathway / MyD88-independent TLR4 cascade / Toll Like Receptor 3 (TLR3) Cascade / NADP+ nucleosidase activity / NAD catabolic process / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / protein localization to mitochondrion / NAD+ nucleotidase, cyclic ADP-ribose generating ...serotonin biosynthetic process / negative regulation of MyD88-independent toll-like receptor signaling pathway / MyD88-independent TLR4 cascade / Toll Like Receptor 3 (TLR3) Cascade / NADP+ nucleosidase activity / NAD catabolic process / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / protein localization to mitochondrion / NAD+ nucleotidase, cyclic ADP-ribose generating / nervous system process / cell fate specification / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / regulation of dendrite morphogenesis / response to axon injury / defense response to fungus / response to glucose / regulation of neuron apoptotic process / signaling adaptor activity / axon cytoplasm / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / small GTPase binding / protein localization / cell-cell signaling / nervous system development / cell body / defense response to Gram-negative bacterium / mitochondrial outer membrane / microtubule / cell differentiation / defense response to bacterium / axon / negative regulation of gene expression / innate immune response / dendrite / synapse / positive regulation of gene expression / protein kinase binding / cell surface / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Sterile alpha and TIR motif-containing protein 1 / TIR domain / SAM domain (Sterile alpha motif) / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. ...Sterile alpha and TIR motif-containing protein 1 / TIR domain / SAM domain (Sterile alpha motif) / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD(+) hydrolase SARM1 / NAD(+) hydrolase tir-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.68 Å
AuthorsIsupov, M.N. / Opatowsky, Y.
Funding support Israel, United States, 3items
OrganizationGrant numberCountry
Israel Science Foundation1425/15 Israel
Israel Science Foundation909/19 Israel
United States - Israel Binational Science Foundation (BSF)2019150 United States
CitationJournal: Cell Rep / Year: 2023
Title: Structure-function analysis of ceTIR-1/hSARM1 explains the lack of Wallerian axonal degeneration in C. elegans.
Authors: Tami Khazma / Atira Grossman / Julia Guez-Haddad / Chengye Feng / Hadas Dabas / Radhika Sain / Michal Weitman / Ran Zalk / Michail N Isupov / Marc Hammarlund / Michael Hons / Yarden Opatowsky /
Abstract: Wallerian axonal degeneration (WD) does not occur in the nematode C. elegans, in contrast to other model animals. However, WD depends on the NADase activity of SARM1, a protein that is also expressed ...Wallerian axonal degeneration (WD) does not occur in the nematode C. elegans, in contrast to other model animals. However, WD depends on the NADase activity of SARM1, a protein that is also expressed in C. elegans (ceSARM/ceTIR-1). We hypothesized that differences in SARM between species might exist and account for the divergence in WD. We first show that expression of the human (h)SARM1, but not ceTIR-1, in C. elegans neurons is sufficient to confer axon degeneration after nerve injury. Next, we determined the cryoelectron microscopy structure of ceTIR-1 and found that, unlike hSARM1, which exists as an auto-inhibited ring octamer, ceTIR-1 forms a readily active 9-mer. Enzymatically, the NADase activity of ceTIR-1 is substantially weaker (10-fold higher Km) than that of hSARM1, and even when fully active, it falls short of consuming all cellular NAD. Our experiments provide insight into the molecular mechanisms and evolution of SARM orthologs and WD across species.
History
DepositionMay 16, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 6, 2023Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
B: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
C: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
D: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
E: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
F: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
G: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
H: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
J: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
I: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
K: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
L: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
M: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
N: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
O: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
P: NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,302,43824
Polymers1,297,13016
Non-polymers5,3078
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area46510 Å2
ΔGint-89 kcal/mol
Surface area211150 Å2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
32A
42C
53A
63D
74A
84E
95A
105F
116A
126G
137A
147H
158B
168C
179B
189D
1910B
2010E
2111B
2211F
2312B
2412G
2513B
2613H
2714C
2814D
2915C
3015E
3116C
3216F
3317C
3417G
3518C
3618H
3719D
3819E
3920D
4020F
4121D
4221G
4322D
4422H
4523E
4623F
4724E
4824G
4925E
5025H
5126F
5226G
5327F
5427H
5528G
5628H
5729J
5829I
5930J
6030K
6131J
6231L
6332J
6432M
6533J
6633N
6734J
6834O
6935J
7035P
7136I
7236K
7337I
7437L
7538I
7638M
7739I
7839N
7940I
8040O
8141I
8241P
8342K
8442L
8543K
8643M
8744K
8844N
8945K
9045O
9146K
9246P
9347L
9447M
9548L
9648N
9749L
9849O
9950L
10050P
10151M
10251N
10352M
10452O
10553M
10653P
10754N
10854O
10955N
11055P
11156O
11256P

NCS domain segments:

Beg auth comp-ID: GLY / Beg label comp-ID: GLY

Dom-IDComponent-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111PROPROAA56 - 55158 - 553
211PROPROBB56 - 55158 - 553
322PROPROAA56 - 55158 - 553
422PROPROCC56 - 55158 - 553
533PROPROAA56 - 55158 - 553
633PROPRODD56 - 55158 - 553
744PROPROAA56 - 55158 - 553
844PROPROEE56 - 55158 - 553
955PROPROAA56 - 55158 - 553
1055PROPROFF56 - 55158 - 553
1166PROPROAA56 - 55158 - 553
1266PROPROGG56 - 55158 - 553
1377PROPROAA56 - 55158 - 553
1477PROPROHH56 - 55158 - 553
1588PROPROBB56 - 55158 - 553
1688PROPROCC56 - 55158 - 553
1799PROPROBB56 - 55158 - 553
1899PROPRODD56 - 55158 - 553
191010PROPROBB56 - 55158 - 553
201010PROPROEE56 - 55158 - 553
211111PROPROBB56 - 55158 - 553
221111PROPROFF56 - 55158 - 553
231212PROPROBB56 - 55158 - 553
241212PROPROGG56 - 55158 - 553
251313PROPROBB56 - 55158 - 553
261313PROPROHH56 - 55158 - 553
271414PROPROCC56 - 55158 - 553
281414PROPRODD56 - 55158 - 553
291515PROPROCC56 - 55158 - 553
301515PROPROEE56 - 55158 - 553
311616PROPROCC56 - 55158 - 553
321616PROPROFF56 - 55158 - 553
331717PROPROCC56 - 55158 - 553
341717PROPROGG56 - 55158 - 553
351818PROPROCC56 - 55158 - 553
361818PROPROHH56 - 55158 - 553
371919PROPRODD56 - 55158 - 553
381919PROPROEE56 - 55158 - 553
392020PROPRODD56 - 55158 - 553
402020PROPROFF56 - 55158 - 553
412121PROPRODD56 - 55158 - 553
422121PROPROGG56 - 55158 - 553
432222PROPRODD56 - 55158 - 553
442222PROPROHH56 - 55158 - 553
452323PROPROEE56 - 55158 - 553
462323PROPROFF56 - 55158 - 553
472424PROPROEE56 - 55158 - 553
482424PROPROGG56 - 55158 - 553
492525PROPROEE56 - 55158 - 553
502525PROPROHH56 - 55158 - 553
512626PROPROFF56 - 55158 - 553
522626PROPROGG56 - 55158 - 553
532727PROPROFF56 - 55158 - 553
542727PROPROHH56 - 55158 - 553
552828PROPROGG56 - 55158 - 553
562828PROPROHH56 - 55158 - 553
572929ASNASNJI705 - 852561 - 708
582929ASNASNIJ705 - 852561 - 708
593030ASNASNJI705 - 852561 - 708
603030ASNASNKK705 - 852561 - 708
613131ASNASNJI705 - 852561 - 708
623131ASNASNLL705 - 852561 - 708
633232ASNASNJI705 - 852561 - 708
643232ASNASNMM705 - 852561 - 708
653333ASNASNJI705 - 852561 - 708
663333ASNASNNN705 - 852561 - 708
673434ASNASNJI705 - 852561 - 708
683434ASNASNOO705 - 852561 - 708
693535ASNASNJI705 - 852561 - 708
703535ASNASNPP705 - 852561 - 708
713636ASNASNIJ705 - 852561 - 708
723636ASNASNKK705 - 852561 - 708
733737ASNASNIJ705 - 852561 - 708
743737ASNASNLL705 - 852561 - 708
753838ASNASNIJ705 - 852561 - 708
763838ASNASNMM705 - 852561 - 708
773939ASNASNIJ705 - 852561 - 708
783939ASNASNNN705 - 852561 - 708
794040ASNASNIJ705 - 852561 - 708
804040ASNASNOO705 - 852561 - 708
814141ASNASNIJ705 - 852561 - 708
824141ASNASNPP705 - 852561 - 708
834242ASNASNKK705 - 852561 - 708
844242ASNASNLL705 - 852561 - 708
854343ASNASNKK705 - 852561 - 708
864343ASNASNMM705 - 852561 - 708
874444ASNASNKK705 - 852561 - 708
884444ASNASNNN705 - 852561 - 708
894545ASNASNKK705 - 852561 - 708
904545ASNASNOO705 - 852561 - 708
914646ASNASNKK705 - 852561 - 708
924646ASNASNPP705 - 852561 - 708
934747ASNASNLL705 - 852561 - 708
944747ASNASNMM705 - 852561 - 708
954848ASNASNLL705 - 852561 - 708
964848ASNASNNN705 - 852561 - 708
974949ASNASNLL705 - 852561 - 708
984949ASNASNOO705 - 852561 - 708
995050ASNASNLL705 - 852561 - 708
1005050ASNASNPP705 - 852561 - 708
1015151ASNASNMM705 - 852561 - 708
1025151ASNASNNN705 - 852561 - 708
1035252ASNASNMM705 - 852561 - 708
1045252ASNASNOO705 - 852561 - 708
1055353ASNASNMM705 - 852561 - 708
1065353ASNASNPP705 - 852561 - 708
1075454ASNASNNN705 - 852561 - 708
1085454ASNASNOO705 - 852561 - 708
1095555ASNASNNN705 - 852561 - 708
1105555ASNASNPP705 - 852561 - 708
1115656ASNASNOO705 - 852561 - 708
1125656ASNASNPP705 - 852561 - 708

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
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42
22Local NCS retraints between domains: 43 44
23Local NCS retraints between domains: 45 46
24Local NCS retraints between domains: 47 48
25Local NCS retraints between domains: 49 50
26Local NCS retraints between domains: 51 52
27Local NCS retraints between domains: 53 54
28Local NCS retraints between domains: 55 56
29Local NCS retraints between domains: 57 58
30Local NCS retraints between domains: 59 60
31Local NCS retraints between domains: 61 62
32Local NCS retraints between domains: 63 64
33Local NCS retraints between domains: 65 66
34Local NCS retraints between domains: 67 68
35Local NCS retraints between domains: 69 70
36Local NCS retraints between domains: 71 72
37Local NCS retraints between domains: 73 74
38Local NCS retraints between domains: 75 76
39Local NCS retraints between domains: 77 78
40Local NCS retraints between domains: 79 80
41Local NCS retraints between domains: 81 82
42Local NCS retraints between domains: 83 84
43Local NCS retraints between domains: 85 86
44Local NCS retraints between domains: 87 88
45Local NCS retraints between domains: 89 90
46Local NCS retraints between domains: 91 92
47Local NCS retraints between domains: 93 94
48Local NCS retraints between domains: 95 96
49Local NCS retraints between domains: 97 98
50Local NCS retraints between domains: 99 100
51Local NCS retraints between domains: 101 102
52Local NCS retraints between domains: 103 104
53Local NCS retraints between domains: 105 106
54Local NCS retraints between domains: 107 108
55Local NCS retraints between domains: 109 110
56Local NCS retraints between domains: 111 112

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Components

#1: Protein
NAD(+) hydrolase SARM1,NAD(+) hydrolase tir-1 / NADase SARM1 / hSARM1 / NADP(+) hydrolase SARM1 / Sterile alpha and Armadillo repeat protein / ...NADase SARM1 / hSARM1 / NADP(+) hydrolase SARM1 / Sterile alpha and Armadillo repeat protein / Sterile alpha and TIR motif-containing protein 1 / Sterile alpha motif domain-containing protein 2 / MyD88-5 / SAM domain-containing protein 2 / Tir-1 homolog / HsTIR / NADase tir-1 / Neuronal symmetry protein 2 / SARM1 homolog / Sterile alpha and TIR motif-containing protein tir-1


Mass: 81070.656 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SARM1, KIAA0524, SAMD2, SARM, tir-1, nsy-2, F13B10.1 / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
References: UniProt: Q6SZW1, UniProt: Q86DA5, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds
#2: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE


Mass: 663.425 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: NAD*YM
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: A CHIMERA construct containing human SARM1 ARM and SAM domains and C. elegans TIR domain.
Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human) / Cell: HEK293F
Buffer solutionpH: 8.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid type: Quantifoil R1.2/1.3
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 41.4 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)
EM imaging opticsEnergyfilter name: GIF Quantum LS

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Processing

SoftwareName: REFMAC / Version: 5.8.0267 / Classification: refinement
EM software
IDNameVersionCategory
2EPUimage acquisition
7Coot9.6model fitting
9REFMAC5model refinement
10UCSF ChimeraXmodel refinement
11ISOLDEmodel refinement
12cryoSPARCinitial Euler assignment
13cryoSPARCfinal Euler assignment
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 298564
3D reconstructionResolution: 2.68 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 136346 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: RECIPROCAL
Atomic model building
ID 3D fitting-IDAccession codeChain residue rangeDetailsSource nameType
117ANW26-560The initial octameric model containing human ARM and SAM domainsOtherexperimental model
21561-708AlphaFoldin silico model
RefinementResolution: 2.68→252 Å / Cor.coef. Fo:Fc: 0.82 / WRfactor Rwork: 0.456 / Average fsc overall: 0.4533 / Average fsc work: 0.4533 / ESU R: 0.196 / Details: Hydrogens have not been used
RfactorNum. reflection% reflection
Rwork0.456 1740894 -
all0.456 --
Rfree--0 %
obs--100 %
Solvent computationSolvent model: BABINET MODEL
Displacement parametersBiso mean: 39.983 Å2
Baniso -1Baniso -2Baniso -3
1--1.02 Å2-0.005 Å20 Å2
2---1.025 Å20.004 Å2
3---2.045 Å2
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0070.01241472
ELECTRON MICROSCOPYr_angle_refined_deg1.6491.63256144
ELECTRON MICROSCOPYr_dihedral_angle_1_deg6.47155136
ELECTRON MICROSCOPYr_dihedral_angle_2_deg28.38521.12328
ELECTRON MICROSCOPYr_dihedral_angle_3_deg13.132157360
ELECTRON MICROSCOPYr_dihedral_angle_4_deg19.98115408
ELECTRON MICROSCOPYr_chiral_restr0.1280.25312
ELECTRON MICROSCOPYr_gen_planes_refined0.0080.0231072
ELECTRON MICROSCOPYr_nbd_refined0.2050.236706
ELECTRON MICROSCOPYr_nbtor_refined0.2930.257962
ELECTRON MICROSCOPYr_xyhbond_nbd_refined0.070.22314
ELECTRON MICROSCOPYr_mcbond_it0420592
ELECTRON MICROSCOPYr_mcangle_it0625712
ELECTRON MICROSCOPYr_scbond_it0420880
ELECTRON MICROSCOPYr_scangle_it0630432
ELECTRON MICROSCOPYr_lrange_it075.943171628
ELECTRON MICROSCOPYr_ncsr_local_group_10.0120.0532888
ELECTRON MICROSCOPYr_ncsr_local_group_20.0030.0532920
ELECTRON MICROSCOPYr_ncsr_local_group_30.0130.0532882
ELECTRON MICROSCOPYr_ncsr_local_group_40.0010.0532920
ELECTRON MICROSCOPYr_ncsr_local_group_50.0120.0532874
ELECTRON MICROSCOPYr_ncsr_local_group_60.0030.0532916
ELECTRON MICROSCOPYr_ncsr_local_group_70.0130.0532864
ELECTRON MICROSCOPYr_ncsr_local_group_80.0120.0532882
ELECTRON MICROSCOPYr_ncsr_local_group_90.0050.0532922
ELECTRON MICROSCOPYr_ncsr_local_group_100.0120.0532886
ELECTRON MICROSCOPYr_ncsr_local_group_110.0040.0532926
ELECTRON MICROSCOPYr_ncsr_local_group_120.0120.0532876
ELECTRON MICROSCOPYr_ncsr_local_group_130.0050.0532904
ELECTRON MICROSCOPYr_ncsr_local_group_140.0130.0532876
ELECTRON MICROSCOPYr_ncsr_local_group_150.0030.0532914
ELECTRON MICROSCOPYr_ncsr_local_group_160.0130.0532882
ELECTRON MICROSCOPYr_ncsr_local_group_170.0040.0532922
ELECTRON MICROSCOPYr_ncsr_local_group_180.0130.0532860
ELECTRON MICROSCOPYr_ncsr_local_group_190.0120.0532882
ELECTRON MICROSCOPYr_ncsr_local_group_200.0060.0532914
ELECTRON MICROSCOPYr_ncsr_local_group_210.0130.0532878
ELECTRON MICROSCOPYr_ncsr_local_group_220.0090.0532912
ELECTRON MICROSCOPYr_ncsr_local_group_230.0120.0532872
ELECTRON MICROSCOPYr_ncsr_local_group_240.0030.0532906
ELECTRON MICROSCOPYr_ncsr_local_group_250.0130.0532858
ELECTRON MICROSCOPYr_ncsr_local_group_260.0130.0532876
ELECTRON MICROSCOPYr_ncsr_local_group_270.0060.0532904
ELECTRON MICROSCOPYr_ncsr_local_group_280.0130.0532868
ELECTRON MICROSCOPYr_ncsr_local_group_290.0020.059878
ELECTRON MICROSCOPYr_ncsr_local_group_300.0180.059856
ELECTRON MICROSCOPYr_ncsr_local_group_310.0030.059870
ELECTRON MICROSCOPYr_ncsr_local_group_320.0030.059898
ELECTRON MICROSCOPYr_ncsr_local_group_330.0030.059876
ELECTRON MICROSCOPYr_ncsr_local_group_340.0170.059858
ELECTRON MICROSCOPYr_ncsr_local_group_350.0030.059876
ELECTRON MICROSCOPYr_ncsr_local_group_360.0170.059838
ELECTRON MICROSCOPYr_ncsr_local_group_370.0030.059896
ELECTRON MICROSCOPYr_ncsr_local_group_380.0030.059882
ELECTRON MICROSCOPYr_ncsr_local_group_390.0020.059898
ELECTRON MICROSCOPYr_ncsr_local_group_400.0170.059840
ELECTRON MICROSCOPYr_ncsr_local_group_410.0030.059906
ELECTRON MICROSCOPYr_ncsr_local_group_420.0170.059838
ELECTRON MICROSCOPYr_ncsr_local_group_430.0180.059868
ELECTRON MICROSCOPYr_ncsr_local_group_440.0170.059838
ELECTRON MICROSCOPYr_ncsr_local_group_450.0050.059912
ELECTRON MICROSCOPYr_ncsr_local_group_460.0170.059840
ELECTRON MICROSCOPYr_ncsr_local_group_470.0010.059878
ELECTRON MICROSCOPYr_ncsr_local_group_480.0030.059898
ELECTRON MICROSCOPYr_ncsr_local_group_490.0180.059838
ELECTRON MICROSCOPYr_ncsr_local_group_500.0030.059902
ELECTRON MICROSCOPYr_ncsr_local_group_510.0030.059876
ELECTRON MICROSCOPYr_ncsr_local_group_520.0170.059872
ELECTRON MICROSCOPYr_ncsr_local_group_530.0030.059882
ELECTRON MICROSCOPYr_ncsr_local_group_540.0170.059840
ELECTRON MICROSCOPYr_ncsr_local_group_550.0020.059906
ELECTRON MICROSCOPYr_ncsr_local_group_560.0170.059842
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AELECTRON MICROSCOPYLocal ncs0.011770.05013
12BELECTRON MICROSCOPYLocal ncs0.011770.05013
23AELECTRON MICROSCOPYLocal ncs0.002930.05013
24CELECTRON MICROSCOPYLocal ncs0.002930.05013
35AELECTRON MICROSCOPYLocal ncs0.012580.05013
36DELECTRON MICROSCOPYLocal ncs0.012580.05013
47AELECTRON MICROSCOPYLocal ncs0.001260.05013
48EELECTRON MICROSCOPYLocal ncs0.001260.05013
59AELECTRON MICROSCOPYLocal ncs0.012210.05013
510FELECTRON MICROSCOPYLocal ncs0.012210.05013
611AELECTRON MICROSCOPYLocal ncs0.002850.05013
612GELECTRON MICROSCOPYLocal ncs0.002850.05013
713AELECTRON MICROSCOPYLocal ncs0.012780.05013
714HELECTRON MICROSCOPYLocal ncs0.012780.05013
815BELECTRON MICROSCOPYLocal ncs0.012150.05013
816CELECTRON MICROSCOPYLocal ncs0.012150.05013
917BELECTRON MICROSCOPYLocal ncs0.005250.05013
918DELECTRON MICROSCOPYLocal ncs0.005250.05013
1019BELECTRON MICROSCOPYLocal ncs0.01190.05013
1020EELECTRON MICROSCOPYLocal ncs0.01190.05013
1121BELECTRON MICROSCOPYLocal ncs0.004090.05013
1122FELECTRON MICROSCOPYLocal ncs0.004090.05013
1223BELECTRON MICROSCOPYLocal ncs0.012050.05013
1224GELECTRON MICROSCOPYLocal ncs0.012050.05013
1325BELECTRON MICROSCOPYLocal ncs0.005090.05013
1326HELECTRON MICROSCOPYLocal ncs0.005090.05013
1427CELECTRON MICROSCOPYLocal ncs0.012540.05013
1428DELECTRON MICROSCOPYLocal ncs0.012540.05013
1529CELECTRON MICROSCOPYLocal ncs0.003240.05013
1530EELECTRON MICROSCOPYLocal ncs0.003240.05013
1631CELECTRON MICROSCOPYLocal ncs0.012540.05013
1632FELECTRON MICROSCOPYLocal ncs0.012540.05013
1733CELECTRON MICROSCOPYLocal ncs0.00390.05013
1734GELECTRON MICROSCOPYLocal ncs0.00390.05013
1835CELECTRON MICROSCOPYLocal ncs0.013010.05013
1836HELECTRON MICROSCOPYLocal ncs0.013010.05013
1937DELECTRON MICROSCOPYLocal ncs0.012430.05013
1938EELECTRON MICROSCOPYLocal ncs0.012430.05013
2039DELECTRON MICROSCOPYLocal ncs0.006310.05013
2040FELECTRON MICROSCOPYLocal ncs0.006310.05013
2141DELECTRON MICROSCOPYLocal ncs0.013070.05013
2142GELECTRON MICROSCOPYLocal ncs0.013070.05013
2243DELECTRON MICROSCOPYLocal ncs0.008580.05013
2244HELECTRON MICROSCOPYLocal ncs0.008580.05013
2345EELECTRON MICROSCOPYLocal ncs0.012270.05013
2346FELECTRON MICROSCOPYLocal ncs0.012270.05013
2447EELECTRON MICROSCOPYLocal ncs0.003080.05013
2448GELECTRON MICROSCOPYLocal ncs0.003080.05013
2549EELECTRON MICROSCOPYLocal ncs0.0130.05013
2550HELECTRON MICROSCOPYLocal ncs0.0130.05013
2651FELECTRON MICROSCOPYLocal ncs0.01250.05013
2652GELECTRON MICROSCOPYLocal ncs0.01250.05013
2753FELECTRON MICROSCOPYLocal ncs0.006280.05013
2754HELECTRON MICROSCOPYLocal ncs0.006280.05013
2855GELECTRON MICROSCOPYLocal ncs0.012660.05013
2856HELECTRON MICROSCOPYLocal ncs0.012660.05013
2957JELECTRON MICROSCOPYLocal ncs0.002350.05011
2958IELECTRON MICROSCOPYLocal ncs0.002350.05011
3059JELECTRON MICROSCOPYLocal ncs0.017890.05011
3060KELECTRON MICROSCOPYLocal ncs0.017890.05011
3161JELECTRON MICROSCOPYLocal ncs0.003450.05011
3162LELECTRON MICROSCOPYLocal ncs0.003450.05011
3263JELECTRON MICROSCOPYLocal ncs0.003140.05011
3264MELECTRON MICROSCOPYLocal ncs0.003140.05011
3365JELECTRON MICROSCOPYLocal ncs0.003110.05011
3366NELECTRON MICROSCOPYLocal ncs0.003110.05011
3467JELECTRON MICROSCOPYLocal ncs0.017460.05011
3468OELECTRON MICROSCOPYLocal ncs0.017460.05011
3569JELECTRON MICROSCOPYLocal ncs0.003250.05011
3570PELECTRON MICROSCOPYLocal ncs0.003250.05011
3671IELECTRON MICROSCOPYLocal ncs0.017230.05011
3672KELECTRON MICROSCOPYLocal ncs0.017230.05011
3773IELECTRON MICROSCOPYLocal ncs0.002960.05011
3774LELECTRON MICROSCOPYLocal ncs0.002960.05011
3875IELECTRON MICROSCOPYLocal ncs0.002740.05011
3876MELECTRON MICROSCOPYLocal ncs0.002740.05011
3977IELECTRON MICROSCOPYLocal ncs0.002490.05011
3978NELECTRON MICROSCOPYLocal ncs0.002490.05011
4079IELECTRON MICROSCOPYLocal ncs0.017380.05011
4080OELECTRON MICROSCOPYLocal ncs0.017380.05011
4181IELECTRON MICROSCOPYLocal ncs0.00280.05011
4182PELECTRON MICROSCOPYLocal ncs0.00280.05011
4283KELECTRON MICROSCOPYLocal ncs0.017450.05011
4284LELECTRON MICROSCOPYLocal ncs0.017450.05011
4385KELECTRON MICROSCOPYLocal ncs0.0180.05011
4386MELECTRON MICROSCOPYLocal ncs0.0180.05011
4487KELECTRON MICROSCOPYLocal ncs0.017340.05011
4488NELECTRON MICROSCOPYLocal ncs0.017340.05011
4589KELECTRON MICROSCOPYLocal ncs0.005240.05011
4590OELECTRON MICROSCOPYLocal ncs0.005240.05011
4691KELECTRON MICROSCOPYLocal ncs0.017380.05011
4692PELECTRON MICROSCOPYLocal ncs0.017380.05011
4793LELECTRON MICROSCOPYLocal ncs0.001370.05011
4794MELECTRON MICROSCOPYLocal ncs0.001370.05011
4895LELECTRON MICROSCOPYLocal ncs0.002880.05011
4896NELECTRON MICROSCOPYLocal ncs0.002880.05011
4997LELECTRON MICROSCOPYLocal ncs0.01750.05011
4998OELECTRON MICROSCOPYLocal ncs0.01750.05011
5099LELECTRON MICROSCOPYLocal ncs0.003150.05011
50100PELECTRON MICROSCOPYLocal ncs0.003150.05011
51101MELECTRON MICROSCOPYLocal ncs0.002840.05011
51102NELECTRON MICROSCOPYLocal ncs0.002840.05011
52103MELECTRON MICROSCOPYLocal ncs0.017430.05011
52104OELECTRON MICROSCOPYLocal ncs0.017430.05011
53105MELECTRON MICROSCOPYLocal ncs0.003160.05011
53106PELECTRON MICROSCOPYLocal ncs0.003160.05011
54107NELECTRON MICROSCOPYLocal ncs0.017390.05011
54108OELECTRON MICROSCOPYLocal ncs0.017390.05011
55109NELECTRON MICROSCOPYLocal ncs0.001560.05011
55110PELECTRON MICROSCOPYLocal ncs0.001560.05011
56111OELECTRON MICROSCOPYLocal ncs0.017440.05011
56112PELECTRON MICROSCOPYLocal ncs0.017440.05011
LS refinement shell

Refine-ID: ELECTRON MICROSCOPY / Num. reflection Rfree: _ / Total num. of bins used: 20 / % reflection obs: 100 %

Resolution (Å)Rfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc workWRfactor Rwork
2.68-2.751.1391288131.1391288130.0981.139
2.75-2.8250.9841254520.9841254520.1150.984
2.825-2.9070.6841222090.6841222090.190.684
2.907-2.9960.6351192220.6351192220.2060.635
2.996-3.0950.5991141810.5991141810.2720.599
3.095-3.2030.5511113650.5511113650.3230.551
3.203-3.3240.5151071410.5151071410.4130.515
3.324-3.460.4841035010.4841035010.5240.484
3.46-3.6140.471986710.471986710.5730.471
3.614-3.790.468950210.468950210.6180.468
3.79-3.9950.464898440.464898440.6650.464
3.995-4.2370.462853370.462853370.6820.462
4.237-4.530.451796940.451796940.6980.451
4.53-4.8930.444745120.444745120.6890.444
4.893-5.3590.439687050.439687050.7040.439
5.359-5.9920.429622170.429622170.6780.429
5.992-6.9180.44544080.44544080.6910.44
6.918-8.4710.428462520.428462520.7310.428
8.471-11.9730.375357200.375357200.8320.375
11.973-2520.406195540.406195540.8940.406

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