PDB-8hcj: Structure of GH43 family enzyme, Xylan 1, 4 Beta- xylosidase from...

ID or keywords:

Entry

Database: PDB / ID: 8hcj

Title

Structure of GH43 family enzyme, Xylan 1, 4 Beta- xylosidase from pseudopedobacter saltans

Components

Xylan 1,4-beta-xylosidase

Keywords

HYDROLASE / GH43 family / Xylan / Xylosidase

Function / homology

Function and homology information

xylan 1,4-beta-xylosidase / xylan 1,4-beta-xylosidase activity / xylan catabolic process / carbohydrate binding / metal ion binding
Similarity search - Function

Biological species

Pseudopedobacter saltans DSM 12145 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.566 Å

Authors

Vishwakarma, P. / Sachdeva, E. / Goyal, A. / Ethayathulla, A.S. / Das, U. / Kaur, P.

Funding support

India, 1items

Citation

Journal: Int.J.Biol.Macromol. / Year: 2024
Title: Deciphering the structural and biochemical aspects of xylosidase from Pseudopedobacter saltans.
Authors: Vishwakarma, P. / Sachdeva, E. / Thakur, A. / Ethayathulla, A.S. / Goyal, A. / Kaur, P.

History

Deposition	Nov 1, 2022	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Nov 15, 2023	Provider: repository / Type: Initial release
Revision 1.1	Jan 15, 2025	Group: Database references / Structure summary / Category: citation / citation_author / pdbx_entry_details Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name / _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	8hcj_validation.pdf.gz	6.5 MB	Display	wwPDB validaton report
Full document	8hcj_full_validation.pdf.gz	6.5 MB	Display
Data in XML	8hcj_validation.xml.gz	127 KB	Display
Data in CIF	8hcj_validation.cif.gz	180.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/hc/8hcj ftp://data.pdbj.org/pub/pdb/validation_reports/hc/8hcj	HTTPS FTP

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Related structure data

Related structure data	4novS S: Starting model for refinement
Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

D: Xylan 1,4-beta-xylosidase

E: Xylan 1,4-beta-xylosidase

H: Xylan 1,4-beta-xylosidase

A: Xylan 1,4-beta-xylosidase

B: Xylan 1,4-beta-xylosidase

G: Xylan 1,4-beta-xylosidase

C: Xylan 1,4-beta-xylosidase

F: Xylan 1,4-beta-xylosidase

hetero molecules

407 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

D: Xylan 1,4-beta-xylosidase

A: Xylan 1,4-beta-xylosidase

B: Xylan 1,4-beta-xylosidase

C: Xylan 1,4-beta-xylosidase

hetero molecules

defined by author
Evidence: gel filtration
204 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: Xylan 1,4-beta-xylosidase

H: Xylan 1,4-beta-xylosidase

G: Xylan 1,4-beta-xylosidase

F: Xylan 1,4-beta-xylosidase

hetero molecules

defined by author
204 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	73.340, 89.662, 138.437
Angle α, β, γ (deg.)	102.734, 93.985, 98.237
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Auth asym-ID: D / Label asym-ID: A

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth seq-ID	Label seq-ID
1	1	1	MET	MET	LYS	LYS	21 - 453	21 - 453
2	1	1	MET	MET	LYS	LYS	21 - 453	21 - 453
3	2	2	MET	MET	LYS	LYS	21 - 453	21 - 453
4	2	2	MET	MET	LYS	LYS	21 - 453	21 - 453
5	3	3	MET	MET	LYS	LYS	21 - 453	21 - 453
6	3	3	MET	MET	LYS	LYS	21 - 453	21 - 453
7	4	4	MET	MET	LYS	LYS	21 - 453	21 - 453
8	4	4	MET	MET	LYS	LYS	21 - 453	21 - 453
9	5	5	GLN	GLN	SER	SER	22 - 452	22 - 452
10	5	5	GLN	GLN	SER	SER	22 - 452	22 - 452
11	6	6	GLN	GLN	SER	SER	22 - 452	22 - 452
12	6	6	GLN	GLN	SER	SER	22 - 452	22 - 452
13	7	7	GLN	GLN	SER	SER	22 - 452	22 - 452
14	7	7	GLN	GLN	SER	SER	22 - 452	22 - 452
15	8	8	MET	MET	LYS	LYS	21 - 453	21 - 453
16	8	8	MET	MET	LYS	LYS	21 - 453	21 - 453
17	9	9	MET	MET	LYS	LYS	21 - 453	21 - 453
18	9	9	MET	MET	LYS	LYS	21 - 453	21 - 453
19	10	10	MET	MET	LYS	LYS	21 - 453	21 - 453
20	10	10	MET	MET	LYS	LYS	21 - 453	21 - 453
21	11	11	GLN	GLN	SER	SER	22 - 452	22 - 452
22	11	11	GLN	GLN	SER	SER	22 - 452	22 - 452
23	12	12	GLN	GLN	SER	SER	22 - 452	22 - 452
24	12	12	GLN	GLN	SER	SER	22 - 452	22 - 452
25	13	13	GLN	GLN	SER	SER	22 - 452	22 - 452
26	13	13	GLN	GLN	SER	SER	22 - 452	22 - 452
27	14	14	MET	MET	LYS	LYS	21 - 453	21 - 453
28	14	14	MET	MET	LYS	LYS	21 - 453	21 - 453
29	15	15	MET	MET	LYS	LYS	21 - 453	21 - 453
30	15	15	MET	MET	LYS	LYS	21 - 453	21 - 453
31	16	16	GLN	GLN	SER	SER	22 - 452	22 - 452
32	16	16	GLN	GLN	SER	SER	22 - 452	22 - 452
33	17	17	GLN	GLN	SER	SER	22 - 452	22 - 452
34	17	17	GLN	GLN	SER	SER	22 - 452	22 - 452
35	18	18	GLN	GLN	SER	SER	22 - 452	22 - 452
36	18	18	GLN	GLN	SER	SER	22 - 452	22 - 452
37	19	19	MET	MET	LYS	LYS	21 - 453	21 - 453
38	19	19	MET	MET	LYS	LYS	21 - 453	21 - 453
39	20	20	GLN	GLN	SER	SER	22 - 452	22 - 452
40	20	20	GLN	GLN	SER	SER	22 - 452	22 - 452
41	21	21	GLN	GLN	SER	SER	22 - 452	22 - 452
42	21	21	GLN	GLN	SER	SER	22 - 452	22 - 452
43	22	22	GLN	GLN	SER	SER	22 - 452	22 - 452
44	22	22	GLN	GLN	SER	SER	22 - 452	22 - 452
45	23	23	GLN	GLN	SER	SER	22 - 452	22 - 452
46	23	23	GLN	GLN	SER	SER	22 - 452	22 - 452
47	24	24	GLN	GLN	SER	SER	22 - 452	22 - 452
48	24	24	GLN	GLN	SER	SER	22 - 452	22 - 452
49	25	25	GLN	GLN	SER	SER	22 - 452	22 - 452
50	25	25	GLN	GLN	SER	SER	22 - 452	22 - 452
51	26	26	GLN	GLN	LYS	LYS	22 - 453	22 - 453
52	26	26	GLN	GLN	LYS	LYS	22 - 453	22 - 453
53	27	27	GLN	GLN	LYS	LYS	22 - 453	22 - 453
54	27	27	GLN	GLN	LYS	LYS	22 - 453	22 - 453
55	28	28	GLN	GLN	LYS	LYS	22 - 453	22 - 453
56	28	28	GLN	GLN	LYS	LYS	22 - 453	22 - 453

NCS ensembles :

ID	Details
1	Local NCS retraints between domains: 1 2
2	Local NCS retraints between domains: 3 4
3	Local NCS retraints between domains: 5 6
4	Local NCS retraints between domains: 7 8
5	Local NCS retraints between domains: 9 10
6	Local NCS retraints between domains: 11 12
7	Local NCS retraints between domains: 13 14
8	Local NCS retraints between domains: 15 16
9	Local NCS retraints between domains: 17 18
10	Local NCS retraints between domains: 19 20
11	Local NCS retraints between domains: 21 22
12	Local NCS retraints between domains: 23 24
13	Local NCS retraints between domains: 25 26
14	Local NCS retraints between domains: 27 28
15	Local NCS retraints between domains: 29 30
16	Local NCS retraints between domains: 31 32
17	Local NCS retraints between domains: 33 34
18	Local NCS retraints between domains: 35 36
19	Local NCS retraints between domains: 37 38
20	Local NCS retraints between domains: 39 40
21	Local NCS retraints between domains: 41 42
22	Local NCS retraints between domains: 43 44
23	Local NCS retraints between domains: 45 46
24	Local NCS retraints between domains: 47 48
25	Local NCS retraints between domains: 49 50
26	Local NCS retraints between domains: 51 52
27	Local NCS retraints between domains: 53 54
28	Local NCS retraints between domains: 55 56

#1: Protein	Xylan 1,4-beta-xylosidase Mass: 50813.023 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudopedobacter saltans DSM 12145 (bacteria) Strain: ATCC 51119 / DSM 12145 / JCM 21818 / CCUG 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643 Gene: Pedsa_2569 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: F0S5E9, xylan 1,4-beta-xylosidase
#2: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1325 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y
Has protein modification	N

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.14 Å³/Da / Density % sol: 42 %
Crystal grow	Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 18% PEG 3350, 5% PROPANOL, 0.15M IMIDAZOLE

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Data collection

Diffraction	Mean temperature: 273 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.96546 Å
Detector	Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Jul 6, 2022
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.96546 Å / Relative weight: 1
Reflection	Resolution: 2.5→134.29 Å / Num. obs: 103346 / % possible obs: 95 % / Redundancy: 1.92 % / B_iso Wilson estimate: 30.2 Å² / CC_1/2: 0.94 / R_merge(I) obs: 0.08 / R_pim(I) all: 0.07 / R_rim(I) all: 0.1 / Net I/σ(I): 0.04
Reflection shell	Resolution: 2.5→2.56 Å / Redundancy: 2.01 % / R_merge(I) obs: 0.02 / Num. unique obs: 5300 / CC_1/2: 0.93 / R_pim(I) all: 0.19 / R_rim(I) all: 0.28 / % possible all: 97

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0352	refinement
Coot		model building
iMOSFLM		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4NOV

4nov

Resolution: 2.566→134.29 Å / Cor.coef. F_o:F_c: 0.95 / Cor.coef. F_o:F_c free: 0.917 / WR_factor R_free: 0.234 / WR_factor R_work: 0.182 / SU B: 10.212 / SU ML: 0.218 / Average fsc free: 0.9701 / Average fsc work: 0.9826 / Cross valid method: FREE R-VALUE / ESU R Free: 0.3 / Details: Hydrogens have not been used

	R_factor	Num. reflection	% reflection
R_free	0.2091	5180	5.012 %
R_work	0.1634	98163	-
all	0.166	-	-
obs	-	103343	95.375 %

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT

Displacement parameters

B_iso mean: 33.093 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.558 Å²	1.763 Å²	0.582 Å²
2-	-	-0.804 Å²	0.843 Å²
3-	-	-	-2.466 Å²

Refinement step

Cycle: LAST / Resolution: 2.566→134.29 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	27430	0	16	1325	28771

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.011	0.011	28254
X-RAY DIFFRACTION	r_angle_refined_deg	1.494	1.648	38367
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.808	5	3453
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	4.871	5	88
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.327	10	4503
X-RAY DIFFRACTION	r_dihedral_angle_6_deg	17.669	10	1311
X-RAY DIFFRACTION	r_chiral_restr	0.086	0.2	3925
X-RAY DIFFRACTION	r_gen_planes_refined	0.009	0.02	21888
X-RAY DIFFRACTION	r_nbd_refined	0.206	0.2	12632
X-RAY DIFFRACTION	r_nbtor_refined	0.319	0.2	19274
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.164	0.2	1490
X-RAY DIFFRACTION	r_metal_ion_refined	0.181	0.2	43
X-RAY DIFFRACTION	r_symmetry_nbd_refined	0.199	0.2	73
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_refined	0.187	0.2	13
X-RAY DIFFRACTION	r_mcbond_it	4.519	3.225	13836
X-RAY DIFFRACTION	r_mcangle_it	6.384	4.824	17281
X-RAY DIFFRACTION	r_scbond_it	5.791	3.358	14418
X-RAY DIFFRACTION	r_scangle_it	7.745	4.911	21086
X-RAY DIFFRACTION	r_lrange_it	10.506	61.295	122532
X-RAY DIFFRACTION	r_ncsr_local_group_1	0.118	0.05	14111
X-RAY DIFFRACTION	r_ncsr_local_group_2	0.12	0.05	14096
X-RAY DIFFRACTION	r_ncsr_local_group_3	0.121	0.05	14029
X-RAY DIFFRACTION	r_ncsr_local_group_4	0.121	0.05	14019
X-RAY DIFFRACTION	r_ncsr_local_group_5	0.121	0.05	13867
X-RAY DIFFRACTION	r_ncsr_local_group_6	0.123	0.05	14048
X-RAY DIFFRACTION	r_ncsr_local_group_7	0.12	0.05	14008
X-RAY DIFFRACTION	r_ncsr_local_group_8	0.111	0.05	14208
X-RAY DIFFRACTION	r_ncsr_local_group_9	0.123	0.05	13967
X-RAY DIFFRACTION	r_ncsr_local_group_10	0.118	0.05	14040
X-RAY DIFFRACTION	r_ncsr_local_group_11	0.122	0.05	13920
X-RAY DIFFRACTION	r_ncsr_local_group_12	0.118	0.05	14054
X-RAY DIFFRACTION	r_ncsr_local_group_13	0.124	0.05	13952
X-RAY DIFFRACTION	r_ncsr_local_group_14	0.124	0.05	14016
X-RAY DIFFRACTION	r_ncsr_local_group_15	0.115	0.05	14113
X-RAY DIFFRACTION	r_ncsr_local_group_16	0.12	0.05	13911
X-RAY DIFFRACTION	r_ncsr_local_group_17	0.113	0.05	14157
X-RAY DIFFRACTION	r_ncsr_local_group_18	0.126	0.05	14011
X-RAY DIFFRACTION	r_ncsr_local_group_19	0.123	0.05	14020
X-RAY DIFFRACTION	r_ncsr_local_group_20	0.124	0.05	13847
X-RAY DIFFRACTION	r_ncsr_local_group_21	0.123	0.05	13959
X-RAY DIFFRACTION	r_ncsr_local_group_22	0.124	0.05	13978
X-RAY DIFFRACTION	r_ncsr_local_group_23	0.126	0.05	13889
X-RAY DIFFRACTION	r_ncsr_local_group_24	0.118	0.05	14037
X-RAY DIFFRACTION	r_ncsr_local_group_25	0.124	0.05	14026
X-RAY DIFFRACTION	r_ncsr_local_group_26	0.123	0.05	13932
X-RAY DIFFRACTION	r_ncsr_local_group_27	0.125	0.05	13921
X-RAY DIFFRACTION	r_ncsr_local_group_28	0.123	0.05	14067

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Refine-ID	Type	Rms dev position (Å)	Weight position
1	1	D	X-RAY DIFFRACTION	Local ncs	0.11792	0.05008
1	2	D	X-RAY DIFFRACTION	Local ncs	0.11792	0.05008
2	3	D	X-RAY DIFFRACTION	Local ncs	0.12034	0.05008
2	4	D	X-RAY DIFFRACTION	Local ncs	0.12034	0.05008
3	5	D	X-RAY DIFFRACTION	Local ncs	0.12145	0.05008
3	6	D	X-RAY DIFFRACTION	Local ncs	0.12145	0.05008
4	7	D	X-RAY DIFFRACTION	Local ncs	0.12145	0.05008
4	8	D	X-RAY DIFFRACTION	Local ncs	0.12145	0.05008
5	9	D	X-RAY DIFFRACTION	Local ncs	0.12099	0.05008
5	10	D	X-RAY DIFFRACTION	Local ncs	0.12099	0.05008
6	11	D	X-RAY DIFFRACTION	Local ncs	0.12274	0.05008
6	12	D	X-RAY DIFFRACTION	Local ncs	0.12274	0.05008
7	13	D	X-RAY DIFFRACTION	Local ncs	0.11984	0.05009
7	14	D	X-RAY DIFFRACTION	Local ncs	0.11984	0.05009
8	15	D	X-RAY DIFFRACTION	Local ncs	0.11097	0.05009
8	16	D	X-RAY DIFFRACTION	Local ncs	0.11097	0.05009
9	17	D	X-RAY DIFFRACTION	Local ncs	0.12341	0.05008
9	18	D	X-RAY DIFFRACTION	Local ncs	0.12341	0.05008
10	19	D	X-RAY DIFFRACTION	Local ncs	0.11798	0.05008
10	20	D	X-RAY DIFFRACTION	Local ncs	0.11798	0.05008
11	21	D	X-RAY DIFFRACTION	Local ncs	0.12177	0.05008
11	22	D	X-RAY DIFFRACTION	Local ncs	0.12177	0.05008
12	23	D	X-RAY DIFFRACTION	Local ncs	0.11836	0.05008
12	24	D	X-RAY DIFFRACTION	Local ncs	0.11836	0.05008
13	25	D	X-RAY DIFFRACTION	Local ncs	0.12385	0.05008
13	26	D	X-RAY DIFFRACTION	Local ncs	0.12385	0.05008
14	27	D	X-RAY DIFFRACTION	Local ncs	0.12419	0.05008
14	28	D	X-RAY DIFFRACTION	Local ncs	0.12419	0.05008
15	29	D	X-RAY DIFFRACTION	Local ncs	0.11493	0.05008
15	30	D	X-RAY DIFFRACTION	Local ncs	0.11493	0.05008
16	31	D	X-RAY DIFFRACTION	Local ncs	0.12014	0.05008
16	32	D	X-RAY DIFFRACTION	Local ncs	0.12014	0.05008
17	33	D	X-RAY DIFFRACTION	Local ncs	0.11261	0.05009
17	34	D	X-RAY DIFFRACTION	Local ncs	0.11261	0.05009
18	35	D	X-RAY DIFFRACTION	Local ncs	0.12622	0.05008
18	36	D	X-RAY DIFFRACTION	Local ncs	0.12622	0.05008
19	37	D	X-RAY DIFFRACTION	Local ncs	0.12298	0.05008
19	38	D	X-RAY DIFFRACTION	Local ncs	0.12298	0.05008
20	39	D	X-RAY DIFFRACTION	Local ncs	0.12353	0.05008
20	40	D	X-RAY DIFFRACTION	Local ncs	0.12353	0.05008
21	41	D	X-RAY DIFFRACTION	Local ncs	0.12285	0.05008
21	42	D	X-RAY DIFFRACTION	Local ncs	0.12285	0.05008
22	43	D	X-RAY DIFFRACTION	Local ncs	0.12427	0.05008
22	44	D	X-RAY DIFFRACTION	Local ncs	0.12427	0.05008
23	45	D	X-RAY DIFFRACTION	Local ncs	0.12626	0.05008
23	46	D	X-RAY DIFFRACTION	Local ncs	0.12626	0.05008
24	47	D	X-RAY DIFFRACTION	Local ncs	0.11792	0.05008
24	48	D	X-RAY DIFFRACTION	Local ncs	0.11792	0.05008
25	49	D	X-RAY DIFFRACTION	Local ncs	0.12384	0.05008
25	50	D	X-RAY DIFFRACTION	Local ncs	0.12384	0.05008
26	51	D	X-RAY DIFFRACTION	Local ncs	0.12302	0.05008
26	52	D	X-RAY DIFFRACTION	Local ncs	0.12302	0.05008
27	53	D	X-RAY DIFFRACTION	Local ncs	0.12456	0.05008
27	54	D	X-RAY DIFFRACTION	Local ncs	0.12456	0.05008
28	55	D	X-RAY DIFFRACTION	Local ncs	0.1226	0.05008
28	56	D	X-RAY DIFFRACTION	Local ncs	0.1226	0.05008

LS refinement shell

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

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	R_factor all	Num. reflection all	Fsc free	Fsc work	% reflection obs (%)	WR_factor R_work
2.566-2.633	0.266	350	0.211	7465	0.213	8040	0.961	0.975	97.2015	0.216
2.633-2.705	0.297	218	0.227	4802	0.23	7805	0.958	0.973	64.3177	0.232
2.705-2.783	0.273	377	0.193	6995	0.197	7585	0.959	0.979	97.1918	0.2
2.783-2.869	0.269	355	0.189	6850	0.193	7378	0.959	0.98	97.6552	0.196
2.869-2.963	0.242	385	0.183	6590	0.187	7147	0.961	0.98	97.5934	0.191
2.963-3.067	0.233	325	0.177	6264	0.18	6956	0.965	0.981	94.724	0.186
3.067-3.182	0.227	329	0.17	6143	0.173	6651	0.967	0.982	97.3087	0.181
3.182-3.312	0.217	317	0.174	5989	0.176	6414	0.971	0.982	98.3162	0.185
3.312-3.459	0.228	309	0.175	5788	0.178	6185	0.966	0.983	98.5772	0.189
3.459-3.628	0.222	301	0.167	5438	0.17	5848	0.971	0.986	98.1361	0.18
3.628-3.824	0.211	285	0.169	5189	0.172	5602	0.973	0.984	97.7151	0.184
3.824-4.056	0.182	277	0.15	4976	0.152	5326	0.981	0.988	98.6294	0.169
4.056-4.336	0.161	235	0.132	4632	0.134	4981	0.984	0.99	97.7113	0.153
4.336-4.683	0.149	217	0.117	4289	0.119	4597	0.987	0.992	98.0204	0.138
4.683-5.129	0.15	216	0.111	4016	0.113	4287	0.988	0.992	98.717	0.131
5.129-5.733	0.166	208	0.138	3581	0.14	3841	0.985	0.99	98.6462	0.161
5.733-6.618	0.187	170	0.155	3183	0.157	3392	0.982	0.987	98.8502	0.178
6.618-8.101	0.199	146	0.16	2735	0.162	2896	0.981	0.986	99.482	0.189
8.101-11.435	0.197	104	0.168	2088	0.169	2201	0.978	0.984	99.5911	0.212
11.435-134.29	0.29	56	0.253	1150	0.255	1222	0.946	0.952	98.6907	0.33

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