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- PDB-2fhh: Crystal Structure of Mycobacterium Tuberculosis Proteasome in com... -

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Basic information

Entry
Database: PDB / ID: 2fhh
TitleCrystal Structure of Mycobacterium Tuberculosis Proteasome in complex with a peptidyl boronate inhibitor MLN-273
Components
  • 20S proteasome, alpha and beta subunitsProteasome
  • proteasome, beta subunit
KeywordsHYDROLASE / multi-subunit protein assembly / inhibitor-complex
Function / homology
Function and homology information


symbiont-mediated perturbation of host defenses / zymogen binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / peptidoglycan-based cell wall / proteolysis involved in protein catabolic process / proteasomal protein catabolic process / modification-dependent protein catabolic process ...symbiont-mediated perturbation of host defenses / zymogen binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / peptidoglycan-based cell wall / proteolysis involved in protein catabolic process / proteasomal protein catabolic process / modification-dependent protein catabolic process / extracellular region / plasma membrane / cytoplasm
Similarity search - Function
Proteasome, alpha subunit, bacterial / Proteasome subunit beta, actinobacteria / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta ...Proteasome, alpha subunit, bacterial / Proteasome subunit beta, actinobacteria / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-M1N / : / : / Proteasome subunit beta / Proteasome subunit alpha
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.99 Å
AuthorsLi, H.
CitationJournal: Mol.Microbiol. / Year: 2006
Title: Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate.
Authors: Hu, G. / Lin, G. / Wang, M. / Dick, L. / Xu, R.M. / Nathan, C. / Li, H.
History
DepositionDec 23, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 28, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.3Aug 30, 2023Group: 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 / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
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.pdbx_leaving_atom_flag / _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 / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 20S proteasome, alpha and beta subunits
H: proteasome, beta subunit
B: 20S proteasome, alpha and beta subunits
C: proteasome, beta subunit
D: 20S proteasome, alpha and beta subunits
E: proteasome, beta subunit
F: 20S proteasome, alpha and beta subunits
G: proteasome, beta subunit
I: 20S proteasome, alpha and beta subunits
J: proteasome, beta subunit
K: 20S proteasome, alpha and beta subunits
L: proteasome, beta subunit
M: 20S proteasome, alpha and beta subunits
N: proteasome, beta subunit
O: 20S proteasome, alpha and beta subunits
P: proteasome, beta subunit
Q: 20S proteasome, alpha and beta subunits
R: proteasome, beta subunit
S: 20S proteasome, alpha and beta subunits
T: proteasome, beta subunit
U: 20S proteasome, alpha and beta subunits
V: proteasome, beta subunit
W: 20S proteasome, alpha and beta subunits
X: proteasome, beta subunit
Y: 20S proteasome, alpha and beta subunits
Z: proteasome, beta subunit
1: 20S proteasome, alpha and beta subunits
2: proteasome, beta subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)740,80842
Polymers734,63028
Non-polymers6,17914
Water5,783321
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area89700 Å2
ΔGint-103 kcal/mol
Surface area225660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)173.957, 116.172, 200.203
Angle α, β, γ (deg.)90.00, 112.71, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31D
41F
51I
61K
71M
81O
91Q
101S
111U
121W
131Y
1411
12H
22C
32E
42G
52J
62L
72N
82P
92R
102T
112V
122X
132Z
1422

NCS domain segments:

Component-ID: 1 / Refine code: 2

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-IDEnd label seq-ID
11SERSERGLNGLNAA8 - 23711 - 240
21SERSERGLNGLNBC8 - 23711 - 240
31SERSERGLNGLNDE8 - 23711 - 240
41SERSERGLNGLNFG8 - 23711 - 240
51SERSERGLNGLNII8 - 23711 - 240
61SERSERGLNGLNKK8 - 23711 - 240
71SERSERGLNGLNMM8 - 23711 - 240
81SERSERGLNGLNOO8 - 23711 - 240
91SERSERGLNGLNQQ8 - 23711 - 240
101SERSERGLNGLNSS8 - 23711 - 240
111SERSERGLNGLNUU8 - 23711 - 240
121SERSERGLNGLNWW8 - 23711 - 240
131SERSERGLNGLNYY8 - 23711 - 240
141SERSERGLNGLN1AA8 - 23711 - 240
12M1NM1NSERSERHCA - B273 - 522222
22M1NM1NSERSERCDA - D273 - 522222
32M1NM1NSERSEREEA - F273 - 522222
42M1NM1NSERSERGFA - H273 - 522222
52M1NM1NSERSERJGA - J273 - 522222
62M1NM1NSERSERLHA - L273 - 522222
72M1NM1NSERSERNIA - N273 - 522222
82M1NM1NSERSERPJA - P273 - 522222
92M1NM1NSERSERRKA - R273 - 522222
102M1NM1NSERSERTLA - T273 - 522222
112M1NM1NSERSERVMA - V273 - 522222
122M1NM1NSERSERXNA - X273 - 522222
132M1NM1NSERSERZOA - Z273 - 522222
142M1NM1NSERSER2PA - BA273 - 522222

NCS ensembles :
ID
1
2
DetailsThe entire complex is deposited. The complex includes 14 copies of PrcA and 14 copies of PrcB, and 14 copies of the inhibitor MLN-273 covalently linked to the first Thr in each of the 14 beta subunits.

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Components

#1: Protein
20S proteasome, alpha and beta subunits / Proteasome


Mass: 27199.297 Da / Num. of mol.: 14
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: PrcA / Plasmid: prcA-prcB-His6 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: GenBank: 76783992, UniProt: P9WHU1*PLUS
#2: Protein
proteasome, beta subunit /


Mass: 25274.264 Da / Num. of mol.: 14
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: PrcB / Plasmid: pACYCDuet / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: GenBank: 13881852, UniProt: P9WHT9*PLUS
#3: Chemical
ChemComp-M1N / (1R)-3-METHYL-1-{[N-(MORPHOLIN-4-YLCARBONYL)-3-(1-NAPHTHYL)-D-ALANYL]AMINO}BUTYLBORONIC ACID / N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID


Mass: 441.328 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C23H32BN3O5
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 321 / Source method: isolated from a natural source / Formula: H2O

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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: 2.54 Å3/Da / Density % sol: 51.56 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.7
Details: 8% PEG 6000, 50 mM sodium citrate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 1, 2005
RadiationMonochromator: Si Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.99→50 Å / Num. all: 398981 / Num. obs: 139848 / % possible obs: 0.944 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 18.6
Reflection shellResolution: 2.99→3.11 Å / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 2.6 / % possible all: 0.844

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
CBASSdata collection
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1Q5Q
Resolution: 2.99→50 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.902 / SU B: 54.114 / SU ML: 0.439 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.486 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26163 7037 5 %RANDOM
Rwork0.22636 ---
all0.228 139848 --
obs0.22814 132804 94.12 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 85.398 Å2
Baniso -1Baniso -2Baniso -3
1-3.28 Å20 Å23.52 Å2
2--1.05 Å20 Å2
3----1.62 Å2
Refinement stepCycle: LAST / Resolution: 2.99→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms46620 0 448 321 47389
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02247824
X-RAY DIFFRACTIONr_angle_refined_deg1.2981.9864792
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.85756146
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.05423.0462114
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.075157672
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.92215476
X-RAY DIFFRACTIONr_chiral_restr0.0860.27322
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0236484
X-RAY DIFFRACTIONr_nbd_refined0.2410.224672
X-RAY DIFFRACTIONr_nbtor_refined0.3080.233213
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1660.21980
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.4120.2144
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2310.210
X-RAY DIFFRACTIONr_mcbond_it0.5711.531145
X-RAY DIFFRACTIONr_mcangle_it1.006248510
X-RAY DIFFRACTIONr_scbond_it0.949318555
X-RAY DIFFRACTIONr_scangle_it1.694.516282
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A880tight positional0.030.05
12H880tight positional0.030.05
13C880tight positional0.030.05
14E880tight positional0.030.05
15I880tight positional0.030.05
16K880tight positional0.030.05
17M880tight positional0.030.05
18O880tight positional0.030.05
19Q880tight positional0.020.05
110S880tight positional0.020.05
111U880tight positional0.030.05
112W880tight positional0.030.05
113Y880tight positional0.030.05
1141880tight positional0.030.05
21G888tight positional0.040.05
22B888tight positional0.030.05
23D888tight positional0.030.05
24F888tight positional0.040.05
25J888tight positional0.030.05
26L888tight positional0.030.05
27N888tight positional0.030.05
28P888tight positional0.030.05
29R888tight positional0.030.05
210T888tight positional0.030.05
211V888tight positional0.030.05
212X888tight positional0.040.05
213Z888tight positional0.040.05
2142888tight positional0.040.05
11A813medium positional0.440.5
12H813medium positional0.320.5
13C813medium positional0.360.5
14E813medium positional0.340.5
15I813medium positional0.340.5
16K813medium positional0.360.5
17M813medium positional0.340.5
18O813medium positional0.330.5
19Q813medium positional0.320.5
110S813medium positional0.390.5
111U813medium positional0.340.5
112W813medium positional0.380.5
113Y813medium positional0.380.5
1141813medium positional0.340.5
21G783medium positional0.340.5
22B783medium positional0.340.5
23D783medium positional0.310.5
24F783medium positional0.340.5
25J783medium positional0.350.5
26L783medium positional0.290.5
27N783medium positional0.280.5
28P783medium positional0.30.5
29R783medium positional0.360.5
210T783medium positional0.310.5
211V783medium positional0.340.5
212X783medium positional0.360.5
213Z783medium positional0.410.5
2142783medium positional0.360.5
11A880tight thermal0.050.5
12H880tight thermal0.040.5
13C880tight thermal0.030.5
14E880tight thermal0.030.5
15I880tight thermal0.030.5
16K880tight thermal0.030.5
17M880tight thermal0.030.5
18O880tight thermal0.020.5
19Q880tight thermal0.030.5
110S880tight thermal0.020.5
111U880tight thermal0.020.5
112W880tight thermal0.030.5
113Y880tight thermal0.030.5
1141880tight thermal0.030.5
21G888tight thermal0.080.5
22B888tight thermal0.070.5
23D888tight thermal0.050.5
24F888tight thermal0.050.5
25J888tight thermal0.050.5
26L888tight thermal0.060.5
27N888tight thermal0.050.5
28P888tight thermal0.050.5
29R888tight thermal0.060.5
210T888tight thermal0.060.5
211V888tight thermal0.050.5
212X888tight thermal0.050.5
213Z888tight thermal0.060.5
2142888tight thermal0.060.5
11A813medium thermal0.362
12H813medium thermal0.32
13C813medium thermal0.222
14E813medium thermal0.242
15I813medium thermal0.232
16K813medium thermal0.212
17M813medium thermal0.222
18O813medium thermal0.192
19Q813medium thermal0.232
110S813medium thermal0.222
111U813medium thermal0.232
112W813medium thermal0.232
113Y813medium thermal0.232
1141813medium thermal0.242
21G783medium thermal0.682
22B783medium thermal0.562
23D783medium thermal0.442
24F783medium thermal0.422
25J783medium thermal0.362
26L783medium thermal0.552
27N783medium thermal0.432
28P783medium thermal0.442
29R783medium thermal0.472
210T783medium thermal0.492
211V783medium thermal0.442
212X783medium thermal0.42
213Z783medium thermal0.482
2142783medium thermal0.462
LS refinement shellResolution: 2.993→3.071 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.348 432 -
Rwork0.347 8245 -
obs--79.55 %
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)
13.3820.9871-0.35771.1404-0.30731.5630.2371-0.70270.45070.1753-0.24090.16830.11330.0390.0039-0.2651-0.15620.14630.0259-0.2962-0.010746.13156.506715.6718
22.8394-0.4649-0.28841.9118-0.63731.64440.1299-0.628-0.2930.3372-0.180.23880.07870.0660.05-0.1209-0.18980.1117-0.02650.0291-0.085440.4674-24.847216.4796
32.39980.3928-0.41781.9499-0.64783.4836-0.2418-0.248-0.2574-0.11420.0638-0.41470.28690.9210.178-0.22340.40240.2680.46270.088-0.2668126.0415-35.5851-56.0898
42.4476-0.7635-0.16252.50660.44272.27240.17380.51170.1251-0.8924-0.0156-0.0381-0.53580.2197-0.15820.5325-0.19950.01430.03540.1132-0.438590.29294.4893-104.3247
52.4169-0.6396-0.39892.1326-0.22942.4746-0.0976-0.3713-0.4610.0240.04080.41740.383-0.42810.0568-0.3176-0.27950.0843-0.0330.11970.130821.1411-42.6564-1.9259
61.96820.1609-0.72.47110.30453.74650.0789-0.11590.0737-0.1489-0.2083-0.4665-0.31871.29950.1294-0.3552-0.1410.08470.66990.2531-0.2289127.7105-3.3827-60.3163
71.4684-0.459-0.73011.79280.18844.0420.21620.02160.1712-0.3414-0.0397-0.0064-0.46330.8602-0.1766-0.0161-0.33320.16750.18820.0671-0.3381111.616513.8067-81.9982
82.52551.2472-0.9362.0018-1.33063.02860.371-0.16560.61990.6354-0.11450.4807-1.4024-0.4978-0.25650.38260.32110.2511-0.2746-0.19430.233332.660928.9111-4.2351
93.18850.3257-0.80942.8806-0.20162.5558-0.2608-0.0106-0.8262-0.3002-0.1005-0.36340.70360.66460.36140.38150.43410.4405-0.15690.0309-0.023107.6729-57.474-71.117
102.019-0.5415-0.23752.23930.74022.5289-0.09110.0073-0.4378-0.02450.00760.78570.2414-0.69220.0836-0.4716-0.2774-0.05060.17410.00810.41041.4734-32.9773-25.3495
112.1433-0.1159-0.70682.6744-0.96893.55460.0750.11380.48380.1024-0.04250.5697-0.8031-0.7895-0.0325-0.25180.45270.0206-0.02880.04070.509211.03824.1171-27.5132
124.548-0.1723-0.67581.39520.01522.4202-0.64080.9714-0.4207-0.32220.23180.03440.2787-0.05620.4090.3242-0.3137-0.01570.1314-0.1614-0.36279.7368-25.06-110.275
134.25960.11611.10422.8110.56232.08430.36511.3018-0.8041-0.6825-0.3609-0.02770.96950.4159-0.00420.86820.26480.17280.0739-0.3059-0.283486.9105-53.1176-95.3982
142.26650.0481-1.22612.29810.29053.1912-0.01980.42080.2469-0.0853-0.06370.9607-0.1798-0.9810.0834-0.54640.1449-0.20010.32660.05410.4756-2.9913-3.1384-37.0084
152.06790.7685-1.44611.3634-0.62461.50340.0238-0.2870.15240.0144-0.02160.215-0.13190.4759-0.0022-0.1709-0.1049-0.01260.0274-0.0813-0.204377.0014-5.8664-5.7706
162.26650.2314-0.8380.68060.0351.4056-0.1144-0.22650.01-0.0517-0.06560.13610.2770.24460.1801-0.09430.05880.0077-0.09260.1053-0.13766.5427-38.4546-10.235
172.08880.6421-0.65971.1304-0.86321.4839-0.0253-0.2479-0.0765-0.1795-0.09980.01790.18610.50060.1251-0.22550.14950.02710.15130.0704-0.2206101.3592-23.1152-27.1376
181.3602-1.0946-1.00831.53950.85562.34930.11110.2150.0535-0.3049-0.0262-0.0321-0.3949-0.3074-0.08490.20730.025-0.2771-0.11240.1622-0.158756.39545.5444-83.9503
192.0763-0.5722-0.57681.20140.52310.9483-0.22-0.0754-0.0987-0.26640.03880.19540.4512-0.1720.18120.1287-0.1931-0.0039-0.2810.0495-0.024143.7254-51.2131-33.0172
200.83020.1096-1.13020.69310.16033.32170.0967-0.17480.0996-0.0221-0.04220.0502-0.12360.5049-0.0545-0.1544-0.2351-0.01050.082-0.0296-0.183398.33679.7423-37.7043
210.9614-0.1527-0.79011.42680.68692.05210.14880.06470.1492-0.20550.06220.106-0.28460.1319-0.2110.1303-0.1868-0.028-0.22030.0794-0.118378.303522.3843-63.1364
221.4430.3203-1.24020.9135-0.16862.14060.201-0.14540.2439-0.0686-0.01580.2261-0.36410.1338-0.18530.0085-0.09460.0445-0.2919-0.0769-0.03167.215422.4586-23.1375
232.71220.8527-1.00981.0915-0.52631.598-0.2986-0.1296-0.2878-0.3455-0.00840.02460.65780.30330.3070.15120.2940.1673-0.28250.0868-0.123284.9369-51.2397-39.1202
241.8186-0.889-0.90661.15970.63911.9271-0.1480.2269-0.1999-0.09320.09130.22730.3381-0.57830.0567-0.1089-0.3459-0.26430.0033-0.03780.087425.4814-34.2121-57.1963
251.09030.2153-0.81340.52550.41852.77140.2940.19010.1389-0.1927-0.09330.2639-0.3341-0.2445-0.20070.03050.1869-0.0869-0.27430.16970.129744.501124.7953-49.1855
262.2614-0.6186-0.55071.02880.22361.4817-0.27280.34740.0717-0.35980.02930.09940.1212-0.32290.24350.2808-0.2616-0.27-0.0305-0.0585-0.219448.956-28.1491-84.7521
272.6829-0.167-0.48960.806-0.19721.1402-0.27140.1636-0.1027-0.36730.04360.14250.5432-0.12350.22790.4617-0.1619-0.0015-0.3683-0.1696-0.174361.5624-53.5623-64.8453
281.3411-0.2583-1.31151.39661.00573.20370.25820.40520.0693-0.1515-0.06770.36980.0247-0.6291-0.1904-0.24220.1252-0.35430.10830.11880.084725.9771-0.285-64.2002
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A8 - 237
2X-RAY DIFFRACTION2B8 - 237
3X-RAY DIFFRACTION3D8 - 237
4X-RAY DIFFRACTION4F8 - 237
5X-RAY DIFFRACTION5I8 - 237
6X-RAY DIFFRACTION6K8 - 237
7X-RAY DIFFRACTION7M8 - 237
8X-RAY DIFFRACTION8O8 - 237
9X-RAY DIFFRACTION9Q8 - 237
10X-RAY DIFFRACTION10S8 - 237
11X-RAY DIFFRACTION11U8 - 237
12X-RAY DIFFRACTION12W8 - 237
13X-RAY DIFFRACTION13Y8 - 237
14X-RAY DIFFRACTION1418 - 237
15X-RAY DIFFRACTION15H301 - 522
16X-RAY DIFFRACTION16C301 - 522
17X-RAY DIFFRACTION17E301 - 522
18X-RAY DIFFRACTION18G301 - 522
19X-RAY DIFFRACTION19J301 - 522
20X-RAY DIFFRACTION20L301 - 522
21X-RAY DIFFRACTION21N301 - 522
22X-RAY DIFFRACTION22P301 - 522
23X-RAY DIFFRACTION23R301 - 522
24X-RAY DIFFRACTION24T301 - 522
25X-RAY DIFFRACTION25V301 - 522
26X-RAY DIFFRACTION26X301 - 522
27X-RAY DIFFRACTION27Z301 - 522
28X-RAY DIFFRACTION282301 - 522

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