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- PDB-3rjr: Crystal Structure of pro-TGF beta 1 -

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Basic information

Entry
Database: PDB / ID: 3rjr
TitleCrystal Structure of pro-TGF beta 1
ComponentsTransforming growth factor beta-1
KeywordsCYTOKINE / TGF beta / activation / integrin
Function / homology
Function and homology information


Platelet degranulation / Cell surface interactions at the vascular wall / Molecules associated with elastic fibres / TGF-beta receptor signaling activates SMADs / Syndecan interactions / RUNX3 regulates CDKN1A transcription / RUNX3 regulates p14-ARF / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of RUNX3 expression and activity ...Platelet degranulation / Cell surface interactions at the vascular wall / Molecules associated with elastic fibres / TGF-beta receptor signaling activates SMADs / Syndecan interactions / RUNX3 regulates CDKN1A transcription / RUNX3 regulates p14-ARF / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of RUNX3 expression and activity / regulation of binding / regulation of DNA binding / positive regulation of microglia differentiation / negative regulation of skeletal muscle tissue development / regulation of striated muscle tissue development / regulation of protein import into nucleus / type III transforming growth factor beta receptor binding / negative regulation of hyaluronan biosynthetic process / extracellular matrix assembly / negative regulation of macrophage cytokine production / odontoblast differentiation / positive regulation of isotype switching to IgA isotypes / membrane protein intracellular domain proteolysis / hyaluronan catabolic process / regulation of transforming growth factor beta receptor signaling pathway / ATP biosynthetic process / receptor catabolic process / type II transforming growth factor beta receptor binding / type I transforming growth factor beta receptor binding / positive regulation of chemotaxis / negative regulation of myoblast differentiation / cell-cell junction organization / response to cholesterol / positive regulation of fibroblast migration / phosphate-containing compound metabolic process / positive regulation of epidermal growth factor receptor signaling pathway / negative regulation of cell-cell adhesion / negative regulation of fat cell differentiation / positive regulation of interleukin-17 production / positive regulation of SMAD protein signal transduction / negative regulation of blood vessel endothelial cell migration / positive regulation of cell division / negative regulation of cell cycle / positive regulation of collagen biosynthetic process / positive regulation of blood vessel endothelial cell migration / epithelial to mesenchymal transition / lymph node development / chondrocyte differentiation / hematopoietic progenitor cell differentiation / positive regulation of epithelial to mesenchymal transition / salivary gland morphogenesis / extrinsic apoptotic signaling pathway / positive regulation of protein dephosphorylation / cellular response to transforming growth factor beta stimulus / positive regulation of protein metabolic process / transforming growth factor beta receptor signaling pathway / extracellular matrix / positive regulation of superoxide anion generation / negative regulation of protein phosphorylation / cytokine activity / response to progesterone / positive regulation of protein secretion / antigen binding / growth factor activity / positive regulation of protein-containing complex assembly / negative regulation of cell growth / response to wounding / positive regulation of protein import into nucleus / negative regulation of epithelial cell proliferation / response to estradiol / regulation of cell population proliferation / positive regulation of ERK1 and ERK2 cascade / blood microparticle / positive regulation of cell migration / inflammatory response / negative regulation of cell population proliferation / protein phosphorylation / negative regulation of gene expression / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / positive regulation of gene expression / positive regulation of DNA-templated transcription / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2330 / Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2330 / Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines / Cystine-knot cytokine / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special / Ribbon / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Transforming growth factor beta-1 proprotein
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.05 Å
AuthorsZhu, J.H. / Shi, M.L. / Springer, T.A.
CitationJournal: Nature / Year: 2011
Title: Latent TGF-Beta structure and activation
Authors: Shi, M. / Zhu, J. / Wang, R. / Chen, X. / Mi, L. / Walz, T. / Springer, T.A.
History
DepositionApr 15, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 15, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 13, 2013Group: Database references
Revision 1.3Nov 8, 2017Group: Refinement description / Category: software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transforming growth factor beta-1
B: Transforming growth factor beta-1
C: Transforming growth factor beta-1
D: Transforming growth factor beta-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)167,46310
Polymers165,7304
Non-polymers1,7346
Water00
1
A: Transforming growth factor beta-1
B: Transforming growth factor beta-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,5104
Polymers82,8652
Non-polymers6462
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9920 Å2
ΔGint-55 kcal/mol
Surface area34660 Å2
MethodPISA
2
C: Transforming growth factor beta-1
D: Transforming growth factor beta-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,9536
Polymers82,8652
Non-polymers1,0884
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10270 Å2
ΔGint-51 kcal/mol
Surface area35870 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.690, 126.940, 137.930
Angle α, β, γ (deg.)90.000, 96.720, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
12A
22B
32C
42D

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain A and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)A26 - 60
121chain A and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)A75 - 190
131chain A and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)A216 - 239
141chain A and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)A264 - 295
151chain A and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)A328 - 360
211chain B and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)B26 - 60
221chain B and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)B75 - 190
231chain B and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)B216 - 239
241chain B and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)B264 - 295
251chain B and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)B328 - 360
311chain C and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)C26 - 60
321chain C and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)C75 - 190
331chain C and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)C216 - 239
341chain C and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)C264 - 295
351chain C and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)C328 - 360
411chain D and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)D26 - 60
421chain D and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)D75 - 190
431chain D and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)D216 - 239
441chain D and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)D264 - 295
451chain D and (resid 26:60 or resid 75:190 or resid 216:239 or resid 264:295 or resid 328:360)D328 - 360
112chain A and resid 193:208A193 - 208
212chain B and resid 193:208B193 - 208
312chain C and resid 193:208C193 - 208
412chain D and resid 193:208D193 - 208

NCS ensembles :
ID
1
2

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Components

#1: Protein
Transforming growth factor beta-1 / TGF-beta-1 / Latency-associated peptide / LAP


Mass: 41432.410 Da / Num. of mol.: 4 / Mutation: C4S, N147Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sus scrofa (pig) / Gene: TGFB1 / Plasmid: pcDNA3.1 / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): Lec 3.2.8.1 / References: UniProt: P07200
#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
Sequence detailsTHE AUTHORS SEQUENCE CORRESPONDS TO REFERENCE SEQUENCE NP_999180.1

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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: 2.87 Å3/Da / Density % sol: 57.13 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 5.6
Details: 7% PEG 3350, 17% isopropanol, 0.1m Na citrate pH 5.6, vapor diffusion, temperature 293K, VAPOR DIFFUSION

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.97934, 0.97932, 0.97956, 0.95667
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 12, 2009
RadiationProtocol: MAD / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.979341
20.979321
30.979561
40.956671
ReflectionResolution: 3.05→50 Å / Num. obs: 35401 / % possible obs: 97.9 % / Redundancy: 5.6 % / Rmerge(I) obs: 0.047

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Phasing

PhasingMethod: MAD

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
PHENIXdev_276refinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementResolution: 3.05→46.554 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.51 / σ(F): 1.44 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.3106 1040 2.95 %
Rwork0.2737 --
obs0.2748 35267 98.8 %
Solvent computationShrinkage radii: 1.2 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 242.989 Å2 / ksol: 0.297 e/Å3
Displacement parametersBiso max: 561.41 Å2 / Biso mean: 214.8624 Å2 / Biso min: 20 Å2
Baniso -1Baniso -2Baniso -3
1--11.6111 Å2-0 Å2-4.7692 Å2
2---17.9314 Å2-0 Å2
3----22.1104 Å2
Refinement stepCycle: LAST / Resolution: 3.05→46.554 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10843 0 112 0 10955
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00211236
X-RAY DIFFRACTIONf_angle_d0.48815215
X-RAY DIFFRACTIONf_chiral_restr0.0321690
X-RAY DIFFRACTIONf_plane_restr0.0021939
X-RAY DIFFRACTIONf_dihedral_angle_d12.4614211
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1945X-RAY DIFFRACTIONPOSITIONAL0.002
12B1945X-RAY DIFFRACTIONPOSITIONAL0.002
13C1945X-RAY DIFFRACTIONPOSITIONAL0.004
14D1945X-RAY DIFFRACTIONPOSITIONAL0.004
21A124X-RAY DIFFRACTIONPOSITIONAL0.009
22B124X-RAY DIFFRACTIONPOSITIONAL0.009
23C124X-RAY DIFFRACTIONPOSITIONAL0.004
24D124X-RAY DIFFRACTIONPOSITIONAL0.004
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 7

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.05-3.21080.41881500.36684857500798
3.2108-3.41190.39011240.33664853497798
3.4119-3.67530.35121450.32074859500499
3.6753-4.04490.32941440.29124873501799
4.0449-4.62980.29771390.25654907504699
4.6298-5.83120.31861590.254907506699
5.8312-46.55950.26811790.24594971515099
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)
10.20170.21360.19290.39060.2850.1301-0.2655-0.7811-0.03490.5686-0.1133-0.4492-1.0960.0066-0.00021.94450.4269-0.69680.784-0.38381.6305-84.699655.2195-39.7024
20.0790.34790.26020.2226-0.03230.02370.4059-1.2910.13290.19880.22710.5414-1.9573-0.2670.00033.32880.4194-0.07951.71240.230.9648-87.804162.7726-16.2105
3-0.01220.28690.60860.8710.2027-0.14370.4943-0.37240.2889-0.2277-0.02880.7157-0.0351-0.2523-0.00011.31450.3273-0.28891.7773-0.3081.8771-85.760350.29191.162
40.1077-0.3149-0.0361.55210.60510.0606-0.744-0.23091.2277-0.63450.1635-0.24930.50870.2131-0.00011.9685-0.02880.02051.7428-0.01650.8955-76.385143.88731.3589
50.08350.0751-0.01380.2811-0.11270.2881-1.22050.03060.08-0.7787-0.13890.3328-0.23781.5903-0.01112.5101-0.38710.04111.765-0.48311.2361-70.138752.19296.9298
60.0442-0.3586-0.09230.3989-0.195-0.05260.3612-0.33411.08170.6895-0.42850.4315-0.06230.8831-02.7190.1987-0.43211.13090.1231.5895-80.279549.4094-24.5551
70.28030.22450.30480.5407-0.64170.6123-0.1371-1.3340.0784-0.65640.1235-0.7324-0.93020.02540.00022.80560.4189-0.26111.5360.16781.1763-80.938357.0859-33.3787
80.0037-0.0015-0.00490.0016-0.00230.0031-0.2822-0.1285-0.1447-0.021-0.1336-0.0203-0.05320.0109-0.00013.98691.2569-0.27831.80390.33691.9711-62.19532.7115-44.6607
9-0.0070.0127-0.0136-0.00140.0243-0.0149-0.3458-0.04-0.006-0.2327-0.5981-0.7786-0.37381.2158-0.00042.1059-0.13380.59930.92430.41073.9801-70.018333.625-39.9448
101.7831.3041-0.76241.3698-0.96531.4357-2.34570.32760.1892-0.0793-0.8912-0.7051-2.36610.7507-0.67052.52780.3234-0.96860.7765-0.29050.5442-83.888451.501-25.1319
110.3836-0.69590.55161.8099-0.9292-0.52471.23240.40922.23880.1263-0.0049-0.0282-0.6485-0.44960.0541.42350.37490.10151.35230.14480.5432-76.544122.4656-43.3148
120.73780.71460.09210.2152-0.07290.21450.7355-0.23021.23861.0330.7795-1.42931.80870.68540.00061.6999-0.47450.07111.5372-0.29960.8526-61.2312.9337-26.4307
130.04610.7583-0.19960.5656-0.37740.1512-0.03190.35290.0329-0.82610.0339-1.0775-1.30361.0347-0.00271.1049-0.1420.09531.6017-0.43120.8237-53.386423.5162-9.73
140.6198-0.86160.67670.410.87330.4917-1.4615-0.49170.45260.62350.6340.87020.2669-0.3103-0.00331.3227-0.1977-0.3221.4963-0.27730.9061-61.064529.1959-4.2023
151.193-0.83830.24530.06791.48390.77120.13170.02590.15660.29070.38240.818-0.1862-0.3311-0.00110.8955-0.5087-0.0051.01720.13631.2443-68.401725.2558-14.7882
16-0.1119-0.0801-0.0040.05450.1826-0.2030.34160.4873-0.92371.04350.2437-0.11560.3934-0.55040.00031.6558-0.2251-0.18551.1146-0.17320.9573-79.091419.0512-35.9327
170.24360.56820.25910.4280.09670.11960.52920.41650.0382-1.11170.2298-0.36430.43670.255601.6443-0.044-0.30221.0635-0.55691.0219-72.604117.1603-36.3774
18-0.03080.0947-0.0263-0.0035-0.06270.0238-0.0323-0.267-1.2834-0.214-0.72720.48040.1794-0.5089-0.00041.8264-0.2497-0.19992.5049-0.09022.1282-95.662239.969-31.9919
19-0.01270.0471-0.0693-0.01280.04530.0358-0.0806-0.7964-0.66420.0979-0.25190.33970.7071-0.501-02.1362-0.6798-0.12741.31750.28791.6361-85.442342.9772-32.7974
200.04820.61530.47630.84980.20410.69670.599-0.50860.7163-0.3895-0.1331-0.45850.8253-0.307101.0504-0.04020.00581.2699-0.02990.6984-69.21724.8029-30.5868
210.40140.2768-0.03831.2791.65270.4588-0.26330.07350.6191.3079-0.0266-0.4164-2.09510.22790.00131.24410.1487-0.32830.3947-0.04831.3973-40.150955.667471.9351
220.1381-0.0684-0.06870.4173-0.22580.49570.4155-0.18690.5966-0.59560.052-1.37421.0482-0.43980.00031.03510.0528-0.010.80680.1851.3587-44.200749.903141.3836
230.20150.28760.01281.6659-0.2463-0.0059-0.37320.9671-0.2128-0.34260.0907-0.6504-0.52380.32740.00011.14490.0312-0.06470.98290.01171.0975-46.13647.40938.4754
240.48350.470.53351.25750.94082.3138-0.29631.11140.4617-0.7254-0.4956-0.13610.5839-0.226-0.35631.54270.19530.350.88050.33410.7728-49.176241.222534.5191
252.30270.790.88550.233-1.21622.3945-1.8827-1.39341.54170.36210.1302-1.3543-0.9201-1.3335-0.09031.04530.32290.42560.59240.03941.3315-48.063448.220537.7475
260.00450.0174-0.0134-0.0526-0.0801-0.0064-0.2461-0.5337-0.395-0.0421-0.91460.1873-0.7988-0.4384-00.79050.5222-0.11052.00890.10912.7489-61.874545.249674.1571
270.0922-0.02780.1290.03440.08510.2170.0593-0.23980.03870.39590.05360.4015-0.77510.34970.00021.55760.4538-0.82510.7447-0.58982.1068-49.686653.869972.5897
280.8847-0.7108-0.18310.84990.45872.0665-2.0485-1.6562.8682.25380.2404-1.0347-1.7441.7293-1.69380.84840.1882-0.1423-0.6881-1.50980.0687-44.846754.432770.4582
29-0.0205-0.10720.13710.02620.03020.03071.77630.50781.53710.6173-0.4929-0.7664-0.6081-0.93180.00031.41460.59170.61591.18650.11671.3869-62.463327.469985.446
302.74381.3742-0.56415.0819-4.4885.512-6.33180.61542.4809-0.1435-1.45020.1731-4.58270.3692-7.1854-4.89233.55321.7252-1.8958-0.9553-0.4432-45.972844.780365.5754
310.53380.22250.08871.46560.34840.76111.0397-1.8659-0.1641.3201-1.4039-0.67410.49630.5556-0.22060.5056-0.02530.12151.03250.4750.5721-53.616117.871978.3028
320.0026-0.02270.07420.0573-0.23150.13890.4651.0687-0.2223-0.7993-0.80651.56291.4696-0.3748-0.00421.67740.045-0.33050.96490.18850.6371-65.679.178258.4109
330.07610.0413-0.00250.0060.028-0.0231-0.29430.3625-0.23171.29960.3642-0.3131-0.67250.19990.00032.34811.08220.08382.0234-0.65930.6937-61.087831.389559
341.07750.581-1.1931.62880.07890.4089-0.04260.0089-0.5402-0.39240.15950.84780.2265-0.236300.8030.1661-0.18810.909-0.14550.7312-70.812721.276743.7745
350.5485-0.3684-0.34770.5212-1.2151-0.182-0.60080.47740.2981-0.52340.153-0.3306-0.14650.0956-0.00021.21790.0744-0.41620.8063-0.08680.9426-66.646729.593438.5411
360.3264-0.47580.31050.18320.0261.1398-0.42732.6128-0.3880.07741.1162-0.1447-0.60791.90090.00270.95450.5192-0.18990.7752-0.50951.3495-60.947225.128426.2959
371.0551-0.74350.62871.1777-0.51321.16170.2392-2.57460.2169-0.2190.2935-0.45330.5230.14640.06950.36080.3009-0.11620.52440.16310.3042-64.529322.130858.7252
38-0.0204-0.03850.23980.26940.02190.2931-0.2439-0.8349-2.69190.165-0.1681-2.4304-1.09492.02520.04120.20960.47740.10580.29970.23031.0551-43.426217.630670.6728
391.1854-0.96630.22431.54310.60031.2295-0.6094-0.1770.1667-0.16460.5301-0.78090.2850.4977-0.38590.2920.3727-0.12580.63060.13380.9859-44.136427.360670.1682
400.9412-1.3594-0.73811.3020.92841.1865-0.5377-0.1991-0.07180.0027-0.0078-0.30490.3959-0.3684-1.12690.30350.02890.04580.4543-0.07580.5608-57.914921.659766.2035
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resid 1:30A1 - 30
2X-RAY DIFFRACTION2chain A and resid 31:61A31 - 61
3X-RAY DIFFRACTION3chain A and resid 62:116A62 - 116
4X-RAY DIFFRACTION4chain A and resid 117:202A117 - 202
5X-RAY DIFFRACTION5chain A and resid 203:227A203 - 227
6X-RAY DIFFRACTION6chain A and resid 228:263A228 - 263
7X-RAY DIFFRACTION7chain A and resid 264:299A264 - 299
8X-RAY DIFFRACTION8chain A and resid 300:313A300 - 313
9X-RAY DIFFRACTION9chain A and resid 314:324A314 - 324
10X-RAY DIFFRACTION10chain A and resid 325:361A325 - 361
11X-RAY DIFFRACTION11chain B and resid 1:30B1 - 30
12X-RAY DIFFRACTION12chain B and resid 31:61B31 - 61
13X-RAY DIFFRACTION13chain B and resid 62:116B62 - 116
14X-RAY DIFFRACTION14chain B and resid 117:200B117 - 200
15X-RAY DIFFRACTION15chain B and resid 201:263B201 - 263
16X-RAY DIFFRACTION16chain B and resid 264:274B264 - 274
17X-RAY DIFFRACTION17chain B and resid 275:296B275 - 296
18X-RAY DIFFRACTION18chain B and resid 297:311B297 - 311
19X-RAY DIFFRACTION19chain B and resid 312:324B312 - 324
20X-RAY DIFFRACTION20chain B and resid 325:361B325 - 361
21X-RAY DIFFRACTION21chain C and resid -1:49C-1 - 49
22X-RAY DIFFRACTION22chain C and resid 50:100C50 - 100
23X-RAY DIFFRACTION23chain C and resid 101:142C101 - 142
24X-RAY DIFFRACTION24chain C and resid 143:200C143 - 200
25X-RAY DIFFRACTION25chain C and resid 201:240C201 - 240
26X-RAY DIFFRACTION26chain C and resid 251:263C251 - 263
27X-RAY DIFFRACTION27chain C and resid 264:274C264 - 274
28X-RAY DIFFRACTION28chain C and resid 275:298C275 - 298
29X-RAY DIFFRACTION29chain C and resid 299:314C299 - 314
30X-RAY DIFFRACTION30chain C and resid 315:361C315 - 361
31X-RAY DIFFRACTION31chain D and resid 1:36D1 - 36
32X-RAY DIFFRACTION32chain D and resid 37:59D37 - 59
33X-RAY DIFFRACTION33chain D and resid 60:73D60 - 73
34X-RAY DIFFRACTION34chain D and resid 74:137D74 - 137
35X-RAY DIFFRACTION35chain D and resid 138:200D138 - 200
36X-RAY DIFFRACTION36chain D and resid 201:223D201 - 223
37X-RAY DIFFRACTION37chain D and resid 224:255D224 - 255
38X-RAY DIFFRACTION38chain D and resid 256:275D256 - 275
39X-RAY DIFFRACTION39chain D and resid 276:324D276 - 324
40X-RAY DIFFRACTION40chain D and resid 325:361D325 - 361

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