[English] 日本語
Yorodumi
- PDB-5ohm: K33-specific affimer bound to K33 diUb -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5ohm
TitleK33-specific affimer bound to K33 diUb
Components
  • K33-specific affimer
  • Polyubiquitin-C
KeywordsSIGNALING PROTEIN / ubiquitin / cystatin
Function / homology
Function and homology information


Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex ...Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Pexophagy / Regulation of innate immune responses to cytosolic DNA / InlA-mediated entry of Listeria monocytogenes into host cells / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLK / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Josephin domain DUBs / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / Regulation of NF-kappa B signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Hh mutants are degraded by ERAD / Recognition of DNA damage by PCNA-containing replication complex / Negative regulation of FGFR3 signaling / Peroxisomal protein import / Degradation of AXIN / Degradation of GLI1 by the proteasome / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Activation of NF-kappaB in B cells / Regulation of TNFR1 signaling / Termination of translesion DNA synthesis / Negative regulation of FGFR2 signaling / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Stabilization of p53 / EGFR downregulation / Negative regulation of FGFR4 signaling / Negative regulation of NOTCH4 signaling / Iron uptake and transport / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of FGFR1 signaling / G2/M Checkpoints / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Vif-mediated degradation of APOBEC3G
Similarity search - Function
Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Polyubiquitin-C / Polyubiquitin-C
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å
AuthorsMichel, M.A. / Komander, D.
CitationJournal: Mol. Cell / Year: 2017
Title: Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling.
Authors: Michel, M.A. / Swatek, K.N. / Hospenthal, M.K. / Komander, D.
History
DepositionJul 17, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 4, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 2, 2019Group: Data collection / Database references / Source and taxonomy
Category: entity_src_gen / struct_ref ...entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id ..._entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id / _entity_src_gen.pdbx_gene_src_scientific_name / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq_dif.pdbx_seq_db_accession_code
Revision 1.3Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Polyubiquitin-C
C: Polyubiquitin-C
E: Polyubiquitin-C
G: Polyubiquitin-C
I: Polyubiquitin-C
K: Polyubiquitin-C
D: K33-specific affimer
H: K33-specific affimer
L: K33-specific affimer
B: K33-specific affimer
F: K33-specific affimer
J: K33-specific affimer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,54414
Polymers131,48412
Non-polymers3,0602
Water00
1
A: Polyubiquitin-C
C: Polyubiquitin-C
D: K33-specific affimer
B: K33-specific affimer


Theoretical massNumber of molelcules
Total (without water)43,8284
Polymers43,8284
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-36 kcal/mol
Surface area14980 Å2
MethodPISA
2
E: Polyubiquitin-C
G: Polyubiquitin-C
H: K33-specific affimer
F: K33-specific affimer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,3585
Polymers43,8284
Non-polymers1,5301
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4870 Å2
ΔGint-36 kcal/mol
Surface area15030 Å2
MethodPISA
3
I: Polyubiquitin-C
K: Polyubiquitin-C
L: K33-specific affimer
J: K33-specific affimer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,3585
Polymers43,8284
Non-polymers1,5301
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-38 kcal/mol
Surface area14950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.866, 149.604, 73.788
Angle α, β, γ (deg.)90.00, 110.44, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Polyubiquitin-C


Mass: 8675.962 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48, UniProt: P0CG64*PLUS
#2: Protein
K33-specific affimer


Mass: 13238.074 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#3: Chemical ChemComp-15P / POLYETHYLENE GLYCOL (N=34) / PEG 1500


Mass: 1529.829 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C69H140O35 / Comment: precipitant*YM

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.2 Å3/Da / Density % sol: 44.03 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.4 / Details: 20% PEG3350 0.2M potassium thiocyanate

-
Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.91741 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 12, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91741 Å / Relative weight: 1
ReflectionResolution: 3.8→48.46 Å / Num. obs: 10962 / % possible obs: 97.9 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.237 / Net I/σ(I): 3.8
Reflection shellResolution: 3.8→4.25 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.779 / Mean I/σ(I) obs: 1.5 / CC1/2: 0.665 / % possible all: 99.2

-
Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5OHV
Resolution: 3.8→48.46 Å / SU ML: 0.59 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 33.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2825 499 4.55 %
Rwork0.2328 --
obs0.2352 10962 97.59 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.8→48.46 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7123 0 36 0 7159
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037285
X-RAY DIFFRACTIONf_angle_d0.6559931
X-RAY DIFFRACTIONf_dihedral_angle_d11.9484300
X-RAY DIFFRACTIONf_chiral_restr0.0441217
X-RAY DIFFRACTIONf_plane_restr0.0041250
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.8-4.18230.35731120.29452648X-RAY DIFFRACTION99
4.1823-4.7870.25481420.2122575X-RAY DIFFRACTION97
4.787-6.02930.28121150.24152571X-RAY DIFFRACTION96
6.0293-48.46420.27261300.21222670X-RAY DIFFRACTION99
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)
12.41641.0558-0.11372.50950.11141.28890.6216-0.4190.30660.4217-0.118-0.325-0.66560.50760.080.725-0.66190.01240.6046-0.35440.125-32.9672-23.549119.3506
22.8640.7627-0.43892.49940.81620.7420.718-0.48370.60940.26090.08920.3287-0.0572-0.09290.71441.6293-1.0776-0.10930.7810.48331.0057-32.4043-25.055322.5693
30.31020.15620.12070.8490.26640.10180.1554-0.58030.01541.04810.4258-0.37220.27280.3437-0.35172.2702-0.5804-0.0371.6149-0.57380.6106-33.5617-30.672328.3508
40.61110.19850.14151.25250.76161.81570.637-0.4031-0.71621.22420.1867-0.24460.96080.2986-0.08741.6716-0.2616-0.66771.0418-0.04220.4103-35.673-36.787322.9399
54.91790.5115-0.9099.85994.37664.88450.155-0.0316-0.89930.25130.0146-0.77850.89961.7516-0.36510.51460.29150.45360.9824-0.68171.0807-26.1783-32.971512.964
63.8746-0.36951.294.17134.40515.39480.5696-1.479-0.84131.79870.0947-1.07191.47811.5997-0.2991.5883-0.0335-0.96291.40330.43711.596-22.3112-33.119421.3759
73.4052-3.56221.51549.48262.69093.85420.651-0.35571.11640.4348-0.3584-0.7589-0.68791.1266-0.17311.1635-1.06510.13551.23190.39090.6301-24.7102-22.024717.194
81.4045-0.3649-1.24470.09480.31741.09890.8703-0.2053-0.0794-0.15040.5679-0.03020.7833-0.1569-0.48541.2997-0.2892-0.36580.66610.10910.8444-36.2675-35.681118.2167
90.49990.73230.06421.523-0.57690.8339-0.3004-0.35810.20081.603-0.52690.85690.9185-0.30790.19230.8093-0.95720.48560.5747-0.08240.9386-52.5287-46.322920.129
106.5665-3.5619-1.09225.2476-1.29181.25170.3905-1.3423-0.7310.8113-0.2741-0.1352-0.16510.1846-0.16671.034-0.64410.03651.25180.13530.6214-52.0526-40.696327.856
110.80270.143-0.94710.3511-0.17891.11440.122-0.27170.10690.062-0.13210.0002-0.12860.24530.0071.0994-0.42011.04581.23520.18310.4922-49.8155-34.591923.0831
124.21891.085-1.44664.8045-3.13674.8343-0.0755-0.14880.03290.2994-0.12590.532-0.0721-0.18740.12081.9520.37650.70681.1077-0.45760.846-59.9717-35.817617.2052
131.54420.2356-0.4460.6271-0.731.18110.23810.15070.76170.6403-0.64270.07040.1359-0.296-0.2630.4484-1.14450.705-0.10470.15461.1929-56.2024-40.193217.8244
141.2794-1.28672.85925.3855-1.10617.16430.18090.32010.0814-0.2104-0.6060.8648-1.0493-1.53920.05070.54380.52730.33250.7394-0.02871.6922-45.0571-0.4505-10.4882
150.0689-0.0420.31940.75050.34012.04-0.18950.1206-0.0950.3312-0.12050.44990.3692-0.833-0.02280.92950.08711.40471.01190.32621.5135-39.85571.4903-9.6066
161.6336-0.9614-2.11860.57221.24272.7517-0.07170.76890.328-0.0733-0.06860.53760.3376-0.60360.33721.09420.26090.35631.7094-0.35571.7108-54.68152.5962-17.6237
174.36552.7334-3.35611.819-1.42986.85310.066-1.0567-0.29250.77050.72070.32430.4323-0.4446-0.50181.06230.35810.25560.94550.5311.3799-43.97677.5495-18.336
180.4650.6651-0.32613.21571.2071.47280.08290.2195-0.1594-0.2786-0.10710.0720.88960.2575-0.0241.62391.0158-0.69520.8762-0.16020.869-37.87933.7149-22.1004
194.9687-1.0889-5.38360.44110.80026.53420.27710.6702-1.2274-0.49810.14630.38781.25210.7981-0.52120.85580.4951-0.29830.8486-0.61462.1594-43.5558-9.1134-20.0496
202.73961.8761-4.56131.2844-3.12497.60010.99150.94580.2662-0.00220.48590.5231-0.4907-0.6064-1.39291.15130.7351-0.41582.09030.31912.4908-47.9452-2.3802-26.3365
210.7437-0.6941.29720.6857-1.24872.29680.97691.416-0.5158-0.10450.40360.91250.0127-1.1032-1.46171.06070.3415-0.40341.75480.44462.4893-52.3149-4.6461-21.1803
224.16494.2454-1.83314.3291-1.85080.93781.26041.3029-0.5856-0.77550.3471.5138-0.3675-0.7447-1.26931.07840.18540.1050.699-0.26321.142-51.4035-5.7662-11.9405
230.7848-0.05650.43010.3927-0.7231.55790.54680.70410.8036-1.1407-0.7522-0.758-0.31550.2764-0.24531.55070.62950.27440.8233-0.16111.2715-35.6340.0809-20.7783
240.35610.2988-0.47110.8191-1.17491.7333-0.148-0.12010.1629-0.4083-0.6412-0.8681-0.38271.0904-0.42442.2381-0.72661.98361.0889-0.23092.2929-18.4647.9442-23.1345
250.17550.10020.30072.03110.13730.5171-0.3264-0.3770.51610.23620.3412-0.4838-0.8215-0.4540.11191.690.41690.60450.91150.01122.205-24.481714.5727-19.5794
262.03531.2259-0.88340.8039-0.21212.16711.0005-0.48680.23681.1267-0.0460.971-0.1775-0.3802-0.23812.053-0.33340.81350.7744-0.10562.2462-23.91217.7579-13.6077
270.6423-0.7144-0.16280.79430.18150.04150.0874-0.20511.0910.2362-0.25670.3368-0.59090.09570.09981.6994-0.8126-0.28190.94390.02482.3734-18.118413.3099-10.3043
286.3876-0.38765.00985.6865-3.74186.0176-1.18271.64651.05790.2484-0.3655-0.2421-0.70720.69661.47630.5546-0.09330.50841.1453-0.06211.949-9.90419.4919-18.1098
291.043-0.3352-0.10376.92890.31623.70150.3039-0.51410.2531-0.2428-0.4586-0.3542-0.2760.6474-0.80711.2196-0.06360.73850.96590.4651.6928-25.89354.6493-14.4041
301.3067-0.9342-0.88854.1478-3.19394.8158-0.091-0.0125-0.24662.0951-0.3857-0.00890.94031.58150.41722.39780.126-1.16450.702-0.04221.6673-48.9759-2.040826.0632
310.27450.2001-0.57830.35330.05152.25580.71640.42110.472-0.88340.5094-0.5218-1.197-0.7281-0.93473.14470.1724-0.36950.9540.01131.2007-55.2933-7.936923.5206
321.989-2.66531.31523.5797-1.62797.36590.76960.1523-0.47770.5464-1.2039-0.31330.57880.27570.50151.8616-0.14030.13050.250.09152.5479-54.2306-2.074916.3684
330.31530.39380.88092.37140.91172.47910.3610.6873-0.6234-0.4162-0.4555-0.42340.94711.17640.1722.40070.5741-0.12980.8977-0.13091.8169-47.643-7.459512.3461
345.33610.68782.85831.7358-2.03365.04220.19910.29830.0699-0.3803-0.1215-0.22610.25841.16410.20291.16770.1572-0.28671.56630.281.0811-40.8005-3.763920.0858
351.1953-0.51-1.88221.8342-0.06713.43450.04230.3267-0.21770.1788-0.1981-0.23840.29351.0817-0.40920.9717-0.1604-1.07240.86650.19421.0099-55.48312.086318.0205
360.5048-0.1071-1.12270.70010.5532.62770.5939-0.2942-0.2746-0.1246-0.01511.11951.2346-1.33170.02641.4723-0.7069-0.82810.94240.04891.5998-76.68785.915811.661
370.83290.18460.82210.11310.17990.82840.248-0.6461-0.09420.5925-0.13171.21151.3146-0.935-0.45141.1804-0.2471-0.02981.08750.39781.5206-74.06044.353715.0723
380.8005-0.8954-0.8761.82860.33911.45070.4348-0.08250.1454-0.29990.0289-0.2481-0.23750.0273-0.13891.6898-0.9288-0.61111.32250.76161.3676-74.2505-1.947420.6992
390.7648-0.85710.06091.2618-0.70583.09960.466-0.9032-0.94120.59540.1854-0.92990.5906-0.2879-0.3021.1015-0.5167-0.03481.96660.42491.8052-70.25136.414323.6621
403.95090.69630.34412.6954-0.20850.6080.0966-0.3501-0.27440.06750.1430.38560.2853-0.6097-0.14081.198-1.2208-0.36631.98650.22851.1553-78.21548.167527.7696
412.63173.3742-1.39565.9019-0.63384.04680.7374-1.06810.08311.2274-0.10820.50270.6943-1.5907-0.80440.6916-0.44020.19311.34020.01411.403-75.69459.715320.0974
427.1655-2.28564.06982.4193-0.18523.28820.20990.18870.64680.13890.24510.04010.34670.66220.28520.6249-0.16780.18890.5264-0.05560.8329-49.0747-23.0488-1.6142
434.2359-1.4331-0.08818.3225-0.49176.83590.45750.35031.1350.1008-0.83380.0383-0.5104-1.0711-0.10280.80650.09060.04990.77050.12560.7248-50.2188-19.1657-1.1683
446.33060.04750.00875.98890.78555.6459-0.14530.45941.14960.15240.27930.0241-0.314-0.29490.14430.4426-0.3972-0.32090.4603-0.12420.4971-45.3035-23.61753.2478
453.61710.026-0.11424.54860.79981.5710.3535-0.28210.60010.16620.403-0.0871-0.07740.08580.53970.0874-0.35620.54950.36180.18961.6461-46.143-26.40725.2391
463.5334-2.18690.52192.4273-1.12734.08430.66011.0364-0.3051-0.35570.3903-1.6327-0.20080.9226-0.20520.8314-0.03760.32690.878-0.10840.8476-19.0373-12.8362-1.7668
471.3231-1.63242.4364.43270.17878.67570.35160.27480.49220.88380.0094-1.03580.19441.8625-0.2190.7705-0.1060.09550.6436-0.15991.9052-14.3968-14.89244.5963
482.01560.2043-0.93581.1684-1.52762.72240.10181.00820.5152-0.12360.63960.449-0.053-0.7160.03250.7105-0.79890.5450.5909-0.2011.6534-37.0324-13.4515-1.8194
492.72582.1761.43333.2437-0.02815.866-0.5440.92790.2381-0.21410.6478-0.16140.12180.1386-0.33070.3334-0.27530.29990.6548-0.02721.3581-27.7768-13.34771.4363
502.92340.4281.85423.93851.89973.3257-0.2850.58280.28890.4120.2183-0.65890.05630.52040.07430.4474-0.18840.54910.8322-0.04231.3417-22.7161-11.06142.95
515.9208-0.57915.19140.6326-0.37044.5378-0.08630.329-0.4101-0.7038-0.2019-0.30210.4008-0.1361-0.07350.5657-0.5593-0.11490.7674-0.16160.5918-28.211-9.0455-7.9158
522.9569-0.76752.53222.16520.23223.80760.3809-0.3195-0.1772-0.13750.36780.48950.86150.3451-1.07450.9223-0.4504-0.87961.35280.1370.8363-59.588328.040126.1555
538.0178-1.7274-3.36288.3381-1.89822.348-0.5435-0.2635-0.76051.1425-0.88520.0514-0.31540.30211.39611.93080.0499-0.55550.96480.13431.4837-63.166134.409929.7128
542.24270.63360.58942.0680.22882.8193-0.3441-0.51840.33641.0817-0.186-0.4872-0.54660.00220.48171.6862-0.1141-0.02621.57080.38520.9987-45.998317.15828.0363
550.69480.14550.62070.77920.32051.8995-0.0383-0.90690.60490.8469-0.033-0.0879-0.5941-0.19291.65542.21240.0842-1.16671.3799-0.32460.8112-56.142425.636330.4406
561.2470.55370.7853.24251.12742.7297-0.2434-1.07190.42050.9799-0.33-0.4674-0.5228-0.34490.38281.1094-0.1471-0.81991.0358-0.34751.2496-55.280215.859921.6149
573.4559-2.0535-1.92987.92721.52664.54680.67440.11920.4485-1.15780.0047-0.7989-0.72850.3682-0.10551.0368-0.21620.49240.2209-0.33430.7201-31.5633-43.249-3.7352
585.1159-0.3128-1.61124.30621.16173.08580.2799-0.0942-0.19830.2785-0.0671-0.2241-0.12590.13250.41080.4574-0.2037-0.05670.63370.17340.871-35.634-48.7158-3.0313
597.71811.67960.80188.76510.50655.88280.45910.9336-1.0472-0.1426-0.654-0.40480.38770.3536-0.11630.6798-0.01150.03310.6689-0.14360.8819-35.0265-48.4809-0.4601
600.0003-0.04240.0235.90881.79436.35450.1696-1.3596-1.0920.70350.444-0.0857-0.15460.2772-0.680.3823-0.2040.07740.42790.26671.097-39.5235-41.20225.3311
615.01241.72580.59029.03540.77756.3046-0.1740.7604-1.3685-1.24430.5769-1.31641.09780.7586-0.05071.45960.1340.19190.9872-0.35131.6553-25.2992-20.9288-24.5119
621.11-0.4566-0.01563.22540.25212.7364-0.01661.0883-1.026-1.2001-0.3658-1.43020.11160.9332-0.68051.36750.14890.81341.0233-0.35690.9206-24.3033-16.3125-25.1106
631.49581.9517-1.57423.0134-0.30848.80640.1407-0.6273-0.41450.377-0.18370.0845-1.29330.2491-0.36570.29340.0160.05060.46910.04621.3858-51.573919.65142.0575
640.01010.13380.24984.0234-0.99954.96030.5663-0.1577-0.2615-0.04930.1491-0.709-0.5347-0.59770.24360.6845-0.2502-0.23960.26240.40271.3504-54.508817.41421.3727
654.4617-1.8882-4.13377.22092.97848.368-0.0626-0.30290.15130.9-0.10190.22681.25640.30880.31080.6851-0.0792-0.280.58830.12821.2669-55.920114.42277.934
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 7 )
2X-RAY DIFFRACTION2chain 'A' and (resid 8 through 22 )
3X-RAY DIFFRACTION3chain 'A' and (resid 23 through 34 )
4X-RAY DIFFRACTION4chain 'A' and (resid 35 through 44 )
5X-RAY DIFFRACTION5chain 'A' and (resid 45 through 49 )
6X-RAY DIFFRACTION6chain 'A' and (resid 50 through 59 )
7X-RAY DIFFRACTION7chain 'A' and (resid 60 through 65 )
8X-RAY DIFFRACTION8chain 'A' and (resid 66 through 74 )
9X-RAY DIFFRACTION9chain 'C' and (resid 1 through 22 )
10X-RAY DIFFRACTION10chain 'C' and (resid 23 through 34 )
11X-RAY DIFFRACTION11chain 'C' and (resid 35 through 44 )
12X-RAY DIFFRACTION12chain 'C' and (resid 45 through 54 )
13X-RAY DIFFRACTION13chain 'C' and (resid 55 through 74 )
14X-RAY DIFFRACTION14chain 'E' and (resid 1 through 7 )
15X-RAY DIFFRACTION15chain 'E' and (resid 8 through 16 )
16X-RAY DIFFRACTION16chain 'E' and (resid 17 through 22 )
17X-RAY DIFFRACTION17chain 'E' and (resid 23 through 34 )
18X-RAY DIFFRACTION18chain 'E' and (resid 35 through 44 )
19X-RAY DIFFRACTION19chain 'E' and (resid 45 through 49 )
20X-RAY DIFFRACTION20chain 'E' and (resid 50 through 54 )
21X-RAY DIFFRACTION21chain 'E' and (resid 55 through 59 )
22X-RAY DIFFRACTION22chain 'E' and (resid 60 through 65 )
23X-RAY DIFFRACTION23chain 'E' and (resid 66 through 75 )
24X-RAY DIFFRACTION24chain 'G' and (resid 1 through 22 )
25X-RAY DIFFRACTION25chain 'G' and (resid 23 through 34 )
26X-RAY DIFFRACTION26chain 'G' and (resid 35 through 49 )
27X-RAY DIFFRACTION27chain 'G' and (resid 50 through 54 )
28X-RAY DIFFRACTION28chain 'G' and (resid 55 through 65 )
29X-RAY DIFFRACTION29chain 'G' and (resid 66 through 74 )
30X-RAY DIFFRACTION30chain 'I' and (resid 1 through 22 )
31X-RAY DIFFRACTION31chain 'I' and (resid 23 through 34 )
32X-RAY DIFFRACTION32chain 'I' and (resid 35 through 49 )
33X-RAY DIFFRACTION33chain 'I' and (resid 50 through 54 )
34X-RAY DIFFRACTION34chain 'I' and (resid 55 through 65 )
35X-RAY DIFFRACTION35chain 'I' and (resid 66 through 73 )
36X-RAY DIFFRACTION36chain 'K' and (resid 1 through 6 )
37X-RAY DIFFRACTION37chain 'K' and (resid 7 through 22 )
38X-RAY DIFFRACTION38chain 'K' and (resid 23 through 34 )
39X-RAY DIFFRACTION39chain 'K' and (resid 35 through 49 )
40X-RAY DIFFRACTION40chain 'K' and (resid 50 through 54 )
41X-RAY DIFFRACTION41chain 'K' and (resid 55 through 73 )
42X-RAY DIFFRACTION42chain 'D' and (resid 33 through 74 )
43X-RAY DIFFRACTION43chain 'D' and (resid 75 through 90 )
44X-RAY DIFFRACTION44chain 'D' and (resid 91 through 105 )
45X-RAY DIFFRACTION45chain 'D' and (resid 106 through 121 )
46X-RAY DIFFRACTION46chain 'H' and (resid 33 through 52 )
47X-RAY DIFFRACTION47chain 'H' and (resid 53 through 62 )
48X-RAY DIFFRACTION48chain 'H' and (resid 63 through 73 )
49X-RAY DIFFRACTION49chain 'H' and (resid 74 through 86 )
50X-RAY DIFFRACTION50chain 'H' and (resid 87 through 103 )
51X-RAY DIFFRACTION51chain 'H' and (resid 104 through 121 )
52X-RAY DIFFRACTION52chain 'L' and (resid 32 through 52 )
53X-RAY DIFFRACTION53chain 'L' and (resid 53 through 62 )
54X-RAY DIFFRACTION54chain 'L' and (resid 63 through 73 )
55X-RAY DIFFRACTION55chain 'L' and (resid 74 through 103 )
56X-RAY DIFFRACTION56chain 'L' and (resid 104 through 120 )
57X-RAY DIFFRACTION57chain 'B' and (resid 32 through 52 )
58X-RAY DIFFRACTION58chain 'B' and (resid 53 through 73 )
59X-RAY DIFFRACTION59chain 'B' and (resid 74 through 104 )
60X-RAY DIFFRACTION60chain 'B' and (resid 105 through 120 )
61X-RAY DIFFRACTION61chain 'F' and (resid 32 through 73 )
62X-RAY DIFFRACTION62chain 'F' and (resid 74 through 122 )
63X-RAY DIFFRACTION63chain 'J' and (resid 32 through 73 )
64X-RAY DIFFRACTION64chain 'J' and (resid 74 through 105 )
65X-RAY DIFFRACTION65chain 'J' and (resid 106 through 121 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more