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- PDB-5a0q: Cryo-EM reveals the conformation of a substrate analogue in the h... -

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Entry
Database: PDB / ID: 5a0q
TitleCryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
Components
  • (PROTEASOME SUBUNIT ALPHA TYPE- ...) x 7
  • (PROTEASOME SUBUNIT BETA TYPE- ...) x 7
KeywordsHYDROLASE / PROTEASOME / 20S / ADAAHX3L3VS / LIGAND / INHIBITOR / DRUG DESIGN
Function / homology
Function and homology information


purine ribonucleoside triphosphate binding / CD8-positive, alpha-beta T cell differentiation / CD8-positive, alpha-beta T cell homeostasis / thymic T cell selection / Antigen processing: Ub, ATP-independent proteasomal degradation / negative regulation of regulatory T cell differentiation / T-helper 1 cell differentiation / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Proteasome assembly ...purine ribonucleoside triphosphate binding / CD8-positive, alpha-beta T cell differentiation / CD8-positive, alpha-beta T cell homeostasis / thymic T cell selection / Antigen processing: Ub, ATP-independent proteasomal degradation / negative regulation of regulatory T cell differentiation / T-helper 1 cell differentiation / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Proteasome assembly / cellular response to type I interferon / T-helper 17 cell differentiation / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / flagellated sperm motility / sperm end piece / myofibril / ciliary tip / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / proteasome endopeptidase complex / NF-kappaB binding / proteasome core complex, beta-subunit complex / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / proteasome assembly / immune system process / regulation of G1/S transition of mitotic cell cycle / proteasome complex / positive regulation of interleukin-2 production / response to type II interferon / : / regulation of proteasomal protein catabolic process / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / negative regulation of inflammatory response to antigenic stimulus / proteasomal protein catabolic process / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / lipopolysaccharide binding / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / positive regulation of type II interferon production / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / P-body / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of DVL / Degradation of AXIN / Degradation of CRY and PER proteins / meiotic cell cycle / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / G2/M Checkpoints / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Autodegradation of the E3 ubiquitin ligase COP1 / Regulation of RUNX3 expression and activity / Defective CFTR causes cystic fibrosis / response to virus / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) / Hedgehog 'on' state / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Vif-mediated degradation of APOBEC3G / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / GSK3B-mediated proteasomal degradation of PD-L1(CD274) / Degradation of CDH1 / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / ABC-family protein mediated transport / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / FCERI mediated NF-kB activation / SPOP-mediated proteasomal degradation of PD-L1(CD274) / nuclear matrix / Regulation of expression of SLITs and ROBOs / Regulation of PTEN stability and activity / Interleukin-1 signaling / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / Orc1 removal from chromatin / Regulation of RUNX2 expression and activity / Regulation of RAS by GAPs / positive regulation of tumor necrosis factor production / The role of GTSE1 in G2/M progression after G2 checkpoint / Separation of Sister Chromatids / peptidase activity / KEAP1-NFE2L2 pathway / UCH proteinases
Similarity search - Function
Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha5 / Proteasome subunit alpha6 ...Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha5 / Proteasome subunit alpha6 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome B-type subunit / Proteasome beta-type subunit profile. / : / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADA-(AHX)3-(LEU)3-VINYL SULFONE / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 ...ADA-(AHX)3-(LEU)3-VINYL SULFONE / Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-6 / Proteasome subunit beta type-7
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsdaFonseca, P.C.A. / Morris, E.P.
CitationJournal: Nat Commun / Year: 2015
Title: Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.
Authors: Paula C A da Fonseca / Edward P Morris /
Abstract: The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, ...The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 Å. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions.
History
DepositionApr 22, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 30, 2015Provider: repository / Type: Initial release
Revision 1.1Aug 2, 2017Group: Data collection / Category: em_software
Item: _em_software.fitting_id / _em_software.image_processing_id / _em_software.name
Revision 1.2Nov 6, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_modification_feature / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Movie
  • Deposited structure unit
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  • Superimposition on EM map
  • EMDB-2981
  • Imaged by UCSF Chimera
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  • Superimposition on EM map
  • EMDB-2981
  • Imaged by UCSF Chimera
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEASOME SUBUNIT ALPHA TYPE-6
B: PROTEASOME SUBUNIT ALPHA TYPE-2
C: PROTEASOME SUBUNIT ALPHA TYPE-4
D: PROTEASOME SUBUNIT ALPHA TYPE-7
E: PROTEASOME SUBUNIT ALPHA TYPE-5
F: PROTEASOME SUBUNIT ALPHA TYPE-1
G: PROTEASOME SUBUNIT ALPHA TYPE-3
H: PROTEASOME SUBUNIT BETA TYPE-6
I: PROTEASOME SUBUNIT BETA TYPE-7
J: PROTEASOME SUBUNIT BETA TYPE-3
K: PROTEASOME SUBUNIT BETA TYPE-2
L: PROTEASOME SUBUNIT BETA TYPE-5
M: PROTEASOME SUBUNIT BETA TYPE-1
N: PROTEASOME SUBUNIT BETA TYPE-4
O: PROTEASOME SUBUNIT ALPHA TYPE-6
P: PROTEASOME SUBUNIT ALPHA TYPE-2
Q: PROTEASOME SUBUNIT ALPHA TYPE-4
R: PROTEASOME SUBUNIT ALPHA TYPE-7
S: PROTEASOME SUBUNIT ALPHA TYPE-5
T: PROTEASOME SUBUNIT ALPHA TYPE-1
U: PROTEASOME SUBUNIT ALPHA TYPE-3
V: PROTEASOME SUBUNIT BETA TYPE-6
W: PROTEASOME SUBUNIT BETA TYPE-7
X: PROTEASOME SUBUNIT BETA TYPE-3
Y: PROTEASOME SUBUNIT BETA TYPE-2
Z: PROTEASOME SUBUNIT BETA TYPE-5
a: PROTEASOME SUBUNIT BETA TYPE-1
b: PROTEASOME SUBUNIT BETA TYPE-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)723,18534
Polymers717,48928
Non-polymers5,6966
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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PROTEASOME SUBUNIT ALPHA TYPE- ... , 7 types, 14 molecules AOBPCQDRESFTGU

#1: Protein PROTEASOME SUBUNIT ALPHA TYPE-6 / 27 KDA PROSOMAL PROTEIN / P27K / MACROPAIN IOTA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA ...27 KDA PROSOMAL PROTEIN / P27K / MACROPAIN IOTA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN / PROTEASOME IOTA CHAIN


Mass: 27432.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P60900, proteasome endopeptidase complex
#2: Protein PROTEASOME SUBUNIT ALPHA TYPE-2 / MACROPAIN SUBUNIT C3 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C3 / PROTEASOME COMPONENT C3


Mass: 25927.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P25787, proteasome endopeptidase complex
#3: Protein PROTEASOME SUBUNIT ALPHA TYPE-4 / MACROPAIN SUBUNIT C9 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C9 / PROTEASOME COMPONENT C9 / ...MACROPAIN SUBUNIT C9 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C9 / PROTEASOME COMPONENT C9 / PROTEASOME SUBUNIT L


Mass: 29525.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P25789, proteasome endopeptidase complex
#4: Protein PROTEASOME SUBUNIT ALPHA TYPE-7 / PROTEASOME SUBUNIT RC6-1 / PROTEASOME SUBUNIT XAPC7


Mass: 27929.891 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: O14818, proteasome endopeptidase complex
#5: Protein PROTEASOME SUBUNIT ALPHA TYPE-5 / MACROPAIN ZETA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX ZETA CHAIN / PROTEASOME ZETA CHAIN


Mass: 26435.977 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P28066, proteasome endopeptidase complex
#6: Protein PROTEASOME SUBUNIT ALPHA TYPE-1 / 30 KDA PROSOMAL PROTEIN / PROS-30 / MACROPAIN SUBUNIT C2 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX ...30 KDA PROSOMAL PROTEIN / PROS-30 / MACROPAIN SUBUNIT C2 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2 / PROTEASOME COMPONENT C2 / PROTEASOME NU CHAIN


Mass: 29595.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P25786, proteasome endopeptidase complex
#7: Protein PROTEASOME SUBUNIT ALPHA TYPE-3 / MACROPAIN SUBUNIT C8 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C8 / PROTEASOME COMPONENT C8


Mass: 28469.252 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P25788, proteasome endopeptidase complex

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PROTEASOME SUBUNIT BETA TYPE- ... , 7 types, 14 molecules HVIWJXKYLZMaNb

#8: Protein PROTEASOME SUBUNIT BETA TYPE-6 / MACROPAIN DELTA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX DELTA CHAIN / PROTEASOME DELTA CHAIN / ...MACROPAIN DELTA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX DELTA CHAIN / PROTEASOME DELTA CHAIN / PROTEASOME SUBUNIT Y


Mass: 21921.836 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: SUBUNIT PARTIALLY BOUND TO THE INHIBITOR ADAMANTANE-ACETYL-(6-AMINOHEXANOYL)3-(LEUCINYL)3-VINYL-(METHYL)-SULFONE (ADAAHX3L3VS)
Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P28072, proteasome endopeptidase complex
#9: Protein PROTEASOME SUBUNIT BETA TYPE-7 / MACROPAIN CHAIN Z / MULTICATALYTIC ENDOPEPTIDASE COMPLEX CHAIN Z / PROTEASOME SUBUNIT Z


Mass: 25321.980 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: SUBUNIT PARTIALLY BOUND TO THE INHIBITOR ADAMANTANE-ACETYL-(6-AMINOHEXANOYL)3-(LEUCINYL)3-VINYL-(METHYL)-SULFONE (ADAAHX3L3VS)
Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: Q99436, proteasome endopeptidase complex
#10: Protein PROTEASOME SUBUNIT BETA TYPE-3 / PROTEASOME CHAIN 13 / PROTEASOME COMPONENT C10-II / PROTEASOME THETA CHAIN


Mass: 22841.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P49720, proteasome endopeptidase complex
#11: Protein PROTEASOME SUBUNIT BETA TYPE-2 / MACROPAIN SUBUNIT C7-I / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C7-I / PROTEASOME COMPONENT C7-I


Mass: 22864.277 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P49721, proteasome endopeptidase complex
#12: Protein PROTEASOME SUBUNIT BETA TYPE-5 / MACROPAIN EPSILON CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX EPSILON CHAIN / PROTEASOME CHAIN 6 / ...MACROPAIN EPSILON CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX EPSILON CHAIN / PROTEASOME CHAIN 6 / PROTEASOME EPSILON CHAIN / PROTEASOME SUBUNIT MB1 / PROTEASOME SUBUNIT X


Mass: 22484.369 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: SUBUNIT BOUND TO THE INHIBITOR ADAMANTANE-ACETYL-(6-AMINOHEXANOYL)3-(LEUCINYL)3-VINYL-(METHYL)-SULFONE (ADAAHX3L3VS)
Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P28074, proteasome endopeptidase complex
#13: Protein PROTEASOME SUBUNIT BETA TYPE-1 / MACROPAIN SUBUNIT C5 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5 / PROTEASOME COMPONENT C5 / ...MACROPAIN SUBUNIT C5 / MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5 / PROTEASOME COMPONENT C5 / PROTEASOME GAMMA CHAIN


Mass: 23578.986 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P20618, proteasome endopeptidase complex
#14: Protein PROTEASOME SUBUNIT BETA TYPE-4 / 26 KDA PROSOMAL PROTEIN / PROS-26 / MACROPAIN BETA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX ...26 KDA PROSOMAL PROTEIN / PROS-26 / MACROPAIN BETA CHAIN / MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN / PROTEASOME BETA CHAIN / PROTEASOME CHAIN 3 / HSN3


Mass: 24414.740 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES
References: UniProt: P28070, proteasome endopeptidase complex

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Non-polymers , 1 types, 6 molecules

#15: Chemical
ChemComp-KNM / ADA-(AHX)3-(LEU)3-VINYL SULFONE


Mass: 949.377 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C51H92N6O8S

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Details

Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: HUMAN 20S PROTEASOME CORE / Type: COMPLEX
Details: THE POWER SPECTRA OF THE IMAGES SELECTED FOR ANALYSIS HAD ISOTROPIC THON RINGS DIRECTLY OBSERVED TO 4 ANGSTROMS OR BETTER
Buffer solutionName: 50 MM TRIS-HCL, 5 MM MGCL2 AND 1MM DITHIOTREITOL / pH: 7.5 / Details: 50 MM TRIS-HCL, 5 MM MGCL2 AND 1MM DITHIOTREITOL
SpecimenConc.: 0.1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: CARBON
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE
Details: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 120, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT 2. 5 SECONDS BEFORE PLUNGING,

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS / Date: Feb 4, 2014
Details: EACH EXPOSURE WAS RECORDED AS 17 INDIVIDUAL FRAMES CAPTURED AT A RATE OF 0.056 SECONDS PER FRAME, WITH AN ELECTRON DOSE OF 2.8 ELECTRONS PER SQUARE ANGSTROM. DATA-SET RECORDED USING EPU SOFTWARE.
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 75000 X / Calibrated magnification: 134461 X / Nominal defocus max: 3000 nm / Nominal defocus min: 1700 nm / Cs: 2.7 mm
Specimen holderTemperature: 85 K
Image recordingElectron dose: 4.8 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k)
Image scansNum. digital images: 960

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Processing

EM software
IDNameCategory
1Cootmodel fitting
2PHENIXmodel fitting
3IMAGIC3D reconstruction
4SPIDER3D reconstruction
5TIGRIS3D reconstruction
CTF correctionDetails: FULL RECORDED IMAGE
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionMethod: PROJECTION MATCHING / Resolution: 3.5 Å / Num. of particles: 76500 / Actual pixel size: 1.04 Å
Details: DISORDERED REGIONS, NOT RECOVERED IN THE EM MAP, WHERE NOT MODELED. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2981. (DEPOSITION ID: 13310).
Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL / Details: METHOD--FLEXIBLE
Atomic model buildingPDB-ID: 3UNE

3une


Accession code: 3UNE / Source name: PDB / Type: experimental model
RefinementHighest resolution: 3.5 Å
Refinement stepCycle: LAST / Highest resolution: 3.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms43264 0 184 0 43448

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