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- PDB-2m66: Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Pr... -

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Basic information

Entry
Database: PDB / ID: 2m66
TitleEndoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites
ComponentsEndoplasmic reticulum resident protein 29
KeywordsCHAPERONE / ERp29 / Erp29-C / GPS-Rosetta
Function / homology
Function and homology information


regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of protein secretion / protein secretion / smooth endoplasmic reticulum / response to endoplasmic reticulum stress / intracellular protein transport / melanosome / protein folding / protein-folding chaperone binding / positive regulation of protein phosphorylation ...regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of protein secretion / protein secretion / smooth endoplasmic reticulum / response to endoplasmic reticulum stress / intracellular protein transport / melanosome / protein folding / protein-folding chaperone binding / positive regulation of protein phosphorylation / endoplasmic reticulum lumen / negative regulation of gene expression / positive regulation of gene expression / cell surface / endoplasmic reticulum / protein homodimerization activity
Similarity search - Function
Endoplasmic reticulum protein erp29 / Endoplasmic reticulum resident protein 29, C-terminal domain / Endoplasmic reticulum resident protein 29, C-terminal / ERp29, N-terminal / Endoplasmic reticulum resident protein 29 / Endoplasmic reticulum resident protein 29, C-terminal domain superfamily / Endoplasmic reticulum protein ERp29, C-terminal domain / ERp29, N-terminal domain / Endoplasmic reticulum targeting sequence. / Thioredoxin-like superfamily ...Endoplasmic reticulum protein erp29 / Endoplasmic reticulum resident protein 29, C-terminal domain / Endoplasmic reticulum resident protein 29, C-terminal / ERp29, N-terminal / Endoplasmic reticulum resident protein 29 / Endoplasmic reticulum resident protein 29, C-terminal domain superfamily / Endoplasmic reticulum protein ERp29, C-terminal domain / ERp29, N-terminal domain / Endoplasmic reticulum targeting sequence. / Thioredoxin-like superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Endoplasmic reticulum resident protein 29
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / PCS-Rosetta simulated annealing
Model detailslowest energy, model1
AuthorsYagi, H. / Pilla, K. / Maleckis, A. / Graham, B. / Huber, T. / Otting, G.
CitationJournal: Structure / Year: 2013
Title: Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites
Authors: Yagi, H. / Pilla, K.B. / Maleckis, A. / Graham, B. / Huber, T. / Otting, G.
History
DepositionMar 26, 2013Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Jul 10, 2013Provider: repository / Type: Initial release
Revision 1.1May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Endoplasmic reticulum resident protein 29


Theoretical massNumber of molelcules
Total (without water)11,7871
Polymers11,7871
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)11 / 100000target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Endoplasmic reticulum resident protein 29 / ERp29 / Endoplasmic reticulum resident protein 31 / ERp31


Mass: 11787.470 Da / Num. of mol.: 1 / Fragment: UNP residues 155-260
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Erp29 / Production host: CELL-FREE SYNTHESIS (others) / References: UniProt: P52555

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D 1H-15N HSQC

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Sample preparation

DetailsContents: 0.3-0.6 mM [U-98% 15N] Endoplasmic reticulum protein 29 (ERp29)-1, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
SampleUnits: mM / Component: Endoplasmic reticulum protein 29 (ERp29)-1 / Isotopic labeling: [U-98% 15N] / Conc. range: 0.3-0.6
Sample conditionsIonic strength: 0 / pH: 4.9 / Pressure: ambient / Temperature: 304 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz

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Processing

NMR software
NameDeveloperClassification
PCS-Rosettaschmitz, vernon, otting, baker, huberstructure solution
PCS-Rosettaschmitz, vernon, otting, baker, huberrefinement
RefinementMethod: PCS-Rosetta simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100000 / Conformers submitted total number: 11 / Representative conformer: 1

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