BMRB Entry 4920

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4920
MolProbity Validation Chart

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Title:
Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer
Deposition date:
2000-12-13
Original release date:
2001-08-08
Authors:
Liepinsh, Edvards; Baryshev, Michail; Sharipo, Anatoly; Ingelman-Sundberg, Magnus; Otting, Gottfried; Mkrtchian, Souren
Citation:

Citation: Liepinsh, Edvards; Baryshev, Michail; Sharipo, Anatoly; Ingelman-Sundberg, Magnus; Otting, Gottfried; Mkrtchian, Souren. "Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer"  Structure 9, 457-471 (2001).
PubMed: 11435111

Assembly members:

Assembly members:
Endoplasmic reticulum protein p29, polymer, 120 residues, 13478 Da.

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Endoplasmic reticulum protein p29: MRGSHHHHHHGIRMPGCLPA YDALAGQFIEASSREARQAI LKQGQDGLSGVKETDKKWAS QYLKIMGKILDQGEDFPASE LARISKLIENKMSEGKKEEL QRSLNILTAFRKKGAEKEEL

Data sets:
Data typeCount
1H chemical shifts838
13C chemical shifts224
15N chemical shifts127

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ERp29 C-domain1

Entities:

Entity 1, ERp29 C-domain 120 residues - 13478 Da.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYILEARGMETPROGLYCYSLEUPROALA
3   TYRASPALALEUALAGLYGLNPHEILEGLU
4   ALASERSERARGGLUALAARGGLNALAILE
5   LEULYSGLNGLYGLNASPGLYLEUSERGLY
6   VALLYSGLUTHRASPLYSLYSTRPALASER
7   GLNTYRLEULYSILEMETGLYLYSILELEU
8   ASPGLNGLYGLUASPPHEPROALASERGLU
9   LEUALAARGILESERLYSLEUILEGLUASN
10   LYSMETSERGLUGLYLYSLYSGLUGLULEU
11   GLNARGSERLEUASNILELEUTHRALAPHE
12   ARGLYSLYSGLYALAGLULYSGLUGLULEU

Samples:

sample_1: Endoplasmic reticulum protein p29, [U-15N; U-13C], 2 mM

sample_2: Endoplasmic reticulum protein p29 2 mM

Ex-cond_1: pH: 4.9; temperature: 308 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H COSYnot availablenot availablenot available
2D 1H-1H CLEAN TOCSYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HNCOnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Varian UnityPlus 800 MHz

Related Database Links:

PDB
EMBL CAA71313
GB AAC15239 AAF93170 AAH91129 EDM13737 EDM13738
REF NP_446413
SP P52555
AlphaFold P52555

Download HSQC peak lists in one of the following formats:
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SPARKY: Backbone or all simulated peaks