BMRB Entry 30583

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30583
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags
Deposition date:
2019-03-06
Original release date:
2019-07-18
Authors:
Bahramzadeh, A.; Huber, T.; Otting, G.
Citation:

Citation: Bahramzadeh, A.; Huber, T.; Otting, G.. "3D protein structure determination using pseudocontact shifts of backbone amide protons generated by double-histidine Co2+-binding motifs at multiple sites."  Biochemistry 58, 3243-3250 (2019).
PubMed: 31282649

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, 11787.470 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pETMCSI

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PGCLPAYDALAGQFIEASSR EARQAILKQGQDGLSGVKET DKKWASQYLKIMGKILDQGE DFPASELARISKLIENKMSE GKKEELQRSLNILTAFRKKG AEKEEL

Data sets:
Data typeCount
13C chemical shifts297
15N chemical shifts103
1H chemical shifts103

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 106 residues - 11787.470 Da.

1   PROGLYCYSLEUPROALATYRASPALALEU
2   ALAGLYGLNPHEILEGLUALASERSERARG
3   GLUALAARGGLNALAILELEULYSGLNGLY
4   GLNASPGLYLEUSERGLYVALLYSGLUTHR
5   ASPLYSLYSTRPALASERGLNTYRLEULYS
6   ILEMETGLYLYSILELEUASPGLNGLYGLU
7   ASPPHEPROALASERGLULEUALAARGILE
8   SERLYSLEUILEGLUASNLYSMETSERGLU
9   GLYLYSLYSGLUGLULEUGLNARGSERLEU
10   ASNILELEUTHRALAPHEARGLYSLYSGLY
11   ALAGLULYSGLUGLULEU

Samples:

sample_1: ERp29-C, [U-13C; U-15N], 0.258 ± 0.002 mM

sample_2: ERp29-C, [U-13C; U-15N], 0.135 ± 0.002 mM

sample_3: ERp29-C, [U-13C; U-15N], 0.153 ± 0.002 mM

sample_4: ERp29-C, [U-13C; U-15N], 0.320 ± 0.002 mM

sample_5: ERp29-C, [U-13C; U-15N], 0.935 ± 0.002 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N HSQCsample_4anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_conditions_1
3D HNCACOsample_5isotropicsample_conditions_1
3D HNCAsample_5isotropicsample_conditions_1
3D HNCACBsample_5isotropicsample_conditions_1
3D HN(COCA)CBsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

GPS-Rosetta, Thomas Huber - structure calculation

CcpNMR, CCPN - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE II 800 MHz

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