BMRB Entry 30422

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30422
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure of the zebrafish granulin AaE
Deposition date:
2018-02-28
Original release date:
2018-06-07
Authors:
Wang, P.; Ni, F.
Citation:

Citation: Wang, P.; Chitramuthu, B.; Bateman, A.; Bennett, H.; Xu, P.; Ni, F.. "Structure Dissection of Zebrafish Progranulins Identifies a Well-Folded Granulin/Epithelin Module Protein with pro-Cell Survival Activities"  Protein Science 27, 1476-1490 (2018).
PubMed: 29732682

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, 5698.431 Da.

Natural source:

Natural source:   Common Name: Zebrafish   Taxonomy ID: 7955   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Danio rerio

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DVQCGGGFSCHDGETCCPTS QTTWGCCPSPKAVCCDDMQH CCPAGYKCGPGGTCIS

Data sets:
Data typeCount
15N chemical shifts55
1H chemical shifts302

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 56 residues - 5698.431 Da.

1   ASPVALGLNCYSGLYGLYGLYPHESERCYS
2   HISASPGLYGLUTHRCYSCYSPROTHRSER
3   GLNTHRTHRTRPGLYCYSCYSPROSERPRO
4   LYSALAVALCYSCYSASPASPMETGLNHIS
5   CYSCYSPROALAGLYTYRLYSCYSGLYPRO
6   GLYGLYTHRCYSILESER

Samples:

sample_1: zebrafish granulin AaE 0.5 mM; sodium chloride 150 mM; EDTA 0.2 mM

sample_2: zebrafish granulin AaE, [U-15N], 0.5 mM; sodium chloride 150 mM; EDTA 0.2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 760 mmHg; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1

Software:

CNS v1.0, Brunger et al. - refinement, structure calculation

ARIA, Nilges et al. - refinement, structure calculation

NMRView, Johnson et al. - chemical shift assignment

NMRview, Johnson et al. - peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

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