BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 30826

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/BMR30826
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: NMR solution structure of Nak1 from the Necator americanus hookworm   PubMed: 34051231

Deposition date: 2020-12-17 Original release date: 2021-10-22

Authors: Smallwood, T.; Rosengren, K.; Clark, R.

Citation: Smallwood, Taylor; Navarro, Severine; Cristofori-Armstrong, Ben; Watkins, Thomas; Tungatt, Katie; Ryan, Rachael; Haigh, Oscar; Lutzky, Viviana; Mulvenna, Jason; Rosengren, K Johan; Loukas, Alex; Miles, John; Clark, Richard. "Synthetic hookworm-derived peptides are potent modulators of primary human immune cell function that protect against experimental colitis in vivo"  J. Biol. Chem. 297, 100834-100834 (2021).

Assembly members:
entity_1, polymer, 40 residues, 4377.214 Da.

Natural source:   Common Name: Human hookworm   Taxonomy ID: 51031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Necator americanus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: CRDRIPQNVCEQMKKNGKCG DPRMSTIAELQCPKTCGKCX

Data sets:
Data typeCount
13C chemical shifts117
15N chemical shifts41
1H chemical shifts255

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 40 residues - 4377.214 Da.

1   CYSARGASPARGILEPROGLNASNVALCYS
2   GLUGLNMETLYSLYSASNGLYLYSCYSGLY
3   ASPPROARGMETSERTHRILEALAGLULEU
4   GLNCYSPROLYSTHRCYSGLYLYSCYSNH2

Samples:

sample_1: Nak1 1 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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