BMRB Entry 30975

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/BMR30975
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:
Truncated Ac-AIP-2
Deposition date:
2021-12-13
Original release date:
2022-10-13
Authors:
Daly, N.; Cobos, C.
Citation:

Citation: Cobos Caceres, C.; Bansal, P.; Wilson, D.; Jones, L.; Zhao, G.; Field, M.; Eichenberger, R.; Pickering, D.; Ryan, R.; Ratnatunga, C.; Miles, J.; Ruscher, R.; Giacomin, P.; Navarro, S.; Loukas, A.; Daly, N.. "Peptides derived from hookworm anti-inflammatory proteins suppress inducible colitis in mice and inflammatory cytokine production by human cells"  Front. Med. (Lausanne) 9, 934852-934852 (2022).
PubMed: 36186812

Assembly members:

Assembly members:
entity_1, polymer, 20 residues, 2301.568 Da.

Natural source:

Natural source:   Common Name: dog hookworm   Taxonomy ID: 29170   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Ancylostoma caninum

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TPEEHDLLMDLMGDPKKAEE

Data sets:
Data typeCount
13C chemical shifts10
15N chemical shifts11
1H chemical shifts117

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 20 residues - 2301.568 Da.

1   THRPROGLUGLUHISASPLEULEUMETASP
2   LEUMETGLYASPPROLYSLYSALAGLUGLU

Samples:

sample_1: AIP2-20 0.5 mM

sample_conditions_1: ionic strength: 0 Not defined; pH: 4; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1
2D 1H-1H COSYsample_1anisotropicsample_conditions_1
2D 1H-1H TOCSYsample_1anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

CcpNmr Analysis v3.98.13, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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