BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30040

Title: Cell surface anchoring domain

Deposition date: 2016-03-23 Original release date: 2017-06-22

Authors: Guo, S.; Langelaan, D.

Citation: Guo, S.; Langelaan, D.; Phippen, S.; Smith, S.; Davies, P.. "Structural insight into host cell surface retention of a 1.5-MDa bacterial ice-binding adhesin"  . ., .-..

Assembly members:
Antifreeze protein, polymer, 76 residues, 7826.605 Da.

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 178399   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Marinomonas primoryensis

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

Entity Sequences (FASTA):
Antifreeze protein: GNAIGFITKLDGSVTVQSIN GQERVLKLGDPIFFGETVLT GGSGSVTIAFVDGTDVVIGG DSIVEMTDEIYNTGDN

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts82
1H chemical shifts490

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 76 residues - 7826.605 Da.

1   GLYASNALAILEGLYPHEILETHRLYSLEU
2   ASPGLYSERVALTHRVALGLNSERILEASN
3   GLYGLNGLUARGVALLEULYSLEUGLYASP
4   PROILEPHEPHEGLYGLUTHRVALLEUTHR
5   GLYGLYSERGLYSERVALTHRILEALAPHE
6   VALASPGLYTHRASPVALVALILEGLYGLY
7   ASPSERILEVALGLUMETTHRASPGLUILE
8   TYRASNTHRGLYASPASN

Samples:

sample_1: CaCl2 2 mM; MgCl2 2 mM; MpAFP_RINM, [U-13C], 3 mM; TRIS 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

Analysis, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

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