BMRB Entry 16902

Title:
Backbone 1H, 15N, 13C and ile, leu, val sidechain CH3 Chemical Shift assignments for Aagglutinin-like ALS1 N-terminal domain
Deposition date:
2010-04-27
Original release date:
2010-07-26
Authors:
Yan, Robert; Cota, Ernesto
Citation:

Citation: Yan, Robert; Simpson, Peter; Matthews, Stephen; Cota, Ernesto. "Backbone 1H, 15N, 13C and Ile, Leu, Val methyl chemical shift assignments for the 33.5 kDa N-terminal domain of Candida albicans ALS1."  Biomol. NMR Assignments 4, 187-190 (2010).
PubMed: 20556550

Assembly members:

Assembly members:
ALS1, polymer, 312 residues, 33556.0 Da.

Natural source:

Natural source:   Common Name: Ascomycetes   Taxonomy ID: 5476   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Candida albicans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32 Xa/LIC

Data sets:
Data typeCount
13C chemical shifts941
15N chemical shifts291
1H chemical shifts547

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ALS11

Entities:

Entity 1, ALS1 312 residues - 33556.0 Da.

Residues 18-329 of ALS1. This is the adhesion domain from full length protein

1   LYSTHRILETHRGLYVALPHEASPSERPHE
2   ASNSERLEUTHRTRPSERASNALAALAASN
3   TYRALAPHELYSGLYPROGLYTYRPROTHR
4   TRPASNALAVALLEUGLYTRPSERLEUASP
5   GLYTHRSERALAASNPROGLYASPTHRPHE
6   THRLEUASNMETPROCYSVALPHELYSTYR
7   THRTHRSERGLNTHRSERVALASPLEUTHR
8   ALAASPGLYVALLYSTYRALATHRCYSGLN
9   PHETYRSERGLYGLUGLUPHETHRTHRPHE
10   SERTHRLEUTHRCYSTHRVALASNASPALA
11   LEULYSSERSERILELYSALAPHEGLYTHR
12   VALTHRLEUPROILEALAPHEASNVALGLY
13   GLYTHRGLYSERSERTHRASPLEUGLUASP
14   SERLYSCYSPHETHRALAGLYTHRASNTHR
15   VALTHRPHEASNASPGLYASPLYSASPILE
16   SERILEASPVALGLUPHEGLULYSSERTHR
17   VALASPPROSERGLYTYRLEUTYRALASER
18   ARGVALMETPROSERLEUASNLYSVALTHR
19   THRLEUPHEVALALAPROGLNCYSGLUASN
20   GLYTYRTHRSERGLYTHRMETGLYPHESER
21   SERSERASNGLYASPVALALAILEASPCYS
22   SERASNILEHISILEGLYILETHRLYSGLY
23   LEUASNASPTRPASNTYRPROVALSERSER
24   GLUSERPHESERTYRTHRLYSTHRCYSTHR
25   SERASNGLYILEGLNILELYSTYRGLNASN
26   VALPROALAGLYTYRARGPROPHEILEASP
27   ALATYRILESERALATHRASPVALASNGLN
28   TYRTHRLEUALATYRTHRASNASPTYRTHR
29   CYSALAGLYSERARGSERGLNSERLYSPRO
30   PHETHRLEUARGTRPTHRGLYTYRLYSASN
31   SERASPALAGLYSERASNGLYILEVALILE
32   VALALA

Samples:

sample_1: ALS1, [U-100% 13C; U-100% 15N; U-80% 2H], 500 uM; H2O 90%; D2O 10%; Sodium Phosphate 50 mM; Sodium Chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D TROSY 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D TROSY HNCACBsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1
3D TROSY HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY 1H-15N NOESYsample_1isotropicsample_conditions_1
3D SIMULTANEOUS 1H-15N/13C NOESYsample_1isotropicsample_conditions_1
3D TROSY H(CCCO)NH TOCSYsample_1isotropicsample_conditions_1
3D TROSY (H)C(CCO)NH TOCSYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

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