BMRB Entry 51293

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51293

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Title:
1H, 15N, and 13C Chemical Shift Backbone Resonance NMR Assignment of Accumulation-Associated Protein (Aap) Lectin Domain from Staphylococcus epidermidis
Deposition date:
2022-01-25
Original release date:
2023-06-29
Authors:
Yadav, Rahul; Shaikh, Tanveer; Tikole, Suhas; Fitzkee, Nicholas
Citation:

Citation: Yadav, Rahul; Shaikh, Tanveer; Tikole, Suhas; Herr, Andrew; Fitzkee, Nicholas. "1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis"  Biomol. NMR Assignments 17, 95-99 (2023).
PubMed: 37022616

Assembly members:

Assembly members:
entity_1, polymer, 253 residues, 27525.84 Da.

Natural source:

Natural source:   Common Name: Staphylococcus epidermidis   Taxonomy ID: 1282   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus epidermidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST-HisMBP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IPPTTVKGRDNYDFYGRVDI ESNPTDLNATNLTRYNYGQP PGTTTAGAVQFKNQVSFDKD FDFNIRVANNRQSNTTGADG WGFMFSKKDGDDFLKNGGIL REKGTPSAAGFRIDTGYYNN DPLDKIQKQAGQGYRGYGTF VKNDSQGNTSKVGSGTPSTD FLNYADNTTNDLDGKFHGQK LNNVNLKYNASNQTFTATYA GKTWTATLSELGLSPTDSYN FLVTSSQYGNGNSGTYASGV MRADLDGATLTYT

Data sets:
Data typeCount
13C chemical shifts577
15N chemical shifts216
1H chemical shifts216

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lectin Domain of (Aap)1

Entities:

Entity 1, Lectin Domain of (Aap) 253 residues - 27525.84 Da.

Ile 353 - Thr 605

1   ILEPROPROTHRTHRVALLYSGLYARGASP
2   ASNTYRASPPHETYRGLYARGVALASPILE
3   GLUSERASNPROTHRASPLEUASNALATHR
4   ASNLEUTHRARGTYRASNTYRGLYGLNPRO
5   PROGLYTHRTHRTHRALAGLYALAVALGLN
6   PHELYSASNGLNVALSERPHEASPLYSASP
7   PHEASPPHEASNILEARGVALALAASNASN
8   ARGGLNSERASNTHRTHRGLYALAASPGLY
9   TRPGLYPHEMETPHESERLYSLYSASPGLY
10   ASPASPPHELEULYSASNGLYGLYILELEU
11   ARGGLULYSGLYTHRPROSERALAALAGLY
12   PHEARGILEASPTHRGLYTYRTYRASNASN
13   ASPPROLEUASPLYSILEGLNLYSGLNALA
14   GLYGLNGLYTYRARGGLYTYRGLYTHRPHE
15   VALLYSASNASPSERGLNGLYASNTHRSER
16   LYSVALGLYSERGLYTHRPROSERTHRASP
17   PHELEUASNTYRALAASPASNTHRTHRASN
18   ASPLEUASPGLYLYSPHEHISGLYGLNLYS
19   LEUASNASNVALASNLEULYSTYRASNALA
20   SERASNGLNTHRPHETHRALATHRTYRALA
21   GLYLYSTHRTRPTHRALATHRLEUSERGLU
22   LEUGLYLEUSERPROTHRASPSERTYRASN
23   PHELEUVALTHRSERSERGLNTYRGLYASN
24   GLYASNSERGLYTHRTYRALASERGLYVAL
25   METARGALAASPLEUASPGLYALATHRLEU
26   THRTYRTHR

Samples:

sample_1: Lectin Domain of (Aap), [U-99% 15N], 600 ± 20 uM; Lectin Domain of (Aap), [U-99% 13C; U-99% 15N], 800 ± 30 uM; Sodium Phosphate 20 mM; Sodium Chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6.1 - collection

NMRPipe - processing

CARA v1.9.1.7 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Related Database Links:

NCBI WP_010959349.1

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