BMRB Entry 52205

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52205

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Title:
MrkA monomer of Klebsiella pneumoniae type III fimbriae
Deposition date:
2023-11-10
Original release date:
2024-08-05
Authors:
Monaci, Valentina; Cantini, Francesca; Micoli, Francesca; Gasperini, Gianmarco
Citation:

Citation: Monaci, Valentina; Gasperini, Gianmarco; Banci, Lucia; Micoli, Francesca; Cantini, Francesca. "1H, 13C and 15N assignment of self-complemented MrkA protein antigen from Klebsiella pneumoniae"  Biomol. NMR Assignments ., .-. (2024).
PubMed: 39018011

Assembly members:

Assembly members:
entity_1, polymer, 201 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Klebsiella pneumoniae   Taxonomy ID: 573   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Klebsiella pneumoniae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSHHHHHHHHHHGSCTVSV NGQGSDANVYLSPVTLTEVK AAAADTYLKPKSFTIDVSNC QAADGTKQDDVSKLGVNWTG GNLLAGATSKQQGYLANTEA SGAQNIQLVLSTDNATALTN KIIPGDSTQPKAKGDASAVA DGARFTYYVGYATSAPTTVT TGVVNSYATYEITYQGGGGG GADTTVGGGQVNFFGKVTDV S

Data sets:
Data typeCount
13C chemical shifts716
15N chemical shifts201
1H chemical shifts1173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MrkA monomer1

Entities:

Entity 1, MrkA monomer 201 residues - Formula weight is not available

1   METGLYSERHISHISHISHISHISHISHIS
2   HISHISHISGLYSERCYSTHRVALSERVAL
3   ASNGLYGLNGLYSERASPALAASNVALTYR
4   LEUSERPROVALTHRLEUTHRGLUVALLYS
5   ALAALAALAALAASPTHRTYRLEULYSPRO
6   LYSSERPHETHRILEASPVALSERASNCYS
7   GLNALAALAASPGLYTHRLYSGLNASPASP
8   VALSERLYSLEUGLYVALASNTRPTHRGLY
9   GLYASNLEULEUALAGLYALATHRSERLYS
10   GLNGLNGLYTYRLEUALAASNTHRGLUALA
11   SERGLYALAGLNASNILEGLNLEUVALLEU
12   SERTHRASPASNALATHRALALEUTHRASN
13   LYSILEILEPROGLYASPSERTHRGLNPRO
14   LYSALALYSGLYASPALASERALAVALALA
15   ASPGLYALAARGPHETHRTYRTYRVALGLY
16   TYRALATHRSERALAPROTHRTHRVALTHR
17   THRGLYVALVALASNSERTYRALATHRTYR
18   GLUILETHRTYRGLNGLYGLYGLYGLYGLY
19   GLYALAASPTHRTHRVALGLYGLYGLYGLN
20   VALASNPHEPHEGLYLYSVALTHRASPVAL
21   SER

Samples:

sample_1: MrkA monomer, [U-99% 15N], 450 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: MrkA monomer, [U-99% 13C; U-99% 15N], 400 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D CBCACONHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
(H)CCH-TOCSY 3Dsample_2isotropicsample_conditions_1
HBHA(CBCACO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1

Software:

CARA v1.9 - chemical shift assignment

TOPSPIN v4.0.6 - processing

PINE - chemical shift assignment

TALOS-N - collection of backbone dihedral angles

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz

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