BMRB Entry 17104

Title:
YP_001336205.1
Deposition date:
2010-08-05
Original release date:
2010-08-18
Authors:
Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wilson, Ian; Wuthrich, Kurt
Citation:

Citation: Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the Klebsiella pneumoniae protein YP_001336205"  .

Assembly members:

Assembly members:
YP_001336205.1, polymer, 83 residues, 9498.662 Da.

Natural source:

Natural source:   Common Name: enterobacteria   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: pSpeedET

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts87
1H chemical shifts575

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_001336205.11

Entities:

Entity 1, YP_001336205.1 83 residues - 9498.662 Da.

1   GLYALAALAGLYILEASPGLNTYRALALEU
2   LYSGLUPHETHRALAASPPHETHRGLNPHE
3   HISILEGLYASPTHRVALPROALAMETTYR
4   LEUTHRPROGLUTYRASNILELYSGLNTRP
5   GLNGLNARGASNLEUPROALAPROASPALA
6   GLYSERHISTRPTHRTYRMETGLYGLYASN
7   TYRVALLEUILETHRASPTHRGLUGLYLYS
8   ILELEULYSVALTYRASPGLYGLUILEPHE
9   TYRHISARG

Samples:

sample_1: YP_001336205.1, [U-98% 13C; U-98% 15N], 1.4 mM; sodium phosphate buffer 20 mM; sodium chloride 50 mM; sodium azide 0.005 mM; D2O, [U-99% 2H], 5%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 15N-1H HSQCsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
15N-resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13C(aliphatic)-resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13C(aromatic)-resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1

Software:

UNIO v2.0.0, Torsten Herrmann - chemical shift assignment, peak picking, structure calculation

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - Structure calculation

TOPSPIN v1.3, Bruker Biospin - data collection, processing

Molmol, Koradi, Billeter and Wuthrich - analysis and display of molecule

CARA v1.8.4_linux, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAH64351 BAS34384
EMBL CCI75772 CCM83848 CCM88948 CCM96984 CCN30640
GB ABR77975 ACI08127 ADC57433 AEJ99058 AEW62316
REF WP_002912749 WP_004201590 WP_016946916 WP_017899344 WP_025713092

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