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Biological Magnetic Resonance Data Bank


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BMRB Entry 17124

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17124
MolProbity Validation Chart

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Title: NP_888769.1   PubMed: 21520320

Deposition date: 2010-08-11 Original release date: 2011-05-04

Authors: Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wilson, Ian; Wuthrich, Kurt

Citation: Wahab, Atia-Tul; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554."  Protein Sci. 20, 1137-1144 (2011).

Assembly members:
NP_888769.1, polymer, 141 residues, 15260.356 Da.

Natural source:   Common Name: B. bronchiseptica   Taxonomy ID: 518   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella bronchiseptica

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

Entity Sequences (FASTA):
NP_888769.1: GMSQDLIRAAFEKRLSDWAK ARTPALPVAWQNTKFTPPAA GVYLRAYVMPAATISRDAAG DHRQYRGVFQVNVVMPIGDG SRSAEQVAAELDALFPVNLV MQSGGLAVRVRTPISNGQPT TGDADHTVPISLGYDVQFYP E

Data sets:
Data typeCount
13C chemical shifts565
15N chemical shifts142
1H chemical shifts947

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_888769.11

Entities:

Entity 1, NP_888769.1 141 residues - 15260.356 Da.

1   GLYMETSERGLNASPLEUILEARGALAALA
2   PHEGLULYSARGLEUSERASPTRPALALYS
3   ALAARGTHRPROALALEUPROVALALATRP
4   GLNASNTHRLYSPHETHRPROPROALAALA
5   GLYVALTYRLEUARGALATYRVALMETPRO
6   ALAALATHRILESERARGASPALAALAGLY
7   ASPHISARGGLNTYRARGGLYVALPHEGLN
8   VALASNVALVALMETPROILEGLYASPGLY
9   SERARGSERALAGLUGLNVALALAALAGLU
10   LEUASPALALEUPHEPROVALASNLEUVAL
11   METGLNSERGLYGLYLEUALAVALARGVAL
12   ARGTHRPROILESERASNGLYGLNPROTHR
13   THRGLYASPALAASPHISTHRVALPROILE
14   SERLEUGLYTYRASPVALGLNPHETYRPRO
15   GLU

Samples:

sample_1: NP_888769.1, [U-98% 13C; U-98% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; D2O 5%; H2O 95%

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, data processing

Molmol v2K.1, 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
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAO70052
EMBL CAE32722 CAE33988 CCN17196
GB KAK74699 KCV36321 KCV51124 KDB85184 KDB90075
REF WP_004566287

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