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BMRB Entry 15746

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR15746
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Title: Bpp3783_115-220

Deposition date: 2008-04-29 Original release date: 2009-11-11

Authors: Shaw, Gary; Revington, Matthew; Savichenko, Alexei; Arrowsmith, Cheryl

Citation: Revington, Matthew; Shaw, Gary; Savichenko, Alexei; Arrowsmith, Cheryl. "Solution structure of a domain of a type three secretion system secretory protein BPP 3783 from Bordetella pertusis"  . ., .-..

Assembly members:
BPP3783_115-120, polymer, 106 residues, 12116.664 Da.

Natural source:   Common Name: Bordetella Parapertussis   Taxonomy ID: 519   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella Parapertussis

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

Entity Sequences (FASTA):
BPP3783_115-120: KQQLQEHAPSHANLDVKWLD GLRAGSMALQGDVKVWMQNL EDLHTRRPDEFTARLQQSTD ALYSHLEAQWAKQHGTPPTA SDVVGMPQWQEYTAMLRERF AGLDTI

Data sets:
Data typeCount
13C chemical shifts359
15N chemical shifts94
1H chemical shifts566

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BPP3783_115-1201

Entities:

Entity 1, BPP3783_115-120 106 residues - 12116.664 Da.

1   LYSGLNGLNLEUGLNGLUHISALAPROSER
2   HISALAASNLEUASPVALLYSTRPLEUASP
3   GLYLEUARGALAGLYSERMETALALEUGLN
4   GLYASPVALLYSVALTRPMETGLNASNLEU
5   GLUASPLEUHISTHRARGARGPROASPGLU
6   PHETHRALAARGLEUGLNGLNSERTHRASP
7   ALALEUTYRSERHISLEUGLUALAGLNTRP
8   ALALYSGLNHISGLYTHRPROPROTHRALA
9   SERASPVALVALGLYMETPROGLNTRPGLN
10   GLUTYRTHRALAMETLEUARGGLUARGPHE
11   ALAGLYLEUASPTHRILE

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 ± 0.2 mM; NaCl 500 ± 10 mM; TRIS 10 ± 1 mM; Zn++ 10 ± 1 uM; Benzamidine 1 ± 0.2 mM; NaN3 0.01 ± 0.01 %

sample_conditions_1: ionic strength: 1 M; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1

Software:

NMRPipe vv2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2, Johnson, One Moon Scientific - data analysis

CYANA v2, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

VNMR v6.1c, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAE39066 CCJ60666 CCK33761 CCN05630 CCN18924
GB KAK50548 KAK74290 KAK75306 KCV30400 KCV45728
REF WP_003820735 WP_004567631 WP_010929242 WP_033450554 WP_033453212

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