BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25700

Title: Solution Structure of R. palustris CsgH   PubMed: 27098162

Deposition date: 2015-07-13 Original release date: 2016-05-23

Authors: Hawthorne, William; Taylor, Jonathan; Escalera-Maurer, Andres; Lambert, Sebastian; Koch, Marion; Scull, Nicola; Sefer, Lea; Xu, Yinqi; Matthews, Steve

Citation: Taylor, Jonathan; Hawthorne, William; Fletcher, Catherine; Lo, Joanne; Koch, Marion; Darvill, Nicholas; Scull, Nicola; Escalera-Maurer, Andres; Sefer, Lea; Wenman, Rosemary; Lambert, Sebastian; Xu, Yinqi; Turner, Benjamin; Kazarian, Sergei; Bubeck, Doryen; de Simone, Alfonso; Knowles, Tuomas; Matthews, Steve. "Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones"  Sci. Rep. 6, 24656-24656 (2016).

Assembly members:
CsgH, polymer, 106 residues, 10492.875 Da.

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 1076   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustris

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

Entity Sequences (FASTA):
CsgH: MVQCEVEAAVSGGHVTLQGV ITAVRDGAGSYKLAVDKAGA AGTSRIKQAGAFTAIAEQRV TVGNVVLDYSSANRYAARLD VSFGSVTIQCNLDPETVKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts399
15N chemical shifts99
1H chemical shifts632

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 106 residues - 10492.875 Da.

Native N-terminal Sequence: MAVDQVPPV has been replaced with a single N-terminal Methionine.

1   METVALGLNCYSGLUVALGLUALAALAVAL
2   SERGLYGLYHISVALTHRLEUGLNGLYVAL
3   ILETHRALAVALARGASPGLYALAGLYSER
4   TYRLYSLEUALAVALASPLYSALAGLYALA
5   ALAGLYTHRSERARGILELYSGLNALAGLY
6   ALAPHETHRALAILEALAGLUGLNARGVAL
7   THRVALGLYASNVALVALLEUASPTYRSER
8   SERALAASNARGTYRALAALAARGLEUASP
9   VALSERPHEGLYSERVALTHRILEGLNCYS
10   ASNLEUASPPROGLUTHRVALLYSLEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 10%; H2O 90%

sample_2: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 292 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure solution

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment

CcpNmr v2.4.0, Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED. - chemical shift assignment, peak picking

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

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