BMRB Entry 18442

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18442
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure of the R. rickettsii cold shock-like protein
Deposition date:
2012-05-04
Original release date:
2012-06-05
Authors:
Veldkamp, C.; Peterson, F.; Gerarden, K.; Fuchs, A.; Koch, J.; Mueller, M.
Citation:

Citation: Gerarden, Kyle; Fuchs, Andrew; Koch, Jonathan; Mueller, Melissa; Graupner, David; Frost, Justin; Heinen, Caleb; Lackner, Heather; Schoeller, Emily; House, Scott; Peterson, Paul; Veldkamp, Francis. "Solution structure of the cold-shock-like protein from Rickettsia rickettsii."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 1284-1288 (2012).
PubMed: 23143233

Assembly members:

Assembly members:
cold_shock-like_protein_[Rickettsia_rickettsii_str._'Sheila_Smith']_, polymer, 70 residues, 7781.821 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cold_shock-like_protein_[Rickettsia_rickettsii_str._'Sheila_Smith']_: MATNIVGKVKWYNSTKNFGF IEQDNGGKDVFVHKSAVDAA GLHSLEEGQDVIFDLEEKQG KAYAVNLRIK

Data sets:
Data typeCount
13C chemical shifts293
15N chemical shifts77
1H chemical shifts489

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1R. rickettsii cold shock-like protein1

Entities:

Entity 1, R. rickettsii cold shock-like protein 70 residues - 7781.821 Da.

1   METALATHRASNILEVALGLYLYSVALLYS
2   TRPTYRASNSERTHRLYSASNPHEGLYPHE
3   ILEGLUGLNASPASNGLYGLYLYSASPVAL
4   PHEVALHISLYSSERALAVALASPALAALA
5   GLYLEUHISSERLEUGLUGLUGLYGLNASP
6   VALILEPHEASPLEUGLUGLULYSGLNGLY
7   LYSALATYRALAVALASNLEUARGILELYS

Samples:

sample: [U-100% 13C; U-100% 15N] 1.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sampleisotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v3.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAK96972
EMBL CDI29705 CEO18020
GB AAL03559 AAY61113 ABV76609 ABV85095 ABY72984
REF WP_004997759 WP_008579233 WP_011270614 WP_014014650 WP_014365526
SP Q4UMU5 Q92GV1
AlphaFold Q4UMU5 Q92GV1

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