BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16997

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16997
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution structure of protein SF1141 from Shigella flexneri 2a. Northeast Structural Genomics Consortium (NESG) TARGET SFT2.

Deposition date: 2010-06-11 Original release date: 2010-07-07

Authors: Lemak, Alexander; Yee, Adelinda; Garcia, Maite; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Garcia, Maite; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution structure of protein SF1141 from Shigella flexneri 2a."  Not known ., .-..

Assembly members:
sf1141, polymer, 112 residues, 13259.014 Da.

Natural source:   Common Name: Shigella flexneri   Taxonomy ID: 42897   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shigella flexneri

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

Entity Sequences (FASTA):
sf1141: MNIGRLRDRITIQTLKQTRD ITGEILETWEDGHTLWASVN MVSSKEAISSGAELAIGTVR IWIRYRKDINATSRIKVSTG PLAGRVLNIIGQPLPDAART RLEILCREGAEK

Data typeCount
13C chemical shifts484
15N chemical shifts115
1H chemical shifts806

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SF11411

Entities:

Entity 1, SF1141 112 residues - 13259.014 Da.

1   METASNILEGLYARGLEUARGASPARGILE
2   THRILEGLNTHRLEULYSGLNTHRARGASP
3   ILETHRGLYGLUILELEUGLUTHRTRPGLU
4   ASPGLYHISTHRLEUTRPALASERVALASN
5   METVALSERSERLYSGLUALAILESERSER
6   GLYALAGLULEUALAILEGLYTHRVALARG
7   ILETRPILEARGTYRARGLYSASPILEASN
8   ALATHRSERARGILELYSVALSERTHRGLY
9   PROLEUALAGLYARGVALLEUASNILEILE
10   GLYGLNPROLEUPROASPALAALAARGTHR
11   ARGLEUGLUILELEUCYSARGGLUGLYALA
12   GLULYS

Samples:

sample_1: sf1141, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 500 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 500 M; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC (IPAP)sample_1anisotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CDK49410 CDX06441 CEP56120 CTS44973 CTS74968
GB AAN42758 AAP16648 ADA73539 AIL35230 AIL40152
REF NP_707051 WP_001020659 WP_001020661 WP_001020662 WP_001020663

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