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 19703

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments and structure of Iron-sulfur cluster binding protein from Ehrlichia chaffeensis

Authors: Barnwal, Ravi Pratap; Varani, Gabriele

Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "Backbone 1H, 13C, and 15N Chemical Shift Assignments and structure of Iron-sulfur cluster binding protein from Ehrlichia chaffeensis"  Not known ., .-..

Assembly members:
Iron-sulfur_cluster_binding_protein, polymer, 116 residues, 12862.470 Da.

Natural source:   Common Name: Ehrlichia chaffeensis   Taxonomy ID: 945   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Ehrlichia chaffeensis

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

Entity Sequences (FASTA):
Iron-sulfur_cluster_binding_protein: MPLITFISPDGSRKTYEAYD GETLLSLAHRNNVDLEGACE GSLACSTCHVIIDPSWYDIV EQHNEISDEENDMLDLAFGL TDTSRLGCQIILTKELDGLC VILPTETRNISFVKNS

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts98
1H chemical shifts563

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Iron-sulfur cluster binding protein1

Entities:

Entity 1, Iron-sulfur cluster binding protein 116 residues - 12862.470 Da.

1   METPROLEUILETHRPHEILESERPROASP
2   GLYSERARGLYSTHRTYRGLUALATYRASP
3   GLYGLUTHRLEULEUSERLEUALAHISARG
4   ASNASNVALASPLEUGLUGLYALACYSGLU
5   GLYSERLEUALACYSSERTHRCYSHISVAL
6   ILEILEASPPROSERTRPTYRASPILEVAL
7   GLUGLNHISASNGLUILESERASPGLUGLU
8   ASNASPMETLEUASPLEUALAPHEGLYLEU
9   THRASPTHRSERARGLEUGLYCYSGLNILE
10   ILELEUTHRLYSGLULEUASPGLYLEUCYS
11   VALILELEUPROTHRGLUTHRARGASNILE
12   SERPHEVALLYSASNSER

Samples:

sample_1: Iron-sulfur cluster binding protein, [U-95% 15N], 1.2 mM; Iron-sulfur cluster binding protein, [U-95% 13C; U-95% 15N], 1.1 mM

sample_conditions_1: pH: 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking, refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CEI85472
GB AAZ68448 ABD45498 AHX03715 AHX04894 AHX05564
REF WP_006011527 WP_011304526 WP_044194855 WP_045171525