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 30199

Title: Solution structure of apo ArCP from yersiniabactin synthetase

Deposition date: 2016-11-02 Original release date: 2017-05-04

Authors: Frueh, D.; Goodrich, A.

Citation: Frueh, D.; Goodrich, A.. "A Network of Dynamic Residues Propagates the Molecular Impact of Covalent Modifications in Nonribosomal Peptide Synthetase Carrier Proteins"  . ., .-..

Assembly members:
Siderophore yersiniabactin, polymer, 82 residues, 9771.064 Da.

Natural source:   Common Name: enterobacteria   Taxonomy ID: 632   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

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

Entity Sequences (FASTA):
Siderophore yersiniabactin: GTDNRHAADYQQLRERLIQE LNLTPQQLHEESNLIQAGLD SIRLMRWLHWFRKNGYRLTL RELYAAPTLAAWNQLMLSRS PE

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts79
1H chemical shifts512

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 82 residues - 9771.064 Da.

1   GLYTHRASPASNARGHISALAALAASPTYR
2   GLNGLNLEUARGGLUARGLEUILEGLNGLU
3   LEUASNLEUTHRPROGLNGLNLEUHISGLU
4   GLUSERASNLEUILEGLNALAGLYLEUASP
5   SERILEARGLEUMETARGTRPLEUHISTRP
6   PHEARGLYSASNGLYTYRARGLEUTHRLEU
7   ARGGLULEUTYRALAALAPROTHRLEUALA
8   ALATRPASNGLNLEUMETLEUSERARGSER
9   PROGLU

Samples:

sample_1: apo-ArCP, [U-99% 15N], 0.25 mM; H2O 90%; D2O 10%

sample_2: apo-ArCP, [U-99% 13C; U-99% 15N], 0.25 mM; H2O 90%; D2O 10%

sample_3: apo-ArCP, [U-99% 13C; U-99% 15N], 0.25 mM; D2O 100%

sample_conditions_1: pH: 6.80; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 6.4 pD; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CA)CBsample_2isotropicsample_conditions_1
3D H(CCCO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
2D hbCBcgcdHDsample_3isotropicsample_conditions_2
2D hbCBcgcdceHEsample_3isotropicsample_conditions_2

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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