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 25787

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25787
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 the salicylate-loaded ArCP from yersiniabactin synthetase   PubMed: 26334259

Deposition date: 2015-08-31 Original release date: 2015-09-21

Authors: Goodrich, Andrew; Harden, Bradley; Frueh, Dominique

Citation: Goodrich, Andrew; Harden, Bradley; Frueh, Dominique. "The Solution Structure of a Nonribosomal Peptide Syn-thetase Carrier Protein Loaded with its Substrate Reveals Transient, Well-defined Contacts"  J. Am. Chem. Soc. 137, 12100-12109 (2015).

Assembly members:
entity, polymer, 80 residues, 9869.335 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):
entity: DNRHAADYQQLRERLIQELN LTPQQLHEESNLIQAGLDXI RLMRWLHWFRKNGYRLTLRE LYAAPTLAAWNQLMLSRSPE

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts81
1H chemical shifts577

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 80 residues - 9869.335 Da.

1   ASPASNARGHISALAALAASPTYRGLNGLN
2   LEUARGGLUARGLEUILEGLNGLULEUASN
3   LEUTHRPROGLNGLNLEUHISGLUGLUSER
4   ASNLEUILEGLNALAGLYLEUASP4HJILE
5   ARGLEUMETARGTRPLEUHISTRPPHEARG
6   LYSASNGLYTYRARGLEUTHRLEUARGGLU
7   LEUTYRALAALAPROTHRLEUALAALATRP
8   ASNGLNLEUMETLEUSERARGSERPROGLU

Samples:

n15: Loaded-ArCP, [U-99% 15N], 0.3-0.4 mM; ACES 50 mM; TCEP 0.5 mM; sodium chloride 150 mM; magnesium chloride 1 mM; DSS 0.1 mM; H2O 90%; D2O 10%

c13_backbone: Loaded-ArCP, [U-99% 13C; U-99% 15N], 0.3-0.4 mM; ACES 50 mM; TCEP 0.5 mM; sodium chloride 150 mM; magnesium chloride 1 mM; DSS 0.1 mM; ATP 2 mM; sodium salicylate 2 mM; Adenylation domain YbtE 20-100 nM; H2O 90%; D2O 10%

c13_noesy: Loaded-ArCP, [U-99% 13C; U-99% 15N], 0.3-0.4 mM; ACES 50 mM; TCEP 0.5 mM; sodium chloride 150 mM; magnesium chloride 1 mM; DSS 0.1 mM; ATP 2 mM; sodium salicylate, [U-100% 13C], 0.5 mM; Adenylation domain YbtE 20-100 nM; D2O 100%

h2o: pH: 6.8; pressure: 1 atm; temperature: 298 K

d20: pD: 6.4 pD; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCn15isotropich2o
3D HNCOc13_backboneisotropich2o
3D HNCAc13_backboneisotropich2o
3D HNCACBc13_backboneisotropich2o
3D H(CCO)NHc13_backboneisotropich2o
3D HN(CA)COc13_backboneisotropich2o
3D 1H-15N NOESYn15isotropich2o
2D 1H-13C HSQCc13_backboneisotropich2o
3D 1H-13C NOESYc13_noesyisotropicd20

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

NMR spectrometers:

  • Bruker Avance 600 MHz

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