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 19504

Title: baa38

Deposition date: 2013-09-18 Original release date: 2014-09-29

Authors: Kier, Brandon; Sheffler, William; Baker, David

Citation: Kier, Brandon; Sheffler, William; Baker, David. "Covalent Assembly of Homooligomeric Proteins Using Structure-templating Hubs"  Biochemistry ., .-..

Assembly members:
entity, polymer, 38 residues, 4599.372 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity: RWLCIWLSDQTLEDLEKMAR REGLSKSEMINVALQHYK

Data sets:
Data typeCount
1H chemical shifts294

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1baa38_11
2baa38_21

Entities:

Entity 1, baa38_1 38 residues - 4599.372 Da.

1   ARGTRPLEUCYSILETRPLEUSERASPGLN
2   THRLEUGLUASPLEUGLULYSMETALAARG
3   ARGGLUGLYLEUSERLYSSERGLUMETILE
4   ASNVALALALEUGLNHISTYRLYS

Samples:

sample_1: baa38 mM; sodium phosphate 50 mM; DSS 0.5 mM; H20 90%; D2O 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 5; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

Foldit, David Baker et al, University of Washington - design

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz