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 16117

Title: NMR structures of GA95 and GB95, two designed proteins with 95% sequence identity but different folds and functions   PubMed: 19998407

Deposition date: 2009-01-12 Original release date: 2010-01-12

Authors: He, Yanan; Alexander, Patrick; Chen, Yihong; Bryan, Philip; Orban, John

Citation: Shen, Yang; Bryan, Philip; He, Yanan; Orban, John; Baker, David; Bax, Ad. "De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds."  Protein Sci. 19, 349-356 (2009).

Assembly members:
entity, polymer, 56 residues, 6317.434 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: over expression in E. Coli

Entity Sequences (FASTA):
entity: TTYKLILNLKQAKEEAIKEA VDAGTAEKYFKLIANAKTVE GVWTYKDEIKTFTVTE

Data sets:
Data typeCount
13C chemical shifts242
15N chemical shifts59
1H chemical shifts354

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 56 residues - 6317.434 Da.

1   THRTHRTYRLYSLEUILELEUASNLEULYS
2   GLNALALYSGLUGLUALAILELYSGLUALA
3   VALASPALAGLYTHRALAGLULYSTYRPHE
4   LYSLEUILEALAASNALALYSTHRVALGLU
5   GLYVALTRPTHRTYRLYSASPGLUILELYS
6   THRPHETHRVALTHRGLU

Samples:

Gb95: Gb95, [U-100% 13C; U-100% 15N], 0.15-0.3 mM; potassium phosphate pH 7.2 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCGb95isotropicsample_conditions_1
3D HNCACBGb95isotropicsample_conditions_1
3D CBCA(CO)NHGb95isotropicsample_conditions_1
3D HBHA(CO)NHGb95isotropicsample_conditions_1
3D H(CCO)NHGb95isotropicsample_conditions_1
3D C(CO)NHGb95isotropicsample_conditions_1
3D HNCOGb95isotropicsample_conditions_1
3D 1H-15N NOESYGb95isotropicsample_conditions_1
3D 1H-13C NOESY(aliphatic)Gb95isotropicsample_conditions_1
3D 1H-13C NOESY(aromatic)Gb95isotropicsample_conditions_1

Software:

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

xwinnmr v2.5, Bruker Biospin - collection

NMRPipe vn/a, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3, Goddard - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17840 17841
PDB

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