BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15132

Title: The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection.   PubMed: 17289578

Authors: Watters, Alexander; Deka, Priti; Corrent, Colin; Callender, David; Varani, Gabriele; Sosnick, Tobin; Baker, David

Citation: Watters, Alexander; Deka, Pritilekha; Corrent, Colin; Callender, David; Varani, Gabriele; Sosnick, Tobin; Baker, David. "The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection."  Cell 128, 613-624 (2007).

Assembly members:
Top7, polymer, 106 residues, Formula weight is not available

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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Top7: MGDIQVQVNIDDNGKNQDLT YTVTTESELQKVLNELKDYI EEQGAKRVRISITARTEKEA EKFAAILIKVFAELGYNDIN VTWDGDTVTVEGQLEGGSLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts102
1H chemical shifts370

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

Entity 1, monomer 106 residues - Formula weight is not available

Residues 1-2 and 95-106 are part of the expression vector and not ordered in the folded strucutre.

1   METGLYASPILEGLNVALGLNVALASNILE
2   ASPASPASNGLYLYSASNGLNASPLEUTHR
3   TYRTHRVALTHRTHRGLUSERGLULEUGLN
4   LYSVALLEUASNGLULEULYSASPTYRILE
5   GLUGLUGLNGLYALALYSARGVALARGILE
6   SERILETHRALAARGTHRGLULYSGLUALA
7   GLULYSPHEALAALAILELEUILELYSVAL
8   PHEALAGLULEUGLYTYRASNASPILEASN
9   VALTHRTRPASPGLYASPTHRVALTHRVAL
10   GLUGLYGLNLEUGLUGLYGLYSERLEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: Top7, [U-99% 15N], 1 mM; H2O 95%; D2O 5%; sodium phosphate 50 mM

sample_2: Top7, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

SPARKY v3.112, Goddard - chemical shift assignment, data analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 7101
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