BMRB Entry 15537

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15537
MolProbity Validation Chart

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Title:
Solution NMR structures of two designed proteins with 88% sequence identity but different fold and function
Deposition date:
2007-10-25
Original release date:
2008-11-03
Authors:
He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John
Citation:

Citation: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John. "NMR structures of two designed proteins with high sequence identity but different fold and function"  Proc. Natl. Acad. Sci. U.S.A. 105, 14412-14417 (2008).
PubMed: 18796611

Assembly members:

Assembly members:
Gb88, polymer, 56 residues, 6317.434 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: over expression in E. Coli   Host organism: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Gb88: TTYKLILNLKQAKEEAIKEL VDAATAEKYFKLYANAKTVE GVWTYKDETKTFTVTE

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts57
1H chemical shifts367

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Gb881

Entities:

Entity 1, Gb88 56 residues - 6317.434 Da.

1   THRTHRTYRLYSLEUILELEUASNLEULYS
2   GLNALALYSGLUGLUALAILELYSGLULEU
3   VALASPALAALATHRALAGLULYSTYRPHE
4   LYSLEUTYRALAASNALALYSTHRVALGLU
5   GLYVALTRPTHRTYRLYSASPGLUTHRLYS
6   THRPHETHRVALTHRGLU

Samples:

Gb88_sample: Gb88, [U-100% 13C; U-100% 15N], 0.2 – 0.4 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H20 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCGb88_sampleisotropicsample_conditions_1
3D HNCACBGb88_sampleisotropicsample_conditions_1
3D CBCA(CO)NHGb88_sampleisotropicsample_conditions_1
3D HBHA(CO)NHGb88_sampleisotropicsample_conditions_1
3D H(CCO)NHGb88_sampleisotropicsample_conditions_1
3D C(CO)NHGb88_sampleisotropicsample_conditions_1
3D HNCOGb88_sampleisotropicsample_conditions_1
3D 1H-15N NOESYGb88_sampleisotropicsample_conditions_1
3D 1H-13C NOESY(aliphatic)Gb88_sampleisotropicsample_conditions_1
3D 1H-13C NOESY(aromatic)Gb88_sampleisotropicsample_conditions_1

Software:

CNS v1.1, 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:

PDB

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