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 15232

Title: proline-free mutant of SNase V8   PubMed: 17887731

Authors: Shan, Lu

Citation: Shan, Lu; Tong, Yufeng; Xie, Tao; Wang, Min; Wang, Jinfeng. "Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease(,)."  Biochemistry 46, 11504-11513 (2007).

Assembly members:
v8pf, polymer, 149 residues, 16678.268 Da.

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
v8pf: ATSTKKLHKEAATLIKAIDG DTVKLMYKGQAMTFRLLLVD TAETKHTKKGVEKYGAEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKGNNT HEQLLRKSEAQAKKEKLNIW SEDNADSGQ

Data sets:
Data typeCount
13C chemical shifts371
15N chemical shifts127
1H chemical shifts666

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1v8pf1

Entities:

Entity 1, v8pf 149 residues - 16678.268 Da.

1   ALATHRSERTHRLYSLYSLEUHISLYSGLU
2   ALAALATHRLEUILELYSALAILEASPGLY
3   ASPTHRVALLYSLEUMETTYRLYSGLYGLN
4   ALAMETTHRPHEARGLEULEULEUVALASP
5   THRALAGLUTHRLYSHISTHRLYSLYSGLY
6   VALGLULYSTYRGLYALAGLUALASERALA
7   PHETHRLYSLYSMETVALGLUASNALALYS
8   LYSILEGLUVALGLUPHEASPLYSGLYGLN
9   ARGTHRASPLYSTYRGLYARGGLYLEUALA
10   TYRILETYRALAASPGLYLYSMETVALASN
11   GLUALALEUVALARGGLNGLYLEUALALYS
12   VALALATYRVALTYRLYSGLYASNASNTHR
13   HISGLUGLNLEULEUARGLYSSERGLUALA
14   GLNALALYSLYSGLULYSLEUASNILETRP
15   SERGLUASPASNALAASPSERGLYGLN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; KCL 100 mM; D2O 10%; H2O 90%; acetate 59 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

FELIX v98, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

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