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 5171

Title: NMR Structure of BPTI Mutant G37A   PubMed: 11841215

Authors: Battiste, J.; Li, R.; Woodward, C.

Citation: Battiste, J.; Li, R.; Woodward, C.. "A Highly Destabilizing Mutation, G37A, of the Bovine Pancreatic Trypsin Inhibitor Retains the Average Native Conformation but Greatly Increases Local Flexibility"  Biochemistry 41, 2237-2245 (2002).

Assembly members:
BPTI, polymer, 58 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: .

Entity Sequences (FASTA):
BPTI: RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGACRA KRNNFKSAEDCMRTCGGA

Data sets:
Data typeCount
1H chemical shifts321

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BPTI G37A1

Entities:

Entity 1, BPTI G37A 58 residues - Formula weight is not available

1   ARGPROASPPHECYSLEUGLUPROPROTYR
2   THRGLYPROCYSLYSALAARGILEILEARG
3   TYRPHETYRASNALALYSALAGLYLEUCYS
4   GLNTHRPHEVALTYRGLYALACYSARGALA
5   LYSARGASNASNPHELYSSERALAGLUASP
6   CYSMETARGTHRCYSGLYGLYALA

Samples:

sample_1: BPTI 5 mM; H2O 90%; D2O 10%

sample_2: BPTI 5 mM; D2O 99.9%

sample_cond_1: ionic strength: 30 mM; pH: 4.6; pressure: 1 atm; temperature: 298 K

sample_cond_2: ionic strength: 30 mM; pH: 4.6; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
DQF-COSYnot availablenot availablenot available

Software:

VNMR v6.1B - data collection

NMRPipe v1.7 - data processing

XEASY v1.2 - data analysis

X-PLOR v3.851 - structure solution, refinement

NMR spectrometers:

  • Varian INOVA 800 MHz

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