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 15107

Title: NMR structure of D4P/K7G mutant of GPM12   PubMed: 18473359

Authors: Terada, T.; Satoh, D.; Mikawa, T.; Ito, Y.; Shimizu, K.

Citation: Terada, Tohru; Satoh, Daisuke; Mikawa, Tsutomu; Ito, Yutaka; Shimizu, Kentaro. "Understanding the roles of amino acid residues in tertiary structure formation of chignolin by using molecular dynamics simulation"  Proteins 73, 621-631 (2008).

Assembly members:
GPM12, polymer, 10 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: chemical synthesis

Entity Sequences (FASTA):
GPM12: GYDPATGTFG

Data sets:
Data typeCount
1H chemical shifts53

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GPM121

Entities:

Entity 1, GPM12 10 residues - Formula weight is not available

1   GLYTYRASPPROALATHRGLYTHRPHEGLY

Samples:

sample: GPM12 2 mM; sodium phosphate 20 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsampleisotropicsample_conditions_1
2D TOCSYsampleisotropicsample_conditions_1
2D ROESYsampleisotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker BioSpin Corporation - collection

AZARA v2.7, Wayne Boucher - processing

ANSIG v3.3 for OpenGL version 1.0.6, Per Kraulis, Takeshi Nishimura - data analysis

CNS v1.1, Axel T.Brunger et al. - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

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