BMRB Entry 19623

Title:
GA-79-MBP cs-rosetta structures
Deposition date:
2013-11-19
Original release date:
2015-04-07
Authors:
He, Yanan; Chen, Yihong; Porter, Lauren; Bryan, Philip; Orban, John
Citation:

Citation: Porter, Lauren; He, Yanan; Chen, Yihong; Orban, John; Bryan, Philip. "Subdomain interactions foster the design of two protein pairs with ~80% sequence identity but different folds"  Biophys J. 108, 154-162 (2015).
PubMed: 25564862

Assembly members:

Assembly members:
entity, polymer, 56 residues, 6312.319 Da.

Natural source:

Natural source:   Common Name: Streptococcus canis   Taxonomy ID: 1329   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus canis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: hisPPAL8

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts162
15N chemical shifts55
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GA-79-MBP1

Entities:

Entity 1, GA-79-MBP 56 residues - 6312.319 Da.

1   ASNGLYASPLYSGLYTYRASNGLYLEUALA
2   GLUALALYSGLULYSALAILELYSASPLEU
3   LYSILETYRGLYILEGLYGLUHISTYRILE
4   LYSLEUILEGLULYSALALYSGLNVALALA
5   ALAVALGLUASPLEULYSASPGLUILELEU
6   LYSALAHISASPARGPHE

Samples:

sample_1: GA-79-MBP, [U-100% 13C; U-100% 15N], 0.27 mM; potassium phosphate 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - structure display

TOPSPIN, Bruker Biospin - Data collection

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - structure quality analysis

CSI, David Wishart, Brian Sykes - Secondary structure prediction

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker Avance III 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks