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 15013

Title: Chimer between Spc-SH3 and P41   PubMed: 17275816

Authors: van Nuland, Nico; Candel, Adela; Martinez, Jose; Conejero-Lara, Francisco; Bruix, Marta

Citation: Candel, Adela; Conejero-Lara, Francisco; Martinez, Jose; van Nuland, Nico; Bruix, Marta. "The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex."  FEBS Lett. 581, 687-692 (2007).

Assembly members:
SPCp41, polymer, 77 residues, 8470.656 Da.

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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SPCp41: GAMGPREVTMKKGDILTLLN STNKDWWKVEVNDRQGFVPA AYVKKLDSGTGKELVLALYD YQESGDNAPSYSPPPPP

Data sets:
Data typeCount
13C chemical shifts282
15N chemical shifts78
1H chemical shifts527

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SPCp411

Entities:

Entity 1, SPCp41 77 residues - 8470.656 Da.

1   GLYALAMETGLYPROARGGLUVALTHRMET
2   LYSLYSGLYASPILELEUTHRLEULEUASN
3   SERTHRASNLYSASPTRPTRPLYSVALGLU
4   VALASNASPARGGLNGLYPHEVALPROALA
5   ALATYRVALLYSLYSLEUASPSERGLYTHR
6   GLYLYSGLULEUVALLEUALALEUTYRASP
7   TYRGLNGLUSERGLYASPASNALAPROSER
8   TYRSERPROPROPROPROPRO

Samples:

sample_1: SPCp41, [U-98% 13C; U-98% 15N], 1 mM; glycine 20 mM; H2O 90%; D2O 10%

sample_2: SPCp41, [U-98% 15N], 1 mM; glycine 20 mM; H2O 90%; D2O 10%

sample_3: SPCp41 1 mM; glycine 20 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, T Goddard - chemical shift assignment, data analysis, peak picking

CYANA, P Guntert, C Mumenthaler and K Wuthrich - structure solution

xwinnmr, Bruker Biospin - collection, processing

TOPSPIN, Bruker Biospin - collection, processing

VNMRJ, Varian - collection

NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

NMRView, B Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian Varian NMR System 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15144 17915
PDB
DBJ BAD52438 BAD93097 BAG57892 BAG62120 BAG72795
EMBL CAA29435 CAA32663 CAF90367 CDQ79062
GB AAA51702 AAA51790 AAA52468 AAB41498 AAB60364
REF NP_001036003 NP_001090674 NP_001091958 NP_001123910 NP_001182461
SP P07751 Q13813