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 1AEY 1M8M 1NEG 1QKW 1SHG 1TUC 1U06 2F2V 2F2X 2JMC 2LJ3 2NUZ 4F16 4F17
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