BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16050

Title: Ca-S100A1 interacting with TRTK12   PubMed: 19452629

Authors: Wright, Nathan; Varney, Kristen; Cannon, Brian; Morgan, Michael; Weber, David

Citation: Wright, Nathan; Cannon, Brian; Wilder, P.; Morgan, Michael; Varney, Kristen; Zimmer, D.; Weber, David. "Solution structure of S100A1 bound to the CapZ peptide (TRTK12)"  J. Mol. Biol. 386, 1265-1277 (2009).

Assembly members:
S100A1, polymer, 93 residues, 10439.711 Da.
TRTK12, polymer, 12 residues, 1477.742 Da.
CA, non-polymer, 40.078 Da.

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
S100A1: GSELETAMETLINVFHAHSG KEGDKYKLSKKELKDLLQTE LSSFLDVQKDADAVDKIMKE LDENGDGEVDFQEFVVLVAA LTVACNNFFWENS
TRTK12: TRTKIDWNKILS

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts93
1H chemical shifts668

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21
3entity_2_12
4entity_2_22
5CALCIUM ION_13
6CALCIUM ION_23
7CALCIUM ION_33

Entities:

Entity 1, entity_1_1 93 residues - 10439.711 Da.

1   GLYSERGLULEUGLUTHRALAMETGLUTHR
2   LEUILEASNVALPHEHISALAHISSERGLY
3   LYSGLUGLYASPLYSTYRLYSLEUSERLYS
4   LYSGLULEULYSASPLEULEUGLNTHRGLU
5   LEUSERSERPHELEUASPVALGLNLYSASP
6   ALAASPALAVALASPLYSILEMETLYSGLU
7   LEUASPGLUASNGLYASPGLYGLUVALASP
8   PHEGLNGLUPHEVALVALLEUVALALAALA
9   LEUTHRVALALACYSASNASNPHEPHETRP
10   GLUASNSER

Entity 2, entity_2_1 12 residues - 1477.742 Da.

1   THRARGTHRLYSILEASPTRPASNLYSILE
2   LEUSER

Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: D2O 10%; H2O 90%; CALCIUM ION 10 mM; DTT 10 mM; TRIS 10 mM; sodium chloride 25 mM; entity_1, [U-100% 13C; U-100% 15N], 500 uM; entity_2 1500 uM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 310 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 C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1anisotropicsample_conditions_1
IPAP-HSQCsample_1anisotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15296 4285
PDB
GB AAB20539 AAB53657 EDM00555
REF NP_001007637 XP_006232665
SP P35467