BMRB Entry 17262

Title:
SOLUTION STRUCTURE OF CALCIUM BOUND S100A16
Deposition date:
2010-10-22
Original release date:
2010-11-15
Authors:
Babini, Elena; Bertini, Ivano; Borsi, Valentina; Calderone, Vito; Hu, Xiaoyu; Luchinat, Claudio; Parigi, Giacomo
Citation:

Citation: Babini, Elena; Bertini, Ivano; Borsi, Valentina; Calderone, Vito; Hu, Xiaoyu; Luchinat, Claudio; Parigi, Giacomo. "Structural characterization of human S100A16, a low-affinity calcium binder."  J. Biol. Inorg. Chem. 16, 243-256 (2011).
PubMed: 21046186

Assembly members:

Assembly members:
S100A16, polymer, 102 residues, 11686.296 Da.
CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts112
1H chemical shifts446

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21
3CALCIUM ION_12
4CALCIUM ION_22
5CALCIUM ION_32
6CALCIUM ION_42

Entities:

Entity 1, entity_1_1 102 residues - 11686.296 Da.

1   SERASPCYSTYRTHRGLULEUGLULYSALA
2   VALILEVALLEUVALGLUASNPHETYRLYS
3   TYRVALSERLYSTYRSERLEUVALLYSASN
4   LYSILESERLYSSERSERPHEARGGLUMET
5   LEUGLNLYSGLULEUASNHISMETLEUSER
6   ASPTHRGLYASNARGLYSALAALAASPLYS
7   LEUILEGLNASNLEUASPALAASNHISASP
8   GLYARGILESERPHEASPGLUTYRTRPTHR
9   LEUILEGLYGLYILETHRGLYPROILEALA
10   LYSLEUILEHISGLUGLNGLUGLNGLNSER
11   SERSER

Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

13C15N_Ca_II_S100A16: S100A16, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; Ca ions 10 mM; KCl 200 mM

15N_Ca_II_S100A16: S100A16, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; Ca ions 10 mM; KCl 200 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_Ca_II_S100A16isotropicsample_conditions_1
2D 1H-13C HSQC13C15N_Ca_II_S100A16isotropicsample_conditions_1
2D 1H-1H NOESY15N_Ca_II_S100A16isotropicsample_conditions_1
3D CBCA(CO)NH13C15N_Ca_II_S100A16isotropicsample_conditions_1
3D HNCO13C15N_Ca_II_S100A16isotropicsample_conditions_1
3D HNCA13C15N_Ca_II_S100A16isotropicsample_conditions_1
3D HNCACB13C15N_Ca_II_S100A16isotropicsample_conditions_1
3D HBHA(CO)NH15N_Ca_II_S100A16isotropicsample_conditions_1
3D HCCH-TOCSY13C15N_Ca_II_S100A16isotropicsample_conditions_1
3D 1H-15N NOESY15N_Ca_II_S100A16isotropicsample_conditions_1
3D 1H-13C NOESY13C15N_Ca_II_S100A16isotropicsample_conditions_1

Software:

AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - data analysis, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

TOPSPIN v2.0, Bruker Biospin - collection, processing

XEASY, Bartels et al. - chemical shift assignment, peak picking

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

WhatIF, Vriend - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 17261
PDB
DBJ BAF83493
EMBL CAE51865
GB AAH10541 AAH19099 AAH95462 AAP46152 AAW88319
REF NP_001303936 NP_001303937 NP_525127 XP_001103071 XP_002760028
SP Q96FQ6
AlphaFold Q96FQ6

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