BMRB Entry 17262

Name: SOLUTION STRUCTURE OF CALCIUM BOUND S100A16
Published: 2010-11-15

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PDB ID: 2l51
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17262
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A16: SDCYTELEKAVIVLVENFYK YVSKYSLVKNKISKSSFREM LQKELNHMLSDTGNRKAADK LIQNLDANHDGRISFDEYWT LIGGITGPIAKLIHEQEQQS SS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	408
15N chemical shifts	112
1H chemical shifts	446

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1_1	1
2	entity_1_2	1
3	CALCIUM ION_1	2
4	CALCIUM ION_2	2
5	CALCIUM ION_3	2
6	CALCIUM ION_4	2

Entities:

Entity 1, entity_1_1 102 residues - 11686.296 Da.

1

SER

ASP

CYS

TYR

THR

GLU

LEU

GLU

LYS

ALA

2

VAL

ILE

VAL

LEU

VAL

GLU

ASN

PHE

TYR

LYS

3

TYR

VAL

SER

LYS

TYR

SER

LEU

VAL

LYS

ASN

4

LYS

ILE

SER

LYS

SER

PHE

ARG

GLU

MET

5

LEU

GLN

LYS

GLU

LEU

ASN

HIS

MET

LEU

SER

6

ASP

THR

GLY

ASN

ARG

LYS

ALA

ASP

LYS

7

LEU

ILE

GLN

ASN

LEU

ASP

ALA

ASN

HIS

ASP

8

GLY

ARG

ILE

SER

PHE

ASP

GLU

TYR

TRP

THR

9

LEU

ILE

GLY

ILE

THR

GLY

PRO

ILE

ALA

10

LYS

LEU

ILE

HIS

GLU

GLN

GLU

GLN

SER

11

SER

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_Ca_II_S100A16	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
2D 1H-1H NOESY	15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D HNCO	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D HNCA	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D HNCACB	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D HBHA(CO)NH	15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_Ca_II_S100A16	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C15N_Ca_II_S100A16	isotropic	sample_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

BMRB	17261
PDB	2L50 2L51 3NXA
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