BMRB Entry 19293

Name: Solution structure of calcium-bound human S100A12
Published: 2014-02-13

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PDB ID: 2m9g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19293
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of calcium-bound human S100A12

Deposition date:

2013-06-07

Original release date:

2014-02-13

Authors:

Hung, Kuo-Wei; Hsu, Chan-Chia; Yu, Chin

Citation:

Citation: Hung, Kuo-Wei; Hsu, Chan-Chia; Yu, Chin. "Solution structure of human Ca(2+)-bound S100A12." J. Biomol. NMR 57, 313-318 (2013).
PubMed: 24057444

Assembly members:

Assembly members:
S100A12, polymer, 92 residues, 10592.145 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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A12: MTKLEEHLEGIVNIFHQYSV RKGHFDTLSKGELKQLLTKE LANTIKNIKDKAVIDEIFQG LDANQDEQVDFQEFISLVAI ALKAAHYHTHKE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	296
15N chemical shifts	75
1H chemical shifts	453

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calcium-bound human S100A12, 1	1
2	calcium-bound human S100A12, 2	1

Entities:

Entity 1, calcium-bound human S100A12, 1 92 residues - 10592.145 Da.

1

MET

THR

LYS

LEU

GLU

HIS

LEU

GLU

GLY

2

ILE

VAL

ASN

ILE

PHE

HIS

GLN

TYR

SER

VAL

3

ARG

LYS

GLY

HIS

PHE

ASP

THR

LEU

SER

LYS

4

GLY

GLU

LEU

LYS

GLN

LEU

THR

LYS

GLU

5

LEU

ALA

ASN

THR

ILE

LYS

ASN

ILE

LYS

ASP

6

LYS

ALA

VAL

ILE

ASP

GLU

ILE

PHE

GLN

GLY

7

LEU

ASP

ALA

ASN

GLN

ASP

GLU

GLN

VAL

ASP

8

PHE

GLN

GLU

PHE

ILE

SER

LEU

VAL

ALA

ILE

9

ALA

LEU

LYS

ALA

HIS

TYR

HIS

THR

HIS

10

LYS

GLU

Samples:

sample_1: S100A12, [U-13C; U-15N], 1 mM; HEPES 10 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02% w/v; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.065 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 13C F1-filtered, F3-edited NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Varian VNMRS 700 MHz

PDB	1E8A 1GQM 1ODB 2M9G 2WC8 2WCB 2WCE 2WCF
DBJ	BAA08497 BAA12030 BAA12036 BAG74208
EMBL	CAA66453 CAB94792
GB	AAH70294 ADR82637 AIC49671 EAW53332
REF	NP_005612 XP_003817231 XP_004026774 XP_525220
SP	P80511
AlphaFold	P80511