BMRB Entry 26738

Name: 1H, 13C, and 15N Chemical Shift Assignments for Ca2+-bound human mS100A9
Published: 2016-09-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26738

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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:

1H, 13C, and 15N Chemical Shift Assignments for Ca2+-bound human mS100A9

Deposition date:

2016-01-27

Original release date:

2016-09-09

Authors:

Chang, Chin-Chi; Chin, Yu

Citation:

Citation: Chang, Chin-Chi; Khan, Imran; Tsai, Kun-Lin; Li, Hongchun; Yang, Lee-Wei; Chou, Ruey-Hwang; Yu, Chin. "Blocking the interaction between S100A9 and RAGE V domain using CHAPS molecule: A novel route to drug development against cell proliferation" Biochim. Biophys. Acta 1864, 1558-1569 (2016).
PubMed: 27524699

Assembly members:

Assembly members:
mS100A9, polymer, 114 residues, 13095 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):
mS100A9: MTSKMSQLERNIETIINTFH QYSVKLGHPDTLNQGEFKEL VRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFI MLMARLTWASHEKMHEGDEG PGHHHKPGLGEGTP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	435
15N chemical shifts	98
1H chemical shifts	668

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mS100A9 subunit A	1
2	mS100A9 subunit B	1

Entities:

Entity 1, mS100A9 subunit A 114 residues - 13095 Da.

1

MET

THR

SER

LYS

MET

SER

GLN

LEU

GLU

ARG

2

ASN

ILE

GLU

THR

ILE

ASN

THR

PHE

HIS

3

GLN

TYR

SER

VAL

LYS

LEU

GLY

HIS

PRO

ASP

4

THR

LEU

ASN

GLN

GLY

GLU

PHE

LYS

GLU

LEU

5

VAL

ARG

LYS

ASP

LEU

GLN

ASN

PHE

LEU

LYS

6

LYS

GLU

ASN

LYS

ASN

GLU

LYS

VAL

ILE

GLU

7

HIS

ILE

MET

GLU

ASP

LEU

ASP

THR

ASN

ALA

8

ASP

LYS

GLN

LEU

SER

PHE

GLU

PHE

ILE

9

MET

LEU

MET

ALA

ARG

LEU

THR

TRP

ALA

SER

10

HIS

GLU

LYS

MET

HIS

GLU

GLY

ASP

GLU

GLY

11

PRO

GLY

HIS

LYS

PRO

GLY

LEU

GLY

12

GLU

GLY

THR

PRO

Samples:

sample_1: mS100A9, [U-100% 13C; U-100% 15N], 2 mM; TRIS 50 mM; sodium chloride 100 mM; calcium chloride 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(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

Software:

VNMRJ v2.3, Varian - collection, processing

SPARKY v3.114, Goddard - chemical shift assignment, data analysis

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

NMR spectrometers:

Varian VNMRS 700 MHz

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