BMRB Entry 18425

Name: Resonance Assignments of Ca2+-bound human S100A11
Published: 2012-09-14

Click here to enlarge.

PDB ID: 2luc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18425
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Resonance Assignments of Ca2+-bound human S100A11

Deposition date:

2012-04-25

Original release date:

2012-09-14

Authors:

Hung, Kuo-Wei; Chang, Yuan-Ming; Yu, Chin

Citation:

Citation: Hung, Kuo-Wei; Chang, Yuan-Ming; Yu, Chin. "Resonance assignments of Ca2+-bound human S100A11." Biomol. NMR Assignments 7, 211-214 (2013).
PubMed: 22825890

Assembly members:

Assembly members:
S100A11, polymer, 105 residues, Formula weight is not available
CALCIUM ION, 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: pET20b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A11: MAKISSPTETERCIESLIAV FQKYAGKDGYNYTLSKTEFL SFMNTELAAFTKNQKDPGVL DRMMKKLDTNSDGQLDFSEF LNLIGGLAMACHDSFLKAVP SQKRT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	354
15N chemical shifts	87
1H chemical shifts	498

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S100A11, chain 1	1
2	S100A11, chain 2	1
3	Ca2+, 1	2
4	Ca2+, 2	2

Entities:

Entity 1, S100A11, chain 1 105 residues - Formula weight is not available

1

MET

ALA

LYS

ILE

SER

PRO

THR

GLU

THR

2

GLU

ARG

CYS

ILE

GLU

SER

LEU

ILE

ALA

VAL

3

PHE

GLN

LYS

TYR

ALA

GLY

LYS

ASP

GLY

TYR

4

ASN

TYR

THR

LEU

SER

LYS

THR

GLU

PHE

LEU

5

SER

PHE

MET

ASN

THR

GLU

LEU

ALA

PHE

6

THR

LYS

ASN

GLN

LYS

ASP

PRO

GLY

VAL

LEU

7

ASP

ARG

MET

LYS

LEU

ASP

THR

ASN

8

SER

ASP

GLY

GLN

LEU

ASP

PHE

SER

GLU

PHE

9

LEU

ASN

LEU

ILE

GLY

LEU

ALA

MET

ALA

10

CYS

HIS

ASP

SER

PHE

LEU

LYS

ALA

VAL

PRO

11

SER

GLN

LYS

ARG

THR

Entity 2, Ca2+, 1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: S100A11, [U-100% 13C; U-100% 15N], 1 mM; TRIS 25 mM; sodium chloride 100 mM; calcium chloride 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.0725 M; pH: 7.5; pressure: 1 atm; temperature: 298 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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

Software:

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

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