BMRB Entry 51795

Name: Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of Annexin A11-PRD(residues 2-52)
Published: 2023-07-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51795

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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:

Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of Annexin A11-PRD(residues 2-52)

Deposition date:

2023-01-23

Original release date:

2023-07-10

Authors:

Shihora, Aman; Elias, Ruben; Deshmukh, Lalit

Citation:

Citation: Shihora, Aman; Elias, Ruben; Hammond, R.; Ghirlando, Rodolfo; Deshmukh, Lalit. "ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution" ACS Chem. Neurosci. 14, 2583-2589 (2023).
PubMed: 37433222

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, Formula weight is not available

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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SYPGYPPPPGGYPPAAPGGG PWGGAAYPPPPSMPPIGLDN VATYAGQFNQDWSHPQFEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	148
15N chemical shifts	58
1H chemical shifts	37

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	proline-rich domain of Annexin A11	1

Entities:

Entity 1, proline-rich domain of Annexin A11 59 residues - Formula weight is not available

The primary seq is as follows: SYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDWSHPQFEK The first residue in the seq is Serine-2. The C-terminal residues (WSHPQFEK) represent non-native strep tag residues used for purification.

1

SER

TYR

PRO

GLY

TYR

PRO

GLY

2

GLY

TYR

PRO

ALA

PRO

GLY

3

PRO

TRP

GLY

ALA

TYR

PRO

4

PRO

SER

MET

PRO

ILE

GLY

LEU

ASP

ASN

5

VAL

ALA

THR

TYR

ALA

GLY

GLN

PHE

ASN

GLN

6

ASP

TRP

SER

HIS

PRO

GLN

PHE

GLU

LYS

Samples:

sample_1: proline-rich domain of Annexin A11 (residues 2-52), [U-100% 13C; U-100% 15N], 0.2 mM; D2O, [U-2H], 7%; HEPES 25 mM; Calcium Chloride 5 mM

sample_conditions_1: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 13C-detected N-CO	sample_1	isotropic	sample_conditions_1
2D 13C-detected N-CO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker Avance 600 MHz