BMRB Entry 17444

Name: transmembrane domain of LR11/SorLA
Published: 2011-03-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17444

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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:

transmembrane domain of LR11/SorLA

Deposition date:

2011-02-06

Original release date:

2011-03-09

Authors:

Tian, Fang; Wang, Xingsheng; Gill, Richard; Zhu, Qin

Citation:

Citation: Wang, Xingsheng; Gill, Richard; Zhu, Qin; Tian, Fang. "Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies." Protein Expr. Purif. 77, 224-230 (2011).
PubMed: 21320603

Assembly members:

Assembly members:
LR11_SorLA, polymer, 29 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: pMTTH

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LR11_SorLA: RSTDVAAVVVPILFLILLSL GVGFAILYT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	71
15N chemical shifts	25
1H chemical shifts	25

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LR11_SorLA	1

Entities:

Entity 1, LR11_SorLA 29 residues - Formula weight is not available

1

ARG

SER

THR

ASP

VAL

ALA

VAL

2

PRO

ILE

LEU

PHE

LEU

ILE

LEU

SER

LEU

3

GLY

VAL

GLY

PHE

ALA

ILE

LEU

TYR

THR

Samples:

sample_1: LR11_SorLA, [U-99% 13C; U-99% 15N], 1 mM; DPC 128 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

DBJ	BAA13075 BAA31219 BAC26276 BAC40177 BAE27834
EMBL	CAA69325
GB	AAC16739 AAC50891 AAI37172 AAI56441 AAI72714
REF	NP_001076133 NP_001179686 NP_003096 NP_035566 XP_001102178
SP	O88307 Q92673 Q95209
TPG	DAA22319
AlphaFold	O88307 Q92673 Q95209