BMRB Entry 19941
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19941
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structural insights of TM domain of LAMP-2A in DPC micelles
Deposition date: 2014-04-25 Original release date: 2014-10-27
Authors: Tjandra, Nico; Rout, Ashok K; S., Marie Paule; P., Grzegorz
Citation: Tjandra, Nico; Rout, Ashok K; S., Marie Paule; P., Grzegorz. "Structure of Transmembrane Domain of Lysosomal-Associated Membrane Protein Type 2a (LAMP-2A) Reveals Key Features for Substrate Specificity in Chaperone Mediated Autophagy" Not known ., .-..
Assembly members:
TM_domain_of_LAMP2A, polymer, 42 residues, 4484.208 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TM_domain_of_LAMP2A: SADDDNFLVPIAVGAALAGV
LILVLLAYFIGLKHHHAGYE
QF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 159 |
| 1H chemical shifts | 235 |
| 15N chemical shifts | 37 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 42 residues - 4484.208 Da.
| 1 | SER | ALA | ASP | ASP | ASP | ASN | PHE | LEU | VAL | PRO | ||||
| 2 | ILE | ALA | VAL | GLY | ALA | ALA | LEU | ALA | GLY | VAL | ||||
| 3 | LEU | ILE | LEU | VAL | LEU | LEU | ALA | TYR | PHE | ILE | ||||
| 4 | GLY | LEU | LYS | HIS | HIS | HIS | ALA | GLY | TYR | GLU | ||||
| 5 | GLN | PHE |
Samples:
sample_1: TM domain of LAMP2A, [U-99% 15N], 0.6 ± 0.1 mM; H2O 90%; D2O 10%
sample_2: TM domain of LAMP2A, [U-99% 13C; U-99% 15N], 0.6 ± 0.1 mM; H2O 90%; D2O 10%
sample_3: TM domain of LAMP2A, [U-99% 13C; U-99% 15N], 0.6 ± 0.1 mM; D2O 100%
sample_conditions_1: temperature: 310 K; pH: 6.3; pressure: 1 atm; ionic strength: 25 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D HCCH NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 13C Filter NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - data analysis
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAE01710 BAF83779 |
| EMBL | CAA54416 |
| GB | AAA60383 AAB41647 AAB67314 EAX11883 EPY76113 |
| PRF | 2106261A |
| REF | NP_001106715 NP_002285 XP_001493687 XP_003262323 XP_003779762 |
| SP | P13473 |
| TPG | DAA13411 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts