BMRB Entry 19941

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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

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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:

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"  .

Assembly members:

Assembly members:
TM_domain_of_LAMP2A, polymer, 42 residues, 4484.208 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: pMAL2px

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TM_domain_of_LAMP2A: SADDDNFLVPIAVGAALAGV LILVLLAYFIGLKHHHAGYE QF

Data sets:
Data typeCount
13C chemical shifts159
1H chemical shifts235
15N chemical shifts37

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 42 residues - 4484.208 Da.

1   SERALAASPASPASPASNPHELEUVALPRO
2   ILEALAVALGLYALAALALEUALAGLYVAL
3   LEUILELEUVALLEULEUALATYRPHEILE
4   GLYLEULYSHISHISHISALAGLYTYRGLU
5   GLNPHE

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D HCCH NOESYsample_3isotropicsample_conditions_1
3D 13C Filter NOESYsample_3isotropicsample_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
AlphaFold P13473

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