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Biological Magnetic Resonance Data Bank


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BMRB Entry 30912

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30912
MolProbity Validation Chart

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Title: AUGbeta - FAM150A - ALKL1 60-128   PubMed: 34819673

Deposition date: 2021-05-24 Original release date: 2021-11-19

Authors: Rossi, P.; Sowaileh, M.; Reshetnyak, A.; Kalodimos, C.

Citation: Reshetnyak, A.; Rossi, P.; Myasnikov, A.; Sowaileh, M.; Mohanty, J.; Nourse, A.; Miller, D.; Lax, I.; Schlessinger, J.; Kalodimos, C.. "Mechanism for the activation of the anaplastic lymphoma kinase receptor"  Nature 600, 153-157 (2021).

Assembly members:
entity_1, polymer, 70 residues, 8187.402 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: SRSAEIFPRDSNLKDKFIKH FTGPVTFSPECSKHFHRLYY NTRECSTPAYYKRCARLLTR LAVSPLCSQT

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts60
1H chemical shifts455

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 70 residues - 8187.402 Da.

1   SERARGSERALAGLUILEPHEPROARGASP
2   SERASNLEULYSASPLYSPHEILELYSHIS
3   PHETHRGLYPROVALTHRPHESERPROGLU
4   CYSSERLYSHISPHEHISARGLEUTYRTYR
5   ASNTHRARGGLUCYSSERTHRPROALATYR
6   TYRLYSARGCYSALAARGLEULEUTHRARG
7   LEUALAVALSERPROLEUCYSSERGLNTHR

Samples:

sample_1: AUGbeta-FAM150A-ALKL1 residues 60-129, [U-10% 13C; U-100% 15N], 300 uM; sodium azide 0.1%; sodium phosphate 20 mM; sodium chloride 150 mM

sample_2: AUGbeta-FAM150A-ALKL1 residues 60-129, [U-10% 13C; U-100% 15N AILTV methyl sample], 300 uM; sodium azide 0.1%; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 2D 1H-13C HMQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D sfHallCmHm_NOESYsample_2isotropicsample_conditions_1
3D sfCCH_NOESYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH_TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRFAM-SPARKY, W.Lee - peak picking

TopSpin v4.06, Bruker Biospin - collection

TALOS-N, Shen and Bax - geometry optimization

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

PdbStat, Tejero and Montelione - processing

PSVS, Bhattacharya and Montelione - processing

NMR spectrometers:

  • Bruker AVANCE NEO 850 MHz
  • Bruker AVANCE NEO 700 MHz

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