BMRB Entry 30910

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30910
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Anaplastic lymphoma kinase (ALK) extracellular ligand binding region 673-1025
Deposition date:
2021-05-24
Original release date:
2021-12-03
Authors:
Rossi, P.; Sowaileh, M.; Reshetnyak, A.; Kalodimos, C.
Citation:

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).
PubMed: 34819673

Assembly members:

Assembly members:
entity_1, polymer, 353 residues, 36452.293 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QTPIFDPTVHWLFTTCGASG PHGPTQAQCNNAYQNSNLSV EVGSEGPLKGIQIWKVPATD TYSISGYGAAGGKGGKNTMM RSHGVSVLGIFNLEKDDMLY ILVGQQGEDACPSTNQLIQK VCIGENNVIEEEIRVNRSVH EWAGGGGGGGGATYVFKMKD GVPVPLIIAAGGGGRAYGAK TDTFHPERLENNSSVLGLNG NSGAAGGGGGWNDNTSLLWA GKSLQEGATGGHSCPQAMKK WGWETRGGFGGGGGGCSSGG GGGGYIGGNAASNNDPEMDG EDGVSFISPLGILYTPALKV MEGHGEVNIKHYLNCSHCEV DECHMDPESHKVICFCDHGT VLAEDGVSCIVSP

Data sets:
Data typeCount
13C chemical shifts1098
15N chemical shifts323
1H chemical shifts810

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 353 residues - 36452.293 Da.

1   GLNTHRPROILEPHEASPPROTHRVALHIS
2   TRPLEUPHETHRTHRCYSGLYALASERGLY
3   PROHISGLYPROTHRGLNALAGLNCYSASN
4   ASNALATYRGLNASNSERASNLEUSERVAL
5   GLUVALGLYSERGLUGLYPROLEULYSGLY
6   ILEGLNILETRPLYSVALPROALATHRASP
7   THRTYRSERILESERGLYTYRGLYALAALA
8   GLYGLYLYSGLYGLYLYSASNTHRMETMET
9   ARGSERHISGLYVALSERVALLEUGLYILE
10   PHEASNLEUGLULYSASPASPMETLEUTYR
11   ILELEUVALGLYGLNGLNGLYGLUASPALA
12   CYSPROSERTHRASNGLNLEUILEGLNLYS
13   VALCYSILEGLYGLUASNASNVALILEGLU
14   GLUGLUILEARGVALASNARGSERVALHIS
15   GLUTRPALAGLYGLYGLYGLYGLYGLYGLY
16   GLYALATHRTYRVALPHELYSMETLYSASP
17   GLYVALPROVALPROLEUILEILEALAALA
18   GLYGLYGLYGLYARGALATYRGLYALALYS
19   THRASPTHRPHEHISPROGLUARGLEUGLU
20   ASNASNSERSERVALLEUGLYLEUASNGLY
21   ASNSERGLYALAALAGLYGLYGLYGLYGLY
22   TRPASNASPASNTHRSERLEULEUTRPALA
23   GLYLYSSERLEUGLNGLUGLYALATHRGLY
24   GLYHISSERCYSPROGLNALAMETLYSLYS
25   TRPGLYTRPGLUTHRARGGLYGLYPHEGLY
26   GLYGLYGLYGLYGLYCYSSERSERGLYGLY
27   GLYGLYGLYGLYTYRILEGLYGLYASNALA
28   ALASERASNASNASPPROGLUMETASPGLY
29   GLUASPGLYVALSERPHEILESERPROLEU
30   GLYILELEUTYRTHRPROALALEULYSVAL
31   METGLUGLYHISGLYGLUVALASNILELYS
32   HISTYRLEUASNCYSSERHISCYSGLUVAL
33   ASPGLUCYSHISMETASPPROGLUSERHIS
34   LYSVALILECYSPHECYSASPHISGLYTHR
35   VALLEUALAGLUASPGLYVALSERCYSILE
36   VALSERPRO

Samples:

sample_1: Anaplastic lymphoma kinase ALK extracellular domain 673-1025, [U-100% 13C; U-100% 15N; U-100% 2H], 300 uM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.1%

sample_2: Anaplastic lymphoma kinase ALK extracellular domain 673-1025, [U-2H,15N-1H13C AILMTV 1H,13C-FY (Ce1,2)], 400 uM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.1%

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D NCmHm_NOESYsample_2isotropicsample_conditions_1
3D CmNH_NOESYsample_2isotropicsample_conditions_1
3D CaCmHm_NOESYsample_2isotropicsample_conditions_1
3D HaCaHa_NOESYsample_2isotropicsample_conditions_1
3D HNH_NOESYsample_2isotropicsample_conditions_1
3D CmCmHm_NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

PINE, Bahrami, Markley, Assadi, and Eghbalnia - peak picking

TopSpin v4.06, Bruker Biospin - collection

NMRFAM-SPARKY, lee - peak picking

TALOS-N, SHEN AND BAX - geometry optimization

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

PdbStat, tejero and montelione - data analysis

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 1100 MHz
  • 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 peaks
SPARKY: Backbone or all simulated peaks