BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30772

Title: Abl 1b isoform inactive2 state   PubMed: 33004676

Deposition date: 2020-07-12 Original release date: 2020-10-05

Authors: Xie, T.; Saleh, T.; Rossi, P.; Kalodimos, C.

Citation: Xie, T.; Saleh, T.; Rossi, P.; Kalodimos, C.. "Conformational states dynamically populated by a kinase determine its function"  Science ., .-. (2020).

Assembly members:
entity_1, polymer, 287 residues, 33296.992 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: SPNYDKWEMERTDITMKHKL GEGQYGEVYEGVWKKYSLTV AVKTLKEDTMEVEEFLKEAA VLKEIKHPNLVQLLGVCTRE PPFYIITEFMTYGNLLDYLR ECNRQEVNAVVLLYMATQIS SAMEYLEKKNFIHRDLAARN CLVGENHLVKVADFGLSRLM YGDTYTAHAGAKFPIKWTAP ESLAYNKFSIKSDVWAFGVL LWEIATYGMSPYPGIDLSQV YELLEKDYRMERPEGCPEKV YELMRACWQWNPSDRPSFAE IHQAFETMFQESSISDEVEK ELGKQGV

Data sets:
Data typeCount
13C chemical shifts139
1H chemical shifts414

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 287 residues - 33296.992 Da.

1   SERPROASNTYRASPLYSTRPGLUMETGLU
2   ARGTHRASPILETHRMETLYSHISLYSLEU
3   GLYGLUGLYGLNTYRGLYGLUVALTYRGLU
4   GLYVALTRPLYSLYSTYRSERLEUTHRVAL
5   ALAVALLYSTHRLEULYSGLUASPTHRMET
6   GLUVALGLUGLUPHELEULYSGLUALAALA
7   VALLEULYSGLUILELYSHISPROASNLEU
8   VALGLNLEULEUGLYVALCYSTHRARGGLU
9   PROPROPHETYRILEILETHRGLUPHEMET
10   THRTYRGLYASNLEULEUASPTYRLEUARG
11   GLUCYSASNARGGLNGLUVALASNALAVAL
12   VALLEULEUTYRMETALATHRGLNILESER
13   SERALAMETGLUTYRLEUGLULYSLYSASN
14   PHEILEHISARGASPLEUALAALAARGASN
15   CYSLEUVALGLYGLUASNHISLEUVALLYS
16   VALALAASPPHEGLYLEUSERARGLEUMET
17   TYRGLYASPTHRTYRTHRALAHISALAGLY
18   ALALYSPHEPROILELYSTRPTHRALAPRO
19   GLUSERLEUALATYRASNLYSPHESERILE
20   LYSSERASPVALTRPALAPHEGLYVALLEU
21   LEUTRPGLUILEALATHRTYRGLYMETSER
22   PROTYRPROGLYILEASPLEUSERGLNVAL
23   TYRGLULEULEUGLULYSASPTYRARGMET
24   GLUARGPROGLUGLYCYSPROGLULYSVAL
25   TYRGLULEUMETARGALACYSTRPGLNTRP
26   ASNPROSERASPARGPROSERPHEALAGLU
27   ILEHISGLNALAPHEGLUTHRMETPHEGLN
28   GLUSERSERILESERASPGLUVALGLULYS
29   GLULEUGLYLYSGLNGLYVAL

Samples:

sample_1: Abl 1b G269E/M309L/T408Y variant, [U-100% 13C; U-100% 15N; U-100% 2H], 250 uM; sodium phosphate 25 mM; sodium chloride 75 mM; beta-mercaptoethanol 2.5 mM

sample_2: Abl 1b G269E/M309L/T408Y variant, N-ILVMAT-FY, 250 uM; sodium phosphate 25 mM; sodium chloride 75 mM; beta-mercaptoethanol 2.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.7; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D CaCmHm_sofastNOESYsample_2isotropicsample_conditions_1
3D CCH NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_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

Sparky, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya and Montelione - refinement

TopSpin, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker AVANCE 1100 MHz
  • Bruker AVANCE 850 MHz