BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18741

Title: The backbone 1H, 13C, 15N resonance assignment of FGFR1 kinase domain in its free form   PubMed: 23325512

Deposition date: 2012-09-26 Original release date: 2013-02-12

Authors: Vajpai, Navratna; Breeze, Alexander

Citation: Vajpai, Navratna; Schott, Anne-Kathrin; Vogtherr, Martin; Breeze, Alexander. "NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1."  Biomol. NMR Assignments ., .-. (2013).

Assembly members:
FGFR1, polymer, 334 residues, 38202 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
FGFR1: MHHHHHHGSTSLYKKAGSSE NLYFQGAGVSEYELPEDPRW ELPRDRLVLGKPLGEGAFGQ VVLAEAIGLDKDKPNRVTKV AVKMLKSDATEKDLSDLISE MEMMKMIGKHKNIINLLGAC TQDGPLYVIVEYASKGNLRE YLQARRPPGLEYSYNPSHNP EEQLSSKDLVSCAYQVARGM EYLASKKCIHRALAARNVLV TEDNVMKIADFGLARDIHHI DYYKKTTNGRLPVKWMAPEA LFDRIYTHQSDVWSFGVLLW EIFTLGGSPYPGVPVEELFK LLKEGHRMDKPSNCTNELYM MMRDCWHAVPSQRPTFKQLV EDLDRIVALTSNQE

Data sets:
Data typeCount
13C chemical shifts814
15N chemical shifts254
1H chemical shifts254

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FGFR1 kinase1

Entities:

Entity 1, FGFR1 kinase 334 residues - 38202 Da.

Sequence used here for human FGFR1 kinase domain (residues 455-765), contains a mutated catalytic Asp (D623A) plus two additional mutations designed to improve stability (C488A and C584S)

1   METHISHISHISHISHISHISGLYSERTHR
2   SERLEUTYRLYSLYSALAGLYSERSERGLU
3   ASNLEUTYRPHEGLNGLYALAGLYVALSER
4   GLUTYRGLULEUPROGLUASPPROARGTRP
5   GLULEUPROARGASPARGLEUVALLEUGLY
6   LYSPROLEUGLYGLUGLYALAPHEGLYGLN
7   VALVALLEUALAGLUALAILEGLYLEUASP
8   LYSASPLYSPROASNARGVALTHRLYSVAL
9   ALAVALLYSMETLEULYSSERASPALATHR
10   GLULYSASPLEUSERASPLEUILESERGLU
11   METGLUMETMETLYSMETILEGLYLYSHIS
12   LYSASNILEILEASNLEULEUGLYALACYS
13   THRGLNASPGLYPROLEUTYRVALILEVAL
14   GLUTYRALASERLYSGLYASNLEUARGGLU
15   TYRLEUGLNALAARGARGPROPROGLYLEU
16   GLUTYRSERTYRASNPROSERHISASNPRO
17   GLUGLUGLNLEUSERSERLYSASPLEUVAL
18   SERCYSALATYRGLNVALALAARGGLYMET
19   GLUTYRLEUALASERLYSLYSCYSILEHIS
20   ARGALALEUALAALAARGASNVALLEUVAL
21   THRGLUASPASNVALMETLYSILEALAASP
22   PHEGLYLEUALAARGASPILEHISHISILE
23   ASPTYRTYRLYSLYSTHRTHRASNGLYARG
24   LEUPROVALLYSTRPMETALAPROGLUALA
25   LEUPHEASPARGILETYRTHRHISGLNSER
26   ASPVALTRPSERPHEGLYVALLEULEUTRP
27   GLUILEPHETHRLEUGLYGLYSERPROTYR
28   PROGLYVALPROVALGLUGLULEUPHELYS
29   LEULEULYSGLUGLYHISARGMETASPLYS
30   PROSERASNCYSTHRASNGLULEUTYRMET
31   METMETARGASPCYSTRPHISALAVALPRO
32   SERGLNARGPROTHRPHELYSGLNLEUVAL
33   GLUASPLEUASPARGILEVALALALEUTHR
34   SERASNGLNGLU

Samples:

sample_1: FGFR1, [U-13C; U-15N; U-2H], 0.45 ± 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_2: FGFR1, [U-15N, U-50% 2H], 0.45 ± 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_3: FGFR1, [U-15N]-Leu, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_4: FGFR1, [U-15N]-Thr, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_5: FGFR1, [U-15N]-Val, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_6: FGFR1, [U-15N]-Tyr, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_7: FGFR1, [U-15N]-Met, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_8: FGFR1, [U-15N]-Phe, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_9: FGFR1, [U-15N]-Ile, 0.05 mM; sodium phosphate' 'natural abundance; natural abundance; natural abundance; .; .

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC-TROSYsample_2isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_3isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_4isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_5isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_6isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_7isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_8isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_9isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

CARA v1.8.4, Rochus Keller, Kurt Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA02059 BAC25899 BAC28662 BAD92156 BAD96438
EMBL CAA36101 CAA36175 CAA37015 CAA40401 CAA40402
GB AAA35835 AAA35836 AAA35837 AAA35840 AAA35958
PRF 1908208A 1909124A 2103285A
REF NP_001073377 NP_001073378 NP_001103677 NP_001127472 NP_001167534
SP P11362 P16092 Q04589
TPG DAA14429

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