BMRB Entry 27082

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27082

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Title:
NMR backbone assignments of the Tyrosine kinase domain of human fibroblast growth receptor 3 in apo state and in complex with inhibitor PD173074
Deposition date:
2017-04-24
Original release date:
2018-03-15
Authors:
Sanfelice, Domenico; Koss, Hans; Bunney, Tom; Thiyagarajan, Nethaji; Thompson, Gary; Farrell, Brendan; Breeze, Alexander; Driscol, Paul; Katan, Matilda
Citation:

Citation: Bunney, Tom; Inglis, Alison; Sanfelice, Domenico; Farrell, Brendan; Kerr, Christopher; Thompson, Gary; Masson, Glenn; Thiyagarajan, Nethaji; Svergun, Dmitri; Williams, Roger; Breeze, Alexander; Katan, Matilda. "Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System"  Structure 26, 446-458 (2018).
PubMed: 29478821

Assembly members:

Assembly members:
FGFR3, polymer, 314 residues, Formula weight is not available

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: pOPINS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FGFR3: SELELPADPKWELSRARLTL GKPLGEGAFGQVVMAEAIGI DKDRAAKPVTVAVKMLKDDA TDKDLSDLVSEMEMMKMIGK HKNIINLLGACTQGGPLYVL VEYAAKGNLREFLRARRPPG LDYSFDTSKPPEEQLTFKDL VSCAYQVARGMEYLASQKCI HRDLAARNVLVTEDNVMKIA DFGLARDVHNLDYYKKTTNG RLPVKWMAPEALFDRVYTHQ SDVWSFGVLLWEIFTLGGSP YPGIPVEELFKLLKEGHRMD KPANCTHDLYMIMRECWHAA PSQRPTFKQLVEDLDRVLTV TSTDEYLDLSAPFE

Data sets:
Data typeCount
13C chemical shifts426
15N chemical shifts205
1H chemical shifts204

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FGFR31

Entities:

Entity 1, FGFR3 314 residues - Formula weight is not available

starting aminoacid is 455

1   SERGLULEUGLULEUPROALAASPPROLYS
2   TRPGLULEUSERARGALAARGLEUTHRLEU
3   GLYLYSPROLEUGLYGLUGLYALAPHEGLY
4   GLNVALVALMETALAGLUALAILEGLYILE
5   ASPLYSASPARGALAALALYSPROVALTHR
6   VALALAVALLYSMETLEULYSASPASPALA
7   THRASPLYSASPLEUSERASPLEUVALSER
8   GLUMETGLUMETMETLYSMETILEGLYLYS
9   HISLYSASNILEILEASNLEULEUGLYALA
10   CYSTHRGLNGLYGLYPROLEUTYRVALLEU
11   VALGLUTYRALAALALYSGLYASNLEUARG
12   GLUPHELEUARGALAARGARGPROPROGLY
13   LEUASPTYRSERPHEASPTHRSERLYSPRO
14   PROGLUGLUGLNLEUTHRPHELYSASPLEU
15   VALSERCYSALATYRGLNVALALAARGGLY
16   METGLUTYRLEUALASERGLNLYSCYSILE
17   HISARGASPLEUALAALAARGASNVALLEU
18   VALTHRGLUASPASNVALMETLYSILEALA
19   ASPPHEGLYLEUALAARGASPVALHISASN
20   LEUASPTYRTYRLYSLYSTHRTHRASNGLY
21   ARGLEUPROVALLYSTRPMETALAPROGLU
22   ALALEUPHEASPARGVALTYRTHRHISGLN
23   SERASPVALTRPSERPHEGLYVALLEULEU
24   TRPGLUILEPHETHRLEUGLYGLYSERPRO
25   TYRPROGLYILEPROVALGLUGLULEUPHE
26   LYSLEULEULYSGLUGLYHISARGMETASP
27   LYSPROALAASNCYSTHRHISASPLEUTYR
28   METILEMETARGGLUCYSTRPHISALAALA
29   PROSERGLNARGPROTHRPHELYSGLNLEU
30   VALGLUASPLEUASPARGVALLEUTHRVAL
31   THRSERTHRASPGLUTYRLEUASPLEUSER
32   ALAPROPHEGLU

Samples:

sample_1: FGFR3, [U-100% 13C; U-100% 15N], 0.150 mM; PIPES-NaOH 50 mM; NaCl 50 mM; TCEP 2 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

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