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 18763

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18763
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: FGFR3tm   PubMed: 24120763

Deposition date: 2012-10-04 Original release date: 2013-10-04

Authors: Lesovoy, Dmitry; Bocharov, Eduard; Goncharuk, Sergey; Arseniev, Alexander

Citation: Bocharov, Eduard; Lesovoy, Dmitry; Goncharuk, Sergey; Goncharuk, Marina; Hristova, Kalina; Arseniev, Alexander. "Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies."  Structure 21, 2087-2093 (2013).

Assembly members:
FGFR3tm, polymer, 43 residues, 4604.369 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

Entity Sequences (FASTA):
FGFR3tm: LPAEEELVEADEAGSVYAGI LSYGVGFFLFILVVAAVTLC RLR

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts47
1H chemical shifts322

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FGFR3tm_11
2FGFR3tm_21

Entities:

Entity 1, FGFR3tm_1 43 residues - 4604.369 Da.

1   LEUPROALAGLUGLUGLULEUVALGLUALA
2   ASPGLUALAGLYSERVALTYRALAGLYILE
3   LEUSERTYRGLYVALGLYPHEPHELEUPHE
4   ILELEUVALVALALAALAVALTHRLEUCYS
5   ARGLEUARG

Samples:

sample_1: FGFR3tm, [U-99% 13C; U-99% 15N], 0.75 mM; FGFR3tm 0.75 mM; DPC, [U-99% 2H], 88 mM; SDS, [U-99% 2H], 10 mM; sodium azide 0.3 mM; TCEP 6 mM; citric acid 5 mM; Na2HPO4 15 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 5.7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C constant time HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C constant time HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
15N,13C-F1-filtered/F3-edited-NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CARA v1.8.4, Rochus Keller - chemical shift assignment

Mathematica, Wolfram Research - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAD92678 BAI45440 BAI45449
GB AAA52450 AAA58470 AAB33323 AAI21176 AAI28611
REF NP_000133 NP_001156685 XP_001101108 XP_002802213 XP_003310269
SP P22607

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