BMRB Entry 18763

Name: FGFR3tm
Published: 2013-10-04

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PDB ID: 2lzl
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

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

FGFR3tm

Deposition date:

2012-10-04

Original release date:

2013-10-04

Authors:

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

Citation:

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).
PubMed: 24120763

Assembly members:

Assembly members:
FGFR3tm, polymer, 43 residues, 4604.369 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 Vector: pGEMEX-1/(TRX-tmFGFR3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FGFR3tm: LPAEEELVEADEAGSVYAGI LSYGVGFFLFILVVAAVTLC RLR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	189
15N chemical shifts	47
1H chemical shifts	322

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FGFR3tm_1	1
2	FGFR3tm_2	1

Entities:

Entity 1, FGFR3tm_1 43 residues - 4604.369 Da.

1

LEU

PRO

ALA

GLU

LEU

VAL

GLU

ALA

2

ASP

GLU

ALA

GLY

SER

VAL

TYR

ALA

GLY

ILE

3

LEU

SER

TYR

GLY

VAL

GLY

PHE

LEU

PHE

4

ILE

LEU

VAL

ALA

VAL

THR

LEU

CYS

5

ARG

LEU

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C constant time HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C constant time HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
15N,13C-F1-filtered/F3-edited-NOESY	sample_1	isotropic	sample_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

PDB	2LZL
DBJ	BAD92678 BAI45440 BAI45449
GB	AAA52450 AAA58470 AAB33323 AAI21176 AAI28611
REF	NP_000133 NP_001156685 XP_001101108 XP_002802213 XP_003310269
SP	P22607
AlphaFold	P22607