BMRB Entry 51510

Name: NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids
Published: 2023-01-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51510

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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:

NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids

Deposition date:

2022-07-02

Original release date:

2023-01-03

Authors:

Li, Yunyan; Liu, Yong; Zhang, Huiqin; Wang, Zhen; Ruan, Maosen; Wang, Jiarong; Yang, Jing; Wu, Bo; Wang, Junfeng

Citation:

Citation: Li, Yunyan; Liu, Yong; Zhang, Huiqin; Wang, Zhen; Ruan, Maosen; Wang, Jiarong; Yang, Jing; Wu, Bo; Wang, Junfeng. "NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids" Magnetic Resonance Letters ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 123 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGENLYFQH RHMSPLYLEIIIYCTGAFLI SCMVGSVIVYKMKSGTKKSD FHSQMAVHKLAKSIPLRRQV TVSADSSASMNSGVLLVRPS RLSSSGTPMLAGVSEYELPE DPR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	131
15N chemical shifts	67
1H chemical shifts	67

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FGFR1 TMD-JMD	1

Entities:

Entity 1, FGFR1 TMD-JMD 123 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

GLU

ASN

LEU

TYR

PHE

GLN

HIS

3

ARG

HIS

MET

SER

PRO

LEU

TYR

LEU

GLU

ILE

4

ILE

TYR

CYS

THR

GLY

ALA

PHE

LEU

ILE

5

SER

CYS

MET

VAL

GLY

SER

VAL

ILE

VAL

TYR

6

LYS

MET

LYS

SER

GLY

THR

LYS

SER

ASP

7

PHE

HIS

SER

GLN

MET

ALA

VAL

HIS

LYS

LEU

8

ALA

LYS

SER

ILE

PRO

LEU

ARG

GLN

VAL

9

THR

VAL

SER

ALA

ASP

SER

ALA

SER

MET

10

ASN

SER

GLY

VAL

LEU

VAL

ARG

PRO

SER

11

ARG

LEU

SER

GLY

THR

PRO

MET

LEU

12

ALA

GLY

VAL

SER

GLU

TYR

GLU

LEU

PRO

GLU

13

ASP

PRO

ARG

Samples:

sample_1: FGFR1 TMD-JMD in Bicelles without DOPS, [U-100% 15N], 0.25 mM; FGFR1 TMD-JMD in Bicelles with 20% DOPS, [U-100% 15N], 0.25 mM; FGFR1 TMD-JMD in Bicelles without DOPS, [U-100% 13C; U-100% 15N], 0.4 mM; FGFR1 TMD-JMD in Bicelles with 20% DOPS, [U-100% 13C; U-100% 15N], 0.4 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.2; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker DMX 850 MHz

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