BMRB Entry 18613

Name: NMR solution structure of Eph receptor
Published: 2013-07-22

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PDB ID: 2lw8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18613
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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 solution structure of Eph receptor

Deposition date:

2012-07-24

Original release date:

2013-07-22

Authors:

Qin, Haina; Song, Jianxing

Citation:

Citation: Qin, Haina; Lim, Liangzhong; Song, Jianxing. "Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations." BMC Biophys. 5, 2-2 (2012).
PubMed: 22277260

Assembly members:

Assembly members:
entity, polymer, 183 residues, 20989.896 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: PET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSNEVTLLDSRSVQGELGWI ASPLEGGWEEVSIMDEKNTP IRTYQVCNVMEPSQNNWLRT DWITREGAQRVYIEIKFTLR DCNSLPGVMGTCKETFNLYY YESDNDKERFIRENQFVKID TIAADESFTQVDIGDRIMKL NTEIRDVGPLSKKGFYLAFQ DVGACIALVSVRVFYKKAPL TVR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	449
15N chemical shifts	163
1H chemical shifts	948

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Eph receptor	1

Entities:

Entity 1, Eph receptor 183 residues - 20989.896 Da.

1

GLY

SER

ASN

GLU

VAL

THR

LEU

ASP

SER

2

ARG

SER

VAL

GLN

GLY

GLU

LEU

GLY

TRP

ILE

3

ALA

SER

PRO

LEU

GLU

GLY

TRP

GLU

4

VAL

SER

ILE

MET

ASP

GLU

LYS

ASN

THR

PRO

5

ILE

ARG

THR

TYR

GLN

VAL

CYS

ASN

VAL

MET

6

GLU

PRO

SER

GLN

ASN

TRP

LEU

ARG

THR

7

ASP

TRP

ILE

THR

ARG

GLU

GLY

ALA

GLN

ARG

8

VAL

TYR

ILE

GLU

ILE

LYS

PHE

THR

LEU

ARG

9

ASP

CYS

ASN

SER

LEU

PRO

GLY

VAL

MET

GLY

10

THR

CYS

LYS

GLU

THR

PHE

ASN

LEU

TYR

11

TYR

GLU

SER

ASP

ASN

ASP

LYS

GLU

ARG

PHE

12

ILE

ARG

GLU

ASN

GLN

PHE

VAL

LYS

ILE

ASP

13

THR

ILE

ALA

ASP

GLU

SER

PHE

THR

GLN

14

VAL

ASP

ILE

GLY

ASP

ARG

ILE

MET

LYS

LEU

15

ASN

THR

GLU

ILE

ARG

ASP

VAL

GLY

PRO

LEU

16

SER

LYS

GLY

PHE

TYR

LEU

ALA

PHE

GLN

17

ASP

VAL

GLY

ALA

CYS

ILE

ALA

LEU

VAL

SER

18

VAL

ARG

VAL

PHE

TYR

LYS

ALA

PRO

LEU

19

THR

VAL

ARG

Samples:

sample_1: protein, [U-99% 15N], 0.5 mM; potassium phosphate 10 mM; sodium azide 0.00002 mM; D2O 10 % v/v; H2O 100 % v/v; DTT 0 w/v

sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	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

Software:

CYANA, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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