BMRB Entry 15496

Name: Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists
Published: 2008-01-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15496

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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:

Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists

Deposition date:

2007-09-27

Original release date:

2008-01-25

Authors:

Fenwick, Michael; Oswald, Robert

Citation:

Citation: Fenwick, Michael; Oswald, Robert. "Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists" Biomol. NMR Assignments 1, 241-243 (2007).
PubMed: 19636875

Assembly members:

Assembly members:
S1S2, polymer, 263 residues, Formula weight is not available
KAI, non-polymer, 215.246 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S1S2: GANKTVVVTTILESPYVMMK KNHEMLEGNERYEGYCVDLA AEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVY GKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDS GSTKEFFRRSKIAVFDKMWT YMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYI EQRKPCDTMKVGGNLDSKGY GIATPKGSSLGNAVNLAVLK LNEQGLLDKLKNKWWYDKGE CGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	509
15N chemical shifts	250
1H chemical shifts	250

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S1S2	1
2	kainate	2

Entities:

Entity 1, S1S2 263 residues - Formula weight is not available

1

GLY

ALA

ASN

LYS

THR

VAL

THR

2

ILE

LEU

GLU

SER

PRO

TYR

VAL

MET

LYS

3

LYS

ASN

HIS

GLU

MET

LEU

GLU

GLY

ASN

GLU

4

ARG

TYR

GLU

GLY

TYR

CYS

VAL

ASP

LEU

ALA

5

ALA

GLU

ILE

ALA

LYS

HIS

CYS

GLY

PHE

LYS

6

TYR

LYS

LEU

THR

ILE

VAL

GLY

ASP

GLY

LYS

7

TYR

GLY

ALA

ARG

ASP

ALA

ASP

THR

LYS

ILE

8

TRP

ASN

GLY

MET

VAL

GLY

GLU

LEU

VAL

TYR

9

GLY

LYS

ALA

ASP

ILE

ALA

ILE

ALA

PRO

LEU

10

THR

ILE

THR

LEU

VAL

ARG

GLU

VAL

ILE

11

ASP

PHE

SER

LYS

PRO

PHE

MET

SER

LEU

GLY

12

ILE

SER

ILE

MET

ILE

LYS

GLY

THR

PRO

13

ILE

GLU

SER

ALA

GLU

ASP

LEU

SER

LYS

GLN

14

THR

GLU

ILE

ALA

TYR

GLY

THR

LEU

ASP

SER

15

GLY

SER

THR

LYS

GLU

PHE

ARG

SER

16

LYS

ILE

ALA

VAL

PHE

ASP

LYS

MET

TRP

THR

17

TYR

MET

ARG

SER

ALA

GLU

PRO

SER

VAL

PHE

18

VAL

ARG

THR

ALA

GLU

GLY

VAL

ALA

ARG

19

VAL

ARG

LYS

SER

LYS

GLY

LYS

TYR

ALA

TYR

20

LEU

GLU

SER

THR

MET

ASN

GLU

TYR

ILE

21

GLU

GLN

ARG

LYS

PRO

CYS

ASP

THR

MET

LYS

22

VAL

GLY

ASN

LEU

ASP

SER

LYS

GLY

TYR

23

GLY

ILE

ALA

THR

PRO

LYS

GLY

SER

LEU

24

GLY

ASN

ALA

VAL

ASN

LEU

ALA

VAL

LEU

LYS

25

LEU

ASN

GLU

GLN

GLY

LEU

ASP

LYS

LEU

26

LYS

ASN

LYS

TRP

TYR

ASP

LYS

GLY

GLU

27

CYS

GLY

SER

Entity 2, kainate - C10 H17 N O4 - 215.246 Da.

1

KAI

Samples:

sample_1: S1S2, [U-98% 13C; U-98% 15N; U-95% 2H], 0.25-0.35 mM; kainate 7 mM; sodium chloride 25 mM; sodium acetate 25 mM; sodium azide 3 mM

sample_conditions_1: ionic strength: 53.0 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 500 MHz

Related Database Links:

BMRB	15492 15493 15494 15495
PDB	1FTJ 1FTK 1FTL 1FTM 1FTO 1FW0 1GR2 1LB8 1LB9 1LBB 1LBC 1M5B 1M5C 1M5D 1M5E 1M5F 1MM6 1MM7 1MQD 1MQG 1MQH 1MQI 1MQJ 1MS7 1MXU 1MXV 1MXW 1MXX 1MXY 1MXZ 1MY0 1MY1 1MY2 1MY3 1MY4 1N0T 1NNK 1NNP 1P1N 1P1O 1P1Q 1P1U 1P1W 1SYH 1SYI 1WVJ 1XHY 2AIX 2AL4 2AL5 2ANJ 2CMO 2GFE 2I3V 2I3W 2P2A 2UXA 2XHD 2XX7 2XX8 2XX9 2XXH 2XXI 3B6Q 3B6T 3B6W 3B7D 3BBR 3BFT 3BFU 3BKI 3DP6 3H03 3H06 3H6T 3H6U 3H6V 3H6W 3IJO 3IJX 3IK6 3IL1 3ILT 3ILU 3KGC 3LSF 3LSL 3M3L 3O28 3O29 3O2A 3O6G 3O6H 3O6I 3PD8 3PD9 3PMV 3PMW 3PMX 3R7X 3RN8 3RNN 3RTF 3RTW 3T93 3T96 3T9H 3T9U 3T9V 3T9X 3TDJ 3TKD 3TZA 3UA8 4FAT 4G8M 4GXS 4H8J 4IGT 4ISU 4IY5 4IY6 4L17 4LZ5 4LZ7 4LZ8 4N07 4O3A 4O3B 4O3C 4Q30 4U1O 4U1Z 4U21 4U22 4U23 4U2R 4U4S 4U4X 4X48 4YMA
GB	AAB03114 ABV25011 EAX04871
REF	XP_010160138

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