BMRB Entry 18348

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain
Published: 2012-11-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18348

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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 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain

Deposition date:

2012-03-26

Original release date:

2012-11-15

Authors:

Kanaba, Teppei; Mishima, Masaki

Citation:

Citation: Kanaba, Teppei; Maesaki, Ryoko; Mori, Tomoyuki; Ito, Yutaka; Hakoshima, Toshio; Mishima, Masaki. "Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR." Biochim. Biophys. Acta 1834, 499-507 (2013).
PubMed: 23128140

Assembly members:

Assembly members:
EB1_CH_domain, polymer, 133 residues, Formula weight is not available

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: pET47b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EB1_CH_domain: GPGMAVNVYSTSVTSDNLSR HDMLAWINESLQLNLTKIEQ LCSGAAYCQFMDMLFPGSIA LKKVKFQAKLEHEYIQNFKI LQAGFKRMGVDKIIPVDKLV KGKFQDNFEFVQWFKKFFDA NYDGKDYDPVAAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	126
1H chemical shifts	126

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EB1 CH domain	1

Entities:

Entity 1, EB1 CH domain 133 residues - Formula weight is not available

1

GLY

PRO

GLY

MET

ALA

VAL

ASN

VAL

TYR

SER

2

THR

SER

VAL

THR

SER

ASP

ASN

LEU

SER

ARG

3

HIS

ASP

MET

LEU

ALA

TRP

ILE

ASN

GLU

SER

4

LEU

GLN

LEU

ASN

LEU

THR

LYS

ILE

GLU

GLN

5

LEU

CYS

SER

GLY

ALA

TYR

CYS

GLN

PHE

6

MET

ASP

MET

LEU

PHE

PRO

GLY

SER

ILE

ALA

7

LEU

LYS

VAL

LYS

PHE

GLN

ALA

LYS

LEU

8

GLU

HIS

GLU

TYR

ILE

GLN

ASN

PHE

LYS

ILE

9

LEU

GLN

ALA

GLY

PHE

LYS

ARG

MET

GLY

VAL

10

ASP

LYS

ILE

PRO

VAL

ASP

LYS

LEU

VAL

11

LYS

GLY

LYS

PHE

GLN

ASP

ASN

PHE

GLU

PHE

12

VAL

GLN

TRP

PHE

LYS

PHE

ASP

ALA

13

ASN

TYR

ASP

GLY

LYS

ASP

TYR

ASP

PRO

VAL

14

ALA

ARG

Samples:

sample_1: EB1 CH domain, [U-13C; U-15N], 1.0 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.4 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz

PDB	1PA7 1UEG 1VKA 2R8U
DBJ	BAE32461 BAE89438 BAG35484 BAG73401
EMBL	CAG31466 CAH92115
GB	AAA96320 AAC09471 AAH52405 AAH64444 AAH81726
REF	NP_001026031 NP_001038078 NP_001068802 NP_001126236 NP_001238875
SP	Q15691 Q3ZBD9 Q5R7Z5 Q5ZLC7 Q61166
TPG	DAA23186
AlphaFold	Q15691 Q3ZBD9 Q5R7Z5 Q5ZLC7 Q61166