BMRB Entry 51730

Name: Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)
Published: 2023-05-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51730

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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:

Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)

Deposition date:

2022-12-13

Original release date:

2023-05-24

Authors:

Adler, Agnes; Frosig Kjaer, Lenette; Baldus, Marc; van Ingen, Hugo

Citation:

Citation: Adler, Agnes; Kjaer, Lenette; Beugelink, J Wouter; Baldus, Marc; van Ingen, Hugo. "Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)" Biomol. NMR Assignments 17, 83-88 (2023).
PubMed: 37099260

Assembly members:

Assembly members:
entity_1, polymer, 112 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: pLICHIS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PVLRVDDRQRLARERREERE KQLAAREIVWLEREERARQH YEKHLEERKKRLEEQRQKEE RRRAAVEEKRRQRLEEDKER HEAVVRRTMERSQKPKQKHN RWSWGGSLHGSP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	348
15N chemical shifts	104
1H chemical shifts	367

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MAP7 MTBD	1

Entities:

Entity 1, MAP7 MTBD 112 residues - Formula weight is not available

1

PRO

VAL

LEU

ARG

VAL

ASP

ARG

GLN

ARG

2

LEU

ALA

ARG

GLU

ARG

GLU

ARG

GLU

3

LYS

GLN

LEU

ALA

ARG

GLU

ILE

VAL

TRP

4

LEU

GLU

ARG

GLU

ARG

ALA

ARG

GLN

HIS

5

TYR

GLU

LYS

HIS

LEU

GLU

ARG

LYS

6

ARG

LEU

GLU

GLN

ARG

GLN

LYS

GLU

7

ARG

ALA

VAL

GLU

LYS

ARG

8

ARG

GLN

ARG

LEU

GLU

ASP

LYS

GLU

ARG

9

HIS

GLU

ALA

VAL

ARG

THR

MET

GLU

10

ARG

SER

GLN

LYS

PRO

LYS

GLN

LYS

HIS

ASN

11

ARG

TRP

SER

TRP

GLY

SER

LEU

HIS

GLY

12

SER

PRO

Samples:

sample_1: MAP7 MTBD, [U-100% 13C; U-100% 15N], 150 uM; DTT 1 mM; sodium phosphate 40 mM; sodium chloride 150 mM; D2O 5%

sample_conditions_1: ionic strength: 212 mM; pH: 6.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CCCONH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY vPOKY version 1 - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 900 MHz

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