BMRB Entry 50120

Name: Intramolecular synergy enhances the microtubule end-binding affinity of EB1
Published: 2020-02-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50120

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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: Intramolecular synergy enhances the microtubule end-binding affinity of EB1

Deposition date: 2019-12-10 Original release date: 2020-02-19

Authors: Xue, Yi; Pan, Ying

Citation: Liang, .; Song, .; Zhang, .; Pan, .; He, .; Wang, .; Chen, .; Guo, .; Deng, .; Xue, Yi; Fang, Ying. "Intramolecular synergy enhances the microtubule end-binding affinity of EB1" .

Assembly members:
entity_1, polymer, 61 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28a-SUMO

Entity Sequences (FASTA):
entity_1: QGQETAVAPSLVAPALNKPK KPLDDDDAAPQRPISTQRTA AAPKAGPGVVRKNPGVGNGD D

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	116
15N chemical shifts	51
1H chemical shifts	50
T1 relaxation values	45
T2 relaxation values	47
heteronuclear NOE values	45

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EB1linker-4D	1

Entities:

Entity 1, EB1linker-4D 61 residues - Formula weight is not available

1

GLN

GLY

GLN

GLU

THR

ALA

VAL

ALA

PRO

SER

2

LEU

VAL

ALA

PRO

ALA

LEU

ASN

LYS

PRO

LYS

3

LYS

PRO

LEU

ASP

ALA

PRO

4

GLN

ARG

PRO

ILE

SER

THR

GLN

ARG

THR

ALA

5

ALA

PRO

LYS

ALA

GLY

PRO

GLY

VAL

6

ARG

LYS

ASN

PRO

GLY

VAL

GLY

ASN

GLY

ASP

7

ASP

Samples:

sample_1: entity_1, [U-99% 15N], 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%; sodium azide 0.01%; DSS 20 uM

sample_2: entity_1, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%; sodium azide 0.01%; DSS 20 uM

sample_conditions_1: ionic strength: 0.17 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
15N-(1H) NOE	sample_1	isotropic	sample_conditions_1
15N R1	sample_1	isotropic	sample_conditions_1
15N R2	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.01, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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