BMRB Entry 50743

Name: dmEB1N+linker
Published: 2021-03-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50743

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

dmEB1N+linker

Deposition date:

2021-02-01

Original release date:

2021-03-01

Authors:

Dimitrova-Paternoga, Lyudmila

Citation:

Citation: Vaishali, Vaishali; Dimitrova-Paternoga, Lyudmila; Haubrich, Kevin; Sun, Mai; Ephrussi, Anne; Hennig, Janosch. "Validation and classification of RNA binding proteins identified by mRNA interactome capture" RNA 27, 1173-1185 (2021).
PubMed: 34215685

Assembly members:

Assembly members:
entity_1, polymer, 209 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAVNVYSTNVTSENLSRHDM LAWVNDCLQSQFSKIEELCT GAAYCQFMDMLFPNSVPVKR VKFRTNLEHEYIQNFKILQA GFKKMSVDKIIPIDKLVKGR FQDNFEFLQWFKKFFDANYD GRDYDASAVREGAPMGFGSG AVKSLPGTAASGVSSSYRRG PSATTRPAMTSAVKPTVSKV LPRTNNAAPASRINACANST GTVKKNDVS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	581
15N chemical shifts	191
1H chemical shifts	191

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EB1-N+Linker	1

Entities:

Entity 1, EB1-N+Linker 209 residues - Formula weight is not available

1

MET

ALA

VAL

ASN

VAL

TYR

SER

THR

ASN

VAL

2

THR

SER

GLU

ASN

LEU

SER

ARG

HIS

ASP

MET

3

LEU

ALA

TRP

VAL

ASN

ASP

CYS

LEU

GLN

SER

4

GLN

PHE

SER

LYS

ILE

GLU

LEU

CYS

THR

5

GLY

ALA

TYR

CYS

GLN

PHE

MET

ASP

MET

6

LEU

PHE

PRO

ASN

SER

VAL

PRO

VAL

LYS

ARG

7

VAL

LYS

PHE

ARG

THR

ASN

LEU

GLU

HIS

GLU

8

TYR

ILE

GLN

ASN

PHE

LYS

ILE

LEU

GLN

ALA

9

GLY

PHE

LYS

MET

SER

VAL

ASP

LYS

ILE

10

ILE

PRO

ILE

ASP

LYS

LEU

VAL

LYS

GLY

ARG

11

PHE

GLN

ASP

ASN

PHE

GLU

PHE

LEU

GLN

TRP

12

PHE

LYS

PHE

ASP

ALA

ASN

TYR

ASP

13

GLY

ARG

ASP

TYR

ASP

ALA

SER

ALA

VAL

ARG

14

GLU

GLY

ALA

PRO

MET

GLY

PHE

GLY

SER

GLY

15

ALA

VAL

LYS

SER

LEU

PRO

GLY

THR

ALA

16

SER

GLY

VAL

SER

TYR

ARG

GLY

17

PRO

SER

ALA

THR

ARG

PRO

ALA

MET

THR

18

SER

ALA

VAL

LYS

PRO

THR

VAL

SER

LYS

VAL

19

LEU

PRO

ARG

THR

ASN

ALA

PRO

ALA

20

SER

ARG

ILE

ASN

ALA

CYS

ALA

ASN

SER

THR

21

GLY

THR

VAL

LYS

ASN

ASP

VAL

SER

Samples:

sample_1: EB1-N+Linker, [U-100% 15N], 200 uM; PO4 20 mM; NaCl 150 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR v2.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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