BMRB Entry 50940

Name: Drosophila melanogaster atypical Tm1 (aTm1) residues 1-213
Published: 2021-06-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50940

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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:

Drosophila melanogaster atypical Tm1 (aTm1) residues 1-213

Deposition date:

2021-05-12

Original release date:

2021-06-14

Authors:

Hennig, Janosch

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, 214 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: pET11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMEHDDSSTSGTGSHTASNT SLVPASLKRRGHQHHPRFSG TRRPNVPNVQEILAALYRGD SKSALSNLRGETQPEEEQPQ QQTEEVLPPSRSTLSLPLSE SVTNSLGSNSPTPTDESSVQ DEGASNPAAALIAEDAAPPA GTTTSKSKKKKREKGERSEK SDKSEKSDRKKKSSGKKERS KRSNPMEQSSDSLATDLSAG AIDEGIALADDDDN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	318
15N chemical shifts	169
1H chemical shifts	169

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	aTm1 (1-213)	1

Entities:

Entity 1, aTm1 (1-213) 214 residues - Formula weight is not available

1

SER

MET

GLU

HIS

ASP

SER

THR

SER

2

GLY

THR

GLY

SER

HIS

THR

ALA

SER

ASN

THR

3

SER

LEU

VAL

PRO

ALA

SER

LEU

LYS

ARG

4

GLY

HIS

GLN

HIS

PRO

ARG

PHE

SER

GLY

5

THR

ARG

PRO

ASN

VAL

PRO

ASN

VAL

GLN

6

GLU

ILE

LEU

ALA

LEU

TYR

ARG

GLY

ASP

7

SER

LYS

SER

ALA

LEU

SER

ASN

LEU

ARG

GLY

8

GLU

THR

GLN

PRO

GLU

GLN

PRO

GLN

9

GLN

THR

GLU

VAL

LEU

PRO

SER

10

ARG

SER

THR

LEU

SER

LEU

PRO

LEU

SER

GLU

11

SER

VAL

THR

ASN

SER

LEU

GLY

SER

ASN

SER

12

PRO

THR

PRO

THR

ASP

GLU

SER

VAL

GLN

13

ASP

GLU

GLY

ALA

SER

ASN

PRO

ALA

14

LEU

ILE

ALA

GLU

ASP

ALA

PRO

ALA

15

GLY

THR

SER

LYS

SER

LYS

16

LYS

ARG

GLU

LYS

GLY

GLU

ARG

SER

GLU

LYS

17

SER

ASP

LYS

SER

GLU

LYS

SER

ASP

ARG

LYS

18

LYS

SER

GLY

LYS

GLU

ARG

SER

19

LYS

ARG

SER

ASN

PRO

MET

GLU

GLN

SER

20

ASP

SER

LEU

ALA

THR

ASP

LEU

SER

ALA

GLY

21

ALA

ILE

ASP

GLU

GLY

ILE

ALA

LEU

ALA

ASP

22

ASP

ASN

Samples:

sample_1: aTm1 (1-213), [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:

CARA v1.9.1 - 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