BMRB Entry 28085

Name: 1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid induced protein 2
Published: 2021-02-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28085

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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:

1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid induced protein 2

Deposition date:

2020-02-18

Original release date:

2021-02-18

Authors:

Lang, Andras; Goradia, Nishit; Wilmanns, Matthias; Ohlenschlaeger, Oliver

Citation:

Citation: Lang, Andras; Goradia, Nishit; Wikman, Harriet; Werner, Stefan; Wilmanns, Matthias; Ohlenschlaeger, Oliver. "1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid induced protein 2" Biomol. NMR Assignments 14, 271-275 (2020).
PubMed: 32557393

Assembly members:

Assembly members:
RAI2, polymer, 153 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: pETGB1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RAI2: GAMDSRHTVIKMGSENEALD LSMKSVPWLKAGEVSPPIFQ EDAALDLSVAAHRKSEPPPE TLYDSGASVDSSGHTVMEKL PSGMEISFAPATSHEAPAMM DSHISSSDAATEMLSQPNHP SGEVKAENNIEMVGESQAAK VIVSVEDAVPTIF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	443
15N chemical shifts	139
1H chemical shifts	289

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RAI2	1

Entities:

Entity 1, RAI2 153 residues - Formula weight is not available

Residues 1-4 represent a non-native cloning artifact

1

GLY

ALA

MET

ASP

SER

ARG

HIS

THR

VAL

ILE

2

LYS

MET

GLY

SER

GLU

ASN

GLU

ALA

LEU

ASP

3

LEU

SER

MET

LYS

SER

VAL

PRO

TRP

LEU

LYS

4

ALA

GLY

GLU

VAL

SER

PRO

ILE

PHE

GLN

5

GLU

ASP

ALA

LEU

ASP

LEU

SER

VAL

ALA

6

ALA

HIS

ARG

LYS

SER

GLU

PRO

GLU

7

THR

LEU

TYR

ASP

SER

GLY

ALA

SER

VAL

ASP

8

SER

GLY

HIS

THR

VAL

MET

GLU

LYS

LEU

9

PRO

SER

GLY

MET

GLU

ILE

SER

PHE

ALA

PRO

10

ALA

THR

SER

HIS

GLU

ALA

PRO

ALA

MET

11

ASP

SER

HIS

ILE

SER

ASP

ALA

12

THR

GLU

MET

LEU

SER

GLN

PRO

ASN

HIS

PRO

13

SER

GLY

GLU

VAL

LYS

ALA

GLU

ASN

ILE

14

GLU

MET

VAL

GLY

GLU

SER

GLN

ALA

LYS

15

VAL

ILE

VAL

SER

VAL

GLU

ASP

ALA

VAL

PRO

16

THR

ILE

PHE

Samples:

sample_1: RAI2, [U-99% 13C; U-99% 15N], 1 mM; TCEP 1.5 uM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.8; pressure: 1 atm; temperature: 297 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D (H)N(COCA)NNH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.6, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz

UNP	Q9Y5P3
AlphaFold	Q8N6X7