BMRB Entry 27997

Name: Chemical shift assignments for RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348
Published: 2020-07-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27997

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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:

Chemical shift assignments for RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348

Deposition date:

2019-08-12

Original release date:

2020-07-09

Authors:

Peti, Wolfgang; Li, Yang; Page, Rebecca; Sheftic, Sarah

Citation:

Citation: Li, Yang; Sheftic, Sarah; Grigoriu, Simina; Schwieters, Charles; Page, Rebecca; Peti, Wolfgang. "The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin" Sci. Adv. 6, 3681-3681 (2020).
PubMed: 32936779

Assembly members:

Assembly members:
RCAN1_residues_128-164, polymer, 40 residues, Formula weight is not available
Calcineurin_catalytic_subunit_A_residues_27-348, polymer, 327 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: pTHMT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RCAN1_residues_128-164: GHMNYDLLYAISKLGPGEKY ELHAATDTTPSVVITVCESD
Calcineurin_catalytic_subunit_A_residues_27-348: GHMHRLTAKEVFDNDGKPRV DILKAHLMKEGRLEESVALR IITEGASILRQEKNLLDIDA PVTVCGDIHGQFFDLMKLFE VGGSPANTRYLFLGDYVDRG YFSIECVLYLWALKILYPKT LFLLRGNHECRHLTEYFTFK QECKIKYSERVYDACMDAFD CLPLAALMNQQFLCVHGGLS PEINTLDDIRKLDRFKEPPA YGPMCDILWSDPLEDFGNEK TQEHFTHNTVRGCSYFYSYP AVCEFLQHNNLLSILRAHEA QDAGYRMYRKSQTTGFPSLI TIFSAPNYLDVYNNKAAVLK YENNVMNIRQFNCSPHPYWL PNFMDDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	83
15N chemical shifts	35
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RCAN1	1
2	Calcineurin subunit A	2

Entities:

Entity 1, RCAN1 40 residues - Formula weight is not available

GHM are cloning artifact; RCAN1 sequence starts with NYDL

1	GLY	HIS	MET	ASN	TYR	ASP	LEU	LEU	TYR	ALA
2	ILE	SER	LYS	LEU	GLY	PRO	GLY	GLU	LYS	TYR
3	GLU	LEU	HIS	ALA	ALA	THR	ASP	THR	THR	PRO
4	SER	VAL	VAL	ILE	THR	VAL	CYS	GLU	SER	ASP

Entity 2, Calcineurin subunit A 327 residues - Formula weight is not available

GHM are cloning artifact; calcineurin sequence starts with HRLT; the C-terminal DD are introduced to increase solubility.

1

GLY

HIS

MET

HIS

ARG

LEU

THR

ALA

LYS

GLU

2

VAL

PHE

ASP

ASN

ASP

GLY

LYS

PRO

ARG

VAL

3

ASP

ILE

LEU

LYS

ALA

HIS

LEU

MET

LYS

GLU

4

GLY

ARG

LEU

GLU

SER

VAL

ALA

LEU

ARG

5

ILE

THR

GLU

GLY

ALA

SER

ILE

LEU

ARG

6

GLN

GLU

LYS

ASN

LEU

ASP

ILE

ASP

ALA

7

PRO

VAL

THR

VAL

CYS

GLY

ASP

ILE

HIS

GLY

8

GLN

PHE

ASP

LEU

MET

LYS

LEU

PHE

GLU

9

VAL

GLY

SER

PRO

ALA

ASN

THR

ARG

TYR

10

LEU

PHE

LEU

GLY

ASP

TYR

VAL

ASP

ARG

GLY

11

TYR

PHE

SER

ILE

GLU

CYS

VAL

LEU

TYR

LEU

12

TRP

ALA

LEU

LYS

ILE

LEU

TYR

PRO

LYS

THR

13

LEU

PHE

LEU

ARG

GLY

ASN

HIS

GLU

CYS

14

ARG

HIS

LEU

THR

GLU

TYR

PHE

THR

PHE

LYS

15

GLN

GLU

CYS

LYS

ILE

LYS

TYR

SER

GLU

ARG

16

VAL

TYR

ASP

ALA

CYS

MET

ASP

ALA

PHE

ASP

17

CYS

LEU

PRO

LEU

ALA

LEU

MET

ASN

GLN

18

GLN

PHE

LEU

CYS

VAL

HIS

GLY

LEU

SER

19

PRO

GLU

ILE

ASN

THR

LEU

ASP

ILE

ARG

20

LYS

LEU

ASP

ARG

PHE

LYS

GLU

PRO

ALA

21

TYR

GLY

PRO

MET

CYS

ASP

ILE

LEU

TRP

SER

22

ASP

PRO

LEU

GLU

ASP

PHE

GLY

ASN

GLU

LYS

23

THR

GLN

GLU

HIS

PHE

THR

HIS

ASN

THR

VAL

24

ARG

GLY

CYS

SER

TYR

PHE

TYR

SER

TYR

PRO

25

ALA

VAL

CYS

GLU

PHE

LEU

GLN

HIS

ASN

26

LEU

SER

ILE

LEU

ARG

ALA

HIS

GLU

ALA

27

GLN

ASP

ALA

GLY

TYR

ARG

MET

TYR

ARG

LYS

28

SER

GLN

THR

GLY

PHE

PRO

SER

LEU

ILE

29

THR

ILE

PHE

SER

ALA

PRO

ASN

TYR

LEU

ASP

30

VAL

TYR

ASN

LYS

ALA

VAL

LEU

LYS

31

TYR

GLU

ASN

VAL

MET

ASN

ILE

ARG

GLN

32

PHE

ASN

CYS

SER

PRO

HIS

PRO

TYR

TRP

LEU

33

PRO

ASN

PHE

MET

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

UNP	P53805-2 Q08209 P53805-2
AlphaFold	Q9UME4 Q8TAW9 Q9UME4

BMRB Entry 27997

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	HIS	MET	ASN	TYR	ASP	LEU	LEU	TYR	ALA
2	ILE	SER	LYS	LEU	GLY	PRO	GLY	GLU	LYS	TYR
3	GLU	LEU	HIS	ALA	ALA	THR	ASP	THR	THR	PRO
4	SER	VAL	VAL	ILE	THR	VAL	CYS	GLU	SER	ASP

1	GLY	HIS	MET	ASN	TYR	ASP	LEU	LEU	TYR	ALA
2	ILE	SER	LYS	LEU	GLY	PRO	GLY	GLU	LYS	TYR
3	GLU	LEU	HIS	ALA	ALA	THR	ASP	THR	THR	PRO
4	SER	VAL	VAL	ILE	THR	VAL	CYS	GLU	SER	ASP

1	GLY	HIS	MET	ASN	TYR	ASP	LEU	LEU	TYR	ALA
2	ILE	SER	LYS	LEU	GLY	PRO	GLY	GLU	LYS	TYR
3	GLU	LEU	HIS	ALA	ALA	THR	ASP	THR	THR	PRO
4	SER	VAL	VAL	ILE	THR	VAL	CYS	GLU	SER	ASP