BMRB Entry 27981

Name: Backbone 1H, 13C, and 15N chemical shift assignments for C. elegans STIM EF-SAM in the presence of calcium.
Published: 2019-11-07

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27981

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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:

Backbone 1H, 13C, and 15N chemical shift assignments for C. elegans STIM EF-SAM in the presence of calcium.

Deposition date:

2019-07-22

Original release date:

2019-11-07

Authors:

Enomoto, Masahiro; Nishikawa, Tadateru; Back, Sung-In; Ishiyama, Noboru; Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko

Citation:

Citation: Enomoto, Masahiro; Nishikawa, Tadateru; Back, Sung-In; Ishiyama, Noboru; Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko. "Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain" J. Mol. Biol. 432, 367-383 (2020).
PubMed: 31626806

Assembly members:

Assembly members:
stromal_interaction_molecule, polymer, 176 residues, Formula weight is not available
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: roundworm Taxonomy ID: 6293 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
stromal_interaction_molecule: GSHMASDRVTRNVEVTAEEE KIRDKLGYEAIRDIHRDMDD DHSGSIDRNESTGFMKEDMQ MRGSERTRRENKFHGDDDAI TVDDLWEAWFESIERTWTNE RLVEWLINDVNLPSIVEAVK AKKIDGKILPRFASPNSDFL NKELGIKSSVYRQKLRLNSL DVVLFGYKDNNNRTKD

Data sets:

assigned_chemical_shifts
- holo

Data type	Count
13C chemical shifts	465
15N chemical shifts	147
1H chemical shifts	147

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	metal	2

Entities:

Entity 1, protein 176 residues - Formula weight is not available

Residues -5 to 0 are residual cloning artifact residues. Residues 23 to 192 are native protein residues.

1

GLY

SER

HIS

MET

ALA

SER

ASP

ARG

VAL

THR

2

ARG

ASN

VAL

GLU

VAL

THR

ALA

GLU

3

LYS

ILE

ARG

ASP

LYS

LEU

GLY

TYR

GLU

ALA

4

ILE

ARG

ASP

ILE

HIS

ARG

ASP

MET

ASP

5

ASP

HIS

SER

GLY

SER

ILE

ASP

ARG

ASN

GLU

6

SER

THR

GLY

PHE

MET

LYS

GLU

ASP

MET

GLN

7

MET

ARG

GLY

SER

GLU

ARG

THR

ARG

GLU

8

ASN

LYS

PHE

HIS

GLY

ASP

ALA

ILE

9

THR

VAL

ASP

LEU

TRP

GLU

ALA

TRP

PHE

10

GLU

SER

ILE

GLU

ARG

THR

TRP

THR

ASN

GLU

11

ARG

LEU

VAL

GLU

TRP

LEU

ILE

ASN

ASP

VAL

12

ASN

LEU

PRO

SER

ILE

VAL

GLU

ALA

VAL

LYS

13

ALA

LYS

ILE

ASP

GLY

LYS

ILE

LEU

PRO

14

ARG

PHE

ALA

SER

PRO

ASN

SER

ASP

PHE

LEU

15

ASN

LYS

GLU

LEU

GLY

ILE

LYS

SER

VAL

16

TYR

ARG

GLN

LYS

LEU

ARG

LEU

ASN

SER

LEU

17

ASP

VAL

LEU

PHE

GLY

TYR

LYS

ASP

ASN

18

ASN

ARG

THR

LYS

ASP

Entity 2, metal - Ca - 40.078 Da.

1

CA

Samples:

sample_1: Stromal interaction molecule, [U-99% 15N], 0.2 mM; TRIS 20 mM; sodium chloride 100 mM; calcium ion 5 mM

condition_1: ionic strength: 110 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

condition_2: ionic strength: 110 mM; pD: 7.9 pD; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	condition_1
3D CBCA(CO)NH	sample_1	isotropic	condition_1
3D HNCACB	sample_1	isotropic	condition_1
3D HNCO	sample_1	isotropic	condition_1
2D 1H-13C HSQC	sample_1	isotropic	condition_2

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMRDraw, Delaglio, Zhengrong and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

NCBI	ABG89384.1
UNP	G5EF60
AlphaFold	H2L0R5