BMRB Entry 15766

Name: human calpastatin Domain 1
Published: 2008-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15766

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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:

human calpastatin Domain 1

Deposition date:

2008-05-09

Original release date:

2008-06-30

Authors:

Kiss, Robert

Citation:

Citation: Kiss, Robert; Kovacs, D.; Tompa, P.; Perczel, Andras. "Local Structural Preferences of Calpastatin, the Intrinsically Unstructured Protein Inhibitor of Calpain" Biochemistry 47, 6936-6945 (2008).
PubMed: 18537264

Assembly members:

Assembly members:
hCSD1, polymer, 141 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: pEThCSD1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hCSD1: AVPVESKPDKPSGKSGMDAA LDDLIDTLGGPEETEEENTT YTGPEVSDPMSSTYIEELGK REVTIPPKYRELLAKKEGIT GPPADSSKPIGPDDAIDALS SDFTCGSPTAAGKKTEKEES TEVLKAQSAGTVRSAAPPQE K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	256
15N chemical shifts	122
1H chemical shifts	249
T1 relaxation values	90
T2 relaxation values	90

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hCSD1	1

Entities:

Entity 1, hCSD1 141 residues - Formula weight is not available

1

ALA

VAL

PRO

VAL

GLU

SER

LYS

PRO

ASP

LYS

2

PRO

SER

GLY

LYS

SER

GLY

MET

ASP

ALA

3

LEU

ASP

LEU

ILE

ASP

THR

LEU

GLY

4

PRO

GLU

THR

GLU

ASN

THR

5

TYR

THR

GLY

PRO

GLU

VAL

SER

ASP

PRO

MET

6

SER

THR

TYR

ILE

GLU

LEU

GLY

LYS

7

ARG

GLU

VAL

THR

ILE

PRO

LYS

TYR

ARG

8

GLU

LEU

ALA

LYS

GLU

GLY

ILE

THR

9

GLY

PRO

ALA

ASP

SER

LYS

PRO

ILE

10

GLY

PRO

ASP

ALA

ILE

ASP

ALA

LEU

SER

11

SER

ASP

PHE

THR

CYS

GLY

SER

PRO

THR

ALA

12

ALA

GLY

LYS

THR

GLU

LYS

GLU

SER

13

THR

GLU

VAL

LEU

LYS

ALA

GLN

SER

ALA

GLY

14

THR

VAL

ARG

SER

ALA

PRO

GLN

GLU

15

LYS

Samples:

sample_1: hCSD1, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 10 M; pH: 6.07; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker DRX 500 MHz

DBJ	BAH14064
GB	AAA52753 AAA52759 AAB59398
SP	P49342
AlphaFold	P49342