BMRB Entry 15719

Name: Assignment of the central region (131-28) of human h1 calponin
Published: 2008-05-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15719

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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:

Assignment of the central region (131-28) of human h1 calponin

Deposition date:

2008-04-07

Original release date:

2008-05-05

Authors:

Pfuhl, Mark; El Mezgueldi, Mohammed

Citation:

Citation: Pfuhl, Mark; Al-Sarayreh, Sameeh; El-Mezgueldi, Mohammed. "The calponin regulatory region is intrinsically unstructured: novel insight into actin-calponin and calmodulin-calponin interfaces using NMR spectroscopy." Biophys. J. 100, 1718-1728 (2011).
PubMed: 21463585

Assembly members:

Assembly members:
calponin, polymer, 98 residues, 10807.3 Da.

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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
calponin: AKTKGNKVNVGVKYAEKQER RFEPEKLREGRNIIGLQMGI NKFASQQGMTAYGTRRHLYD PKLGTDQPLDQATISLQMGT NKGASQAGMTAPGTKRQI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	307
15N chemical shifts	83
1H chemical shifts	425

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calponin h1 131-228	1

Entities:

Entity 1, calponin h1 131-228 98 residues - 10807.3 Da.

1

ALA

LYS

THR

LYS

GLY

ASN

LYS

VAL

ASN

VAL

2

GLY

VAL

LYS

TYR

ALA

GLU

LYS

GLN

GLU

ARG

3

ARG

PHE

GLU

PRO

GLU

LYS

LEU

ARG

GLU

GLY

4

ARG

ASN

ILE

GLY

LEU

GLN

MET

GLY

ILE

5

ASN

LYS

PHE

ALA

SER

GLN

GLY

MET

THR

6

ALA

TYR

GLY

THR

ARG

HIS

LEU

TYR

ASP

7

PRO

LYS

LEU

GLY

THR

ASP

GLN

PRO

LEU

ASP

8

GLN

ALA

THR

ILE

SER

LEU

GLN

MET

GLY

THR

9

ASN

LYS

GLY

ALA

SER

GLN

ALA

GLY

MET

THR

10

ALA

PRO

GLY

THR

LYS

ARG

GLN

ILE

Samples:

sample_1: calponin, [U-100% 15N], 1.5 ± 0.1 mM; D2O 5 ± 0.1 %; H2O 95 ± 0.1 %; DTT 2 ± 0.05 mM; potassium phosphate 20 ± 1 mM; sodium chloride 20 ± 1 mM; sodium azide 0.02 ± 0.0005 %

sample_2: calponin, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; D2O 5 ± 0.1 %; H2O 95 ± 0.1 %; DTT 2 ± 0.05 mM; potassium phosphate 20 ± 1 mM; sodium chloride 20 ± 1 mM; sodium azide 0.02 ± 0.0005 %

sample_conditions_1: ionic strength: 0.4 M; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D (H)C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CBCA)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CBCACO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - processing

CCPN_analysis v1.1, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz