BMRB Entry 25691

Name: The solution structure of the kallikrein inhibitor SPINK6
Published: 2016-03-14

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PDB ID: 2n52
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25691
MolProbity Validation Chart

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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:

The solution structure of the kallikrein inhibitor SPINK6

Deposition date:

2015-07-06

Original release date:

2016-03-14

Authors:

Groetzinger, Joachim

Citation:

Citation: Jung, Sascha; Fischer, Jan; Spudy, Bjorn; Kerkow, Tim; Sonnichsen, Frank; Xue, Li; Bonvin, Alexandre; Goettig, Peter; Magdolen, Viktor; Meyer-Hoffert, Ulf; Groetzinger, Joachim. "The solution structure of the kallikrein-related peptidases inhibitor SPINK6" Biochem. Biophys. Res. Commun. 471, 103-108 (2016).
PubMed: 26828269

Assembly members:

Assembly members:
entity, polymer, 57 residues, 6077.895 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: pet32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QGGQVDCGEFQDTKVYCTRE SNPHCGSDGQTYGNKCAFCK AIVKSGGKISLKHPGKC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	55
1H chemical shifts	263

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 57 residues - 6077.895 Da.

1

GLN

GLY

GLN

VAL

ASP

CYS

GLY

GLU

PHE

2

GLN

ASP

THR

LYS

VAL

TYR

CYS

THR

ARG

GLU

3

SER

ASN

PRO

HIS

CYS

GLY

SER

ASP

GLY

GLN

4

THR

TYR

GLY

ASN

LYS

CYS

ALA

PHE

CYS

LYS

5

ALA

ILE

VAL

LYS

SER

GLY

LYS

ILE

SER

6

LEU

LYS

HIS

PRO

GLY

LYS

CYS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM; Phosphat 10 mM; NaCl 150 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 303 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 HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker AMX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks