BMRB Entry 16370

Name: Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158.
Published: 2009-06-29

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PDB ID: 2kkq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16370
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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:

Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158.

Deposition date:

2009-06-29

Original release date:

2009-06-29

Authors:

Rossi, Paolo; Shastry, Ritu; Ciccosanti, Colleen; Hamilton, Keith; Xiao, Rong; Acton, Thomas; G.V.T., Swapna; Nair, Rajeesh; Everett, John; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Montelione, Gaetano. "Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158." .

Assembly members:

Assembly members:
Ig-like C2-type 2 Domain, polymer, 116 residues, 13338.323 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: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ig-like C2-type 2 Domain: MGHHHHHHSHEHKRAPMFIY KPQSKKVLEGDSVKLECQIS AIPPPKLFWKRNNEMVQFNT DRISLYQDNTGRVTLLIKDV NKKDAGWYTVSAVNEAGVTT CNTRLDVTARPNQTLP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	458
15N chemical shifts	113
1H chemical shifts	726

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ig-like C2-type 2 Domain	1

Entities:

Entity 1, Ig-like C2-type 2 Domain 116 residues - 13338.323 Da.

1

MET

GLY

HIS

SER

HIS

2

GLU

HIS

LYS

ARG

ALA

PRO

MET

PHE

ILE

TYR

3

LYS

PRO

GLN

SER

LYS

VAL

LEU

GLU

GLY

4

ASP

SER

VAL

LYS

LEU

GLU

CYS

GLN

ILE

SER

5

ALA

ILE

PRO

LYS

LEU

PHE

TRP

LYS

6

ARG

ASN

GLU

MET

VAL

GLN

PHE

ASN

THR

7

ASP

ARG

ILE

SER

LEU

TYR

GLN

ASP

ASN

THR

8

GLY

ARG

VAL

THR

LEU

ILE

LYS

ASP

VAL

9

ASN

LYS

ASP

ALA

GLY

TRP

TYR

THR

VAL

10

SER

ALA

VAL

ASN

GLU

ALA

GLY

VAL

THR

11

CYS

ASN

THR

ARG

LEU

ASP

VAL

THR

ALA

ARG

12

PRO

ASN

GLN

THR

LEU

PRO

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC hires	sample_2	isotropic	sample_conditions_1
2D 1H-15N het_NOE	sample_2	isotropic	sample_conditions_1
1D 15N_T1 series	sample_2	isotropic	sample_conditions_1
1D 15N_T2 series	sample_2	isotropic	sample_conditions_1

BMRB Entry 16370

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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