BMRB Entry 11212

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PDB ID: 2dav
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11212
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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 structure of the first ig-like domain of Myosin-binding protein C, slow-type

Deposition date:

2010-07-22

Original release date:

2011-07-21

Authors:

Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation:

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the first ig-like domain of Myosin-binding protein C, slow-type" .

Assembly members:

Assembly members:
IG domain, polymer, 126 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: cell free synthesis Host organism: E. coli - cell free Vector: P050302-60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IG domain: GSSGSSGILFIEKPQGGTVK VGEDITFIAKVKAEDLLRKP TIKWFKGKWMDLASKAGKHL QLKETFERHSRVYTFEMQII KAKDNFAGNYRCEVTYKDKF DSCSFDLEVHESTGTTPNID SGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	550
15N chemical shifts	114
1H chemical shifts	865

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IG domain of Myosin-binding protein C, slow-type	1

Entities:

Entity 1, IG domain of Myosin-binding protein C, slow-type 126 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ILE

LEU

PHE

2

ILE

GLU

LYS

PRO

GLN

GLY

THR

VAL

LYS

3

VAL

GLY

GLU

ASP

ILE

THR

PHE

ILE

ALA

LYS

4

VAL

LYS

ALA

GLU

ASP

LEU

ARG

LYS

PRO

5

THR

ILE

LYS

TRP

PHE

LYS

GLY

LYS

TRP

MET

6

ASP

LEU

ALA

SER

LYS

ALA

GLY

LYS

HIS

LEU

7

GLN

LEU

LYS

GLU

THR

PHE

GLU

ARG

HIS

SER

8

ARG

VAL

TYR

THR

PHE

GLU

MET

GLN

ILE

9

LYS

ALA

LYS

ASP

ASN

PHE

ALA

GLY

ASN

TYR

10

ARG

CYS

GLU

VAL

THR

TYR

LYS

ASP

LYS

PHE

11

ASP

SER

CYS

SER

PHE

ASP

LEU

GLU

VAL

HIS

12

GLU

SER

THR

GLY

THR

PRO

ASN

ILE

ASP

13

SER

GLY

PRO

SER

GLY

Samples:

sample_1: IG domain, [U-13C; U-15N], 1.32 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 900 MHz

PDB	2DAV
DBJ	BAF85665 BAG51755 BAG59277 BAH13954
EMBL	CAD38625 CAD38925 CAD89907 CAD89927 CAD91144
GB	AAI43504 AAI43505 ACE86664 ACE87348 EAW97664
REF	NP_001241647 NP_001241648 NP_001241649 NP_002456 NP_996555
SP	Q00872
AlphaFold	Q00872