BMRB Entry 18627

Name: 1H, 13C, and 15N Chemical Shift Assignments for Calcium free, Myristoylated Visinin-like protein 3
Published: 2013-02-14

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PDB ID: 5t7c
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18627
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for Calcium free, Myristoylated Visinin-like protein 3

Deposition date:

2012-07-31

Original release date:

2013-02-14

Authors:

Li, Congmin; Ames, James

Citation:

Citation: Li, Congmin; Ames, James. "H, 13C, and 15N chemical shift assignments of neuronal calcium sensor protein, hippocalcin." Biomol. NMR Assignments 8, 63-66 (2014).
PubMed: 23250791

Assembly members:

Assembly members:
VILIP-3 monomer, polymer, 193 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: pET3d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VILIP-3 monomer: MGKQNSKLRPEVLQDLRENT EFTDHELQEWYKGFLKDCPT GHLTVDEFKKIYANFFPYGD ASKFAEHVFRTFDTNGDGTI DFREFIIALSVTSRGKLEQK LKWAFSMYDLDGNGYISRSE MLEIVQAIYKMVSSVMKMPE DESTPEKRTDKIFRQMDTNN DGKLSLEEFIRGAKSDPSIV RLLQCDPSSASQF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	599
15N chemical shifts	174
1H chemical shifts	1103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VILIP-3 monomer	1

Entities:

Entity 1, VILIP-3 monomer 193 residues - Formula weight is not available

1

MET

GLY

LYS

GLN

ASN

SER

LYS

LEU

ARG

PRO

2

GLU

VAL

LEU

GLN

ASP

LEU

ARG

GLU

ASN

THR

3

GLU

PHE

THR

ASP

HIS

GLU

LEU

GLN

GLU

TRP

4

TYR

LYS

GLY

PHE

LEU

LYS

ASP

CYS

PRO

THR

5

GLY

HIS

LEU

THR

VAL

ASP

GLU

PHE

LYS

6

ILE

TYR

ALA

ASN

PHE

PRO

TYR

GLY

ASP

7

ALA

SER

LYS

PHE

ALA

GLU

HIS

VAL

PHE

ARG

8

THR

PHE

ASP

THR

ASN

GLY

ASP

GLY

THR

ILE

9

ASP

PHE

ARG

GLU

PHE

ILE

ALA

LEU

SER

10

VAL

THR

SER

ARG

GLY

LYS

LEU

GLU

GLN

LYS

11

LEU

LYS

TRP

ALA

PHE

SER

MET

TYR

ASP

LEU

12

ASP

GLY

ASN

GLY

TYR

ILE

SER

ARG

SER

GLU

13

MET

LEU

GLU

ILE

VAL

GLN

ALA

ILE

TYR

LYS

14

MET

VAL

SER

VAL

MET

LYS

MET

PRO

GLU

15

ASP

GLU

SER

THR

PRO

GLU

LYS

ARG

THR

ASP

16

LYS

ILE

PHE

ARG

GLN

MET

ASP

THR

ASN

17

ASP

GLY

LYS

LEU

SER

LEU

GLU

PHE

ILE

18

ARG

GLY

ALA

LYS

SER

ASP

PRO

SER

ILE

VAL

19

ARG

LEU

GLN

CYS

ASP

PRO

SER

ALA

20

SER

GLN

PHE

Samples:

sample_1: Myristoylated VILIP-3, [U-100% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%

sample_2: Myristoylated VILIP-3, [U-100% 13C; U-100% 15N], 0.5-1 mM; H2O 90%; D2O 10%

sample_3: Myristoylated VILIP-3, [U-100% 13C; U-100% 15N], 0.5-1 mM; D2O 100%

sample_4: Myristoylated VILIP-3 0.5-1 mM; D2O 100%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 800 MHz

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