BMRB Entry 16867

Name: VAMP7(1-180):CYTOPLASMIC DOMAIN OF VAMP7.
Published: 2010-04-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16867

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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:

VAMP7(1-180):CYTOPLASMIC DOMAIN OF VAMP7.

Deposition date:

2010-04-14

Original release date:

2010-04-29

Authors:

Vivona, Sandro; Liu, Corey; Strop, Pavel; Rossi, Valeria; Filippini, Francesco; Brunger, Axel

Citation:

Citation: Vivona, Sandro; Liu, Corey; Strop, Pavel; Rossi, Valeria; Filippini, Francesco; Brunger, Axel. "The longin SNARE VAMP7/TI-VAMP adopts a closed conformation." J. Biol. Chem. 285, 17965-17973 (2010).
PubMed: 20378544

Assembly members:

Assembly members:
VAMP7(1-180), polymer, 183 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET47b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VAMP7(1-180): GPGMAILFAVVARGTTILAK HAWCGGNFLEVTEQILAKIP SENNKLTYSHGNYLFHYICQ DRIVYLCITDDDFERSRAFN FLNEIKKRFQTTYGSRAQTA LPYAMNSEFSSVLAAQLKHH SENKGLDKVMETQAQVDELK GIMVRNIDLVAQRGERLELL IDKTENLVDSSVTFKTTSRN LAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VAMP7(1-180)	1

Entities:

Entity 1, VAMP7(1-180) 183 residues - Formula weight is not available

1

GLY

PRO

GLY

MET

ALA

ILE

LEU

PHE

ALA

VAL

2

VAL

ALA

ARG

GLY

THR

ILE

LEU

ALA

LYS

3

HIS

ALA

TRP

CYS

GLY

ASN

PHE

LEU

GLU

4

VAL

THR

GLU

GLN

ILE

LEU

ALA

LYS

ILE

PRO

5

SER

GLU

ASN

LYS

LEU

THR

TYR

SER

HIS

6

GLY

ASN

TYR

LEU

PHE

HIS

TYR

ILE

CYS

GLN

7

ASP

ARG

ILE

VAL

TYR

LEU

CYS

ILE

THR

ASP

8

ASP

PHE

GLU

ARG

SER

ARG

ALA

PHE

ASN

9

PHE

LEU

ASN

GLU

ILE

LYS

ARG

PHE

GLN

10

THR

TYR

GLY

SER

ARG

ALA

GLN

THR

ALA

11

LEU

PRO

TYR

ALA

MET

ASN

SER

GLU

PHE

SER

12

SER

VAL

LEU

ALA

GLN

LEU

LYS

HIS

13

SER

GLU

ASN

LYS

GLY

LEU

ASP

LYS

VAL

MET

14

GLU

THR

GLN

ALA

GLN

VAL

ASP

GLU

LEU

LYS

15

GLY

ILE

MET

VAL

ARG

ASN

ILE

ASP

LEU

VAL

16

ALA

GLN

ARG

GLY

GLU

ARG

LEU

GLU

LEU

17

ILE

ASP

LYS

THR

GLU

ASN

LEU

VAL

ASP

SER

18

SER

VAL

THR

PHE

LYS

THR

SER

ARG

ASN

19

LEU

ALA

ARG

Samples:

sample_1: VAMP7(1-180), [U-100% 15N], 300 uM; D2O 10%; potassium phosphate 20 mM; sodium chloride 100 mM; Dithiothreitol 1 mM; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian INOVA 800 MHz

BMRB	16866
PDB	2DMW 2VX8 4AFI 4B93
DBJ	BAB22386 BAB27667 BAC40712 BAD96514 BAE38126
EMBL	CAA63133 CAA65509 CAB94231 CAB96816 CAC16891
GB	AAH03764 AAH56141 AAI18342 ABK42476 ACV04838
REF	NP_001069770 NP_001124684 NP_001159676 NP_001172112 NP_001230522
SP	P51809 P70280 Q17QI5 Q5RF94
TPG	DAA13239
AlphaFold	P51809 P70280 Q17QI5 Q5RF94