BMRB Entry 27099

Name: Chemical shift assignment of gp17.1 by proton-detected solid-state NMR
Published: 2017-06-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27099

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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:

Chemical shift assignment of gp17.1 by proton-detected solid-state NMR

Deposition date:

2017-05-08

Original release date:

2017-06-29

Authors:

Zinke, Maximilian; Fricke, Pascal; Lange, Sascha; Lange, Adam

Citation:

Citation: Zinke, Maximilian; Fricke, Pascal; Samson, Camille; Hwang, Songhwan; Wall, Joseph; Lange, Sascha; Zinn-Justin, Sophie; Lange, Adam. "Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR" Angew. Chem. Int. Ed. Engl. 56, 9497-9501 (2017).
PubMed: 28644511

Assembly members:

Assembly members:
gp17-1, polymer, 185 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus phage SPP1 Taxonomy ID: 10724 Superkingdom: Viruses Kingdom: not available Genus/species: Lambdavirus SPP1

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM13

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gp17-1: MGMPETPIMGQDVKYLFQSI DAATGSAPLFPAYQTDGSVS GERELFDEQTKNGRILGPGS VADSGEVTYYGKRGDAGQKA IEDAYQNGKQIKFWRVDTVK NENDKYDAQFGFAYIESREY SDGVEGAVEISISLQVIGEL KNGEIDTLPEEIVNVSKGGY DFQQPGQTTGEAPGTVPAPH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	460
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gp17.1	1

Entities:

Entity 1, gp17.1 185 residues - Formula weight is not available

1

MET

GLY

MET

PRO

GLU

THR

PRO

ILE

MET

GLY

2

GLN

ASP

VAL

LYS

TYR

LEU

PHE

GLN

SER

ILE

3

ASP

ALA

THR

GLY

SER

ALA

PRO

LEU

PHE

4

PRO

ALA

TYR

GLN

THR

ASP

GLY

SER

VAL

SER

5

GLY

GLU

ARG

GLU

LEU

PHE

ASP

GLU

GLN

THR

6

LYS

ASN

GLY

ARG

ILE

LEU

GLY

PRO

GLY

SER

7

VAL

ALA

ASP

SER

GLY

GLU

VAL

THR

TYR

8

GLY

LYS

ARG

GLY

ASP

ALA

GLY

GLN

LYS

ALA

9

ILE

GLU

ASP

ALA

TYR

GLN

ASN

GLY

LYS

GLN

10

ILE

LYS

PHE

TRP

ARG

VAL

ASP

THR

VAL

LYS

11

ASN

GLU

ASN

ASP

LYS

TYR

ASP

ALA

GLN

PHE

12

GLY

PHE

ALA

TYR

ILE

GLU

SER

ARG

GLU

TYR

13

SER

ASP

GLY

VAL

GLU

GLY

ALA

VAL

GLU

ILE

14

SER

ILE

SER

LEU

GLN

VAL

ILE

GLY

GLU

LEU

15

LYS

ASN

GLY

GLU

ILE

ASP

THR

LEU

PRO

GLU

16

GLU

ILE

VAL

ASN

VAL

SER

LYS

GLY

TYR

17

ASP

PHE

GLN

PRO

GLY

GLN

THR

GLY

18

GLU

ALA

PRO

GLY

THR

VAL

PRO

ALA

PRO

HIS

19

HIS

Samples:

sample_1: gp17.1, [U-13C; U-15N; U-2H]; 100% back-exchange, 13 mg

sample_conditions_1: ionic strength: 0.5 M; pH: 7.4; pressure: 1 atm; temperature: 291 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D (H)NH	sample_1	isotropic	sample_conditions_1
3D (H)CANH	sample_1	isotropic	sample_conditions_1
3D (H)CNONH	sample_1	isotropic	sample_conditions_1
3D (H)N(CACO)NH	sample_1	isotropic	sample_conditions_1
4D (H)COCANH	sample_1	isotropic	sample_conditions_1
4D (H)CBCANH	sample_1	isotropic	sample_conditions_1
4D (H)CACONH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

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