BMRB Entry 27331

Name: 1H, 13C and 15N resonance assignment of SpyCatcher part of complex
Published: 2021-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27331

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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:

1H, 13C and 15N resonance assignment of SpyCatcher part of complex

Deposition date:

2017-12-05

Original release date:

2021-07-22

Authors:

Liu, Jing; Wang, Shenlin

Citation:

Citation: Zhang, Nan; Liu, Jing; Liu, Yajie; Wu, Wen-Hao; Fang, Jing; Da, Xiao-Di; Wang, Shenlin; Zhang, Wen-Bin. "NMR Spectroscopic Studies Reveal the Critical Role of the Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes" Biochemistry 59, 2226-2236 (2020).
PubMed: 32469203

Assembly members:

Assembly members:
SpyCatcher, polymer, 114 residues, Formula weight is not available
SpyTag, polymer, 16 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SpyCatcher: AMVDTLSGLSSEQGQSGDMT IEEDSATHIKFSKRDEDGKE LAGATMELRDSSGKTISTWI SDGQVKDFYLYPGKYTFVET AAPDGYEVATAITFTVNEQG QVTVNGKATKGDAH
SpyTag: AHIVMVDAYKPTKLDC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	312
15N chemical shifts	109
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SpyCatcher	1
2	SpyTag	2

Entities:

Entity 1, SpyCatcher 114 residues - Formula weight is not available

1

ALA

MET

VAL

ASP

THR

LEU

SER

GLY

LEU

SER

2

SER

GLU

GLN

GLY

GLN

SER

GLY

ASP

MET

THR

3

ILE

GLU

ASP

SER

ALA

THR

HIS

ILE

LYS

4

PHE

SER

LYS

ARG

ASP

GLU

ASP

GLY

LYS

GLU

5

LEU

ALA

GLY

ALA

THR

MET

GLU

LEU

ARG

ASP

6

SER

GLY

LYS

THR

ILE

SER

THR

TRP

ILE

7

SER

ASP

GLY

GLN

VAL

LYS

ASP

PHE

TYR

LEU

8

TYR

PRO

GLY

LYS

TYR

THR

PHE

VAL

GLU

THR

9

ALA

PRO

ASP

GLY

TYR

GLU

VAL

ALA

THR

10

ALA

ILE

THR

PHE

THR

VAL

ASN

GLU

GLN

GLY

11

GLN

VAL

THR

VAL

ASN

GLY

LYS

ALA

THR

LYS

12

GLY

ASP

ALA

HIS

Entity 2, SpyTag 16 residues - Formula weight is not available

1

ALA

HIS

ILE

VAL

MET

VAL

ASP

ALA

TYR

LYS

2

PRO

THR

LYS

LEU

ASP

CYS

Samples:

sample_1: SpyCatcher, [U-100% 13C; U-100% 15N], 0.3 mM; SpyTag 0.3 mM

sample_conditions_1: ionic strength: 16 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

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

Software:

TOPSIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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