BMRB Entry 52475

Name: Solution NMR backbone assignment of SorcinFL
Published: 2024-09-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52475

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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 NMR backbone assignment of SorcinFL

Deposition date:

2024-05-21

Original release date:

2024-09-09

Authors:

Carillo, Kathleen Joyce; Ye, Qiushi; Delaeter, Nicolas; He, Yanan; Chen, Yihong; Orban, John; Liu, Yanxin

Citation:

Citation: Carillo, Kathleen Joyce; Ye, Qiushi; Delaeter, Nicolas; He, Yanan; Chen, Yihong; Orban, John; Liu, Yanxin. "Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin" Biomol. NMR Assign. 18, 253-256 (2024).
PubMed: 39215797

Assembly members:

Assembly members:
entity_1, polymer, 203 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: pET151D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GIDPFTAYPGHPGAGGGYYP GGYGGAPGGPAFPGQTQDPL YGYFAAVAGQDGQIDADELQ RCLTQSGIAGGYKPFNLETC RLMVSMLDRDMSGTMGFNEF KELWAVLNGWRQHFISFDTD RSGTVDPQELQKALTTMGFR LSPQAVNSIAKRYSTNGKIT FDDYIACCVKLRALTDSFRR RDTAQQGVVNFPYDDFIQCV MSV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	532
15N chemical shifts	185
1H chemical shifts	185

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SorcinFL	1

Entities:

Entity 1, SorcinFL 203 residues - Formula weight is not available

1

GLY

ILE

ASP

PRO

PHE

THR

ALA

TYR

PRO

GLY

2

HIS

PRO

GLY

ALA

GLY

TYR

PRO

3

GLY

TYR

GLY

ALA

PRO

GLY

PRO

4

ALA

PHE

PRO

GLY

GLN

THR

GLN

ASP

PRO

LEU

5

TYR

GLY

TYR

PHE

ALA

VAL

ALA

GLY

GLN

6

ASP

GLY

GLN

ILE

ASP

ALA

ASP

GLU

LEU

GLN

7

ARG

CYS

LEU

THR

GLN

SER

GLY

ILE

ALA

GLY

8

GLY

TYR

LYS

PRO

PHE

ASN

LEU

GLU

THR

CYS

9

ARG

LEU

MET

VAL

SER

MET

LEU

ASP

ARG

ASP

10

MET

SER

GLY

THR

MET

GLY

PHE

ASN

GLU

PHE

11

LYS

GLU

LEU

TRP

ALA

VAL

LEU

ASN

GLY

TRP

12

ARG

GLN

HIS

PHE

ILE

SER

PHE

ASP

THR

ASP

13

ARG

SER

GLY

THR

VAL

ASP

PRO

GLN

GLU

LEU

14

GLN

LYS

ALA

LEU

THR

MET

GLY

PHE

ARG

15

LEU

SER

PRO

GLN

ALA

VAL

ASN

SER

ILE

ALA

16

LYS

ARG

TYR

SER

THR

ASN

GLY

LYS

ILE

THR

17

PHE

ASP

TYR

ILE

ALA

CYS

VAL

LYS

18

LEU

ARG

ALA

LEU

THR

ASP

SER

PHE

ARG

19

ARG

ASP

THR

ALA

GLN

GLY

VAL

ASN

20

PHE

PRO

TYR

ASP

PHE

ILE

GLN

CYS

VAL

21

MET

SER

VAL

Samples:

sample_1: SorcinFL, [U-13C; U-15N; U-2H], 0.44 mM; D2O, [U-100% 2H], 10%; H2O 90%; potassium chloride 150 mM; HEPES 40 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

CARA v1.9.1.7 - chemical shift assignment

TOPSPIN v3.6 - collection

NMRFAM-SPARKY v3.115 - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz