BMRB Entry 50310

Name: Backbone 1H, and 15N chemical shift Assignments for the ligand-free GlnBP
Published: 2022-05-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50310

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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:

Backbone 1H, and 15N chemical shift Assignments for the ligand-free GlnBP

Deposition date:

2020-06-08

Original release date:

2022-05-09

Authors:

Qin, Peiwu; Yu, Dongmei; Chen, Qun

Citation:

Citation: Chen, Qun; Li, Fang; Zuo, Xiaobing; Chen, Jin; Qin, Peiwu; Wang, Chuhui; Xu, Jin; Yang, Danyu; Xing, Baogang; Liu, Ying; Jia, Peng; Li, Linling; Yang, Chengming; Yu, Dongmei. "Reversible domain closure modulates GlnBP ligand binding affinity" PLoS One 17, e0263102-e0263102 (2022).
PubMed: 35446849

Assembly members:

Assembly members:
entity_1, polymer, 248 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKSVLKVSLAALTLAFAVSS HAADKKLVVATDTAFVPFEF KQGDKYVGFDVDLWAAIAKE LKLDYELKPMDFSGIIPALQ TKNVDLALAGITITDERKKA IDFSDGYYKSGLLVMVKANN NDVKSVKDLDGKVVAVKSGT GSVDYAKANIKTKDKRQFPN IDNAYMELGTNRADAVLHDT PNILYFIKTAGNGQFKAVGD SLEAQQYGIAFPKGSDEQRD KVNGALKTLRENGTYNEIYK KWFGTEPK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GlnBP	1

Entities:

Entity 1, GlnBP 248 residues - Formula weight is not available

1

MET

LYS

SER

VAL

LEU

LYS

VAL

SER

LEU

ALA

2

ALA

LEU

THR

LEU

ALA

PHE

ALA

VAL

SER

3

HIS

ALA

ASP

LYS

LEU

VAL

ALA

4

THR

ASP

THR

ALA

PHE

VAL

PRO

PHE

GLU

PHE

5

LYS

GLN

GLY

ASP

LYS

TYR

VAL

GLY

PHE

ASP

6

VAL

ASP

LEU

TRP

ALA

ILE

ALA

LYS

GLU

7

LEU

LYS

LEU

ASP

TYR

GLU

LEU

LYS

PRO

MET

8

ASP

PHE

SER

GLY

ILE

PRO

ALA

LEU

GLN

9

THR

LYS

ASN

VAL

ASP

LEU

ALA

LEU

ALA

GLY

10

ILE

THR

ILE

THR

ASP

GLU

ARG

LYS

ALA

11

ILE

ASP

PHE

SER

ASP

GLY

TYR

LYS

SER

12

GLY

LEU

VAL

MET

VAL

LYS

ALA

ASN

13

ASN

ASP

VAL

LYS

SER

VAL

LYS

ASP

LEU

ASP

14

GLY

LYS

VAL

ALA

VAL

LYS

SER

GLY

THR

15

GLY

SER

VAL

ASP

TYR

ALA

LYS

ALA

ASN

ILE

16

LYS

THR

LYS

ASP

LYS

ARG

GLN

PHE

PRO

ASN

17

ILE

ASP

ASN

ALA

TYR

MET

GLU

LEU

GLY

THR

18

ASN

ARG

ALA

ASP

ALA

VAL

LEU

HIS

ASP

THR

19

PRO

ASN

ILE

LEU

TYR

PHE

ILE

LYS

THR

ALA

20

GLY

ASN

GLY

GLN

PHE

LYS

ALA

VAL

GLY

ASP

21

SER

LEU

GLU

ALA

GLN

TYR

GLY

ILE

ALA

22

PHE

PRO

LYS

GLY

SER

ASP

GLU

GLN

ARG

ASP

23

LYS

VAL

ASN

GLY

ALA

LEU

LYS

THR

LEU

ARG

24

GLU

ASN

GLY

THR

TYR

ASN

GLU

ILE

TYR

LYS

25

LYS

TRP

PHE

GLY

THR

GLU

PRO

LYS

Samples:

sample_1: Glutamine binding protein (GlnBP), [U-100% 15N], 500 uM

sample_conditions_1: ionic strength: 0.003 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

MARS - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHZ MHz

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