BMRB Entry 51382

Name: Backbone assignment of the Sec14 domain of the RhoGEF Kalirin
Published: 2023-07-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51382

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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 assignment of the Sec14 domain of the RhoGEF Kalirin

Deposition date:

2022-03-30

Original release date:

2023-07-04

Authors:

Pustovalova, Yulia; Li, Yunfeng; Hoch, Jeffrey; Hao, Bing

Citation:

Citation: Li, Yunfeng; Pustovalova, Yulia; Doukov, Tzanko; Hoch, Jeffrey; Mains, Richard; Eipper, Betty; Hao, Bing. "Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs" Nat. Commun. 14, 96-96 (2023).
PubMed: 36609407

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGGRGSFRNDGLKASDVLPI LKEKVAFVSGGRDKRGGPIL TFPARSNHDRIRQEDLRKLV TYLASVPSEDVCKRGFTVII DMRGSKWDLIKPLLKTLQEA FPAEIHVALIIKPDNFWQKQ KTNFGSSKFIFETSMVSVEG LTKLVDPSQLTEEFDGSLDY NHEEWIELRLSL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	454
15N chemical shifts	149
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Kalirin Sec14 domain	1

Entities:

Entity 1, Kalirin Sec14 domain 172 residues - Formula weight is not available

The first four residues are from an affinity tag (-4 to -1). The protein sequence starts with the fifth residue in a sequence that has numbers from G25 to L192. There are two mutations in the protein sequence: T66S and N82Y.

1

GLY

ARG

GLY

SER

PHE

ARG

ASN

ASP

2

GLY

LEU

LYS

ALA

SER

ASP

VAL

LEU

PRO

ILE

3

LEU

LYS

GLU

LYS

VAL

ALA

PHE

VAL

SER

GLY

4

GLY

ARG

ASP

LYS

ARG

GLY

PRO

ILE

LEU

5

THR

PHE

PRO

ALA

ARG

SER

ASN

HIS

ASP

ARG

6

ILE

ARG

GLN

GLU

ASP

LEU

ARG

LYS

LEU

VAL

7

THR

TYR

LEU

ALA

SER

VAL

PRO

SER

GLU

ASP

8

VAL

CYS

LYS

ARG

GLY

PHE

THR

VAL

ILE

9

ASP

MET

ARG

GLY

SER

LYS

TRP

ASP

LEU

ILE

10

LYS

PRO

LEU

LYS

THR

LEU

GLN

GLU

ALA

11

PHE

PRO

ALA

GLU

ILE

HIS

VAL

ALA

LEU

ILE

12

ILE

LYS

PRO

ASP

ASN

PHE

TRP

GLN

LYS

GLN

13

LYS

THR

ASN

PHE

GLY

SER

LYS

PHE

ILE

14

PHE

GLU

THR

SER

MET

VAL

SER

VAL

GLU

GLY

15

LEU

THR

LYS

LEU

VAL

ASP

PRO

SER

GLN

LEU

16

THR

GLU

PHE

ASP

GLY

SER

LEU

ASP

TYR

17

ASN

HIS

GLU

TRP

ILE

GLU

LEU

ARG

LEU

18

SER

LEU

Samples:

sample_1: Kalirin Sec14 domain, [U-100% 13C; U-100% 15N], 0.4 mM; Na/K phosphate buffer pH 7.2 20 mM; sodium chloride 120 mM; beta-mercaptoethanol 2 mM; EDTA 0.2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 140 mM; pH: 7.2; pressure: 1 atm; temperature: 298 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

VNMRj - collection

CARA - chemical shift assignment

CcpNMR - data analysis

NMRPipe - processing

NMR spectrometers:

Agilent VNMRS 800 MHz