BMRB Entry 15136

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Endosulfine alpha
Published: 2008-01-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15136

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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, 13C, and 15N Chemical Shift Assignments for Endosulfine alpha

Deposition date:

2007-02-15

Original release date:

2008-01-09

Authors:

Boettcher, John; Hartman, Kevin; Ladror, Daniel; Qi, Zhi; Woods, Wendy; Rienstra, Chad; George, Julia

Citation:

Citation: Boettcher, John; Hartman, Kevin; Ladror, Daniel; Qi, Zhi; Woods, Wendy; George, Julia; Rienstra, Chad. "(1)H, (13)C, and (15)N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states" Biomol. NMR Assignments 1, 167-169 (2007).
PubMed: 19636856

Assembly members:

Assembly members:
ENSA, polymer, 121 residues, 13.389 Da.

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: ????

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ENSA: MSQKQEEENPAEETGEEKQD TQEKEGILPERAEEAKLKAK YPSLGQKPGGSDFLMKRLQK GQKYFDSGDYNMAKAKMKNK QLPSAGPDKNLVTGDHIPTP QDLPQRKSSLVTSKLAGGQV E

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	304
15N chemical shifts	96
1H chemical shifts	96

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ENSA, chain 1	1
2	ENSA, chain 2	1

Entities:

Entity 1, ENSA, chain 1 121 residues - 13.389 Da.

1

MET

SER

GLN

LYS

GLN

GLU

ASN

PRO

2

ALA

GLU

THR

GLY

GLU

LYS

GLN

ASP

3

THR

GLN

GLU

LYS

GLU

GLY

ILE

LEU

PRO

GLU

4

ARG

ALA

GLU

ALA

LYS

LEU

LYS

ALA

LYS

5

TYR

PRO

SER

LEU

GLY

GLN

LYS

PRO

GLY

6

SER

ASP

PHE

LEU

MET

LYS

ARG

LEU

GLN

LYS

7

GLY

GLN

LYS

TYR

PHE

ASP

SER

GLY

ASP

TYR

8

ASN

MET

ALA

LYS

ALA

LYS

MET

LYS

ASN

LYS

9

GLN

LEU

PRO

SER

ALA

GLY

PRO

ASP

LYS

ASN

10

LEU

VAL

THR

GLY

ASP

HIS

ILE

PRO

THR

PRO

11

GLN

ASP

LEU

PRO

GLN

ARG

LYS

SER

LEU

12

VAL

THR

SER

LYS

LEU

ALA

GLY

GLN

VAL

13

GLU

Samples:

sample_1: sodium phosphate 50 mM; sodium azide 0.02%; ENSA, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HNN	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15135
DBJ	BAB24433 BAB27552 BAB31584 BAE29049 BAE36298
EMBL	CAA06798 CAA06799 CAA06800 CAA06801 CAA65196
GB	AAD32454 AAF80340 AAF80341 AAH00436 AAH04461
REF	NP_001021383 NP_001029146 NP_001300934 NP_004427 NP_062507
SP	O43768 P60840 P60841 P68210 P68211
TPG	DAA31642
AlphaFold	O43768 P60840 P60841 P68210 P68211