BMRB Entry 17948

Name: NMR structure of Hsp12 in the presence of DPC
Published: 2011-10-28

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PDB ID: 2ljl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17948
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of Hsp12 in the presence of DPC

Deposition date:

2011-09-20

Original release date:

2011-10-28

Authors:

Singarapu, Kiran; Markley, John

Citation:

Citation: Singarapu, Kiran; Tonelli, Marco; Chow, Darius; Frederick, Ronnie; Westler, William; Markley, John. "Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical." J. Biol. Chem. 286, 43447-43453 (2011).
PubMed: 21998307

Assembly members:

Assembly members:
Hsp12, polymer, 109 residues, 11712.830 Da.

Natural source:

Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pvp68k

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hsp12: MSDAGRKGFGEKASEALKPD SQKSYAEQGKEYITDKADKV AGKVQPEDNKGVFQGVHDSA EKGKDNAEGQGESLADQARD YMGAAKSKLNDAVEYVSGRV HGEEDPTKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	223
15N chemical shifts	102
1H chemical shifts	537

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hsp12	1

Entities:

Entity 1, Hsp12 109 residues - 11712.830 Da.

1

MET

SER

ASP

ALA

GLY

ARG

LYS

GLY

PHE

GLY

2

GLU

LYS

ALA

SER

GLU

ALA

LEU

LYS

PRO

ASP

3

SER

GLN

LYS

SER

TYR

ALA

GLU

GLN

GLY

LYS

4

GLU

TYR

ILE

THR

ASP

LYS

ALA

ASP

LYS

VAL

5

ALA

GLY

LYS

VAL

GLN

PRO

GLU

ASP

ASN

LYS

6

GLY

VAL

PHE

GLN

GLY

VAL

HIS

ASP

SER

ALA

7

GLU

LYS

GLY

LYS

ASP

ASN

ALA

GLU

GLY

GLN

8

GLY

GLU

SER

LEU

ALA

ASP

GLN

ALA

ARG

ASP

9

TYR

MET

GLY

ALA

LYS

SER

LYS

LEU

ASN

10

ASP

ALA

VAL

GLU

TYR

VAL

SER

GLY

ARG

VAL

11

HIS

GLY

GLU

ASP

PRO

THR

LYS

Samples:

sample_1: Hsp12, [U-13C; U-15N], 0.7 mM; DPC 200 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

VNMR, Varian - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	17482 17483 18523
PDB	2L9Q 2LJL 4AXP
DBJ	BAA09224 BAA14033 GAA23069
EMBL	CAA39306 CAA86349 CAY79436
GB	AAA34647 AAL06077 AAS56790 AHY75775 AJP38487
REF	NP_116640
SP	P22943
TPG	DAA12425
AlphaFold	P22943