BMRB Entry 17880

Name: 1H, 13C, and 15N Chemical Shift Assignments for a yeast protein
Published: 2012-04-23

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PDB ID: 2li6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17880
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for a yeast protein

Deposition date:

2011-08-23

Original release date:

2012-04-23

Authors:

Wang, Tao

Citation:

Citation: Wang, Tao; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution structure of SWI1 AT-rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA." Proteins 80, 1911-1917 (2012).
PubMed: 22488857

Assembly members:

Assembly members:
yeast_protein, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's 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: pET 22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
yeast_protein: MQSLNPALQEKISTELNNKQ YELFMKSLIENCKKRNMPLQ SIPEIGNRKINLFYLYMLVQ KFGGADQVTRTQQWSMVAQR LQISDYQQLESIYFRILLPY ERHMISQEGIKETQAKRLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	303
15N chemical shifts	110
1H chemical shifts	485

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	yeast_protein	1

Entities:

Entity 1, yeast_protein 125 residues - Formula weight is not available

1

MET

GLN

SER

LEU

ASN

PRO

ALA

LEU

GLN

GLU

2

LYS

ILE

SER

THR

GLU

LEU

ASN

LYS

GLN

3

TYR

GLU

LEU

PHE

MET

LYS

SER

LEU

ILE

GLU

4

ASN

CYS

LYS

ARG

ASN

MET

PRO

LEU

GLN

5

SER

ILE

PRO

GLU

ILE

GLY

ASN

ARG

LYS

ILE

6

ASN

LEU

PHE

TYR

LEU

TYR

MET

LEU

VAL

GLN

7

LYS

PHE

GLY

ALA

ASP

GLN

VAL

THR

ARG

8

THR

GLN

TRP

SER

MET

VAL

ALA

GLN

ARG

9

LEU

GLN

ILE

SER

ASP

TYR

GLN

LEU

GLU

10

SER

ILE

TYR

PHE

ARG

ILE

LEU

PRO

TYR

11

GLU

ARG

HIS

MET

ILE

SER

GLN

GLU

GLY

ILE

12

LYS

GLU

THR

GLN

ALA

LYS

ARG

LEU

GLU

HIS

13

HIS

Samples:

sample_1: yeast protein, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; sodium phosphate 2 mM; EDTA 1.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DMX 500 MHz

PDB	1KKX 1KN5 2LI6
DBJ	GAA26956
EMBL	CAA31013 CAY86943
GB	AAB68089 AHY78155 AJP42124 AJV91214 AJV91652
REF	NP_015309
SP	P09547
TPG	DAA11412
AlphaFold	P09547