BMRB Entry 16113

Name: H, 13C, and 15N Chemical Shift Assignments of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213
Published: 2009-03-02

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16113

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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:

H, 13C, and 15N Chemical Shift Assignments of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213

Deposition date:

2009-01-09

Original release date:

2009-03-02

Authors:

Liu, Gaohua; SINGARAPU, Kiran; Parish, David; Eletsky, Alexandre; Xu, Duanxiang; HO, Chi Kent; Fang, Yinyi; CUNNINGHAM, Kellie; MA, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Liu, Gaohua; Singarapu, Kiran; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213" .

Assembly members:

Assembly members:
yppe, polymer, 131 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
yppe: MLSQTLLEMTEQMIEVAEKG ADRYQEGKNSNHSYDFFETI KPAVEENDELAARWAEGALE LIKVRRPKYVHKEQIEAVKD NFLELVLQSYVHHIHKKRFK DITESVLYTLHAVKDEIARE DSRLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	388
15N chemical shifts	101
1H chemical shifts	814

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	yppe	1

Entities:

Entity 1, yppe 131 residues - Formula weight is not available

1

MET

LEU

SER

GLN

THR

LEU

GLU

MET

THR

2

GLU

GLN

MET

ILE

GLU

VAL

ALA

GLU

LYS

GLY

3

ALA

ASP

ARG

TYR

GLN

GLU

GLY

LYS

ASN

SER

4

ASN

HIS

SER

TYR

ASP

PHE

GLU

THR

ILE

5

LYS

PRO

ALA

VAL

GLU

ASN

ASP

GLU

LEU

6

ALA

ARG

TRP

ALA

GLU

GLY

ALA

LEU

GLU

7

LEU

ILE

LYS

VAL

ARG

PRO

LYS

TYR

VAL

8

HIS

LYS

GLU

GLN

ILE

GLU

ALA

VAL

LYS

ASP

9

ASN

PHE

LEU

GLU

LEU

VAL

LEU

GLN

SER

TYR

10

VAL

HIS

ILE

HIS

LYS

ARG

PHE

LYS

11

ASP

ILE

THR

GLU

SER

VAL

LEU

TYR

THR

LEU

12

HIS

ALA

VAL

LYS

ASP

GLU

ILE

ALA

ARG

GLU

13

ASP

SER

ARG

LEU

GLU

HIS

14

HIS

Name	Sample	Sample state	Sample conditions
SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
GFT (4,3)D HNNCABCA	sample_1	isotropic	sample_conditions_1
GFT (4,3)D CABCA(CO)NHN	sample_1	isotropic	sample_conditions_1
GFT (4,3) HCCH	sample_1	isotropic	sample_conditions_1
HNCACB	sample_1	isotropic	sample_conditions_1
HABCONH	sample_1	isotropic	sample_conditions_1

PDB	2HFI 2IM8
DBJ	BAI85724 BAM52709 BAM58284 GAK79397
EMBL	CAB14144 CCU58728 CEI57439 CEJ77864 CJT23466
GB	AAB38463 ADV92956 AEP91245 AFQ58175 AGA23534
REF	NP_390109 WP_003246080 WP_015483369 WP_015714151 WP_017696991
SP	P50833
AlphaFold	P50833

BMRB Entry 16113

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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