BMRB Entry 25994

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for designed protein E_1r26
Published: 2016-10-13

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PDB ID: 2nbs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25994
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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 designed protein E_1r26 PubMed: 27522946

Deposition date: 2016-03-12 Original release date: 2016-10-13

Authors: Zhou, Xiaoqun

Citation: Zhou, Xiaoqun; Xiong, Peng; Wang, Meng; Ma, Rongsheng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Proteins of well-defined structures can be designed without backbone readjustment by a statistical model." J. Struct. Biol. 196, 350-357 (2016).

Assembly members:
E_1r26, polymer, 122 residues, Formula weight is not available

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

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

Entity Sequences (FASTA):
E_1r26: MARPSNVKPSPHVIKSLEEL REATASNRISVIVFTHPDSK RSKEIKEKLKKLAEEFPDVD IYLVDTSTNPEAREWYNITS VPTFVIEKGGEPLGEVKGPD IDKLRETLDELLARLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	106
1H chemical shifts	591

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 122 residues - Formula weight is not available

1

MET

ALA

ARG

PRO

SER

ASN

VAL

LYS

PRO

SER

2

PRO

HIS

VAL

ILE

LYS

SER

LEU

GLU

LEU

3

ARG

GLU

ALA

THR

ALA

SER

ASN

ARG

ILE

SER

4

VAL

ILE

VAL

PHE

THR

HIS

PRO

ASP

SER

LYS

5

ARG

SER

LYS

GLU

ILE

LYS

GLU

LYS

LEU

LYS

6

LYS

LEU

ALA

GLU

PHE

PRO

ASP

VAL

ASP

7

ILE

TYR

LEU

VAL

ASP

THR

SER

THR

ASN

PRO

8

GLU

ALA

ARG

GLU

TRP

TYR

ASN

ILE

THR

SER

9

VAL

PRO

THR

PHE

VAL

ILE

GLU

LYS

GLY

10

GLU

PRO

LEU

GLY

GLU

VAL

LYS

GLY

PRO

ASP

11

ILE

ASP

LYS

LEU

ARG

GLU

THR

LEU

ASP

GLU

12

LEU

ALA

ARG

LEU

GLU

HIS

13

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], mM; sodium phosphate 0.02 mM; EDTA 0.01 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker DMX 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts