BMRB Entry 16717

Name: Backbone chemical shifts of NI3C DARPin
Published: 2010-08-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16717

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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 chemical shifts of NI3C DARPin

Deposition date:

2010-02-10

Original release date:

2010-08-12

Authors:

Wetzel, Svava; Ewald, Christina; Jurt, Simon; Zerbe, Oliver; Plueckthun, Andreas

Citation:

Citation: Wetzel, Svava; Ewald, Christina; Settanni, Giovanni; Jurt, Simon; Pluckthun, Andreas; Zerbe, Oliver. "Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR." J. Mol. Biol. 402, 241-258 (2010).
PubMed: 20654623

Assembly members:

Assembly members:
NI3C, polymer, 166 residues, 17896.91 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSW_NI3C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NI3C: MRGSHHHHHHGSDLGKKLLE AARAGQDDEVRILMANGADV NAKDKDGYTPLHLAAREGHL EIVEVLLKAGADVNAKDKDG YTPLHLAAREGHLEIVEVLL KAGADVNAKDKDGYTPLHLA AREGHLEIVEVLLKAGADVN AQDKFGKTAFDISIDNGNED LAEILQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	346
15N chemical shifts	149
1H chemical shifts	149

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NI3C monomer	1

Entities:

Entity 1, NI3C monomer 166 residues - 17896.91 Da.

1

MET

ARG

GLY

SER

HIS

2

GLY

SER

ASP

LEU

GLY

LYS

LEU

GLU

3

ALA

ARG

ALA

GLY

GLN

ASP

GLU

VAL

4

ARG

ILE

LEU

MET

ALA

ASN

GLY

ALA

ASP

VAL

5

ASN

ALA

LYS

ASP

LYS

ASP

GLY

TYR

THR

PRO

6

LEU

HIS

LEU

ALA

ARG

GLU

GLY

HIS

LEU

7

GLU

ILE

VAL

GLU

VAL

LEU

LYS

ALA

GLY

8

ALA

ASP

VAL

ASN

ALA

LYS

ASP

LYS

ASP

GLY

9

TYR

THR

PRO

LEU

HIS

LEU

ALA

ARG

GLU

10

GLY

HIS

LEU

GLU

ILE

VAL

GLU

VAL

LEU

11

LYS

ALA

GLY

ALA

ASP

VAL

ASN

ALA

LYS

ASP

12

LYS

ASP

GLY

TYR

THR

PRO

LEU

HIS

LEU

ALA

13

ALA

ARG

GLU

GLY

HIS

LEU

GLU

ILE

VAL

GLU

14

VAL

LEU

LYS

ALA

GLY

ALA

ASP

VAL

ASN

15

ALA

GLN

ASP

LYS

PHE

GLY

LYS

THR

ALA

PHE

16

ASP

ILE

SER

ILE

ASP

ASN

GLY

ASN

GLU

ASP

17

LEU

ALA

GLU

ILE

LEU

GLN

Samples:

sample_1: NI3C, [U-99% 15N], 700 uM; potassium phosphate 50 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_2: NI3C, [U-100% 13C; U-100% 15N; U-80% 2H], 700 uM; potassium phosphate 50 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HN(COCA)NH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.3, R. Keller - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz