BMRB Entry 16345

Name: Solution structure and backbone dynamics of the permutant P54-55
Published: 2009-12-16

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PDB ID: 2kjw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16345
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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:

Solution structure and backbone dynamics of the permutant P54-55

Deposition date:

2009-06-10

Original release date:

2009-12-16

Authors:

Ohman, Anders; Oliveberg, Mikael; Oman, Tommy

Citation:

Citation: Haglund, Ellinor; Lind, Jesper; Oman, Tommy; Ohman, Anders; Maler, Lena; Oliveberg, Mikael. "The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway." Proc. Natl. Acad. Sci. U.S.A. 106, 21619-21624 (2009).
PubMed: 19966220

Assembly members:

Assembly members:
permutant P54-55, polymer, 96 residues, 11258.984 Da.

Natural source:

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
permutant P54-55: MDPQGYFLWYQVEMPEDRVN DLARELRIRDNVRRVMVVAS TTPGRYEVNIVLNPNLDQSQ LALEKEIIQRALENYGARVE KVEELGLRRLAYPIAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	104
1H chemical shifts	659

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	permutant P54-55	1

Entities:

Entity 1, permutant P54-55 96 residues - 11258.984 Da.

1

MET

ASP

PRO

GLN

GLY

TYR

PHE

LEU

TRP

TYR

2

GLN

VAL

GLU

MET

PRO

GLU

ASP

ARG

VAL

ASN

3

ASP

LEU

ALA

ARG

GLU

LEU

ARG

ILE

ARG

ASP

4

ASN

VAL

ARG

VAL

MET

VAL

ALA

SER

5

THR

PRO

GLY

ARG

TYR

GLU

VAL

ASN

ILE

6

VAL

LEU

ASN

PRO

ASN

LEU

ASP

GLN

SER

GLN

7

LEU

ALA

LEU

GLU

LYS

GLU

ILE

GLN

ARG

8

ALA

LEU

GLU

ASN

TYR

GLY

ALA

ARG

VAL

GLU

9

LYS

VAL

GLU

LEU

GLY

LEU

ARG

LEU

10

ALA

TYR

PRO

ILE

ALA

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

BMRB Entry 16345

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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