BMRB Entry 15132

Name: The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection.
Published: 2007-03-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15132

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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:

The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection.

Deposition date:

2007-02-14

Original release date:

2007-03-29

Authors:

Watters, Alexander; Deka, Priti; Corrent, Colin; Callender, David; Varani, Gabriele; Sosnick, Tobin; Baker, David

Citation:

Citation: Watters, Alexander; Deka, Pritilekha; Corrent, Colin; Callender, David; Varani, Gabriele; Sosnick, Tobin; Baker, David. "The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection." Cell 128, 613-624 (2007).
PubMed: 17289578

Assembly members:

Assembly members:
Top7, polymer, 106 residues, Formula weight is not available

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: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Top7: MGDIQVQVNIDDNGKNQDLT YTVTTESELQKVLNELKDYI EEQGAKRVRISITARTEKEA EKFAAILIKVFAELGYNDIN VTWDGDTVTVEGQLEGGSLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	271
15N chemical shifts	102
1H chemical shifts	370

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	monomer	1

Entities:

Entity 1, monomer 106 residues - Formula weight is not available

Residues 1-2 and 95-106 are part of the expression vector and not ordered in the folded strucutre.

1

MET

GLY

ASP

ILE

GLN

VAL

GLN

VAL

ASN

ILE

2

ASP

ASN

GLY

LYS

ASN

GLN

ASP

LEU

THR

3

TYR

THR

VAL

THR

GLU

SER

GLU

LEU

GLN

4

LYS

VAL

LEU

ASN

GLU

LEU

LYS

ASP

TYR

ILE

5

GLU

GLN

GLY

ALA

LYS

ARG

VAL

ARG

ILE

6

SER

ILE

THR

ALA

ARG

THR

GLU

LYS

GLU

ALA

7

GLU

LYS

PHE

ALA

ILE

LEU

ILE

LYS

VAL

8

PHE

ALA

GLU

LEU

GLY

TYR

ASN

ASP

ILE

ASN

9

VAL

THR

TRP

ASP

GLY

ASP

THR

VAL

THR

VAL

10

GLU

GLY

GLN

LEU

GLU

GLY

SER

LEU

GLU

11

HIS

Samples:

sample_1: Top7, [U-99% 15N], 1 mM; H2O 95%; D2O 5%; sodium phosphate 50 mM

sample_2: Top7, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; 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_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

SPARKY v3.112, Goddard - chemical shift assignment, data analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

Bruker DRX 500 MHz

BMRB	7101
PDB	2GJH