BMRB Entry 30574

Name: NMR ensemble of computationally designed protein XAA
Published: 2020-04-17

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PDB ID: 6o0i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30574
MolProbity Validation Chart

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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:

NMR ensemble of computationally designed protein XAA

Deposition date:

2019-02-16

Original release date:

2020-04-17

Authors:

Wei, K.; Moschidi, D.; Nerli, S.; Sgourakis, N.; Baker, D.

Citation:

Citation: Wei, K.; Moschidi, D.; Bick, M.; Nerli, S.; McShan, A.; Carter, L.; Huang, P.; Fletcher, D.; Sgourakis, N.; Boyken, S.; Baker, D.. "Computational design of closely related proteins that adopt two well-defined but structurally divergent folds" Proc. Natl. Acad. Sci. U. S. A. 117, 7208-7215 (2020).
PubMed: 32188784

Assembly members:

Assembly members:
entity_1, polymer, 98 residues, 11094.648 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMGTEDLKYSLERLREIL ERLEENPSEKQIVEAIRAIV ENNAQIVEAIRAIVENNAQI VENNRAIIEALEAIGGGTKI LEEMKKQLKDLKRSLERG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	864
15N chemical shifts	261
1H chemical shifts	558

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1
3	entity_1, 3	1

Entities:

Entity 1, entity_1, 1 98 residues - 11094.648 Da.

1

GLY

SER

HIS

MET

GLY

THR

GLU

ASP

LEU

LYS

2

TYR

SER

LEU

GLU

ARG

LEU

ARG

GLU

ILE

LEU

3

GLU

ARG

LEU

GLU

ASN

PRO

SER

GLU

LYS

4

GLN

ILE

VAL

GLU

ALA

ILE

ARG

ALA

ILE

VAL

5

GLU

ASN

ALA

GLN

ILE

VAL

GLU

ALA

ILE

6

ARG

ALA

ILE

VAL

GLU

ASN

ALA

GLN

ILE

7

VAL

GLU

ASN

ARG

ALA

ILE

GLU

ALA

8

LEU

GLU

ALA

ILE

GLY

THR

LYS

ILE

9

LEU

GLU

MET

LYS

GLN

LEU

LYS

ASP

10

LEU

LYS

ARG

SER

LEU

GLU

ARG

GLY

Samples:

sample_1: XAA_MAI(LV)proS, U-[15N, 12C, 2H] 13Ce Met 13Cb Ala 13Cd1 Ile 13Cd2 Leu 13Cg2 Val, 440 uM; NaCl 100 mM

sample_2: XAA_ILVstar, U-[15N, 13C, 2H], 500 uM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 310.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CM-CMHM NOESY	sample_1	isotropic	sample_conditions_1
3D CM-NHN NOESY	sample_1	isotropic	sample_conditions_1
3D HNHa-CMHM NOESY	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 HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Software:

Rosetta, Rohl CA, Strauss CE, Misura KM, Baker D - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks