BMRB Entry 30129

Name: Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR485
Published: 2016-09-23

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PDB ID: 5kph
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30129
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:

Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR485

Deposition date:

2016-07-04

Original release date:

2016-09-23

Authors:

Tang, Y.; Liu, G.; Montelione, G.; Northeast Structural Genomics Consortium (NESG), NESG

Citation:

Citation: Marcos, Enrique; Basanta, Benjamin; Chidyausiku, Tamuka; Tang, Yuefeng; Oberdorfer, Gustav; Liu, Gaohua; Swapna, G.; Guan, Rongjin; Silva, Daniel-Adriano; Dou, Jiayi; Pereira, Jose Henrique; Xiao, Rong; Sankaran, Banumathi; Zwart, Peter; Montelione, Gaetano; Baker, David. "Principles for designing proteins with cavities formed by curved beta sheets" Science 355, 201-206 (2017).
PubMed: 28082595

Assembly members:

Assembly members:
entity_1, polymer, 85 residues, 10097.393 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPSEEEEKRQVKQVAKEKLL EQSPNSKVQVRRVQKQGNTI RVELELRTNGKKENYTVEVE RQGNTWTVKRITRTVGSLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	337
15N chemical shifts	80
1H chemical shifts	573

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 85 residues - 10097.393 Da.

1

MET

PRO

SER

GLU

LYS

ARG

GLN

2

VAL

LYS

GLN

VAL

ALA

LYS

GLU

LYS

LEU

3

GLU

GLN

SER

PRO

ASN

SER

LYS

VAL

GLN

VAL

4

ARG

VAL

GLN

LYS

GLN

GLY

ASN

THR

ILE

5

ARG

VAL

GLU

LEU

GLU

LEU

ARG

THR

ASN

GLY

6

LYS

GLU

ASN

TYR

THR

VAL

GLU

VAL

GLU

7

ARG

GLN

GLY

ASN

THR

TRP

THR

VAL

LYS

ARG

8

ILE

THR

ARG

THR

VAL

GLY

SER

LEU

GLU

HIS

9

HIS

Samples:

sample_1: OR485, [U-99% 13C; U-99% 15N], 0.80 ± 0.2 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNcoCACB	sample_1	isotropic	sample_conditions_1
3D SIMUTANEOUS 13C-AROMATIC, 13-CALIPHATIC,15N EDITED 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-AROMATIC NOESY	sample_1	isotropic	sample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStructure, Huang, Tejero, Powers and Montelione - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

XEASY, Bartels et al. - peak picking

NMR spectrometers:

Bruker Avance 800 MHz

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