BMRB Entry 17915

Name: PFBD: High-throughput Strategy of Backbone fold Determination for small well-folded proteins in less than a day
Published: 2011-10-07

Click here to enlarge.

PDB ID: 2lj3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17915
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

PFBD: High-throughput Strategy of Backbone fold Determination for small well-folded proteins in less than a day

Deposition date:

2011-09-04

Original release date:

2011-10-07

Authors:

Kumar, Dinesh; Hosur, Ramakrishna V

Citation:

Citation: Kumar, Dinesh; Borkar, Aditi; Hosur, Ramakrishna. "Facile backbone (1H, 15N, 13Ca, and 13C') assignment of 13C/15N-labeled proteins using orthogonal projection planes of HNN and HN(C)N experiments and its automation." Magn. Reson. Chem. 50, 357-363 (2012).
PubMed: 22508472

Assembly members:

Assembly members:
SH3, polymer, 62 residues, 7229.313 Da.
LL5, non-polymer, 334.436 Da.

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus Gallus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3: MDETGKELVLALYDYQEKSP REVTMKKGDILTLLNSTNKD WWKVEVNDRQGFVPAAYVKK LD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	114
15N chemical shifts	59
1H chemical shifts	59

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3	1
2	LL5_1	2
3	LL5_2	2
4	LL5_3	2
5	LL5_4	2
6	LL5_5	2

Entities:

Entity 1, SH3 62 residues - 7229.313 Da.

1

MET

ASP

GLU

THR

GLY

LYS

GLU

LEU

VAL

LEU

2

ALA

LEU

TYR

ASP

TYR

GLN

GLU

LYS

SER

PRO

3

ARG

GLU

VAL

THR

MET

LYS

GLY

ASP

ILE

4

LEU

THR

LEU

ASN

SER

THR

ASN

LYS

ASP

5

TRP

LYS

VAL

GLU

VAL

ASN

ASP

ARG

GLN

6

GLY

PHE

VAL

PRO

ALA

TYR

VAL

LYS

7

LEU

ASP

Entity 2, LL5_1 - C16 H22 N4 O2 S - 334.436 Da.

1

LL5

Samples:

sample_1: SH3, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 50 ± 0.05 mM; NaCl 150 ± 0.05 mM; H2O 90 ± 0.05 %; D2O" 10 ± 0.05 %

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D hNcnH	sample_1	isotropic	sample_conditions_1
2D hncNH-G	sample_1	isotropic	sample_conditions_1
2D hncNH-A	sample_1	isotropic	sample_conditions_1
2D hncNH-ST	sample_1	isotropic	sample_conditions_1
2D cbcacoNH	sample_1	isotropic	sample_conditions_1
2D HnCO	sample_1	isotropic	sample_conditions_1
2D hnCOcanH	sample_1	isotropic	sample_conditions_1
2D-HncoCA	sample_1	isotropic	sample_conditions_1
2D hncoCAnH	sample_1	isotropic	sample_conditions_1
2D-(HN)NH-G, A, ST	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0 Beta, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	15013 15144
PDB	1AEY 1BK2 1HD3 1M8M 1NEG 1PWT 1QKW 1QKX 1SHG 1U06 2CDT 2F2V 2F2W 2F2X 2JM8 2JM9 2JMA 2JMC 2LJ3 2NUZ 3M0P 3M0Q 3M0R 3M0S 3M0T 3M0U 3THK 4F16 4F17
DBJ	BAD52438 BAD93097 BAG57892 BAG62120 BAG72795
EMBL	CAA29435 CAA32663 CAA62350 CAB53710 CAF90367
GB	AAA51702 AAA51790 AAA52468 AAB41498 AAB60364
REF	NP_001036003 NP_001090674 NP_001091958 NP_001107628 NP_001123910
SP	P07751 P16086 P16546 Q13813
TPG	DAA24188
AlphaFold	P07751 P16086 P16546 Q13813