BMRB Entry 25700

Name: Solution Structure of R. palustris CsgH
Published: 2016-05-23

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PDB ID: 2n59
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25700
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 Structure of R. palustris CsgH

Deposition date:

2015-07-13

Original release date:

2016-05-23

Authors:

Hawthorne, William; Taylor, Jonathan; Escalera-Maurer, Andres; Lambert, Sebastian; Koch, Marion; Scull, Nicola; Sefer, Lea; Xu, Yinqi; Matthews, Steve

Citation:

Citation: Taylor, Jonathan; Hawthorne, William; Fletcher, Catherine; Lo, Joanne; Koch, Marion; Darvill, Nicholas; Scull, Nicola; Escalera-Maurer, Andres; Sefer, Lea; Wenman, Rosemary; Lambert, Sebastian; Xu, Yinqi; Turner, Benjamin; Kazarian, Sergei; Bubeck, Doryen; de Simone, Alfonso; Knowles, Tuomas; Matthews, Steve. "Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones" Sci. Rep. 6, 24656-24656 (2016).
PubMed: 27098162

Assembly members:

Assembly members:
CsgH, polymer, 106 residues, 10492.875 Da.

Natural source:

Natural source: Common Name: a-proteobacteria Taxonomy ID: 1076 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodopseudomonas palustris

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CsgH: MVQCEVEAAVSGGHVTLQGV ITAVRDGAGSYKLAVDKAGA AGTSRIKQAGAFTAIAEQRV TVGNVVLDYSSANRYAARLD VSFGSVTIQCNLDPETVKLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	399
15N chemical shifts	99
1H chemical shifts	632

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 106 residues - 10492.875 Da.

Native N-terminal Sequence: MAVDQVPPV has been replaced with a single N-terminal Methionine.

1

MET

VAL

GLN

CYS

GLU

VAL

GLU

ALA

VAL

2

SER

GLY

HIS

VAL

THR

LEU

GLN

GLY

VAL

3

ILE

THR

ALA

VAL

ARG

ASP

GLY

ALA

GLY

SER

4

TYR

LYS

LEU

ALA

VAL

ASP

LYS

ALA

GLY

ALA

5

ALA

GLY

THR

SER

ARG

ILE

LYS

GLN

ALA

GLY

6

ALA

PHE

THR

ALA

ILE

ALA

GLU

GLN

ARG

VAL

7

THR

VAL

GLY

ASN

VAL

LEU

ASP

TYR

SER

8

SER

ALA

ASN

ARG

TYR

ALA

ARG

LEU

ASP

9

VAL

SER

PHE

GLY

SER

VAL

THR

ILE

GLN

CYS

10

ASN

LEU

ASP

PRO

GLU

THR

VAL

LYS

LEU

GLU

11

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 25700

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: