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
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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

Samples:

sample_1: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 10%; H2O 90%

sample_2: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 292 K

Experiments:

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

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure solution

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment

CcpNmr v2.4.0, Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED. - chemical shift assignment, peak picking

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 950 MHz

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