BMRB Entry 34929

Name: NMR solution structure of the Thermus thermophilus PilF-GSPIIA domain
Published: 2025-05-23

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PDB ID: 9g1w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34929
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NMR-STAR v3 text file.
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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 solution structure of the Thermus thermophilus PilF-GSPIIA domain

Deposition date:

2024-07-10

Original release date:

2025-05-23

Authors:

Neissner, K.; Woehnert, J.; Hacker, C.

Citation:

Citation: Neissner, Konstantin; Frohnapfel, Carolin; Keller, Heiko; Duchardt-Ferner, Elke; Schneider, Vanessa; Kamjou, Zeinab; Averhoff, Beate; Wohnert, Jens. "NMR Solution Structure of the N-Terminal GSPII Domain from the Thermus Thermophilus Traffic ATPase PilF and Reconstruction of its c-di-GMP Binding Capability" Chembiochem 26, e202400959-e202400959 (2025).
PubMed: 39960869

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, 16924.604 Da.

Natural source:

Natural source: Common Name: Thermus thermophilus HB27 Taxonomy ID: 262724 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSVLTIGDKRLGAALLDAGL LTDEELQRALERHREVGGSL AEVLVDMGLLSERRIAQTIE DRFGIPLVELHRVEIPPKVK ALLPAEKAKELKAIPFALDE EAGVVRVAFLNPLDTLSLEE VEDLTGLVVEPYQTTKSAFL YALAKHYPELGLPV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	698
15N chemical shifts	149
1H chemical shifts	1137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 154 residues - 16924.604 Da.

1

MET

SER

VAL

LEU

THR

ILE

GLY

ASP

LYS

ARG

2

LEU

GLY

ALA

LEU

ASP

ALA

GLY

LEU

3

LEU

THR

ASP

GLU

LEU

GLN

ARG

ALA

LEU

4

GLU

ARG

HIS

ARG

GLU

VAL

GLY

SER

LEU

5

ALA

GLU

VAL

LEU

VAL

ASP

MET

GLY

LEU

6

SER

GLU

ARG

ILE

ALA

GLN

THR

ILE

GLU

7

ASP

ARG

PHE

GLY

ILE

PRO

LEU

VAL

GLU

LEU

8

HIS

ARG

VAL

GLU

ILE

PRO

LYS

VAL

LYS

9

ALA

LEU

PRO

ALA

GLU

LYS

ALA

LYS

GLU

10

LEU

LYS

ALA

ILE

PRO

PHE

ALA

LEU

ASP

GLU

11

GLU

ALA

GLY

VAL

ARG

VAL

ALA

PHE

LEU

12

ASN

PRO

LEU

ASP

THR

LEU

SER

LEU

GLU

13

VAL

GLU

ASP

LEU

THR

GLY

LEU

VAL

GLU

14

PRO

TYR

GLN

THR

LYS

SER

ALA

PHE

LEU

15

TYR

ALA

LEU

ALA

LYS

HIS

TYR

PRO

GLU

LEU

16

GLY

LEU

PRO

VAL

Samples:

sample_1: PilF1-154, [U-13C; U-15N], 438 uM; NaCl 200 mM

sample_2: PilF1-154, [U-100% 15N], 500 uM; NaCl 200 mM

sample_3: PilF1-154, [U-100% 15N], 550 uM; NaCl 200 mM

sample_4: PilF1-154, [U-15N]-Leu/Val-13C, 608 uM; NaCl 200 mM

sample_5: PilF1-154, [U-13C; U-15N], 335 uM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 5.8; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_5	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CcpNmr Analysis, CCPN - peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE II 600 MHz
Bruker AVANCE III 950 MHz
Bruker AVANCE NEO 600 MHz
Bruker AVANCE III HD 800 MHz

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