BMRB Entry 18437

Name: Solution structure of gpFI C-terminal domain
Published: 2012-07-23

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PDB ID: 2lsm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18437
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of gpFI C-terminal domain

Deposition date:

2012-05-02

Original release date:

2012-07-23

Authors:

Popovic, Ana; Wu, Bin; Edwards, Aled; Davidson, Alan; Maxwell, Karen

Citation:

Citation: Popovic, Ana; Wu, Bin; Arrowsmith, Cheryl; Edwards, Aled; Davidson, Alan; Maxwell, Karen. "Structural and biochemical characterization of phage FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity." J. Biol. Chem. 287, 32085-32095 (2012).
PubMed: 22801427

Assembly members:

Assembly members:
polypeptide, polymer, 61 residues, 6495.518 Da.

Natural source:

Natural source: Common Name: Enterobacteria phage lambda Taxonomy ID: 10710 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage lambda

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
polypeptide: PDTVILDTSELVTVVALVKL HTDALHATRDEPVAFVLPGT AFRVSAGVAAEMTERGLARM Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	60
1H chemical shifts	419

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gpFI C-terminal domain	1

Entities:

Entity 1, gpFI C-terminal domain 61 residues - 6495.518 Da.

1

PRO

ASP

THR

VAL

ILE

LEU

ASP

THR

SER

GLU

2

LEU

VAL

THR

VAL

ALA

LEU

VAL

LYS

LEU

3

HIS

THR

ASP

ALA

LEU

HIS

ALA

THR

ARG

ASP

4

GLU

PRO

VAL

ALA

PHE

VAL

LEU

PRO

GLY

THR

5

ALA

PHE

ARG

VAL

SER

ALA

GLY

VAL

ALA

6

GLU

MET

THR

GLU

ARG

GLY

LEU

ALA

ARG

MET

7

GLN

Samples:

sample_1: gpFI, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 25 mM; sodium chloride 250 mM; H2O 90 mM; D2O 10 mM

sample_2: gpFI, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; potassium chloride 250 mM; D2O 100%

sample_conditions_1: ionic strength: 250 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

software_2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA_2.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 500 MHz

PDB	2LSM
DBJ	BAB35059 BAB35596 BAI29411
EMBL	CAQ31255 CBG34515 CCP95075 CDK54019 CDK83941
GB	AAA96541 AAG55986 ACF32390 ACI36443 ACI39211
REF	NP_040588 NP_309663 NP_310200 WP_000158905 WP_000158906
SP	P03709
AlphaFold	P03709