BMRB Entry 17028

Name: The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein
Published: 2010-09-24

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PDB ID: 2l04
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17028
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein

Deposition date:

2010-06-30

Original release date:

2010-09-24

Authors:

Pell, Lisa; Gasmi-Seabrook, Genevieve; Donaldson, Logan; Howell, P Lynne; Davidson, Alan; Maxwell, Karen

Citation:

Citation: Pell, Lisa; Gasmi-Seabrook, Genevieve; Morais, Marc; Neudecker, Philipp; Kanelis, Voula; Bona, Diane; Donaldson, Logan; Edwards, Aled; Howell, P. Lynne; Davidson, Alan; Maxwell, Karen. "The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage Tail Tube Protein." J. Mol. Biol. 403, 468-479 (2010).
PubMed: 20826161

Assembly members:

Assembly members:
gpV-C, polymer, 91 residues, 8882.101 Da.

Natural source:

Natural source: Common Name: Bacteriophage 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: pET32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gpV-C: GAMAAATGMTVTPASTSVVK GQSTTLTVAFQPEGVTDKSF RAVSADKTKATVSVSGMTIT VNGVAAGKVNIPVVSGNGEF AAVAEITVTAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	91
1H chemical shifts	566

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gpV-C	1

Entities:

Entity 1, gpV-C 91 residues - 8882.101 Da.

1

GLY

ALA

MET

ALA

THR

GLY

MET

THR

2

VAL

THR

PRO

ALA

SER

THR

SER

VAL

LYS

3

GLY

GLN

SER

THR

LEU

THR

VAL

ALA

PHE

4

GLN

PRO

GLU

GLY

VAL

THR

ASP

LYS

SER

PHE

5

ARG

ALA

VAL

SER

ALA

ASP

LYS

THR

LYS

ALA

6

THR

VAL

SER

VAL

SER

GLY

MET

THR

ILE

THR

7

VAL

ASN

GLY

VAL

ALA

GLY

LYS

VAL

ASN

8

ILE

PRO

VAL

SER

GLY

ASN

GLY

GLU

PHE

9

ALA

VAL

ALA

GLU

ILE

THR

VAL

THR

ALA

10

SER

Samples:

sample_1: gpV-C, 15N, 13C, 0.71 – 2.5 mM; sodium phosphate 50 mM; sodium chloride 200 mM; H20 90%; D20 10%

sample_2: sodium phosphate 50 mM; sodium chloride 200 mM; D20 100%

sample_conditions_1: ionic strength: 0.2 M; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(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 H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 500 MHz

PDB	2L04
DBJ	BAG77580 BAI29415
EMBL	CAP75673 CAQ31259 CAR01926 CAR02528 CAR16659
GB	AAA96545 ACF32394 ACR63704 ACT29881 ACT42628
REF	NP_040592 WP_000056728 WP_000306529 WP_000419939 WP_001297108
SP	P03733
AlphaFold	P03733