BMRB Entry 6127

Name: Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III
Published: 2005-02-15

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PDB ID: 1se7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6127
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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 the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III

Deposition date:

2004-03-03

Original release date:

2005-02-15

Authors:

DeRose, E.; Kirby, T.; Mueller, G.; Chikova, A.; Schaaper, R.; London, R.

Citation:

Citation: DeRose, E.; Kirby, T.; Mueller, G.; Chikova, A.; Schaaper, R.; London, R.. "Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III" Structure 12, 2221-2231 (2004).
PubMed: 15576035

Assembly members:

Assembly members:
p1 encoded protein, polymer, 83 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli bacteriophage P1 Taxonomy ID: not available Superkingdom: Bacteriophage Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET30HOT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p1 encoded protein: MYDWNIAAKSQEERDKVNVD LAASGVAYKERLNIPVIAEQ VAREQPENLRTYFMERLRHY RQLSLQLPKGSDPAYQKDDA VKK

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	341
1H chemical shifts	466
15N chemical shifts	87

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HOT protein	1

Entities:

Entity 1, HOT protein 83 residues - Formula weight is not available

1

MET

TYR

ASP

TRP

ASN

ILE

ALA

LYS

SER

2

GLN

GLU

ARG

ASP

LYS

VAL

ASN

VAL

ASP

3

LEU

ALA

SER

GLY

VAL

ALA

TYR

LYS

GLU

4

ARG

LEU

ASN

ILE

PRO

VAL

ILE

ALA

GLU

GLN

5

VAL

ALA

ARG

GLU

GLN

PRO

GLU

ASN

LEU

ARG

6

THR

TYR

PHE

MET

GLU

ARG

LEU

ARG

HIS

TYR

7

ARG

GLN

LEU

SER

LEU

GLN

LEU

PRO

LYS

GLY

8

SER

ASP

PRO

ALA

TYR

GLN

LYS

ASP

ALA

9

VAL

LYS

Samples:

sample_1: p1 encoded protein, [U-13C; U-15N], 1.3 mM; Tris 5 mM; NaCl 100 mM; NaN3 5 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7; temperature: 298 K; ionic strength: 100 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	sample_cond_1
3D 15N-separated NOESY	sample_1	not available	sample_cond_1

Software:

NMRPipe v2.1 Rev 2002.044.17.08 - processing

NMRView v5.0.4 - data analysis

ARIA v1.2 - structure solution

CNS v1.1 - structure solution, refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	1SE7 2IDO
GB	AAQ14071 AAQ14179 EHN41319 EHU11765 EII43590
REF	WP_001286531 WP_001667237 WP_024224114 YP_006567