BMRB Entry 4239

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4239

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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:

Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA binding protein of the bacteriophage f29

Deposition date:

1998-10-08

Original release date:

2000-03-17

Authors:

Pineda-Lucena, A.; Vuister, G.; Hilbers, C.

Citation:

Citation: Pineda-Lucena, A.; Vuister, G.; Hilbers, C.. "Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA binding protein of the bacteriophage phi 29." J. Biomol. NMR 13, 303-304 (1999).

Assembly members:

Assembly members:
f29-SSB, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source: Common Name: bacteriophage f29 Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGM26

Entity Sequences (FASTA):

Entity Sequences (FASTA):
f29-SSB: MENTNIVKATFDTETLEGQI KIFNAQTGGGQSFKNLPDGT IIEANAIAQYKQVSDTYGDA KEETVTTIFAADGSLYSAIS KTVAEAASDLIDLVTRHKLE TFKVKVVQGTSSKGNVWFSL QLSL

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_f29-SSB

Data type	Count
13C chemical shifts	220
15N chemical shifts	88
1H chemical shifts	462

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	f29-SSB	1

Entities:

Entity 1, f29-SSB 124 residues - Formula weight is not available

1

MET

GLU

ASN

THR

ASN

ILE

VAL

LYS

ALA

THR

2

PHE

ASP

THR

GLU

THR

LEU

GLU

GLY

GLN

ILE

3

LYS

ILE

PHE

ASN

ALA

GLN

THR

GLY

4

GLN

SER

PHE

LYS

ASN

LEU

PRO

ASP

GLY

THR

5

ILE

GLU

ALA

ASN

ALA

ILE

ALA

GLN

TYR

6

LYS

GLN

VAL

SER

ASP

THR

TYR

GLY

ASP

ALA

7

LYS

GLU

THR

VAL

THR

ILE

PHE

ALA

8

ALA

ASP

GLY

SER

LEU

TYR

SER

ALA

ILE

SER

9

LYS

THR

VAL

ALA

GLU

ALA

SER

ASP

LEU

10

ILE

ASP

LEU

VAL

THR

ARG

HIS

LYS

LEU

GLU

11

THR

PHE

LYS

VAL

LYS

VAL

GLN

GLY

THR

12

SER

LYS

GLY

ASN

VAL

TRP

PHE

SER

LEU

13

GLN

LEU

SER

LEU

Samples:

sample_one: f29-SSB 0.85 mM; sodium phosphate 10 mM; D2O 100%

sample_two: f29-SSB, [U-15N], 0.85 mM; sodium phosphate 10 mM; CHAPS 5 mM; D2O 10%; H2O 90%

sample_three: f29-SSB, [U-15N], reverse labeled for Thr/Leu, 0.85 mM; sodium phosphate 10 mM; CHAPS 5 mM; D2O 10%; H2O 90%

sample_four: f29-SSB, [U-15N; U-13C], reverse labeled for Thr/Leu, 0.85 mM; sodium phosphate 10 mM; CHAPS 5 mM; D2O 10%; H2O 90%

experimental_conditions_f29-SSB: pH: 6.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

Varian Unity Inova 500 MHz
Varian Unity Inova 750 MHz

EMBL	CAA24483
GB	AAA88475 ACE96026
PRF	1112171H
REF	YP_002004532
SP	P06953 Q38504
AlphaFold	P06953 Q38504