BMRB Entry 19446

Name: Single-stranded DNA binding protein from E. coli (SSB)
Published: 2013-09-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19446

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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:

Single-stranded DNA binding protein from E. coli (SSB)

Deposition date:

2013-08-21

Original release date:

2013-09-19

Authors:

Shishmarev, Dmitry; Wang, Yao; Yagi, Hiromasa; Dixon, Nicholas; Su, Xun-Cheng; Yagi, Hiromasa

Citation:

Citation: Su, Xun-Cheng; Wang, Yao; Yagi, Hiromasa; Shishmarev, Dmitry; Mason, Claire; Smith, Paul; Vandevenne, Marylene; Dixon, Nicholas; Otting, Gottfried. "Bound or Free: Interaction of the C-Terminal Domain of Escherichia coli Single-Stranded DNA-Binding Protein (SSB) with the Tetrameric Core of SSB." Biochemistry 53, 1925-1934 (2014).
PubMed: 24606314

Assembly members:

Assembly members:
SSB, polymer, 177 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SSB: ASRGVNKVILVGNLGQDPEV RYMPNGGAVANITLATSESW RDKATGEMKEQTEWHRVVLF GKLAEVASEYLRKGSQVYIE GQLRTRKWTDQSGQDRYTTE VVVNVGGTMQMLGGRQGGGA PAGGNIGGGQPQGGWGQPQQ PQGGNQFSGGAQSRPQQSAP AAPSNEPPMDFDDDIPF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	701
15N chemical shifts	178
1H chemical shifts	948

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Single-stranded DNA binding protein	1

Entities:

Entity 1, Single-stranded DNA binding protein 177 residues - Formula weight is not available

1

ALA

SER

ARG

GLY

VAL

ASN

LYS

VAL

ILE

LEU

2

VAL

GLY

ASN

LEU

GLY

GLN

ASP

PRO

GLU

VAL

3

ARG

TYR

MET

PRO

ASN

GLY

ALA

VAL

ALA

4

ASN

ILE

THR

LEU

ALA

THR

SER

GLU

SER

TRP

5

ARG

ASP

LYS

ALA

THR

GLY

GLU

MET

LYS

GLU

6

GLN

THR

GLU

TRP

HIS

ARG

VAL

LEU

PHE

7

GLY

LYS

LEU

ALA

GLU

VAL

ALA

SER

GLU

TYR

8

LEU

ARG

LYS

GLY

SER

GLN

VAL

TYR

ILE

GLU

9

GLY

GLN

LEU

ARG

THR

ARG

LYS

TRP

THR

ASP

10

GLN

SER

GLY

GLN

ASP

ARG

TYR

THR

GLU

11

VAL

ASN

VAL

GLY

THR

MET

GLN

12

MET

LEU

GLY

ARG

GLN

GLY

ALA

13

PRO

ALA

GLY

ASN

ILE

GLY

GLN

14

PRO

GLN

GLY

TRP

GLY

GLN

PRO

GLN

15

PRO

GLN

GLY

ASN

GLN

PHE

SER

GLY

16

ALA

GLN

SER

ARG

PRO

GLN

SER

ALA

PRO

17

ALA

PRO

SER

ASN

GLU

PRO

MET

ASP

18

PHE

ASP

ILE

PRO

PHE

Samples:

sample_1: SSB, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 3.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

Analysis v2.1.5, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

PDB	1EQQ 1EYG 1KAW 1QVC 1SRU 4MZ9
DBJ	BAB38464 BAE78061 BAG79877 BAI28321 BAI33498
EMBL	CAP78525 CAQ34408 CAQ91583 CAR01039 CAR05708
GB	AAA24649 AAC43153 AAC77029 AAG59257 AAN45567
PIR	E86099
REF	NP_313068 NP_418483 NP_709860 WP_000157064 WP_000168295
SP	P0AGE0 P0AGE1 P0AGE2 P0AGE3
AlphaFold	P0AGE0 P0AGE1 P0AGE2 P0AGE3