BMRB Entry 6535

Name: 'Backbone 1H and 15N Chemical Shift Assignments for T antigen origin binding domain in the presence of RPA32C'
Published: 2005-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6535

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 'Backbone 1H and 15N Chemical Shift Assignments for T antigen origin binding domain in the presence of RPA32C' PubMed: 15793585

Deposition date: 2005-03-04 Original release date: 2005-09-28

Authors: Arunkumar, Alphonse; Chazin, Walter

Citation: Arunkumar, Alphonse; Klimovich, Vitaly; Jiang, Xiaohua; Ott, Robert; Mizoue, Laura; Fanning, Ellen; Chazin, Walter. "Insights into hRPA32 C-terminal domain-mediated assembly of the simian virus 40 replisome." Nat. Struct. Mol. Biol. 12, 332-339 (2005).

Assembly members:
Tag-OBD, polymer, 131 residues, Formula weight is not available
RPA32 C-terminal domain, polymer, 103 residues, Formula weight is not available

Natural source: Common Name: Simian viurs40 Taxonomy ID: not available Superkingdom: Viruses Kingdom: not available Genus/species: Simian viurs40 Simian virus40

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):
Tag-OBD: GSKVEDPKDFPSELLSFLSH AVFSNRTLACFAIYTTKEKA ALLYKKIMEKYSVTFISRHN SYNHNILFFLTPHRHRVSAI NNYAQKLCTFSFLICKGVNK EYLMYSALTRDPFSVIEESL PGGLKEHDFNP
RPA32 C-terminal domain: ANGLTVAQNQVLNLIKACPR PEGLNFQDLKNQLKHMSVSS IKQAVDFLSNEGHIYSTVDD DHFKSTDAE

Data sets:

assigned_chemical_shifts
- chem_shift_list_1
- chem_shift_list_2

Data type	Count
15N chemical shifts	165
1H chemical shifts	165

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tag-OBD	1
2	RPA32C	2

Entities:

Entity 1, Tag-OBD 131 residues - Formula weight is not available

1

GLY

SER

LYS

VAL

GLU

ASP

PRO

LYS

ASP

PHE

2

PRO

SER

GLU

LEU

SER

PHE

LEU

SER

HIS

3

ALA

VAL

PHE

SER

ASN

ARG

THR

LEU

ALA

CYS

4

PHE

ALA

ILE

TYR

THR

LYS

GLU

LYS

ALA

5

ALA

LEU

TYR

LYS

ILE

MET

GLU

LYS

6

TYR

SER

VAL

THR

PHE

ILE

SER

ARG

HIS

ASN

7

SER

TYR

ASN

HIS

ASN

ILE

LEU

PHE

LEU

8

THR

PRO

HIS

ARG

HIS

ARG

VAL

SER

ALA

ILE

9

ASN

TYR

ALA

GLN

LYS

LEU

CYS

THR

PHE

10

SER

PHE

LEU

ILE

CYS

LYS

GLY

VAL

ASN

LYS

11

GLU

TYR

LEU

MET

TYR

SER

ALA

LEU

THR

ARG

12

ASP

PRO

PHE

SER

VAL

ILE

GLU

SER

LEU

13

PRO

GLY

LEU

LYS

GLU

HIS

ASP

PHE

ASN

14

PRO

Entity 2, RPA32C 103 residues - Formula weight is not available

1

ALA

ASN

GLY

LEU

THR

VAL

ALA

GLN

ASN

GLN

2

VAL

LEU

ASN

LEU

ILE

LYS

ALA

CYS

PRO

ARG

3

PRO

GLU

GLY

LEU

ASN

PHE

GLN

ASP

LEU

LYS

4

ASN

GLN

LEU

LYS

HIS

MET

SER

VAL

SER

5

ILE

LYS

GLN

ALA

VAL

ASP

PHE

LEU

SER

ASN

6

GLU

GLY

HIS

ILE

TYR

SER

THR

VAL

ASP

7

ASP

HIS

PHE

LYS

SER

THR

ASP

ALA

GLU

Samples:

sample_1: Tag-OBD, [U-15N], 0.2 mM; RPA32 C-terminal domain, unlabeled, 0.6 mM; Tris, 2H, 20 mM; MgCl2 5 mM; DTT 2 mM

sample_2: Tag-OBD, unlabeled, 0.2 mM; RPA32 C-terminal domain, [U-15N], 0.6 mM; Tris, 2H, 20 mM; MgCl2 5 mM; DTT 2 mM

conditions_1: pH: 7.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N_HSQC	not available	isotropic	conditions_1

Software:

FELIX, Accelrys Inc -

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	17060 4460
PDB	1DPU 1Z1D 2PI2 2Z6K 4MQV 4OU0
DBJ	BAG35795 BAG59456 BAG60901 BAG62374 BAI47325
EMBL	CAG29344 CAH90667
GB	AAA36560 AAH01630 AAH12157 AAH21257 AAX84514
REF	NP_001125362 NP_001231871 NP_001247563 NP_001273005 NP_001284487
SP	P15927 Q5RC43

Biological Magnetic Resonance Data Bank