BMRB Entry 4718

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4718

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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:

Assignments of amide 1H, amide 15N, and Ca, CO, Cb 13C shifts for the replication terminator protein

Deposition date:

2000-04-12

Original release date:

2001-05-01

Authors:

Wilce, Jackie; Vivian, Julian; Hastings, Adam; Otting, Gottfried; Folmer, Rutger; Duggin, I.; Wake, R.; Wilce, Matthew

Citation:

Citation: Wilce, Jackie; Vivian, Julian; Hastings, Adam; Otting, Gottfried; Folmer, Rutger; Duggin, I.; Wake, R.; Wilce, Matthew. "Structure of the RTP-DNA Complex and the Mechanism of Polar Replication Fork Arrest" Nat. Struct. Biol. 8, 206-210 (2001).
PubMed: 11224562

Assembly members:

Assembly members:
replication termination protein, polymer, 122 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
replication termination protein: MKEEKRSSTGFLVKQRAFLK LYMITMTEQERLYGLKLLEV LRSEFKEIGFKPNHTEVYRS LHELLDDGILKQIKVKKEGA KLQEVVLYQFKDYEAAKLYK KQLKVELDRSKKLIEKALSD NF

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	131
13C chemical shifts	333
15N chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RTP subunit 1	1
2	RTP subunit 2	1

Entities:

Entity 1, RTP subunit 1 122 residues - Formula weight is not available

1

MET

LYS

GLU

LYS

ARG

SER

THR

GLY

2

PHE

LEU

VAL

LYS

GLN

ARG

ALA

PHE

LEU

LYS

3

LEU

TYR

MET

ILE

THR

MET

THR

GLU

GLN

GLU

4

ARG

LEU

TYR

GLY

LEU

LYS

LEU

GLU

VAL

5

LEU

ARG

SER

GLU

PHE

LYS

GLU

ILE

GLY

PHE

6

LYS

PRO

ASN

HIS

THR

GLU

VAL

TYR

ARG

SER

7

LEU

HIS

GLU

LEU

ASP

GLY

ILE

LEU

8

LYS

GLN

ILE

LYS

VAL

LYS

GLU

GLY

ALA

9

LYS

LEU

GLN

GLU

VAL

LEU

TYR

GLN

PHE

10

LYS

ASP

TYR

GLU

ALA

LYS

LEU

TYR

LYS

11

LYS

GLN

LEU

LYS

VAL

GLU

LEU

ASP

ARG

SER

12

LYS

LEU

ILE

GLU

LYS

ALA

LEU

SER

ASP

13

ASN

PHE

Samples:

sample_1: replication termination protein, [U-100% 13C; U-100% 15N; U-70% 2H], 0.25 mM

condition_1: pH: 6.0; temperature: 298 K; ionic strength: 0.11 M

Experiments:

Name	Sample	Sample state	Sample conditions
TROSY-HNCA	not available	not available	not available
TROSY-HNCO	not available	not available	not available
TROSY-HNCACB	not available	not available	not available
TROSY-HN(CO)CACB	not available	not available	not available
TROSY-HN(CA)CO	not available	not available	not available
3D NOESY-15N-HSQC	not available	not available	not available

Software:

XEASY -

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DMX 600 MHz

PDB	1BM9 1F4K 1J0R 2DPD 2DPU 2DQR 2EFW
DBJ	BAM52503 BAM58079 BAO93415 GAK78159
EMBL	CAA29534 CAB13742 CCU58469 CEI57043 CEJ77468
GB	AAA22721 AAC38659 AAC38660 AAC38662 ADM38012
REF	NP_389731 WP_003220337 WP_010334473 WP_024715459 WP_041849904
SP	E0TY12 P0CI76 P68733
AlphaFold	E0TY12 P0CI76 P68733