BMRB Entry 6284

Name: 1H, 13C, and 15N Chemical Shift Assignments for DnaG-C
Published: 2006-06-29

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PDB ID: 2haj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6284
MolProbity Validation Chart

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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:

1H, 13C, and 15N Chemical Shift Assignments for DnaG-C

Deposition date:

2004-08-05

Original release date:

2006-06-29

Authors:

Oakley, Aaron; Loscha, Karin; Schaeffer, Patrick; Liepinsh, Edvards; Pintacuda, Guido; Wilce, Matthew; Otting, Gottfried; Dixon, Nicholas

Citation:

Citation: Oakley, Aaron; Loscha, Karin; Schaeffer, Patrick; Liepinsh, Edvards; Pintacuda, Guido; Wilce, Matthew; Otting, Gottfried; Dixon, Nicholas. "Crystal and solution structures of the helicase-binding domain of Escherichia coli primase" J. Biol. Chem. 280, 11495-11504 (2005).
PubMed: 15649896

Assembly members:

Assembly members:
DnaG-C, polymer, 148 residues, 16690 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DnaG-C: AAESGVSRPVPQLKRTTMRI LIGLLVQNPELATLVPPLEN LDENKLPGLGLFRELVNTCL SQPGLTTGQLLEHYRGTNNA ATLEKLSMWDDIADKNIAEQ TFTDSLNHMFDSLLELRQEE LIARERTHGLSNEERLELWT LNQELAKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	757
15N chemical shifts	300
1H chemical shifts	1278

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaG-C	1

Entities:

Entity 1, DnaG-C 148 residues - 16690 Da.

1

ALA

GLU

SER

GLY

VAL

SER

ARG

PRO

VAL

2

PRO

GLN

LEU

LYS

ARG

THR

MET

ARG

ILE

3

LEU

ILE

GLY

LEU

VAL

GLN

ASN

PRO

GLU

4

LEU

ALA

THR

LEU

VAL

PRO

LEU

GLU

ASN

5

LEU

ASP

GLU

ASN

LYS

LEU

PRO

GLY

LEU

GLY

6

LEU

PHE

ARG

GLU

LEU

VAL

ASN

THR

CYS

LEU

7

SER

GLN

PRO

GLY

LEU

THR

GLY

GLN

LEU

8

LEU

GLU

HIS

TYR

ARG

GLY

THR

ASN

ALA

9

ALA

THR

LEU

GLU

LYS

LEU

SER

MET

TRP

ASP

10

ASP

ILE

ALA

ASP

LYS

ASN

ILE

ALA

GLU

GLN

11

THR

PHE

THR

ASP

SER

LEU

ASN

HIS

MET

PHE

12

ASP

SER

LEU

GLU

LEU

ARG

GLN

GLU

13

LEU

ILE

ALA

ARG

GLU

ARG

THR

HIS

GLY

LEU

14

SER

ASN

GLU

ARG

LEU

GLU

LEU

TRP

THR

15

LEU

ASN

GLN

GLU

LEU

ALA

LYS

Samples:

sample_1: DnaG-C, [U-90% 13C; U-15N], 0.6 mM; phosphate buffer 10 mM; DTT 1 mM; NaCl 100 mM; NaN3 0.1%

sample_2: DnaG-C, [U-90% 13C; U-15N], 0.4 mM; phosphate buffer 10 mM; DTT 1 mM; NaCl 100 mM; NaN3 0.1%

sample_conditions: pH: 6; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
not available	not available	not available	sample_conditions

Software:

xwinnmr v2.8 - peak assignments

PROSA v2.8 - spectrum processing

NMR spectrometers:

Bruker DMX 600 MHz

PDB	1T3W 2HAJ
DBJ	BAB37372 BAE77117 BAG78871 BAI27347 BAI32464
EMBL	CAA23531 CAP77540 CAQ33403 CAQ90500 CAR00028
GB	AAA24600 AAA89146 AAC76102 AAG58200 AAN44583
PIR	D85967
PRF	0902269A
REF	NP_289641 NP_311976 NP_417538 NP_708876 NP_755688
SP	P0ABS5 P0ABS6 P0ABS7 Q8FDG5
AlphaFold	P0ABS5 P0ABS6 P0ABS7 Q8FDG5