BMRB Entry 16262

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16262

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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:

NMR solution structure of the N-terminal domain of the DNA polymerase alpha p68 subunit

Deposition date:

2009-04-22

Original release date:

2012-08-06

Authors:

Huang, Hao; Weiner, Brian; Zhang, Haijiang; Fuller, Brian; Gao, Yue; Wile, Brian; Chazin, Walter; Fanning, Ellen

Citation:

Citation: Huang, Hao; Weiner, Brian; Zhang, Haijiang; Fuller, Brian; Gao, Yue; Wile, Brian; Chazin, Walter; Fanning, Ellen. "The N-terminal domain of the p68 subunit tethers DNA polymerase alpha-primase to a replicative helicase for primosome function" .

Assembly members:

Assembly members:
p68N, polymer, 101 residues, 8700.943 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBG100

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p68N: MGSSHHHHHHGSSLEVLFQG PGSMSASAQQLAEELQIFGL DCEEALIEKLVELCVQYGQN EEGMVGELIAFCTSTHKVGL TSEILNSFEHEFLSKRLSKA R

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	235
15N chemical shifts	83
1H chemical shifts	550

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p68N	1

Entities:

Entity 1, p68N 101 residues - 8700.943 Da.

1

MET

GLY

SER

HIS

2

GLY

SER

LEU

GLU

VAL

LEU

PHE

GLN

GLY

3

PRO

GLY

SER

MET

SER

ALA

SER

ALA

GLN

4

LEU

ALA

GLU

LEU

GLN

ILE

PHE

GLY

LEU

5

ASP

CYS

GLU

ALA

LEU

ILE

GLU

LYS

LEU

6

VAL

GLU

LEU

CYS

VAL

GLN

TYR

GLY

GLN

ASN

7

GLU

GLY

MET

VAL

GLY

GLU

LEU

ILE

ALA

8

PHE

CYS

THR

SER

THR

HIS

LYS

VAL

GLY

LEU

9

THR

SER

GLU

ILE

LEU

ASN

SER

PHE

GLU

HIS

10

GLU

PHE

LEU

SER

LYS

ARG

LEU

SER

LYS

ALA

11

ARG

Samples:

sample_1: p68N, [U-100% 13C; U-100% 15N], 0.75 mM; NACL 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1.0 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 HNCO	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2KEB 4E2I 4Y97
DBJ	BAG73551
EMBL	CAG33018
GB	AAA16459 AAH01347 AAH02990 ABM82949 ABM86141
REF	NP_001253937 NP_002680 XP_001169495 XP_003828668 XP_003909632
SP	Q14181
AlphaFold	Q14181