BMRB Entry 7259

Click here to enlarge.

PDB ID: 2htf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7259
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: The solution structure of the BRCT domain from human polymerase reveals homology with the TdT BRCT domain PubMed: 17915942

Deposition date: 2006-08-10 Original release date: 2007-11-21

Authors: DeRose, E.; Clarkson, M.; Gilmore, S.; Ramsden, D.; Mueller, G.; London, R.; Lee, A.

Citation: DeRose, E.; Clarkson, M.; Gilmore, S.; Galban, C.; Tripathy, A.; Havener, J.; Mueller, G.; Ramsden, D.; London, R.; Lee, A.. "Solution Structure of Polymerase mu's BRCT Domain Reveals an Element Essential for Its Role in Nonhomologous End Joining." Biochemistry 46, 12100-12110 (2007).

Assembly members:
DNA polymerase mu (E.C.2.7.7.7), polymer, 105 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
DNA polymerase mu (E.C.2.7.7.7): GTPPSTRFPGVAIYLVEPRM GRSRRAFLTGLARSKGFRVL DACSSEATHVVMEETSAEEA VSWQERRMAAAPPGCTPPAL LDISWLTESLGAGQPVPVEC RHRLE

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	413
15N chemical shifts	100
1H chemical shifts	651

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DNA polymerase mu	1

Entities:

Entity 1, DNA polymerase mu 105 residues - Formula weight is not available

1

GLY

THR

PRO

SER

THR

ARG

PHE

PRO

GLY

2

VAL

ALA

ILE

TYR

LEU

VAL

GLU

PRO

ARG

MET

3

GLY

ARG

SER

ARG

ALA

PHE

LEU

THR

GLY

4

LEU

ALA

ARG

SER

LYS

GLY

PHE

ARG

VAL

LEU

5

ASP

ALA

CYS

SER

GLU

ALA

THR

HIS

VAL

6

VAL

MET

GLU

THR

SER

ALA

GLU

ALA

7

VAL

SER

TRP

GLN

GLU

ARG

MET

ALA

8

ALA

PRO

GLY

CYS

THR

PRO

ALA

LEU

9

LEU

ASP

ILE

SER

TRP

LEU

THR

GLU

SER

LEU

10

GLY

ALA

GLY

GLN

PRO

VAL

PRO

VAL

GLU

CYS

11

ARG

HIS

ARG

LEU

GLU

Samples:

sample_1: DNA polymerase mu (E.C.2.7.7.7), [U-13C; U-15N], 1 mM; d-Tris 25 mM; KCl 50 mM; NaN3 0.02%; DTT 5 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 50 mM; pH: 7.9; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	not available	not available	not available
3D 15N-separated NOESY	not available	not available	not available

Software:

VNMR v1.1C, VNMRJ 1.1C - collection

NMRPipe v2003, 2004 - processing

NMRView v5.0.4 - processing

CYANA v2.1 - structure solution

ARIA v2.0a - refinement

NMR spectrometers:

Varian INOVA 800 MHz

PDB	2DUN 2HTF
DBJ	BAB14353 BAF84327 BAG57686
EMBL	CAB65075
GB	AAF26284 AAH26306 AAH49202 AAH62590 AAW65376
REF	NP_001271259 NP_001271260 NP_037416 XP_001142751 XP_001142835
SP	Q9NP87

Biological Magnetic Resonance Data Bank