BMRB Entry 5868

Name: Solution structure of XPC binding domain of hHR23B
Published: 2005-05-19

Click here to enlarge.

PDB ID: 1pve
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5868
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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:

Solution structure of XPC binding domain of hHR23B

Deposition date:

2003-07-14

Original release date:

2005-05-19

Authors:

Kim, B.; Ryu, K.-S.; Kim, H.; Choi, B.-S.

Citation:

Citation: Kim, B.; Ryu, K.-S.; Kim, H.; Cho, S.; Choi, B.-S.. "Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B." FEBS J. 272, 2467-2476 (2005).
PubMed: 15885096

Assembly members:

Assembly members:
RAD23 homolog B, polymer, 72 residues, Formula weight is not available

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: PET15B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RAD23 homolog B: GSHMPLEFLRNQPQFQQMRQ IIQQNPSLLPALLQQIGREN PQLLQQISQHQEHFIQMLNE PVQEAGGQGGGG

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	269
15N chemical shifts	82
1H chemical shifts	461

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RAD23 homolog B	1

Entities:

Entity 1, RAD23 homolog B 72 residues - Formula weight is not available

1

GLY

SER

HIS

MET

PRO

LEU

GLU

PHE

LEU

ARG

2

ASN

GLN

PRO

GLN

PHE

GLN

MET

ARG

GLN

3

ILE

GLN

ASN

PRO

SER

LEU

PRO

4

ALA

LEU

GLN

ILE

GLY

ARG

GLU

ASN

5

PRO

GLN

LEU

GLN

ILE

SER

GLN

HIS

6

GLN

GLU

HIS

PHE

ILE

GLN

MET

LEU

ASN

GLU

7

PRO

VAL

GLN

GLU

ALA

GLY

GLN

GLY

8

GLY

Samples:

sample_1: RAD23 homolog B, [U-15N; U-13C], 1 mM; phosphate buffer NA 40 mM; CHAPS NA 10 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 210 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

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

Software:

VNMR v6.3c - collection

NMRPipe - processing

CYANA v1.6 - structure solution

AMBER v7 - refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	1PVE 2F4M 2F4O
DBJ	BAA04652 BAD97199 BAE89144 BAE89405 BAG54170
EMBL	CAA63146
GB	AAH20973 AAH27747 AAH70960 AAH90351 AAH98674
PRF	2206377B
REF	NP_001020446 NP_001039775 NP_001231638 NP_001231642 NP_001231653
SP	P54727 Q29RK4 Q4KMA2
TPG	DAA26518
AlphaFold	P54727 Q29RK4 Q4KMA2