BMRB Entry 19530

Name: Resonance assignment of RQC domain of human Bloom syndrome protein
Published: 2014-04-16

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PDB ID: 2mh9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19530
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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:

Resonance assignment of RQC domain of human Bloom syndrome protein

Deposition date:

2013-09-25

Original release date:

2014-04-16

Authors:

Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok

Citation:

Citation: Park, Chin-Ju; Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok. "Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein." J. Biomol. NMR 58, 141-147 (2014).
PubMed: 24435566

Assembly members:

Assembly members:
BLM_RQC, polymer, 144 residues, 16089.5 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BLM_RQC: CKTKDYKTRDVTDDVKSIVR FVQEHSSSQGMRNIKHVGPS GRFTMNMLVDIFLGSKSAKI QSGIFGKGSAYSRHNAERLF KKLILDKILDEDLYINANDQ AIAYVMLGNKAQTVLNGNLK VDFMETENSSSVKKQKALVA KVSQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	796
13C chemical shifts	324
15N chemical shifts	120

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BLM RQC	1

Entities:

Entity 1, BLM RQC 144 residues - 16089.5 Da.

1

CYS

LYS

THR

LYS

ASP

TYR

LYS

THR

ARG

ASP

2

VAL

THR

ASP

VAL

LYS

SER

ILE

VAL

ARG

3

PHE

VAL

GLN

GLU

HIS

SER

GLN

GLY

4

MET

ARG

ASN

ILE

LYS

HIS

VAL

GLY

PRO

SER

5

GLY

ARG

PHE

THR

MET

ASN

MET

LEU

VAL

ASP

6

ILE

PHE

LEU

GLY

SER

LYS

SER

ALA

LYS

ILE

7

GLN

SER

GLY

ILE

PHE

GLY

LYS

GLY

SER

ALA

8

TYR

SER

ARG

HIS

ASN

ALA

GLU

ARG

LEU

PHE

9

LYS

LEU

ILE

LEU

ASP

LYS

ILE

LEU

ASP

10

GLU

ASP

LEU

TYR

ILE

ASN

ALA

ASN

ASP

GLN

11

ALA

ILE

ALA

TYR

VAL

MET

LEU

GLY

ASN

LYS

12

ALA

GLN

THR

VAL

LEU

ASN

GLY

ASN

LEU

LYS

13

VAL

ASP

PHE

MET

GLU

THR

GLU

ASN

SER

14

SER

VAL

LYS

GLN

LYS

ALA

LEU

VAL

ALA

15

LYS

VAL

SER

GLN

Samples:

sample_1: BLM RQC, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%; DTT 1 mM; Tris 20 mM; Sodium Chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

GB	NP_000048 .1 AAA87850 AAH93622 AAI01568 AAI15031 AAI15033
PDB	2MH9 3WE2 3WE3 4CDG 4CGZ 4O3M
DBJ	BAG36927 BAH12008 BAH13907
REF	NP_000048 NP_001274175 NP_001274177 XP_001097543 XP_003268551
SP	P54132
AlphaFold	P54132