BMRB Entry 11147

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PDB ID: 2yrq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11147
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:

Solution structure of the tandem HMG box domain from Human High mobility group protein B1

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the tandem HMG box domain from Human High mobility group protein B1" .

Assembly members:

Assembly members:
HMG box domain, polymer, 173 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: cell free synthesis Host organism: E. coli - cell free Vector: P061030-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HMG box domain: GSSGSSGMGKGDPKKPRGKM SSYAFFVQTCREEHKKKHPD ASVNFSEFSKKCSERWKTMS AKEKGKFEDMAKADKARYER EMKTYIPPKGETKKKFKDPN APKRPPSAFFLFCSEYRPKI KGEHPGLSIGDVAKKLGEMW NNTAADDKQPYEKKAAKLKE KYEKDIAAYRAKG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	769
15N chemical shifts	168
1H chemical shifts	1196

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HMG box domain	1

Entities:

Entity 1, HMG box domain 173 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

GLY

LYS

2

GLY

ASP

PRO

LYS

PRO

ARG

GLY

LYS

MET

3

SER

TYR

ALA

PHE

VAL

GLN

THR

CYS

4

ARG

GLU

HIS

LYS

HIS

PRO

ASP

5

ALA

SER

VAL

ASN

PHE

SER

GLU

PHE

SER

LYS

6

LYS

CYS

SER

GLU

ARG

TRP

LYS

THR

MET

SER

7

ALA

LYS

GLU

LYS

GLY

LYS

PHE

GLU

ASP

MET

8

ALA

LYS

ALA

ASP

LYS

ALA

ARG

TYR

GLU

ARG

9

GLU

MET

LYS

THR

TYR

ILE

PRO

LYS

GLY

10

GLU

THR

LYS

PHE

LYS

ASP

PRO

ASN

11

ALA

PRO

LYS

ARG

PRO

SER

ALA

PHE

12

LEU

PHE

CYS

SER

GLU

TYR

ARG

PRO

LYS

ILE

13

LYS

GLY

GLU

HIS

PRO

GLY

LEU

SER

ILE

GLY

14

ASP

VAL

ALA

LYS

LEU

GLY

GLU

MET

TRP

15

ASN

THR

ALA

ASP

LYS

GLN

PRO

16

TYR

GLU

LYS

ALA

LYS

LEU

LYS

GLU

17

LYS

TYR

GLU

LYS

ASP

ILE

ALA

TYR

ARG

18

ALA

LYS

GLY

Samples:

sample_1: HMG box domain, [U-13C; U-15N], 1.09 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

TOPSPIN v1.3, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9823, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

Bruker AVANCE II 900 MHz

BMRB	15148 15149 15502
PDB	2YRQ
DBJ	BAA09924 BAC29902 BAC34367 BAC34773 BAC38678
EMBL	CAA31110 CAA31284 CAA56631 CAA68441 CAA68526
GB	AAA20508 AAA31050 AAA40729 AAA57042 AAA64970
PIR	S29857
REF	NP_001002937 NP_001004034 NP_001075304 NP_001102843 NP_001162380
SP	A9RA84 B0CM99 B1MTB0 P07156 P09429
TPG	DAA21468 DAA23902
AlphaFold	A9RA84 B0CM99 B1MTB0 P07156 P09429