BMRB Entry 7411

Name: Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach
Published: 2008-02-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7411

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:

Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach

Deposition date:

2007-10-02

Original release date:

2008-02-11

Authors:

Watson, Matthew; Stott, Katherine; Thomas, Jean

Citation:

Citation: Watson, Matthew; Stott, Katherine; Thomas, Jean. "Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach" J. Mol. Biol. 374, 1286-1297 (2007).
PubMed: 17988686

Assembly members:

Assembly members:
HMGB1-delta15, polymer, 199 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBAT4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HMGB1-delta15: GKGDPKKPRGKMSSYAFFVQ TCREEHKKKHPDASVNFSEF SKKCSERWKTMSAKEKGKFE DMAKADKARYEREMKTYIPP KGETKKKFKDPNAPKRPPSA FFLFCSEYRPKIKGEHPGLS IGDVAKKLGEMWNNTAADDK QPYEKKAAKLKEKYEKDIAA YRAKGKPDAAKKGVVKAEKS KKKKEEEDDEEDEEDEEEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	171
1H chemical shifts	177

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HMGB1, delta15	1

Entities:

Entity 1, HMGB1, delta15 199 residues - Formula weight is not available

1

GLY

LYS

GLY

ASP

PRO

LYS

PRO

ARG

GLY

2

LYS

MET

SER

TYR

ALA

PHE

VAL

GLN

3

THR

CYS

ARG

GLU

HIS

LYS

HIS

4

PRO

ASP

ALA

SER

VAL

ASN

PHE

SER

GLU

PHE

5

SER

LYS

CYS

SER

GLU

ARG

TRP

LYS

THR

6

MET

SER

ALA

LYS

GLU

LYS

GLY

LYS

PHE

GLU

7

ASP

MET

ALA

LYS

ALA

ASP

LYS

ALA

ARG

TYR

8

GLU

ARG

GLU

MET

LYS

THR

TYR

ILE

PRO

9

LYS

GLY

GLU

THR

LYS

PHE

LYS

ASP

10

PRO

ASN

ALA

PRO

LYS

ARG

PRO

SER

ALA

11

PHE

LEU

PHE

CYS

SER

GLU

TYR

ARG

PRO

12

LYS

ILE

LYS

GLY

GLU

HIS

PRO

GLY

LEU

SER

13

ILE

GLY

ASP

VAL

ALA

LYS

LEU

GLY

GLU

14

MET

TRP

ASN

THR

ALA

ASP

LYS

15

GLN

PRO

TYR

GLU

LYS

ALA

LYS

LEU

16

LYS

GLU

LYS

TYR

GLU

LYS

ASP

ILE

ALA

17

TYR

ARG

ALA

LYS

GLY

LYS

PRO

ASP

ALA

18

LYS

GLY

VAL

LYS

ALA

GLU

LYS

SER

19

LYS

GLU

ASP

GLU

20

GLU

ASP

GLU

ASP

GLU

Samples:

sample_1: HMGB1, delta15, [U-98% 15N], 0.3-1.4 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 800 MHz

BMRB	11147 15148 15149 15502 7408 7409 7410 7412 7413
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