BMRB Entry 31035

Name: Solution Structure of the H3 protein
Published: 2023-08-03

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PDB ID: 8dwq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31035
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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 H3 protein

Deposition date:

2022-08-01

Original release date:

2023-08-03

Authors:

Kelly, M.

Citation:

Citation: Kelly, M.. "Solution Structure of the H3 protein" .

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 18471.723 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMASMTGGQQMGRMEIFH TSPVEITTINTQGRFGEFLC FAADEYVMTAGDHVTYRIKV DESDIIMAGSIFYHERAADL SGLVERVMQLTGCDEDTAEE LISQRIDVFNLDDIDASDAA ELSWEIQAITAKAAKTLGFR GVSMQDEQGTCYMIDMLGHD AELVRVK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	424
15N chemical shifts	147
1H chemical shifts	849

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 167 residues - 18471.723 Da.

1

GLY

SER

HIS

MET

ALA

SER

MET

THR

GLY

2

GLN

MET

GLY

ARG

MET

GLU

ILE

PHE

HIS

3

THR

SER

PRO

VAL

GLU

ILE

THR

ILE

ASN

4

THR

GLN

GLY

ARG

PHE

GLY

GLU

PHE

LEU

CYS

5

PHE

ALA

ASP

GLU

TYR

VAL

MET

THR

ALA

6

GLY

ASP

HIS

VAL

THR

TYR

ARG

ILE

LYS

VAL

7

ASP

GLU

SER

ASP

ILE

MET

ALA

GLY

SER

8

ILE

PHE

TYR

HIS

GLU

ARG

ALA

ASP

LEU

9

SER

GLY

LEU

VAL

GLU

ARG

VAL

MET

GLN

LEU

10

THR

GLY

CYS

ASP

GLU

ASP

THR

ALA

GLU

11

LEU

ILE

SER

GLN

ARG

ILE

ASP

VAL

PHE

ASN

12

LEU

ASP

ILE

ASP

ALA

SER

ASP

ALA

13

GLU

LEU

SER

TRP

GLU

ILE

GLN

ALA

ILE

THR

14

ALA

LYS

ALA

LYS

THR

LEU

GLY

PHE

ARG

15

GLY

VAL

SER

MET

GLN

ASP

GLU

GLN

GLY

THR

16

CYS

TYR

MET

ILE

ASP

MET

LEU

GLY

HIS

ASP

17

ALA

GLU

LEU

VAL

ARG

VAL

LYS

Samples:

sample_1: H3 Protein, [U-100% 13C; U-100% 15N], 0.7 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - refinement

CcpNmr Analysis v2.4.2, CCPN - data analysis

TopSpin v4.0.8, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks