BMRB Entry 50304

Name: EapH1
Published: 2023-02-20

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PDB ID: 8gdh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50304
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:

EapH1

Deposition date:

2020-06-04

Original release date:

2023-02-20

Authors:

Pal, Indrani; Herrera, Alvaro; Mishra, Nitin; Prakash, Om

Citation:

Citation: Mishra, Nitin; Pal, Indrani; Herrera, Alvaro; Dubey, Abhinav; Arthanari, Haribabu; Geisbrecht, Brian; Prakash, Om. "Complete non-proline backbone resonance assignments of the S. aureus neutrophil serine protease inhibitor, EapH1" Biomol. NMR Assign. 17, 129-134 (2023).
PubMed: 37160842

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSTDSNNGYKELTMDGKHTV PYTISVDGITALHRTYFVFP ENKKVLYQEIDSKVKNELAS QRGVTTEKINNAQTATYTLT LNDGNKKVVNLKKNDDAKNS IDPSTIKQIQIVVK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	325
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EapH1	1

Entities:

Entity 1, EapH1 114 residues - Formula weight is not available

1

GLY

SER

THR

ASP

SER

ASN

GLY

TYR

LYS

2

GLU

LEU

THR

MET

ASP

GLY

LYS

HIS

THR

VAL

3

PRO

TYR

THR

ILE

SER

VAL

ASP

GLY

ILE

THR

4

ALA

LEU

HIS

ARG

THR

TYR

PHE

VAL

PHE

PRO

5

GLU

ASN

LYS

VAL

LEU

TYR

GLN

GLU

ILE

6

ASP

SER

LYS

VAL

LYS

ASN

GLU

LEU

ALA

SER

7

GLN

ARG

GLY

VAL

THR

GLU

LYS

ILE

ASN

8

ASN

ALA

GLN

THR

ALA

THR

TYR

THR

LEU

THR

9

LEU

ASN

ASP

GLY

ASN

LYS

VAL

ASN

10

LEU

LYS

ASN

ASP

ALA

LYS

ASN

SER

11

ILE

ASP

PRO

SER

THR

ILE

LYS

GLN

ILE

GLN

12

ILE

VAL

LYS

Samples:

sample_1: EapH1, [U-100% 13C; U-100% 15N], 800 uM

sample_conditions_1: pH: 6.6; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMR spectrometers:

Varian INOVA 700 MHz

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