BMRB Entry 50210

Name: EAP34
Published: 2021-07-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50210

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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:

EAP34

Deposition date:

2020-03-12

Original release date:

2021-07-27

Authors:

Pal, Indrani; Prakash, Om

Citation:

Citation: Pal, Indrani; Mishra, Nitin; Herrera, Alvaro; Dubey, Abhinav; Arthanari, Haribabu; Geisbrecht, Brian; Prakash, Om. "1H, 15N, and 13C backbone resonance assignments of the C4b-binding region from the S. aureus extracellular adherence protein" Biomol. NMR Assign. 15, 183-186 (2021).
PubMed: 33423171

Assembly members:

Assembly members:
entity_1, polymer, 208 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: obtained from a collaborator Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VPYSINLNGTSTNILSNLSF SNKPWTNYKNLTSQIKSVLK HDRGISEQDLKYAKKAYYTV YFKNGGKRILQLNSKNYTAN LVHAKDVKRIEITVKTGTKA KADRYVPYTIAVNGTSTPIL SKLKISNKQLISYKYLNDKV KSVLKSERGISDLDLKFAKQ AKYTVYFKNGKKQVVNLKSD IFTPNLFSAKDIKKIDIDVK QYTKSKKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	581
15N chemical shifts	199
1H chemical shifts	199

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EAP34	1

Entities:

Entity 1, EAP34 208 residues - Formula weight is not available

1

VAL

PRO

TYR

SER

ILE

ASN

LEU

ASN

GLY

THR

2

SER

THR

ASN

ILE

LEU

SER

ASN

LEU

SER

PHE

3

SER

ASN

LYS

PRO

TRP

THR

ASN

TYR

LYS

ASN

4

LEU

THR

SER

GLN

ILE

LYS

SER

VAL

LEU

LYS

5

HIS

ASP

ARG

GLY

ILE

SER

GLU

GLN

ASP

LEU

6

LYS

TYR

ALA

LYS

ALA

TYR

THR

VAL

7

TYR

PHE

LYS

ASN

GLY

LYS

ARG

ILE

LEU

8

GLN

LEU

ASN

SER

LYS

ASN

TYR

THR

ALA

ASN

9

LEU

VAL

HIS

ALA

LYS

ASP

VAL

LYS

ARG

ILE

10

GLU

ILE

THR

VAL

LYS

THR

GLY

THR

LYS

ALA

11

LYS

ALA

ASP

ARG

TYR

VAL

PRO

TYR

THR

ILE

12

ALA

VAL

ASN

GLY

THR

SER

THR

PRO

ILE

LEU

13

SER

LYS

LEU

LYS

ILE

SER

ASN

LYS

GLN

LEU

14

ILE

SER

TYR

LYS

TYR

LEU

ASN

ASP

LYS

VAL

15

LYS

SER

VAL

LEU

LYS

SER

GLU

ARG

GLY

ILE

16

SER

ASP

LEU

ASP

LEU

LYS

PHE

ALA

LYS

GLN

17

ALA

LYS

TYR

THR

VAL

TYR

PHE

LYS

ASN

GLY

18

LYS

GLN

VAL

ASN

LEU

LYS

SER

ASP

19

ILE

PHE

THR

PRO

ASN

LEU

PHE

SER

ALA

LYS

20

ASP

ILE

LYS

ILE

ASP

ILE

ASP

VAL

LYS

21

GLN

TYR

THR

LYS

SER

LYS

Samples:

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

sample_conditions_1: pH: 6.8; pressure: 1 atm; 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