BMRB Entry 4897

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4897

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:

Sequential assignment, secondary structure and binding site of the carbohydrate-binding domain of papg from Uropathogenic E.coli

Deposition date:

2000-11-08

Original release date:

2001-02-27

Authors:

Sung, Mei-an; Chen, Ho An; Matthews, Stephen

Citation:

Citation: Sung, Mei-an; Chen, Ho An; Matthews, Stephen. "Letter to the Editor: Sequential assignment and secondary structure of the triple-labelled carbohydrate-binding domain of papG from uropathogenic E. coli" J. Biomol. NMR 19, 197-198 (2001).

Assembly members:

Assembly members:
papG, polymer, 198 residues, 22729.6 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
papG: WNNIVFYSLGNVNSYQGGNV VITQRPQFITSWRPGIATVT WNQCNGPEFADGSWAYYREY IAWVVFPKKVMTQNGYPLFI EVHNKGSWSEENTGDNDSYF FLKGYKWDERAFDAGNLCQK PGETTRLTEKFDDIIFKVAL PADLPLGDYSVTIPYTSGIQ RHFASYLGARFKIPYNVAKT LPRENEMLFLFKNIGGLE

Data sets:

assigned_chemical_shifts
- papgII_shift_1

Data type	Count
13C chemical shifts	569
15N chemical shifts	184
1H chemical shifts	184

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	papG	1

Entities:

Entity 1, papG 198 residues - 22729.6 Da.

1

TRP

ASN

ILE

VAL

PHE

TYR

SER

LEU

GLY

2

ASN

VAL

ASN

SER

TYR

GLN

GLY

ASN

VAL

3

VAL

ILE

THR

GLN

ARG

PRO

GLN

PHE

ILE

THR

4

SER

TRP

ARG

PRO

GLY

ILE

ALA

THR

VAL

THR

5

TRP

ASN

GLN

CYS

ASN

GLY

PRO

GLU

PHE

ALA

6

ASP

GLY

SER

TRP

ALA

TYR

ARG

GLU

TYR

7

ILE

ALA

TRP

VAL

PHE

PRO

LYS

VAL

8

MET

THR

GLN

ASN

GLY

TYR

PRO

LEU

PHE

ILE

9

GLU

VAL

HIS

ASN

LYS

GLY

SER

TRP

SER

GLU

10

GLU

ASN

THR

GLY

ASP

ASN

ASP

SER

TYR

PHE

11

PHE

LEU

LYS

GLY

TYR

LYS

TRP

ASP

GLU

ARG

12

ALA

PHE

ASP

ALA

GLY

ASN

LEU

CYS

GLN

LYS

13

PRO

GLY

GLU

THR

ARG

LEU

THR

GLU

LYS

14

PHE

ASP

ILE

PHE

LYS

VAL

ALA

LEU

15

PRO

ALA

ASP

LEU

PRO

LEU

GLY

ASP

TYR

SER

16

VAL

THR

ILE

PRO

TYR

THR

SER

GLY

ILE

GLN

17

ARG

HIS

PHE

ALA

SER

TYR

LEU

GLY

ALA

ARG

18

PHE

LYS

ILE

PRO

TYR

ASN

VAL

ALA

LYS

THR

19

LEU

PRO

ARG

GLU

ASN

GLU

MET

LEU

PHE

LEU

20

PHE

LYS

ASN

ILE

GLY

LEU

GLU

Samples:

Sample_1: papG, [U-99% 13C; U-99% 15N; U-90% 2H], 1.0 mM

Ex-cond_1: ionic strength: 0.03 M; pH: 5.2; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	not available	not available	not available
d-HNCA	not available	not available	not available
d-HN(CO)CA	not available	not available	not available
d-HNCO	not available	not available	not available
d-HN(CA)CO	not available	not available	not available
d-HN(CA)CB	not available	not available	not available
d-HN(COCA)CB	not available	not available	not available
z-shielded gradient, triple-resonance probe was equipped	not available	not available	not available

Software:

AURELIA v2.1.1 - sequence assignments

NMR spectrometers:

Bruker DRX 500 MHz

EMBL	CAA43555 CAR04491 CCP97646
GB	AAA24293 AAL67407 AAN82031 AAN83601 AAP48795
REF	NP_755458 NP_757027 WP_000758683 WP_000758684 WP_000758685