BMRB Entry 7316

Name: Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY
Published: 2007-05-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7316

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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:

Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY

Deposition date:

2006-10-17

Original release date:

2007-05-04

Authors:

Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey

Citation:

Citation: Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey. "NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7." J. Mol. Biol. 366, 1001-1015 (2007).
PubMed: 17188712

Assembly members:

Assembly members:
Im7*, polymer, 94 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Im7*: MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTDL IYYPSDNRDDSPEGIVKEIK EWRAANGKPGFKQG

Data sets:

assigned_chemical_shifts
- Im7*_chemical_shifts

Data type	Count
13C chemical shifts	247
15N chemical shifts	80
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Monomer	1

Entities:

Entity 1, Monomer 94 residues - Formula weight is not available

The sequence of Im7* contains an N-terminal His-tag (denoted by *). Residue numbering starts at residue 2 of wt Im7 (no his-tag).

1

MET

GLU

HIS

GLU

LEU

2

LYS

ASN

SER

ILE

SER

ASP

TYR

THR

GLU

ALA

3

GLU

PHE

VAL

GLN

LEU

LYS

GLU

ILE

GLU

4

LYS

GLU

ASN

VAL

ALA

THR

ASP

VAL

5

LEU

ASP

VAL

LEU

GLU

HIS

PHE

VAL

LYS

6

ILE

THR

GLU

HIS

PRO

ASP

GLY

THR

ASP

LEU

7

ILE

TYR

PRO

SER

ASP

ASN

ARG

ASP

8

SER

PRO

GLU

GLY

ILE

VAL

LYS

GLU

ILE

LYS

9

GLU

TRP

ARG

ALA

ASN

GLY

LYS

PRO

GLY

10

PHE

LYS

GLN

GLY

Samples:

sample_1: Im7*, [U-13C; U-15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%

sample_2: Im7*, [U-99% 15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%

conditions_1: pH: 7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N HSQC	All_samples	not available	conditions_1
HNCO	Samples_1_and_3_and_5	not available	conditions_1
HNCA	Samples_3_and_5	not available	conditions_1
HNCOCA	Samples_3_and_5_again	not available	conditions_1
CBCACONH	Samples_3_and_5_again2	not available	conditions_1
HNCACB	sample_1	not available	conditions_1
1H-1H-15N NOESY-HSQC	sample_2	not available	conditions_1

Software:

VNMR v6.1C, Varian - Data acquisition

NMRView v5.1.1, Varian - Data analysis

NMR spectrometers:

Varian Inova 500 MHz
Varian Inova 600 MHz
Varian Inova 750 MHz

BMRB	7188 7317
PDB	1AYI 1CEI 1MZ8 1UJZ 1UNK 1ZNV 2ERH 2JAZ 2JB0 2JBG 7CEI
EMBL	CAA45165 CDK50318
GB	AAA23071 AIC79148 ELE46623 EOW15734 EQR11492
REF	WP_001560791 WP_032277812 YP_009060494
SP	Q03708
AlphaFold	Q03708