BMRB Entry 16016

Name: NMR structure of TM0212 at 40 C
Published: 2012-07-19

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PDB ID: 2ka7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16016
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of TM0212 at 40 C

Deposition date:

2008-10-31

Original release date:

2012-07-19

Authors:

Pedrini, Bill; Herrmann, Torsten; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Pedrini, Bill; Herrmann, Torsten; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt. "Chemical shift assignment of TM0212" .

Assembly members:

Assembly members:
TM0212, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TM0212: MKMKKYTKTHEWVSIEDKVA TVGITNHAQEQLGDVVYVDL PEVGREVKKGEVVASIESVK AAADVYAPLSGKIVEVNEKL DTEPELINKDPEGEGWLFKM EISDEGELEDLLDEQAYQEF CAQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	128
1H chemical shifts	825

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TM0212	1

Entities:

Entity 1, TM0212 124 residues - Formula weight is not available

1

MET

LYS

MET

LYS

TYR

THR

LYS

THR

HIS

2

GLU

TRP

VAL

SER

ILE

GLU

ASP

LYS

VAL

ALA

3

THR

VAL

GLY

ILE

THR

ASN

HIS

ALA

GLN

GLU

4

GLN

LEU

GLY

ASP

VAL

TYR

VAL

ASP

LEU

5

PRO

GLU

VAL

GLY

ARG

GLU

VAL

LYS

GLY

6

GLU

VAL

ALA

SER

ILE

GLU

SER

VAL

LYS

7

ALA

ASP

VAL

TYR

ALA

PRO

LEU

SER

8

GLY

LYS

ILE

VAL

GLU

VAL

ASN

GLU

LYS

LEU

9

ASP

THR

GLU

PRO

GLU

LEU

ILE

ASN

LYS

ASP

10

PRO

GLU

GLY

GLU

GLY

TRP

LEU

PHE

LYS

MET

11

GLU

ILE

SER

ASP

GLU

GLY

GLU

LEU

GLU

ASP

12

LEU

ASP

GLU

GLN

ALA

TYR

GLN

GLU

PHE

13

CYS

ALA

GLN

GLU

Samples:

sample_1: TM0212, [U-100% 13C; U-100% 15N], 2.4 ± 0.2 mM; NaP 25 mM; NaCl 50 mM; DTT, [U-2H], 5 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 313.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
6D APSY HNCOCANH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aliphatic NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aromatic NOESY	sample_1	isotropic	sample_conditions_1

Software:

GAPRO, Hiller and Fiorito - Automated analysis of 2D APSY NMR projection

MATCH, Volk and Herrmann - Automated backbone assignment

ASCAN, Fiorito and Herrmann - NOESY-based sidechain assignment

ATHNOS-CANDID, Herrmann and Guntert - peak assignment and constraint collection, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	1ZKO 2KA7
GB	AAD35304 ACB09088 AGL49136 AHD18024 AKE26151
REF	NP_228027 WP_004082886 WP_010865076 WP_012310713
SP	Q9WY55
AlphaFold	Q9WY55