BMRB Entry 16007

Name: NMR structure of the protein TM1367
Published: 2009-04-14

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PDB ID: 2ka0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16007
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the protein TM1367

Deposition date:

2008-10-27

Original release date:

2009-04-14

Authors:

Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Geralt, Michel; Horst, Reto; Wilson, Ian; Wuthrich, Kurt

Citation:

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Pedrini, Bill; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Herrmann, Torsten; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures for the proteins TM1112 and TM1367." Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1381-1392 (2010).
PubMed: 20944235

Assembly members:

Assembly members:
TM1367, polymer, 124 residues, 13923 Da.

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: thermotogae Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TM1367: MRVELLFESGKCVIDLNEEY EVVKLLKEKIPFESVVNTWG EEIYFSTPVNVQKMENPREV VEIGDVGYWPPGKALCLFFG KTPMSDDKIQPASAVNVIGK IVEGLEDLKKIKDGEKVAVR FASS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	439
15N chemical shifts	126
1H chemical shifts	920

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TM1367	1

Entities:

Entity 1, TM1367 124 residues - 13923 Da.

1

MET

ARG

VAL

GLU

LEU

PHE

GLU

SER

GLY

2

LYS

CYS

VAL

ILE

ASP

LEU

ASN

GLU

TYR

3

GLU

VAL

LYS

LEU

LYS

GLU

LYS

ILE

4

PRO

PHE

GLU

SER

VAL

ASN

THR

TRP

GLY

5

GLU

ILE

TYR

PHE

SER

THR

PRO

VAL

ASN

6

VAL

GLN

LYS

MET

GLU

ASN

PRO

ARG

GLU

VAL

7

VAL

GLU

ILE

GLY

ASP

VAL

GLY

TYR

TRP

PRO

8

PRO

GLY

LYS

ALA

LEU

CYS

LEU

PHE

GLY

9

LYS

THR

PRO

MET

SER

ASP

LYS

ILE

GLN

10

PRO

ALA

SER

ALA

VAL

ASN

VAL

ILE

GLY

LYS

11

ILE

VAL

GLU

GLY

LEU

GLU

ASP

LEU

LYS

12

ILE

LYS

ASP

GLY

GLU

LYS

VAL

ALA

VAL

ARG

13

PHE

ALA

SER

Samples:

sample_1: DTT 0.5 mM; D10-DTT 4.5 mM; sodium azide 0.03%; sodium chloride 50 mM; sodium phosphate 25 mM; D2O 10%; H2O 90%; TM1367, [U-98% 13C; U-98% 15N], 1.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D [15N,1H] HSQC	sample_1	isotropic	sample_conditions_1
2D [13C,1H] HSQC	sample_1	isotropic	sample_conditions_1
3D 15N - resolved [1H,1H] NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aliphatic 13C	sample_1	isotropic	sample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aromatic 13C	sample_1	isotropic	sample_conditions_1
4D-APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D-APSY-HACACONH	sample_1	isotropic	sample_conditions_1
5D-APSY-CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

TOPSPIN v1.3, Bruker Biospin - processing

ASCAN, (ASCAN)-Fiorito,Herrmann,Damberger and Wuthrich - chemical shift assignment

MATCH, (MATCH)-Volk, Herrmann and K. Wuthrich - chemical shift assignment

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	1ZX8 2KA0
GB	AAD36437 ABQ47429 ACB09806 ADA67518 AGL50298
REF	NP_229168 WP_004081563 WP_011943885 WP_012311149 WP_038034479