BMRB Entry 16498

Name: Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A.
Published: 2009-10-16

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PDB ID: 2kob
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16498
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A.

Deposition date:

2009-09-15

Original release date:

2009-10-16

Authors:

Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A." .

Assembly members:

Assembly members:
QlR8A, polymer, 108 residues, 13000 Da.

Natural source:

Natural source: Common Name: Clostridium leptum Taxonomy ID: 1535 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium leptum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
QlR8A: RDSFGDWAEKFLKSKEADGV SVSQLNSYKNYCRNHLSPLY MKSLSEILPADIQSIINETK LAKNTLKAIRNTASQIFRLA IENRAIDFNPADYVRIPKIA LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	113
1H chemical shifts	746

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	QlR8A	1

Entities:

Entity 1, QlR8A 108 residues - 13000 Da.

8 non-native residues at C-terminus (LEHHHHHH)

1

ARG

ASP

SER

PHE

GLY

ASP

TRP

ALA

GLU

LYS

2

PHE

LEU

LYS

SER

LYS

GLU

ALA

ASP

GLY

VAL

3

SER

VAL

SER

GLN

LEU

ASN

SER

TYR

LYS

ASN

4

TYR

CYS

ARG

ASN

HIS

LEU

SER

PRO

LEU

TYR

5

MET

LYS

SER

LEU

SER

GLU

ILE

LEU

PRO

ALA

6

ASP

ILE

GLN

SER

ILE

ASN

GLU

THR

LYS

7

LEU

ALA

LYS

ASN

THR

LEU

LYS

ALA

ILE

ARG

8

ASN

THR

ALA

SER

GLN

ILE

PHE

ARG

LEU

ALA

9

ILE

GLU

ASN

ARG

ALA

ILE

ASP

PHE

ASN

PRO

10

ALA

ASP

TYR

VAL

ARG

ILE

PRO

LYS

ILE

ALA

11

LEU

GLU

HIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliph	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC_sample	isotropic	sample_conditions_1
4D HCCH NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-13C NOESY arom	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC edHN2	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC swN	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC arom ct	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC arom no ct	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Varian INOVA 600 MHz
Bruker AvanceIII 850 MHz

PDB	2KOB
GB	EDO61441
REF	WP_003530379