BMRB Entry 16102

Name: Solution NMR Structure of the Integrase-Like Domain from Bacillus cereus Ordered Locus BC_1272. Northeast Structural Genomics Target BcR268F
Published: 2009-02-19

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PDB ID: 2kd1
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/BMR16102
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of the Integrase-Like Domain from Bacillus cereus Ordered Locus BC_1272. Northeast Structural Genomics Target BcR268F

Deposition date:

2008-12-31

Original release date:

2009-02-19

Authors:

Rossi, Paolo; Lee, Hsiau-Wei; Maglaqui, Melissa; Foote, Erica; Buchwald, William; Jiang, Mei; Gurla, Swapna; Nair, Rajesh; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Prestegard, James; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Lee, Hsiau-Wei; Xiao, Rong; Acton, Thomas; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of the Integrase-Like Domain from Bacillus cereus Ordered Locus BC_1272. Northeast Structural Genomics Target BcR268F" .

Assembly members:

Assembly members:
BcR268F, polymer, 118 residues, 13570.846 Da.

Natural source:

Natural source: Common Name: Bacillus cereus Taxonomy ID: 1396 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BcR268F: MEPSKLSYGEYLESWFNTKR HSVGIQTAKVLKGYLNSRII PSLGNIKLAKLTSLHMQNYV NSLRDEGLKRGTIEKIIKVI RNSLEHAIDLELITKNVAAK TKLPKADKEELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	511
15N chemical shifts	123
1H chemical shifts	840

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BcR268F	1

Entities:

Entity 1, BcR268F 118 residues - 13570.846 Da.

1

MET

GLU

PRO

SER

LYS

LEU

SER

TYR

GLY

GLU

2

TYR

LEU

GLU

SER

TRP

PHE

ASN

THR

LYS

ARG

3

HIS

SER

VAL

GLY

ILE

GLN

THR

ALA

LYS

VAL

4

LEU

LYS

GLY

TYR

LEU

ASN

SER

ARG

ILE

5

PRO

SER

LEU

GLY

ASN

ILE

LYS

LEU

ALA

LYS

6

LEU

THR

SER

LEU

HIS

MET

GLN

ASN

TYR

VAL

7

ASN

SER

LEU

ARG

ASP

GLU

GLY

LEU

LYS

ARG

8

GLY

THR

ILE

GLU

LYS

ILE

LYS

VAL

ILE

9

ARG

ASN

SER

LEU

GLU

HIS

ALA

ILE

ASP

LEU

10

GLU

LEU

ILE

THR

LYS

ASN

VAL

ALA

LYS

11

THR

LYS

LEU

PRO

LYS

ALA

ASP

LYS

GLU

12

LEU

GLU

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.986 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; NaN3 0.02%; Calcium Chloride 5 mM

sample_2: entity, [5% 13C; U-100% 15N], 0.953 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; NaN3 0.02%; Calcium Chloride 5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
N15 T1	sample_2	isotropic	sample_conditions_1
N15 T2	sample_2	isotropic	sample_conditions_1
HET noe	sample_2	isotropic	sample_conditions_1
N15 trosy iso	sample_2	isotropic	sample_conditions_1
N15 trosy PolyAcrylamide Gel	sample_2	anisotropic	sample_conditions_1
2D 1H-13C HSQC stereomethyls	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

CYANA v3.0 beta, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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

PSVS, Bhattacharya and Montelione - validation

Molmol, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation

PDBStat v5.1, Tejero, Montelione - refinement

MolProbity, Richardson - processing

NMR spectrometers:

Bruker Avance 600 MHz
Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2KD1
GB	AAP08256 EEL12452
REF	NP_831055 WP_000678909