BMRB Entry 15850

Name: Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A.
Published: 2008-10-13

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PDB ID: 2k5w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR15850
MolProbity Validation Chart

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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 Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A.

Deposition date:

2008-06-30

Original release date:

2008-10-13

Authors:

Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A." .

Assembly members:

Assembly members:
BcR103A, polymer, 117 residues, 13091.908 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):
BcR103A: MERASLNRIGKDVYYMQIKG EGTIEKVDGRNLRNYTLPAY DEDGVKKQITFRSTKKENDH KLNKYAFLRLYVDQDDNSKN EISSIEVKSYEEIQKADLPE KVKDKFTIKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	436
15N chemical shifts	95
1H chemical shifts	680

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BcR103A	1

Entities:

Entity 1, BcR103A 117 residues - 13091.908 Da.

21 residues lipobox was removed.

1

MET

GLU

ARG

ALA

SER

LEU

ASN

ARG

ILE

GLY

2

LYS

ASP

VAL

TYR

MET

GLN

ILE

LYS

GLY

3

GLU

GLY

THR

ILE

GLU

LYS

VAL

ASP

GLY

ARG

4

ASN

LEU

ARG

ASN

TYR

THR

LEU

PRO

ALA

TYR

5

ASP

GLU

ASP

GLY

VAL

LYS

GLN

ILE

THR

6

PHE

ARG

SER

THR

LYS

GLU

ASN

ASP

HIS

7

LYS

LEU

ASN

LYS

TYR

ALA

PHE

LEU

ARG

LEU

8

TYR

VAL

ASP

GLN

ASP

ASN

SER

LYS

ASN

9

GLU

ILE

SER

ILE

GLU

VAL

LYS

SER

TYR

10

GLU

ILE

GLN

LYS

ALA

ASP

LEU

PRO

GLU

11

LYS

VAL

LYS

ASP

LYS

PHE

THR

ILE

LYS

LEU

12

GLU

HIS

Samples:

sample_1: BcR103A, [U-100% 13C; U-100% 15N], 0.6 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_2: BcR103A, [5% 13C; U-100% 15N], 1.37 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_3: BcR103A, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 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 1H-13C NOESY ARO	sample_1	isotropic	sample_conditions_1
3D 1H-13C-15N SIM NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC stereo	sample_2	isotropic	sample_conditions_1
HETNOE	sample_2	isotropic	sample_conditions_1
slow exch 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - refinement

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - validation

PDBStat v5.1, Tejero R.; Montelione GT - validation

Molmol v2k2, Koradi, Billeter and Wuthrich - visualization

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

MolProbity, Richardson - Validation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz
Varian INOVA 500 MHz

PDB	2K5W
EMBL	CGG02256 CJA31281 CJB35032 CJC25384 CJC28010
GB	AAP09401 ADH07006 EEL11492 EJR35492 EJR82496
REF	NP_832200 WP_000713860 WP_000713863