BMRB Entry 17370

Name: Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155.
Published: 2011-01-05

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PDB ID: 2l7q
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17370
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155.

Deposition date:

2010-12-20

Original release date:

2011-01-05

Authors:

Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155." .

Assembly members:

Assembly members:
protein_BVU, polymer, 248 residues, 14645.2 Da.

Natural source:

Natural source: Common Name: Bacteroides Vulgatus Taxonomy ID: 821 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides Vulgatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein_BVU: MNELDIQQEYPFTVESMPVA DEIAGDETVEIRLEIKPSGN FIGTVYTLRYFQPDGKGSLK MEDGTVLKPNDRYLLNEWKF RLYYTSQSDKEAQTIDLYFE DNWGNLQQLTYDFNGKLEHH HHHHMNELDIQQEYPFTVES MPVADEIAGDETVEIRLEIK PSGNFIGTVYTLRYFQPDGK GSLKMEDGTVLKPNDRYLLN EWKFRLYYTSQSDKEAQTID LYFEDNWGNLQQLTYDFNGK LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	549
15N chemical shifts	132
1H chemical shifts	858

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein BVU 1572(27-141)	1

Entities:

Entity 1, protein BVU 1572(27-141) 248 residues - 14645.2 Da.

1

MET

ASN

GLU

LEU

ASP

ILE

GLN

GLU

TYR

2

PRO

PHE

THR

VAL

GLU

SER

MET

PRO

VAL

ALA

3

ASP

GLU

ILE

ALA

GLY

ASP

GLU

THR

VAL

GLU

4

ILE

ARG

LEU

GLU

ILE

LYS

PRO

SER

GLY

ASN

5

PHE

ILE

GLY

THR

VAL

TYR

THR

LEU

ARG

TYR

6

PHE

GLN

PRO

ASP

GLY

LYS

GLY

SER

LEU

LYS

7

MET

GLU

ASP

GLY

THR

VAL

LEU

LYS

PRO

ASN

8

ASP

ARG

TYR

LEU

ASN

GLU

TRP

LYS

PHE

9

ARG

LEU

TYR

THR

SER

GLN

SER

ASP

LYS

10

GLU

ALA

GLN

THR

ILE

ASP

LEU

TYR

PHE

GLU

11

ASP

ASN

TRP

GLY

ASN

LEU

GLN

LEU

THR

12

TYR

ASP

PHE

ASN

GLY

LYS

LEU

GLU

HIS

13

HIS

MET

ASN

GLU

LEU

ASP

ILE

14

GLN

GLU

TYR

PRO

PHE

THR

VAL

GLU

SER

15

MET

PRO

VAL

ALA

ASP

GLU

ILE

ALA

GLY

ASP

16

GLU

THR

VAL

GLU

ILE

ARG

LEU

GLU

ILE

LYS

17

PRO

SER

GLY

ASN

PHE

ILE

GLY

THR

VAL

TYR

18

THR

LEU

ARG

TYR

PHE

GLN

PRO

ASP

GLY

LYS

19

GLY

SER

LEU

LYS

MET

GLU

ASP

GLY

THR

VAL

20

LEU

LYS

PRO

ASN

ASP

ARG

TYR

LEU

ASN

21

GLU

TRP

LYS

PHE

ARG

LEU

TYR

THR

SER

22

GLN

SER

ASP

LYS

GLU

ALA

GLN

THR

ILE

ASP

23

LEU

TYR

PHE

GLU

ASP

ASN

TRP

GLY

ASN

LEU

24

GLN

LEU

THR

TYR

ASP

PHE

ASN

GLY

LYS

25

LEU

GLU

HIS

Samples:

NC_sample: conjugate transposon protein BVU_1572(27-141), [U-100% 13C; U-100% 15N], 0.53 ± 0.05 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 mM; DTT 10 ± 0.5 mM; D2O 10%; H2O 90%

NC5_sample: conjugate transposon protein BVU_1572(27-141), [U-5% 13C; U-100% 15N], 0.48 ± 0.05 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 mM; D2O 10%; H2O 90%

NC_sample_in_D2O: conjugate transposon protein BVU_1572(27-141), [U-100% 13C; U-100% 15N], 0.53 ± 0.05 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY-aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC-NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-13C HSQC-aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HNHA	NC5_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC 150ppm	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic 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 v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

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

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz
Varian INOVA 800 MHz