BMRB Entry 17039

Name: Solution NMR Structure of putative cell surface protein MA_4588 (272-376 domain) from Methanosarcina acetivorans, Northeast Structural Genomics Consortium Target MvR254A
Published: 2012-08-02

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PDB ID: 2l0d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17039
MolProbity Validation Chart

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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 cell surface protein MA_4588 (272-376 domain) from Methanosarcina acetivorans, Northeast Structural Genomics Consortium Target MvR254A

Deposition date:

2010-06-30

Original release date:

2012-08-02

Authors:

Cort, John; Lee, D.; Ciccosanti, C.; Janjua, H.; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Ramelot, T.; Kennedy, M.

Citation:

Citation: Cort, John; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; KENNEDY, M.. "Northeast Structural Genomics Consortium Target MvR254A" To be published ., .-..

Assembly members:

Assembly members:
MvR254A, polymer, 114 residues, 12299.430 Da.

Natural source:

Natural source: Common Name: Methanosarcina acetivorans Taxonomy ID: 2214 Superkingdom: Archaea Kingdom: not available Genus/species: Methanosarcina acetivorans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MvR254A: MIPDLVPVSLTPVTVVPNTV NTMTATIENQGNKDSTSFNV SLLVDGIVVDTQTVTSLESE NSTNVDFHWTLDGTANSYTL TVNVDPENAVNEGNESNNTL TALVGTLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	458
15N chemical shifts	119
1H chemical shifts	736

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MvR254A	1

Entities:

Entity 1, MvR254A 114 residues - 12299.430 Da.

Residue 2 corresponds with residue 272 of the predicted protein

1

MET

ILE

PRO

ASP

LEU

VAL

PRO

VAL

SER

LEU

2

THR

PRO

VAL

THR

VAL

PRO

ASN

THR

VAL

3

ASN

THR

MET

THR

ALA

THR

ILE

GLU

ASN

GLN

4

GLY

ASN

LYS

ASP

SER

THR

SER

PHE

ASN

VAL

5

SER

LEU

VAL

ASP

GLY

ILE

VAL

ASP

6

THR

GLN

THR

VAL

THR

SER

LEU

GLU

SER

GLU

7

ASN

SER

THR

ASN

VAL

ASP

PHE

HIS

TRP

THR

8

LEU

ASP

GLY

THR

ALA

ASN

SER

TYR

THR

LEU

9

THR

VAL

ASN

VAL

ASP

PRO

GLU

ASN

ALA

VAL

10

ASN

GLU

GLY

ASN

GLU

SER

ASN

THR

LEU

11

THR

ALA

LEU

VAL

GLY

THR

LEU

GLU

HIS

12

HIS

Samples:

sample_1: MvR254A, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; H2O 95%; D2O 5%

sample_2: MvR254A, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; D2O 100%

sample_3: MvR254A, [5% biosynthetically-directed 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aliph NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
4D 1H-13C-13C-1H HMQC-NOESY-HMQC	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

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

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz