BMRB Entry 16810

Name: Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A
Published: 2010-04-28

Click here to enlarge.

PDB ID: 2kw7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16810
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A

Deposition date:

2010-03-31

Original release date:

2010-04-28

Authors:

Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A" To be published ., .-..

Assembly members:

Assembly members:
PgR37A, polymer, 157 residues, 17546.934 Da.

Natural source:

Natural source: Common Name: Porphyromonas gingivalis Taxonomy ID: 837 Superkingdom: Bacteria Kingdom: not available Genus/species: Porphyromonas gingivalis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PgR37A: MRVYKPEDVPNVQLADSTRL VTDEAGLLSNAQEEVMNGRL RAIRSSHAVEFAVVTLPSIG DAPLEDFTLKLARQWGVGNE KNNNGLLLVLVLDQRRVRFE TGYGLEGYLPDGLLSRIIHD RMIPHFRSGNYAEGLSEGVL AVQQVLDGSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	667
15N chemical shifts	169
1H chemical shifts	1101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PgR37A	1

Entities:

Entity 1, PgR37A 157 residues - 17546.934 Da.

1

MET

ARG

VAL

TYR

LYS

PRO

GLU

ASP

VAL

PRO

2

ASN

VAL

GLN

LEU

ALA

ASP

SER

THR

ARG

LEU

3

VAL

THR

ASP

GLU

ALA

GLY

LEU

SER

ASN

4

ALA

GLN

GLU

VAL

MET

ASN

GLY

ARG

LEU

5

ARG

ALA

ILE

ARG

SER

HIS

ALA

VAL

GLU

6

PHE

ALA

VAL

THR

LEU

PRO

SER

ILE

GLY

7

ASP

ALA

PRO

LEU

GLU

ASP

PHE

THR

LEU

LYS

8

LEU

ALA

ARG

GLN

TRP

GLY

VAL

GLY

ASN

GLU

9

LYS

ASN

GLY

LEU

VAL

LEU

10

VAL

LEU

ASP

GLN

ARG

VAL

ARG

PHE

GLU

11

THR

GLY

TYR

GLY

LEU

GLU

GLY

TYR

LEU

PRO

12

ASP

GLY

LEU

SER

ARG

ILE

HIS

ASP

13

ARG

MET

ILE

PRO

HIS

PHE

ARG

SER

GLY

ASN

14

TYR

ALA

GLU

GLY

LEU

SER

GLU

GLY

VAL

LEU

15

ALA

VAL

GLN

VAL

LEU

ASP

GLY

SER

LEU

16

GLU

HIS

Samples:

NC_sample: PgR37A, [U-100% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%

NC5_sample: PgR37A, [U-5% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_conditions_1: 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 aliphatic	NC_sample	isotropic	sample_conditions_1
3D HNCO	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 simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY aliphatic	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
2D long-range 1H-15N HSQC for histidine	NC_sample	isotropic	sample_conditions_1
3D HN(CA)CO	NC_sample	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation

AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, processing

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 900 MHz
Varian INOVA 750 MHz

PDB	2KW7
DBJ	BAG34119 BAK25626 GAP82223
GB	AAQ65571 AIJ36374 AKV64744 ALA94086 ALJ26010
REF	WP_005873820 WP_012458397 WP_013816169 WP_039417602 WP_043894154