BMRB Entry 15317

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PDB ID: 2jr2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15317
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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:

NMR Solution Structure of Colwellia psychrerythraea protein CPS_2611. Northeast Structural Genomics target CsR4.

Deposition date:

2007-06-19

Original release date:

2007-08-15

Authors:

Ramelot, Theresa; Cort, John; Wang, Huang; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Cort, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of Colwellia psychrerythraea protein CPS_2611. Northeast Structural Genomics target CsR4." .

Assembly members:

Assembly members:
protein, polymer, 76 residues, 17170 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 28229 Superkingdom: Bacteria Kingdom: not available Genus/species: Colwellia psychrerythraea

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein: MPIVSKYSNERVEKIIQDLL DVLVKEEVTPDLALMCLGNA VTNIIAQVPESKRVAVVDNF TKALKQSVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	336
15N chemical shifts	80
1H chemical shifts	556

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1
2	subunit 2	1

Entities:

Entity 1, subunit 1 76 residues - 17170 Da.

8 non-native residues C-terminal His tag (LEHHHHHH)

1

MET

PRO

ILE

VAL

SER

LYS

TYR

SER

ASN

GLU

2

ARG

VAL

GLU

LYS

ILE

GLN

ASP

LEU

3

ASP

VAL

LEU

VAL

LYS

GLU

VAL

THR

PRO

4

ASP

LEU

ALA

LEU

MET

CYS

LEU

GLY

ASN

ALA

5

VAL

THR

ASN

ILE

ALA

GLN

VAL

PRO

GLU

6

SER

LYS

ARG

VAL

ALA

VAL

ASP

ASN

PHE

7

THR

LYS

ALA

LEU

LYS

GLN

SER

VAL

LEU

GLU

8

HIS

Samples:

NC_sample: protein, [U-13C; U-15N], 1 ± 0.1 mM; sodium chloride 100 ± 5 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; calcium chloride 5 ± 0.25 mM

NC5_sample: protein, [U-5% 13C; U-100% 15N], 1.1 ± 0.1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %

NC_in_D2O: protein, [U-13C; U-15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %

NC50_sample_in_D2O: protein, [U-13C; U-15N], 0.5 ± 0.05 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; protein 0.5 ± 0.05 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; 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 (aliph)	NC_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliph	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
4D 1H-13C NOESY	NC_in_D2O	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNHA	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 HNCO	NC_sample	isotropic	sample_conditions_1
3D C(CO)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
2D 1H-13C HSQC	NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC (15 min)	NC_in_D2O	isotropic	sample_conditions_1
3D edited filtered 1H-13C NOESY	NC50_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-13C NOESY arom	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC (arom ct)	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC (arom no ct)	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC (30 min)	NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC (1 hr)	NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC (6 days)	NC_in_D2O	isotropic	sample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2JR2 2OTA
GB	AAZ26870
REF	WP_011043419
SP	Q481E4
AlphaFold	Q481E4