BMRB Entry 17031

Name: Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C
Published: 2010-08-24

Click here to enlarge.

PDB ID: 2l06
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17031
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 PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C

Deposition date:

2010-06-30

Original release date:

2010-08-24

Authors:

Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C" .

Assembly members:

Assembly members:
SLR0335, polymer, 155 residues, 17840 Da.

Natural source:

Natural source: Common Name: Synechocystis sp. Taxonomy ID: 1143 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SLR0335: PQSYFNAAAKRQKYAMKPGL SALEKNAVIKAAYRQIFERD ITKAYSQSISYLESQVRNGD ISMKEFVRRLAKSPLYRKQF FEPFINSRALELAFRHILGR GPSSREEVQKYFSIVSSGGL PALVDALVDSQEYADYFGEE TVPYLRGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	652
15N chemical shifts	156
1H chemical shifts	1025

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SLR0335	1

Entities:

Entity 1, SLR0335 155 residues - 17840 Da.

1

PRO

GLN

SER

TYR

PHE

ASN

ALA

LYS

2

ARG

GLN

LYS

TYR

ALA

MET

LYS

PRO

GLY

LEU

3

SER

ALA

LEU

GLU

LYS

ASN

ALA

VAL

ILE

LYS

4

ALA

TYR

ARG

GLN

ILE

PHE

GLU

ARG

ASP

5

ILE

THR

LYS

ALA

TYR

SER

GLN

SER

ILE

SER

6

TYR

LEU

GLU

SER

GLN

VAL

ARG

ASN

GLY

ASP

7

ILE

SER

MET

LYS

GLU

PHE

VAL

ARG

LEU

8

ALA

LYS

SER

PRO

LEU

TYR

ARG

LYS

GLN

PHE

9

PHE

GLU

PRO

PHE

ILE

ASN

SER

ARG

ALA

LEU

10

GLU

LEU

ALA

PHE

ARG

HIS

ILE

LEU

GLY

ARG

11

GLY

PRO

SER

ARG

GLU

VAL

GLN

LYS

12

TYR

PHE

SER

ILE

VAL

SER

GLY

LEU

13

PRO

ALA

LEU

VAL

ASP

ALA

LEU

VAL

ASP

SER

14

GLN

GLU

TYR

ALA

ASP

TYR

PHE

GLY

GLU

15

THR

VAL

PRO

TYR

LEU

ARG

GLY

LEU

GLU

HIS

16

HIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%

NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1.2 ± .05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; 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	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
4D 1H-13C NOESY	NC_sample_in_D2O	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 (H)CC(CO)NH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
3D H(CC)(CO)NH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY arom	NC_sample	isotropic	sample_conditions_1
(H)CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe vlinux9, 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

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Bruker AvanceIII 850 MHz
Varian INOVA 500 MHz
Varian INOVA 750 MHz