BMRB Entry 16934

Name: Solution NMR structure of the PBS linker domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E
Published: 2010-07-08

Click here to enlarge.

PDB ID: 2ky4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16934
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 domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E

Deposition date:

2010-05-14

Original release date:

2010-07-08

Authors:

He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the PBS linker domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E" .

Assembly members:

Assembly members:
PBS, polymer, 149 residues, 17254.771 Da.

Natural source:

Natural source: Common Name: Anabaena sp. Taxonomy ID: 1167 Superkingdom: Bacteria Kingdom: not available Genus/species: Anabaena Anabaena sp.

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PBS: MKVFKRVAGIKDKAAIKTLI SAAYRQIFERDIAPYIAQNE FSGWESKLGNGEITVKEFIE GLGYSNLYLKEFYTPYPNTK VIELGTKHFLGRAPIDQAEI RKYNQILATQGIRAFINALV NSQEYNEVFGEDTVPYRRFP TLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	671
15N chemical shifts	156
1H chemical shifts	1078

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PBS	1

Entities:

Entity 1, PBS 149 residues - 17254.771 Da.

1

MET

LYS

VAL

PHE

LYS

ARG

VAL

ALA

GLY

ILE

2

LYS

ASP

LYS

ALA

ILE

LYS

THR

LEU

ILE

3

SER

ALA

TYR

ARG

GLN

ILE

PHE

GLU

ARG

4

ASP

ILE

ALA

PRO

TYR

ILE

ALA

GLN

ASN

GLU

5

PHE

SER

GLY

TRP

GLU

SER

LYS

LEU

GLY

ASN

6

GLY

GLU

ILE

THR

VAL

LYS

GLU

PHE

ILE

GLU

7

GLY

LEU

GLY

TYR

SER

ASN

LEU

TYR

LEU

LYS

8

GLU

PHE

TYR

THR

PRO

TYR

PRO

ASN

THR

LYS

9

VAL

ILE

GLU

LEU

GLY

THR

LYS

HIS

PHE

LEU

10

GLY

ARG

ALA

PRO

ILE

ASP

GLN

ALA

GLU

ILE

11

ARG

LYS

TYR

ASN

GLN

ILE

LEU

ALA

THR

GLN

12

GLY

ILE

ARG

ALA

PHE

ILE

ASN

ALA

LEU

VAL

13

ASN

SER

GLN

GLU

TYR

ASN

GLU

VAL

PHE

GLY

14

GLU

ASP

THR

VAL

PRO

TYR

ARG

PHE

PRO

15

THR

LEU

GLU

HIS

Samples:

sample_4: entity, [U-5% 13C; U-100% 15N], 0.851 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; poly acrylamide gel 7%; H2O 83%; D2O 17%

sample_1: entity, [U-100% 13C; U-100% 15N], 0.95 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-100% 15N], 0.975 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_3: entity, [U-5% 13C; U-100% 15N], 0.664 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; poly ethylene glycol 4%; H2O 82%; D2O 18%

sample_conditions_1: ionic strength: 117.5 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC ali	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aro	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC (methyl)	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY ali	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY aro	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
13C/15N-NOESY	sample_1	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	sample_3	anisotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	sample_4	anisotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

NMRPipe v2007.030.16.06, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PROSA v6.4, Guntert - processing

XEASY, Bartels et al. - data analysis

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

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

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

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

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

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - validation

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

Molmol, Koradi, Billeter and Wuthrich - refinement

TOPSPIN v2.1, Bruker Biospin - data analysis

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz
Bruker Avance 900 MHz