BMRB Entry 17429

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PDB ID: 2l8v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17429
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A

Deposition date:

2011-01-26

Original release date:

2011-02-11

Authors:

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

Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A" .

Assembly members:

Assembly members:
CpcC, polymer, 143 residues, 16906.959 Da.

Natural source:

Natural source: Common Name: Thermosynechococcus elongatus Taxonomy ID: 146786 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermosynechococcus elongatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CpcC: MPVELRANWSEEDLETVIRA VYRQVLGNDYVMASERLVSA ESLLRNGKITVREFVRAVAK SELYKEKFLYGNFQTRVIEL NYKHLLGRAPYDESEVIFHL DLYENEGFDADIDSYIDSPE YTNSFGDWVVPYYRGLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	522
15N chemical shifts	113
1H chemical shifts	831

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CpcC	1

Entities:

Entity 1, CpcC 143 residues - 16906.959 Da.

1

MET

PRO

VAL

GLU

LEU

ARG

ALA

ASN

TRP

SER

2

GLU

ASP

LEU

GLU

THR

VAL

ILE

ARG

ALA

3

VAL

TYR

ARG

GLN

VAL

LEU

GLY

ASN

ASP

TYR

4

VAL

MET

ALA

SER

GLU

ARG

LEU

VAL

SER

ALA

5

GLU

SER

LEU

ARG

ASN

GLY

LYS

ILE

THR

6

VAL

ARG

GLU

PHE

VAL

ARG

ALA

VAL

ALA

LYS

7

SER

GLU

LEU

TYR

LYS

GLU

LYS

PHE

LEU

TYR

8

GLY

ASN

PHE

GLN

THR

ARG

VAL

ILE

GLU

LEU

9

ASN

TYR

LYS

HIS

LEU

GLY

ARG

ALA

PRO

10

TYR

ASP

GLU

SER

GLU

VAL

ILE

PHE

HIS

LEU

11

ASP

LEU

TYR

GLU

ASN

GLU

GLY

PHE

ASP

ALA

12

ASP

ILE

ASP

SER

TYR

ILE

ASP

SER

PRO

GLU

13

TYR

THR

ASN

SER

PHE

GLY

ASP

TRP

VAL

14

PRO

TYR

ARG

GLY

LEU

GLU

HIS

15

HIS

Samples:

NC_sample: protein, [U-100% 13C; U-100% 15N], 1.3 ± 0.1 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 5 ± 0.5 mM

NC5_sample: protein, [U-5% 13C; U-100% 15N], 1.3 ± 0.1 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 5 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

NC_sample_in_D2O: protein, [U-100% 13C; U-100% 15N], 1.3 ± 0.1 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; 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
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY-aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CCO)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
3D CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC-NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-13C NOESY-aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC His	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC 150ppm	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, 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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance III 850 MHz