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Biological Magnetic Resonance Data Bank


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BMRB Entry 17429

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17429
MolProbity Validation Chart

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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: 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"  Not known ., .-..

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts113
1H chemical shifts831

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CpcC1

Entities:

Entity 1, CpcC 143 residues - 16906.959 Da.

1   METPROVALGLULEUARGALAASNTRPSER
2   GLUGLUASPLEUGLUTHRVALILEARGALA
3   VALTYRARGGLNVALLEUGLYASNASPTYR
4   VALMETALASERGLUARGLEUVALSERALA
5   GLUSERLEULEUARGASNGLYLYSILETHR
6   VALARGGLUPHEVALARGALAVALALALYS
7   SERGLULEUTYRLYSGLULYSPHELEUTYR
8   GLYASNPHEGLNTHRARGVALILEGLULEU
9   ASNTYRLYSHISLEULEUGLYARGALAPRO
10   TYRASPGLUSERGLUVALILEPHEHISLEU
11   ASPLEUTYRGLUASNGLUGLYPHEASPALA
12   ASPILEASPSERTYRILEASPSERPROGLU
13   TYRTHRASNSERPHEGLYASPTRPVALVAL
14   PROTYRTYRARGGLYLEUGLUHISHISHIS
15   HISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY-aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY-aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC HisNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC 150ppmNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlyNC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_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

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts