BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16498

Title: Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A.

Authors: Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A."  Not known ., .-..

Assembly members:
QlR8A, polymer, 108 residues, 13000 Da.

Natural source:   Common Name: Clostridium leptum   Taxonomy ID: 1535   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium leptum

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

Entity Sequences (FASTA):
QlR8A: RDSFGDWAEKFLKSKEADGV SVSQLNSYKNYCRNHLSPLY MKSLSEILPADIQSIINETK LAKNTLKAIRNTASQIFRLA IENRAIDFNPADYVRIPKIA LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts113
1H chemical shifts746

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1QlR8A1

Entities:

Entity 1, QlR8A 108 residues - 13000 Da.

8 non-native residues at C-terminus (LEHHHHHH)

1   ARGASPSERPHEGLYASPTRPALAGLULYS
2   PHELEULYSSERLYSGLUALAASPGLYVAL
3   SERVALSERGLNLEUASNSERTYRLYSASN
4   TYRCYSARGASNHISLEUSERPROLEUTYR
5   METLYSSERLEUSERGLUILELEUPROALA
6   ASPILEGLNSERILEILEASNGLUTHRLYS
7   LEUALALYSASNTHRLEULYSALAILEARG
8   ASNTHRALASERGLNILEPHEARGLEUALA
9   ILEGLUASNARGALAILEASPPHEASNPRO
10   ALAASPTYRVALARGILEPROLYSILEALA
11   LEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sampleisotropicsample_conditions_1
4D HCCH NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC edHN2NC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC swNNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC arom ctNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC arom no ctNC_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 v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, 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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
GB EDO61441
REF WP_003530379