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Biological Magnetic Resonance Data Bank


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BMRB Entry 15462

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15462
MolProbity Validation Chart

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Title: Solution NMR Structure of HI0947 from Haemophilus influenzae, Northeast Structural Genomics Consortium Target IR123

Deposition date: 2007-09-09 Original release date: 2007-10-16

Authors: Ding, Keyang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ding, Keyang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR Structure of HI0947 from Haemophilus influenzae."  . ., .-..

Assembly members:
HI0947, polymer, 160 residues, 17510.121 Da.

Natural source:   Common Name: Haemophilus influenzae   Taxonomy ID: 727   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Haemophilus influenzae

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

Entity Sequences (FASTA):
HI0947: MAQHSKYSDAQLSAIVNDMI AVLEKHKAPVDLSLIALGNM ASNLLTTSVPQTQCEALAQA FSNSLINAVKTRLEHHHHHH MAQHSKYSDAQLSAIVNDMI AVLEKHKAPVDLSLIALGNM ASNLLTTSVPQTQCEALAQA FSNSLINAVKTRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts330
15N chemical shifts86
1H chemical shifts547

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 160 residues - 17510.121 Da.

The full sequence is cloned with his-tag LEHHHHHH added at the C terminal.

1   METALAGLNHISSERLYSTYRSERASPALA
2   GLNLEUSERALAILEVALASNASPMETILE
3   ALAVALLEUGLULYSHISLYSALAPROVAL
4   ASPLEUSERLEUILEALALEUGLYASNMET
5   ALASERASNLEULEUTHRTHRSERVALPRO
6   GLNTHRGLNCYSGLUALALEUALAGLNALA
7   PHESERASNSERLEUILEASNALAVALLYS
8   THRARGLEUGLUHISHISHISHISHISHIS
9   METALAGLNHISSERLYSTYRSERASPALA
10   GLNLEUSERALAILEVALASNASPMETILE
11   ALAVALLEUGLULYSHISLYSALAPROVAL
12   ASPLEUSERLEUILEALALEUGLYASNMET
13   ALASERASNLEULEUTHRTHRSERVALPRO
14   GLNTHRGLNCYSGLUALALEUALAGLNALA
15   PHESERASNSERLEUILEASNALAVALLYS
16   THRARGLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.66 mM; CaCl2 5 mM; NaCl 100 mM; NH4OAc 20 mM; DTT 10 mM; NaN3 0.02%; H2O 95%; D2O 5%

sample_2: protein, [U-100% 13C; U-100% 15N], 0.66 mM; CaCl2 5 mM; NaCl 100 mM; NH4OAc 20 mM; DTT 10 mM; NaN3 0.02%; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C Arom HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C Arom NOESYsample_1isotropicsample_conditions_1
4D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis

SPARKY v3.1, Goddard - peak picking

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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