BMRB Entry 17090

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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/BMR17090
MolProbity Validation Chart

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Title:
Solution NMR structure of the protein YP_399305.1
Deposition date:
2010-07-30
Original release date:
2010-08-18
Authors:
Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt
Citation:

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt. "Solution NMR structure of the protein YP_399305.1"  .

Assembly members:

Assembly members:
entity, polymer, 120 residues, 13856.833 Da.

Natural source:

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 32046   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechococcus elongatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGITITDELLWAILKDELSD AEANALVWQALGYVWDEAQS CWKTDLVAPEWRQDYPEPPD FIASRPATVKLTRSIPAPYK QLLKEELGFAGYSINELVPR KTRRATMTNWLLAYRRSQQD

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts130
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_399305.11

Entities:

Entity 1, YP_399305.1 120 residues - 13856.833 Da.

1   METGLYILETHRILETHRASPGLULEULEU
2   TRPALAILELEULYSASPGLULEUSERASP
3   ALAGLUALAASNALALEUVALTRPGLNALA
4   LEUGLYTYRVALTRPASPGLUALAGLNSER
5   CYSTRPLYSTHRASPLEUVALALAPROGLU
6   TRPARGGLNASPTYRPROGLUPROPROASP
7   PHEILEALASERARGPROALATHRVALLYS
8   LEUTHRARGSERILEPROALAPROTYRLYS
9   GLNLEULEULYSGLUGLULEUGLYPHEALA
10   GLYTYRSERILEASNGLULEUVALPROARG
11   LYSTHRARGARGALATHRMETTHRASNTRP
12   LEULEUALATYRARGARGSERGLNGLNASP

Samples:

sample_1: YP_399305.1, [U-98% 13C; U-98% 15N], 1.1 mM; H2O 95%; D2O 5%; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Cali Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Caro Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol v2K.1, Koradi, Billeter and Wuthrich - Analysis and display of molecules

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - collection, processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

UNIO v2.0.0, (UNIO)-Torsten Herrmann - peak picking, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAD79416
GB ABB56318 AJD56633
REF WP_011243538

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks