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Biological Magnetic Resonance Data Bank


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BMRB Entry 15718

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15718
MolProbity Validation Chart

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Title: Solution Structure of the inner DysF domain of human myoferlin   PubMed: 18495154

Deposition date: 2008-04-07 Original release date: 2008-06-30

Authors: Patel, Pryank; Harris, Richard; Keep, Nicholas; Driscoll, Paul

Citation: Patel, Pryank; Harris, Richard; Geddes, Stella; Strehle, Eugen-Matthias; Watson, James; Bashir, Rumaisa; Bushby, Katherine; Driscoll, Paul; Keep, Nicholas. "Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b"  J. Mol. Biol. 379, 981-990 (2008).

Assembly members:
DysF, polymer, 123 residues, 14195.573 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
DysF: IDPFTADAGHTEFTDEVYQN ESRYPGGDWKPAEDTYTDAN GDKAASPSELTCPPGWEWED DAWSYDINRAVDEKGWEYGI TIPPDHKPKSWVAAEKMYHT HRRRRLVRKRKKDLTQTASS TAR

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts132
1H chemical shifts821

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1DysF1

Entities:

Entity 1, DysF 123 residues - 14195.573 Da.

Residues 1-5 represent part of a non-native affinity tag.

1   ILEASPPROPHETHRALAASPALAGLYHIS
2   THRGLUPHETHRASPGLUVALTYRGLNASN
3   GLUSERARGTYRPROGLYGLYASPTRPLYS
4   PROALAGLUASPTHRTYRTHRASPALAASN
5   GLYASPLYSALAALASERPROSERGLULEU
6   THRCYSPROPROGLYTRPGLUTRPGLUASP
7   ASPALATRPSERTYRASPILEASNARGALA
8   VALASPGLULYSGLYTRPGLUTYRGLYILE
9   THRILEPROPROASPHISLYSPROLYSSER
10   TRPVALALAALAGLULYSMETTYRHISTHR
11   HISARGARGARGARGLEUVALARGLYSARG
12   LYSLYSASPLEUTHRGLNTHRALASERSER
13   THRALAARG

Samples:

15N_DysF: DysF, [U-100% 15N], 1.3 mM; MES 20 mM; sodium chloride 100 mM; D2O 10%; H2O 90%

15N_13C_DysF: DysF, [U-100% 13C; U-100% 15N], 1.3 mM; MES 20 mM; sodium chloride 100 mM; D2O 10%; H2O 90%

15N_13C_DysF_in_D2O: DysF, [U-100% 13C; U-100% 15N], 1.3 mM; MES 20 mM; sodium chloride 100 mM; D2O 100%

Standard_Conditions: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_DysFisotropicStandard_Conditions
2D 1H-15N HSQC15N_13C_DysFisotropicStandard_Conditions
2D 1H-15N HSQC15N_13C_DysF_in_D2OisotropicStandard_Conditions
3D 1H-15N NOESY15N_DysFisotropicStandard_Conditions
3D 1H-15N TOCSY15N_DysFisotropicStandard_Conditions
3D HNCA15N_13C_DysFisotropicStandard_Conditions
3D HN(CO)CA15N_13C_DysFisotropicStandard_Conditions
3D HNCACB15N_13C_DysFisotropicStandard_Conditions
3D CBCA(CO)NH15N_13C_DysFisotropicStandard_Conditions
3D HNCO15N_13C_DysFisotropicStandard_Conditions
3D HN(CA)CO15N_13C_DysFisotropicStandard_Conditions
3D HA(CA)NH15N_13C_DysFisotropicStandard_Conditions
3D HA(CACO)NH15N_13C_DysFisotropicStandard_Conditions
2D 1H-13C HSQC15N_13C_DysF_in_D2OisotropicStandard_Conditions
aro-HSQC15N_13C_DysF_in_D2OisotropicStandard_Conditions
aro-TOCSY-HSQC15N_13C_DysF_in_D2OisotropicStandard_Conditions
aro-NOESY-HSQC15N_13C_DysF_in_D2OisotropicStandard_Conditions
3D HCCH-TOCSY15N_13C_DysF_in_D2OisotropicStandard_Conditions
3D 1H-13C NOESY15N_13C_DysF_in_D2OisotropicStandard_Conditions
IPAP15N_DysFisotropicStandard_Conditions
IPAP15N_DysFanisotropicStandard_Conditions

Software:

CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - Protein Dihedral Angle Backbone Prediction

ProcheckNMR, Laskowski and MacArthur - data analysis

CNSSOLVE v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Varian UnityPlus 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA86521 BAG10438
EMBL CAB46370
GB AAF27176 AAF27177 AAG23737 AAH52617 AIC59956
REF NP_038479 NP_579899 XP_001089235 XP_002756458 XP_003255276
SP Q9NZM1

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