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 18156

Title: Solution NMR Structure of the mitochondrial inner membrane domain (residues 164-251), FtsH_ext, from the paraplegin-like protein AFGL32 from Homo sapiens, Northeast Structural Genomics Consortium Target HR6741A

Authors: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Janua, Haleema; Kohan, Eitan; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Janua, Haleema; Kohan, Eitan; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael. "Northeast Structural Genomics Consortium Target HR6741A"  To be published ., .-..

Assembly members:
HR6741A, polymer, 99 residues, 11999.1 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):
HR6741A: MGHHHHHHSHMKRSGREITW KDFVNNYLSKGVVDRLEVVN KRFVRVTFTPGKTPVDGQYV WFNIGSVDTFERNLETLQQE LGIEGENRVPVVYIAESDG

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts101
1H chemical shifts657

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR6741A1

Entities:

Entity 1, HR6741A 99 residues - 11999.1 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METLYSARGSERGLYARGGLUILETHRTRP
3   LYSASPPHEVALASNASNTYRLEUSERLYS
4   GLYVALVALASPARGLEUGLUVALVALASN
5   LYSARGPHEVALARGVALTHRPHETHRPRO
6   GLYLYSTHRPROVALASPGLYGLNTYRVAL
7   TRPPHEASNILEGLYSERVALASPTHRPHE
8   GLUARGASNLEUGLUTHRLEUGLNGLNGLU
9   LEUGLYILEGLUGLYGLUASNARGVALPRO
10   VALVALTYRILEALAGLUSERASPGLY

Samples:

HR6741.001: HR6741A, [U-100% 13C; U-100% 15N], 0.7 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; H2O 90%; D2O 10%

HR6741.002: HR6741A, NC5, 1.0 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; H2O 90%; D2O 10%

HR6741.001_D2O: HR6741A, [U-100% 13C; U-100% 15N], 0.7 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; D2O 100%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR6741.001isotropicsample_conditions_1
2D 1H-13C HSQCHR6741.001isotropicsample_conditions_1
3D HNCOHR6741.001isotropicsample_conditions_1
3D CBCA(CO)NHHR6741.001isotropicsample_conditions_1
3D HNCACBHR6741.001isotropicsample_conditions_1
3D 1H-13C arom NOESYHR6741.001isotropicsample_conditions_1
3D 1H-13C NOESYaliphHR6741.001isotropicsample_conditions_1
3D 1H-15N NOESYHR6741.001isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHR6741.002isotropicsample_conditions_1
2D 1H-15N hetNOEHR6741.002isotropicsample_conditions_1
3D HN(CO)CAHR6741.001isotropicsample_conditions_1
3D HCCH-TOCSYHR6741.001isotropicsample_conditions_1
3D HCCH-COSYHR6741.001isotropicsample_conditions_1
3D H(CCO)NHHR6741.001isotropicsample_conditions_1
3D C(CO)NHHR6741.001isotropicsample_conditions_1
3D HBHA(CO)NHHR6741.001isotropicsample_conditions_1
4D CC-HMQC-NOESY-HMQCHR6741.001_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCHR6741.001_D2Oisotropicsample_conditions_1
3D CCH-TOCSYHR6741.001_D2Oisotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

NMRPipe v2008 linux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1.4 and 3.1, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.113, Goddard - data analysis

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES v2000, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure determination

NMR spectrometers:

  • Bruker AvanceIII 850 MHz
  • Varian INOVA 600 MHz
  • Bruker AvanceIII 600 MHz

Related Database Links:

PDB
DBJ BAE29204 BAE30959 BAE31449
EMBL CAB48398
GB AAH24282 AAH36999 AAH43056 AAH65016 AAI05323
REF NP_001039676 NP_001128336 NP_006787 NP_081406 XP_001094146
SP Q2KJI7 Q8JZQ2 Q9Y4W6
TPG DAA15802