BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 19654

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19654
MolProbity Validation Chart

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Title: NMR Structure of human Mcl-1   PubMed: 24789074

Deposition date: 2013-12-04 Original release date: 2014-05-12

Authors: Liu, Gaohua; Poppe, Leszek; Aoki, Ken; Yamane, Harvey; Lewis, Jeffrey; Szyperski, Thomas

Citation: Liu, Gaohua; Poppe, Leszek; Aoki, Ken; Yamane, Harvey; Lewis, Jeffrey; Szyperski, Thomas. "High-quality NMR Structure of Human Anti-apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design"  PLOS 9, e96521-e96521 (2014).

Assembly members:
entity, polymer, 328 residues, 37715.047 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):
entity: MEDELYRQSLEIISRYLREQ ATGAKDTKPMGRSGATSRKA LETLRRVGDGVQRNHETAFQ GMLRKLDIKNEDDVKSLSRV MIHVFSDGVTNWGRIVTLIS FGAFVAKHLKTINQESSIEP LAESITDVLVRTKRDWLVKQ RGWDGFVEFFHVEDLEGGHH HHHHMEDELYRQSLEIISRY LREQATGAKDTKPMGRSGAT SRKALETLRRVGDGVQRNHE TAFQGMLRKLDIKNEDDVKS LSRVMIHVFSDGVTNWGRIV TLISFGAFVAKHLKTINQES SIEPLAESITDVLVRTKRDW LVKQRGWDGFVEFFHVEDLE GGHHHHHH

Data sets:
Data typeCount
13C chemical shifts548
15N chemical shifts175
1H chemical shifts1153

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1human Mcl-11

Entities:

Entity 1, human Mcl-1 328 residues - 37715.047 Da.

1   METGLUASPGLULEUTYRARGGLNSERLEU
2   GLUILEILESERARGTYRLEUARGGLUGLN
3   ALATHRGLYALALYSASPTHRLYSPROMET
4   GLYARGSERGLYALATHRSERARGLYSALA
5   LEUGLUTHRLEUARGARGVALGLYASPGLY
6   VALGLNARGASNHISGLUTHRALAPHEGLN
7   GLYMETLEUARGLYSLEUASPILELYSASN
8   GLUASPASPVALLYSSERLEUSERARGVAL
9   METILEHISVALPHESERASPGLYVALTHR
10   ASNTRPGLYARGILEVALTHRLEUILESER
11   PHEGLYALAPHEVALALALYSHISLEULYS
12   THRILEASNGLNGLUSERSERILEGLUPRO
13   LEUALAGLUSERILETHRASPVALLEUVAL
14   ARGTHRLYSARGASPTRPLEUVALLYSGLN
15   ARGGLYTRPASPGLYPHEVALGLUPHEPHE
16   HISVALGLUASPLEUGLUGLYGLYHISHIS
17   HISHISHISHISMETGLUASPGLULEUTYR
18   ARGGLNSERLEUGLUILEILESERARGTYR
19   LEUARGGLUGLNALATHRGLYALALYSASP
20   THRLYSPROMETGLYARGSERGLYALATHR
21   SERARGLYSALALEUGLUTHRLEUARGARG
22   VALGLYASPGLYVALGLNARGASNHISGLU
23   THRALAPHEGLNGLYMETLEUARGLYSLEU
24   ASPILELYSASNGLUASPASPVALLYSSER
25   LEUSERARGVALMETILEHISVALPHESER
26   ASPGLYVALTHRASNTRPGLYARGILEVAL
27   THRLEUILESERPHEGLYALAPHEVALALA
28   LYSHISLEULYSTHRILEASNGLNGLUSER
29   SERILEGLUPROLEUALAGLUSERILETHR
30   ASPVALLEUVALARGTHRLYSARGASPTRP
31   LEUVALLYSGLNARGGLYTRPASPGLYPHE
32   VALGLUPHEPHEHISVALGLUASPLEUGLU
33   GLYGLYHISHISHISHISHISHIS

Samples:

sample_NC: mcl-1, [U-100% 13C; U-100% 15N], 0.7 mM

sample_NC5: mcl-1, [U-5% 13C; U-100% 15N], 0.7 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N/13Caliphatic/13Caromatic-resolved NOESYsample_NCisotropicsample_conditions_1
GFT(4,3)D HNNCabCasample_NCisotropicsample_conditions_1
GFT(4,3)DCabCacoNHNsample_NCisotropicsample_conditions_1
GFT(4,3)D HabCabcoNHNsample_NCisotropicsample_conditions_1
GFT(4,3)D HNNCOsample_NCisotropicsample_conditions_1
GFT (4,3)D HCCHsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_NCisotropicsample_conditions_1

Software:

VNMR, Varian - collection

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

XEASY, Bartels et al. - data analysis

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

SPSCAN, Glaser - processing

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • 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