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 4668

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4668

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Title: Assignment of 1H, 13C and 15N Resonances of FKBP from Methanococcus thermolithotrophicus

Deposition date: 2000-02-15 Original release date: 2004-10-25

Authors: Suzuki, Rintaro; Nagata, Koji; Kawakami, Masaru; Nemoto, Nobuaki; Furutani, Masahiro; Adachi, Kyoko; Maruyama, Tadashi; Tanokura, Masaru

Citation: Suzuki, Rintaro; Nagata, Koji; Kawakami, Masaru; Nemoto, Nobuaki; Furutani, Masahiro; Adachi, Kyoko; Maruyama, Tadashi; Tanokura, Masaru. "Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of FKBP from Methanococcus thermolithotrophicus"  J. Biomol. NMR 17, 183-184 (2000).

Assembly members:
FK506 binding protein from Methanococcus thermolithotrophicus, polymer, 151 residues, 16810.09 Da.

Natural source:   Common Name: Methanococcus thermolithotrophicus   Taxonomy ID: 2186   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus thermolithotrophicus

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

Entity Sequences (FASTA):
FK506 binding protein from Methanococcus thermolithotrophicus: MVDKGVKIKVDYIGKLESGD VFDTSIEEVAKEAGIYAPDR EYEPLEFVVGEGQLIQGFEE AVLDMEVGDEKTVKIPAEKA YGNRNEMLIQKIPRDAFKEA DFEPEEGMVILAEGIPATIT EVTDNEVTLDFNHELAGKDL VFTIKIIEVVE

Data sets:
Data typeCount
13C chemical shifts637
1H chemical shifts1029
15N chemical shifts151

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MTFK1

Entities:

Entity 1, MTFK 151 residues - 16810.09 Da.

1   METVALASPLYSGLYVALLYSILELYSVAL
2   ASPTYRILEGLYLYSLEUGLUSERGLYASP
3   VALPHEASPTHRSERILEGLUGLUVALALA
4   LYSGLUALAGLYILETYRALAPROASPARG
5   GLUTYRGLUPROLEUGLUPHEVALVALGLY
6   GLUGLYGLNLEUILEGLNGLYPHEGLUGLU
7   ALAVALLEUASPMETGLUVALGLYASPGLU
8   LYSTHRVALLYSILEPROALAGLULYSALA
9   TYRGLYASNARGASNGLUMETLEUILEGLN
10   LYSILEPROARGASPALAPHELYSGLUALA
11   ASPPHEGLUPROGLUGLUGLYMETVALILE
12   LEUALAGLUGLYILEPROALATHRILETHR
13   GLUVALTHRASPASNGLUVALTHRLEUASP
14   PHEASNHISGLULEUALAGLYLYSASPLEU
15   VALPHETHRILELYSILEILEGLUVALVAL
16   GLU

Samples:

sample_1: FK506 binding protein from Methanococcus thermolithotrophicus, [U-15N], 4.5 mM

sample_2: FK506 binding protein from Methanococcus thermolithotrophicus, [U-13C; U-15N], 8.0 mM

Ex-cond: pH*: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availablenot availableEx-cond
3D 1H-1H-15N NOESYnot availablenot availableEx-cond
3D 1H-1H-15N TOCSYnot availablenot availableEx-cond
3D HNCAnot availablenot availableEx-cond
3D HNCACBnot availablenot availableEx-cond
3D CBCA(CO)NHnot availablenot availableEx-cond
3D HNCOnot availablenot availableEx-cond
3D (HCA)CO(CA)NHnot availablenot availableEx-cond
3D H(CCO)NHnot availablenot availableEx-cond
3D C(CO)NHnot availablenot availableEx-cond
3D 1H-13C-1H DE-H(C)CH-TOCSYnot availablenot availableEx-cond

Software:

nmrPipe v1.7 -

P-ROI system v1.0 - spectral analysis on papers

SPARKY v3.76 -

CSI v1.0 -

TALOS v98.040.21.02 -

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAA24446
REF WP_018154854
SP O52980

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