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 6829

Title: Chemical shift assignments for Chitin-binding Domain of Hyperthermophilic Chitinase from Pyrococcus furiosus   PubMed: 17016669

Deposition date: 2005-09-20 Original release date: 2006-10-17

Authors: Uegaki, Koichi; Ikegami, Takahisa

Citation: Mine, Shouhei; Nakamura, Tsutomu; Hagihara, Yoshihisa; Ishikawa, Kazuhiko; Ikegami, Takahisa; Uegaki, Koichi. "NMR assignment of the chitin-binding domain of a hyperthermophilic chitinase from Pyrococcus furiosus"  J. Biomol. NMR 36, 70-70 (2006).

Assembly members:
Chitin binding domain, polymer, 103 residues, 10957 Da.

Natural source:   Common Name: Pyrococcus furiosus   Taxonomy ID: 2261   Superkingdom: Archaea   Kingdom: Not applicable   Genus/species: Pyrococcus furiosus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Chitin binding domain: GPTTPVPVSGSLEVKVNDWG SGAEYDVTLNLDGQYDWTVK VKLAPGATVGSFWSANKQEG NGYVIFTPVSWNKGPTATFG FIVNGPQGDKVEEITLEING QVI

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts109
1H chemical shifts671

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Chitin binding domain1

Entities:

Entity 1, Chitin binding domain 103 residues - 10957 Da.

1   GLYPROTHRTHRPROVALPROVALSERGLY
2   SERLEUGLUVALLYSVALASNASPTRPGLY
3   SERGLYALAGLUTYRASPVALTHRLEUASN
4   LEUASPGLYGLNTYRASPTRPTHRVALLYS
5   VALLYSLEUALAPROGLYALATHRVALGLY
6   SERPHETRPSERALAASNLYSGLNGLUGLY
7   ASNGLYTYRVALILEPHETHRPROVALSER
8   TRPASNLYSGLYPROTHRALATHRPHEGLY
9   PHEILEVALASNGLYPROGLNGLYASPLYS
10   VALGLUGLUILETHRLEUGLUILEASNGLY
11   GLNVALILE

Samples:

sample_1: Chitin binding domain, [U-95% 13C; U-95% 15N], 1.8 ± 0.2 mM; KH2PO4 / K2HPO4 20 mM; NaCl 25 mM

sample_2: Chitin binding domain, [U-10% 13C], 1.8 ± 0.2 mM; KH2PO4 / K2HPO4 20 mM; NaCl 25 mM

conditions_1: pD: 5.7; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCnot availablenot availableconditions_1
Homonuclear TOCSYnot availablenot availableconditions_1
Homonuclear NOESYnot availablenot availableconditions_1
1H-13C CT-HSQCnot availablenot availableconditions_1
CBCACOHNnot availablenot availableconditions_1
CBCANHnot availablenot availableconditions_1
HNCOnot availablenot availableconditions_1
HNCACOnot availablenot availableconditions_1
CCONHnot availablenot availableconditions_1
HCCONHnot availablenot availableconditions_1
HBHACONHnot availablenot availableconditions_1
HCCH-TOCSYnot availablenot availableconditions_1
(HB)CB(CGCD)HDnot availablenot availableconditions_1
(HB)CB(CGCDCE)HEnot availablenot availableconditions_1
1H-15N NOESY-HSQCnot availablenot availableconditions_1
1H-13C NOESY-HSQCnot availablenot availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Bruker DRX 400 MHz
  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB AAL81357 AFN04020
REF NP_578962 WP_011012376 YP_006492312

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