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 6475

Title: 1H, 13C and 15N Chemical Shift assignments for Man5C-CBM35 from C. japonicus   PubMed: 15740741

Deposition date: 2005-01-31 Original release date: 2006-11-13

Authors: Tunnicliffe, Richard; Williamson, Mike

Citation: Tunnicliffe, Richard; Bolam, David; Pell, Gavin; Gilbert, Harry; Williamson, Mike. "Structure of a Mannan-specific Family 35 Carbohydrate-Binding Module: Evidence for Significant Conformational Changes upon Ligand Binding"  J. Mol. Biol. 347, 287-296 (2005).

Assembly members:
Man5C-CBM35, polymer, 132 residues, 14933.7 Da.

Natural source:   Common Name: Cellvibrio japonicus   Taxonomy ID: 155077   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Cellvibrio Cellvibrio japonicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia Coli   Vector: pET22b

Entity Sequences (FASTA):
Man5C-CBM35: MAVPEGNSWTYTAASASITA PAQLVGNVGELQGAGSAVIW NVDVPVTGEYRINLTWSSPY SSKVNTLVMDGTALSYAFAE ATVPVTYVQTKTLSAGNHSF GVRVGSSDWGYMNVHSLKLE LLGGLTIRSPAN

Data sets:
Data typeCount
1H chemical shifts835
13C chemical shifts524
15N chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Man5C-CBM351

Entities:

Entity 1, Man5C-CBM35 132 residues - 14933.7 Da.

1   METALAVALPROGLUGLYASNSERTRPTHR
2   TYRTHRALAALASERALASERILETHRALA
3   PROALAGLNLEUVALGLYASNVALGLYGLU
4   LEUGLNGLYALAGLYSERALAVALILETRP
5   ASNVALASPVALPROVALTHRGLYGLUTYR
6   ARGILEASNLEUTHRTRPSERSERPROTYR
7   SERSERLYSVALASNTHRLEUVALMETASP
8   GLYTHRALALEUSERTYRALAPHEALAGLU
9   ALATHRVALPROVALTHRTYRVALGLNTHR
10   LYSTHRLEUSERALAGLYASNHISSERPHE
11   GLYVALARGVALGLYSERSERASPTRPGLY
12   TYRMETASNVALHISSERLEULYSLEUGLU
13   LEULEUGLYGLYLEUTHRILEARGSERPRO
14   ALAASN

Samples:

sample_1: Man5C-CBM35, [U-95% 13C; U-95% 15N], 1.0 mM; sodium phosphate 50 mM

conditions_1: pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
HSQC (15N and 13C)sample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
HN(CA)COsample_1not availableconditions_1
HN(CO)CAsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
HBHA(CBCACO)NHsample_1not availableconditions_1
CCH-TOCSYsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
15N,13C-edited NOESYsample_1not availableconditions_1

Software:

Felix v2000, Accelrys - Processing, analysis

NMR spectrometers:

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

Related Database Links:

PDB
GB AAO31761 ACE82655
REF WP_012489045 YP_001983923

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