BMRB Entry 5181

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5181
MolProbity Validation Chart

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Title:
Virtually complete 1H, 13C and 15N resonance assignments of the second family 4 xylan binding module of Rhodothermus marinus xylanase 10A
Deposition date:
2001-10-16
Original release date:
2002-05-07
Authors:
Jamieson, Stuart; Williamson, Michael; Abou-Hachem, Maher; Nordberg Karlsson, Eva; Simpson, Peter
Citation:

Citation: Jamieson, Stuart; Williamson, Michael; Abou-Hachem, Maher; Nordberg, K.; Simpson, Peter. "Letter to the Editor: Virtually Complete 1H, 13C and 15N Resonance Assignments of the Second Family 4 Xylan Binding Module of Rhodothermus marinus xylanase 10A"  J. Biomol. NMR 22, 187-188 (2002).
PubMed: 11883782

Assembly members:

Assembly members:
cbm4-2, polymer, 168 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rhodothermus marinus   Taxonomy ID: 29549   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Rhodothermus marinus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-25b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cbm4-2: MLVANINGGFESTPAGVVTD LAEGVEGWDLNVGSSVTNPP VFEVLETSDAPEGNKVLAVT VNGVGNNPWDIEATAFPVNV RPGVTYTYTIWARAEQDGAV VSFTVGNQSFQEYGRLHEQQ ITTEWQPFTFEFTVSDQETV IRAPIHFGYAANVGNTIYID GLAIASQP

Data sets:
Data typeCount
1H chemical shifts1128
13C chemical shifts712
15N chemical shifts183

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1cbm4-21

Entities:

Entity 1, cbm4-2 168 residues - Formula weight is not available

1   METLEUVALALAASNILEASNGLYGLYPHE
2   GLUSERTHRPROALAGLYVALVALTHRASP
3   LEUALAGLUGLYVALGLUGLYTRPASPLEU
4   ASNVALGLYSERSERVALTHRASNPROPRO
5   VALPHEGLUVALLEUGLUTHRSERASPALA
6   PROGLUGLYASNLYSVALLEUALAVALTHR
7   VALASNGLYVALGLYASNASNPROTRPASP
8   ILEGLUALATHRALAPHEPROVALASNVAL
9   ARGPROGLYVALTHRTYRTHRTYRTHRILE
10   TRPALAARGALAGLUGLNASPGLYALAVAL
11   VALSERPHETHRVALGLYASNGLNSERPHE
12   GLNGLUTYRGLYARGLEUHISGLUGLNGLN
13   ILETHRTHRGLUTRPGLNPROPHETHRPHE
14   GLUPHETHRVALSERASPGLNGLUTHRVAL
15   ILEARGALAPROILEHISPHEGLYTYRALA
16   ALAASNVALGLYASNTHRILETYRILEASP
17   GLYLEUALAILEALASERGLNPRO

Samples:

sample_1: cbm4-2, [U-13C; U-15N], 1.5 mM; CaCl2 50 mM; sodium acetate, [U-2H], 50 mM; sodium azide 10 mM; TSP 0.1 mM

conditions_1: pH: 6.0; temperature: 313 K; ionic strength: 0.2 M

Experiments:

NameSampleSample stateSample conditions
HNHAnot availablenot availablenot available
HSQCnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HNCOnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available
CCH-TOCSYnot availablenot availablenot available
HB(CBCGCD)HDnot availablenot availablenot available
2D-NOESYnot availablenot availablenot available
13C-15N NOESYnot availablenot availablenot available
3D 15N-dispersed TOCSYnot availablenot availablenot available
3D 15N-dispersed NOESYnot availablenot availablenot available

Software:

FELIX v2000 - processing, analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AAR06926 AAT07003 AAT07004 AAT07006 AAT07022

Download HSQC peak lists in one of the following formats:
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