BMRB Entry 16895

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16895
MolProbity Validation Chart

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Title:
The solution structure of UBB+1, frameshift mutant of ubiquitin B
Deposition date:
2010-04-22
Original release date:
2011-05-02
Authors:
Lee, Weontae; Ko, Sunggeon
Citation:

Citation: Lee, Weontae; Ko, Sunggeon. "Null"  To be Published ., .-..

Assembly members:

Assembly members:
UBB+1, polymer, 103 residues, 11539.073 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBB+1: GSLVPRGSMQIFVKTLTGKT ITLEVEPSDTIENVKAKIQD KEGIPPDQQRLIFAGKQLED GRTLSEYNIQKESTLHLVLR LRGYADLREDPDRQDHHPGS GAQ

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts93
1H chemical shifts644

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBB+11

Entities:

Entity 1, UBB+1 103 residues - 11539.073 Da.

Sequences "GSLVPRGS" were expressed from pGEX 4T-1 vector.

1   GLYSERLEUVALPROARGGLYSERMETGLN
2   ILEPHEVALLYSTHRLEUTHRGLYLYSTHR
3   ILETHRLEUGLUVALGLUPROSERASPTHR
4   ILEGLUASNVALLYSALALYSILEGLNASP
5   LYSGLUGLYILEPROPROASPGLNGLNARG
6   LEUILEPHEALAGLYLYSGLNLEUGLUASP
7   GLYARGTHRLEUSERGLUTYRASNILEGLN
8   LYSGLUSERTHRLEUHISLEUVALLEUARG
9   LEUARGGLYTYRALAASPLEUARGGLUASP
10   PROASPARGGLNASPHISHISPROGLYSER
11   GLYALAGLN

Samples:

sample_1: UBB+1, [U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaPO4 50 mM; NaCl 100 mM

sample_2: UBB+1, [U-100% 13C], 1 mM; D2O 100%; NaPO4 50 mM; NaCl 100 mM

sample_3: UBB+1, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaPO4 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.2.5, P.GUNTERT ET AL. - chemical shift assignment, refinement, structure solution

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

xwinnmr, Bruker Biospin - collection

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

SPARKY, Goddard - peak picking

ProcheckNMR, Laskowski and MacArthur - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 900 MHz

Related Database Links:

BMRB 11505 11547 15047 15410 15689 15907 16582 16626 17181 17439 17769 17919 18582 18583 18584 18610 18611 18737 19406 19412 25070 25123 26604 4245 4375
PDB
DBJ BAA03983 BAA09860 BAA11842 BAA11843 BAA23486
EMBL CAA28495 CAA30815 CAA35999 CAA37227 CAA37599
GB AAA28154 AAA28997 AAA28998 AAA28999 AAA29000
PIR I50437 I51568 I65237 S13928 S21083
PRF 0412265A 1212243A 1212243B 1212243C 1212243D
REF NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286
SP P0C273 P0C275 P0C276 P0CG47 P0CG48
TPE CEL68433 CEL70397 CEL75964 CEL78064
TPG DAA18802 DAA20663 DAA20672 DAA24675 DAA28295
AlphaFold P0C273 P0C275 P0C276 P0CG47 P0CG48

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