BMRB Entry 5022

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5022
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Converting a DNA Damage Checkpoint Effector (UmuD2C) into a Lesion Bypass Polymerase (UmuD'2C)
Deposition date:
2001-05-21
Original release date:
2003-01-07
Authors:
Ferentz, A.; Walker, G.; Wagner, G.
Citation:

Citation: Ferentz, A.; Walker, G.; Wagner, G.. "Converting a DNA Damage Checkpoint Effector (UmuD2C) into a Lesion Bypass Polymerase (UmuD'2C) "  EMBO J. 20, 4287-4298 (2001).
PubMed: 11483531

Assembly members:

Assembly members:
UMUD PROTEIN, polymer, 115 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UMUD PROTEIN: AFPSPAADYVEQRIDLNQLL IQHPSATYFVKASGDSMIDG GISDGDLLIVDSAITASHGD IVIAAVDGEFTVKKLQLRPT VQLIPMNSAYSPITISSEDT LDVFGVVIHVVKAMR

Data sets:
Data typeCount
1H chemical shifts583
13C chemical shifts290
15N chemical shifts106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UMUD PROTEIN, chain A1
2UMUD PROTEIN, chain B1

Entities:

Entity 1, UMUD PROTEIN, chain A 115 residues - Formula weight is not available

1   ALAPHEPROSERPROALAALAASPTYRVAL
2   GLUGLNARGILEASPLEUASNGLNLEULEU
3   ILEGLNHISPROSERALATHRTYRPHEVAL
4   LYSALASERGLYASPSERMETILEASPGLY
5   GLYILESERASPGLYASPLEULEUILEVAL
6   ASPSERALAILETHRALASERHISGLYASP
7   ILEVALILEALAALAVALASPGLYGLUPHE
8   THRVALLYSLYSLEUGLNLEUARGPROTHR
9   VALGLNLEUILEPROMETASNSERALATYR
10   SERPROILETHRILESERSERGLUASPTHR
11   LEUASPVALPHEGLYVALVALILEHISVAL
12   VALLYSALAMETARG

Samples:

sample_1: UMUD PROTEIN, [U-15N], 0.9 mM; NaCl 150 mM; phosphate 10 mM; DTT 1 mM; EDTA 0.1 mM; H2O 95%; D2O 5%

sample_2: UMUD PROTEIN, [U-15N; U-13C], 1.3 mM; NaCl 150 mM; phosphate 20 mM; DTT 1 mM; EDTA 0.1 mM; H2O 95%; D2O 5%

sample_3: UMUD PROTEIN 1.5 mM; NaCl 150 mM; phosphate 10 mM; DTT 1 mM; EDTA 0.1 mM; H2O 95%; D2O 5%

sample_4: UMUD PROTEIN 1.4 mM; NaCl 150 mM; phosphate 10 mM; DTT 1 mM; EDTA 0.1 mM; D2O 100%

sample_cond_1: pH: 6.0; temperature: 303 K; ionic strength: 160 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
HNHAnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available

Software:

FELIX v97.0 - processing

XEASY v1.3.9 - data analysis

X-PLOR v3.851 - refinement

NMR spectrometers:

  • Varian VXR 500 MHz

Related Database Links:

PDB
DBJ BAA36030 BAB35101 BAG76755 BAI24995 BAI30119
EMBL CAP75718 CAQ31685 CAQ98062 CAR02572 CAR07525
GB AAA24728 AAA98073 AAC74267 AAG56034 AAN42787
REF NP_287422 NP_309705 NP_415701 NP_707080 NP_753536
SP P0AG11 P0AG12 P0AG13
AlphaFold P0AG11 P0AG12 P0AG13

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