BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 15566

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15566

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Title: POLYMERASE LAMBDA BRCT DOMAIN   PubMed: 18585102

Deposition date: 2007-11-27 Original release date: 2008-07-15

Authors: Mueller, Geoffrey; Moon, Andrea; Derose, Eugene; Pederson, Lars; London, Robert

Citation: Mueller, G.; Moon, A.; Derose, E.; Havener, J.; Ramsden, D.; Pedersen, L.; London, R.. "A comparison of BRCT domains involved in nonhomologous end-joining: Introducing the solution structure of the BRCT domain of polymerase lambda"  DNA Repair (Amst). 7, 1340-1351 (2008).

Assembly members:
DNA_POLYMERASE_LAMBDA, polymer, 106 residues, 11648.480 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET

Entity Sequences (FASTA):
DNA_POLYMERASE_LAMBDA: GSNSGEEAEEWLSSLRAHVV RTGIGRARAELFEKQIVQHG GQLCPAQGPGVTHIVVDEGM DYERALRLLRLPQLPPGAQL VKSAWLSLCLQERRLVDVAG FSIFIP

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts94
1H chemical shifts591

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA POLYMERASE LAMBDA1

Entities:

Entity 1, DNA POLYMERASE LAMBDA 106 residues - 11648.480 Da.

1   GLYSERASNSERGLYGLUGLUALAGLUGLU
2   TRPLEUSERSERLEUARGALAHISVALVAL
3   ARGTHRGLYILEGLYARGALAARGALAGLU
4   LEUPHEGLULYSGLNILEVALGLNHISGLY
5   GLYGLNLEUCYSPROALAGLNGLYPROGLY
6   VALTHRHISILEVALVALASPGLUGLYMET
7   ASPTYRGLUARGALALEUARGLEULEUARG
8   LEUPROGLNLEUPROPROGLYALAGLNLEU
9   VALLYSSERALATRPLEUSERLEUCYSLEU
10   GLNGLUARGARGLEUVALASPVALALAGLY
11   PHESERILEPHEILEPRO

Samples:

sample: TRIS 25 mM; sodium chloride 75 mM; DSS 10 uM; EDTA 0.2 mM; DTT 1 mM; D2O, [U-100% 2H], 10%; H2O 90%

RDC_sample: TRIS 25 mM; sodium chloride 75 mM; DSS 10 uM; EDTA 0.2 mM; DTT 1 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.075 M; pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D C(CO) NHsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D H(CCO)NHsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1
3D HNHAsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H- 13C NOESYsampleisotropicsample_conditions_1
2D 1H-15N HSQCRDC_sampleanisotropicsample_conditions_1

Software:

X-PLOR NIH, SCHWIETERS, C.D. ET AL. - refinement

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • VARIAN INOVA 500 MHz

Related Database Links:

PDB
DBJ BAB13852 BAE02437 BAF84914 BAG10573 BAK63678
EMBL CAB65074
GB AAF27541 AAG22519 AAH68529 AAM77696 AAQ74388
REF NP_001167555 NP_001167556 NP_001253835 NP_001267179 NP_001270218
SP Q4R380 Q9UGP5
AlphaFold Q4R380 Q9UGP5

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