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Biological Magnetic Resonance Data Bank


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BMRB Entry 15109

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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/BMR15109
MolProbity Validation Chart

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Title: Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.   PubMed: 17298945

Deposition date: 2007-01-23 Original release date: 2007-05-21

Authors: Lemak, Alexander; Kaustov, Lilia; Lukin, Jonathan; Duan, Shili; Arrowsmith, Cheryl

Citation: Kaustov, Lilia; Lukin, Jonathan; Lemak, Alexander; Duan, Shili; Ho, Melissa; Doherty, Ryan; Penn, Liinda; Arrowsmith, Cheryl. "The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of P53"  J. Biol. Chem. 282, 11300-11307 (2007).

Assembly members:
CPH domain, polymer, 105 residues, 9327.353 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

Entity Sequences (FASTA):
CPH domain: GSHMRSEFASGNTYALYVRD TLQPGMRVRMLDDYEEISAG DEGEFRQSNNGVPPVQVFWE STGRTYWVHWHMLEILGFEE DIEDMVEADEYQGAVASRVL GRALP

Data typeCount
13C chemical shifts404
15N chemical shifts105
1H chemical shifts677

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CPH domain1

Entities:

Entity 1, CPH domain 105 residues - 9327.353 Da.

residues 1-4 represent a non-native tag; residues 80-105 represent unstructured part of the protein.

1   GLYSERHISMETARGSERGLUPHEALASER
2   GLYASNTHRTYRALALEUTYRVALARGASP
3   THRLEUGLNPROGLYMETARGVALARGMET
4   LEUASPASPTYRGLUGLUILESERALAGLY
5   ASPGLUGLYGLUPHEARGGLNSERASNASN
6   GLYVALPROPROVALGLNVALPHETRPGLU
7   SERTHRGLYARGTHRTYRTRPVALHISTRP
8   HISMETLEUGLUILELEUGLYPHEGLUGLU
9   ASPILEGLUASPMETVALGLUALAASPGLU
10   TYRGLNGLYALAVALALASERARGVALLEU
11   GLYARGALALEUPRO

Samples:

sample_1: CPH domain, [U-15N; U-13C], 0.7 mM; TRIS 25 mM; sodium chloride 250 mM; H2O 55 M; PMSF 0.5 mM; TCEP 0.5 mM; Benzamidine 1 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (13C/15N) NOESYsample_1isotropicsample_conditions_1
3D 13C_aromatic NOESYsample_1isotropicsample_conditions_1
3D (H)C(CO)NHsample_1isotropicsample_conditions_1
Jmodulated N15 HSQCsample_1anisotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

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

SPARKY v3.106, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA07551 BAF85495 BAG09593 BAG63902
EMBL CAH90514
GB AAH33647 EAX04144 EAX04145
REF NP_001125271 NP_001161842 NP_055595 XP_001136655 XP_003311343
SP Q14999 Q5RCJ3

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts