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BMRB Entry 15896

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15896
MolProbity Validation Chart

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Title: Solution structures of copper loaded form PCuA (trans conformation of the peptide bond involving the nitrogen of P14)   PubMed: 18758441

Deposition date: 2008-07-28 Original release date: 2008-11-14

Authors: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Wang, Shenlin

Citation: Abriata, Luciano; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Gkazonis, Petros; Spyroulias, Georgios; Vila, Alejandro; Wang, Shenlin. "Mechanism of Cu(A) assembly."  Nat. Chemical Biol. 4, 599-601 (2008).

Assembly members:
PCuA, polymer, 120 residues, 13222.670 Da.
CU, non-polymer, 63.546 Da.

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

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

Entity Sequences (FASTA):
PCuA: GSFTEGWVRFSPGPNAAAYL TLENPGDLPLRLVGARTPVA ERVELHETFMREVEGKKVMG MRPVPFLEVPPKGRVELKPG GYHFMLLGLKRPLKAGEEVE LDLLFAGGKVLKVVLPVEAR

Data sets:
Data typeCount
13C chemical shifts505
15N chemical shifts107
1H chemical shifts844

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PCuA1
2COPPER (II) ION2

Entities:

Entity 1, PCuA 120 residues - 13222.670 Da.

1   GLYSERPHETHRGLUGLYTRPVALARGPHE
2   SERPROGLYPROASNALAALAALATYRLEU
3   THRLEUGLUASNPROGLYASPLEUPROLEU
4   ARGLEUVALGLYALAARGTHRPROVALALA
5   GLUARGVALGLULEUHISGLUTHRPHEMET
6   ARGGLUVALGLUGLYLYSLYSVALMETGLY
7   METARGPROVALPROPHELEUGLUVALPRO
8   PROLYSGLYARGVALGLULEULYSPROGLY
9   GLYTYRHISPHEMETLEULEUGLYLEULYS
10   ARGPROLEULYSALAGLYGLUGLUVALGLU
11   LEUASPLEULEUPHEALAGLYGLYLYSVAL
12   LEULYSVALVALLEUPROVALGLUALAARG

Entity 2, COPPER (II) ION - Cu - 63.546 Da.

1   CU

Samples:

sample_1: entity_1, [U-100% 15N], 0.8 ± 0.1 mM; D2O, [U-99.9% 2H], 10%; H2O 90%; Pi 50 mM

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; D2O, [U-99.9% 2H], 10%; H2O 90%; Pi 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
15N R1sample_1isotropicsample_conditions_1
15N R2sample_1isotropicsample_conditions_1
1H-15N NOEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 400 MHz

Related Database Links:

BMRB 15894 15895 15897
PDB
DBJ BAD71766
GB AAS81922 AEG34334 AFH39883
REF WP_011173952 WP_011229034 WP_014510965 WP_014630387 YP_145209

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