BMRBj - BMREntryMaster

Found 1 Document (1.96 seconds)

BMRB: 4919

1G7E

Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer

Authors

Liepinsh, E., Baryshev, M., Sharipo, A., Ingelman-Sundberg, M., Otting, G., Mkrtchian, S.

Assembly

ERp29 N-domain

Entity

1. ERp29 N-domain (polymer, Thiol state: all free), 137 monomers, 15513.39 Da Detail

MRGSHHHHHH GSLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGC

Formula weight

15513.39 Da

Source organism

Rattus norvegicus

Exptl. method

NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.1 %, Completeness: 73.8 %, Completeness (bb): 81.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.8 % (1199 of 1624)	91.7 % (775 of 845)	45.9 % (294 of 641)	94.2 % (130 of 138)
Backbone	81.2 % (656 of 808)	94.6 % (265 of 280)	67.6 % (269 of 398)	93.8 % (122 of 130)
Sidechain	59.7 % (561 of 940)	90.3 % (510 of 565)	11.7 % (43 of 367)	100.0 % (8 of 8)
Aromatic	44.5 % (81 of 182)	83.5 % (76 of 91)	4.4 % (4 of 90)	100.0 % (1 of 1)
Methyl	55.5 % (71 of 128)	100.0 % (64 of 64)	10.9 % (7 of 64)

1. Endoplasmic reticulum protein p29

MRGSHHHHHH GSLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGC

Show sample condition

Sample

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 1G7E, Strand ID: A Detail

Release date

2001-08-07

Citation

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer
Liepinsh, E., Baryshev, M., Sharipo, A., Ingelman-Sundberg, M., Otting, G., Mkrtchian, S.
Structure (2001), 9, 457-471, PubMed 11435111 , DOI: , Abstract

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

  BMRB: 4920 released on 2001-08-07
    Title Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer
  Swiss-Prot: P52555 released on 1996-10-01
    Title ERP29_RAT Entity Endoplasmic reticulum resident protein 29

Related entities 1. ERp29 N-domain, : 1 : 2 : 17 entities Detail

Interaction partners 1. ERp29 N-domain, : 5 interactors Detail

More details for 5 interactors identified by 2 citations

Experiments performed 8 experiments Detail

1 2D 1H-1H NOESY

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

2 2D 1H-1H COSY

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

3 2D 1H-1H CLEAN TOCSY

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

4 2D 1H-15N HSQC

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

5 3D 1H-1H-15N NOESY

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

6 3D HNCA

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

7 3D HN(CO)CA

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

8 3D HNCO

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Varian UnityPlus (800 MHz)

Sample #1

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Endoplasmic reticulum protein p29	[U-15N; U-13C]		0.3 mM

Sample #2

Temperature 308 (±1) K, pH 4.9 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	Endoplasmic reticulum protein p29			0.3 mM

nullKeywords Nuclear magnetic resonance spectroscopy, protein structure

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Found 1 Document (1.96 seconds)

BMRB: 4919

Sample

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

Related entities 1. ERp29 N-domain, : 1 : 2 : 17 entities Detail

Interaction partners 1. ERp29 N-domain, : 5 interactors Detail

Experiments performed 8 experiments Detail

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