BMRB: 5152

Designed Protein G Core Variants Fold to Native-like Structures: Sequence Selection by ORBIT Tolerates Variation in Backbone Specification

Authors

Ross, S.A., Sarisky, C.A., Su, A., Mayo, S.L.

Assembly

IMMUNOGLOBULIN G BINDING PROTEIN G

Entity

1. IMMUNOGLOBULIN G BINDING PROTEIN G (polymer, Thiol state: not present), 56 monomers, 6210.767 Da Detail

TTFKLIINGK TLKGETTTEA VDAATAEKVL KQYINDNGID GEWTYDDATK TWTVTE

Formula weight

6210.767 Da

Source organism

Streptococcus sp.

Exptl. method

NMR

Refine. method

Standard Distance Geometry/simulated Annealing Methods

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 95.3 %, Completeness (bb): 99.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	95.3 % (305 of 320)	95.3 % (305 of 320)
Backbone	99.1 % (115 of 116)	99.1 % (115 of 116)
Sidechain	93.1 % (190 of 204)	93.1 % (190 of 204)
Aromatic	80.0 % (20 of 25)	80.0 % (20 of 25)
Methyl	97.3 % (36 of 37)	97.3 % (36 of 37)

1. IMMUNOGLOBULIN G BINDING PROTEIN G

TTFKLIINGK TLKGETTTEA VDAATAEKVL KQYINDNGID GEWTYDDATK TWTVTE

Show sample condition

Sample

Pressure 1 atm, Temperature 298 (±1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	IMMUNOGLOBULIN G BINDING PROTEIN G			1 mM
2	sodium phosphate			50 mM
3	H2O			90 %
4	D2O			10 %

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Calculated from 40 models in PDB: 1FCL, Strand ID: A Detail

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Release date

2001-10-16

Citation

Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification
Ross, S.A., Sarisky, C.A., Su, A., Mayo, S.L.
Protein Sci. (2001), 10, 450-454, PubMed 11266631 , DOI 10.1110/ps.32501 , Abstract

Related entities 1. IMMUNOGLOBULIN G BINDING PROTEIN G, : 1 : 104 entities Detail

Interaction partners 1. IMMUNOGLOBULIN G BINDING PROTEIN G, : 1 interactors Detail

Experiments performed 4 experiments Detail