BMRBj - BMREntryMaster

2L2W

Thiostrepton

Authors

Assembly

thiostrepton

Entity

1. thiostrepton (polymer, Thiol state: all free), 19 monomers, 1805.984 Da Detail

XIAXASXTXX XXTXXXXXX

Formula weight

1805.984 Da

Entity Connection

peptide 11, ester 1, covalent 14 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	ester	sing	1:THR13:OG1	1:QUA1:C11
2	covalent	sing	1:QUA1:C7	1:ILE2:N
3	peptide	sing	1:ILE2:C	1:ALA3:N
4	peptide	sing	1:ALA3:C	1:DHA4:N
5	peptide	sing	1:DHA4:C	1:ALA5:N
6	peptide	sing	1:ALA5:C	1:SER6:N
7	covalent	sing	1:SER6:C	1:BB97:SG
8	covalent	doub	1:SER6:C	1:BB97:N
9	covalent	sing	1:SER6:CA	1:BB914:C
10	covalent	sing	1:SER6:CB	1:MH615:CB
11	peptide	sing	1:BB97:C	1:THR8:N
12	peptide	sing	1:THR8:C	1:DBU9:N
13	covalent	sing	1:DBU9:C	1:DCY10:SG
14	covalent	doub	1:DBU9:C	1:DCY10:N
15	peptide	sing	1:DCY10:C	1:TS911:N
16	covalent	sing	1:TS911:C	1:BB912:SG
17	covalent	doub	1:TS911:C	1:BB912:SG
18	peptide	sing	1:BB912:C	1:THR13:N
19	covalent	sing	1:THR13:C	1:BB914:SG
20	covalent	doub	1:THR13:C	1:BB914:N
21	covalent	sing	1:BB914:C	1:MH615:N
22	covalent	sing	1:MH615:C	1:BB916:SG
23	covalent	doub	1:MH615:C	1:BB916:N
24	peptide	sing	1:BB916:C	1:DHA17:N
25	peptide	sing	1:DHA17:C	1:DHA18:N
26	peptide	sing	1:DHA18:C	1:NH219:N

Source organism

Streptomyces azureus

Exptl. method

solution NMR

Refine. method

simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 31.6 %, Completeness: 94.4 %, Completeness (bb): 91.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	94.4 % (51 of 54)	92.0 % (23 of 25)	100.0 % (23 of 23)	83.3 % (5 of 6)
Backbone	91.7 % (33 of 36)	83.3 % (10 of 12)	100.0 % (18 of 18)	83.3 % (5 of 6)
Sidechain	100.0 % (24 of 24)	100.0 % (13 of 13)	100.0 % (11 of 11)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. thiostrepton

XIAXASXTXX XXTXXX

Solvent system chloroform-d/ethanol-d5 5:1, Pressure 1 atm, Temperature 298 K

#	Name	Isotope labeling	Concentration
1	thiostrepton	natural abundance	10 mM
2	chloroform-d	natural abundance	83 %
3	ethanol-d5	natural abundance	17 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2L2W, Strand ID: A Detail

Release date

2012-08-27

Citation

NMR structures of thiostrepton derivatives for characterization of the ribosomal binding site
Jonker, H.R.A., Baumann, S., Wolf, A., Schoof, S., Hiller, F., Schulte, K.W., Kirschner, K.N., Schwalbe, H., Arndt, H.
Angew. Chem Int Ed Engl. (2011), 50, 3308-3312, PubMed 21365717 , DOI 10.1002/anie.201003582 , Abstract

1 2D 1H-15N HSQC