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BMRB: 17657

2LDA

Solution structure of the estrogen receptor-binding stapled peptide SP2 (Ac-HKXLHQXLQDS-NH2)

Authors

Phillips, C., Bazin, R., Bent, A., Davies, N., Moore, R., Pannifer, A., Pickford, A., Prior, S., Read, C., Roberts, L., Schade, M., Scott, A., Brown, D., Xu, B., Irving, S.

Assembly

stapled peptide SP2

Entity

1. stapled peptide SP2 (polymer, Thiol state: not present), 13 monomers, 1383.616 Da Detail

XHKXLHQXLQ DSX

Formula weight

1383.616 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 69.2 %, Completeness: 100.0 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	100.0 % (60 of 60)	100.0 % (60 of 60)
Backbone	100.0 % (18 of 18)	100.0 % (18 of 18)
Sidechain	100.0 % (42 of 42)	100.0 % (42 of 42)
Aromatic	100.0 % (4 of 4)	100.0 % (4 of 4)
Methyl	100.0 % (4 of 4)	100.0 % (4 of 4)

1. stapled peptide SP2

XHKXLHQXLQ DSX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Concentration
1	stapled peptide SP2	natural abundance	5 (±1.0) mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %
4	phosphate buffer	natural abundance	50 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Concentration
5	stapled peptide SP2	natural abundance	5 (±1.0) mM
6	D2O	natural abundance	100 %
7	phosphate buffer	natural abundance	50 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 2LDA, Strand ID: A Detail

Release date

2011-10-25

Citation

Design and structure of stapled peptides binding to estrogen receptors
Phillips, C., Roberts, L.R., Schade, M., Bazin, R., Bent, A., Davies, N.L., Moore, R., Pannifer, A.D., Pickford, A.R., Prior, S.H., Read, C.M., Scott, A., Brown, D.G., Xu, B., Irving, S.L.
J. Am. Chem. Soc. (2011), 133, 9696-9699, PubMed 21612236 , DOI 10.1021/ja202946k , Abstract

Experiments performed 6 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_17657_2lda.nef
Input source #2: Coordindates	2lda.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	True (see coodinates for details)
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:1:ACE:C	1:2:HIS:N	unknown	unknown	n/a
1:3:LYS:C	1:4:MK8:N	unknown	unknown	n/a
1:4:MK8:C	1:5:LEU:N	unknown	unknown	n/a
1:7:GLN:C	1:8:MK8:N	unknown	unknown	n/a
1:8:MK8:C	1:9:LEU:N	unknown	unknown	n/a
1:12:SER:C	1:13:NH2:N	unknown	unknown	n/a
1:4:MK8:CE	1:8:MK8:CE	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	0	ACE	ACETYL GROUP	Assigned chemical shifts, Distance restraints, Coordinates
A	3	MK8	2-methyl-L-norleucine	Assigned chemical shifts, Distance restraints, Coordinates
A	7	MK8	2-methyl-L-norleucine	Assigned chemical shifts, Distance restraints, Coordinates
A	12	NH2	AMINO GROUP	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

0--------10--
XHKXLHQXLQDSX
|||||||||||||
XHKXLHQXLQDSX
--------10---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	13	0	0	100.0

Content subtype: combined_17657_2lda.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	7		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	78		100.0 (chain: A, length: 13)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	317 (1)	noe	100.0 (chain: A, length: 13)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 13, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 78
- Completeness of assignments
  - Entity_assemble_ID: A
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	82	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	19	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	63	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 13, Sequence coverage: 100.0%
- Total number of restraints: 317
- Weight of restraints: 1.0 (317)
- Potential type of restraints: square-well-parabolic (317)
- Range of distance target values: 1.81, 3.39 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords Estrogen receptor ligand, Stapled peptide

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Found 1 Document (0.384 seconds)

BMRB: 17657

Sample #1

Sample #2

Experiments performed 6 experiments Detail

Instrument

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NMR combined restraints 3 contents Detail