BMRBj - BMREntryMaster

Found 1 Document (1.427 seconds)

BMRB: 5687

1P68

Stably folded de novo proteins from a designed combinatorial library

Authors

Hecht, M.H., Wei, Y.

Assembly

protein S-824

Entity

1. protein S-824 (polymer, Thiol state: not present), 102 monomers, 11928.20 Da Detail

MYGKLNDLLE DLQEVLKNLH KNWHGGKDNL HDVDNHLQNV IEDIHDFMQG GGSGGKLQEM MKEFQQVLDE LNNHLQGGKH TVHHIEQNIK EIFHHLEELV HR

Formula weight

11928.2 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 92.5 %, Completeness (bb): 99.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.5 % (1139 of 1231)	94.7 % (611 of 645)	87.6 % (408 of 466)	100.0 % (120 of 120)
Backbone	99.2 % (607 of 612)	99.1 % (212 of 214)	99.0 % (293 of 296)	100.0 % (102 of 102)
Sidechain	87.6 % (623 of 711)	92.6 % (399 of 431)	78.6 % (206 of 262)	100.0 % (18 of 18)
Aromatic	30.6 % (30 of 98)	59.2 % (29 of 49)	0.0 % (0 of 48)	100.0 % (1 of 1)
Methyl	96.1 % (98 of 102)	96.1 % (49 of 51)	96.1 % (49 of 51)

1. de novo protein

MYGKLNDLLE DLQEVLKNLH KNWHGGKDNL HDVDNHLQNV IEDIHDFMQG GGSGGKLQEM MKEFQQVLDE LNNHLQGGKH TVHHIEQNIK EIFHHLEELV HR

Show sample condition

Sample

Temperature 298 (±1) K, pH 4.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	de novo protein	[U-13C; U-15N]		2.0 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.5 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.5 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.55 ppm, Outliers: 2 Detail

Heteronucl. T₁

202 T₁ values in 2 lists
Coherence Sz, Field strength (¹H) 500 MHz, 600 MHz, Temperature 298 (±1) K, pH 4.0 (±0.2) Detail

Heteronucl. T₂

202 T₂ values in 2 lists
Coherence S(+,-), Field strength (¹H) 500 MHz, 600 MHz, Temperature 298 (±1) K, pH 4.0 (±0.2) Detail

Heteronucl. NOE

202 NOE values in 2 lists
Value type relative intensities, Field strength (¹H) 500 MHz, 600 MHz, Temperature 298 (±1) K, pH 4.0 (±0.2) Detail

Heteronucl. T₁/T₂

202 T₁/T₂ values in 2 lists
Field strength (¹H) 500 MHz, 600 MHz, Temperature 298 (±1) K, pH 4.0 (±0.2) Detail

Release date

2003-02-24

Citation 1

Letter to the Editor: 1H, 13C and 15N resonance assignments of S-824, a de novo four_helix bundle from a designed combinatorial library
Wei, Y., Fela, D., Kim, S., Hecht, M.H., Baum, J.
J. Biomol. NMR (2003), 27, 395-396, PubMed , DOI:

Show more 1 citaion

Citation 2

Stably folded de novo proteins from a designed combinatorial library
Wei, Y., Liu, T., Sazinsky, S.L., Moffet, D.A., Pelczer, I., Hecht, M.H.
Protein Sci. (2003), 12, 92-102, PubMed 12493832 , DOI 10.1110/ps.0228003 , Abstract

Hide non-primary 1 citaion

Related entities 1. protein S-824, : 1 : 46 entities Detail

Experiments performed 10 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data	bmr5687_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr5687_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1251		100.0 (chain: 1, length: 102)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 102, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 718
  - ¹³C chemical shifts: 414
  - ¹⁵N chemical shifts: 119
- Completeness of assignments
  - Entity_assemble_ID: 1
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	645	616	95.5
¹³C chemical shifts	466	414	88.8
¹⁵N chemical shifts	121	119	98.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	214	213	99.5
¹³C chemical shifts	204	204	100.0
¹⁵N chemical shifts	102	101	99.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	431	403	93.5
¹³C chemical shifts	262	210	80.2
¹⁵N chemical shifts	19	18	94.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	51	92.7
¹³C chemical shifts	55	51	92.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	28	57.1
¹³C chemical shifts	48	0	0.0
¹⁵N chemical shifts	1	1	100.0

Keywords de novo protein, four helix bundle

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Found 1 Document (1.427 seconds)

BMRB: 5687

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. protein S-824, : 1 : 46 entities Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 3 contents Detail