BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	83.9 % (648 of 772)	97.6 % (408 of 418)	64.1 % (182 of 284)	82.9 % (58 of 70)
Backbone	95.3 % (347 of 364)	99.2 % (122 of 123)	92.3 % (167 of 181)	96.7 % (58 of 60)
Sidechain	76.7 % (358 of 467)	96.9 % (286 of 295)	44.4 % (72 of 162)	0.0 % (0 of 10)
Aromatic	50.0 % (25 of 50)	100.0 % (25 of 25)	0.0 % (0 of 24)	0.0 % (0 of 1)
Methyl	73.9 % (34 of 46)	100.0 % (23 of 23)	47.8 % (11 of 23)

1. SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED

GDEKRPRTAF SSEQLARAKR EFNENRYLTE RRRQQLSSEL GLNEAQIKIW FQNKRAKIKK S

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 278 K, pH 5.7, Details U-15N, 50MM D-ACETATE, 100MM NACL, 7% D2O;

#	Name	Isotope labeling	Concentration
1	SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED	[U-15N]	500 uM
2	D-ACETATE		50 mM
3	NACL		100 mM
4	D2O		7 %
5	H2O		93 %

Sample #2

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 278 K, pH 5.7, Details U-15N, 100%D, PHE, TYR- BACKPROTONATED, 50MM D- ACETATE, 100MM NACL, 7% D2O;

#	Name	Isotope labeling	Concentration
6	SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED	[U-15N; U-2H] [U-15N; U-1H]-Phe,Trp	500 uM
7	D-ACETATE		50 mM
8	NACL		100 mM
9	D2O		7 %
10	H2O		93 %

Sample #3

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 278 K, pH 5.7, Details U-15N, 100%D, 50MM D-ACETATE, 100MM NACL, 7% D2O;

#	Name	Isotope labeling	Concentration
11	SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED	[U-15N; U-2H]	500 uM
12	D-ACETATE		50 mM
13	NACL		100 mM
14	D2O		7 %
15	H2O		93 %

Sample #4

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 278 K, pH 5.7, Details U-13C,U-15N, 50MM D-ACETATE, 100MM NACL, 7% D2O;

#	Name	Isotope labeling	Concentration
16	SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED	[U-13C; U-15N]	500 uM
17	D-ACETATE		50 mM
18	NACL		100 mM
19	D2O		7 %
20	H2O		93 %

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	TSP	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.12 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	TSP	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.12 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	TSP	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.02 ppm, Outliers: 2 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	TSP	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.23 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 25 models in PDB: 1ZTR, Strand ID: A Detail

Coupling constant

51 J values in 1 lists
Pressure 1 atm, Temperature 278 K, pH 5.7 Detail

Release date

2007-10-15

Citation

Solution structure of a protein denatured state and folding intermediate
Religa, T.L., Markson, J.S., Mayor, U., Freund, S.M.V., Fersht, A.R.
Nature (2005), 437, 1053-1056, PubMed 16222301 , DOI 10.1038/nature04054 , Abstract

Related entities 1. EnHD L16A, : 1 : 9 : 290 entities Detail

Interaction partners 1. EnHD L16A, : 10 interactors Detail

More details for 10 interactors identified by 1 citations

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15520_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr15520_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	675		100.0 (chain: 1, length: 61)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 61, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 454
  - ¹³C chemical shifts: 163
  - ¹⁵N chemical shifts: 58
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- 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	418	408	97.6
¹³C chemical shifts	284	163	57.4
¹⁵N chemical shifts	79	58	73.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	123	122	99.2
¹³C chemical shifts	122	108	88.5
¹⁵N chemical shifts	60	58	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	295	286	96.9
¹³C chemical shifts	162	55	34.0
¹⁵N chemical shifts	19	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	23	100.0
¹³C chemical shifts	23	5	21.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	25	100.0
¹³C chemical shifts	24	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords DENATURED STATE, ENGRAILED HOMEODOMAIN, FOLDING INTERMEDIATE, MUTANT, PROTEIN FOLDING

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Found 1 Document (0.658 seconds)

BMRB: 15520

Sample #1

Sample #2

Sample #3

Sample #4

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. EnHD L16A, : 1 : 9 : 290 entities Detail

Interaction partners 1. EnHD L16A, : 10 interactors Detail

Experiments performed 5 experiments Detail

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Sample

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Sample

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Chemical shift validation 3 contents Detail