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Found 1 Document (3.317 seconds)

BMRB: 7249

2JNB

Complete 1H, 13C, and 15N Chemical Shift Assignments for the 15.5K Protein

Authors

Soss, S.E., Flynn, P.F.

Assembly

His-15.5K

Entity

1. His-15.5K (polymer, Thiol state: all free), 144 monomers, 16000.29 Da Detail

MGHHHHHHSS GIEEGRMTEA DVNPKAYPLA DAHLTKKLLD LVQQSCNYKQ LRKGANEATK TLNRGISEFI VMAADAEPLE IILHLPLLCE DKNVPYVFVR SKQALGRACG VSRPVIACSV TIKEGSQLKQ QIQSIQQSIE RLLV

Formula weight

16000.29 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.1 %, Completeness: 86.9 %, Completeness (bb): 93.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.9 % (1454 of 1674)	86.2 % (753 of 874)	87.9 % (569 of 647)	86.3 % (132 of 153)
Backbone	93.4 % (796 of 852)	93.4 % (271 of 290)	93.4 % (396 of 424)	93.5 % (129 of 138)
Sidechain	82.2 % (787 of 958)	82.5 % (482 of 584)	84.1 % (302 of 359)	20.0 % (3 of 15)
Aromatic	43.4 % (33 of 76)	55.3 % (21 of 38)	31.6 % (12 of 38)
Methyl	93.8 % (167 of 178)	95.5 % (85 of 89)	92.1 % (82 of 89)

1. His-15.5K

MGHHHHHHSS GIEEGRMTEA DVNPKAYPLA DAHLTKKLLD LVQQSCNYKQ LRKGANEATK TLNRGISEFI VMAADAEPLE IILHLPLLCE DKNVPYVFVR SKQALGRACG VSRPVIACSV TIKEGSQLKQ QIQSIQQSIE RLLV

Show sample condition

Sample #1

Temperature 293 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

Sample #2

Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

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: -0.13 ppm, Outliers: 3 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: -0.13 ppm, Outliers: 3 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: -0.08 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: -0.1 ppm, Outliers: 2 Detail

Release date

2006-12-03

Citation

NMR assignment of the human spliceosomal 15.5K protein
Soss, S.E., Flynn, P.F.
J. Biomol. NMR (2007), 38, 175-175, PubMed 17122951 , DOI 10.1007/s10858-006-9100-3 , Abstract

Related entities 1. His-15.5K, : 1 : 35 : 108 entities Detail

Interaction partners 1. His-15.5K, : 46 interactors Detail

More details for 46 interactors identified by 17 citations

Experiments performed 11 experiments Detail

1 HNCACB

Instrument

Varian Inova - 600 MHz EMSL 600 MHz equipped with cold probe

Sample

State isotropic, Temperature 297 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

2 CBCA_CO_NH

Instrument

Varian Inova - 600 MHz EMSL 600 MHz equipped with cold probe

Sample

State isotropic, Temperature 297 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

3 HNCA

Instrument

Varian Inova - 600 MHz EMSL 600 MHz equipped with cold probe

Sample

State isotropic, Temperature 297 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

4 HN_CO_CA

Instrument

Varian Inova - 600 MHz EMSL 600 MHz equipped with cold probe

Sample

State isotropic, Temperature 297 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

5 HCCH-COSY

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

6 HCCH-TOCSY

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

7 HBHA_CCO_NH

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

8 C_CO_NH

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

9 HNCO

Instrument

Varian Inova - 600 MHz EMSL 600 MHz equipped with cold probe

Sample

State isotropic, Temperature 297 (±0.1) K, pH 6.0 (±0.05), Details Sample first used for backbone assignment

#	Name	Isotope labeling	Type	Concentration
1	His-15.5K	[U-98% 13C; U-98% 15N]	protein	0.9 (±0.1) mM
2	sodium phosphate		buffer	50 (±5.0) mM
3	sodium chloride		salt	200 (±20.0) mM
4	sodium azide		salt	0.1 (±0.1) % w/w

10 1H15N_HSQC

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

11 1H13C_HSQC

Instrument

Varian Inova - 600 MHz University of Utah Dept of Biochemistry 600 MHz with cold probe

Sample

State isotropic, Temperature 293 (±0.1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
5	His-15.5K	[U-98% 13C; U-98% 15N]	protein	1.6 (±0.2) mM
6	sodium phosphate		buffer	100 (±10.0) mM
7	sodium chloride		salt	100 (±10.0) mM
8	sodium azide		salt	0.1 (±0.1) % w/w

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7249_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: bmr7249_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	1602		94.4 (chain: 1, length: 144)
1	Chemical shift references	chemical_shift_referencing	OK	3		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 144, Sequence coverage: 94.4%
- Total number of assignments
  - ¹H chemical shifts: 915
  - ¹³C chemical shifts: 557
  - ¹⁵N chemical shifts: 130
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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	290	270	93.1
¹³C chemical shifts	288	261	90.6
¹⁵N chemical shifts	138	128	92.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	18	47.4
¹³C chemical shifts	38	9	23.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	874	741	84.8
¹³C chemical shifts	647	557	86.1
¹⁵N chemical shifts	160	130	81.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	584	471	80.7
¹³C chemical shifts	359	296	82.5
¹⁵N chemical shifts	22	2	9.1

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Found 1 Document (3.317 seconds)

BMRB: 7249

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. His-15.5K, : 1 : 35 : 108 entities Detail

Interaction partners 1. His-15.5K, : 46 interactors Detail

Experiments performed 11 experiments Detail

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Chemical shift validation 3 contents Detail