BMRBj - BMREntryMaster

Found 1 Document (1.395 seconds)

BMRB: 4865

1YU6

Backbone 1H, 13C, 15N Chemical shift Assignment for OMTKY3 bound to bovine Chymotrypsin Aa

Authors

Song, J., Markley, J.L.

Assembly

Turkey Ovomucoid Third Domain bound to bovine chymotrypsin Aa

Entity

1. Ovomucoid Third Domain from Turkey (polymer, Thiol state: all disulfide bound), 56 monomers, 6020.759 Da Detail

LAAVSVDCSE YPKPACTLEY RPLCGSDNKT YGNKCNFCNA VVESNGTLTL SHFGKC

2. bovine chymotrypsin Aa (polymer, Thiol state: not reported), 241 monomers, 25207.36 Da Detail

CGVPAIQPVL SGLIVNGEEA VPGSWPWQVS LQDKTGFHFC GGSLINENWV VTAAHCGVTT SDVVVAGEFD QGSSSEKIQK LKIAKVFKNS KYNSLTINND ITLLKLSTAA SFSQTVSAVC LPSASDDFAA GTTCVTTGWG LTRYANTPDR LQQASLPLLS NTNCKKYWGT KIKDAMICAG ASGVSSCMGD SGGPLVCKKN GAWTLVGIVS WGSSTCSTST PGVYARVTAL VNWVQQTLAA N

Total weight

31228.117 Da

Max. entity weight

25207.36 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	0:CYS8:SG	1:CYS38:SG
2	disulfide	sing	0:CYS16:SG	1:CYS35:SG
3	disulfide	sing	0:CYS24:SG	1:CYS56:SG

Source organism

Meleagris gallopavo , Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 17.5 %, Completeness: 6.7 %, Completeness (bb): 11.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	6.7 % (218 of 3237)	4.1 % (67 of 1648)	8.0 % (101 of 1268)	15.6 % (50 of 321)
Backbone	11.3 % (199 of 1758)	8.9 % (54 of 609)	11.2 % (97 of 864)	16.8 % (48 of 285)
Sidechain	1.5 % (26 of 1749)	1.3 % (14 of 1039)	1.5 % (10 of 674)	5.6 % (2 of 36)
Aromatic	0.0 % (0 of 244)	0.0 % (0 of 122)	0.0 % (0 of 114)	0.0 % (0 of 8)
Methyl	2.3 % (8 of 348)	2.9 % (5 of 174)	1.7 % (3 of 174)

1. Ovomucoid Third Domain from Turkey

LAAVSVDCSE YPKPACTLEY RPLCGSDNKT YGNKCNFCNA VVESNGTLTL SHFGKC

2. bovine chymotrypsin Aa

Show sample condition

Sample

Temperature 298 (±1) K, pH 7.3 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	Ovomucoid Third Domain from Turkey	[U-13C; U-15N]		2 mM
2	bovine chymotrypsin Aa			2 mM

Release date

2000-11-30

Citation

NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa
Song, J., Markley, J.L.
J. Mol. Recognit. (2001), 14, 166-171, PubMed , DOI 10.1002/jmr.530

Related entities 1. Ovomucoid Third Domain from Turkey, : 3 : 9 : 6 : 35 : 170 entities Detail

Related entities 2. bovine chymotrypsin Aa, : 108 entities Detail

Interaction partners 1. Ovomucoid Third Domain from Turkey, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4865_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:8:CYS:SG	1:38:CYS:SG	unknown	unknown, CA 55.34 ppm	n/a
1:16:CYS:SG	1:35:CYS:SG	unknown, CA 51.3 ppm	unknown, CA 58.24 ppm	n/a
1:24:CYS:SG	1:56:CYS:SG	unknown, CA 54.48 ppm	unknown, CA 55.75 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr4865_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shifts_OMTKY3_pH7.3	Warning	176		85.7 (chain: 1, length: 56)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: chemical_shifts_OMTKY3_pH7.3
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 56, Sequence coverage: 85.7%
- Total number of assignments
  - ¹³C chemical shifts: 85
  - ¹H chemical shifts: 45
  - ¹⁵N chemical shifts: 46
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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 (%)
¹³C chemical shifts	238	85	35.7
¹H chemical shifts	313	45	14.4
¹⁵N chemical shifts	59	46	78.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	112	85	75.9
¹H chemical shifts	113	44	38.9
¹⁵N chemical shifts	53	44	83.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	126	0	0.0
¹H chemical shifts	200	1	0.5
¹⁵N chemical shifts	6	2	33.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	26	0	0.0
¹H chemical shifts	26	0	0.0

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

Keywords OMTKY3:CTR complex

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Found 1 Document (1.395 seconds)

BMRB: 4865

Sample

Related entities 1. Ovomucoid Third Domain from Turkey, : 3 : 9 : 6 : 35 : 170 entities Detail

Related entities 2. bovine chymotrypsin Aa, : 108 entities Detail

Interaction partners 1. Ovomucoid Third Domain from Turkey, : 3 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail