BMRBj - BMREntryMaster

Found 1 Document (0.729 seconds)

BMRB: 7304

1XHH

beta-microseminoprotein

Authors

Ghasriani, H., Teilum, K., Johnsson, Y., Fernlund, P., Drakenberg, T.

Assembly

pMSP

Entity

1. pMSP (polymer, Thiol state: all disulfide bound), 91 monomers, 10094.44 Da Detail

QCYFIPNQSL KPNECQDLKG VSHPLNSVWK TKDCEECTCG QDAISCCNTA AIPTGYDTNK CQKILNKKTC TYTVVEKKDP GKTCDVTGWV L

Formula weight

10094.44 Da

Entity Connection

disulfide 5 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS2:SG	1:CYS47:SG
2	disulfide	sing	1:CYS15:SG	1:CYS39:SG
3	disulfide	sing	1:CYS34:SG	1:CYS70:SG
4	disulfide	sing	1:CYS37:SG	1:CYS46:SG
5	disulfide	sing	1:CYS61:SG	1:CYS84:SG

Source organism

Sus scrofa

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 86.5 %, Completeness (bb): 98.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	86.5 % (468 of 541)	86.5 % (468 of 541)
Backbone	98.4 % (179 of 182)	98.4 % (179 of 182)
Sidechain	80.5 % (289 of 359)	80.5 % (289 of 359)
Aromatic	74.2 % (23 of 31)	74.2 % (23 of 31)
Methyl	100.0 % (43 of 43)	100.0 % (43 of 43)

1. beta-microseminoprotein

QCYFIPNQSL KPNECQDLKG VSHPLNSVWK TKDCEECTCG QDAISCCNTA AIPTGYDTNK CQKILNKKTC TYTVVEKKDP GKTCDVTGWV L

Show sample condition

Sample

Temperature 310 (±1) K, pH 6.0 (±0.1)

#	Name	Concentration
1	beta-microseminoprotein	4.0 (±0.2) mM
2	H2O	90 %
3	D2O	10 %

Release date

2006-10-19

Citation

Solution structures of human and porcine beta-microseminoprotein
Ghasriani, H., Teilum, K., Johnsson, Y., Fernlund, P., Drakenberg, T.
J. Mol. Biol. (2006), 362, 502-515, PubMed 16930619 , DOI 10.1016/j.jmb.2006.07.029 , Abstract

Related entities 1. pMSP, : 1 : 1 : 1 : 21 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7304_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)
1:2:CYS:SG	1:47:CYS:SG	unknown	unknown	n/a
1:15:CYS:SG	1:39:CYS:SG	unknown	unknown	n/a
1:34:CYS:SG	1:70:CYS:SG	unknown	unknown	n/a
1:37:CYS:SG	1:46:CYS:SG	unknown	unknown	n/a
1:61:CYS:SG	1:84:CYS:SG	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr7304_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	555		100.0 (chain: 1, length: 91)
1	Chemical shift references	chemical_shift_referencing	OK	1		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 91, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 555
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

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Found 1 Document (0.729 seconds)

BMRB: 7304

Sample

Related entities 1. pMSP, : 1 : 1 : 1 : 21 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail