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Found 1 Document (0.634 seconds)

BMRB: 18784

2LZY

SOLUTION NMR STRUCTURE OF ASTEROPSIN C FROM A MARINE SPONGE ASTEROPUS SP.

Authors

Li, H., Bowling, J.J., Hamann, M.T., Jung, J.H.

Assembly

ABU8-3

Entity

1. ABU8-3 (polymer, Thiol state: all disulfide bound), 35 monomers, 3773.245 Da Detail

XDCPGEGEQC DVEFNPCCPP LTCIPGDPYG ICYII

Formula weight

3773.245 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS18:SG
2	disulfide	sing	1:CYS10:SG	1:CYS23:SG
3	disulfide	sing	1:CYS17:SG	1:CYS32:SG

Source organism

Asteropus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.1 %, Completeness: 90.5 %, Completeness (bb): 80.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	90.5 % (304 of 336)	99.5 % (190 of 191)	78.6 % (114 of 145)
Backbone	80.5 % (132 of 164)	98.5 % (65 of 66)	68.4 % (67 of 98)
Sidechain	100.0 % (202 of 202)	100.0 % (125 of 125)	100.0 % (77 of 77)
Aromatic	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)
Methyl	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)

1. ABU8-3

XDCPGEGEQC DVEFNPCCPP LTCIPGDPYG ICYII

Show sample condition

Sample

Solvent system CD3OH, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Type	Concentration
1	ABU8-3	natural abundance		10 mM
2	CD3OH	natural abundance		100 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2LZY, Strand ID: A Detail

Release date

2013-10-20

Citation

Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc
Temel, D.B., Dutta, K., Ghose, R.
Biomol. NMR Assign. (2014), 8, 37-41, PubMed 23225198 , DOI 10.1007/s12104-012-9448-0 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 18791 released on 2013-01-28
Title Sequence-specific backbone 1H, 13C and 15N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc

Related entities 1. ABU8-3, : 1 : 1 : 54 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18784_2lzy.nef
Input source #2: Coordindates	2lzy.cif
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	True (see coodinates for details)
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)
A:3:CYS:SG	A:18:CYS:SG	oxidized, CA 52.412, CB 42.621 ppm	oxidized, CA 52.558, CB 38.522 ppm	2.032
A:10:CYS:SG	A:23:CYS:SG	oxidized, CA 53.615, CB 51.227 ppm	oxidized, CA 55.375, CB 40.173 ppm	2.031
A:17:CYS:SG	A:32:CYS:SG	oxidized, CA 56.207, CB 43.242 ppm	oxidized, CA 55.648, CB 41.925 ppm	2.033

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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:1:PCA:C	1:2:ASP:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	1	PCA	PYROGLUTAMIC ACID	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30-----
XDCPGEGEQCDVEFNPCCPPLTCIPGDPYGICYII
|||||||||||||||||||||||||||||||||||
XDCPGEGEQCDVEFNPCCPPLTCIPGDPYGICYII

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	35	0	0	100.0

Content subtype: combined_18784_2lzy.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	4		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	310		100.0 (chain: A, length: 35)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	629 (1)	noe	100.0 (chain: A, length: 35)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 196
  - ¹³C chemical shifts: 114
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	197	195	99.0
¹³C chemical shifts	148	114	77.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	68	66	97.1
¹³C chemical shifts	69	35	50.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	129	129	100.0
¹³C chemical shifts	79	79	100.0

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

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

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of restraints: 629
- Weight of restraints: 1.0 (629)
- Potential type of restraints: square-well-parabolic (629)
- Range of distance target values: 1.19, 4.15 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords KNOTTIN, SPONGE, TOXIN

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Found 1 Document (0.634 seconds)

BMRB: 18784

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. ABU8-3, : 1 : 1 : 54 entities Detail

Experiments performed 5 experiments Detail

Instrument

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NMR combined restraints 3 contents Detail