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Found 1 Document (0.737 seconds)

BMRB: 25238

2MV1

Solution NMR structure of Human Relaxin-2

Authors

Haugaard-Kedstrom, L.M., Rosengren, K.

Assembly

Human Relaxin-2

Entity

1. Human Relaxin-2, entity 1 (polymer), 29 monomers, 3312.858 Da Detail

DSWMEEVIKL CGRELVRAQI AICGMSTWS

2. Human Relaxin-2, entity 2 (polymer), 24 monomers, 2656.137 Da Detail

XLYSALANKC CHVGCTKRSL ARFC

Total weight

5968.995 Da

Max. entity weight

3312.858 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.2 %, Completeness: 65.2 %, Completeness (bb): 60.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	65.2 % (350 of 537)	86.9 % (266 of 306)	36.4 % (84 of 231)
Backbone	60.8 % (158 of 260)	75.7 % (81 of 107)	50.3 % (77 of 153)
Sidechain	67.2 % (219 of 326)	93.0 % (185 of 199)	26.8 % (34 of 127)
Aromatic	45.5 % (20 of 44)	87.0 % (20 of 23)	0.0 % (0 of 21)
Methyl	62.1 % (36 of 58)	96.6 % (28 of 29)	27.6 % (8 of 29)

1. entity 1

DSWMEEVIKL CGRELVRAQI AICGMSTWS

2. entity 2

XLYSALANKC CHVGCTKRSL ARFC

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4 (±0.2)

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	1 (±0.2) mM
2	entity_2	natural abundance	1 (±0.2) mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 4 (±0.2)

#	Name	Isotope labeling	Concentration
5	entity_1	natural abundance	1 (±0.2) mM
6	entity_2	natural abundance	1 (±0.2) mM
7	D2O	natural abundance	100 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2MV1, Strand ID: A, B Detail

Release date

2016-09-21

Citation

Solution structure, aggregation behavior, and flexibility of human relaxin-2
Haugaard-Kedstrom, L.M., Hossain, M., Daly, N.L., Bathgate, R.AD., Rinderknecht, E., Wade, J.D., Craik, D.J., Rosengren, K.
ACS Chem. Biol. (2015), 10, 891-900, PubMed 25547165 , DOI 10.1021/cb500918v , Abstract

Related entities 1. Human Relaxin-2, entity 1, : 1 : 2 : 1 : 1 : 28 entities Detail

Related entities 2. Human Relaxin-2, entity 2, : 1 : 4 : 14 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25238_2mv1.nef
Input source #2: Coordindates	2mv1.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)
B:11:CYS:SG	A:11:CYS:SG	oxidized, CA 54.937, CB 49.359 ppm	oxidized, CA 55.847, CB 39.443 ppm	2.033
B:23:CYS:SG	A:24:CYS:SG	unknown, CA 54.909 ppm	unknown, CA 54.362 ppm	2.026
A:10:CYS:SG	A:15:CYS:SG	oxidized, CA 57.536, CB 43.049 ppm	unknown, CA 53.425 ppm	2.009

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)
2:1:PCA:C	2:2:LEU:N	unknown	unknown	n/a
1:29:SER:C	1:30:NH2:N	unknown	unknown	n/a
2:24:CYS:C	2:25:NH2: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, Torsion angle restraints, Coordinates
A	25	NH2	AMINO GROUP	Coordinates
B	30	NH2	AMINO GROUP	Coordinates

Sequence alignments

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

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
B	B	30	0	0	100.0
A	A	25	0	0	100.0

Content subtype: combined_25238_2mv1.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	6		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	364		96.0 (chain: A, length: 25), 93.3 (chain: B, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	381 (1)	noe	96.0 (chain: A, length: 25), 93.3 (chain: B, length: 30)
2	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	30 (1)	hbond	52.0 (chain: A, length: 25), 40.0 (chain: B, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	86 (86)	.	92.0 (chain: A, length: 25), 96.7 (chain: B, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 25, Sequence coverage: 96.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 93.3%
- Total number of assignments
  - ¹H chemical shifts: 277
  - ¹³C chemical shifts: 87
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- 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
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
9	LYS	HZ1	7.672
9	LYS	HZ2	7.672
9	LYS	HZ3	7.672

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	141	111	78.7
¹³C chemical shifts	104	38	36.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	25	51.0
¹³C chemical shifts	47	23	48.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	92	86	93.5
¹³C chemical shifts	57	15	26.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	11	91.7
¹³C chemical shifts	12	2	16.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	10	90.9
¹³C chemical shifts	11	0	0.0

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
9	LYS	HZ1	7.519
9	LYS	HZ2	7.519
9	LYS	HZ3	7.519

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	175	160	91.4
¹³C chemical shifts	130	49	37.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	57	95.0
¹³C chemical shifts	58	28	48.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	115	103	89.6
¹³C chemical shifts	72	21	29.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	17	89.5
¹³C chemical shifts	19	6	31.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	10	83.3
¹³C chemical shifts	10	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 25, Sequence coverage: 96.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 93.3%
- Total number of restraints: 381
- Weight of restraints: 1.0 (381)
- Potential type of restraints: square-well-parabolic (381)
- Range of distance target values: 2.1, 5.78 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_2
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 25, Sequence coverage: 52.0%
    - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 40.0%
  - Total number of restraints: 30
  - Weight of restraints: 1.0 (30)
  - Potential type of restraints: square-well-parabolic (30)
  - Range of distance target values: 1.75, 2.55 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 25, Sequence coverage: 92.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 96.7%
- Total number of restraints: 86
- Total number of restraints per polymer type: 86
- Weight of restraints: 1.0 (86)
- Potential type of restraints: square-well-parabolic (86)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords insulin/relaxin family fold, signalling protein

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Found 1 Document (0.737 seconds)

BMRB: 25238

Sample #1

Sample #2

Related entities 1. Human Relaxin-2, entity 1, : 1 : 2 : 1 : 1 : 28 entities Detail

Related entities 2. Human Relaxin-2, entity 2, : 1 : 4 : 14 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

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NMR combined restraints 5 contents Detail