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BMRB: 18521

2LUH

The NMR structure of the Vta1-Vps60 complex

Authors

Yang, Z., Vild, C., Ju, J., Zhang, X., Liu, J., Shen, J., Zhao, B., Lan, W., Gong, F., Liu, M., Cao, C., Xu, Z.

Assembly

Vta1-Vps60 complex

Entity

1. Vta1-Vps60 complex, entity 1 (polymer, Thiol state: all free), 167 monomers, 19037.83 Da Detail

MASNAARVVA TAKDFDKVGL GIIGYYLQLY AVELILSEED RSQEMTALAT ELLDTIEAFK KEIGGESEAE DSDKSLHVMN TLIHDQEKAK IYMLNFTMSL YNEKLKQLKD GPWDVMLKRS LWCCIDLFSC ILHLWKENIS ETSTNSLQKR IKYCKIYLSK LAKGEIG

2. Vta1-Vps60 complex, entity 2 (polymer, Thiol state: not present), 59 monomers, 6608.082 Da Detail

INIDKLQDMQ DEMLDLIEQG DELQEVLAMN NNSGELDDIS DAELDAELDA LAQEDFTLP

Total weight

25645.912 Da

Max. entity weight

19037.83 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.8 %, Completeness: 92.5 %, Completeness (bb): 95.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.5 % (2452 of 2651)	93.4 % (1284 of 1375)	90.7 % (933 of 1029)	95.1 % (235 of 247)
Backbone	95.0 % (1284 of 1352)	94.8 % (436 of 460)	94.6 % (632 of 668)	96.4 % (216 of 224)
Sidechain	89.8 % (1361 of 1515)	92.1 % (843 of 915)	86.7 % (500 of 577)	78.3 % (18 of 23)
Aromatic	90.9 % (140 of 154)	97.4 % (75 of 77)	83.8 % (62 of 74)	100.0 % (3 of 3)
Methyl	94.6 % (261 of 276)	94.9 % (131 of 138)	94.2 % (130 of 138)

1. entity 1

MASNAARVVA TAKDFDKVGL GIIGYYLQLY AVELILSEED RSQEMTALAT ELLDTIEAFK KEIGGESEAE DSDKSLHVMN TLIHDQEKAK IYMLNFTMSL YNEKLKQLKD GPWDVMLKRS LWCCIDLFSC ILHLWKENIS ETSTNSLQKR IKYCKIYLSK LAKGEIG

2. entity 2

INIDKLQDMQ DEMLDLIEQG DELQEVLAMN NNSGELDDIS DAELDAELDA LAQEDFTLP

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

Sample #4

Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.16 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2012-11-04

Citation

Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway
Yang, Z., Vild, C., Ju, J., Zhang, X., Liu, J., Shen, J., Zhao, B., Lan, W., Gong, F., Liu, M., Cao, C., Xu, Z.
J. Biol. Chem. (2012), 287, 43899-43908, PubMed 23105107 , DOI 10.1074/jbc.M112.390724 , Abstract

Related entities 1. Vta1-Vps60 complex, entity 1, : 1 : 1 entities Detail

Related entities 2. Vta1-Vps60 complex, entity 2, : 1 : 2 : 30 entities Detail

Interaction partners 2. Vta1-Vps60 complex, entity 2, : 8 interactors Detail

More details for 8 interactors identified by 3 citations

Experiments performed 24 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

2 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

3 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

4 2D 1H-13C HSQC aliphatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

5 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

6 2D 1H-13C HSQC aromatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

7 3D CBCA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

8 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

9 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

10 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

11 3D HNCA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

12 3D HNCA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

13 3D HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

14 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

15 3D HN(CO)CA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

16 3D HN(CO)CA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

17 3D HCCH-TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

18 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

19 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-13C; U-15N]		1.0-1.2 mM
2	entity_2	natural abundance		1.0-1.2 mM

20 3D 1H-15N NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
5	entity_1	natural abundance		1.0-1.2 mM
6	entity_2	[U-13C; U-15N]		1.0-1.2 mM

21 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

22 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

23 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vta1NTD with unlabled Vps60 peptide

#	Name	Isotope labeling	Type	Concentration
3	entity_1	[U-13C; U-15N]		1.0-1.2 mM
4	entity_2	natural abundance		1.0-1.2 mM

24 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 15N,13C labled Vps60 peptide with unlabled Vta1NTD

#	Name	Isotope labeling	Type	Concentration
7	entity_1	natural abundance		1.0-1.2 mM
8	entity_2	[U-13C; U-15N]		1.0-1.2 mM

NMR combined restraints 8 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18521_2luh.nef
Input source #2: Coordindates	2luh.cif
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

Sequence alignments

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

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSL

-------110-------120-------130-------140-------150-------160-------
YNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIG
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
YNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIG

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

--130-----140-------150-------160-------170-------180------
INIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGELDDISDAELDAELDALAQEDFTLP
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
INIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGELDDISDAELDAELDALAQEDFTLP
--------10--------20--------30--------40--------50---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	167	0	0	100.0
B	B	59	0	0	100.0

Content subtype: combined_18521_2luh.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	2473		100.0 (chain: A, length: 167), 91.5 (chain: B, length: 59)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	966 (1)	noe	91.5 (chain: B, length: 59)
2	Distance restraints	CNS/XPLOR_distance_constraints_7	OK	4036 (1)	noe	100.0 (chain: A, length: 167)
3	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	56 (1)	hbond	66.1 (chain: B, length: 59)
4	Distance restraints	CNS/XPLOR_distance_constraints_6	OK	204 (1)	hbond	77.8 (chain: A, length: 167)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	100 (100)	.	94.9 (chain: B, length: 59)
2	Dihedral angle restraints	CNS/XPLOR_dihedral_5	OK	290 (290)	.	94.0 (chain: A, length: 167)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 59, Sequence coverage: 91.5%
- Total number of assignments
  - ¹³C chemical shifts: 926
  - ¹H chemical shifts: 1315
  - ¹⁵N chemical shifts: 232
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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)
46	THR	HG1	5.996
50	THR	HG1	5.416
55	THR	HG1	6.425
77	HIS	HE2	9.407
81	THR	HG1	5.83
84	HIS	HE2	9.618
142	THR	HG1	5.656
144	THR	HG1	5.827

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	780	729	93.5
¹H chemical shifts	1036	1009	97.4
¹⁵N chemical shifts	184	172	93.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	334	329	98.5
¹H chemical shifts	341	338	99.1
¹⁵N chemical shifts	166	163	98.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	446	400	89.7
¹H chemical shifts	695	671	96.5
¹⁵N chemical shifts	18	9	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	108	104	96.3
¹H chemical shifts	108	107	99.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	69	62	89.9
¹H chemical shifts	72	72	100.0
¹⁵N chemical shifts	3	3	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	249	197	79.1
¹H chemical shifts	339	297	87.6
¹⁵N chemical shifts	67	60	89.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	118	105	89.0
¹H chemical shifts	119	105	88.2
¹⁵N chemical shifts	58	52	89.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	131	92	70.2
¹H chemical shifts	220	192	87.3
¹⁵N chemical shifts	9	8	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	39	32	82.1
¹H chemical shifts	39	38	97.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	5	0	0.0
¹H chemical shifts	5	5	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 59, Sequence coverage: 91.5%
- Total number of restraints: 963
- Weight of restraints: 1.0 (963)
- Potential type of restraints: square-well-parabolic (963)
- Range of distance target values: 2.35, 3.9 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
    None
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_7
  - Status: OK
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 100.0%
  - Total number of restraints: 4033
  - Weight of restraints: 1.0 (4033)
  - Potential type of restraints: square-well-parabolic (4033)
  - Range of distance target values: 2.35, 3.9 (Å)
  - Histogram of distance target values
  - Histogram of discrepancy in distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_4
    - Status: OK
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: B, Chain length: 59, Sequence coverage: 66.1%
    - Total number of restraints: 56
    - Weight of restraints: 1.0 (56)
    - Potential type of restraints: square-well-parabolic (56)
    - Range of distance target values: 2.05, 2.9 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
        None
      - Chain_ID: B
    - Distance restraints on contact map
    - Saveframe: CNS/XPLOR_distance_constraints_6
      - Status: OK
      - Experiment type: hbond
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 77.8%
        --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSL |||||||||||||||| | ||||||||||||||| |||||||||||||||||||| ||||||||||| ||||||||||||||| .ASNAARVVATAKDFDK..L.IIGYYLQLYAVELIL......QEMTALATELLDTIEAFKKE...........KSLHVMNTLIH.QEKAKIYMLNFTMSL --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 -------110-------120-------130-------140-------150-------160------- YNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIG ||||||||| |||||||||||||||||||| ||||||||||||||||||||||| YNEKLKQLK.....VMLKRSLWCCIDLFSCILHL......ETSTNSLQKRIKYCKIYLSKLAK -------110-------120-------130-------140-------150-------160---
      - Total number of restraints: 204
        Total hydrogen bond restraints: 204
        O...H-x: 102
        O...h-N: 102
      - Weight of restraints: 1.0 (204)
        Total hydrogen bond restraints: 1.0 (204)
        O...H-x: 1.0 (102)
        O...h-N: 1.0 (102)
      - Potential type of restraints: square-well-parabolic (204)
        Total hydrogen bond restraints: square-well-parabolic (204)
        O...H-x: square-well-parabolic (102)
        O...h-N: square-well-parabolic (102)
      - Range of distance target values: 2.05, 2.9 (Å)
      - Histogram of distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        None
      - Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 59, Sequence coverage: 94.9%
- Total number of restraints: 100
- Total number of restraints per polymer type: 100
- Weight of restraints: 1.0 (100)
- Potential type of restraints: square-well-parabolic (100)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: B
- Saveframe: CNS/XPLOR_dihedral_5
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 94.0%
  - Total number of restraints: 290
  - Total number of restraints per polymer type: 290
  - Weight of restraints: 1.0 (290)
  - Potential type of restraints: square-well-parabolic (290)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: A

Keywords Complex, NMR structure, Protein/Protein, Vps60, Vta1

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Found 1 Document (1.24 seconds)

BMRB: 18521

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Vta1-Vps60 complex, entity 1, : 1 : 1 entities Detail

Related entities 2. Vta1-Vps60 complex, entity 2, : 1 : 2 : 30 entities Detail

Interaction partners 2. Vta1-Vps60 complex, entity 2, : 8 interactors Detail

Experiments performed 24 experiments Detail

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