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Found 1 Document (0.662 seconds)

BMRB: 18115

2LMG

Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70

Authors

Zhou, C., Gao, X., Wu, M., Hu, H.

Assembly

C-terminal Domain (537-610) of Human Heat Shock Protein 70

Entity

1. C-terminal Domain (537-610) of Human Heat Shock Protein 70 (polymer, Thiol state: all free), 75 monomers, 8369.379 Da Detail

GSAKNALESY AFNMKSAVED EGLKGKISEA DKKKVLDKCQ EVISWLDANT LAEKDEFEHK RKELEQVCNP IISGL

Formula weight

8369.379 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.7 %, Completeness: 90.8 %, Completeness (bb): 96.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	90.8 % (796 of 877)	88.7 % (409 of 461)	92.2 % (309 of 335)	96.3 % (78 of 81)
Backbone	96.9 % (434 of 448)	96.1 % (147 of 153)	97.3 % (215 of 221)	97.3 % (72 of 74)
Sidechain	86.4 % (432 of 500)	85.4 % (263 of 308)	88.1 % (163 of 185)	85.7 % (6 of 7)
Aromatic	27.3 % (12 of 44)	50.0 % (11 of 22)	0.0 % (0 of 21)	100.0 % (1 of 1)
Methyl	100.0 % (76 of 76)	100.0 % (38 of 38)	100.0 % (38 of 38)

1. entity

GSAKNALESY AFNMKSAVED EGLKGKISEA DKKKVLDKCQ EVISWLDANT LAEKDEFEHK RKELEQVCNP IISGL

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-100% 13C; U-100% 15N]	1 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	H2O	natural abundance	90 %
10	D2O	natural abundance	10 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	[U-100% 13C; U-100% 15N]	1 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	D2O	natural abundance	100 %

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: -0.4 ppm, Outliers: 4 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: -0.4 ppm, Outliers: 4 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: 0.1 ppm, Outliers: 2 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: -0.37 ppm, Outliers: 3 Detail

Protein Blocks Logo

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

Release date

2012-08-28

Citation

The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation
Gao, X., Zhou, C., Zhou, Z., Wu, M., Cao, C., Hu, H.
J. Biol. Chem. (2012), 287, 6044-6052, PubMed 22219199 , DOI 10.1074/jbc.M111.294728 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 17825 released on 2012-01-08
Title Solution Structure of the J Domain of HSJ1a

Related entities 1. C-terminal Domain (537-610) of Human Heat Shock Protein 70, : 1 : 12 : 199 entities Detail

Interaction partners 1. C-terminal Domain (537-610) of Human Heat Shock Protein 70, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

2 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-100% 13C; U-100% 15N]	1 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	H2O	natural abundance	90 %
10	D2O	natural abundance	10 %

3 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-100% 13C; U-100% 15N]	1 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	H2O	natural abundance	90 %
10	D2O	natural abundance	10 %

4 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-100% 13C; U-100% 15N]	1 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	H2O	natural abundance	90 %
10	D2O	natural abundance	10 %

5 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	[U-100% 13C; U-100% 15N]	1 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	D2O	natural abundance	100 %

6 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	[U-100% 13C; U-100% 15N]	1 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	D2O	natural abundance	100 %

7 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

8 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	entity	[U-100% 13C; U-100% 15N]	1 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	H2O	natural abundance	90 %
10	D2O	natural abundance	10 %

9 2D (HB)CB(CGCD)HD

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	[U-100% 13C; U-100% 15N]	1 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	D2O	natural abundance	100 %

10 2D (HB)CB(CGCDCE)HE

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	entity	[U-100% 13C; U-100% 15N]	1 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	D2O	natural abundance	100 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18115_2lmg.nef
Input source #2: Coordindates	2lmg.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

--540-------550-------560-------570-------580-------590-------600-------610
GSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGL
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGL
--------10--------20--------30--------40--------50--------60--------70-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	75	0	0	100.0

Content subtype: combined_18115_2lmg.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	794		98.7 (chain: A, length: 75)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1354 (1)	noe	98.7 (chain: A, length: 75)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 98.7%
- Total number of assignments
  - ¹H chemical shifts: 406
  - ¹³C chemical shifts: 310
  - ¹⁵N chemical shifts: 78
- 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	461	406	88.1
¹³C chemical shifts	335	310	92.5
¹⁵N chemical shifts	82	78	95.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	149	97.4
¹³C chemical shifts	150	146	97.3
¹⁵N chemical shifts	74	72	97.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	308	257	83.4
¹³C chemical shifts	185	164	88.6
¹⁵N chemical shifts	8	6	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	39	100.0
¹³C chemical shifts	39	39	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	13	59.1
¹³C chemical shifts	21	0	0.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 98.7%
- Total number of restraints: 1354
- Weight of restraints: 1.0 (1354)
- Potential type of restraints: square-well-parabolic (1354)
- Range of distance target values: 1.49, 6.12 (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 C-terminal Domain, Helix, HSP70

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Found 1 Document (0.662 seconds)

BMRB: 18115

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. C-terminal Domain (537-610) of Human Heat Shock Protein 70, : 1 : 12 : 199 entities Detail

Interaction partners 1. C-terminal Domain (537-610) of Human Heat Shock Protein 70, : 2 interactors Detail

Experiments performed 10 experiments Detail

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NMR combined restraints 3 contents Detail