BMRBj - BMREntryMaster

Found 1 Document (3.254 seconds)

BMRB: 18901

2M26

NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS

Authors

Serrano, P., Geralt, M., Dutta, S.K., Wuthrich, K.

Assembly

C-terminal domain of the protein HCFC1

Entity

1. C-terminal domain of the protein HCFC1 (polymer, Thiol state: all free), 126 monomers, 13333.93 Da Detail

GCLPGFPGAP CAIKISKSPD GAHLTWEPPS VTSGKIIEYS VYLAIQSSQA SGEPKSSTPA QLAFMRVYCG PSPSCLVQSS SLSNAHIDYT TKPAIIFRIA ARNEKGYGPA TQVRWLQETS KDSSGT

Formula weight

13333.93 Da

Source organism

Exptl. method

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.3 %, Completeness: 86.9 %, Completeness (bb): 87.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.9 % (1215 of 1398)	86.8 % (629 of 725)	86.2 % (473 of 549)	91.1 % (113 of 124)
Backbone	87.4 % (640 of 732)	89.6 % (224 of 250)	84.8 % (312 of 368)	91.2 % (104 of 114)
Sidechain	87.1 % (681 of 782)	85.3 % (405 of 475)	89.9 % (267 of 297)	90.0 % (9 of 10)
Aromatic	82.4 % (84 of 102)	80.4 % (41 of 51)	83.7 % (41 of 49)	100.0 % (2 of 2)
Methyl	95.2 % (118 of 124)	95.2 % (59 of 62)	95.2 % (59 of 62)

1. entity

GCLPGFPGAP CAIKISKSPD GAHLTWEPPS VTSGKIIEYS VYLAIQSSQA SGEPKSSTPA QLAFMRVYCG PSPSCLVQSS SLSNAHIDYT TKPAIIFRIA ARNEKGYGPA TQVRWLQETS KDSSGT

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

LACS Plot; CA

Referencing offset: -0.08 ppm, Outliers: 3 Detail

LACS Plot; CB

Referencing offset: -0.08 ppm, Outliers: 3 Detail

LACS Plot; HA

Referencing offset: -0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Referencing offset: -0.24 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2M26, Strand ID: A Detail

Release date

2013-02-14

Citation

NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS
Serrano, P., Wuthrich, K.
Not known

Related entities 1. C-terminal domain of the protein HCFC1, : 1 : 7 : 58 entities Detail

Interaction partners 1. C-terminal domain of the protein HCFC1, : 11 interactors Detail

More details for 11 interactors identified by 4 citations

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

2 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

3 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

4 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

5 4D APSY HACANH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

6 5D APSY CBCACONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

7 5D APSY HACACONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		1.2 mM
2	sodium chloride	natural abundance		50 mM
3	sodium phosphate	natural abundance		20 mM
4	sodium azide	natural abundance		5 mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18901_2m26.nef
Input source #2: Coordindates	2m26.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
GCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQASGEPKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQASGEPKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIA

-------110-------120------
ARNEKGYGPATQVRWLQETSKDSSGT
||||||||||||||||||||||||||
ARNEKGYGPATQVRWLQETSKDSSGT

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	126	0	0	100.0

Content subtype: combined_18901_2m26.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1191		90.5 (chain: A, length: 126)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1687 (1)	noe	90.5 (chain: A, length: 126)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 126, Sequence coverage: 90.5%
- Total number of assignments
  - ¹H chemical shifts: 616
  - ¹³C chemical shifts: 464
  - ¹⁵N chemical shifts: 111
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 126, Sequence coverage: 90.5%
- Total number of restraints: 1687
- Weight of restraints: 1.0 (1687)
- Potential type of restraints: upper-bound-parabolic (1687)
- Range of distance target values: 2.48, 5.5 (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 HCFC1, JCSG, PSI:Biology