BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	90.1 % (1279 of 1420)	90.0 % (665 of 739)	89.2 % (485 of 544)	94.2 % (129 of 137)
Backbone	95.4 % (691 of 724)	96.4 % (243 of 252)	94.1 % (333 of 354)	97.5 % (115 of 118)
Sidechain	85.7 % (691 of 806)	86.7 % (422 of 487)	85.0 % (255 of 300)	73.7 % (14 of 19)
Aromatic	52.7 % (58 of 110)	60.0 % (33 of 55)	44.4 % (24 of 54)	100.0 % (1 of 1)
Methyl	97.0 % (128 of 132)	95.5 % (63 of 66)	98.5 % (65 of 66)

1. entity 1

GSDEEVDSVL FGSLRGHVVG LRYYTGVVNN NEMVALQRDP NNPYDKNAIK VNNVNGNQVG HLKKELAGAL AYIMDNKLAQ IEGVVPFGAN NAFTMPLHMT FWGKEENRKA VSDQLKKHGF KL

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 1 mM [U-99% 13C; U-99% 15N] HLTF HIRAN domain, 20 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

LACS Plot; CA

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

Referencing offset: -1.08 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -1.08 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.31 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.48 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5K5F, Strand ID: A Detail

Release date

2016-06-05

Citation

Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins
Korzhnev, D.M., Neculai, D., Dhe-Paganon, S., Arrowsmith, C.H., Bezsonova, I.
J. Biomol. NMR (2016), 66, 209-219, PubMed 27771863 , DOI 10.1007/s10858-016-0070-9 , Abstract

Related entities 1. Helicase-like transcription factor (E.C.3.6.4.-,6.3.2.-), : 1 : 1 : 6 : 11 entities Detail

Interaction partners 1. Helicase-like transcription factor (E.C.3.6.4.-,6.3.2.-), : 30 interactors Detail

More details for 30 interactors identified by 14 citations

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Agilent VNMRS - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 1 mM [U-99% 13C; U-99% 15N] HLTF HIRAN domain, 20 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

2 2D 1H-13C HSQC aliphatic

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

3 3D HNCO

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

4 3D HNCA

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

5 3D HN(CO)CA

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

6 3D 1H-13C NOESY

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

7 3D 1H-15N NOESY

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

8 3D CCH-TOCSY

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

9 3D HCCH-TOCSY

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

10 3D CBCA(CO)NH

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

11 3D 1H-13C NOESY aromatic

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

12 3D HBHA(CO)NH

Instrument

Agilent VNMRS - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HLTF HIRAN domain	[U-99% 13C; U-99% 15N]	1 mM
2	sodium chloride	natural abundance	100 mM
3	sodium phosphate	natural abundance	20 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30098_5k5f.nef
Input source #2: Coordindates	5k5f.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

50-------60--------70--------80--------90-------100-------110-------120-------130-------140-------15
GSDEEVDSVLFGSLRGHVVGLRYYTGVVNNNEMVALQRDPNNPYDKNAIKVNNVNGNQVGHLKKELAGALAYIMDNKLAQIEGVVPFGANNAFTMPLHMT
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSDEEVDSVLFGSLRGHVVGLRYYTGVVNNNEMVALQRDPNNPYDKNAIKVNNVNGNQVGHLKKELAGALAYIMDNKLAQIEGVVPFGANNAFTMPLHMT
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

0-------160-------170-
FWGKEENRKAVSDQLKKHGFKL
||||||||||||||||||||||
FWGKEENRKAVSDQLKKHGFKL
-------110-------120--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	122	0	0	100.0

Content subtype: combined_30098_5k5f.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1286		99.2 (chain: A, length: 122)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3273 (1)	noe	98.4 (chain: A, length: 122)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	40 (1)	hbond	19.7 (chain: A, length: 122)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	192 (192)	.	95.9 (chain: A, length: 122)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 122, Sequence coverage: 99.2%
- Total number of assignments
  - ¹H chemical shifts: 670
  - ¹³C chemical shifts: 487
  - ¹⁵N chemical shifts: 129
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	739	670	90.7
¹³C chemical shifts	544	487	89.5
¹⁵N chemical shifts	141	129	91.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	252	245	97.2
¹³C chemical shifts	244	231	94.7
¹⁵N chemical shifts	118	115	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	487	425	87.3
¹³C chemical shifts	300	256	85.3
¹⁵N chemical shifts	23	14	60.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	70	69	98.6
¹³C chemical shifts	70	69	98.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	33	60.0
¹³C chemical shifts	54	24	44.4
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: 122, Sequence coverage: 98.4%
- Total number of restraints: 3273
- Weight of restraints: 1.0 (3273)
- Potential type of restraints: square-well-parabolic (3273)
- Range of distance target values: 2.25, 3.9 (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
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 122, Sequence coverage: 19.7%
  - Total number of restraints: 40
  - Weight of restraints: 1.0 (40)
  - Potential type of restraints: square-well-parabolic (40)
  - Range of distance target values: 2.05, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - 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: 122, Sequence coverage: 95.9%
- Total number of restraints: 192
- Total number of restraints per polymer type: 192
- Weight of restraints: 1.0 (192)
- Potential type of restraints: square-well-parabolic (192)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DNA replication, DNA-binding, PSI-Biology, Protein Structure Initiative, SGC, Structural Genomics, Structural Genomics Consortium

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Found 1 Document (2.018 seconds)

BMRB: 30098

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Helicase-like transcription factor (E.C.3.6.4.-,6.3.2.-), : 1 : 1 : 6 : 11 entities Detail

Interaction partners 1. Helicase-like transcription factor (E.C.3.6.4.-,6.3.2.-), : 30 interactors Detail

Experiments performed 12 experiments Detail

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NMR combined restraints 5 contents Detail