BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	96.4 % (951 of 987)	97.5 % (497 of 510)	94.6 % (365 of 386)	97.8 % (89 of 91)
Backbone	99.0 % (509 of 514)	99.4 % (176 of 177)	98.8 % (249 of 252)	98.8 % (84 of 85)
Sidechain	94.2 % (521 of 553)	96.4 % (321 of 333)	91.1 % (195 of 214)	83.3 % (5 of 6)
Aromatic	47.8 % (22 of 46)	73.9 % (17 of 23)	21.7 % (5 of 23)
Methyl	99.1 % (109 of 110)	98.2 % (54 of 55)	100.0 % (55 of 55)

1. entity

HIEGRHMDLT ISNELTGEIY GPIEVSEDMA LTDLIALLQA DCGFDKTKHD LYYNMDILDS NRTQSLKELG LKTDDLLLIR GKISNS

Show sample condition

Sample

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

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	25 mM
2	sodium chloride	natural abundance	100 mM
3	entity	[U-13C; U-15N]	0.4 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: 2.22 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: 2.22 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: 0.01 ppm, Outliers: 4 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: 2.87 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 43 models in PDB: 2N7E, Strand ID: A Detail

Release date

2016-07-12

Citation

Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein
Klima, M., Toth, D.J., Hexnerova, R., Baumlova, A., Chalupska, D., Tykvart, J., Rezabkova, L., Sengupta, N., Man, P., Dubankova, A., Humpolickova, J., Nencka, R., Veverka, V., Balla, T., Boura, E.
Sci. Rep. (2016), 6, 23641-23641, PubMed 27009356 , DOI 10.1038/srep23641 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 25790 released on 2016-07-12
    Title Solution structure of regulatory protein
  BMRB: 25791 released on 2016-07-12
    Title Solution structure of kinase in complex with its regulatory protein

Related entities 1. UBL domain of the yeast DNA damage-inducible protein homolog 1, : 1 : 4 : 11 entities Detail

Interaction partners 1. UBL domain of the yeast DNA damage-inducible protein homolog 1, : 10 interactors Detail

More details for 10 interactors identified by 7 citations

Experiments performed 6 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25803_2n7e.nef
Input source #2: Coordindates	2n7e.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

---100-------110-------120-------130-------140-------150-------160-------170-------180
HIEGRHMDLTISNELTGEIYGPIEVSEDMALTDLIALLQADCGFDKTKHDLYYNMDILDSNRTQSLKELGLKTDDLLLIRGKISNS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
HIEGRHMDLTISNELTGEIYGPIEVSEDMALTDLIALLQADCGFDKTKHDLYYNMDILDSNRTQSLKELGLKTDDLLLIRGKISNS
--------10--------20--------30--------40--------50--------60--------70--------80------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	86	0	0	100.0

Content subtype: combined_25803_2n7e.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	949		100.0 (chain: A, length: 86)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2216 (1)	noe	98.8 (chain: A, length: 86)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	128 (128)	.	89.5 (chain: A, length: 86)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 500
  - ¹³C chemical shifts: 360
  - ¹⁵N chemical shifts: 89
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
104	THR	HG1	5.216
120	SER	HG	4.311
167	THR	HG1	4.477

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	510	497	97.5
¹³C chemical shifts	386	360	93.3
¹⁵N chemical shifts	94	89	94.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	177	176	99.4
¹³C chemical shifts	172	170	98.8
¹⁵N chemical shifts	85	84	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	333	321	96.4
¹³C chemical shifts	214	190	88.8
¹⁵N chemical shifts	9	5	55.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	57	98.3
¹³C chemical shifts	58	58	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	23	17	73.9
¹³C chemical shifts	23	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 98.8%
- Total number of restraints: 2216
- Weight of restraints: 1.0 (2216)
- Potential type of restraints: square-well-parabolic (2216)
- Range of distance target values: 1.23, 2.75 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 89.5%
- Total number of restraints: 128
- Total number of restraints per polymer type: 128
- Weight of restraints: 1.0 (128)
- Potential type of restraints: square-well-parabolic (128)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DDI1

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Found 1 Document (0.857 seconds)

BMRB: 25803

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. UBL domain of the yeast DNA damage-inducible protein homolog 1, : 1 : 4 : 11 entities Detail

Interaction partners 1. UBL domain of the yeast DNA damage-inducible protein homolog 1, : 10 interactors Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 4 contents Detail