BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	90.6 % (1138 of 1256)	91.8 % (593 of 646)	89.1 % (442 of 496)	90.4 % (103 of 114)
Backbone	94.4 % (606 of 642)	94.1 % (207 of 220)	94.6 % (300 of 317)	94.3 % (99 of 105)
Sidechain	87.6 % (626 of 715)	90.6 % (386 of 426)	84.3 % (236 of 280)	44.4 % (4 of 9)
Aromatic	65.2 % (90 of 138)	78.3 % (54 of 69)	50.7 % (34 of 67)	100.0 % (2 of 2)
Methyl	99.1 % (107 of 108)	100.0 % (54 of 54)	98.1 % (53 of 54)

1. Ubiquitin-Binding Motif

MQYKLILNGK TLKGETTTEA VDAATAEKVF KQYANDNGVD GEWTYDDATK TFTVTEGSDE KITFPSDIDP QVFYELPEAV QKELLAEWKR TGSDFHIGHK LEHHHHHH

Show sample condition

Sample

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Type	Concentration
1	UBM2	[U-100% 13C; U-100% 15N]		1.0 ~ 4.0 mM
2	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: -0.02 ppm, Outliers: 3 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: -0.02 ppm, Outliers: 3 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: 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: -0.03 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 25 models in PDB: 2KHU, Strand ID: A Detail

Release date

2010-06-14

Citation

Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1
Bomar, M.G., Bienko, S., Dikic, M., Walker, I., Zhou, G.C.
Mol. Cell (2010), 37, 408-417, PubMed 20159559 , DOI 10.1016/j.molcel.2009.12.038 , Abstract

Related entities 1. Ubiquitin-Binding Motif, : 1 : 1 : 8 entities Detail

Experiments performed 8 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_16882_2khu.nef
Input source #2: Coordindates	2khu.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
MQYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEGSDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MQYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEGSDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK

--------
LEHHHHHH
||||||||
LEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	108	0	0	100.0

Content subtype: combined_16882_2khu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1124		95.4 (chain: A, length: 108)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1090 (1)	noe	41.7 (chain: A, length: 108)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	17 (1)	hbond	21.3 (chain: A, length: 108)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	80 (80)	.	34.3 (chain: A, length: 108)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_5	OK	98 (98)	.	30.6 (chain: A, length: 108)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 95.4%
- Total number of assignments
  - ¹H chemical shifts: 586
  - ¹³C chemical shifts: 435
  - ¹⁵N chemical shifts: 103
- Completeness of assignments
  - Entity_assemble_ID: A
- 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)
96	HIS	HD1	7.012
99	HIS	HD1	6.97

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	646	584	90.4
¹³C chemical shifts	496	435	87.7
¹⁵N chemical shifts	115	103	89.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	220	209	95.0
¹³C chemical shifts	216	206	95.4
¹⁵N chemical shifts	105	99	94.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	426	375	88.0
¹³C chemical shifts	280	229	81.8
¹⁵N chemical shifts	10	4	40.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	54	98.2
¹³C chemical shifts	55	53	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	52	75.4
¹³C chemical shifts	67	31	46.3
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 41.7%
- Total number of restraints: 1087
- Weight of restraints: 1.0 (1087)
- Potential type of restraints: square-well-parabolic (1087)
- Range of distance target values: 2.0, 4.25 (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_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 21.3%
  - Total number of restraints: 17
  - Weight of restraints: 1.0 (17)
  - Potential type of restraints: square-well-parabolic (17)
  - Range of distance target values: 2.0, 2.75 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 34.3%
- Total number of restraints: 80
- Total number of restraints per polymer type: 80
- Weight of restraints: 1.0 (80)
- Potential type of restraints: square-well-parabolic (80)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 30.6%
- Total number of restraints: 98
- Potential type of restraints: undefined (98)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue

Keywords TLS, UBM, polymerase iota, translesion synthesis, ubiquitin-binding domain

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Found 1 Document (0.766 seconds)

BMRB: 16882

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Ubiquitin-Binding Motif, : 1 : 1 : 8 entities Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 6 contents Detail