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Found 1 Document (2.278 seconds)

BMRB: 30275

5VEY

Solution NMR structure of histone H2A-H2B mono-ubiquitylated at H2A Lys15 in complex with RNF169 (653-708)

Authors

Hu, Q., Botuyan, M.V., Cui, G., Mer, G.

Assembly

Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27)

Entity

1. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 1 (polymer, Thiol state: not present), 194 monomers, 21617.58 Da Detail

MHHHHHHMRK ESYSIYVYKV LKQVHPDTGI SSKAMGIMNS FVNDIFERIA GEASRLAHYN KRSTITSREI QTAVRLLLPG ELAKHAVSEG TKAVTKYTSS ASAKTRSSRA GLQFPVGRVH RLLRKGNYSE RVGAGAPVYL AAVLEYLTAE ILELAGNAAR DNKKTRIIPR HLQLAIRNDE ELNKLLGRVT IAQG

2. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 2 (polymer, Thiol state: not present), 76 monomers, 8564.731 Da Detail

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

3. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 3 (polymer, Thiol state: not present), 59 monomers, 7004.839 Da Detail

GHMDPVLREM EQKLQQEEED RQLALQLQRM FDNERRTVSR RKGSVDQYLL RSSNMAGAK

Total weight

37187.152 Da

Max. entity weight

21617.58 Da

Source organism

Mus musculus , Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.2 %, Completeness: 88.4 %, Completeness (bb): 93.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.4 % (3415 of 3864)	88.2 % (1787 of 2027)	87.4 % (1300 of 1487)	93.7 % (328 of 350)
Backbone	93.9 % (1836 of 1956)	95.4 % (640 of 671)	92.5 % (893 of 965)	94.7 % (303 of 320)
Sidechain	84.6 % (1874 of 2215)	84.6 % (1147 of 1356)	84.7 % (702 of 829)	83.3 % (25 of 30)
Aromatic	56.3 % (108 of 192)	74.0 % (71 of 96)	38.5 % (37 of 96)
Methyl	100.0 % (386 of 386)	100.0 % (193 of 193)	100.0 % (193 of 193)

1. entity 1

2. entity 2

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

3. entity 3

GHMDPVLREM EQKLQQEEED RQLALQLQRM FDNERRTVSR RKGSVDQYLL RSSNMAGAK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6, Details 1 mM Ubiquitylated H2A-H2B, 3 mM RNF169, 25 mM MES-Bis-TRIS, 50 mM KCl, 4 mM EDTA, 90% H2O/10% D2O.

#	Name	Isotope labeling	Concentration
1	EDTA	natural abundance	4 mM
2	KCl	natural abundance	50 mM
3	MES-Bis-TRIS	natural abundance	25 mM
4	RNF169	natural abundance	3 mM
5	Ubiquitylated H2A-H2B	natural abundance	1 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: -0.13 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: -0.13 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: -0.02 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: -0.03 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5VEY, Strand ID: A, B, C Detail

Release date

2017-05-08

Citation

Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18
Hu, Q., Botuyan, M.V., Cui, G., Zhao, D., Mer, G.
Mol. Cell (2017), 66, 473-487, PubMed 28506460 , DOI 10.1016/j.molcel.2017.04.009 , Abstract

Related entities 1. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 1, : 6 entities Detail

Related entities 2. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 2, : 92 : 6 : 47 : 182 entities Detail

Related entities 3. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 3, : 1 : 14 entities Detail

Interaction partners 3. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 3, : 6 interactors Detail

More details for 6 interactors identified by 3 citations

Experiments performed 1 experiments Detail

NMR combined restraints 8 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30275_5vey.nef
Input source #2: Coordindates	5vey.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:104:LYS:NZ	2:76:GLY:C	unknown	unknown	n/a

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
MHHHHHHMRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MHHHHHHMRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSS

-------110-------120-------130-------140-------150-------160-------170-------180-------190----
ASAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ASAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQG

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

--------10--------20--------30--------40--------50--------60--------70------
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG

Entity_assembly_ID (NMR): C vs Auth_asym_ID (model): C

650-----660-------670-------680-------690-------700--------
GHMDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSNMAGAK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GHMDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSNMAGAK
--------10--------20--------30--------40--------50---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	194	100.0
B	B	76	100.0
C	C	59	100.0

Content subtype: combined_30275_5vey.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	3338		94.3 (chain: A, length: 194), 100.0 (chain: B, length: 76), 94.9 (chain: C, length: 59)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3225 (1)	noe	94.3 (chain: A, length: 194)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	48 (1)	noe	2.1 (chain: A, length: 194)
3	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	279 (1)	noe	14.5 (chain: B, length: 76), 30.5 (chain: C, length: 59)
4	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	2474 (1)	noe	4.1 (chain: A, length: 194), 98.7 (chain: B, length: 76), 67.8 (chain: C, length: 59)
5	Distance restraints	CNS/XPLOR_distance_constraints_7	OK	294 (1)	hbond	54.6 (chain: A, length: 194), 71.1 (chain: B, length: 76), 47.5 (chain: C, length: 59)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_8	OK	412 (412)	.	80.4 (chain: A, length: 194), 82.9 (chain: B, length: 76), 49.2 (chain: C, length: 59)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 94.3%
  - Entity_assembly_ID: B, Chain length: 76, Sequence coverage: 100.0%
  - Entity_assembly_ID: C, Chain length: 59, Sequence coverage: 94.9%
- Total number of assignments
  - ¹H chemical shifts: 1750
  - ¹³C chemical shifts: 1269
  - ¹⁵N chemical shifts: 319
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
  - Entity_assemble_ID: C
- 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
  - Chain_ID: B
  - Chain_ID: C

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1167	940	80.5
¹³C chemical shifts	876	691	78.9
¹⁵N chemical shifts	219	186	84.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	396	370	93.4
¹³C chemical shifts	388	336	86.6
¹⁵N chemical shifts	189	175	92.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	771	570	73.9
¹³C chemical shifts	488	355	72.7
¹⁵N chemical shifts	30	11	36.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	124	121	97.6
¹³C chemical shifts	124	121	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	49	71.0
¹³C chemical shifts	69	13	18.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	478	465	97.3
¹³C chemical shifts	350	337	96.3
¹⁵N chemical shifts	85	73	85.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	155	147	94.8
¹³C chemical shifts	152	140	92.1
¹⁵N chemical shifts	73	65	89.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	323	318	98.5
¹³C chemical shifts	198	197	99.5
¹⁵N chemical shifts	12	8	66.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	49	98.0
¹³C chemical shifts	50	49	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	16	16	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	382	345	90.3
¹³C chemical shifts	261	240	92.0
¹⁵N chemical shifts	75	60	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	113	94.2
¹³C chemical shifts	118	108	91.5
¹⁵N chemical shifts	58	55	94.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	262	232	88.5
¹³C chemical shifts	143	132	92.3
¹⁵N chemical shifts	17	5	29.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	27	96.4
¹³C chemical shifts	28	27	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	4	36.4
¹³C chemical shifts	11	4	36.4

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 94.3%
- Total number of restraints: 3223
- Weight of restraints: 1.0 (3223)
- Potential type of restraints: square-well-parabolic (3223)
- Range of distance target values: 2.55, 4.65 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
  - Chain_ID: C
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 2.1%
  - Total number of restraints: 48
  - Weight of restraints: 1.0 (48)
  - Potential type of restraints: square-well-parabolic (48)
  - Range of distance target values: 2.4, 3.9 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
    - Chain_ID: C
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_5
    - Status: Warning
    - Experiment type: noe
    - Sequence coverage of experimental data
      - Entity_assembly_ID: B, Chain length: 76, Sequence coverage: 14.5%
      - Entity_assembly_ID: C, Chain length: 59, Sequence coverage: 30.5%
    - Total number of restraints: 278
    - Weight of restraints: 1.0 (278)
    - Potential type of restraints: square-well-parabolic (278)
    - Range of distance target values: 2.4, 3.9 (Å)
    - Histogram of distance target values
    - Histogram of discrepancy in distance target values
    - Distance restraints per residue
      - Chain_ID: A
        None
      - Chain_ID: B
      - Chain_ID: C
    - Distance restraints on contact map
    - Saveframe: CNS/XPLOR_distance_constraints_4
      - Status: Warning
      - Experiment type: noe
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 4.1%
        Entity_assembly_ID: B, Chain length: 76, Sequence coverage: 98.7%
        --------10--------20--------30--------40--------50--------60--------70------ MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG --------10--------20--------30--------40--------50--------60--------70-----
        Entity_assembly_ID: C, Chain length: 59, Sequence coverage: 67.8%
        650-----660-------670-------680-------690-------700-------- GHMDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSNMAGAK ||||||||||||||||||||||||||||||||||||| ||| GHMDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRT...........LLR 650-----660-------670-------680-------690-------700
      - Total number of restraints: 2470
        Intra-residue restraints, i = j : 479
        Sequential restraints, | i - j | = 1 : 661
        Backbone-backbone: 173
        Backbone-side chain: 402
        Side chain-side chain: 86
        Medium range restraints, 1 < | i - j | < 5 : 573
        Backbone-backbone: 175
        Backbone-side chain: 240
        Side chain-side chain: 158
        Long range restraints, | i - j | >= 5 : 694
        Inter-chain restraints: 9
        Symmetric restraints: 54
      - Weight of restraints: 1.0 (2470)
        Intra-residue restraints, i = j : 1.0 (479)
        Sequential restraints, | i - j | = 1 : 1.0 (661)
        Backbone-backbone: 1.0 (173)
        Backbone-side chain: 1.0 (402)
        Side chain-side chain: 1.0 (86)
        Medium range restraints, 1 < | i - j | < 5 : 1.0 (573)
        Backbone-backbone: 1.0 (175)
        Backbone-side chain: 1.0 (240)
        Side chain-side chain: 1.0 (158)
        Long range restraints, | i - j | >= 5 : 1.0 (694)
        Inter-chain restraints: 1.0 (9)
        Symmetric restraints: 1.0 (54)
      - Potential type of restraints: square-well-parabolic (2470)
        Intra-residue restraints, i = j : square-well-parabolic (479)
        Sequential restraints, | i - j | = 1 : square-well-parabolic (661)
        Backbone-backbone: square-well-parabolic (173)
        Backbone-side chain: square-well-parabolic (402)
        Side chain-side chain: square-well-parabolic (86)
        Medium range restraints, 1 < | i - j | < 5 : square-well-parabolic (573)
        Backbone-backbone: square-well-parabolic (175)
        Backbone-side chain: square-well-parabolic (240)
        Side chain-side chain: square-well-parabolic (158)
        Long range restraints, | i - j | >= 5 : square-well-parabolic (694)
        Inter-chain restraints: square-well-parabolic (9)
        Symmetric restraints: square-well-parabolic (54)
      - Range of distance target values: 2.4, 4.65 (Å)
      - Histogram of distance target values
      - Histogram of discrepancy in distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        Chain_ID: C
      - Distance restraints on contact map
        Chain_ID_1: B - Chain_ID_2: B
        Chain_ID_1: C - Chain_ID_2: C
        Chain_ID_1: B - Chain_ID_2: C
        None
      - Saveframe: CNS/XPLOR_distance_constraints_7
        Status: OK
        Experiment type: hbond
        Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 54.6%
        --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MHHHHHHMRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSS |||||||||| | | | ||||||||||||||||||||||||||| |||||||||||| || |||||||||| ............YSIYVYKVLK.V....G.S..AMGIMNSFVNDIFERIAGEASRLAHYN.....TSREIQTAVRLL....LA.HAVSEGTKAV...... --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 -------110-------120-------130-------140-------150-------160-------170-------180-------190---- ASAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQG |||||||||||||||||||||||| ||||||||||||| ||| || .................................AGAPVYLAAVLEYLTAEILELAGN.........IIPRHLQLAIRND.ELN.LL -------110-------120-------130-------140-------150-------160-------170-------180------
        Entity_assembly_ID: B, Chain length: 76, Sequence coverage: 71.1%
        --------10--------20--------30--------40--------50--------60--------70------ MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG ||||||| | | | ||| ||||||||||||||| || |||||| | ||| ||||||| || |||| | MQIFVKT...K.I.L.VEP.DTIENVKAKIQDKEG.PP.QQRLIF..K.LED.RTLSDYN...ES.LHLV.R --------10--------20--------30--------40--------50--------60--------70--
        Entity_assembly_ID: C, Chain length: 59, Sequence coverage: 47.5%
        Total number of restraints: 294
        Total hydrogen bond restraints: 294
        O...H-x: 124
        O...h-N: 124
        N...H-x: 1
        N...h_N: 1
        Long range: 44
        O...H-x: 22
        O...h-N: 22
        Weight of restraints: 1.0 (294)
        Total hydrogen bond restraints: 1.0 (294)
        O...H-x: 1.0 (124)
        O...h-N: 1.0 (124)
        N...H-x: 1.0 (1)
        N...h_N: 1.0 (1)
        Long range: 1.0 (44)
        O...H-x: 1.0 (22)
        O...h-N: 1.0 (22)
        Potential type of restraints: square-well-parabolic (294)
        Total hydrogen bond restraints: square-well-parabolic (294)
        O...H-x: square-well-parabolic (124)
        O...h-N: square-well-parabolic (124)
        N...H-x: square-well-parabolic (1)
        N...h_N: square-well-parabolic (1)
        Long range: square-well-parabolic (44)
        O...H-x: square-well-parabolic (22)
        O...h-N: square-well-parabolic (22)
        Range of distance target values: 2.05, 3.05 (Å)
        Histogram of distance target values
        Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        Chain_ID: C
        Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A
        Chain_ID_1: B - Chain_ID_2: B

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_8
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 194, Sequence coverage: 80.4%
  - Entity_assembly_ID: B, Chain length: 76, Sequence coverage: 82.9%
  - Entity_assembly_ID: C, Chain length: 59, Sequence coverage: 49.2%
- Total number of restraints: 412
- Total number of restraints per polymer type: 412
- Weight of restraints: 1.0 (412)
- Potential type of restraints: square-well-parabolic (412)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Complex, Nucleosome, TRANSFERASE, Ubiquitin, Ubiquitin ligase

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Found 1 Document (2.278 seconds)

BMRB: 30275

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 1, : 6 entities Detail

Related entities 2. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 2, : 92 : 6 : 47 : 182 entities Detail

Related entities 3. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 3, : 1 : 14 entities Detail

Interaction partners 3. Histone H2A, Polyubiquitin-B, E3 ubiquitin-protein ligase RNF169 (E.C.2.3.2.27), entity 3, : 6 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 8 contents Detail