BMRBj - BMREntryMaster

Found 1 Document (4.505 seconds)

BMRB: 6535

1TBD

'Backbone 1H and 15N Chemical Shift Assignments for T antigen origin binding domain in the presence of RPA32C'

Authors

Arunkumar, A.I., Chazin, W.J.

Assembly

Tag-OBD (131-259) - RPA32C complex

Entity

1. Tag-OBD (polymer, Thiol state: all free), 131 monomers, 15089.17 Da Detail

GSKVEDPKDF PSELLSFLSH AVFSNRTLAC FAIYTTKEKA ALLYKKIMEK YSVTFISRHN SYNHNILFFL TPHRHRVSAI NNYAQKLCTF SFLICKGVNK EYLMYSALTR DPFSVIEESL PGGLKEHDFN P

2. RPA32 C-terminal domain (polymer, Thiol state: all free), 69 monomers, 7642.418 Da Detail

ANGLTVAQNQ VLNLIKACPR PEGLNFQDLK NQLKHMSVSS IKQAVDFLSN EGHIYSTVDD DHFKSTDAE

Total weight

22731.588 Da

Max. entity weight

15089.17 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

Rigid body docking, Semi-flexible simulated annealing, Refinement using explicit water

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 83.5 %, Completeness: 26.3 %, Completeness (bb): 58.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	26.3 % (381 of 1449)	17.2 % (213 of 1237)	79.2 % (168 of 212)
Backbone	58.2 % (344 of 591)	44.4 % (177 of 399)	87.0 % (167 of 192)
Sidechain	4.5 % (39 of 858)	4.5 % (38 of 838)	5.0 % (1 of 20)
Aromatic	0.0 % (0 of 120)	0.0 % (0 of 120)
Methyl	4.7 % (5 of 107)	4.7 % (5 of 107)

1. Tag-OBD

GSKVEDPKDF PSELLSFLSH AVFSNRTLAC FAIYTTKEKA ALLYKKIMEK YSVTFISRHN SYNHNILFFL TPHRHRVSAI NNYAQKLCTF SFLICKGVNK EYLMYSALTR DPFSVIEESL PGGLKEHDFN P

2. RPA32 C-terminal domain

ANGLTVAQNQ VLNLIKACPR PEGLNFQDLK NQLKHMSVSS IKQAVDFLSN EGHIYSTVDD DHFKSTDAE

Show sample condition

Sample

Temperature 298 (±2) K, pH 7.0 (±0.02)

#	Name	Isotope labeling	Concentration
1	Tag-OBD	[U-15N]	0.2 mM
2	RPA32 C-terminal domain	unlabeled	0.6 mM
3	Tris	2H	20 mM
4	MgCl2		5 mM
5	DTT		2 mM

Chem. Shift Complete2

Sequence coverage: 33.5 %, Completeness: 18.5 %, Completeness (bb): 40.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	18.5 % (535 of 2898)	12.2 % (302 of 2474)	55.0 % (233 of 424)
Backbone	40.6 % (480 of 1182)	31.1 % (248 of 798)	60.4 % (232 of 384)
Sidechain	3.3 % (57 of 1716)	3.3 % (56 of 1676)	2.5 % (1 of 40)
Aromatic	0.0 % (0 of 240)	0.0 % (0 of 240)
Methyl	4.2 % (9 of 214)	4.2 % (9 of 214)

1. Tag-OBD

GSKVEDPKDF PSELLSFLSH AVFSNRTLAC FAIYTTKEKA ALLYKKIMEK YSVTFISRHN SYNHNILFFL TPHRHRVSAI NNYAQKLCTF SFLICKGVNK EYLMYSALTR DPFSVIEESL PGGLKEHDFN P

2. RPA32 C-terminal domain

ANGLTVAQNQ VLNLIKACPR PEGLNFQDLK NQLKHMSVSS IKQAVDFLSN EGHIYSTVDD DHFKSTDAE

Show sample condition

Sample

Temperature 298 (±2) K, pH 7.0 (±0.02)

#	Name	Isotope labeling	Concentration
6	Tag-OBD	unlabeled	0.2 mM
7	RPA32 C-terminal domain	[U-15N]	0.6 mM
8	Tris	2H	20 mM
9	MgCl2		5 mM
10	DTT		2 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 1Z1D, Strand ID: A, B Detail

Release date

2005-09-27

Citation

Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome
Arunkumar, A.I., Klimovich, V., Jiang, X., Ott, R.D., Mizoue, L., Fanning, E., Chazin, W.J.
Nat. Struct. Mol. Biol. (2005), 12, 332-339, PubMed 15793585 , DOI 10.1038/nsmb916 , Abstract

Related entities 1. Tag-OBD, : 1 : 5 : 10 : 21 entities Detail

Related entities 2. RPA32 C-terminal domain, : 7 : 1 : 1 : 21 entities Detail

Interaction partners 1. Tag-OBD, : 64 : 1 interactors Detail

More details for 65 interactors identified by 24 citations

Interaction partners 2. RPA32 C-terminal domain, : 93 : 1 interactors Detail

More details for 94 interactors identified by 29 citations

Experiments performed 1 experiments Detail

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6535_3.str
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

Content subtype: bmr6535_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	330	82.4 (chain: 1, length: 131), 82.6 (chain: 2, length: 69)
2	Assigned chemical shifts	chem_shift_list_2	OK	114	82.6 (chain: 2, length: 69)
1	Chemical shift references	chemical_shift_referencing	OK	2	No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 131, Sequence coverage: 82.4%
  - Entity_assembly_ID: 2, Chain length: 69, Sequence coverage: 82.6%
- Total number of assignments
  - ¹H chemical shifts: 165
  - ¹⁵N chemical shifts: 165
- Completeness of assignments
  - Entity_assemble_ID: 1
  - Entity_assemble_ID: 2
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
  - Chain_ID: 2
Saveframe: chem_shift_list_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 69, Sequence coverage: 82.6%
- Total number of assignments
  - ¹H chemical shifts: 57
  - ¹⁵N chemical shifts: 57
- Completeness of assignments
  - Entity_assemble_ID: 2
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	827	108	13.1
¹⁵N chemical shifts	139	108	77.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	260	108	41.5
¹⁵N chemical shifts	125	108	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	567	0	0.0
¹⁵N chemical shifts	14	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	95	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	410	57	13.9
¹⁵N chemical shifts	79	57	72.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	139	57	41.0
¹⁵N chemical shifts	67	57	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	271	0	0.0
¹⁵N chemical shifts	12	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	410	57	13.9
¹⁵N chemical shifts	79	57	72.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	139	57	41.0
¹⁵N chemical shifts	67	57	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	271	0	0.0
¹⁵N chemical shifts	12	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	0	0.0

Keywords DNA replication, NMR, NMR derived structural model

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Found 1 Document (4.505 seconds)

BMRB: 6535

Sample

Sample

Related entities 1. Tag-OBD, : 1 : 5 : 10 : 21 entities Detail

Related entities 2. RPA32 C-terminal domain, : 7 : 1 : 1 : 21 entities Detail

Interaction partners 1. Tag-OBD, : 64 : 1 interactors Detail

Interaction partners 2. RPA32 C-terminal domain, : 93 : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 5 contents Detail