BMRBj - BMREntryMaster

Found 1 Document (1.889 seconds)

BMRB: 6019

1Y9X

Solution structure of Archaeon DNA-binding protein ssh10b P62A mutant

Authors

Cui, Q., Tong, Y., Wang, J.

Assembly

P62A dimer

Entity

1. P62A dimer (polymer, Thiol state: not present), 97 monomers, 10559.27 × 2 Da Detail

MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV DTVEIVRNRF LADKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK

Total weight

21118.54 Da

Max. entity weight

10559.27 Da

Source organism

Saccharolobus shibatae

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 80.4 %, Completeness (bb): 82.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.4 % (903 of 1123)	82.2 % (481 of 585)	75.5 % (329 of 436)	91.2 % (93 of 102)
Backbone	82.8 % (477 of 576)	95.9 % (189 of 197)	69.5 % (198 of 285)	95.7 % (90 of 94)
Sidechain	80.9 % (516 of 638)	75.3 % (292 of 388)	91.3 % (221 of 242)	37.5 % (3 of 8)
Aromatic	33.3 % (6 of 18)	55.6 % (5 of 9)	11.1 % (1 of 9)
Methyl	92.5 % (135 of 146)	93.2 % (68 of 73)	91.8 % (67 of 73)

1. P62A

MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV DTVEIVRNRF LADKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK

Show sample condition

Sample

Temperature 310 (±0.1) K, pH 5.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	P62A	[U-95% 13C; U-98% 15N]		1.5 mM

LACS Plot; CA

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

Referencing offset: -0.18 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.18 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: -0.19 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1Y9X, Strand ID: A, B Detail

Release date

2004-06-24

Citation 1

A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b
Fang, X., Cui, Q., Tong, Y., Feng, Y., Shan, L., Huang, L., Wang, J.
Biochemistry (2008), 47, 11212-11221, PubMed 18821773 , DOI 10.1021/bi8007593 , Abstract

Show more 2 citaions

Citation 2

Two conformations of archaeal Ssh10b. The origin of its temperature-dependent interaction with DNA
Cui, Q., Tong, Y., Xue, H., Huang, L., Feng, Y., Wang, J.
J. Biol. Chem. (2003), 278, 51015-51022, PubMed 14523014 , DOI 10.1074/jbc.M308510200 , Abstract

Citation 3

An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion
Xue, H., Guo, R., Wen, Y., Liu, D., Huang, L.
J. Bacteriol. (2000), 182, 3929-3933, PubMed 10869069 , DOI: , Abstract

Hide non-primary 2 citaions

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

  BMRB: 5226 released on 2002-12-26
    Title Letter to the Editor: 1H, 15N and 13C resonance assignments and secondary structure determination of the Ssh10b from Hyperthermphilic Archaeon Sulfolobus shibatae
  Swiss-Prot: P60848 released on 2004-04-13
    Title ALBA1_SULSH Entity DNA/RNA-binding protein Alba 1

Related entities 1. P62A dimer, : 1 : 5 : 43 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6019_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: bmr6019_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_C	Warning	1012		99.0 (chain: 1, length: 97)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_C
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 97, Sequence coverage: 99.0%
- Total number of assignments
  - ¹³C chemical shifts: 317
  - ¹⁵N chemical shifts: 92
  - ¹H chemical shifts: 603
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	194	96	49.5
¹⁵N chemical shifts	94	91	96.8
¹H chemical shifts	197	190	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	436	317	72.7
¹⁵N chemical shifts	110	92	83.6
¹H chemical shifts	585	465	79.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	242	221	91.3
¹⁵N chemical shifts	16	1	6.2
¹H chemical shifts	388	275	70.9

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Found 1 Document (1.889 seconds)

BMRB: 6019

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

Related entities 1. P62A dimer, : 1 : 5 : 43 entities Detail

Experiments performed 5 experiments Detail

Instrument

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Sample

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Chemical shift validation 3 contents Detail