BMRBj - BMREntryMaster

Found 1 Document (1.652 seconds)

BMRB: 5539

1PM6

Solution Structure and Stability of the Full-Length Excisionase (Xis) from Bacteriophage HK022

Authors

Rogov, V., Luecke, C., Muresanu, L., Wienk, H., Kleinhaus, I., Werner, K., Loehr, F., Pristovsek, P., Rueterjans, H.

Assembly

Xis C28S

Entity

1. Xis C28S (polymer, Thiol state: not present), 72 monomers, 8618.899 Da Detail

MYLTLQEWNA RQRRPRSLET VRRWVRESRI FPPPVKDGRE YLFHESAVKV DLNRPVTGSL LKRIRNGKKA KS

Formula weight

8618.899 Da

Entity Connection

covalent 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	covalent	sing	0:ASN66:ND2	1:GLY67:C

Source organism

Escherichia virus HK022

Exptl. method

NMR

Refine. method

energy minimization

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 94.1 %, Completeness (bb): 99.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	94.1 % (852 of 905)	96.7 % (469 of 485)	89.9 % (311 of 346)	97.3 % (72 of 74)
Backbone	99.1 % (418 of 422)	99.3 % (141 of 142)	99.1 % (211 of 213)	98.5 % (66 of 67)
Sidechain	91.1 % (503 of 552)	95.6 % (328 of 343)	83.7 % (169 of 202)	85.7 % (6 of 7)
Aromatic	53.1 % (34 of 64)	100.0 % (32 of 32)	0.0 % (0 of 30)	100.0 % (2 of 2)
Methyl	100.0 % (72 of 72)	100.0 % (36 of 36)	100.0 % (36 of 36)

1. excisionase

MYLTLQEWNA RQRRPRSLET VRRWVRESRI FPPPVKDGRE YLFHESAVKV DLNRPVTGSL LKRIRNGKKA KS

Show sample condition

Sample

Temperature 303 (±0.1) K, pH 6.5 (±0.3)

#	Name	Isotope labeling	Type	Concentration
1	excisionase	[U-99% 13C; U-99% 15N]		0.8 ~ 1.2 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: -0.08 ppm, Outliers: 2 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: -0.08 ppm, Outliers: 2 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: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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: 0.06 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1PM6, Strand ID: A Detail

Release date

2004-02-13

Citation

Solution structure and stability of the full-length excisionase from bacteriophage HK022
Rogov, V.V., Luecke, C., Muresanu, L., Wienk, H., Kleinhaus, I., Werner, K., Loehr, F., Pristovsek, P., Rueterjans, H.
Eur. J. Biochem. (2003), 270, 4846-4858, PubMed 14653811 , DOI: , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P68927 released on 2005-02-01
Title VXIS_BPHK0 Entity Excisionase

Related entities 1. Xis C28S, : 1 : 2 : 5 entities Detail

Interaction partners 1. Xis C28S, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5539_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	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)
1:66:ASN:ND2	1:67:GLY:C	unknown	unknown	n/a

Non-standard residues

None

Content subtype: bmr5539_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	set_1	Warning	922		100.0 (chain: 1, length: 72)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 72, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 541
  - ¹³C chemical shifts: 309
  - ¹⁵N chemical shifts: 72
- 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

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Found 1 Document (1.652 seconds)

BMRB: 5539

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. Xis C28S, : 1 : 2 : 5 entities Detail

Interaction partners 1. Xis C28S, : 1 interactors Detail

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	485	469	96.7
¹³C chemical shifts	346	309	89.3
¹⁵N chemical shifts	86	72	83.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	142	141	99.3
¹³C chemical shifts	144	142	98.6
¹⁵N chemical shifts	67	66	98.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	343	328	95.6
¹³C chemical shifts	202	167	82.7
¹⁵N chemical shifts	19	6	31.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	32	100.0
¹³C chemical shifts	30	0	0.0
¹⁵N chemical shifts	2	2	100.0