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Found 1 Document (1.509 seconds)

BMRB: 5931

1O1W

Dynamics of the RNase H Domain of HIV-1 Reverse Transcriptase in the Presence of Magnesium and AMP

Authors

Pari, K., Mueller, G.A., DeRose, E.F., Kirby, T.W., London, R.E.

Assembly

RNase H domain of the HIV-1 reverse transcriptase

Entity

1. HIV-1 RNase H (polymer, Thiol state: not present), 138 monomers, 15260.14 × 3 Da Detail

MNELYQLEKE PIVGAETFYV DGAANRETKL GKAGYVTNRG RQKVVTLTDT TNQKTELQAI YLALQDSGLE VNIVTDSQYA LGIIQAQPDQ SESELVNQII EQLIKKEKVY LAWVPAHKGI GGNEQVDKLV SAGIRKVL

Total weight

45780.418 Da

Max. entity weight

15260.14 Da

Source organism

HIV-1 M:B_HXB2R

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 94.4 %, Completeness (bb): 96.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	94.4 % (1520 of 1610)	94.7 % (792 of 836)	93.7 % (580 of 619)	95.5 % (148 of 155)
Backbone	96.1 % (790 of 822)	96.5 % (274 of 284)	96.0 % (387 of 403)	95.6 % (129 of 135)
Sidechain	93.2 % (853 of 915)	93.8 % (518 of 552)	92.1 % (316 of 343)	95.0 % (19 of 20)
Aromatic	62.2 % (46 of 74)	62.2 % (23 of 37)	61.1 % (22 of 36)	100.0 % (1 of 1)
Methyl	97.3 % (183 of 188)	97.9 % (92 of 94)	96.8 % (91 of 94)

1. HIV-1 RNase H

MNELYQLEKE PIVGAETFYV DGAANRETKL GKAGYVTNRG RQKVVTLTDT TNQKTELQAI YLALQDSGLE VNIVTDSQYA LGIIQAQPDQ SESELVNQII EQLIKKEKVY LAWVPAHKGI GGNEQVDKLV SAGIRKVL

Show sample condition

Sample

Temperature 298 (±0.25) K, pH 6.8 (±0.01)

#	Name	Isotope labeling	Type	Concentration
1	HIV-1 RNase H			1.1 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: -0.12 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: -0.12 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: -0.09 ppm, Outliers: 2 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: 0.11 ppm, Outliers: 3 Detail

Release date

2004-04-06

Citation

Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
Pari, K., Mueller, G.A., DeRose, E.F., Kirby, T.W., London, R.E.
Biochemistry (2003), 42, 639-650, PubMed 12534276 , DOI 10.1021/bi0204894 , Abstract

Related entities 1. HIV-1 RNase H, : 1 : 1 : 94 : 116 entities Detail

Interaction partners 1. HIV-1 RNase H, : 5 interactors Detail

More details for 5 interactors identified by 4 citations

Experiments performed 10 experiments Detail

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5931_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: bmr5931_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1717		100.0 (chain: 1, length: 137)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 137, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 587
  - ¹H chemical shifts: 980
  - ¹⁵N chemical shifts: 150
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	614	587	95.6
¹H chemical shifts	829	796	96.0
¹⁵N chemical shifts	158	150	94.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	274	265	96.7
¹H chemical shifts	282	279	98.9
¹⁵N chemical shifts	134	132	98.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	340	322	94.7
¹H chemical shifts	547	517	94.5
¹⁵N chemical shifts	24	18	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	94	92	97.9
¹H chemical shifts	94	92	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	36	22	61.1
¹H chemical shifts	37	23	62.2
¹⁵N chemical shifts	1	1	100.0

Keywords HIV, Reverse Transcription, RNase H, NMR, Relaxation

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Found 1 Document (1.509 seconds)

BMRB: 5931

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. HIV-1 RNase H, : 1 : 1 : 94 : 116 entities Detail

Interaction partners 1. HIV-1 RNase H, : 5 interactors Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 5 contents Detail