BMRBj - BMREntryMaster

Found 1 Document (2.472 seconds)

BMRB: 6944

2G2K

Resonance assignment for the N-terminal region of eukaryotic initiation factor 5 (eIF5)

Authors

Conte, M.R., Kelly, G., Babon, J., Proud, C.G.

Assembly

eIF5(1-170)

Entity

1. Protein (polymer, Thiol state: free and other bound), 170 monomers, 19195.80 Da Detail

LSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN

2. ZN (non-polymer), 65.409 Da

Total weight

19261.209 Da

Max. entity weight

19195.8 Da

Entity Connection

na 4 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS99:SG	2:ZN1:ZN
2	na	sing	1:CYS102:SG	2:ZN1:ZN
3	na	sing	1:CYS122:SG	2:ZN1:ZN
4	na	sing	1:CYS125:SG	2:ZN1:ZN

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.5 %, Completeness: 72.4 %, Completeness (bb): 85.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	72.4 % (1464 of 2022)	66.9 % (716 of 1071)	77.4 % (596 of 770)	84.0 % (152 of 181)
Backbone	85.8 % (860 of 1002)	82.0 % (282 of 344)	86.9 % (432 of 497)	90.7 % (146 of 161)
Sidechain	62.3 % (733 of 1177)	59.7 % (434 of 727)	68.1 % (293 of 430)	30.0 % (6 of 20)
Aromatic	56.5 % (70 of 124)	56.5 % (35 of 62)	56.5 % (35 of 62)
Methyl	85.3 % (128 of 150)	85.3 % (64 of 75)	85.3 % (64 of 75)

1. Protein

LSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN

Show sample condition

Sample

Temperature 298 (±0.05) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	eIF5(1-170)	[U-13C; U-15N]	0.5 mM
2	sodium phosphate		20 mM
3	DTT		2 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
³¹P	DSS	methyl protons	null	indirect	0.4048086

Referencing offset: -0.34 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
³¹P	DSS	methyl protons	null	indirect	0.4048086

Referencing offset: -0.34 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
³¹P	DSS	methyl protons	null	indirect	0.4048086

Referencing offset: -0.07 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
³¹P	DSS	methyl protons	null	indirect	0.4048086

Referencing offset: 0.31 ppm, Outliers: 1 Detail

Release date

2006-08-10

Citation

Resonance assignment for the N-terminal region of the eukaryotic initiation factor 5 (eIF5)
Conte, M.R., Kelly, G., Babon, J., Proud, C.G.
J. Biomol. NMR (2006), 36 Suppl 1, 42-42, PubMed 16738784 , DOI 10.1007/s10858-006-9014-0 , Abstract

Related entities 1. Protein, : 1 : 3 : 45 entities Detail

Interaction partners 1. Protein, : 11 interactors Detail

More details for 11 interactors identified by 10 citations

Experiments performed 9 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6944_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)
1:99:CYS:SG	2:1:ZN:ZN	reduced, CA 57.934, CB 28.2 ppm	unknown	n/a
1:102:CYS:SG	2:1:ZN:ZN	oxidized 12.8%, reduced 87.2%, CA 58.82, CB 32.331 ppm	unknown	n/a
1:122:CYS:SG	2:1:ZN:ZN	oxidized 92.5%, reduced 7.5%, CA 58.486, CB 34.987 ppm	unknown	n/a
1:125:CYS:SG	2:1:ZN:ZN	oxidized 18.3%, reduced 81.7%, CA 58.82, CB 32.626 ppm	unknown	n/a

Non-standard residues

None

Content subtype: bmr6944_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	1521		91.8 (chain: 1, length: 170)
1	Chemical shift references	chemical_shift_referencing	OK	4		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 170, Sequence coverage: 91.8%
- Total number of assignments
  - ¹³C chemical shifts: 567
  - ¹H chemical shifts: 806
  - ¹⁵N chemical shifts: 148
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	770	567	73.6
¹H chemical shifts	1071	672	62.7
¹⁵N chemical shifts	188	148	78.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	340	294	86.5
¹H chemical shifts	344	273	79.4
¹⁵N chemical shifts	161	144	89.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	430	273	63.5
¹H chemical shifts	727	399	54.9
¹⁵N chemical shifts	27	4	14.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	79	67	84.8
¹H chemical shifts	79	67	84.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	62	31	50.0
¹H chemical shifts	62	31	50.0

Keywords NMR structure

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Found 1 Document (2.472 seconds)

BMRB: 6944

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Protein, : 1 : 3 : 45 entities Detail

Interaction partners 1. Protein, : 11 interactors Detail

Experiments performed 9 experiments Detail

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Chemical shift validation 4 contents Detail