BMRBj - BMREntryMaster

Found 1 Document (2.958 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

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (2.958 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

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail