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BMRB: 16236

2KHC

Bruno RRM3+

Authors

Lyon, A.M., Reveal, B.S., Macdonald, P.M., Hoffman, D.W.

Assembly

Bruno RRM3+

Entity

1. Bruno RRM3+ (polymer, Thiol state: all free), 118 monomers, 12284.92 Da Detail

AAGLPQFGSA SALSTSPLAS VALSAAAAAA AGKQIEGPEG CNLFIYHLPQ EFTDTDLAST FLPFGNVISA KVFIDKQTSL SKCFGFVSFD NPDSAQVAIK AMNGFQVGTK RLKVQLKK

Formula weight

12284.92 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS41:SG	1:CYS83:SG

Source organism

Drosophila melanogaster

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.3 %, Completeness: 91.8 %, Completeness (bb): 97.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.8 % (1215 of 1323)	96.2 % (652 of 678)	84.7 % (442 of 522)	98.4 % (121 of 123)
Backbone	97.6 % (679 of 696)	97.9 % (234 of 239)	97.1 % (335 of 345)	98.2 % (110 of 112)
Sidechain	87.4 % (643 of 736)	95.2 % (418 of 439)	74.8 % (214 of 286)	100.0 % (11 of 11)
Aromatic	51.8 % (58 of 112)	98.2 % (55 of 56)	5.4 % (3 of 56)
Methyl	94.3 % (132 of 140)	94.3 % (66 of 70)	94.3 % (66 of 70)

1. Bruno RRM3+

AAGLPQFGSA SALSTSPLAS VALSAAAAAA AGKQIEGPEG CNLFIYHLPQ EFTDTDLAST FLPFGNVISA KVFIDKQTSL SKCFGFVSFD NPDSAQVAIK AMNGFQVGTK RLKVQLKK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1.0 atm, Temperature 298 K, pH 6

#	Name	Isotope labeling	Concentration
1	1,0 mM Bruno RRM3+	[U-100% 13C; U-100% 15N]	1 mM
2	potassium phosphate	natural abundance	1 mM
3	sodium chloride	natural abundance	300.0 ~ 400.0 mM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

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

Referencing offset: -0.01 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

Referencing offset: -0.01 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

Referencing offset: -0.08 ppm, Outliers: 1 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

Referencing offset: 1.08 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2KHC, Strand ID: A Detail

Release date

2009-11-22

Citation

Bruno protein contains an expanded RNA recognition motif
Lyon, A.M., Reveal, B.S., Macdonald, P.M., Hoffman, D.W.
Biochemistry (2009), 48, 12202-12212, PubMed 19919093 , DOI 10.1021/bi900624j , Abstract

Related entities 1. Bruno RRM3+, : 1 : 1 : 54 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16236_2khc.nef
Input source #2: Coordindates	2khc.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

480-----490-------500-------510-------520-------530-------540-------550-------560-------570-------58
AAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
AAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIK
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

0-------590-------
AMNGFQVGTKRLKVQLKK
||||||||||||||||||
AMNGFQVGTKRLKVQLKK
-------110--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	118	0	0	100.0

Content subtype: combined_16236_2khc.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1199		95.8 (chain: A, length: 118)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	2463 (1)	noe	83.9 (chain: A, length: 118)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	132 (1)	hbond	34.7 (chain: A, length: 118)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	223 (223)	.	98.3 (chain: A, length: 118)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 118, Sequence coverage: 95.8%

480-----490-------500-------510-------520-------530-------540-------550-------560-------570-------58
AAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIK
||||||||||||||||    ||| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
AAGLPQFGSASALSTS....VAL.AAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIK

0-------590-------
AMNGFQVGTKRLKVQLKK
||||||||||||||||||
AMNGFQVGTKRLKVQLKK

Total number of assignments
- ¹H chemical shifts: 650
- ¹³C chemical shifts: 432
- ¹⁵N chemical shifts: 117

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
485	GLN	CD	180.0
513	GLN	CD	179.1
521	ASN	CG	176.2
526	HIS	HD1	7.44
526	HIS	HE2	7.67
545	ASN	CG	174.9
557	THR	HG1	4.36
570	ASN	CG	176.5
582	ASN	CG	176.1
590	ARG	HH11	6.98
590	ARG	HH12	6.98
590	ARG	HH21	7.04
590	ARG	HH22	7.04

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	678	643	94.8
¹³C chemical shifts	522	426	81.6
¹⁵N chemical shifts	124	117	94.4

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	239	228	95.4
¹³C chemical shifts	236	221	93.6
¹⁵N chemical shifts	112	106	94.6

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	439	415	94.5
¹³C chemical shifts	286	205	71.7
¹⁵N chemical shifts	12	11	91.7

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	71	66	93.0
¹³C chemical shifts	71	65	91.5

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	55	98.2
¹³C chemical shifts	56	0	0.0

Redox state of CYS
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: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 118, Sequence coverage: 83.9%
- Total number of restraints: 2434
- Weight of restraints: 1.0 (2434)
- Potential type of restraints: square-well-parabolic (2434)
- Range of distance target values: 1.75, 4.7 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 118, Sequence coverage: 34.7%
  - Total number of restraints: 132
  - Weight of restraints: 1.0 (132)
  - Potential type of restraints: square-well-parabolic (132)
  - Range of distance target values: 2.15, 4.35 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 118, Sequence coverage: 98.3%
- Total number of restraints: 223
- Total number of restraints per polymer type: 223
- Weight of restraints: 1.0 (223)
- Potential type of restraints: square-well-parabolic (223)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Bruno, RNA Recognition Motif, RRM

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Found 1 Document (0.7 seconds)

BMRB: 16236

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Bruno RRM3+, : 1 : 1 : 54 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail