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Found 1 Document (1.148 seconds)

BMRB: 25040

2MQN

Structural Investigation of hnRNP L

Authors

Blatter, M., Allain, F.

Assembly

most two C-terminal RNA Recognition Motif Domain of hnRNP L

Entity

1. most two C-terminal RNA Recognition Motif Domain of hnRNP L (polymer), 216 monomers, 24228.09 Da Detail

DYGPHADSPV LMVYGLDQSK MNCDRVFNVF CLYGNVEKVK FMKSKPGAAM VEMADGYAVD RAITHLNNNF MFGQKMNVCV SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN RFSTPEQAAK NRIQHPSNVL HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS SGLLEWDSKS DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS

Formula weight

24228.09 Da

Source organism

Rattus norvegicus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.6 %, Completeness: 77.8 %, Completeness (bb): 80.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	77.8 % (1954 of 2513)	83.9 % (1100 of 1311)	65.8 % (640 of 973)	93.4 % (214 of 229)
Backbone	80.4 % (1023 of 1272)	93.5 % (406 of 434)	65.3 % (414 of 634)	99.5 % (203 of 204)
Sidechain	77.3 % (1115 of 1443)	79.1 % (694 of 877)	75.8 % (410 of 541)	44.0 % (11 of 25)
Aromatic	48.8 % (121 of 248)	62.9 % (78 of 124)	34.1 % (42 of 123)	100.0 % (1 of 1)
Methyl	97.7 % (172 of 176)	96.6 % (85 of 88)	98.9 % (87 of 88)

1. entity

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303.15 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 15N]	0.5 ~ 0.7 mM
2	sodium chloride	natural abundance	200 mM
3	sodium phosphate	natural abundance	50 mM
4	DTT	natural abundance	1 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303.15 K, pH 6.5

#	Name	Isotope labeling	Concentration
7	entity	[U-100% 13C; U-100% 15N]	0.5 ~ 0.7 mM
8	sodium chloride	natural abundance	200 mM
9	sodium phosphate	natural abundance	50 mM
10	DTT	natural abundance	1 mM
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 303.15 K, pH 6.5

#	Name	Isotope labeling	Concentration
13	entity	[U-100% 15N]	0.5 ~ 0.7 mM
14	sodium chloride	natural abundance	200 mM
15	sodium phosphate	natural abundance	50 mM
16	DTT	natural abundance	1 mM
17	D2O	natural abundance	100 %

LACS Plot; CA

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

Referencing offset: 2.57 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 2.57 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.02 ppm, Outliers: 8 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MQN, Strand ID: A Detail

Release date

2015-05-03

Citation

The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein
Blatter, M., Allain, F.
J. Mol. Biol. (2015), 427, 3001-3022, PubMed 26051023 , DOI 10.1016/j.jmb.2015.05.020 , Abstract

Related entities 1. most two C-terminal RNA Recognition Motif Domain of hnRNP L, : 1 : 4 : 2 : 4 : 54 entities Detail

Interaction partners 1. most two C-terminal RNA Recognition Motif Domain of hnRNP L, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 5 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25040_2mqn.nef
Input source #2: Coordindates	2mqn.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

-------380-------390-------400-------410-------420-------430-------440-------450-------460-------470
DYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKMNVCVSKQPAIMPGQSYGLEDGSCS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKMNVCVSKQPAIMPGQSYGLEDGSCS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-------480-------490-------500-------510-------520-------530-------540-------550-------560-------570
YKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPTSVKVFSGKSERSSSGLLEWDSKSDALETLGFLNHYQMKNPNGP
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
YKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPTSVKVFSGKSERSSSGLLEWDSKSDALETLGFLNHYQMKNPNGP
-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200

-------580------
YPYTLKLCFSTAQHAS
||||||||||||||||
YPYTLKLCFSTAQHAS
-------210------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	216	0	0	100.0

Content subtype: combined_25040_2mqn.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1886		98.6 (chain: A, length: 216)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	6458 (1)	noe	97.7 (chain: A, length: 216)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	239 (1)	hbond	39.8 (chain: A, length: 216)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_4	OK	128 (128)	.	50.5 (chain: A, length: 216)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 1083
  - ¹³C chemical shifts: 587
  - ¹⁵N chemical shifts: 216
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1311	1081	82.5
¹³C chemical shifts	973	587	60.3
¹⁵N chemical shifts	236	216	91.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	434	402	92.6
¹³C chemical shifts	432	186	43.1
¹⁵N chemical shifts	204	203	99.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	877	679	77.4
¹³C chemical shifts	541	401	74.1
¹⁵N chemical shifts	32	13	40.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	97	95	97.9
¹³C chemical shifts	97	94	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	124	78	62.9
¹³C chemical shifts	123	42	34.1
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 97.7%
- Total number of restraints: 6424
- Weight of restraints: 1.0 (6424)
- Potential type of restraints: upper-bound-parabolic (6424)
- Range of distance target values: 3.08, 6.0 (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: DYANA/DIANA_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 39.8%
  - Total number of restraints: 239
  - Weight of restraints: 1.0 (239)
  - Potential type of restraints: upper-bound-parabolic (239)
  - Range of distance target values: 1.8, 3.8 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 216, Sequence coverage: 50.5%
- Total number of restraints: 128
- Total number of restraints per polymer type: 128
- Weight of restraints: 1.0 (128)
- Potential type of restraints: square-well-parabolic (128)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Protein, RRM

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Found 1 Document (1.148 seconds)

BMRB: 25040

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. most two C-terminal RNA Recognition Motif Domain of hnRNP L, : 1 : 4 : 2 : 4 : 54 entities Detail

Interaction partners 1. most two C-terminal RNA Recognition Motif Domain of hnRNP L, : 1 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail