BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	72.3 % (1142 of 1579)	74.5 % (608 of 816)	65.9 % (408 of 619)	87.5 % (126 of 144)
Backbone	78.0 % (615 of 788)	90.2 % (248 of 275)	65.7 % (253 of 385)	89.1 % (114 of 128)
Sidechain	68.8 % (626 of 910)	65.4 % (354 of 541)	73.9 % (261 of 353)	68.8 % (11 of 16)
Aromatic	51.6 % (96 of 186)	52.7 % (49 of 93)	49.5 % (45 of 91)	100.0 % (2 of 2)
Methyl	87.7 % (128 of 146)	87.7 % (64 of 73)	87.7 % (64 of 73)

1. entity 1

EHPEFLKAGK EPGLQIWRVE KFDLVPVPTN LYGDFFTGDA YVILKTVQLR NGNLQYDLHY WLGNECSQDE SGAAAIFTVQ LDDYLNGRAV QHREVQGFES ATFLGYFKSG LKYKKGGVAS GFKHVVPNEV VVQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.01) atm, Temperature 298 (±0.1) K, pH 7.3 (±0.1), Details 0.70 mM 13C, 15N human Gelsolin, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	human Gelsolin	[U-13C; U-15N]	protein	0.70 (±0.1) mM
2	H2O	natural abundance	solvent	90 %
3	D2O	[U-2H]	solvent	10 %

LACS Plot; CA

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

Referencing offset: 0.17 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: 0.17 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: -0.02 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5H3N, Strand ID: A Detail

Release date

2016-11-09

Citation

Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1
Fan, J.S., Goh, H., Ding, K., Xue, B., Robinson, R.C., Yang, D.
Sci. Rep. (2017), 7, 45230-45230, PubMed 28349924 , DOI 10.1038/srep45230 , Abstract

Related entities 1. Human Gelsolin protein domain 1, : 1 : 13 : 36 : 226 entities Detail

Interaction partners 1. Human Gelsolin protein domain 1, : 73 interactors Detail

More details for 73 interactors identified by 27 citations

Experiments performed 1 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36027_5h3n.nef
Input source #2: Coordindates	5h3n.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

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
EHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFES
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
EHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFES

-------110-------120-------130---
ATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQ
|||||||||||||||||||||||||||||||||
ATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	133	0	0	100.0

Content subtype: combined_36027_5h3n.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1081		95.5 (chain: A, length: 133)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1311 (1)	noe	91.7 (chain: A, length: 133)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	88 (1)	hbond	43.6 (chain: A, length: 133)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	162 (162)	.	75.2 (chain: A, length: 133)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 95.5%
- Total number of assignments
  - ¹H chemical shifts: 578
  - ¹³C chemical shifts: 377
  - ¹⁵N chemical shifts: 126
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	816	578	70.8
¹³C chemical shifts	619	377	60.9
¹⁵N chemical shifts	148	126	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	275	251	91.3
¹³C chemical shifts	266	124	46.6
¹⁵N chemical shifts	128	115	89.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	541	327	60.4
¹³C chemical shifts	353	253	71.7
¹⁵N chemical shifts	20	11	55.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	63	86.3
¹³C chemical shifts	73	63	86.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	93	43	46.2
¹³C chemical shifts	91	41	45.1
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 91.7%
- Total number of restraints: 1311
- Weight of restraints: 1.0 (1311)
- Potential type of restraints: square-well-parabolic (1311)
- Range of distance target values: 2.35, 5.6 (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: 133, Sequence coverage: 43.6%
  - Total number of restraints: 88
  - Weight of restraints: 1.0 (88)
  - Potential type of restraints: square-well-parabolic (88)
  - Range of distance target values: 2.0, 2.75 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 75.2%
- Total number of restraints: 162
- Total number of restraints per polymer type: 162
- Weight of restraints: 1.0 (162)
- Potential type of restraints: square-well-parabolic (162)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords STRUCTURAL PROTEIN, gelsolin

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Found 1 Document (4.076 seconds)

BMRB: 36027

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Human Gelsolin protein domain 1, : 1 : 13 : 36 : 226 entities Detail

Interaction partners 1. Human Gelsolin protein domain 1, : 73 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 5 contents Detail