BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	45.1 % (553 of 1227)	46.3 % (280 of 605)	32.7 % (158 of 483)	82.7 % (115 of 139)
Backbone	66.3 % (496 of 748)	89.2 % (231 of 259)	41.4 % (151 of 365)	91.9 % (114 of 124)
Sidechain	13.3 % (79 of 594)	14.2 % (49 of 346)	12.4 % (29 of 233)	6.7 % (1 of 15)
Aromatic	0.0 % (0 of 62)	0.0 % (0 of 31)	0.0 % (0 of 31)
Methyl	6.7 % (11 of 164)	6.1 % (5 of 82)	7.3 % (6 of 82)

1. entity

GNAFAQSLSS NLLSSGDFVQ MISSTTSTDQ AVSVATSVAQ NVGNQLGLDA NAMNSLLGAV SGYVSTLGNA ISDASAYANA ISSAIGNVLA NSGSISESTA SSAASSAASS VTTTLTSYGP AVFYA

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 302 K, pH 7

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	0.6 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

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

Release date

2015-06-14

Citation

3D structure of RP domain of MiSp
Gao, D., Yang, D.
Not known

Experiments performed 1 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25024_2mqa.nef
Input source #2: Coordindates	2mqa.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
MHHHHHHSSGLVPRGSGNAFAQSLSSNLLSSGDFVQMISSTTSTDQAVSVATSVAQNVGNQLGLDANAMNSLLGAVSGYVSTLGNAISDASAYANAISSA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MHHHHHHSSGLVPRGSGNAFAQSLSSNLLSSGDFVQMISSTTSTDQAVSVATSVAQNVGNQLGLDANAMNSLLGAVSGYVSTLGNAISDASAYANAISSA

-------110-------120-------130-------140--------
IGNVLANSGSISESTASSAASSAASSVTTTLTSYGPAVFYAPTSSAGG
||||||||||||||||||||||||||||||||||||||||||||||||
IGNVLANSGSISESTASSAASSAASSVTTTLTSYGPAVFYAPTSSAGG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	148	0	0	100.0

Content subtype: combined_25024_2mqa.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	505		80.4 (chain: A, length: 148)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	1415 (1)	noe	83.8 (chain: A, length: 148)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	194 (194)	.	79.7 (chain: A, length: 148)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 80.4%
- Total number of assignments
  - ¹H chemical shifts: 257
  - ¹³C chemical shifts: 136
  - ¹⁵N chemical shifts: 112
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	722	257	35.6
¹³C chemical shifts	574	136	23.7
¹⁵N chemical shifts	161	112	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	307	230	74.9
¹³C chemical shifts	296	119	40.2
¹⁵N chemical shifts	145	112	77.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	415	27	6.5
¹³C chemical shifts	278	17	6.1
¹⁵N chemical shifts	16	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	91	3	3.3
¹³C chemical shifts	91	3	3.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	0	0.0
¹³C chemical shifts	43	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 83.8%
- Total number of restraints: 1415
- Weight of restraints: 1.0 (1415)
- Potential type of restraints: upper-bound-parabolic (1415)
- Range of distance target values: 2.8, 5.0 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 148, Sequence coverage: 79.7%
- Total number of restraints: 194
- Total number of restraints per polymer type: 194
- Weight of restraints: 1.0 (194)
- Potential type of restraints: square-well-parabolic (194)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NMR, Protein, Repetitive domain, Spider silk

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BMRB: 25024

Sample

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail