BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.9 % (1092 of 1228)	89.4 % (579 of 648)	88.0 % (409 of 465)	90.4 % (104 of 115)
Backbone	88.2 % (552 of 626)	89.3 % (192 of 215)	86.8 % (269 of 310)	90.1 % (91 of 101)
Sidechain	89.4 % (626 of 700)	89.4 % (387 of 433)	89.3 % (226 of 253)	92.9 % (13 of 14)
Aromatic	75.0 % (60 of 80)	75.0 % (30 of 40)	75.0 % (30 of 40)
Methyl	100.0 % (80 of 80)	100.0 % (40 of 40)	100.0 % (40 of 40)

1. Small ubiquitin-related modifier 2

MGSSHHHHHH SQDPMADEKP KEGVKTENND HINLKVAGQD GSVVQFXIKR HTPLSKLMKA YCERQGLSMR QIRFRFDGQP INETDTPAQL EMEDEDTIDV FQQQTGG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 290 (±0.1) K, pH 6.5 (±0.05), Details 1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	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	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.1 ppm, Outliers: 4 Detail

LACS Plot; CB

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

Referencing offset: -0.1 ppm, Outliers: 4 Detail

LACS Plot; HA

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

Referencing offset: 0.0 ppm, Outliers: 2 Detail

LACS Plot; CO

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

Referencing offset: 0.18 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2016-07-04

Citation

Structures Of Human Sumo
Naik, M.T., Naik, N., Shih, H., Huang, T.

Related entities 1. Small ubiquitin-related modifier 1, : 1 : 13 : 66 entities Detail

Interaction partners 1. Small ubiquitin-related modifier 1, : 34 interactors Detail

More details for 34 interactors identified by 18 citations

Experiments performed 21 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 290 (±0.1) K, pH 6.5 (±0.05), Details 1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

3 3D HNCO

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

4 3D HNCA

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

5 3D HN(CO)CA

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

6 3D HNCACB

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

7 3D CBCA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

8 3D HCCH- TOCSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

9 3D HCCH-COSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

10 3D HBHACONH

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

11 2D-HBCBCGCDHD

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

12 2D-HBCBCGCDCEHE

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

13 3D 1H-15N TOCSY

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

14 2D 1H-1H NOESY

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

15 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

16 3D 1H-13C NOESY

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

17 2D 1H-15N HSQC IPAP

Instrument

Bruker AvanceIII - 600 MHz

Sample

State anisotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 290 (±0.1) K, pH 6.5 (±0.05), Details 1 mM SUMO2 K33Ac, 10 mM potassium phosphate, 100 mM potassium chloride, 2 mM DTT, 0.1 mM EDTA, 0.001 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

18 2D NOESY F1 FILTERED

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

19 2D NOESY F2 FILTERED

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

20 2D NOESY F1/F2 FILTERED

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

21 2D TOCSY F1/F2 FILTERED

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	DTT	natural abundance		2 mM
2	EDTA	natural abundance		0.1 mM
3	SUMO2 K33Ac	natural abundance	protein	1 mM
4	potassium chloride	natural abundance	salt	100 mM
5	potassium phosphate	natural abundance	buffer	10 mM
6	sodium azide	natural abundance		0.001 %
7	H2O	natural abundance	solvent	90 %
8	D2O	[U-2H]	solvent	10 %

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_36007_5ghc.nef
Input source #2: Coordindates	5ghc.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	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)
1:46:PHE:C	1:47:ALY:N	unknown	unknown	n/a
1:47:ALY:C	1:48:ILE:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	33	ALY	N(6)-ACETYLLYSINE	Assigned chemical shifts, Coordinates

Sequence alignments

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

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

--90---
FQQQTGG
|||||||
FQQQTGG
-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	107	0	0	100.0

Content subtype: combined_36007_5ghc.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1083		86.9 (chain: A, length: 107)
1	Distance restraints	CNS/XPLOR_distance_constraints_5	OK	3130 (1)	noe	86.0 (chain: A, length: 107)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	52 (1)	hbond	32.7 (chain: A, length: 107)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	120 (120)	.	69.2 (chain: A, length: 107)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	58 (58)	.	54.2 (chain: A, length: 107)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 86.9%
- Total number of assignments
  - ¹H chemical shifts: 579
  - ¹³C chemical shifts: 399
  - ¹⁵N chemical shifts: 105
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
33	ALY	HZ	7.71

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	659	578	87.7
¹³C chemical shifts	467	399	85.4
¹⁵N chemical shifts	120	105	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	216	188	87.0
¹³C chemical shifts	212	178	84.0
¹⁵N chemical shifts	101	88	87.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	443	390	88.0
¹³C chemical shifts	255	221	86.7
¹⁵N chemical shifts	19	17	89.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	46	45	97.8
¹³C chemical shifts	46	44	95.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	28	70.0
¹³C chemical shifts	40	27	67.5

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_5
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 86.0%
- Total number of restraints: 3119
- Weight of restraints: 1.0 (3119)
- Potential type of restraints: square-well-parabolic (3119)
- Range of distance target values: 2.1, 3.9 (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_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 32.7%
  - Total number of restraints: 52
  - Weight of restraints: 1.0 (52)
  - Potential type of restraints: square-well-parabolic (52)
  - Range of distance target values: 1.96, 2.46 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 69.2%
- Total number of restraints: 120
- Total number of restraints per polymer type: 120
- Weight of restraints: 1.0 (120)
- Potential type of restraints: square-well-parabolic (120)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 107, Sequence coverage: 54.2%

----------------------10--------20--------30--------40--------50--------60--------70--------80------
MGSSHHHHHHSQDPMADEKPKEGVKTENNDHINLKVAGQDGSVVQFXIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDV
               | || | | |||| |||   |||  ||||||    ||   ||  |||  ||||  ||| | ||| || |||   |  |||||| |
...............A.EK.K.G.KTEN.DHI...VAG..GSVVQF....HT...KL..AYC..QGLS..QIR.R.DGQ.IN.TDT...L..EDEDTI.V

--90---
FQQQTGG
|||| ||
FQQQ.GG

Total number of restraints: 58
Potential type of restraints: undefined (58)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None

Keywords ACETYLATED PROTEIN, STRUCTURAL GENOMICS, UBIQUITIN-LIKE PROTEIN

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Found 1 Document (1.068 seconds)

BMRB: 36007

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Small ubiquitin-related modifier 1, : 1 : 13 : 66 entities Detail

Interaction partners 1. Small ubiquitin-related modifier 1, : 34 interactors Detail

Experiments performed 21 experiments Detail

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NMR combined restraints 6 contents Detail