BMRBj - BMREntryMaster

Found 1 Document (3.159 seconds)

BMRB: 30083

5JTO

The structure of chaperone SecB in complex with unstructured proPhoA binding site d

Authors

Huang, C., Saio, T., Rossi, P., Kalodimos, C.G.

Assembly

Protein-export protein SecB, Alkaline phosphatase (E.C.3.1.3.1)

Entity

1. Protein-export protein SecB (polymer), 155 monomers, 17277.16 × 4 Da Detail

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase (polymer), 40 monomers, 4320.944 × 4 Da Detail

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Total weight

86392.414 Da

Max. entity weight

17277.16 Da

Source organism

Escherichia coli O157:H7 , Escherichia coli K-12

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 80.5 %, Completeness: 50.7 %, Completeness (bb): 67.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	50.7 % (1133 of 2236)	36.6 % (423 of 1155)	64.9 % (565 of 870)	68.7 % (145 of 211)
Backbone	67.2 % (770 of 1146)	49.4 % (193 of 391)	76.0 % (435 of 572)	77.6 % (142 of 183)
Sidechain	39.5 % (502 of 1272)	30.1 % (230 of 764)	56.0 % (269 of 480)	10.7 % (3 of 28)
Aromatic	46.8 % (88 of 188)	48.9 % (46 of 94)	44.6 % (41 of 92)	50.0 % (1 of 2)
Methyl	75.9 % (161 of 212)	76.4 % (81 of 106)	75.5 % (80 of 106)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 301 K, pH 7, Details 300 uM [U-100% 13C; U-100% 15N] E.coli chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site d, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete2

Sequence coverage: 80.5 %, Completeness: 51.3 %, Completeness (bb): 66.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	51.3 % (2295 of 4472)	38.4 % (887 of 2310)	64.4 % (1120 of 1740)	68.2 % (288 of 422)
Backbone	66.8 % (1532 of 2292)	50.9 % (398 of 782)	74.7 % (854 of 1144)	76.5 % (280 of 366)
Sidechain	40.4 % (1028 of 2544)	31.7 % (485 of 1528)	55.7 % (535 of 960)	14.3 % (8 of 56)
Aromatic	46.5 % (175 of 376)	47.9 % (90 of 188)	45.1 % (83 of 184)	50.0 % (2 of 4)
Methyl	73.8 % (313 of 424)	74.1 % (157 of 212)	73.6 % (156 of 212)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete3

Sequence coverage: 80.5 %, Completeness: 52.4 %, Completeness (bb): 67.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.4 % (3515 of 6708)	39.6 % (1372 of 3465)	65.3 % (1705 of 2610)	69.2 % (438 of 633)
Backbone	67.9 % (2335 of 3438)	52.3 % (614 of 1173)	75.6 % (1297 of 1716)	77.2 % (424 of 549)
Sidechain	41.6 % (1586 of 3816)	32.9 % (755 of 2292)	56.7 % (817 of 1440)	16.7 % (14 of 84)
Aromatic	47.7 % (269 of 564)	49.3 % (139 of 282)	46.0 % (127 of 276)	50.0 % (3 of 6)
Methyl	75.0 % (477 of 636)	75.2 % (239 of 318)	74.8 % (238 of 318)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete4

Sequence coverage: 79.0 %, Completeness: 52.0 %, Completeness (bb): 67.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.0 % (4650 of 8944)	39.0 % (1804 of 4620)	64.9 % (2260 of 3480)	69.4 % (586 of 844)
Backbone	67.6 % (3101 of 4584)	52.0 % (814 of 1564)	75.3 % (1722 of 2288)	77.2 % (565 of 732)
Sidechain	41.1 % (2091 of 5088)	32.3 % (987 of 3056)	56.4 % (1083 of 1920)	18.8 % (21 of 112)
Aromatic	46.0 % (346 of 752)	47.3 % (178 of 376)	44.6 % (164 of 368)	50.0 % (4 of 8)
Methyl	75.5 % (640 of 848)	75.5 % (320 of 424)	75.5 % (320 of 424)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete5

Sequence coverage: 50.8 %, Completeness: 47.5 %, Completeness (bb): 61.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.5 % (5308 of 11180)	36.5 % (2109 of 5775)	58.0 % (2525 of 4350)	63.9 % (674 of 1055)
Backbone	61.9 % (3548 of 5730)	49.1 % (960 of 1955)	67.8 % (1939 of 2860)	70.9 % (649 of 915)
Sidechain	37.4 % (2376 of 6360)	29.8 % (1138 of 3820)	50.5 % (1213 of 2400)	17.9 % (25 of 140)
Aromatic	39.3 % (369 of 940)	41.9 % (197 of 470)	36.3 % (167 of 460)	50.0 % (5 of 10)
Methyl	67.8 % (719 of 1060)	67.9 % (360 of 530)	67.7 % (359 of 530)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete6

Sequence coverage: 53.3 %, Completeness: 45.0 %, Completeness (bb): 58.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	45.0 % (6035 of 13416)	35.4 % (2452 of 6930)	53.9 % (2811 of 5220)	61.0 % (772 of 1266)
Backbone	58.3 % (4012 of 6876)	47.5 % (1114 of 2346)	62.9 % (2158 of 3432)	67.4 % (740 of 1098)
Sidechain	35.7 % (2726 of 7632)	29.0 % (1328 of 4584)	47.4 % (1366 of 2880)	19.0 % (32 of 168)
Aromatic	35.6 % (402 of 1128)	39.0 % (220 of 564)	31.9 % (176 of 552)	50.0 % (6 of 12)
Methyl	64.5 % (820 of 1272)	64.8 % (412 of 636)	64.2 % (408 of 636)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete7

Sequence coverage: 54.9 %, Completeness: 43.4 %, Completeness (bb): 55.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.4 % (6792 of 15652)	34.8 % (2817 of 8085)	51.0 % (3106 of 6090)	58.8 % (869 of 1477)
Backbone	55.9 % (4487 of 8022)	46.4 % (1271 of 2737)	59.6 % (2385 of 4004)	64.9 % (831 of 1281)
Sidechain	34.8 % (3097 of 8904)	28.7 % (1536 of 5348)	45.3 % (1523 of 3360)	19.4 % (38 of 196)
Aromatic	32.7 % (430 of 1316)	36.5 % (240 of 658)	28.4 % (183 of 644)	50.0 % (7 of 14)
Methyl	61.4 % (911 of 1484)	61.7 % (458 of 742)	61.1 % (453 of 742)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete8

Sequence coverage: 50.8 %, Completeness: 41.8 %, Completeness (bb): 53.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	41.8 % (7481 of 17888)	34.2 % (3157 of 9240)	48.4 % (3366 of 6960)	56.8 % (958 of 1688)
Backbone	53.6 % (4912 of 9168)	45.2 % (1414 of 3128)	56.4 % (2582 of 4576)	62.6 % (916 of 1464)
Sidechain	33.7 % (3430 of 10176)	28.3 % (1730 of 6112)	43.2 % (1658 of 3840)	18.8 % (42 of 224)
Aromatic	29.3 % (440 of 1504)	33.1 % (249 of 752)	24.9 % (183 of 736)	50.0 % (8 of 16)
Methyl	59.1 % (1002 of 1696)	59.4 % (504 of 848)	58.7 % (498 of 848)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	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: 0.05 ppm, Outliers: 1 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: 0.05 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTO, Strand ID: A, B, C, D, E, F, G, H Detail

Release date

2016-08-17

Citation

Structural basis for the antifolding activity of a molecular chaperone
Huang, C., Saio, T., Rossi, P., Kalodimos, C.G.
Nature (2016), 537, 202-206, PubMed 27501151 , DOI 10.1038/nature18965 , Abstract

Related entities 1. Protein-export protein SecB, : 1 : 8 : 3 : 1 : 99 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 3 entities Detail

Experiments performed 5 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 301 K, pH 7, Details 300 uM [U-100% 13C; U-100% 15N] E.coli chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site d, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

3 2D 1H-13C HSQC aromatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

4 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

5 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site d	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

NMR combined restraints 11 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30083_5jto.nef
Input source #2: Coordindates	5jto.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
MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGA

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

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

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

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

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

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

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

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

-------280-------290-------300-------310
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
||||||||||||||||||||||||||||||||||||||||
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
--------10--------20--------30--------40

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

-------280-------290-------300-------310
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
||||||||||||||||||||||||||||||||||||||||
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
--------10--------20--------30--------40

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

-------280-------290-------300-------310
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
||||||||||||||||||||||||||||||||||||||||
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
--------10--------20--------30--------40

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

-------280-------290-------300-------310
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
||||||||||||||||||||||||||||||||||||||||
ANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTP
--------10--------20--------30--------40

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	155	100.0
B	B	155	100.0
C	C	155	100.0
D	D	155	100.0
E	E	40	100.0
F	F	40	100.0
G	G	40	100.0
H	H	40	100.0

Content subtype: combined_30083_5jto.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	891		94.8 (chain: A, length: 155)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	886		94.8 (chain: B, length: 155)
3	Assigned chemical shifts	assigned_chemical_shifts_3	Warning	886		94.8 (chain: C, length: 155)
4	Assigned chemical shifts	assigned_chemical_shifts_4	Warning	891		94.8 (chain: D, length: 155)
5	Assigned chemical shifts	assigned_chemical_shifts_5	Warning	181		95.0 (chain: E, length: 40)
6	Assigned chemical shifts	assigned_chemical_shifts_6	Warning	181		95.0 (chain: F, length: 40)
7	Assigned chemical shifts	assigned_chemical_shifts_7	Warning	181		95.0 (chain: G, length: 40)
8	Assigned chemical shifts	assigned_chemical_shifts_8	Warning	181		95.0 (chain: H, length: 40)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1494 (1)	noe	77.4 (chain: A, length: 155), 77.4 (chain: B, length: 155), 77.4 (chain: C, length: 155), 78.1 (chain: D, length: 155)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	1012 (1012)	.	87.1 (chain: A, length: 155), 87.1 (chain: B, length: 155), 86.5 (chain: C, length: 155), 88.4 (chain: D, length: 155)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 251
  - ¹³C chemical shifts: 506
  - ¹⁵N chemical shifts: 134
- 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
Saveframe: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 250
  - ¹³C chemical shifts: 503
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: B
- 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: B
Saveframe: assigned_chemical_shifts_3
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 250
  - ¹³C chemical shifts: 503
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: C
- 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: C
Saveframe: assigned_chemical_shifts_4
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 251
  - ¹³C chemical shifts: 506
  - ¹⁵N chemical shifts: 134
- Completeness of assignments
  - Entity_assemble_ID: D
- 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: D
Saveframe: assigned_chemical_shifts_5
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: E, Chain length: 40, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 62
  - ¹³C chemical shifts: 86
  - ¹⁵N chemical shifts: 33
- Completeness of assignments
  - Entity_assemble_ID: E
- 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: E
Saveframe: assigned_chemical_shifts_6
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: F, Chain length: 40, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 62
  - ¹³C chemical shifts: 86
  - ¹⁵N chemical shifts: 33
- Completeness of assignments
  - Entity_assemble_ID: F
- 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: F
Saveframe: assigned_chemical_shifts_7
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: G, Chain length: 40, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 62
  - ¹³C chemical shifts: 86
  - ¹⁵N chemical shifts: 33
- Completeness of assignments
  - Entity_assemble_ID: G
- 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: G
Saveframe: assigned_chemical_shifts_8
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: H, Chain length: 40, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 62
  - ¹³C chemical shifts: 86
  - ¹⁵N chemical shifts: 33
- Completeness of assignments
  - Entity_assemble_ID: H
- 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: H

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	251	27.5
¹³C chemical shifts	691	506	73.2
¹⁵N chemical shifts	174	134	77.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	133	42.6
¹³C chemical shifts	310	276	89.0
¹⁵N chemical shifts	148	133	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	230	60.4
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	250	27.4
¹³C chemical shifts	691	503	72.8
¹⁵N chemical shifts	174	133	76.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	132	42.3
¹³C chemical shifts	310	275	88.7
¹⁵N chemical shifts	148	132	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	228	59.8
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	250	27.4
¹³C chemical shifts	691	503	72.8
¹⁵N chemical shifts	174	133	76.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	132	42.3
¹³C chemical shifts	310	275	88.7
¹⁵N chemical shifts	148	132	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	228	59.8
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	251	27.5
¹³C chemical shifts	691	506	73.2
¹⁵N chemical shifts	174	134	77.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	133	42.6
¹³C chemical shifts	310	276	89.0
¹⁵N chemical shifts	148	133	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	230	60.4
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	241	61	25.3
¹³C chemical shifts	179	86	48.0
¹⁵N chemical shifts	42	33	78.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	31	39.2
¹³C chemical shifts	80	36	45.0
¹⁵N chemical shifts	35	32	91.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	162	30	18.5
¹³C chemical shifts	99	50	50.5
¹⁵N chemical shifts	7	1	14.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	21	95.5
¹³C chemical shifts	22	21	95.5

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 155, Sequence coverage: 77.4%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 77.4%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 77.4%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 78.1%
- Total number of restraints: 1494
- Weight of restraints: 1.0 (1494)
- Potential type of restraints: square-well-parabolic (1494)
- Range of distance target values: 1.89, 3.52 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
  - Chain_ID: D
  - Chain_ID: E
    None
  - Chain_ID: F
    None
  - Chain_ID: G
    None
  - Chain_ID: H
    None
- 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: 155, Sequence coverage: 87.1%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 87.1%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 86.5%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 88.4%
- Total number of restraints: 1012
- Total number of restraints per polymer type: 1012
- Weight of restraints: 1.0 (1012)
- Potential type of restraints: square-well-parabolic (1012)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
  - Chain_ID: D

Keywords Molecular chaperone

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	9	52.9
¹³C chemical shifts	16	0	0.0
¹⁵N chemical shifts	1	1	100.0

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Found 1 Document (3.159 seconds)

BMRB: 30083

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Chemical shift reference

Chemical shift reference

Related entities 1. Protein-export protein SecB, : 1 : 8 : 3 : 1 : 99 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 3 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 11 contents Detail