BMRBj - BMREntryMaster

Found 1 Document (3.169 seconds)

BMRB: 30086

5JTR

The structure of chaperone SecB in complex with unstructured MBP binding site e

Authors

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

Assembly

Protein-export protein SecB, Maltose-binding periplasmic protein

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. Maltose-binding periplasmic protein (polymer, Thiol state: not present), 40 monomers, 4590.168 × 4 Da Detail

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Total weight

87469.31 Da

Max. entity weight

17277.16 Da

Source organism

Escherichia coli O157:H7

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 80.5 %, Completeness: 52.6 %, Completeness (bb): 68.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.6 % (1192 of 2267)	40.1 % (469 of 1170)	64.2 % (568 of 885)	73.1 % (155 of 212)
Backbone	68.9 % (794 of 1152)	53.3 % (210 of 394)	76.2 % (436 of 572)	79.6 % (148 of 186)
Sidechain	41.4 % (537 of 1297)	33.4 % (259 of 776)	54.7 % (271 of 495)	26.9 % (7 of 26)
Aromatic	45.6 % (104 of 228)	49.1 % (56 of 114)	42.0 % (47 of 112)	50.0 % (1 of 2)
Methyl	77.5 % (158 of 204)	77.5 % (79 of 102)	77.5 % (79 of 102)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

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 Maltose Binding Protein (MBP) binding site e, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 82.6 %, Completeness: 52.6 %, Completeness (bb): 68.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.6 % (2383 of 4534)	39.9 % (934 of 2340)	64.5 % (1142 of 1770)	72.4 % (307 of 424)
Backbone	68.8 % (1584 of 2304)	52.5 % (414 of 788)	76.4 % (874 of 1144)	79.6 % (296 of 372)
Sidechain	41.6 % (1078 of 2594)	33.6 % (521 of 1552)	55.2 % (546 of 990)	21.2 % (11 of 52)
Aromatic	42.3 % (193 of 456)	45.2 % (103 of 228)	39.3 % (88 of 224)	50.0 % (2 of 4)
Methyl	76.0 % (310 of 408)	76.0 % (155 of 204)	76.0 % (155 of 204)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 81.5 %, Completeness: 52.6 %, Completeness (bb): 68.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.6 % (3578 of 6801)	40.1 % (1409 of 3510)	64.5 % (1712 of 2655)	71.9 % (457 of 636)
Backbone	68.7 % (2375 of 3456)	52.6 % (622 of 1182)	76.5 % (1312 of 1716)	79.0 % (441 of 558)
Sidechain	41.7 % (1622 of 3891)	33.8 % (788 of 2328)	55.1 % (818 of 1485)	20.5 % (16 of 78)
Aromatic	40.8 % (279 of 684)	43.9 % (150 of 342)	37.5 % (126 of 336)	50.0 % (3 of 6)
Methyl	76.6 % (469 of 612)	76.8 % (235 of 306)	76.5 % (234 of 306)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 81.0 %, Completeness: 52.1 %, Completeness (bb): 68.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.1 % (4720 of 9068)	39.4 % (1843 of 4680)	64.2 % (2271 of 3540)	71.5 % (606 of 848)
Backbone	68.7 % (3164 of 4608)	52.7 % (830 of 1576)	76.3 % (1746 of 2288)	79.0 % (588 of 744)
Sidechain	40.7 % (2113 of 5188)	32.7 % (1015 of 3104)	54.5 % (1080 of 1980)	17.3 % (18 of 104)
Aromatic	40.9 % (373 of 912)	43.9 % (200 of 456)	37.7 % (169 of 448)	50.0 % (4 of 8)
Methyl	77.0 % (628 of 816)	77.2 % (315 of 408)	76.7 % (313 of 408)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 58.5 %, Completeness: 49.4 %, Completeness (bb): 65.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	49.4 % (5595 of 11335)	37.7 % (2205 of 5850)	60.3 % (2670 of 4425)	67.9 % (720 of 1060)
Backbone	65.2 % (3753 of 5760)	50.6 % (996 of 1970)	72.0 % (2059 of 2860)	75.1 % (698 of 930)
Sidechain	38.5 % (2496 of 6485)	31.2 % (1211 of 3880)	51.0 % (1263 of 2475)	16.9 % (22 of 130)
Aromatic	33.9 % (386 of 1140)	36.5 % (208 of 570)	31.1 % (174 of 560)	40.0 % (4 of 10)
Methyl	71.8 % (732 of 1020)	72.2 % (368 of 510)	71.4 % (364 of 510)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 59.5 %, Completeness: 47.6 %, Completeness (bb): 62.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.6 % (6473 of 13602)	36.7 % (2573 of 7020)	57.9 % (3072 of 5310)	65.1 % (828 of 1272)
Backbone	62.8 % (4342 of 6912)	49.2 % (1163 of 2364)	69.3 % (2377 of 3432)	71.9 % (802 of 1116)
Sidechain	37.1 % (2886 of 7782)	30.3 % (1412 of 4656)	48.8 % (1448 of 2970)	16.7 % (26 of 156)
Aromatic	31.4 % (430 of 1368)	33.6 % (230 of 684)	29.2 % (196 of 672)	33.3 % (4 of 12)
Methyl	66.7 % (816 of 1224)	67.0 % (410 of 612)	66.3 % (406 of 612)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 54.4 %, Completeness: 45.9 %, Completeness (bb): 60.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	45.9 % (7282 of 15869)	35.9 % (2941 of 8190)	55.1 % (3414 of 6195)	62.5 % (927 of 1484)
Backbone	60.3 % (4866 of 8064)	48.2 % (1329 of 2758)	66.0 % (2643 of 4004)	68.7 % (894 of 1302)
Sidechain	35.9 % (3259 of 9079)	29.7 % (1614 of 5432)	46.5 % (1612 of 3465)	18.1 % (33 of 182)
Aromatic	28.3 % (451 of 1596)	30.6 % (244 of 798)	25.9 % (203 of 784)	28.6 % (4 of 14)
Methyl	63.6 % (908 of 1428)	64.0 % (457 of 714)	63.2 % (451 of 714)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 61.0 %, Completeness: 45.0 %, Completeness (bb): 59.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	45.0 % (8153 of 18136)	35.5 % (3323 of 9360)	53.5 % (3789 of 7080)	61.4 % (1041 of 1696)
Backbone	59.0 % (5439 of 9216)	47.5 % (1497 of 3152)	64.2 % (2940 of 4576)	67.3 % (1002 of 1488)
Sidechain	35.2 % (3654 of 10376)	29.4 % (1828 of 6208)	45.1 % (1787 of 3960)	18.8 % (39 of 208)
Aromatic	26.8 % (489 of 1824)	29.2 % (266 of 912)	24.4 % (219 of 896)	25.0 % (4 of 16)
Methyl	60.4 % (985 of 1632)	60.7 % (495 of 816)	60.0 % (490 of 816)

1. Protein-export protein SecB

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

2. Maltose-binding periplasmic protein

KGKSALMFNL QEPYFTWPLI AADGGYAFKY ENGKYDIKDV

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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: 0.01 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: 0.01 ppm, Outliers: 1 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: 0.42 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTR, 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. Maltose-binding periplasmic protein, : 1 : 100 : 6 entities Detail

Experiments performed 3 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 Maltose Binding Protein (MBP) binding site e, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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 Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Maltose Binding Protein (MBP) binding site e	[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_30086_5jtr.nef
Input source #2: Coordindates	5jtr.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

--170-----180-------190-------200-------
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
||||||||||||||||||||||||||||||||||||||||
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
--------10--------20--------30--------40

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

--170-----180-------190-------200-------
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
||||||||||||||||||||||||||||||||||||||||
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
--------10--------20--------30--------40

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

--170-----180-------190-------200-------
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
||||||||||||||||||||||||||||||||||||||||
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
--------10--------20--------30--------40

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

--170-----180-------190-------200-------
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
||||||||||||||||||||||||||||||||||||||||
KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
--------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_30086_5jtr.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	224		100.0 (chain: E, length: 40)
6	Assigned chemical shifts	assigned_chemical_shifts_6	Warning	224		100.0 (chain: F, length: 40)
7	Assigned chemical shifts	assigned_chemical_shifts_7	Warning	224		100.0 (chain: G, length: 40)
8	Assigned chemical shifts	assigned_chemical_shifts_8	Warning	224		100.0 (chain: H, length: 40)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1673 (1)	noe	78.1 (chain: A, length: 155), 78.1 (chain: B, length: 155), 78.1 (chain: C, length: 155), 78.1 (chain: D, length: 155)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	976 (976)	.	87.1 (chain: A, length: 155), 86.5 (chain: B, length: 155), 85.8 (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: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 53
  - ¹³C chemical shifts: 133
  - ¹⁵N chemical shifts: 38
- 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: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 53
  - ¹³C chemical shifts: 133
  - ¹⁵N chemical shifts: 38
- 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: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 53
  - ¹³C chemical shifts: 133
  - ¹⁵N chemical shifts: 38
- 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: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 53
  - ¹³C chemical shifts: 133
  - ¹⁵N chemical shifts: 38
- 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	256	52	20.3
¹³C chemical shifts	194	133	68.6
¹⁵N chemical shifts	42	38	90.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	37	45.1
¹³C chemical shifts	80	78	97.5
¹⁵N chemical shifts	38	38	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	174	15	8.6
¹³C chemical shifts	114	55	48.2
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	15	83.3
¹³C chemical shifts	18	15	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	0	0.0
¹³C chemical shifts	36	0	0.0
¹⁵N chemical shifts	1	0	0.0

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: 78.1%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 78.1%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 78.1%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 78.1%
- Total number of restraints: 1673
- Weight of restraints: 1.0 (1673)
- Potential type of restraints: square-well-parabolic (1673)
- 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: 86.5%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 85.8%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 88.4%
- Total number of restraints: 976
- Total number of restraints per polymer type: 976
- Weight of restraints: 1.0 (976)
- Potential type of restraints: square-well-parabolic (976)
- 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

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Found 1 Document (3.169 seconds)

BMRB: 30086

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Chemical shift reference

Chemical shift reference

Chemical shift reference

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

Related entities 2. Maltose-binding periplasmic protein, : 1 : 100 : 6 entities Detail

Experiments performed 3 experiments Detail

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NMR combined restraints 11 contents Detail