REFINED STRUCTURE OF OUTER MEMBRANE PROTEIN X IN NANODISC BY MEASURING RESIDUAL DIPOLAR COUPLINGS
ATSTVTGGYA QSDAQGQMNK MGGFNLKYRY EEDNSPLGVI GSFTYTEKSR TASSGDYNKN QYYGITAGPA YRINDWASIY GVVGVGYGKF QTTEYPTYKN DTSDYGFSYG AGLQFNPMEN VALDFSYEQS RIRSVDVGTW IAGVGYRF
Polymer type: polypeptide(L)
Total | 1H | 15N | |
---|---|---|---|
All | 23.5 % (239 of 1019) | 14.2 % (122 of 857) | 72.2 % (117 of 162) |
Backbone | 51.5 % (235 of 456) | 37.8 % (118 of 312) | 81.3 % (117 of 144) |
Sidechain | 0.7 % (4 of 563) | 0.7 % (4 of 545) | 0.0 % (0 of 18) |
Aromatic | 3.5 % (4 of 113) | 3.6 % (4 of 111) | 0.0 % (0 of 2) |
Methyl | 0.0 % (0 of 60) | 0.0 % (0 of 60) |
1. OUTER MEMBRANE PROTEIN X
ATSTVTGGYA QSDAQGQMNK MGGFNLKYRY EEDNSPLGVI GSFTYTEKSR TASSGDYNKN QYYGITAGPA YRINDWASIY GVVGVGYGKF QTTEYPTYKN DTSDYGFSYG AGLQFNPMEN VALDFSYEQS RIRSVDVGTW IAGVGYRFSolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 7.4, Details 10 MM TRIS-HCL, 100 MM NACL, 1 MM EDTA, 0.05 % SODIUM AZIDE, 0.5 MM
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | OUTER MEMBRANE PROTEIN X | [U-100% 13C; U-100% 15N] | 0.5 mM | |
2 | Tris-HCl | natural abundance | 10 mM | |
3 | sodium azide | natural abundance | 0.05 % | |
4 | NaCl | natural abundance | 100 mM | |
5 | EDTA | natural abundance | 1 mM | |
6 | H2O | natural abundance | 90 % | |
7 | D2O | natural abundance | 10 % |
Bruker AVANCE I and AVANCE III - na MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 7.4, Details 10 MM TRIS-HCL, 100 MM NACL, 1 MM EDTA, 0.05 % SODIUM AZIDE, 0.5 MM
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | OUTER MEMBRANE PROTEIN X | [U-100% 13C; U-100% 15N] | 0.5 mM | |
2 | Tris-HCl | natural abundance | 10 mM | |
3 | sodium azide | natural abundance | 0.05 % | |
4 | NaCl | natural abundance | 100 mM | |
5 | EDTA | natural abundance | 1 mM | |
6 | H2O | natural abundance | 90 % | |
7 | D2O | natural abundance | 10 % |
Bruker AVANCE I and AVANCE III - na MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 7.4, Details 10 MM TRIS-HCL, 100 MM NACL, 1 MM EDTA, 0.05 % SODIUM AZIDE, 0.5 MM
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | OUTER MEMBRANE PROTEIN X | [U-100% 13C; U-100% 15N] | 0.5 mM | |
2 | Tris-HCl | natural abundance | 10 mM | |
3 | sodium azide | natural abundance | 0.05 % | |
4 | NaCl | natural abundance | 100 mM | |
5 | EDTA | natural abundance | 1 mM | |
6 | H2O | natural abundance | 90 % | |
7 | D2O | natural abundance | 10 % |
Bruker AVANCE I and AVANCE III - na MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 7.4, Details 10 MM TRIS-HCL, 100 MM NACL, 1 MM EDTA, 0.05 % SODIUM AZIDE, 0.5 MM
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | OUTER MEMBRANE PROTEIN X | [U-100% 13C; U-100% 15N] | 0.5 mM | |
2 | Tris-HCl | natural abundance | 10 mM | |
3 | sodium azide | natural abundance | 0.05 % | |
4 | NaCl | natural abundance | 100 mM | |
5 | EDTA | natural abundance | 1 mM | |
6 | H2O | natural abundance | 90 % | |
7 | D2O | natural abundance | 10 % |
Bruker AVANCE I and AVANCE III - na MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 7.4, Details 10 MM TRIS-HCL, 100 MM NACL, 1 MM EDTA, 0.05 % SODIUM AZIDE, 0.5 MM
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | OUTER MEMBRANE PROTEIN X | [U-100% 13C; U-100% 15N] | 0.5 mM | |
2 | Tris-HCl | natural abundance | 10 mM | |
3 | sodium azide | natural abundance | 0.05 % | |
4 | NaCl | natural abundance | 100 mM | |
5 | EDTA | natural abundance | 1 mM | |
6 | H2O | natural abundance | 90 % | |
7 | D2O | natural abundance | 10 % |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints | combined_19892_2mnh.nef |
Input source #2: Coordindates | 2mnh.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 | Error |
Disulfide bonds
NoneOther bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)
NoneNon-standard residues
NoneSequence alignments
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF |||||||||||||||||||||||||||||||||||||||||||||||| DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF
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_19892_2mnh.nef
Assigned chemical shifts
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN |||||||| ||||||||||||||||||||||| | ||||||||||| | | |||||||||||||| |||| ||||||||||| | | | || .TSTVTGGY.QSDAQGQMNKMGGFNLKYRYEED.S.LGVIGSFTYTE.S..A..GDYNKNQYYGITAG.AYRI...ASIYGVVGVGY.K.Q...Y..YK. -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF |||||| |||||| | ||||||||| | ||| ||||| |||||||| .TSDYGF.YGAGLQ.N.MENVALDFS..Q.RIR.VDVGT.IAGVGYRF
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 857 | 118 | 13.8 |
15N chemical shifts | 168 | 117 | 69.6 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 312 | 118 | 37.8 |
15N chemical shifts | 144 | 117 | 81.2 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 545 | 0 | 0.0 |
15N chemical shifts | 24 | 0 | 0.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 63 | 0 | 0.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 111 | 0 | 0.0 |
15N chemical shifts | 2 | 0 | 0.0 |
Distance restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN ||||||||| |||| ||||||||||||||| |||||||||| |||||||| || || ||| |||||||| .TSTVTGGYA.SDAQ.....MGGFNLKYRYEEDNS..GVIGSFTYTE.............QYYGITAG.AY.IN...SIY.VVGVGYGK........... -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF | |||||||||| |||||||| | |||||||||| ||||||| ...D.GFSYGAGLQF..MENVALDF.Y.QSRIRSVDVG...AGVGYRF
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN |||||||| || | |||||||||| |||||||||| ||||||||||| |||||||||||| ..STVTGGYA.SD.Q.....MGGFNLKYRY.......GVIGSFTYTE.............QYYGITAGPAY......SIYGVVGVGYGK........... -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF | |||||||||| |||||| |||| |||| |||||| | ...D.GFSYGAGLQF......ALDFSY.QSRI..VDVG..IAGVGY.F
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN |||||||| || | |||||||||| |||||||||| ||||||||||| |||||||||||| ..STVTGGYA.SD.Q.....MGGFNLKYRY.......GVIGSFTYTE.............QYYGITAGPAY......SIYGVVGVGYGK........... -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF | |||||||||| |||||| |||| |||| |||||| | ...D.GFSYGAGLQF......ALDFSY.QSRI..VDVG..IAGVGY.F
Dihedral angle restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN ||||||||||||||||| |||||||||||||||||||||||||||||||| ||||||||||||||| ||||||||||||||| ||| .TSTVTGGYAQSDAQGQM.KMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRT.......KNQYYGITAGPAYRI...ASIYGVVGVGYGKFQ..EYP.... -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF ||||||||||||||| ||||||||||||||||||||||||||||||| .TSDYGFSYGAGLQFN.MENVALDFSYEQSRIRSVDVGTWIAGVGYRF
RDC restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKN | ||||| | || ||||| |||| |||| | ||||| ||| | || |||| |||||| ||| || |||| | | | .T.TVTGG.....A.GQ.NKMGG.NLKY.YEED.S.LGVIG.FTY.E.......GD.NKNQ.YGITAG.AYR.......YG.VGVG....Q...Y...K. -------110-------120-------130-------140-------- DTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF |||||| || ||| | | |||||| || |||| |||||| .TSDYGF.YG.GLQ.N.M.NVALDF......IR.VDVG....GVGYRF