Solution structure of the human Raf-1 kinase inhibitor protein
MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP TSISWDGLDS GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY VWLVYEQDRP LKCDEPILSN RSGDHRGKFK VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL YEQLSGK
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 90.1 % (1973 of 2190) | 90.5 % (1035 of 1144) | 88.2 % (757 of 858) | 96.3 % (181 of 188) |
Backbone | 98.8 % (1079 of 1092) | 97.9 % (366 of 374) | 99.1 % (541 of 546) | 100.0 % (172 of 172) |
Sidechain | 83.9 % (1065 of 1270) | 86.9 % (669 of 770) | 80.0 % (387 of 484) | 56.3 % (9 of 16) |
Aromatic | 10.3 % (20 of 194) | 20.6 % (20 of 97) | 0.0 % (0 of 92) | 0.0 % (0 of 5) |
Methyl | 99.5 % (185 of 186) | 98.9 % (92 of 93) | 100.0 % (93 of 93) |
1. Raf-1 kinase inhibitor protein
MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP TSISWDGLDS GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY VWLVYEQDRP LKCDEPILSN RSGDHRGKFK VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL YEQLSGKSolvent system 90% H2O/10% D2O, Temperature 298 K, pH 4.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Raf-1 kinase inhibitor protein | [U-100% 13C; U-100% 15N] | 3 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methylene protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methylene protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methylene protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methylene protons | 0.0 ppm | internal | indirect | 0.1013291 |
Varian INOVA - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 4.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Raf-1 kinase inhibitor protein | [U-100% 13C; U-100% 15N] | 3 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 4.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Raf-1 kinase inhibitor protein | [U-100% 13C; U-100% 15N] | 3 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints | combined_17382_2l7w.nef |
Input source #2: Coordindates | 2l7w.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
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 MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG -------110-------120-------130-------140-------150-------160-------170-------180------- TVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| TVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 187 | 0 | 0 | 100.0 |
Content subtype: combined_17382_2l7w.nef
Assigned chemical shifts
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG -------110-------120-------130-------140-------150-------160-------170-------180------- TVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK |||||||||| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| TVLSDYVGSG.PKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK
Comp_index_ID | Comp_ID | Atom_ID | CS value (ppm) |
---|---|---|---|
44 | THR | HG1 | 4.761 |
65 | THR | HG1 | 4.973 |
115 | THR | HG1 | 4.766 |
145 | HIS | HD1 | 7.257 |
148 | LYS | HZ1 | 6.917 |
148 | LYS | HZ2 | 6.917 |
148 | LYS | HZ3 | 6.917 |
150 | LYS | HZ1 | 7.025 |
150 | LYS | HZ2 | 7.025 |
150 | LYS | HZ3 | 7.025 |
157 | LYS | HZ1 | 6.758 |
157 | LYS | HZ2 | 6.758 |
157 | LYS | HZ3 | 6.758 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 1144 | 1039 | 90.8 |
13C chemical shifts | 858 | 755 | 88.0 |
15N chemical shifts | 197 | 181 | 91.9 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 374 | 372 | 99.5 |
13C chemical shifts | 374 | 369 | 98.7 |
15N chemical shifts | 172 | 172 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 770 | 667 | 86.6 |
13C chemical shifts | 484 | 386 | 79.8 |
15N chemical shifts | 25 | 9 | 36.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 95 | 94 | 98.9 |
13C chemical shifts | 95 | 93 | 97.9 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 97 | 14 | 14.4 |
13C chemical shifts | 92 | 0 | 0.0 |
15N chemical shifts | 5 | 0 | 0.0 |
Distance restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSG -------110-------120-------130-------140-------150-------160-------170-------180------- TVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK |||||||||| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| TVLSDYVGSG.PKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK