data_4978 #Corrected using PDB structure: 1Q56A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 17 I HA 4.67 5.73 # 24 Y HA 5.66 4.84 # 26 E HA 4.77 3.26 # 28 H HA 5.57 4.66 # 30 A HA 4.31 5.38 # 38 L HA 5.45 4.06 # 42 H HA 4.86 5.70 # 48 K HA 4.22 4.95 # 54 G HA 4.36 5.31 # 55 L HA 5.43 4.15 # 56 I HA 5.22 4.14 # 68 Y HA 3.77 5.28 # 73 I HA 4.04 4.98 # 74 V HA 4.49 5.32 # 81 M HA 4.60 5.51 # 82 Y HA 4.13 5.77 # 89 V HA 4.76 4.00 # 96 P HA 3.78 4.63 #111 Q HA 4.58 2.78 #114 G HA 3.68 4.65 #120 N HA 4.94 4.20 #130 L HA 4.49 3.51 #137 T HA 4.49 5.76 #140 A HA 5.12 4.28 #144 G HA 3.32 4.24 #146 M HA 3.68 4.53 #152 A HA 4.14 3.04 #153 H HA 4.77 4.02 #157 K HA 4.76 4.02 #158 A HA 4.76 4.02 #163 F HA 4.13 5.03 #177 L HA 5.21 3.62 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #110 V CA 58.18 63.34 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 29 N CB 37.34 42.48 # 38 L CB 46.25 40.51 # 40 S CB 60.78 65.98 # 51 A CB 19.53 26.17 # 57 L CB 38.51 46.13 # 58 W CB 28.90 34.11 # 70 A CB 16.95 23.59 #109 R CB 26.32 32.13 #154 K CB 30.31 35.54 #176 E CB 33.12 27.62 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 62 G C 174.95 169.65 # 67 D C 177.62 171.30 # 88 P C 171.29 176.46 #162 G C 175.09 168.77 #195 K C 182.05 175.77 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 23 T N 118.26 107.60 # 25 M N 114.22 124.37 # 31 V N 127.63 116.00 # 34 S N 111.41 127.02 # 52 T N 103.91 117.46 # 54 G N 107.32 121.05 # 58 W N 111.24 134.85 # 60 G N 105.35 116.12 # 61 K N 120.15 133.24 # 62 G N 111.55 123.98 # 67 D N 122.41 111.37 # 69 I N 114.60 124.84 # 84 L N 116.71 127.80 #109 R N 114.95 125.99 #120 N N 122.79 112.15 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 42 H H 7.11 9.84 # 58 W H 7.36 10.22 #147 E H 7.12 9.34 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.04 0.52 0.78 0.21 -1.21 -0.24 # #bmr4978.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4978.str file): #HA CA CB CO N HN #N/A +0.65 +0.65 +0.21 -1.21 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.15 +/-0.18 +/-0.16 +/-0.37 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.495 0.933 0.985 0.503 0.563 0.240 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.185 1.030 1.156 1.091 2.436 0.484 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignments for the Ca2+-bound B0 isoform of the C-terminal globular domain of agrin (agrin-G3) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Maciejewski Mark W. . 3 Ruegg Markus A. . 4 Engel Jurgen . . 5 Kammerer Richard A. . stop_ _BMRB_accession_number 4978 _BMRB_flat_file_name bmr4978.str _Entry_type new _Submission_date 2001-03-25 _Accession_date 2001-03-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 484 '15N chemical shifts' 193 '13C chemical shifts' 548 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Maciejewski Mark W. . 3 Ruegg Markus A. . 4 Engel Jurgen . . 5 Kammerer Richard A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 20 _Journal_issue 3 _Page_first 295 _Page_last 296 _Year 2001 loop_ _Keyword "synapse development" "neuromuscular junction" "AChR clustering" "sequence isoforms" stop_ save_ ################################## # Molecular system description # ################################## save_system_agrin-G3 _Saveframe_category molecular_system _Mol_system_name "B0 isoform of the 3rd(C-terminal) globular domain of agrin" _Abbreviation_common agrin-G3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label agrin-G3 $agrin_G3_monomer "Ca 2+" $CA_2+ stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function "domain acts as a signal to induce aggregation (clustering) of acetylcholine receptors on the postynaptic membrane (muscle) of neuromuscular junctions." stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1QU0 . ; non-homologus predicted to belong to same fold family as agrin-G3 For the purposes of structural genomics lumping, the agrin G3 domain is predicted to belong to a b-jellyroll fold family that includes laminin G, thrombospondin N, and the pentraxin family. Although sequence homologies within this superfamily are below the 'twilight' threshold, the fold assignment is based on the alignment of hydrophobic consensus strings with conserved hydrophobic residues in the b-strands of the known structures of two pentraxins [1] The closest structural siblings to agrin-G3 are beleived to be the laminin G domains (PDB:1QU0, 1DYK) and the ligand binding domain of neurexin 1-beta (PDB:1C4R) [1] Beckmann,G., Hanke, J., Bork, P. & Reich, J.G. (1998). Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 275: 725-730. ; PDB 1DYK . . PDB 1C4R . . stop_ _Details ; oligomeric state was determined by by analytical ultracentrifugation ; save_ ######################## # Monomeric polymers # ######################## save_agrin_G3_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common agrin-G3 _Name_variant . _Abbreviation_common agrin-G3 _Molecular_mass 21310 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Ambiguous_sequence_features ; Corresponds to the BO splice variant of the chicken agrin G3 domain (residues 1748-1940 of chicken "agrin related protein 2" in Swiss-Prot). First two residues, GS, are the result of an engineered thrombin cleavage site (e.g. cloning artifact) and are not part of the agrin-G3 sequence ; ############################## # Polymer residue sequence # ############################## _Residue_count 195 _Mol_residue_sequence ; GSEKVIIEKAAGDAEAIAFD GRTYMEYHNAVTKSEKALQS NHFELSIKTEATQGLILWSG KGLERSDYIALAIVDGFVQM MYDLGSKPVVLRSTVPINTN HWTHIKAYRVQREGSLQVGN EAPITGSSPLGATQLDTDGA LWLGGMERLSVAHKLPKAYS TGFIGCIRDVIVDRQELHLV EDALNNPTILHCSAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 1748 GLU 4 1749 LYS 5 1750 VAL 6 1751 ILE 7 1752 ILE 8 1753 GLU 9 1754 LYS 10 1755 ALA 11 1756 ALA 12 1757 GLY 13 1758 ASP 14 1759 ALA 15 1760 GLU 16 1761 ALA 17 1762 ILE 18 1763 ALA 19 1764 PHE 20 1765 ASP 21 1766 GLY 22 1767 ARG 23 1768 THR 24 1769 TYR 25 1770 MET 26 1771 GLU 27 1772 TYR 28 1773 HIS 29 1774 ASN 30 1775 ALA 31 1776 VAL 32 1777 THR 33 1778 LYS 34 1779 SER 35 1780 GLU 36 1781 LYS 37 1782 ALA 38 1783 LEU 39 1784 GLN 40 1785 SER 41 1786 ASN 42 1787 HIS 43 1788 PHE 44 1789 GLU 45 1790 LEU 46 1791 SER 47 1792 ILE 48 1793 LYS 49 1794 THR 50 1795 GLU 51 1796 ALA 52 1797 THR 53 1798 GLN 54 1799 GLY 55 1800 LEU 56 1801 ILE 57 1802 LEU 58 1803 TRP 59 1804 SER 60 1805 GLY 61 1806 LYS 62 1807 GLY 63 1808 LEU 64 1809 GLU 65 1810 ARG 66 1811 SER 67 1812 ASP 68 1813 TYR 69 1814 ILE 70 1815 ALA 71 1816 LEU 72 1817 ALA 73 1818 ILE 74 1819 VAL 75 1820 ASP 76 1821 GLY 77 1822 PHE 78 1823 VAL 79 1824 GLN 80 1825 MET 81 1826 MET 82 1827 TYR 83 1828 ASP 84 1829 LEU 85 1830 GLY 86 1831 SER 87 1832 LYS 88 1833 PRO 89 1834 VAL 90 1835 VAL 91 1836 LEU 92 1837 ARG 93 1838 SER 94 1839 THR 95 1840 VAL 96 1841 PRO 97 1842 ILE 98 1843 ASN 99 1844 THR 100 1845 ASN 101 1846 HIS 102 1847 TRP 103 1848 THR 104 1849 HIS 105 1850 ILE 106 1851 LYS 107 1852 ALA 108 1853 TYR 109 1854 ARG 110 1855 VAL 111 1856 GLN 112 1857 ARG 113 1858 GLU 114 1859 GLY 115 1860 SER 116 1861 LEU 117 1862 GLN 118 1863 VAL 119 1864 GLY 120 1865 ASN 121 1866 GLU 122 1867 ALA 123 1868 PRO 124 1869 ILE 125 1870 THR 126 1871 GLY 127 1872 SER 128 1873 SER 129 1874 PRO 130 1875 LEU 131 1876 GLY 132 1877 ALA 133 1878 THR 134 1879 GLN 135 1880 LEU 136 1881 ASP 137 1882 THR 138 1883 ASP 139 1884 GLY 140 1885 ALA 141 1886 LEU 142 1887 TRP 143 1888 LEU 144 1889 GLY 145 1890 GLY 146 1891 MET 147 1892 GLU 148 1893 ARG 149 1894 LEU 150 1895 SER 151 1896 VAL 152 1897 ALA 153 1898 HIS 154 1899 LYS 155 1900 LEU 156 1901 PRO 157 1902 LYS 158 1903 ALA 159 1904 TYR 160 1905 SER 161 1906 THR 162 1907 GLY 163 1908 PHE 164 1909 ILE 165 1910 GLY 166 1911 CYS 167 1912 ILE 168 1913 ARG 169 1914 ASP 170 1915 VAL 171 1916 ILE 172 1917 VAL 173 1918 ASP 174 1919 ARG 175 1920 GLN 176 1921 GLU 177 1922 LEU 178 1923 HIS 179 1924 LEU 180 1925 VAL 181 1926 GLU 182 1927 ASP 183 1928 ALA 184 1929 LEU 185 1930 ASN 186 1931 ASN 187 1932 PRO 188 1933 THR 189 1934 ILE 190 1935 LEU 191 1936 HIS 192 1937 CYS 193 1938 SER 194 1939 ALA 195 1940 LYS stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-06-24 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1Q56 "A Chain A, Nmr Structure Of The B0 Isoform OfThe Agrin G3 Domain In Its Ca2+ Bound State" 100.00 195 100 100 1e-108 GenBank AAA48586.1 "agrin-related protein 1" 23.90 816 100 100 1e-107 stop_ save_ ############# # Ligands # ############# save_CA_2+ _Saveframe_category ligand _Mol_type non-polymer _Name_common 'CALCIUM (II) ION' _Abbreviation_common Ca _Name_IUPAC . _BMRB_code CA_2+ _PDB_code CA _Mol_empirical_formula CA1 _Mol_charge 2+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA ? 2+ ? ? stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Details single disulfide agrin-G3 166 CYS SG agrin-G3 192 CYS SG ; Unique disulfide in agrin-G3 sequence. The two cysteines that participate in the disulfide bond have unusual chemical shifts. ; stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $agrin_G3_monomer chicken 9031 Eukaryota Metazoa Gallus gallus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $agrin_G3_monomer 'recombinant technology' "E. coli" Escherichia coli JM109 plasmid "pGSTHis: a derivative of pGEX-1 (Amersham Pharmacia Biotech) that contains a 6xHis tag followed by a thrombin cleavage site between the gluthathione S-transferase (GST) carrier protein and the agrin-G3 domain." ; The recombinant agrin-G3 domain corresponds to residues 1748-1940 of the B0 mRNA alternative splice variant of the C-terminal globular domain of chicken agrin. The sequence is given in SWISS-PROT under accession number P31696. This sequence corresponds to the "B11" isoform of the agrin G3 domain. To obtain the sequence of the BO isoform of agrin-G3 for which NMR assignments are reported -> follow the hyperlink "Agrin related protein 2" under "VARSPLIC 1783 1793" Residues 1748-1940 of the sequence you arrive at from this hyperlink correspond to residues 3-195 of the agrin-G3 domain studied by NMR. The first two residues of the agrin-G3 domain for which NMR assignments are reported, GS, are a cloning artifact (part of a thrombin cleavage site used to separate agrin-G3 from the GST carrier protein used in the recombinant fusion protein). ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $agrin_G3_monomer 1.0 mM "[U-13C; U-15N; U-90% 2H]" CaCl2 4 mM . immidazole 10 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $agrin_G3_monomer 1.0 mM "[U-15N]" CaCl2 4 mM . immidazole 10 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D HSQC-NOESY-HSQC (200 ms mix time) deuterium-decoupled TROSY versions of: 3D HNCACB HNCO HN(CA)CO 3D 15N TOCSY-HSQC (39 ms mix time) 3D 15N NOESY-HSQC (100 mix time) ; _Details "NMR spectrometer of UCONN Health Center @ Farmington" save_ ####################### # Sample conditions # ####################### save_Ex-Cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 1 K pressure 1 . atm stop_ save_ save_Ex-Cond_2 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.1 0.1 n/a temperature 298 1 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_agrin_shifts _Saveframe_category assigned_chemical_shifts _Details ; All aliphatic proton chemical shifts were obtained from a 15N labeled sample. All other chemical shifts were obtained from a 2H/13C/15N labled sample and the values reported are not corrected for 2H isotope effects. ; loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name agrin-G3 loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 SER C C 174.52 0.15 1 2 2 SER CA C 58.31 0.25 1 3 2 SER CB C 63.46 0.25 1 4 3 GLU H H 8.66 0.03 1 5 3 GLU HA H 4.25 0.07 1 6 3 GLU HB2 H 1.91 0.07 2 7 3 GLU C C 176.49 0.15 1 8 3 GLU CA C 56.67 0.25 1 9 3 GLU CB C 29.24 0.25 1 10 3 GLU N N 122.54 0.10 1 11 4 LYS H H 8.27 0.03 1 12 4 LYS HA H 4.27 0.07 1 13 4 LYS HB2 H 1.65 0.07 2 14 4 LYS C C 176.35 0.15 1 15 4 LYS CA C 56.20 0.25 1 16 4 LYS CB C 32.28 0.25 1 17 4 LYS N N 122.01 0.10 1 18 5 VAL H H 8.10 0.03 1 19 5 VAL HA H 4.05 0.07 1 20 5 VAL HB H 1.90 0.07 1 21 5 VAL HG1 H 0.80 0.07 2 22 5 VAL C C 175.93 0.15 1 23 5 VAL CA C 62.29 0.25 1 24 5 VAL CB C 32.28 0.25 1 25 5 VAL N N 122.26 0.10 1 26 6 ILE H H 8.25 0.03 1 27 6 ILE HA H 4.09 0.07 1 28 6 ILE HB H 1.75 0.07 1 29 6 ILE C C 176.07 0.15 1 30 6 ILE CA C 60.65 0.25 1 31 6 ILE CB C 37.91 0.25 1 32 6 ILE N N 125.62 0.10 1 33 7 ILE H H 8.20 0.03 1 34 7 ILE HA H 4.09 0.07 1 35 7 ILE HB H 1.83 0.07 1 36 7 ILE C C 176.07 0.15 1 37 7 ILE CA C 60.65 0.25 1 38 7 ILE CB C 37.91 0.25 1 39 7 ILE N N 125.80 0.10 1 40 8 GLU H H 8.42 0.03 1 41 8 GLU C C 176.21 0.15 1 42 8 GLU CA C 56.43 0.25 1 43 8 GLU CB C 29.95 0.25 1 44 8 GLU N N 125.49 0.10 1 45 9 LYS H H 8.30 0.03 1 46 9 LYS HA H 4.18 0.07 1 47 9 LYS C C 176.21 0.15 1 48 9 LYS CA C 55.96 0.25 1 49 9 LYS CB C 32.52 0.25 1 50 9 LYS N N 122.72 0.10 1 51 10 ALA H H 8.36 0.03 1 52 10 ALA HA H 4.45 0.07 1 53 10 ALA HB H 1.35 0.07 1 54 10 ALA C C 177.76 0.15 1 55 10 ALA CA C 52.21 0.25 1 56 10 ALA CB C 18.69 0.25 1 57 10 ALA N N 125.56 0.10 1 58 11 ALA H H 8.29 0.03 1 59 11 ALA HA H 4.31 0.07 1 60 11 ALA HB H 1.29 0.07 1 61 11 ALA C C 178.60 0.15 1 62 11 ALA CA C 52.45 0.25 1 64 11 ALA N N 123.27 0.10 1 65 12 GLY H H 8.27 0.03 1 66 12 GLY HA2 H 3.91 0.07 2 67 12 GLY C C 174.38 0.15 1 68 12 GLY CA C 45.18 0.25 1 69 12 GLY N N 107.42 0.10 1 70 13 ASP H H 8.20 0.03 1 71 13 ASP HA H 4.72 0.07 1 72 13 ASP HB2 H 2.55 0.07 2 73 13 ASP C C 176.49 0.15 1 74 13 ASP CA C 54.79 0.25 1 75 13 ASP CB C 40.96 0.25 1 76 13 ASP N N 120.31 0.10 1 77 14 ALA H H 8.17 0.03 1 78 14 ALA HA H 4.18 0.07 1 79 14 ALA HB H 1.30 0.07 1 80 14 ALA C C 177.90 0.15 1 81 14 ALA CA C 52.44 0.25 1 82 14 ALA CB C 18.69 0.25 1 83 14 ALA N N 123.00 0.10 1 84 15 GLU H H 8.22 0.03 1 85 15 GLU HA H 4.26 0.07 1 86 15 GLU HB2 H 1.93 0.07 2 87 15 GLU C C 175.79 0.15 1 88 15 GLU CA C 56.67 0.25 1 89 15 GLU CB C 29.71 0.25 1 90 15 GLU N N 118.39 0.10 1 91 16 ALA H H 8.22 0.03 1 92 16 ALA HA H 4.99 0.07 1 93 16 ALA HB H 1.47 0.07 1 94 16 ALA C C 176.77 0.15 1 95 16 ALA CA C 51.04 0.25 1 96 16 ALA CB C 21.27 0.25 1 97 16 ALA N N 123.56 0.10 1 98 17 ILE H H 8.55 0.03 1 99 17 ILE HA H 4.63 0.07 1 100 17 ILE C C 174.81 0.15 1 101 17 ILE CA C 58.54 0.25 1 102 17 ILE CB C 38.14 0.25 1 103 17 ILE N N 122.68 0.10 1 104 18 ALA H H 8.33 0.03 1 105 18 ALA HA H 5.17 0.07 1 106 18 ALA HB H 1.11 0.07 1 107 18 ALA C C 175.37 0.15 1 108 18 ALA CA C 50.81 0.25 1 109 18 ALA CB C 21.04 0.25 1 110 18 ALA N N 126.30 0.10 1 111 19 PHE H H 8.95 0.03 1 112 19 PHE HA H 4.45 0.07 1 113 19 PHE HB2 H 2.77 0.07 2 114 19 PHE C C 176.92 0.15 1 115 19 PHE CA C 57.60 0.25 1 116 19 PHE CB C 40.96 0.25 1 117 19 PHE N N 117.52 0.10 1 118 20 ASP H H 8.03 0.03 1 119 20 ASP HA H 4.53 0.07 1 120 20 ASP HB2 H 3.19 0.07 2 121 20 ASP C C 176.63 0.15 1 122 20 ASP CA C 53.15 0.25 1 124 20 ASP N N 122.08 0.10 1 125 21 GLY H H 7.83 0.03 1 126 21 GLY HA2 H 3.11 0.07 2 127 21 GLY HA3 H 4.24 0.07 2 128 21 GLY C C 173.68 0.15 1 129 21 GLY CA C 45.88 0.25 1 130 21 GLY N N 111.77 0.10 1 131 22 ARG H H 8.07 0.03 1 132 22 ARG HA H 4.45 0.07 1 133 22 ARG HB2 H 1.47 0.07 2 134 22 ARG C C 175.23 0.15 1 135 22 ARG CA C 54.09 0.25 1 136 22 ARG CB C 29.71 0.25 1 137 22 ARG N N 118.91 0.10 1 138 23 THR H H 7.79 0.03 1 139 23 THR HA H 4.00 0.07 1 140 23 THR HB H 4.18 0.07 1 141 23 THR HG2 H 1.04 0.07 1 142 23 THR C C 171.43 0.15 1 143 23 THR CA C 62.52 0.25 1 144 23 THR CB C 70.26 0.25 1 145 23 THR N N 118.26 0.10 1 146 24 TYR H H 7.89 0.03 1 147 24 TYR HA H 5.62 0.07 1 148 24 TYR C C 173.40 0.15 1 150 24 TYR CB C 38.38 0.25 1 151 24 TYR N N 125.88 0.10 1 152 25 MET H H 8.94 0.03 1 153 25 MET C C 176.63 0.15 1 154 25 MET CB C 33.93 0.25 1 155 25 MET N N 114.22 0.10 1 156 26 GLU H H 8.71 0.03 1 157 26 GLU HA H 4.73 0.07 1 158 26 GLU C C 173.26 0.15 1 159 26 GLU CA C 54.55 0.25 1 160 26 GLU CB C 30.41 0.25 1 161 26 GLU N N 119.31 0.10 1 162 27 TYR H H 8.85 0.03 1 163 27 TYR HA H 4.54 0.07 1 164 27 TYR HB2 H 2.37 0.07 2 165 27 TYR C C 177.62 0.15 1 166 27 TYR CA C 56.43 0.25 1 167 27 TYR CB C 41.20 0.25 1 168 27 TYR N N 121.84 0.10 1 169 28 HIS H H 9.62 0.03 1 170 28 HIS HA H 5.53 0.07 1 171 28 HIS C C 173.40 0.15 1 172 28 HIS CA C 55.96 0.25 1 173 28 HIS CB C 28.77 0.25 1 174 28 HIS N N 120.02 0.10 1 175 29 ASN H H 8.87 0.03 1 176 29 ASN HA H 5.71 0.07 1 177 29 ASN HB2 H 2.57 0.07 2 178 29 ASN HB3 H 2.93 0.07 2 179 29 ASN HD21 H 6.71 0.03 2 180 29 ASN HD22 H 7.51 0.03 2 181 29 ASN C C 174.52 0.15 1 182 29 ASN CA C 53.62 0.25 1 183 29 ASN CB C 37.21 0.25 1 184 29 ASN CG C 179.18 0.15 1 185 29 ASN N N 125.93 0.10 1 186 29 ASN ND2 N 112.87 0.10 1 187 30 ALA H H 8.21 0.03 1 188 30 ALA HA H 4.27 0.07 1 189 30 ALA HB H 1.20 0.07 1 190 30 ALA C C 172.83 0.15 1 191 30 ALA CA C 51.04 0.25 1 192 30 ALA CB C 20.57 0.25 1 193 30 ALA N N 122.03 0.10 1 194 31 VAL H H 9.70 0.03 1 195 31 VAL C C 176.21 0.15 1 196 31 VAL CA C 61.12 0.25 1 197 31 VAL CB C 36.27 0.25 1 198 31 VAL N N 127.63 0.10 1 199 32 THR H H 9.15 0.03 1 204 34 SER H H 8.35 0.03 1 205 34 SER HA H 4.70 0.07 1 206 34 SER HB2 H 3.94 0.07 2 208 34 SER N N 111.41 0.10 1 209 35 GLU H H 8.11 0.00 1 210 35 GLU HA H 4.21 0.07 1 212 36 LYS C C 176.07 0.15 1 213 36 LYS CA C 53.85 0.25 1 214 37 ALA H H 8.52 0.03 1 215 37 ALA HA H 5.08 0.07 1 216 37 ALA C C 176.77 0.15 1 217 37 ALA CA C 47.52 0.25 1 218 37 ALA CB C 18.69 0.25 1 219 37 ALA N N 125.83 0.10 1 220 38 LEU H H 7.79 0.03 1 221 38 LEU HA H 5.41 0.07 1 222 38 LEU C C 174.38 0.15 1 223 38 LEU CA C 53.85 0.25 1 224 38 LEU CB C 46.12 0.25 1 225 38 LEU N N 117.31 0.10 1 226 39 GLN H H 9.31 0.03 1 227 39 GLN HA H 5.17 0.07 1 228 39 GLN C C 174.95 0.15 1 229 39 GLN CA C 57.60 0.25 1 230 39 GLN CB C 33.70 0.25 1 231 39 GLN N N 124.64 0.10 1 232 40 SER H H 8.16 0.03 1 233 40 SER HA H 5.49 0.07 1 234 40 SER C C 173.82 0.15 1 235 40 SER CA C 57.13 0.25 1 236 40 SER CB C 60.65 0.25 1 237 40 SER N N 114.79 0.10 1 238 41 ASN H H 8.96 0.03 1 239 41 ASN HA H 5.62 0.07 1 240 41 ASN C C 173.54 0.15 1 242 41 ASN CB C 37.21 0.25 1 243 41 ASN N N 121.09 0.10 1 244 42 HIS H H 7.35 0.03 1 245 42 HIS HA H 4.82 0.07 1 246 42 HIS C C 173.54 0.15 1 247 42 HIS CB C 30.88 0.25 1 248 42 HIS N N 115.11 0.10 1 249 43 PHE H H 9.22 0.03 1 250 43 PHE HA H 5.62 0.07 1 251 43 PHE HB2 H 2.80 0.07 2 252 43 PHE C C 174.67 0.15 1 253 43 PHE CA C 55.73 0.25 1 254 43 PHE CB C 42.37 0.25 1 255 43 PHE N N 123.17 0.10 1 256 44 GLU H H 8.92 0.03 1 257 44 GLU HA H 5.44 0.07 1 258 44 GLU HB2 H 1.95 0.07 2 259 44 GLU C C 174.53 0.15 1 260 44 GLU CA C 55.26 0.25 1 261 44 GLU CB C 33.46 0.25 1 262 44 GLU N N 120.02 0.10 1 263 45 LEU H H 8.42 0.03 1 264 45 LEU HA H 5.08 0.07 1 265 45 LEU C C 174.53 0.15 1 266 45 LEU CA C 55.96 0.25 1 267 45 LEU CB C 42.84 0.25 1 268 45 LEU N N 115.36 0.10 1 269 46 SER H H 8.26 0.03 1 270 46 SER HA H 5.89 0.07 1 271 46 SER HB2 H 3.73 0.07 2 272 46 SER C C 173.40 0.15 1 273 46 SER CA C 57.60 0.25 1 274 46 SER CB C 65.10 0.25 1 275 46 SER N N 114.59 0.10 1 276 47 ILE H H 8.97 0.03 1 277 47 ILE HA H 5.73 0.07 1 278 47 ILE C C 173.40 0.15 1 279 47 ILE CA C 58.77 0.25 1 280 47 ILE CB C 42.60 0.25 1 281 47 ILE N N 116.55 0.10 1 282 48 LYS H H 8.01 0.03 1 283 48 LYS HA H 4.18 0.07 1 284 48 LYS C C 175.51 0.15 1 285 48 LYS CA C 55.02 0.25 1 286 48 LYS CB C 33.89 0.25 1 287 48 LYS N N 122.25 0.10 1 288 49 THR H H 9.70 0.03 1 289 49 THR HA H 4.63 0.07 1 290 49 THR HG2 H 1.04 0.07 1 291 49 THR C C 171.01 0.15 1 292 49 THR CA C 61.59 0.25 1 293 49 THR CB C 69.55 0.25 1 294 49 THR N N 122.65 0.10 1 295 50 GLU H H 8.52 0.03 1 296 50 GLU HA H 4.18 0.07 1 297 50 GLU C C 175.51 0.15 1 298 50 GLU CA C 55.02 0.25 1 299 50 GLU CB C 30.88 0.25 1 300 50 GLU N N 121.81 0.10 1 301 51 ALA H H 9.04 0.03 1 302 51 ALA HA H 4.09 0.07 1 303 51 ALA HB H 1.65 0.07 1 304 51 ALA C C 175.79 0.15 1 305 51 ALA CA C 52.91 0.25 1 306 51 ALA CB C 19.40 0.25 1 307 51 ALA N N 128.46 0.10 1 308 52 THR H H 8.14 0.03 1 309 52 THR HA H 3.91 0.07 1 310 52 THR HB H 3.81 0.07 1 311 52 THR HG2 H 1.74 0.07 1 312 52 THR C C 175.09 0.15 1 313 52 THR CA C 61.35 0.25 1 314 52 THR CB C 69.55 0.25 1 315 52 THR N N 103.91 0.10 1 316 53 GLN H H 7.45 0.03 1 317 53 GLN HA H 5.26 0.07 1 318 53 GLN HB2 H 1.65 0.07 2 319 53 GLN C C 177.20 0.15 1 320 53 GLN CA C 52.91 0.25 1 322 53 GLN N N 117.22 0.10 1 323 54 GLY H H 8.37 0.03 1 324 54 GLY HA2 H 3.91 0.07 2 325 54 GLY HA3 H 4.72 0.07 2 326 54 GLY C C 170.45 0.15 1 327 54 GLY CA C 45.88 0.25 1 328 54 GLY N N 107.32 0.10 1 329 55 LEU H H 8.30 0.03 1 330 55 LEU HA H 5.39 0.07 1 331 55 LEU C C 174.67 0.15 1 332 55 LEU CA C 55.79 0.25 1 333 55 LEU CB C 41.43 0.25 1 334 55 LEU N N 126.84 0.10 1 335 56 ILE H H 9.15 0.03 1 336 56 ILE HA H 5.18 0.07 1 337 56 ILE C C 175.93 0.15 1 338 56 ILE CA C 60.65 0.25 1 339 56 ILE CB C 41.43 0.25 1 340 56 ILE N N 119.29 0.10 1 341 57 LEU H H 8.30 0.03 1 342 57 LEU C C 173.40 0.15 1 343 57 LEU CA C 52.44 0.25 1 344 57 LEU CB C 38.38 0.25 1 345 57 LEU N N 126.55 0.10 1 346 58 TRP H H 7.60 0.03 1 347 58 TRP HE1 H 7.32 0.07 1 348 58 TRP C C 174.53 0.15 1 349 58 TRP CA C 59.24 0.25 1 350 58 TRP CB C 28.77 0.25 1 351 58 TRP N N 111.24 0.10 1 352 58 TRP NE1 N 130.63 0.10 1 353 59 SER H H 7.48 0.03 1 355 59 SER CA C 56.66 0.25 1 357 59 SER N N 111.45 0.10 1 358 60 GLY H H 9.60 0.03 1 360 60 GLY N N 105.35 0.10 1 361 61 LYS H H 7.95 0.03 1 362 61 LYS C C 178.04 0.15 1 364 61 LYS N N 120.15 0.10 1 365 62 GLY H H 9.13 0.03 1 366 62 GLY C C 174.95 0.15 1 367 62 GLY CA C 44.71 0.25 1 368 62 GLY N N 111.55 0.10 1 369 63 LEU H H 8.19 0.03 1 370 63 LEU HA H 5.08 0.07 1 371 63 LEU C C 173.12 0.15 1 372 63 LEU CA C 54.55 0.25 1 373 63 LEU CB C 40.96 0.25 1 374 63 LEU N N 121.74 0.10 1 375 64 GLU H H 8.63 0.03 1 376 64 GLU HA H 4.81 0.07 1 377 64 GLU C C 176.92 0.15 1 378 64 GLU CA C 56.20 0.25 1 379 64 GLU CB C 32.99 0.25 1 380 64 GLU N N 122.73 0.10 1 381 65 ARG H H 8.65 0.03 1 382 65 ARG HA H 4.72 0.07 1 383 65 ARG C C 175.79 0.15 1 384 65 ARG CA C 58.07 0.25 1 385 65 ARG CB C 27.83 0.25 1 386 65 ARG N N 116.60 0.10 1 387 66 SER H H 7.60 0.03 1 388 66 SER HA H 4.72 0.07 1 389 66 SER C C 174.10 0.15 1 390 66 SER CA C 58.07 0.25 1 391 66 SER CB C 64.87 0.25 1 392 66 SER N N 114.17 0.10 1 393 67 ASP H H 8.80 0.03 1 394 67 ASP HA H 4.54 0.07 1 395 67 ASP C C 177.62 0.15 1 396 67 ASP CA C 54.32 0.25 1 397 67 ASP CB C 40.96 0.25 1 398 67 ASP N N 122.41 0.10 1 399 68 TYR H H 7.98 0.03 1 400 68 TYR HA H 3.73 0.07 4 401 68 TYR C C 173.26 0.15 1 402 68 TYR CA C 56.90 0.25 1 403 68 TYR CB C 41.20 0.25 1 404 68 TYR N N 115.20 0.10 1 405 69 ILE H H 8.17 0.03 1 406 69 ILE HA H 4.81 0.07 1 407 69 ILE C C 175.79 0.15 1 409 69 ILE CB C 40.87 0.25 1 410 69 ILE N N 114.60 0.10 1 411 70 ALA H H 7.51 0.03 1 412 70 ALA HA H 4.45 0.07 1 413 70 ALA C C 174.53 0.15 1 415 70 ALA N N 122.12 0.10 1 416 71 LEU H H 9.47 0.03 1 417 71 LEU HA H 5.44 0.07 1 418 71 LEU HD1 H 0.21 0.07 2 419 71 LEU C C 175.23 0.15 1 420 71 LEU CA C 53.15 0.25 1 421 71 LEU N N 121.20 0.10 1 422 72 ALA H H 8.94 0.03 1 423 72 ALA HA H 4.72 0.07 1 424 72 ALA HB H 0.65 0.07 1 425 72 ALA C C 174.24 0.15 1 426 72 ALA CA C 50.33 0.25 1 427 72 ALA CB C 22.45 0.25 1 428 72 ALA N N 124.02 0.10 1 429 73 ILE H H 9.36 0.03 1 430 73 ILE HA H 4.00 0.07 1 431 73 ILE C C 174.53 0.15 1 432 73 ILE CA C 61.12 0.25 1 433 73 ILE CB C 38.85 0.25 1 434 73 ILE N N 120.60 0.10 1 435 74 VAL H H 8.71 0.03 1 436 74 VAL HA H 4.45 0.07 1 437 74 VAL HB H 1.93 0.07 1 438 74 VAL C C 176.21 0.15 1 439 74 VAL CA C 61.35 0.25 1 440 74 VAL CB C 33.93 0.25 1 441 74 VAL N N 124.55 0.10 1 442 75 ASP H H 8.63 0.03 1 443 75 ASP HA H 4.27 0.07 1 444 75 ASP C C 175.93 0.15 1 445 75 ASP CA C 55.96 0.25 1 447 75 ASP N N 128.12 0.10 1 448 76 GLY H H 8.93 0.03 1 449 76 GLY HA2 H 3.91 0.07 2 450 76 GLY HA3 H 4.09 0.07 2 451 76 GLY C C 171.85 0.15 1 452 76 GLY CA C 45.18 0.25 1 453 76 GLY N N 100.14 0.10 1 454 77 PHE H H 7.56 0.03 1 455 77 PHE HA H 4.72 0.07 1 456 77 PHE HB2 H 2.74 0.07 2 457 77 PHE C C 175.79 0.15 1 458 77 PHE CA C 56.67 0.25 1 459 77 PHE CB C 41.90 0.00 1 460 77 PHE N N 117.40 0.10 1 461 78 VAL H H 10.00 0.03 1 462 78 VAL HA H 4.41 0.07 1 463 78 VAL C C 174.38 0.15 1 464 78 VAL CA C 63.23 0.25 1 465 78 VAL CB C 30.88 0.25 1 466 78 VAL N N 124.89 0.10 1 467 79 GLN H H 8.05 0.03 1 468 79 GLN HA H 4.81 0.07 1 469 79 GLN C C 172.13 0.15 1 470 79 GLN CA C 55.96 0.25 1 471 79 GLN CB C 29.95 0.25 1 472 79 GLN N N 115.34 0.10 1 473 80 MET H H 7.69 0.03 1 474 80 MET HA H 4.09 0.07 1 475 80 MET C C 174.38 0.15 1 476 80 MET CA C 54.55 0.25 1 477 80 MET CB C 30.65 0.25 1 478 80 MET N N 124.27 0.10 1 479 81 MET H H 8.63 0.03 1 480 81 MET HA H 4.56 0.07 1 482 81 MET CA C 57.60 0.25 1 483 81 MET CB C 29.24 0.25 1 484 81 MET N N 124.37 0.10 1 485 82 TYR H H 8.24 0.03 1 486 82 TYR HA H 4.09 0.07 1 487 82 TYR CA C 53.62 0.25 1 488 82 TYR CB C 43.54 0.25 1 489 82 TYR N N 126.77 0.10 1 490 83 ASP H H 8.55 0.03 1 491 83 ASP HA H 4.72 0.07 1 492 83 ASP C C 172.27 0.15 1 493 83 ASP CA C 55.73 0.25 1 494 83 ASP CB C 39.55 0.25 1 495 83 ASP N N 122.11 0.10 1 496 84 LEU H H 7.51 0.03 1 497 84 LEU HA H 4.27 0.07 1 499 84 LEU CA C 53.38 0.25 1 501 84 LEU N N 116.71 0.10 1 502 85 GLY H H 9.27 0.03 1 503 85 GLY HA2 H 3.82 0.07 2 505 85 GLY N N 114.79 0.10 1 506 86 SER H H 8.34 0.03 1 507 86 SER HA H 4.72 0.07 1 508 86 SER HB2 H 3.64 0.07 2 509 86 SER HB3 H 3.81 0.07 2 511 86 SER CB C 64.63 0.25 1 512 86 SER N N 115.19 0.10 1 513 87 LYS H H 7.95 0.03 1 514 87 LYS HA H 4.18 0.07 1 515 87 LYS HB2 H 1.65 0.07 4 516 87 LYS HB3 H 1.75 0.07 4 517 87 LYS CA C 54.79 0.25 1 518 87 LYS CB C 34.87 0.25 1 520 88 PRO HA H 4.24 0.07 1 521 88 PRO C C 171.29 0.15 1 522 88 PRO CA C 59.71 0.25 1 523 88 PRO CB C 35.10 0.25 1 524 89 VAL H H 7.64 0.03 1 525 89 VAL HA H 4.72 0.07 1 526 89 VAL C C 170.87 0.15 1 527 89 VAL CA C 60.65 0.25 1 528 89 VAL CB C 33.70 0.25 1 529 89 VAL N N 122.95 0.10 1 530 90 VAL H H 7.58 0.03 1 531 90 VAL HA H 4.63 0.07 1 532 90 VAL C C 174.95 0.15 1 533 90 VAL CA C 60.65 0.25 1 534 90 VAL CB C 33.70 0.25 1 535 90 VAL N N 122.86 0.10 1 536 91 LEU H H 9.26 0.03 1 537 91 LEU HA H 4.63 0.07 1 538 91 LEU C C 174.95 0.15 1 539 91 LEU CA C 53.38 0.25 1 540 91 LEU CB C 42.37 0.25 1 541 91 LEU N N 127.79 0.10 1 542 92 ARG H H 8.54 0.03 1 543 92 ARG HA H 4.63 0.07 1 544 92 ARG HB2 H 1.57 0.07 2 545 92 ARG C C 174.52 0.15 1 546 92 ARG CA C 55.49 0.25 1 547 92 ARG CB C 31.59 0.25 1 548 92 ARG N N 122.19 0.10 1 549 93 SER H H 8.22 0.03 1 550 93 SER HA H 4.63 0.07 1 551 93 SER HB2 H 4.18 0.07 2 552 93 SER C C 174.24 0.15 1 553 93 SER CA C 57.60 0.25 1 554 93 SER CB C 62.99 0.25 1 555 93 SER N N 116.61 0.10 1 556 94 THR H H 9.70 0.03 1 557 94 THR HA H 4.27 0.07 1 558 94 THR C C 175.93 0.15 1 559 94 THR CA C 62.29 0.25 1 560 94 THR CB C 70.49 0.25 1 561 94 THR N N 114.43 0.10 1 562 95 VAL H H 7.96 0.03 1 563 95 VAL HA H 4.54 0.07 1 564 95 VAL HB H 1.83 0.07 1 565 95 VAL C C 172.98 0.15 1 566 95 VAL CA C 59.71 0.25 1 567 95 VAL CB C 33.69 0.25 1 569 96 PRO HA H 3.74 0.07 1 570 96 PRO C C 177.90 0.15 1 571 96 PRO CA C 63.23 0.25 1 572 96 PRO CB C 30.88 0.25 1 573 97 ILE H H 7.94 0.03 1 574 97 ILE HA H 4.69 0.07 1 575 97 ILE C C 175.09 0.15 1 576 97 ILE CA C 56.66 0.25 1 577 97 ILE CB C 41.20 0.25 1 578 97 ILE N N 121.44 0.10 1 579 98 ASN H H 8.99 0.03 1 580 98 ASN HA H 4.69 0.07 1 581 98 ASN C C 176.07 0.15 1 582 98 ASN CA C 53.38 0.25 1 583 98 ASN CB C 34.40 0.25 1 584 98 ASN N N 120.82 0.10 1 585 99 THR H H 7.88 0.03 1 586 99 THR HA H 4.00 0.07 1 587 99 THR HB H 4.15 0.07 1 588 99 THR HG2 H 0.99 0.07 1 589 99 THR C C 174.95 0.15 1 590 99 THR CA C 60.88 0.25 1 591 99 THR CB C 70.26 0.25 1 592 99 THR N N 108.14 0.10 1 593 100 ASN H H 8.62 0.03 1 594 100 ASN HA H 4.73 0.07 1 595 100 ASN HB2 H 2.12 0.07 2 596 100 ASN HB3 H 3.20 0.07 2 597 100 ASN HD21 H 6.58 0.03 2 598 100 ASN HD22 H 7.18 0.03 2 599 100 ASN C C 173.82 0.15 1 600 100 ASN CA C 52.91 0.25 1 601 100 ASN CB C 38.62 0.25 1 602 100 ASN CG C 177.50 0.15 1 603 100 ASN N N 119.78 0.10 1 604 100 ASN ND2 N 109.28 0.10 1 605 101 HIS H H 7.68 0.03 1 606 101 HIS HA H 4.92 0.07 1 607 101 HIS HB2 H 2.83 0.07 2 608 101 HIS C C 176.63 0.15 1 609 101 HIS CA C 53.65 0.25 1 610 101 HIS CB C 31.59 0.25 1 611 101 HIS N N 113.49 0.10 1 612 102 TRP H H 8.86 0.03 1 613 102 TRP HA H 4.72 0.07 1 614 102 TRP HD1 H 7.21 0.07 1 615 102 TRP HE1 H 10.26 0.03 1 616 102 TRP C C 177.90 0.15 1 617 102 TRP CA C 59.01 0.25 1 618 102 TRP CB C 29.01 0.25 1 619 102 TRP N N 125.96 0.10 1 620 102 TRP NE1 N 130.63 0.10 1 621 103 THR H H 9.81 0.03 1 622 103 THR HA H 4.63 0.07 1 623 103 THR C C 172.42 0.15 1 624 103 THR CA C 62.76 0.25 1 625 103 THR CB C 71.90 0.25 1 626 103 THR N N 121.80 0.10 1 627 104 HIS H H 9.29 0.03 1 628 104 HIS HA H 5.17 0.07 1 629 104 HIS C C 173.83 0.15 1 630 104 HIS CA C 56.43 0.25 1 631 104 HIS CB C 30.65 0.25 1 632 104 HIS N N 127.30 0.10 1 633 105 ILE H H 9.13 0.03 1 634 105 ILE HA H 4.63 0.07 1 635 105 ILE HB H 1.54 0.07 1 636 105 ILE C C 174.10 0.15 1 637 105 ILE CA C 61.12 0.25 1 638 105 ILE CB C 40.73 0.25 1 639 105 ILE N N 125.47 0.10 1 640 106 LYS H H 8.72 0.03 1 641 106 LYS HA H 4.90 0.07 1 642 106 LYS HB2 H 1.65 0.07 2 643 106 LYS C C 174.53 0.15 1 644 106 LYS CA C 57.60 0.25 1 645 106 LYS CB C 35.10 0.25 1 646 106 LYS N N 124.60 0.10 1 647 107 ALA H H 9.23 0.03 1 648 107 ALA HA H 5.35 0.07 1 649 107 ALA HB H 1.47 0.07 1 650 107 ALA C C 171.29 0.15 1 651 107 ALA CA C 50.57 0.25 1 652 107 ALA CB C 22.67 0.25 1 653 107 ALA N N 129.87 0.10 1 654 108 TYR H H 8.90 0.03 1 655 108 TYR HA H 5.27 0.07 1 656 108 TYR C C 176.21 0.15 1 657 108 TYR CA C 55.96 0.25 1 658 108 TYR CB C 36.04 0.25 1 659 108 TYR N N 125.11 0.10 1 660 109 ARG H H 8.16 0.03 1 661 109 ARG HA H 4.36 0.07 1 662 109 ARG C C 175.79 0.15 1 663 109 ARG CA C 59.01 0.25 1 664 109 ARG CB C 26.19 0.25 1 665 109 ARG N N 114.95 0.10 1 666 110 VAL H H 8.47 0.03 1 667 110 VAL HA H 4.45 0.07 1 668 110 VAL C C 179.45 0.15 1 669 110 VAL CA C 58.31 0.25 1 670 110 VAL CB C 30.18 0.25 1 671 110 VAL N N 119.12 0.10 1 672 111 GLN H H 8.13 0.03 1 673 111 GLN HA H 4.54 0.07 1 674 111 GLN HB2 H 2.11 0.07 2 675 111 GLN HB3 H 1.85 0.07 2 676 111 GLN HG2 H 2.34 0.07 2 677 111 GLN HG3 H 2.44 0.07 2 678 111 GLN HE21 H 6.76 0.03 2 679 111 GLN HE22 H 7.38 0.03 2 680 111 GLN C C 178.32 0.15 1 681 111 GLN CA C 57.13 0.25 1 682 111 GLN CB C 30.18 0.25 1 683 111 GLN CD C 180.31 0.15 1 684 111 GLN N N 122.08 0.10 1 685 111 GLN NE2 N 112.12 0.10 1 686 112 ARG H H 8.67 0.03 1 687 112 ARG HA H 4.72 0.07 1 688 112 ARG C C 175.79 0.15 1 689 112 ARG CA C 55.96 0.25 1 690 112 ARG CB C 35.81 0.25 1 691 112 ARG N N 121.45 0.10 1 692 113 GLU H H 7.89 0.03 1 693 113 GLU C C 175.23 0.15 1 694 113 GLU CA C 57.60 0.25 1 696 113 GLU N N 126.07 0.10 1 697 114 GLY H H 9.33 0.03 1 698 114 GLY HA2 H 3.64 0.07 2 699 114 GLY C C 173.40 0.15 1 700 114 GLY CA C 44.01 0.25 1 701 114 GLY N N 115.42 0.10 1 702 115 SER H H 8.69 0.03 1 703 115 SER HA H 5.26 0.07 1 704 115 SER C C 172.13 0.15 1 705 115 SER CA C 56.43 0.25 1 706 115 SER CB C 64.17 0.25 1 707 115 SER N N 114.59 0.10 1 708 116 LEU H H 9.07 0.03 1 709 116 LEU HA H 5.08 0.07 1 710 116 LEU C C 173.68 0.15 1 711 116 LEU CA C 53.38 0.25 1 712 116 LEU CB C 46.35 0.25 1 713 116 LEU N N 127.77 0.10 1 714 117 GLN H H 9.00 0.03 1 715 117 GLN HA H 4.54 0.07 1 716 117 GLN C C 173.40 0.15 1 717 117 GLN CA C 55.73 0.25 1 718 117 GLN CB C 31.59 0.25 1 719 117 GLN N N 125.19 0.10 1 720 118 VAL H H 10.14 0.03 1 721 118 VAL HA H 4.72 0.07 1 722 118 VAL HG1 H 0.39 0.07 2 723 118 VAL C C 176.21 0.15 1 724 118 VAL CA C 61.12 0.25 1 726 118 VAL N N 131.22 0.10 1 727 119 GLY H H 9.18 0.03 1 728 119 GLY HA2 H 4.00 0.07 2 729 119 GLY C C 175.37 0.15 1 730 119 GLY CA C 47.05 0.25 1 731 119 GLY N N 113.06 0.10 1 732 120 ASN H H 8.80 0.03 1 733 120 ASN HA H 4.90 0.07 1 734 120 ASN HB2 H 2.48 0.07 2 735 120 ASN HB3 H 2.93 0.07 2 736 120 ASN HD21 H 7.52 0.03 2 737 120 ASN HD22 H 6.83 0.03 2 738 120 ASN C C 175.79 0.15 1 739 120 ASN CA C 52.21 0.25 1 740 120 ASN CB C 38.62 0.25 1 741 120 ASN CG C 178.62 0.15 1 742 120 ASN N N 122.79 0.10 1 743 120 ASN ND2 N 112.75 0.10 1 744 121 GLU H H 7.53 0.03 1 745 121 GLU HA H 4.36 0.07 1 746 121 GLU C C 175.09 0.15 1 747 121 GLU CA C 55.73 0.25 1 748 121 GLU CB C 29.24 0.25 1 749 121 GLU N N 119.65 0.10 1 750 122 ALA H H 8.27 0.03 1 751 122 ALA HA H 4.09 0.07 1 752 122 ALA C C 176.49 0.15 1 753 122 ALA CA C 50.34 0.25 1 754 122 ALA CB C 16.58 0.25 1 756 123 PRO HA H 4.19 0.07 1 757 123 PRO C C 176.35 0.15 1 758 123 PRO CA C 63.70 0.25 1 759 123 PRO CB C 31.12 0.25 1 760 124 ILE H H 9.30 0.03 1 761 124 ILE HA H 4.27 0.07 1 762 124 ILE HB H 2.01 0.07 1 763 124 ILE C C 176.21 0.15 1 764 124 ILE CA C 59.24 0.25 1 765 124 ILE CB C 37.45 0.25 1 766 124 ILE N N 126.54 0.10 1 767 125 THR H H 8.14 0.03 1 768 125 THR HA H 5.53 0.07 1 769 125 THR C C 174.95 0.15 1 770 125 THR CA C 59.01 0.25 1 772 125 THR N N 114.20 0.10 1 773 126 GLY H H 7.97 0.03 1 774 126 GLY HA2 H 3.91 0.07 2 775 126 GLY HA3 H 4.18 0.07 2 776 126 GLY C C 171.01 0.15 1 777 126 GLY CA C 45.18 0.25 1 778 126 GLY N N 107.11 0.10 1 779 127 SER H H 8.41 0.03 1 780 127 SER HA H 5.71 0.07 1 781 127 SER HB2 H 3.46 0.07 2 782 127 SER C C 174.38 0.15 1 783 127 SER CA C 56.43 0.25 1 784 127 SER CB C 65.57 0.25 1 785 127 SER N N 112.03 0.10 1 786 128 SER H H 8.70 0.03 1 787 128 SER HA H 4.27 0.07 1 788 128 SER C C 172.13 0.15 1 789 128 SER CA C 58.23 0.25 1 790 128 SER CB C 60.41 0.25 1 792 129 PRO HA H 4.73 0.07 1 793 129 PRO C C 176.07 0.15 1 794 129 PRO CA C 63.46 0.25 1 795 129 PRO CB C 31.58 0.25 1 796 130 LEU H H 8.22 0.03 1 797 130 LEU HA H 4.45 0.07 1 798 130 LEU HB2 H 1.56 0.07 4 799 130 LEU HD1 H 0.48 0.07 2 800 130 LEU C C 176.92 0.15 1 801 130 LEU CA C 56.66 0.25 1 803 130 LEU N N 120.67 0.10 1 804 131 GLY H H 8.03 0.03 1 805 131 GLY HA2 H 4.72 0.07 2 806 131 GLY HA3 H 3.46 0.07 2 807 131 GLY C C 173.54 0.15 1 808 131 GLY CA C 44.95 0.25 1 809 131 GLY N N 109.04 0.10 1 810 132 ALA H H 7.84 0.03 1 811 132 ALA HA H 4.09 0.07 1 812 132 ALA HB H 1.47 0.07 1 813 132 ALA C C 177.34 0.15 1 814 132 ALA CA C 51.51 0.25 1 815 132 ALA CB C 21.04 0.25 1 816 132 ALA N N 123.70 0.10 1 817 133 THR H H 8.90 0.03 1 818 133 THR HA H 4.63 0.07 1 819 133 THR C C 175.22 0.15 1 820 133 THR CA C 62.29 0.25 1 821 133 THR CB C 68.23 0.25 1 822 133 THR N N 119.19 0.10 1 823 134 GLN H H 9.19 0.03 1 824 134 GLN HA H 4.09 0.07 1 825 134 GLN HG2 H 2.03 0.07 4 826 134 GLN HE21 H 6.69 0.03 2 827 134 GLN HE22 H 7.59 0.03 2 828 134 GLN C C 178.06 0.15 1 829 134 GLN CA C 54.09 0.25 1 830 134 GLN CB C 32.52 0.25 1 831 134 GLN CD C 181.43 0.15 1 832 134 GLN N N 127.69 0.10 1 833 134 GLN NE2 N 112.33 0.10 1 834 135 LEU H H 8.72 0.03 1 835 135 LEU HA H 4.28 0.07 1 836 135 LEU C C 174.95 0.15 1 837 135 LEU CA C 55.39 0.25 1 838 135 LEU CB C 42.02 0.25 1 839 135 LEU N N 120.81 0.10 1 840 136 ASP H H 8.84 0.03 1 841 136 ASP HA H 4.72 0.07 1 842 136 ASP C C 174.24 0.15 1 843 136 ASP CA C 52.91 0.25 1 845 136 ASP N N 120.94 0.10 1 846 137 THR H H 8.56 0.03 1 847 137 THR HA H 4.45 0.07 1 848 137 THR HB H 4.71 0.07 1 849 137 THR C C 176.92 0.15 1 850 137 THR CA C 62.76 0.25 1 851 137 THR N N 115.55 0.10 1 852 138 ASP H H 8.53 0.03 1 853 138 ASP HA H 4.72 0.07 1 854 138 ASP C C 177.76 0.15 1 855 138 ASP CA C 51.98 0.25 1 857 138 ASP N N 120.86 0.10 1 858 139 GLY H H 8.62 0.03 1 859 139 GLY HA2 H 4.09 0.07 2 860 139 GLY HA3 H 3.45 0.07 2 861 139 GLY C C 172.98 0.15 1 862 139 GLY CA C 44.95 0.25 1 863 139 GLY N N 106.36 0.10 1 864 140 ALA H H 7.81 0.03 1 865 140 ALA HA H 5.08 0.07 1 866 140 ALA C C 172.42 0.15 1 867 140 ALA CA C 52.68 0.25 1 868 140 ALA CB C 20.57 0.25 1 869 140 ALA N N 123.41 0.10 1 870 141 LEU H H 9.16 0.03 1 871 141 LEU HA H 5.00 0.07 1 872 141 LEU C C 172.84 0.15 1 873 141 LEU CA C 54.55 0.25 1 874 141 LEU CB C 45.41 0.25 1 875 141 LEU N N 114.08 0.10 1 876 142 TRP H H 9.63 0.03 1 877 142 TRP HA H 5.89 0.07 1 878 142 TRP HD1 H 7.31 0.07 1 879 142 TRP HE1 H 10.28 0.03 1 880 142 TRP C C 177.06 0.15 1 881 142 TRP CA C 55.96 0.25 1 882 142 TRP CB C 31.59 0.25 1 883 142 TRP N N 126.28 0.10 1 884 142 TRP NE1 N 130.11 0.10 1 885 143 LEU H H 9.87 0.03 1 886 143 LEU HA H 5.53 0.07 1 887 143 LEU C C 177.76 0.15 1 890 143 LEU N N 121.57 0.10 1 891 144 GLY H H 8.62 0.03 1 892 144 GLY HA2 H 3.28 0.07 2 893 144 GLY C C 172.42 0.15 1 894 144 GLY N N 108.44 0.10 1 895 145 GLY H H 7.38 0.03 1 896 145 GLY HA2 H 3.84 0.07 2 897 145 GLY C C 170.16 0.15 1 898 145 GLY CA C 46.35 0.25 1 899 145 GLY N N 105.09 0.10 1 900 146 MET H H 7.13 0.03 1 901 146 MET HA H 3.64 0.07 1 902 146 MET HB2 H 0.75 0.07 4 903 146 MET C C 175.08 0.15 1 904 146 MET CA C 52.91 0.25 1 905 146 MET CB C 34.16 0.25 1 906 146 MET N N 112.81 0.10 1 907 147 GLU H H 7.36 0.03 1 908 147 GLU HA H 3.91 0.07 1 909 147 GLU HB2 H 1.47 0.07 2 910 147 GLU C C 175.93 0.15 1 911 147 GLU CA C 57.60 0.25 1 912 147 GLU CB C 31.59 0.25 1 913 147 GLU N N 122.25 0.10 1 914 148 ARG H H 7.56 0.03 1 915 148 ARG HA H 4.18 0.07 1 916 148 ARG HB2 H 1.56 0.07 2 917 148 ARG C C 175.65 0.15 1 918 148 ARG CA C 55.26 0.25 1 919 148 ARG CB C 31.35 0.25 1 920 148 ARG N N 118.18 0.10 1 921 149 LEU H H 7.30 0.03 1 922 149 LEU HA H 4.54 0.07 1 923 149 LEU HD1 H 1.20 0.07 4 924 149 LEU C C 174.24 0.15 1 925 149 LEU CA C 52.21 0.25 1 926 149 LEU CB C 41.66 0.25 1 927 149 LEU N N 121.44 0.10 1 928 150 SER H H 7.48 0.03 1 929 150 SER HA H 4.72 0.07 1 930 150 SER HB2 H 3.83 0.07 2 931 150 SER HB3 H 3.91 0.07 2 932 150 SER C C 175.65 0.15 1 933 150 SER CA C 56.66 0.25 1 935 150 SER N N 112.29 0.10 1 936 151 VAL H H 8.91 0.03 1 937 151 VAL C C 174.38 0.15 1 939 151 VAL N N 123.04 0.10 1 940 152 ALA H H 8.66 0.03 1 941 152 ALA HA H 4.10 0.07 1 942 152 ALA HB H 1.21 0.07 1 943 152 ALA C C 175.93 0.15 1 944 152 ALA CB C 17.99 0.25 1 945 152 ALA N N 125.78 0.10 1 946 153 HIS H H 7.43 0.03 1 947 153 HIS HA H 4.73 0.07 1 948 153 HIS HB2 H 3.64 0.07 2 949 153 HIS C C 176.49 0.15 1 950 153 HIS CA C 58.31 0.25 1 951 153 HIS CB C 29.01 0.25 1 952 153 HIS N N 122.13 0.10 1 953 154 LYS H H 7.46 0.03 1 954 154 LYS HA H 4.00 0.07 1 955 154 LYS HB2 H 1.48 0.07 2 956 154 LYS C C 174.38 0.15 1 957 154 LYS CA C 55.49 0.25 1 958 154 LYS CB C 30.18 0.25 1 959 154 LYS N N 115.65 0.10 1 960 155 LEU H H 7.80 0.03 1 961 155 LEU HA H 4.09 0.07 1 962 155 LEU C C 177.90 0.15 1 963 155 LEU CA C 54.09 0.25 1 964 155 LEU CB C 42.60 0.25 1 966 156 PRO HA H 4.46 0.07 1 967 156 PRO C C 178.18 0.15 1 968 156 PRO CA C 62.99 0.25 1 969 156 PRO CB C 32.05 0.25 1 970 157 LYS H H 8.96 0.03 1 971 157 LYS HA H 4.72 0.07 1 972 157 LYS HB2 H 1.38 0.07 2 973 157 LYS C C 178.88 0.15 1 974 157 LYS CA C 59.01 0.25 1 975 157 LYS CB C 31.12 0.25 1 976 157 LYS N N 126.05 0.10 1 977 158 ALA H H 8.80 0.03 1 978 158 ALA HA H 4.72 0.07 1 979 158 ALA HB H 1.62 0.07 1 980 158 ALA C C 178.46 0.15 1 981 158 ALA CA C 55.49 0.25 1 982 158 ALA CB C 21.74 0.25 1 983 158 ALA N N 122.49 0.10 1 984 159 TYR H H 7.85 0.03 1 985 159 TYR HA H 3.82 0.07 1 986 159 TYR HB2 H 2.66 0.07 2 987 159 TYR HB3 H 2.80 0.07 2 988 159 TYR C C 175.09 0.15 1 989 159 TYR CA C 61.12 0.25 1 990 159 TYR CB C 36.98 0.25 1 991 159 TYR N N 110.22 0.10 1 992 160 SER H H 7.54 0.03 1 993 160 SER HA H 4.45 0.07 1 994 160 SER HB2 H 3.82 0.07 2 995 160 SER C C 173.40 0.15 1 996 160 SER CA C 57.37 0.25 1 997 160 SER CB C 62.99 0.25 1 998 160 SER N N 110.00 0.10 1 999 161 THR H H 7.35 0.03 1 1000 161 THR HA H 4.36 0.07 1 1001 161 THR HB H 4.00 0.07 1 1002 161 THR HG2 H 1.17 0.07 1 1003 161 THR C C 173.40 0.15 1 1004 161 THR CA C 61.35 0.25 1 1006 161 THR N N 118.18 0.10 1 1007 162 GLY H H 8.87 0.03 1 1008 162 GLY HA2 H 4.27 0.07 2 1009 162 GLY C C 175.09 0.15 1 1010 162 GLY CA C 45.41 0.25 1 1011 162 GLY N N 115.29 0.10 1 1012 163 PHE H H 8.80 0.03 1 1013 163 PHE HA H 4.09 0.07 1 1014 163 PHE HB2 H 2.48 0.07 2 1015 163 PHE HB3 H 3.20 0.07 2 1016 163 PHE C C 173.96 0.15 1 1017 163 PHE CA C 58.54 0.25 1 1018 163 PHE CB C 39.81 0.25 1 1019 163 PHE N N 126.14 0.10 1 1020 164 ILE H H 6.20 0.03 1 1021 164 ILE HA H 4.09 0.07 1 1022 164 ILE HB H 1.20 0.07 4 1023 164 ILE HG12 H 2.11 0.07 4 1024 164 ILE C C 175.23 0.15 1 1025 164 ILE CA C 59.95 0.25 1 1027 164 ILE N N 124.95 0.10 1 1028 165 GLY H H 8.08 0.03 1 1029 165 GLY HA2 H 3.82 0.07 2 1030 165 GLY C C 171.71 0.15 1 1031 165 GLY CA C 44.71 0.25 1 1032 165 GLY N N 114.42 0.10 1 1033 166 CYS H H 9.30 0.03 1 1034 166 CYS HA H 6.43 0.07 1 1035 166 CYS HB2 H 3.10 0.07 2 1036 166 CYS C C 172.84 0.15 1 1037 166 CYS CA C 54.09 0.25 1 1038 166 CYS CB C 47.99 0.25 1 1039 166 CYS N N 117.33 0.10 1 1040 167 ILE H H 9.10 0.03 1 1041 167 ILE HA H 5.35 0.07 1 1042 167 ILE C C 173.54 0.15 1 1043 167 ILE CA C 61.59 0.25 1 1044 167 ILE CB C 41.66 0.25 1 1045 167 ILE N N 119.66 0.10 1 1046 168 ARG H H 8.86 0.03 1 1047 168 ARG HA H 4.90 0.07 1 1048 168 ARG C C 172.70 0.15 1 1049 168 ARG CA C 54.55 0.25 1 1050 168 ARG CB C 33.69 0.25 1 1051 168 ARG N N 120.63 0.10 1 1052 169 ASP H H 8.68 0.03 1 1053 169 ASP HA H 4.18 0.07 1 1054 169 ASP C C 174.10 0.15 1 1055 169 ASP CA C 55.02 0.25 1 1056 169 ASP CB C 39.09 0.25 1 1057 169 ASP N N 117.16 0.10 1 1058 170 VAL H H 8.86 0.03 1 1059 170 VAL HA H 4.70 0.07 1 1060 170 VAL C C 175.93 0.15 1 1061 170 VAL CA C 62.06 0.25 1 1062 170 VAL CB C 30.65 0.25 1 1063 170 VAL N N 119.14 0.10 1 1064 171 ILE H H 9.47 0.03 1 1065 171 ILE HA H 4.53 0.07 1 1066 171 ILE HB H 1.65 0.07 1 1067 171 ILE C C 176.07 0.15 1 1068 171 ILE CA C 59.95 0.25 1 1069 171 ILE CB C 39.09 0.25 1 1070 171 ILE N N 129.29 0.10 1 1071 172 VAL H H 8.85 0.03 1 1072 172 VAL HA H 4.63 0.07 1 1073 172 VAL C C 176.21 0.15 1 1074 172 VAL CA C 60.65 0.25 1 1075 172 VAL CB C 32.99 0.25 1 1076 172 VAL N N 126.69 0.10 1 1077 173 ASP H H 9.69 0.03 1 1078 173 ASP HA H 4.27 0.07 1 1079 173 ASP C C 175.23 0.15 1 1080 173 ASP CA C 56.67 0.25 1 1081 173 ASP CB C 39.09 0.25 1 1082 173 ASP N N 128.74 0.10 1 1083 174 ARG H H 8.35 0.03 1 1084 174 ARG HA H 3.37 0.07 4 1085 174 ARG C C 175.09 0.15 1 1086 174 ARG CA C 58.07 0.25 1 1087 174 ARG CB C 27.13 0.25 1 1088 174 ARG N N 106.58 0.10 1 1089 175 GLN H H 7.95 0.03 1 1090 175 GLN HA H 4.54 0.07 1 1091 175 GLN HB2 H 2.01 0.07 2 1092 175 GLN HG2 H 2.50 0.07 2 1093 175 GLN HE21 H 7.99 0.03 2 1094 175 GLN HE22 H 6.76 0.03 2 1095 175 GLN C C 174.38 0.15 1 1097 175 GLN CB C 30.65 0.25 1 1098 175 GLN CD C 181.29 0.15 1 1100 175 GLN NE2 N 112.46 0.10 1 1101 176 GLU C C 173.26 0.15 1 1102 176 GLU CB C 32.99 0.25 1 1103 177 LEU H H 9.05 0.03 1 1104 177 LEU HA H 5.17 0.07 1 1105 177 LEU C C 174.10 0.15 1 1106 177 LEU CA C 54.32 0.25 1 1107 177 LEU CB C 41.43 0.25 1 1108 177 LEU N N 121.29 0.10 1 1109 178 HIS H H 8.68 0.03 1 1110 178 HIS HA H 5.44 0.07 1 1111 178 HIS C C 175.37 0.15 1 1112 178 HIS CA C 54.79 0.25 1 1113 178 HIS CB C 26.89 0.25 1 1114 178 HIS N N 116.95 0.10 1 1115 179 LEU H H 8.56 0.03 1 1116 179 LEU HA H 4.00 0.07 1 1117 179 LEU C C 178.46 0.15 1 1118 179 LEU CA C 58.31 0.25 1 1119 179 LEU CB C 41.43 0.25 1 1120 179 LEU N N 124.02 0.10 1 1121 180 VAL H H 8.27 0.03 1 1122 180 VAL HA H 3.91 0.07 1 1123 180 VAL HB H 2.11 0.07 1 1124 180 VAL C C 179.31 0.15 1 1125 180 VAL CA C 65.10 0.25 1 1126 180 VAL CB C 31.59 0.25 1 1127 180 VAL N N 113.75 0.10 1 1128 181 GLU H H 8.80 0.03 1 1129 181 GLU HA H 4.00 0.07 1 1130 181 GLU C C 178.60 0.15 1 1131 181 GLU CA C 60.41 0.25 1 1132 181 GLU CB C 29.01 0.25 1 1133 181 GLU N N 117.52 0.10 1 1134 182 ASP H H 8.58 0.03 1 1135 182 ASP HA H 4.99 0.07 1 1136 182 ASP HB2 H 3.09 0.07 2 1137 182 ASP C C 175.93 0.15 1 1138 182 ASP CA C 55.49 0.25 1 1139 182 ASP CB C 40.49 0.25 1 1140 182 ASP N N 113.80 0.10 1 1141 183 ALA H H 6.94 0.03 1 1142 183 ALA HA H 3.99 0.07 1 1143 183 ALA HB H 1.29 0.07 1 1144 183 ALA C C 180.29 0.15 1 1145 183 ALA CA C 52.68 0.25 1 1146 183 ALA CB C 17.76 0.25 1 1147 183 ALA N N 121.71 0.10 1 1148 184 LEU H H 8.98 0.03 1 1149 184 LEU HA H 4.27 0.07 1 1150 184 LEU C C 178.32 0.15 1 1151 184 LEU CA C 54.79 0.25 1 1152 184 LEU CB C 42.37 0.25 1 1153 184 LEU N N 119.40 0.10 1 1154 185 ASN H H 8.53 0.03 1 1155 185 ASN HA H 4.72 0.07 1 1156 185 ASN HB2 H 2.60 0.07 2 1157 185 ASN C C 174.10 0.15 1 1158 185 ASN CA C 53.15 0.25 1 1159 185 ASN CB C 42.37 0.25 1 1160 185 ASN N N 113.92 0.10 1 1161 186 ASN H H 8.60 0.03 1 1162 186 ASN HA H 4.45 0.07 1 1163 186 ASN C C 174.95 0.15 1 1164 186 ASN CA C 53.62 0.25 1 1165 186 ASN CB C 38.15 0.25 1 1167 187 PRO HA H 4.51 0.07 1 1168 187 PRO C C 176.77 0.15 1 1169 187 PRO CA C 62.99 0.25 1 1170 187 PRO CB C 31.82 0.25 1 1171 188 THR H H 8.48 0.03 1 1172 188 THR HA H 4.09 0.07 1 1173 188 THR HB H 4.02 0.07 1 1174 188 THR C C 173.96 0.15 1 1175 188 THR CA C 62.99 0.25 1 1176 188 THR CB C 68.62 0.25 1 1177 188 THR N N 117.12 0.10 1 1178 189 ILE H H 8.30 0.03 1 1179 189 ILE HA H 4.00 0.07 1 1180 189 ILE HB H 1.83 0.07 1 1181 189 ILE C C 175.23 0.15 1 1182 189 ILE CA C 59.01 0.25 1 1183 189 ILE CB C 36.74 0.25 1 1184 189 ILE N N 126.84 0.10 1 1185 190 LEU H H 9.16 0.03 1 1186 190 LEU HA H 4.54 0.07 1 1187 190 LEU C C 176.35 0.15 1 1188 190 LEU CA C 53.15 0.25 1 1189 190 LEU CB C 43.31 0.25 1 1190 190 LEU N N 130.20 0.10 1 1191 191 HIS H H 8.68 0.03 1 1192 191 HIS HA H 4.81 0.07 1 1193 191 HIS HB2 H 2.87 0.07 2 1194 191 HIS C C 175.37 0.15 1 1195 191 HIS CA C 56.18 0.25 1 1196 191 HIS CB C 29.95 0.25 1 1197 191 HIS N N 118.80 0.10 1 1198 192 CYS H H 8.28 0.03 1 1199 192 CYS HA H 4.72 0.07 1 1200 192 CYS C C 174.24 0.15 1 1201 192 CYS CA C 57.13 0.00 1 1202 192 CYS CB C 44.01 0.25 1 1203 192 CYS N N 120.82 0.10 1 1204 193 SER H H 8.58 0.03 1 1205 193 SER HA H 4.00 0.07 1 1206 193 SER HB2 H 3.91 0.07 2 1207 193 SER C C 170.45 0.15 1 1208 193 SER CA C 58.54 0.25 1 1209 193 SER CB C 63.46 0.25 1 1210 193 SER N N 119.97 0.10 1 1211 194 ALA H H 8.28 0.03 1 1212 194 ALA HA H 4.27 0.07 1 1213 194 ALA HB H 1.39 0.07 1 1214 194 ALA C C 176.76 0.15 1 1215 194 ALA CA C 52.45 0.25 1 1216 194 ALA CB C 18.93 0.25 1 1217 194 ALA N N 126.24 0.10 1 1218 195 LYS H H 7.78 0.03 1 1219 195 LYS HA H 4.09 0.07 1 1220 195 LYS HB2 H 1.65 0.07 4 1221 195 LYS HB3 H 1.29 0.07 4 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _PubMed_ID 10202544 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