data_16031 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Nav1.5 C-terminal EF-Hand Domain ; _BMRB_accession_number 16031 _BMRB_flat_file_name bmr16031.str _Entry_type original _Submission_date 2008-11-15 _Accession_date 2008-11-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone chemical shifts of the human Voltage-gated Sodium Channel, cardiac isoform (Nav1.5)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miloushev Vesselin Z. . 2 Levine Joshua A. . 3 Arbing Mark A. . 4 Hunt John F. . 5 Pitt Geoff S. . 6 Palmer Arthur G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 315 "13C chemical shifts" 296 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-04 update BMRB 'complete entry citation' 2009-02-17 update BMRB 'correct residue numbers in data table' 2009-01-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of the NaV1.2 C-terminal EF-hand domain.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19129176 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miloushev Vesselin Z. . 2 Levine Joshua A. . 3 Arbing Mark A. . 4 Hunt John F. . 5 Pitt Geoff S. . 6 Palmer Arthur G. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 284 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6446 _Page_last 6454 _Year 2009 _Details . loop_ _Keyword 'Voltage-gated Sodium Channel' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Nav1.5 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Nav1.5 $Nav1.5 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'channel inactivation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Nav1.5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Nav1.5 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MASENFSVATEESTEPLSED DFDMFYEIWEKFDPEATQFI EYSVLSDFADALSEPLRIAK PNQISLINMDLPMVSGDRIH CMDILFAFTKRVLGESGEMD ALKIQMEEK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1750 MET 2 1751 GLY 3 1752 SER 4 1753 SER 5 1754 HIS 6 1755 HIS 7 1756 HIS 8 1757 HIS 9 1758 HIS 10 1759 HIS 11 1760 SER 12 1761 SER 13 1762 GLY 14 1763 LEU 15 1764 VAL 16 1765 PRO 17 1766 ARG 18 1767 GLY 19 1768 SER 20 1769 HIS 21 1770 MET 22 1771 ALA 23 1772 SER 24 1773 GLU 25 1774 ASN 26 1775 PHE 27 1776 SER 28 1777 VAL 29 1778 ALA 30 1779 THR 31 1780 GLU 32 1781 GLU 33 1782 SER 34 1783 THR 35 1784 GLU 36 1785 PRO 37 1786 LEU 38 1787 SER 39 1788 GLU 40 1789 ASP 41 1790 ASP 42 1791 PHE 43 1792 ASP 44 1793 MET 45 1794 PHE 46 1795 TYR 47 1796 GLU 48 1797 ILE 49 1798 TRP 50 1799 GLU 51 1800 LYS 52 1801 PHE 53 1802 ASP 54 1803 PRO 55 1804 GLU 56 1805 ALA 57 1806 THR 58 1807 GLN 59 1808 PHE 60 1809 ILE 61 1810 GLU 62 1811 TYR 63 1812 SER 64 1813 VAL 65 1814 LEU 66 1815 SER 67 1816 ASP 68 1817 PHE 69 1818 ALA 70 1819 ASP 71 1820 ALA 72 1821 LEU 73 1822 SER 74 1823 GLU 75 1824 PRO 76 1825 LEU 77 1826 ARG 78 1827 ILE 79 1828 ALA 80 1829 LYS 81 1830 PRO 82 1831 ASN 83 1832 GLN 84 1833 ILE 85 1834 SER 86 1835 LEU 87 1836 ILE 88 1837 ASN 89 1838 MET 90 1839 ASP 91 1840 LEU 92 1841 PRO 93 1842 MET 94 1843 VAL 95 1844 SER 96 1845 GLY 97 1846 ASP 98 1847 ARG 99 1848 ILE 100 1849 HIS 101 1850 CYS 102 1851 MET 103 1852 ASP 104 1853 ILE 105 1854 LEU 106 1855 PHE 107 1856 ALA 108 1857 PHE 109 1858 THR 110 1859 LYS 111 1860 ARG 112 1861 VAL 113 1862 LEU 114 1863 GLY 115 1864 GLU 116 1865 SER 117 1866 GLY 118 1867 GLU 119 1868 MET 120 1869 ASP 121 1870 ALA 122 1871 LEU 123 1872 LYS 124 1873 ILE 125 1874 GLN 126 1875 MET 127 1876 GLU 128 1877 GLU 129 1878 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 BMRB 16045 hH1 73.64 97 98.95 98.95 5.63e-61 PDB 2KBI "Solution Nmr Structure Of The C-Terminal Ef-Hand Domain Of Human Cardiac Sodium Channel Nav1.5" 73.64 97 98.95 98.95 5.63e-61 PDB 4DCK "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" 82.17 168 100.00 100.00 2.17e-70 PDB 4JQ0 "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" 100.00 191 100.00 100.00 6.11e-89 DBJ BAD12084 "TTX-resistant sodium channel [Homo sapiens]" 82.17 2016 100.00 100.00 4.85e-63 DBJ BAD12085 "TTX-resistant sodium channel splicing variant [Homo sapiens]" 82.17 1962 100.00 100.00 4.39e-63 DBJ BAD92103 "voltage-gated sodium channel type V alpha isoform b variant [Homo sapiens]" 82.17 1576 100.00 100.00 4.69e-63 DBJ BAE27800 "unnamed protein product [Mus musculus]" 82.17 2020 98.11 98.11 1.37e-61 DBJ BAE27966 "unnamed protein product [Mus musculus]" 82.17 2020 98.11 98.11 1.37e-61 EMBL CAB70096 "voltage-gated sodium channel [Mus musculus]" 82.17 2019 98.11 98.11 1.38e-61 EMBL CAC80974 "voltage-gated sodium channel alpha subunit [Bos taurus]" 82.17 2022 97.17 97.17 8.22e-61 EMBL CAD88248 "voltage-gated sodium channel alpha subunit [Canis lupus familiaris]" 82.17 2013 99.06 99.06 1.97e-62 GB AAA42114 "sodium channel alpha-subunit [Rattus norvegicus]" 82.17 2019 98.11 98.11 1.29e-61 GB AAA58644 "sodium channel alpha subunit [Homo sapiens]" 82.17 2016 100.00 100.00 5.09e-63 GB AAI40814 "SCN5A protein [Homo sapiens]" 82.17 1983 100.00 100.00 5.09e-63 GB AAI44622 "SCN5A protein [Homo sapiens]" 82.17 1983 100.00 100.00 5.09e-63 GB AAI72643 "Sodium channel, voltage-gated, type V, alpha [synthetic construct]" 82.17 2020 98.11 98.11 1.37e-61 REF NP_000326 "sodium channel protein type 5 subunit alpha isoform b [Homo sapiens]" 82.17 2015 100.00 100.00 5.03e-63 REF NP_001002994 "sodium channel protein type 5 subunit alpha [Canis lupus familiaris]" 82.17 2013 99.06 99.06 1.97e-62 REF NP_001092874 "sodium channel protein type 5 subunit alpha isoform c [Homo sapiens]" 82.17 2016 100.00 100.00 4.85e-63 REF NP_001092875 "sodium channel protein type 5 subunit alpha isoform d [Homo sapiens]" 82.17 1998 100.00 100.00 4.48e-63 REF NP_001153632 "sodium channel protein type 5 subunit alpha isoform e [Homo sapiens]" 82.17 1983 100.00 100.00 5.29e-63 SP P15389 "RecName: Full=Sodium channel protein type 5 subunit alpha; AltName: Full=Sodium channel protein cardiac muscle subunit alpha; A" 82.17 2019 98.11 98.11 1.29e-61 SP Q14524 "RecName: Full=Sodium channel protein type 5 subunit alpha; AltName: Full=HH1; AltName: Full=Sodium channel protein cardiac musc" 82.17 2016 100.00 100.00 5.04e-63 SP Q9JJV9 "RecName: Full=Sodium channel protein type 5 subunit alpha; AltName: Full=Sodium channel protein cardiac muscle subunit alpha; A" 82.17 2019 98.11 98.11 1.38e-61 TPG DAA17127 "TPA: voltage-gated sodium channel type V alpha [Bos taurus]" 82.17 2022 97.17 97.17 8.22e-61 TPG DAA34921 "TPA_inf: voltage-dependent sodium channel SCN5A [Monodelphis domestica]" 82.17 1840 98.11 99.06 5.96e-62 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $Nav1.5 Human 9606 Eukaryota Metazoa Homo sapiens SCN5A stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $Nav1.5 'recombinant technology' . Escherichia coli Bl21 pET28 'Construct retains 6x His tag (MGSSHHHHHHSSGLVPRGSHMAS)' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nav1.5 0.5 mM '[U-98% 13C; U-98% 15N]' TRIS 20 mM '[D-11 98 %]' glycine 100 mM '[D-5 98 %]' EDTA 0.1 mM '[D-16 98 %]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' NaN3 0.02 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.4 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.01 M pH 7.4 0.1 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $SPARKY stop_ loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '3D HNCACB' '3D HBHA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Nav1.5 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1773 24 GLU H H 8.324 0.005 1 2 1773 24 GLU HA H 4.140 0.010 1 3 1773 24 GLU HB2 H 1.813 0.010 2 4 1773 24 GLU HB3 H 1.879 0.010 2 5 1773 24 GLU C C 173.717 0.004 1 6 1773 24 GLU CA C 54.622 0.019 1 7 1773 24 GLU CB C 27.679 0.100 1 8 1773 24 GLU N N 121.574 0.023 1 9 1774 25 ASN H H 8.162 0.002 1 10 1774 25 ASN HA H 4.544 0.010 1 11 1774 25 ASN HB2 H 2.547 0.010 2 12 1774 25 ASN HB3 H 2.653 0.010 2 13 1774 25 ASN C C 172.379 0.020 1 14 1774 25 ASN CA C 50.895 0.043 1 15 1774 25 ASN CB C 36.609 0.100 1 16 1774 25 ASN N N 117.932 0.018 1 17 1775 26 PHE H H 7.983 0.003 1 18 1775 26 PHE HA H 4.520 0.010 1 19 1775 26 PHE HB2 H 2.921 0.010 2 20 1775 26 PHE HB3 H 3.058 0.010 2 21 1775 26 PHE C C 173.162 0.001 1 22 1775 26 PHE CA C 55.537 0.074 1 23 1775 26 PHE CB C 37.166 0.100 1 24 1775 26 PHE N N 119.963 0.038 1 25 1776 27 SER H H 8.072 0.001 1 26 1776 27 SER HA H 4.360 0.010 1 27 1776 27 SER HB2 H 3.718 0.010 2 28 1776 27 SER HB3 H 3.718 0.010 2 29 1776 27 SER C C 171.742 0.100 1 30 1776 27 SER CA C 55.841 0.027 1 31 1776 27 SER CB C 61.639 0.002 1 32 1776 27 SER N N 116.885 0.026 1 33 1777 28 VAL H H 7.965 0.002 1 34 1777 28 VAL HA H 4.052 0.010 1 35 1777 28 VAL HB H 2.002 0.010 1 36 1777 28 VAL C C 173.370 0.002 1 37 1777 28 VAL CA C 59.692 0.012 1 38 1777 28 VAL CB C 30.514 0.100 1 39 1777 28 VAL N N 120.735 0.019 1 40 1778 29 ALA H H 8.275 0.002 1 41 1778 29 ALA HA H 4.311 0.010 1 42 1778 29 ALA HB H 1.304 0.010 1 43 1778 29 ALA C C 175.477 0.002 1 44 1778 29 ALA CA C 50.220 0.034 1 45 1778 29 ALA CB C 16.987 0.006 1 46 1778 29 ALA N N 127.031 0.021 1 47 1779 30 THR H H 8.020 0.002 1 48 1779 30 THR HB H 4.193 0.010 1 49 1779 30 THR C C 172.345 0.002 1 50 1779 30 THR CA C 59.561 0.046 1 51 1779 30 THR CB C 67.531 0.006 1 52 1779 30 THR N N 112.913 0.026 1 53 1780 31 GLU H H 8.345 0.002 1 54 1780 31 GLU HA H 4.231 0.010 1 55 1780 31 GLU HB2 H 1.857 0.010 2 56 1780 31 GLU HB3 H 1.997 0.010 2 57 1780 31 GLU C C 174.069 0.003 1 58 1780 31 GLU CA C 54.517 0.100 1 59 1780 31 GLU CB C 27.951 0.100 1 60 1780 31 GLU N N 122.146 0.020 1 61 1781 32 GLU H H 8.321 0.002 1 62 1781 32 GLU CA C 54.272 0.100 1 63 1781 32 GLU CB C 27.978 0.100 1 64 1781 32 GLU N N 120.965 0.052 1 65 1782 33 SER HA H 4.446 0.010 1 66 1782 33 SER HB2 H 3.796 0.010 2 67 1782 33 SER HB3 H 3.796 0.010 2 68 1782 33 SER C C 172.301 0.100 1 69 1782 33 SER CA C 55.894 0.032 1 70 1782 33 SER CB C 61.622 0.100 1 71 1783 34 THR H H 8.164 0.003 1 72 1783 34 THR HA H 4.139 0.010 1 73 1783 34 THR HB H 4.310 0.010 1 74 1783 34 THR C C 171.973 0.005 1 75 1783 34 THR CA C 59.311 0.006 1 76 1783 34 THR CB C 67.559 0.005 1 77 1783 34 THR N N 115.697 0.030 1 78 1784 35 GLU H H 8.323 0.003 1 79 1784 35 GLU HA H 4.306 0.010 1 80 1784 35 GLU HB2 H 2.156 0.010 2 81 1784 35 GLU HB3 H 1.716 0.010 2 82 1784 35 GLU C C 172.832 0.100 1 83 1784 35 GLU CA C 51.949 0.100 1 84 1784 35 GLU CB C 27.672 0.100 1 85 1784 35 GLU N N 123.813 0.028 1 86 1785 36 PRO C C 173.965 0.100 1 87 1785 36 PRO CA C 61.531 0.100 1 88 1785 36 PRO CB C 30.062 0.100 1 89 1786 37 LEU H H 7.430 0.003 1 90 1786 37 LEU HA H 4.533 0.010 1 91 1786 37 LEU HB2 H 1.464 0.010 2 92 1786 37 LEU HB3 H 1.135 0.010 2 93 1786 37 LEU C C 173.568 0.003 1 94 1786 37 LEU CA C 51.301 0.054 1 95 1786 37 LEU CB C 42.215 0.016 1 96 1786 37 LEU N N 116.998 0.028 1 97 1787 38 SER H H 9.423 0.003 1 98 1787 38 SER HA H 4.666 0.010 1 99 1787 38 SER HB2 H 4.163 0.010 2 100 1787 38 SER HB3 H 3.843 0.010 2 101 1787 38 SER C C 172.876 0.003 1 102 1787 38 SER CA C 54.386 0.032 1 103 1787 38 SER CB C 64.328 0.022 1 104 1787 38 SER N N 118.947 0.037 1 105 1788 39 GLU H H 8.970 0.002 1 106 1788 39 GLU HA H 4.282 0.120 1 107 1788 39 GLU HB2 H 2.624 0.010 2 108 1788 39 GLU HB3 H 2.474 0.010 2 109 1788 39 GLU C C 176.020 0.007 1 110 1788 39 GLU CA C 57.782 0.027 1 111 1788 39 GLU CB C 27.154 0.001 1 112 1788 39 GLU N N 120.816 0.036 1 113 1789 40 ASP H H 8.087 0.002 1 114 1789 40 ASP C C 176.273 0.016 1 115 1789 40 ASP CA C 54.873 0.004 1 116 1789 40 ASP CB C 38.255 0.100 1 117 1789 40 ASP N N 116.754 0.039 1 118 1790 41 ASP H H 7.676 0.004 1 119 1790 41 ASP HA H 4.335 0.010 1 120 1790 41 ASP HB2 H 2.602 0.010 2 121 1790 41 ASP HB3 H 2.148 0.010 2 122 1790 41 ASP C C 176.019 0.003 1 123 1790 41 ASP CA C 55.537 0.078 1 124 1790 41 ASP CB C 38.799 0.100 1 125 1790 41 ASP N N 120.025 0.021 1 126 1791 42 PHE H H 7.457 0.001 1 127 1791 42 PHE HA H 4.083 0.010 1 128 1791 42 PHE HB2 H 3.031 0.010 2 129 1791 42 PHE HB3 H 3.031 0.010 2 130 1791 42 PHE C C 174.943 0.017 1 131 1791 42 PHE CA C 59.365 0.059 1 132 1791 42 PHE CB C 36.058 0.014 1 133 1791 42 PHE N N 118.306 0.020 1 134 1792 43 ASP H H 8.456 0.002 1 135 1792 43 ASP HA H 4.579 0.010 1 136 1792 43 ASP HB2 H 2.864 0.010 2 137 1792 43 ASP HB3 H 2.785 0.010 2 138 1792 43 ASP C C 176.855 0.100 1 139 1792 43 ASP CA C 55.791 0.100 1 140 1792 43 ASP CB C 37.855 0.100 1 141 1792 43 ASP N N 119.469 0.036 1 142 1793 44 MET H H 7.913 0.002 1 143 1793 44 MET C C 175.153 0.020 1 144 1793 44 MET CA C 56.183 0.100 1 145 1793 44 MET N N 120.021 0.022 1 146 1794 45 PHE H H 7.976 0.005 1 147 1794 45 PHE HA H 3.815 0.010 1 148 1794 45 PHE C C 174.922 0.009 1 149 1794 45 PHE CA C 59.455 0.100 1 150 1794 45 PHE N N 120.763 0.063 1 151 1795 46 TYR H H 8.256 0.004 1 152 1795 46 TYR HA H 4.310 0.010 1 153 1795 46 TYR HB2 H 3.025 0.010 2 154 1795 46 TYR HB3 H 2.754 0.010 2 155 1795 46 TYR C C 176.063 0.004 1 156 1795 46 TYR CA C 60.441 0.028 1 157 1795 46 TYR CB C 35.481 0.100 1 158 1795 46 TYR N N 116.296 0.024 1 159 1796 47 GLU H H 8.295 0.003 1 160 1796 47 GLU HA H 4.114 0.010 1 161 1796 47 GLU HB2 H 2.235 0.010 2 162 1796 47 GLU HB3 H 2.235 0.010 2 163 1796 47 GLU C C 176.946 0.002 1 164 1796 47 GLU CA C 57.483 0.056 1 165 1796 47 GLU CB C 27.247 0.074 1 166 1796 47 GLU N N 122.595 0.059 1 167 1797 48 ILE H H 8.047 0.004 1 168 1797 48 ILE HA H 3.849 0.010 1 169 1797 48 ILE HB H 1.982 0.010 1 170 1797 48 ILE C C 176.739 0.002 1 171 1797 48 ILE CA C 59.910 0.028 1 172 1797 48 ILE CB C 32.462 0.007 1 173 1797 48 ILE N N 119.144 0.027 1 174 1798 49 TRP H H 9.123 0.001 1 175 1798 49 TRP HA H 3.633 0.010 1 176 1798 49 TRP HB2 H 2.850 0.010 2 177 1798 49 TRP HB3 H 3.328 0.010 2 178 1798 49 TRP C C 175.548 0.004 1 179 1798 49 TRP CA C 59.840 0.027 1 180 1798 49 TRP CB C 26.479 0.014 1 181 1798 49 TRP N N 122.260 0.028 1 182 1799 50 GLU H H 7.884 0.002 1 183 1799 50 GLU HA H 3.870 0.010 1 184 1799 50 GLU HB2 H 2.190 0.010 2 185 1799 50 GLU HB3 H 2.130 0.010 2 186 1799 50 GLU C C 175.904 0.012 1 187 1799 50 GLU CA C 56.931 0.018 1 188 1799 50 GLU CB C 27.424 0.002 1 189 1799 50 GLU N N 115.046 0.025 1 190 1800 51 LYS H H 7.383 0.003 1 191 1800 51 LYS HA H 3.871 0.010 1 192 1800 51 LYS HB2 H 1.972 0.010 2 193 1800 51 LYS HB3 H 1.652 0.010 2 194 1800 51 LYS C C 175.822 0.014 1 195 1800 51 LYS CA C 56.176 0.031 1 196 1800 51 LYS CB C 29.576 0.100 1 197 1800 51 LYS N N 115.520 0.026 1 198 1801 52 PHE H H 7.346 0.004 1 199 1801 52 PHE HA H 4.038 0.010 1 200 1801 52 PHE HB2 H 2.659 0.010 2 201 1801 52 PHE HB3 H 2.159 0.010 2 202 1801 52 PHE C C 171.972 0.003 1 203 1801 52 PHE CA C 56.821 0.017 1 204 1801 52 PHE CB C 37.828 0.100 1 205 1801 52 PHE N N 115.954 0.038 1 206 1802 53 ASP H H 7.746 0.002 1 207 1802 53 ASP C C 171.356 0.100 1 208 1802 53 ASP CA C 49.382 0.036 1 209 1802 53 ASP CB C 37.098 0.100 1 210 1802 53 ASP N N 119.232 0.021 1 211 1803 54 PRO HA H 4.507 0.010 1 212 1803 54 PRO HB2 H 2.274 0.010 2 213 1803 54 PRO HB3 H 1.939 0.010 2 214 1803 54 PRO C C 176.500 0.100 1 215 1803 54 PRO CA C 62.930 0.044 1 216 1803 54 PRO CB C 29.590 0.100 1 217 1804 55 GLU H H 8.927 0.002 1 218 1804 55 GLU HB2 H 2.224 0.010 2 219 1804 55 GLU C C 173.420 0.100 1 220 1804 55 GLU CA C 53.537 0.055 1 221 1804 55 GLU CB C 26.238 0.026 1 222 1804 55 GLU N N 116.468 0.022 1 223 1805 56 ALA H H 8.233 0.001 1 224 1805 56 ALA HA H 4.225 0.010 1 225 1805 56 ALA HB H 1.338 0.010 1 226 1805 56 ALA C C 175.334 0.100 1 227 1805 56 ALA CA C 51.109 0.100 1 228 1805 56 ALA CB C 13.716 0.003 1 229 1805 56 ALA N N 121.896 0.014 1 230 1806 57 THR H H 9.766 0.003 1 231 1806 57 THR HA H 4.181 0.010 1 232 1806 57 THR HB H 4.397 0.010 1 233 1806 57 THR C C 174.785 0.004 1 234 1806 57 THR CA C 62.265 0.039 1 235 1806 57 THR CB C 68.886 0.009 1 236 1806 57 THR N N 113.970 0.029 1 237 1807 58 GLN H H 10.443 0.002 1 238 1807 58 GLN HA H 3.508 0.010 1 239 1807 58 GLN HB2 H 1.695 0.010 2 240 1807 58 GLN HB3 H 2.258 0.010 2 241 1807 58 GLN C C 170.643 0.013 1 242 1807 58 GLN CA C 56.197 0.005 1 243 1807 58 GLN CB C 24.264 0.014 1 244 1807 58 GLN N N 113.293 0.025 1 245 1808 59 PHE H H 8.388 0.003 1 246 1808 59 PHE HA H 5.531 0.010 1 247 1808 59 PHE HB2 H 2.700 0.010 2 248 1808 59 PHE HB3 H 2.700 0.010 2 249 1808 59 PHE C C 172.575 0.004 1 250 1808 59 PHE CA C 54.583 0.100 1 251 1808 59 PHE CB C 41.892 0.012 1 252 1808 59 PHE N N 117.021 0.019 1 253 1809 60 ILE H H 8.411 0.003 1 254 1809 60 ILE HB H 1.309 0.010 1 255 1809 60 ILE C C 172.374 0.003 1 256 1809 60 ILE CA C 57.061 0.062 1 257 1809 60 ILE CB C 39.550 0.015 1 258 1809 60 ILE N N 112.166 0.023 1 259 1810 61 GLU H H 8.310 0.009 1 260 1810 61 GLU HA H 4.543 0.010 1 261 1810 61 GLU HB2 H 2.266 0.010 2 262 1810 61 GLU HB3 H 1.922 0.010 2 263 1810 61 GLU C C 175.546 0.004 1 264 1810 61 GLU CA C 54.230 0.016 1 265 1810 61 GLU CB C 28.692 0.025 1 266 1810 61 GLU N N 121.853 0.064 1 267 1811 62 TYR H H 9.047 0.003 1 268 1811 62 TYR HA H 3.908 0.010 1 269 1811 62 TYR HB2 H 3.182 0.010 2 270 1811 62 TYR HB3 H 3.056 0.010 2 271 1811 62 TYR C C 175.707 0.002 1 272 1811 62 TYR CA C 59.444 0.046 1 273 1811 62 TYR CB C 36.260 0.005 1 274 1811 62 TYR N N 123.169 0.100 1 275 1812 63 SER H H 8.586 0.001 1 276 1812 63 SER HA H 3.972 0.010 1 277 1812 63 SER C C 173.544 0.100 1 278 1812 63 SER CA C 58.825 0.002 1 279 1812 63 SER CB C 60.273 0.001 1 280 1812 63 SER N N 110.997 0.017 1 281 1813 64 VAL H H 7.449 0.002 1 282 1813 64 VAL HA H 4.643 0.010 1 283 1813 64 VAL HB H 2.564 0.010 1 284 1813 64 VAL C C 173.670 0.005 1 285 1813 64 VAL CA C 59.123 0.100 1 286 1813 64 VAL CB C 30.068 0.002 1 287 1813 64 VAL N N 116.235 0.029 1 288 1814 65 LEU H H 7.644 0.001 1 289 1814 65 LEU HA H 3.813 0.010 1 290 1814 65 LEU HB2 H 1.699 0.010 2 291 1814 65 LEU HB3 H 1.272 0.010 2 292 1814 65 LEU C C 174.987 0.003 1 293 1814 65 LEU CA C 55.779 0.007 1 294 1814 65 LEU CB C 39.887 0.012 1 295 1814 65 LEU N N 123.860 0.029 1 296 1815 66 SER H H 8.339 0.002 1 297 1815 66 SER HA H 3.880 0.010 1 298 1815 66 SER C C 175.635 0.100 1 299 1815 66 SER CA C 58.965 0.011 1 300 1815 66 SER CB C 60.174 0.006 1 301 1815 66 SER N N 111.395 0.011 1 302 1816 67 ASP H H 7.683 0.005 1 303 1816 67 ASP HA H 4.209 0.010 1 304 1816 67 ASP HB2 H 2.897 0.010 2 305 1816 67 ASP HB3 H 2.757 0.010 2 306 1816 67 ASP C C 175.880 0.100 1 307 1816 67 ASP CA C 55.071 0.100 1 308 1816 67 ASP CB C 38.055 0.070 1 309 1816 67 ASP N N 119.923 0.028 1 310 1817 68 PHE H H 8.076 0.002 1 311 1817 68 PHE HA H 3.058 0.010 1 312 1817 68 PHE HB2 H 2.525 0.010 2 313 1817 68 PHE HB3 H 1.703 0.010 2 314 1817 68 PHE C C 173.060 0.100 1 315 1817 68 PHE CA C 58.861 0.024 1 316 1817 68 PHE CB C 36.362 0.003 1 317 1817 68 PHE N N 122.344 0.038 1 318 1818 69 ALA H H 8.677 0.010 1 319 1818 69 ALA C C 176.624 0.003 1 320 1818 69 ALA CA C 52.300 0.011 1 321 1818 69 ALA CB C 16.659 0.100 1 322 1818 69 ALA N N 117.604 0.009 1 323 1819 70 ASP H H 7.037 0.004 1 324 1819 70 ASP HA H 4.253 0.010 1 325 1819 70 ASP HB3 H 2.526 0.010 2 326 1819 70 ASP C C 173.441 0.004 1 327 1819 70 ASP CA C 53.834 0.042 1 328 1819 70 ASP CB C 42.751 0.004 1 329 1819 70 ASP N N 112.904 0.014 1 330 1820 71 ALA H H 7.332 0.001 1 331 1820 71 ALA HA H 4.101 0.010 1 332 1820 71 ALA HB H 1.461 0.010 1 333 1820 71 ALA C C 175.507 0.100 1 334 1820 71 ALA CA C 50.368 0.017 1 335 1820 71 ALA CB C 17.053 0.003 1 336 1820 71 ALA N N 119.791 0.026 1 337 1821 72 LEU H H 6.242 0.004 1 338 1821 72 LEU HA H 3.936 0.010 1 339 1821 72 LEU C C 173.513 0.100 1 340 1821 72 LEU CA C 52.313 0.017 1 341 1821 72 LEU CB C 41.115 0.005 1 342 1821 72 LEU N N 115.588 0.031 1 343 1822 73 SER H H 7.986 0.003 1 344 1822 73 SER C C 174.058 0.005 1 345 1822 73 SER CA C 55.329 0.041 1 346 1822 73 SER CB C 61.954 0.003 1 347 1822 73 SER N N 113.226 0.019 1 348 1823 74 GLU H H 9.058 0.002 1 349 1823 74 GLU C C 173.423 0.100 1 350 1823 74 GLU CA C 54.919 0.100 1 351 1823 74 GLU CB C 25.661 0.100 1 352 1823 74 GLU N N 124.576 0.031 1 353 1824 75 PRO HA H 4.737 0.010 1 354 1824 75 PRO HB2 H 2.171 0.010 2 355 1824 75 PRO HB3 H 2.171 0.010 2 356 1824 75 PRO C C 173.035 0.100 1 357 1824 75 PRO CA C 61.275 0.100 1 358 1824 75 PRO CB C 31.921 0.100 1 359 1825 76 LEU H H 7.502 0.003 1 360 1825 76 LEU HA H 3.935 0.010 1 361 1825 76 LEU HB2 H 1.430 0.010 2 362 1825 76 LEU HB3 H 1.754 0.010 2 363 1825 76 LEU C C 173.105 0.001 1 364 1825 76 LEU CA C 54.519 0.008 1 365 1825 76 LEU CB C 41.680 0.031 1 366 1825 76 LEU N N 121.733 0.022 1 367 1826 77 ARG H H 6.605 0.004 1 368 1826 77 ARG HA H 3.654 0.010 1 369 1826 77 ARG HB2 H 1.146 0.010 2 370 1826 77 ARG HB3 H 1.037 0.010 2 371 1826 77 ARG C C 172.957 0.003 1 372 1826 77 ARG CA C 54.685 0.019 1 373 1826 77 ARG CB C 28.904 0.001 1 374 1826 77 ARG N N 115.196 0.017 1 375 1827 78 ILE H H 7.060 0.003 1 376 1827 78 ILE HA H 3.941 0.010 1 377 1827 78 ILE HB H 1.413 0.010 1 378 1827 78 ILE C C 172.499 0.100 1 379 1827 78 ILE CA C 58.339 0.021 1 380 1827 78 ILE CB C 35.001 0.009 1 381 1827 78 ILE N N 125.398 0.025 1 382 1828 79 ALA H H 8.407 0.001 1 383 1828 79 ALA HA H 4.358 0.010 1 384 1828 79 ALA HB H 1.141 0.010 1 385 1828 79 ALA C C 176.261 0.001 1 386 1828 79 ALA CA C 50.101 0.041 1 387 1828 79 ALA CB C 16.224 0.009 1 388 1828 79 ALA N N 128.817 0.027 1 389 1829 80 LYS H H 8.332 0.002 1 390 1829 80 LYS C C 173.033 0.100 1 391 1829 80 LYS CA C 53.906 0.100 1 392 1829 80 LYS CB C 29.905 0.100 1 393 1829 80 LYS N N 119.422 0.066 1 394 1832 83 GLN HA H 4.187 0.010 1 395 1832 83 GLN HB2 H 2.207 0.010 2 396 1832 83 GLN HB3 H 1.885 0.010 2 397 1832 83 GLN C C 176.044 0.100 1 398 1833 84 ILE H H 8.248 0.012 1 399 1833 84 ILE HA H 3.727 0.010 1 400 1833 84 ILE HB H 1.795 0.010 1 401 1833 84 ILE C C 175.556 0.032 1 402 1833 84 ILE CA C 61.614 0.100 1 403 1833 84 ILE N N 117.994 0.025 1 404 1834 85 SER H H 7.472 0.003 1 405 1834 85 SER HA H 4.072 0.010 1 406 1834 85 SER HB2 H 3.576 0.010 2 407 1834 85 SER HB3 H 3.682 0.010 2 408 1834 85 SER C C 174.183 0.100 1 409 1834 85 SER CA C 59.984 0.037 1 410 1834 85 SER N N 115.106 0.024 1 411 1835 86 LEU H H 7.627 0.004 1 412 1835 86 LEU C C 177.931 0.014 1 413 1835 86 LEU CA C 55.404 0.100 1 414 1835 86 LEU CB C 39.025 0.100 1 415 1835 86 LEU N N 119.335 0.054 1 416 1836 87 ILE H H 8.290 0.010 1 417 1836 87 ILE HA H 3.852 0.010 1 418 1836 87 ILE HB H 1.918 0.010 1 419 1836 87 ILE C C 176.740 0.032 1 420 1836 87 ILE CA C 62.444 0.017 1 421 1836 87 ILE N N 121.250 0.016 1 422 1837 88 ASN H H 7.723 0.005 1 423 1837 88 ASN HA H 4.533 0.010 1 424 1837 88 ASN HB2 H 2.830 0.010 2 425 1837 88 ASN HB3 H 2.745 0.010 2 426 1837 88 ASN C C 173.592 0.016 1 427 1837 88 ASN CA C 52.002 0.015 1 428 1837 88 ASN CB C 36.123 0.100 1 429 1837 88 ASN N N 117.052 0.046 1 430 1838 89 MET H H 7.376 0.002 1 431 1838 89 MET C C 173.120 0.100 1 432 1838 89 MET CA C 55.615 0.044 1 433 1838 89 MET CB C 31.030 0.100 1 434 1838 89 MET N N 118.055 0.025 1 435 1839 90 ASP H H 7.913 0.003 1 436 1839 90 ASP HA H 4.330 0.010 1 437 1839 90 ASP HB2 H 2.909 0.010 2 438 1839 90 ASP HB3 H 2.297 0.010 2 439 1839 90 ASP C C 172.957 0.171 1 440 1839 90 ASP CA C 51.895 0.038 1 441 1839 90 ASP CB C 37.087 0.021 1 442 1839 90 ASP N N 119.119 0.095 1 443 1840 91 LEU H H 8.730 0.004 1 444 1840 91 LEU C C 172.684 0.100 1 445 1840 91 LEU CA C 50.766 0.100 1 446 1840 91 LEU CB C 39.340 0.100 1 447 1840 91 LEU N N 121.397 0.027 1 448 1841 92 PRO C C 173.702 0.100 1 449 1841 92 PRO CA C 60.400 0.100 1 450 1842 93 MET H H 8.234 0.002 1 451 1842 93 MET HA H 5.118 0.010 1 452 1842 93 MET HB2 H 1.858 0.010 2 453 1842 93 MET HB3 H 1.858 0.010 2 454 1842 93 MET C C 174.657 0.001 1 455 1842 93 MET CA C 52.201 0.003 1 456 1842 93 MET CB C 33.849 0.004 1 457 1842 93 MET N N 121.156 0.031 1 458 1843 94 VAL H H 8.924 0.002 1 459 1843 94 VAL HA H 4.509 0.010 1 460 1843 94 VAL HB H 2.179 0.010 1 461 1843 94 VAL C C 173.517 0.004 1 462 1843 94 VAL CA C 57.858 0.020 1 463 1843 94 VAL CB C 31.418 0.008 1 464 1843 94 VAL N N 118.272 0.022 1 465 1844 95 SER H H 8.142 0.003 1 466 1844 95 SER HA H 4.067 0.010 1 467 1844 95 SER HB2 H 3.776 0.010 2 468 1844 95 SER HB3 H 3.776 0.010 2 469 1844 95 SER C C 172.406 0.100 1 470 1844 95 SER CA C 57.096 0.100 1 471 1844 95 SER CB C 60.716 0.006 1 472 1844 95 SER N N 114.589 0.025 1 473 1845 96 GLY H H 8.641 0.003 1 474 1845 96 GLY HA2 H 4.044 0.010 2 475 1845 96 GLY HA3 H 3.568 0.010 2 476 1845 96 GLY C C 171.961 0.005 1 477 1845 96 GLY CA C 43.227 0.100 1 478 1845 96 GLY N N 111.352 0.041 1 479 1846 97 ASP H H 8.292 0.002 1 480 1846 97 ASP HA H 4.482 0.010 1 481 1846 97 ASP HB2 H 3.005 0.010 2 482 1846 97 ASP HB3 H 2.844 0.010 2 483 1846 97 ASP C C 171.993 0.024 1 484 1846 97 ASP CA C 52.646 0.100 1 485 1846 97 ASP CB C 37.075 0.002 1 486 1846 97 ASP N N 118.735 0.014 1 487 1847 98 ARG H H 7.263 0.003 1 488 1847 98 ARG HA H 5.053 0.010 1 489 1847 98 ARG HB2 H 1.422 0.010 2 490 1847 98 ARG HB3 H 1.422 0.010 2 491 1847 98 ARG C C 172.927 0.002 1 492 1847 98 ARG CA C 52.974 0.019 1 493 1847 98 ARG CB C 30.721 0.005 1 494 1847 98 ARG N N 116.578 0.039 1 495 1848 99 ILE H H 9.195 0.001 1 496 1848 99 ILE HA H 4.718 0.010 1 497 1848 99 ILE HB H 1.643 0.010 1 498 1848 99 ILE C C 172.488 0.008 1 499 1848 99 ILE CA C 58.257 0.039 1 500 1848 99 ILE CB C 39.600 0.008 1 501 1848 99 ILE N N 119.583 0.044 1 502 1849 100 HIS H H 9.755 0.003 1 503 1849 100 HIS HA H 4.177 0.010 1 504 1849 100 HIS HB2 H 2.860 0.010 2 505 1849 100 HIS HB3 H 2.860 0.010 2 506 1849 100 HIS C C 174.563 0.015 1 507 1849 100 HIS CA C 55.791 0.026 1 508 1849 100 HIS CB C 30.053 0.003 1 509 1849 100 HIS N N 128.352 0.028 1 510 1850 101 CYS H H 7.953 0.004 1 511 1850 101 CYS HA H 2.870 0.010 1 512 1850 101 CYS HB2 H 1.458 0.010 2 513 1850 101 CYS HB3 H 1.458 0.010 2 514 1850 101 CYS C C 173.358 0.001 1 515 1850 101 CYS CA C 59.978 0.100 1 516 1850 101 CYS CB C 25.136 0.005 1 517 1850 101 CYS N N 125.946 0.031 1 518 1851 102 MET H H 10.064 0.009 1 519 1851 102 MET HA H 4.063 0.010 1 520 1851 102 MET HB2 H 1.834 0.010 2 521 1851 102 MET HB3 H 1.986 0.010 2 522 1851 102 MET C C 177.010 0.019 1 523 1851 102 MET CA C 55.431 0.026 1 524 1851 102 MET CB C 29.426 0.025 1 525 1851 102 MET N N 117.853 0.055 1 526 1852 103 ASP H H 7.204 0.001 1 527 1852 103 ASP HA H 4.584 0.010 1 528 1852 103 ASP HB2 H 2.859 0.010 2 529 1852 103 ASP HB3 H 2.579 0.010 2 530 1852 103 ASP C C 177.065 0.011 1 531 1852 103 ASP CA C 55.416 0.009 1 532 1852 103 ASP CB C 38.474 0.019 1 533 1852 103 ASP N N 118.283 0.030 1 534 1853 104 ILE H H 7.496 0.003 1 535 1853 104 ILE HA H 3.449 0.010 1 536 1853 104 ILE HB H 1.809 0.010 1 537 1853 104 ILE C C 174.222 0.009 1 538 1853 104 ILE CA C 62.314 0.015 1 539 1853 104 ILE CB C 34.827 0.018 1 540 1853 104 ILE N N 121.634 0.012 1 541 1854 105 LEU H H 8.614 0.003 1 542 1854 105 LEU HA H 3.353 0.010 1 543 1854 105 LEU HB2 H 1.402 0.010 2 544 1854 105 LEU HB3 H 0.871 0.010 2 545 1854 105 LEU C C 177.767 0.003 1 546 1854 105 LEU CA C 56.159 0.100 1 547 1854 105 LEU CB C 38.365 0.028 1 548 1854 105 LEU N N 120.044 0.029 1 549 1855 106 PHE H H 8.154 0.002 1 550 1855 106 PHE HB2 H 3.251 0.010 2 551 1855 106 PHE HB3 H 3.099 0.010 2 552 1855 106 PHE C C 174.976 0.006 1 553 1855 106 PHE CA C 59.230 0.100 1 554 1855 106 PHE CB C 36.528 0.100 1 555 1855 106 PHE N N 119.097 0.029 1 556 1856 107 ALA H H 7.843 0.003 1 557 1856 107 ALA HA H 4.015 0.010 1 558 1856 107 ALA HB H 1.751 0.010 1 559 1856 107 ALA C C 178.624 0.002 1 560 1856 107 ALA CA C 53.053 0.006 1 561 1856 107 ALA CB C 17.419 0.100 1 562 1856 107 ALA N N 120.872 0.008 1 563 1857 108 PHE H H 9.494 0.005 1 564 1857 108 PHE HB2 H 3.341 0.010 2 565 1857 108 PHE HB3 H 2.904 0.010 2 566 1857 108 PHE C C 176.672 0.003 1 567 1857 108 PHE CA C 57.346 0.100 1 568 1857 108 PHE CB C 34.903 0.100 1 569 1857 108 PHE N N 118.902 0.033 1 570 1858 109 THR H H 8.215 0.002 1 571 1858 109 THR HA H 3.727 0.010 1 572 1858 109 THR HB H 4.060 0.010 1 573 1858 109 THR C C 173.810 0.100 1 574 1858 109 THR CA C 64.548 0.100 1 575 1858 109 THR CB C 65.831 0.002 1 576 1858 109 THR N N 115.843 0.036 1 577 1859 110 LYS H H 8.003 0.002 1 578 1859 110 LYS HA H 3.726 0.010 1 579 1859 110 LYS HB2 H 1.625 0.010 2 580 1859 110 LYS HB3 H 1.625 0.010 2 581 1859 110 LYS C C 176.375 0.004 1 582 1859 110 LYS CA C 57.272 0.100 1 583 1859 110 LYS CB C 29.506 0.006 1 584 1859 110 LYS N N 122.522 0.047 1 585 1860 111 ARG H H 7.293 0.003 1 586 1860 111 ARG HA H 3.923 0.010 1 587 1860 111 ARG HB3 H 1.670 0.010 2 588 1860 111 ARG C C 175.375 0.100 1 589 1860 111 ARG CA C 56.553 0.100 1 590 1860 111 ARG CB C 27.216 0.005 1 591 1860 111 ARG N N 117.287 0.043 1 592 1861 112 VAL H H 6.986 0.002 1 593 1861 112 VAL HA H 3.716 0.010 1 594 1861 112 VAL HB H 2.090 0.010 1 595 1861 112 VAL C C 175.183 0.006 1 596 1861 112 VAL CA C 62.641 0.008 1 597 1861 112 VAL CB C 29.849 0.009 1 598 1861 112 VAL N N 116.699 0.023 1 599 1862 113 LEU H H 7.936 0.003 1 600 1862 113 LEU HA H 4.074 0.010 1 601 1862 113 LEU HB2 H 1.647 0.010 2 602 1862 113 LEU HB3 H 1.464 0.010 2 603 1862 113 LEU C C 176.298 0.003 1 604 1862 113 LEU CA C 54.118 0.100 1 605 1862 113 LEU CB C 39.907 0.100 1 606 1862 113 LEU N N 118.610 0.061 1 607 1863 114 GLY H H 7.946 0.002 1 608 1863 114 GLY HA2 H 3.903 0.010 2 609 1863 114 GLY HA3 H 3.859 0.010 2 610 1863 114 GLY C C 172.049 0.011 1 611 1863 114 GLY CA C 43.201 0.015 1 612 1863 114 GLY N N 106.535 0.030 1 613 1864 115 GLU H H 8.083 0.001 1 614 1864 115 GLU HA H 4.234 0.010 1 615 1864 115 GLU HB2 H 1.982 0.010 2 616 1864 115 GLU HB3 H 1.846 0.010 2 617 1864 115 GLU C C 174.593 0.100 1 618 1864 115 GLU CA C 54.283 0.034 1 619 1864 115 GLU CB C 28.008 0.100 1 620 1864 115 GLU N N 119.887 0.020 1 621 1865 116 SER H H 8.252 0.002 1 622 1865 116 SER HA H 4.385 0.010 1 623 1865 116 SER HB2 H 3.836 0.010 2 624 1865 116 SER HB3 H 3.836 0.010 2 625 1865 116 SER C C 172.858 0.100 1 626 1865 116 SER CA C 56.490 0.007 1 627 1865 116 SER CB C 61.625 0.009 1 628 1865 116 SER N N 116.312 0.100 1 629 1866 117 GLY H H 8.293 0.002 1 630 1866 117 GLY HA2 H 3.901 0.010 2 631 1866 117 GLY HA3 H 3.901 0.010 2 632 1866 117 GLY C C 172.066 0.003 1 633 1866 117 GLY CA C 43.231 0.003 1 634 1866 117 GLY N N 110.195 0.027 1 635 1867 118 GLU H H 8.221 0.004 1 636 1867 118 GLU HA H 4.192 0.010 1 637 1867 118 GLU HB3 H 1.910 0.060 2 638 1867 118 GLU C C 174.690 0.003 1 639 1867 118 GLU CA C 54.613 0.003 1 640 1867 118 GLU CB C 27.853 0.100 1 641 1867 118 GLU N N 120.303 0.028 1 642 1868 119 MET H H 8.293 0.003 1 643 1868 119 MET C C 174.283 0.100 1 644 1868 119 MET CA C 53.712 0.100 1 645 1868 119 MET CB C 30.433 0.100 1 646 1868 119 MET N N 120.267 0.053 1 647 1869 120 ASP H H 8.221 0.003 1 648 1869 120 ASP HA H 4.417 0.010 1 649 1869 120 ASP HB2 H 2.582 0.010 2 650 1869 120 ASP HB3 H 2.582 0.010 2 651 1869 120 ASP C C 174.313 0.011 1 652 1869 120 ASP CA C 52.891 0.030 1 653 1869 120 ASP CB C 38.645 0.003 1 654 1869 120 ASP N N 121.003 0.014 1 655 1870 121 ALA H H 8.038 0.002 1 656 1870 121 ALA HA H 4.113 0.010 1 657 1870 121 ALA HB H 1.311 0.010 1 658 1870 121 ALA C C 175.993 0.001 1 659 1870 121 ALA CA C 51.068 0.007 1 660 1870 121 ALA CB C 16.630 0.005 1 661 1870 121 ALA N N 123.029 0.022 1 662 1871 122 LEU H H 7.910 0.004 1 663 1871 122 LEU HB2 H 1.610 0.010 2 664 1871 122 LEU HB3 H 1.506 0.010 2 665 1871 122 LEU C C 175.301 0.002 1 666 1871 122 LEU CA C 53.380 0.100 1 667 1871 122 LEU CB C 39.684 0.100 1 668 1871 122 LEU N N 118.946 0.053 1 669 1872 123 LYS H H 7.894 0.003 1 670 1872 123 LYS HA H 4.139 0.010 1 671 1872 123 LYS HB2 H 1.715 0.010 2 672 1872 123 LYS HB3 H 1.715 0.010 2 673 1872 123 LYS C C 174.481 0.100 1 674 1872 123 LYS CA C 54.570 0.005 1 675 1872 123 LYS CB C 30.413 0.100 1 676 1872 123 LYS N N 120.836 0.023 1 677 1873 124 ILE H H 7.824 0.004 1 678 1873 124 ILE HA H 3.982 0.010 1 679 1873 124 ILE HB H 1.747 0.010 1 680 1873 124 ILE C C 174.061 0.003 1 681 1873 124 ILE CA C 59.274 0.003 1 682 1873 124 ILE CB C 36.298 0.100 1 683 1873 124 ILE N N 120.559 0.042 1 684 1874 125 GLN H H 8.193 0.004 1 685 1874 125 GLN C C 173.657 0.007 1 686 1874 125 GLN CA C 53.677 0.100 1 687 1874 125 GLN CB C 27.034 0.100 1 688 1874 125 GLN N N 123.238 0.018 1 689 1875 126 MET H H 8.259 0.005 1 690 1875 126 MET CB C 30.817 0.100 1 691 1875 126 MET N N 121.283 0.060 1 692 1876 127 GLU HA H 4.197 0.010 1 693 1876 127 GLU HB2 H 1.944 0.010 2 694 1876 127 GLU HB3 H 1.855 0.010 2 695 1876 127 GLU C C 173.844 0.100 1 696 1877 128 GLU H H 8.315 0.004 1 697 1877 128 GLU HA H 4.196 0.010 1 698 1877 128 GLU HB2 H 1.966 0.010 2 699 1877 128 GLU HB3 H 1.841 0.010 2 700 1877 128 GLU C C 173.063 0.002 1 701 1877 128 GLU CA C 54.296 0.032 1 702 1877 128 GLU CB C 27.991 0.037 1 703 1877 128 GLU N N 122.641 0.034 1 704 1878 129 LYS H H 7.868 0.002 1 705 1878 129 LYS C C 178.902 0.100 1 706 1878 129 LYS CA C 55.201 0.100 1 707 1878 129 LYS CB C 31.473 0.100 1 708 1878 129 LYS N N 127.635 0.027 1 stop_ save_