data_16032 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Nav1.2 C-terminal EF-Hand Domain ; _BMRB_accession_number 16032 _BMRB_flat_file_name bmr16032.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 'Solution structure of the human Voltage-gated Sodium Channel, brain isoform (Nav1.2)' 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 structure_coordinate_set 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 631 "13C chemical shifts" 344 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-27 update BMRB 'edit entity/assembly name' 2009-03-04 update BMRB 'complete entry citation' 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 . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'NaV1.2 C-terminal EF-hand domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NaV1.2 C-terminal EF-hand domain' $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'NaV1.2 C-terminal EF-hand domain' _Molecular_mass 12130.777 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MASENFSVATEESAEPLSED DFEMFYEVWEKFDPDATQFI EFAKLSDFADALDPPLLIAK PNKVQLIAMDLPMVSGDRIH CLDILFAFTKRVLGESGEMD ALRIQMEER ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1754 MET 2 1755 GLY 3 1756 SER 4 1757 SER 5 1758 HIS 6 1759 HIS 7 1760 HIS 8 1761 HIS 9 1762 HIS 10 1763 HIS 11 1764 SER 12 1765 SER 13 1766 GLY 14 1767 LEU 15 1768 VAL 16 1769 PRO 17 1770 ARG 18 1771 GLY 19 1772 SER 20 1773 HIS 21 1774 MET 22 1775 ALA 23 1776 SER 24 1777 GLU 25 1778 ASN 26 1779 PHE 27 1780 SER 28 1781 VAL 29 1782 ALA 30 1783 THR 31 1784 GLU 32 1785 GLU 33 1786 SER 34 1787 ALA 35 1788 GLU 36 1789 PRO 37 1790 LEU 38 1791 SER 39 1792 GLU 40 1793 ASP 41 1794 ASP 42 1795 PHE 43 1796 GLU 44 1797 MET 45 1798 PHE 46 1799 TYR 47 1800 GLU 48 1801 VAL 49 1802 TRP 50 1803 GLU 51 1804 LYS 52 1805 PHE 53 1806 ASP 54 1807 PRO 55 1808 ASP 56 1809 ALA 57 1810 THR 58 1811 GLN 59 1812 PHE 60 1813 ILE 61 1814 GLU 62 1815 PHE 63 1816 ALA 64 1817 LYS 65 1818 LEU 66 1819 SER 67 1820 ASP 68 1821 PHE 69 1822 ALA 70 1823 ASP 71 1824 ALA 72 1825 LEU 73 1826 ASP 74 1827 PRO 75 1828 PRO 76 1829 LEU 77 1830 LEU 78 1831 ILE 79 1832 ALA 80 1833 LYS 81 1834 PRO 82 1835 ASN 83 1836 LYS 84 1837 VAL 85 1838 GLN 86 1839 LEU 87 1840 ILE 88 1841 ALA 89 1842 MET 90 1843 ASP 91 1844 LEU 92 1845 PRO 93 1846 MET 94 1847 VAL 95 1848 SER 96 1849 GLY 97 1850 ASP 98 1851 ARG 99 1852 ILE 100 1853 HIS 101 1854 CYS 102 1855 LEU 103 1856 ASP 104 1857 ILE 105 1858 LEU 106 1859 PHE 107 1860 ALA 108 1861 PHE 109 1862 THR 110 1863 LYS 111 1864 ARG 112 1865 VAL 113 1866 LEU 114 1867 GLY 115 1868 GLU 116 1869 SER 117 1870 GLY 118 1871 GLU 119 1872 MET 120 1873 ASP 121 1874 ALA 122 1875 LEU 123 1876 ARG 124 1877 ILE 125 1878 GLN 126 1879 MET 127 1880 GLU 128 1881 GLU 129 1882 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-26 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 2KAV "Solution Structure Of The Human Voltage-Gated Sodium Channel, Brain Isoform (Nav1.2)" 100.00 129 100.00 100.00 3.28e-88 PDB 4JPZ "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" 100.00 184 100.00 100.00 1.62e-89 DBJ BAA92594 "KIAA1356 protein [Homo sapiens]" 82.17 519 97.17 99.06 3.55e-65 DBJ BAC27748 "unnamed protein product [Mus musculus]" 82.17 404 98.11 98.11 1.40e-65 DBJ BAC30078 "unnamed protein product [Mus musculus]" 82.17 253 98.11 98.11 3.18e-68 DBJ BAG63295 "unnamed protein product [Homo sapiens]" 82.17 483 97.17 99.06 1.64e-65 DBJ BAK62861 "sodium channel protein type 3 subunit alpha [Pan troglodytes]" 82.17 468 97.17 99.06 1.01e-65 EMBL CAA27287 "unnamed protein product [Rattus norvegicus]" 82.17 2005 98.11 98.11 2.87e-63 EMBL CAA46438 "brain type II sodium channel alpha-subunit (HBSC II) [Homo sapiens]" 82.17 245 100.00 100.00 8.71e-69 EMBL CAA68735 "unnamed protein product [Rattus norvegicus]" 82.17 1951 97.17 98.11 2.84e-63 EMBL CAB85895 "type III sodium channel protein [Homo sapiens]" 82.17 1951 97.17 99.06 2.32e-63 GB AAA18895 "voltage-gated sodium channel [Homo sapiens]" 82.17 2005 100.00 100.00 5.52e-65 GB AAA67695 "sodium channel, partial [Mus musculus]" 82.17 510 98.11 98.11 1.09e-66 GB AAB22226 "human brain sodium channel subtype II, HBSC II [human, brain, Peptide Partial, 303 aa]" 82.17 303 100.00 100.00 1.64e-68 GB AAG53412 "voltage-gated sodium channel type II alpha subunit [Homo sapiens]" 82.17 2005 100.00 100.00 5.52e-65 GB AAG53413 "voltage-gated sodium channel type II alpha subunit [Homo sapiens]" 82.17 2005 100.00 100.00 5.52e-65 PIR S29185 "sodium channel protein II - human (fragment)" 82.17 303 100.00 100.00 1.64e-68 PRF 1204264B "Na channel II protein" 82.17 2005 98.11 98.11 2.87e-63 REF NP_001035232 "sodium channel protein type 2 subunit alpha isoform 1 [Homo sapiens]" 82.17 2005 100.00 100.00 5.52e-65 REF NP_001035233 "sodium channel protein type 2 subunit alpha isoform 2 [Homo sapiens]" 82.17 2005 100.00 100.00 5.52e-65 REF NP_001075145 "sodium channel protein type 3 subunit alpha isoform 2 [Homo sapiens]" 82.17 1951 97.17 99.06 2.58e-63 REF NP_001075146 "sodium channel protein type 3 subunit alpha isoform 3 [Homo sapiens]" 82.17 1951 97.17 99.06 2.32e-63 REF NP_001092768 "sodium channel protein type 2 subunit alpha [Mus musculus]" 82.17 2006 98.11 98.11 2.88e-63 SP P04775 "RecName: Full=Sodium channel protein type 2 subunit alpha; AltName: Full=Sodium channel protein brain II subunit alpha; AltName" 82.17 2005 98.11 98.11 2.87e-63 SP P08104 "RecName: Full=Sodium channel protein type 3 subunit alpha; AltName: Full=Sodium channel protein brain III subunit alpha; AltNam" 82.17 1951 97.17 98.11 2.84e-63 SP Q99250 "RecName: Full=Sodium channel protein type 2 subunit alpha; AltName: Full=HBSC II; AltName: Full=Sodium channel protein brain II" 82.17 2005 100.00 100.00 5.52e-65 SP Q9NY46 "RecName: Full=Sodium channel protein type 3 subunit alpha; AltName: Full=Sodium channel protein brain III subunit alpha; AltNam" 82.17 2000 97.17 99.06 2.76e-63 TPG DAA32692 "TPA: sodium channel, voltage-gated, type II, alpha subunit [Bos taurus]" 82.17 2006 98.11 99.06 1.81e-63 TPG DAA32708 "TPA: sodium channel, voltage-gated, type III, alpha subunit isoform 1 [Bos taurus]" 82.17 1999 97.17 99.06 1.98e-63 TPG DAA32709 "TPA: sodium channel, voltage-gated, type III, alpha subunit isoform 2 [Bos taurus]" 82.17 2000 97.17 99.06 1.96e-63 TPG DAA32710 "TPA: sodium channel, voltage-gated, type III, alpha subunit isoform 3 [Bos taurus]" 82.17 1951 97.17 99.06 1.70e-63 TPG DAA32711 "TPA: sodium channel, voltage-gated, type III, alpha subunit isoform 4 [Bos taurus]" 82.17 1951 97.17 99.06 1.60e-63 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 $entity Humans 9606 Eukaryota Metazoa Homo sapiens SCN2A 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 $entity 'recombinant technology' . Escherichia coli BL21 pET28 'Construct retains 6x His tag (MGSSHHHHHHSSGLVPRGSHMAS).' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_13C-15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-99% 13C; U-99% 15N]' glycine 100 mM [D5-98%] TRIS 20 mM '[D11-98 %]' EDTA 0.1 mM [D16-98%] D2O 10 % '[U-99% 2H]' DTT 1 mM [D10-98%] NaN3 0.02 % 'natural abundance' stop_ save_ save_10%13-C _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-10% 13C; U-99% 15N]' glycine 100 mM [D5-98%] TRIS 20 mM '[D11-98 %]' EDTA 0.1 mM [D16-98%] D2O 10 % '[U-99% 2H]' DTT 1 mM [D10-98%] NaN3 0.02 % 'natural abundance' stop_ save_ save_phage _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-99% 13C; U-99% 15N]' glycine 100 mM [D5-98%] TRIS 20 mM '[D11-98 %]' EDTA 0.1 mM [D16-98%] D2O 10 % '[U-99% 2H]' DTT 1 mM [D10-98%] NaN3 0.02 % 'natural abundance' 'pF1 phage' 15 mg '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' 'peak picking' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 2.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'initial structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'initial structure solution' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.18 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_4 _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 $13C-15N save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $13C-15N save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $13C-15N save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $13C-15N save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $13C-15N save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $13C-15N save_ save_3D_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $13C-15N save_ save_3D_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $13C-15N save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $13C-15N save_ save_3D_1H-13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $13C-15N save_ save_2D_1H-13C_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $10%13-C save_ save_3D_HCACO_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $phage save_ save_2D_IPAP_HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D IPAP HSQC' _Sample_label $phage save_ save_3D_quant_HNCO_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D quant HNCO' _Sample_label $phage save_ save_3D_CCa_HNCO_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCa HNCO' _Sample_label $phage save_ ####################### # Sample conditions # ####################### save_sample_conditions _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 1.0 . atm temperature 290.5 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 $SPARKY stop_ loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '3D HNCACB' '3D CBCA(CO)NH' '3D HCCH-TOCSY' '3D HBHA(CO)NH' '3D HCACO' stop_ loop_ _Sample_label $13C-15N $phage stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'NaV1.2 C-terminal EF-hand domain' _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 1777 24 GLU H H 8.456 0.003 1 2 1777 24 GLU HA H 4.222 0.001 1 3 1777 24 GLU HB2 H 1.967 0.010 2 4 1777 24 GLU HB3 H 1.885 0.010 2 5 1777 24 GLU HG2 H 2.181 0.013 2 6 1777 24 GLU HG3 H 2.181 0.013 2 7 1777 24 GLU N N 121.899 0.008 1 8 1778 25 ASN H H 8.291 0.008 1 9 1778 25 ASN HA H 4.639 0.004 1 10 1778 25 ASN HB2 H 2.740 0.003 2 11 1778 25 ASN HB3 H 2.634 0.002 2 12 1778 25 ASN HD21 H 7.567 0.010 2 13 1778 25 ASN HD22 H 6.931 0.001 2 14 1778 25 ASN CA C 52.921 0.018 1 15 1778 25 ASN CB C 38.645 0.014 1 16 1778 25 ASN N N 118.251 0.048 1 17 1779 26 PHE H H 8.132 0.004 1 18 1779 26 PHE HA H 4.608 0.001 1 19 1779 26 PHE HB2 H 3.140 0.003 2 20 1779 26 PHE HB3 H 3.011 0.002 2 21 1779 26 PHE HD1 H 7.204 0.008 3 22 1779 26 PHE HD2 H 7.204 0.008 3 23 1779 26 PHE CA C 57.605 0.001 1 24 1779 26 PHE CB C 39.179 0.025 1 25 1779 26 PHE CD1 C 131.676 0.027 3 26 1779 26 PHE N N 120.325 0.005 1 27 1780 27 SER H H 8.202 0.003 1 28 1780 27 SER HA H 4.446 0.002 1 29 1780 27 SER HB2 H 3.804 0.005 2 30 1780 27 SER HB3 H 3.804 0.005 2 31 1780 27 SER CA C 57.861 0.001 1 32 1780 27 SER CB C 63.673 0.002 1 33 1780 27 SER N N 117.257 0.015 1 34 1781 28 VAL H H 8.123 0.005 1 35 1781 28 VAL HA H 4.136 0.002 1 36 1781 28 VAL HB H 2.086 0.002 1 37 1781 28 VAL HG1 H 0.935 0.003 1 38 1781 28 VAL HG2 H 0.925 0.001 1 39 1781 28 VAL CA C 61.715 0.016 1 40 1781 28 VAL CB C 32.574 0.100 1 41 1781 28 VAL CG1 C 20.924 0.007 1 42 1781 28 VAL CG2 C 20.107 0.022 1 43 1781 28 VAL N N 121.163 0.009 1 44 1782 29 ALA H H 8.420 0.005 1 45 1782 29 ALA HA H 4.387 0.001 1 46 1782 29 ALA HB H 1.391 0.001 1 47 1782 29 ALA CA C 52.233 0.028 1 48 1782 29 ALA N N 127.400 0.003 1 49 1783 30 THR H H 8.166 0.003 1 50 1783 30 THR HA H 4.329 0.001 1 51 1783 30 THR HB H 4.254 0.010 1 52 1783 30 THR HG2 H 1.194 0.003 1 53 1783 30 THR CA C 61.511 0.005 1 54 1783 30 THR CB C 69.631 0.100 1 55 1783 30 THR CG2 C 21.398 0.005 1 56 1783 30 THR N N 113.231 0.014 1 57 1784 31 GLU H H 8.475 0.003 1 58 1784 31 GLU HB2 H 2.072 0.010 2 59 1784 31 GLU HB3 H 1.944 0.010 2 60 1784 31 GLU HG2 H 2.266 0.004 2 61 1784 31 GLU HG3 H 2.266 0.004 2 62 1784 31 GLU CG C 36.007 0.100 1 63 1784 31 GLU N N 122.410 0.006 1 64 1785 32 GLU H H 8.476 0.002 1 65 1785 32 GLU HB2 H 2.070 0.003 2 66 1785 32 GLU HB3 H 1.937 0.003 2 67 1785 32 GLU HG2 H 2.263 0.001 2 68 1785 32 GLU HG3 H 2.263 0.001 2 69 1785 32 GLU CB C 30.011 0.002 1 70 1785 32 GLU N N 121.416 0.001 1 71 1786 33 SER H H 8.334 0.001 1 72 1786 33 SER HA H 4.433 0.002 1 73 1786 33 SER HB2 H 3.854 0.010 2 74 1786 33 SER HB3 H 3.854 0.010 2 75 1786 33 SER CA C 57.921 0.100 1 76 1786 33 SER N N 116.650 0.008 1 77 1787 34 ALA H H 8.392 0.002 1 78 1787 34 ALA HA H 4.379 0.002 1 79 1787 34 ALA HB H 1.371 0.001 1 80 1787 34 ALA CA C 51.911 0.100 1 81 1787 34 ALA N N 126.129 0.001 1 82 1788 35 GLU H H 8.402 0.002 1 83 1788 35 GLU HA H 4.589 0.001 1 84 1788 35 GLU HB2 H 2.105 0.003 2 85 1788 35 GLU HB3 H 1.894 0.002 2 86 1788 35 GLU HG2 H 2.369 0.002 2 87 1788 35 GLU HG3 H 2.308 0.003 2 88 1788 35 GLU CA C 53.900 0.058 1 89 1788 35 GLU CB C 29.698 0.023 1 90 1788 35 GLU CG C 35.726 0.012 1 91 1788 35 GLU N N 121.313 0.002 1 92 1789 36 PRO HA H 4.382 0.001 1 93 1789 36 PRO HB2 H 2.250 0.001 2 94 1789 36 PRO HB3 H 1.819 0.005 2 95 1789 36 PRO HD2 H 3.785 0.009 2 96 1789 36 PRO HD3 H 3.760 0.006 2 97 1789 36 PRO HG2 H 2.001 0.002 2 98 1789 36 PRO HG3 H 1.932 0.010 2 99 1789 36 PRO CA C 63.310 0.054 1 100 1789 36 PRO CB C 32.038 0.020 1 101 1789 36 PRO CD C 50.220 0.024 1 102 1789 36 PRO CG C 27.085 0.016 1 103 1790 37 LEU H H 7.674 0.003 1 104 1790 37 LEU HA H 4.613 0.002 1 105 1790 37 LEU HB2 H 1.547 0.007 2 106 1790 37 LEU HB3 H 1.244 0.004 2 107 1790 37 LEU HD1 H 0.749 0.005 1 108 1790 37 LEU HD2 H 0.717 0.004 1 109 1790 37 LEU CA C 53.507 0.027 1 110 1790 37 LEU CB C 44.046 0.044 1 111 1790 37 LEU CD1 C 26.023 0.022 1 112 1790 37 LEU CD2 C 23.956 0.015 1 113 1790 37 LEU N N 117.807 0.018 1 114 1791 38 SER H H 9.544 0.004 1 115 1791 38 SER HA H 4.740 0.007 1 116 1791 38 SER HB2 H 4.255 0.004 2 117 1791 38 SER HB3 H 3.919 0.004 2 118 1791 38 SER CA C 56.408 0.002 1 119 1791 38 SER CB C 66.372 0.025 1 120 1791 38 SER N N 119.366 0.009 1 121 1792 39 GLU H H 9.119 0.005 1 122 1792 39 GLU HA H 4.279 0.005 1 123 1792 39 GLU HB2 H 2.134 0.004 2 124 1792 39 GLU HB3 H 2.134 0.004 2 125 1792 39 GLU HG2 H 2.449 0.006 2 126 1792 39 GLU HG3 H 2.449 0.006 2 127 1792 39 GLU CA C 59.644 0.060 1 128 1792 39 GLU CB C 29.107 0.025 1 129 1792 39 GLU CG C 36.109 0.014 1 130 1792 39 GLU N N 120.930 0.100 1 131 1793 40 ASP H H 8.270 0.003 1 132 1793 40 ASP HA H 4.456 0.001 1 133 1793 40 ASP HB2 H 2.696 0.004 2 134 1793 40 ASP HB3 H 2.537 0.002 2 135 1793 40 ASP CB C 40.181 0.021 1 136 1793 40 ASP N N 117.772 0.007 1 137 1794 41 ASP H H 7.816 0.002 1 138 1794 41 ASP HA H 4.449 0.002 1 139 1794 41 ASP HB2 H 2.718 0.003 2 140 1794 41 ASP HB3 H 2.255 0.007 2 141 1794 41 ASP CA C 57.442 0.050 1 142 1794 41 ASP CB C 40.787 0.038 1 143 1794 41 ASP N N 120.773 0.015 1 144 1795 42 PHE H H 7.555 0.004 1 145 1795 42 PHE HA H 4.198 0.006 1 146 1795 42 PHE HB2 H 3.147 0.010 2 147 1795 42 PHE HB3 H 3.147 0.010 2 148 1795 42 PHE HD1 H 7.112 0.006 3 149 1795 42 PHE HD2 H 7.112 0.006 3 150 1795 42 PHE HE1 H 7.139 0.003 3 151 1795 42 PHE HE2 H 7.139 0.003 3 152 1795 42 PHE HZ H 7.138 0.002 1 153 1795 42 PHE CA C 61.178 0.036 1 154 1795 42 PHE CB C 38.295 0.066 1 155 1795 42 PHE CD1 C 131.096 0.021 3 156 1795 42 PHE CE1 C 131.148 0.030 3 157 1795 42 PHE CZ C 129.724 0.022 1 158 1795 42 PHE N N 118.046 0.011 1 159 1796 43 GLU H H 8.333 0.002 1 160 1796 43 GLU HA H 4.297 0.002 1 161 1796 43 GLU HB2 H 2.243 0.002 2 162 1796 43 GLU HB3 H 2.243 0.002 2 163 1796 43 GLU HG2 H 2.583 0.003 2 164 1796 43 GLU HG3 H 2.471 0.010 2 165 1796 43 GLU CA C 59.599 0.009 1 166 1796 43 GLU CB C 29.021 0.013 1 167 1796 43 GLU CG C 36.009 0.012 1 168 1796 43 GLU N N 118.541 0.015 1 169 1797 44 MET H H 8.025 0.005 1 170 1797 44 MET HA H 4.287 0.001 1 171 1797 44 MET HB2 H 2.469 0.002 2 172 1797 44 MET HB3 H 2.267 0.010 2 173 1797 44 MET HE H 2.293 0.001 1 174 1797 44 MET HG2 H 2.988 0.004 2 175 1797 44 MET HG3 H 2.653 0.113 2 176 1797 44 MET CA C 58.345 0.009 1 177 1797 44 MET CB C 28.730 0.020 1 178 1797 44 MET CE C 16.421 0.009 1 179 1797 44 MET CG C 30.615 0.030 1 180 1797 44 MET N N 120.154 0.021 1 181 1798 45 PHE H H 8.117 0.004 1 182 1798 45 PHE HA H 3.888 0.004 1 183 1798 45 PHE HB2 H 3.397 0.004 2 184 1798 45 PHE HB3 H 2.814 0.002 2 185 1798 45 PHE HD1 H 6.475 0.005 3 186 1798 45 PHE HD2 H 6.475 0.005 3 187 1798 45 PHE HE1 H 6.681 0.004 3 188 1798 45 PHE HE2 H 6.681 0.004 3 189 1798 45 PHE HZ H 6.780 0.003 1 190 1798 45 PHE CA C 61.579 0.026 1 191 1798 45 PHE CB C 38.234 0.035 1 192 1798 45 PHE CD1 C 132.182 0.018 3 193 1798 45 PHE CE1 C 130.380 0.033 3 194 1798 45 PHE CZ C 129.148 0.037 1 195 1798 45 PHE N N 120.474 0.017 1 196 1799 46 TYR H H 8.299 0.007 1 197 1799 46 TYR HA H 4.377 0.005 1 198 1799 46 TYR HB2 H 3.092 0.017 2 199 1799 46 TYR HB3 H 2.868 0.002 2 200 1799 46 TYR HD1 H 7.186 0.006 3 201 1799 46 TYR HD2 H 7.186 0.006 3 202 1799 46 TYR HE1 H 6.583 0.003 3 203 1799 46 TYR HE2 H 6.583 0.003 3 204 1799 46 TYR CA C 62.631 0.037 1 205 1799 46 TYR CB C 37.639 0.034 1 206 1799 46 TYR CD1 C 132.913 0.032 3 207 1799 46 TYR CE1 C 117.622 0.025 3 208 1799 46 TYR N N 116.311 0.015 1 209 1800 47 GLU H H 8.464 0.004 1 210 1800 47 GLU HA H 4.218 0.003 1 211 1800 47 GLU HB2 H 2.337 0.006 2 212 1800 47 GLU HB3 H 2.337 0.006 2 213 1800 47 GLU HG2 H 2.528 0.006 2 214 1800 47 GLU HG3 H 2.528 0.006 2 215 1800 47 GLU CA C 59.585 0.017 1 216 1800 47 GLU CB C 29.265 0.019 1 217 1800 47 GLU CG C 36.263 0.001 1 218 1800 47 GLU N N 123.373 0.008 1 219 1801 48 VAL H H 8.317 0.004 1 220 1801 48 VAL HA H 3.715 0.003 1 221 1801 48 VAL HB H 1.982 0.006 1 222 1801 48 VAL HG1 H 0.879 0.010 1 223 1801 48 VAL HG2 H 1.065 0.003 1 224 1801 48 VAL CA C 66.567 0.014 1 225 1801 48 VAL CB C 30.961 0.142 1 226 1801 48 VAL CG1 C 22.671 0.012 1 227 1801 48 VAL CG2 C 23.215 0.019 1 228 1801 48 VAL N N 120.814 0.025 1 229 1802 49 TRP H H 9.190 0.003 1 230 1802 49 TRP HA H 3.704 0.003 1 231 1802 49 TRP HB2 H 3.415 0.006 2 232 1802 49 TRP HB3 H 2.914 0.003 2 233 1802 49 TRP HD1 H 7.277 0.002 1 234 1802 49 TRP HE1 H 11.281 0.003 1 235 1802 49 TRP HE3 H 6.413 0.003 1 236 1802 49 TRP HH2 H 6.601 0.003 1 237 1802 49 TRP HZ2 H 6.525 0.004 1 238 1802 49 TRP HZ3 H 6.006 0.003 1 239 1802 49 TRP CA C 61.622 0.047 1 240 1802 49 TRP CB C 28.527 0.036 1 241 1802 49 TRP CD1 C 127.475 0.026 1 242 1802 49 TRP CE3 C 120.631 0.073 1 243 1802 49 TRP CH2 C 123.361 0.046 1 244 1802 49 TRP CZ2 C 112.899 0.019 1 245 1802 49 TRP CZ3 C 119.596 0.030 1 246 1802 49 TRP N N 121.634 0.018 1 247 1802 49 TRP NE1 N 131.471 0.007 1 248 1803 50 GLU H H 7.968 0.003 1 249 1803 50 GLU HA H 3.957 0.003 1 250 1803 50 GLU HB2 H 2.300 0.002 2 251 1803 50 GLU HB3 H 2.200 0.002 2 252 1803 50 GLU HG2 H 2.703 0.005 2 253 1803 50 GLU HG3 H 2.508 0.004 2 254 1803 50 GLU CA C 59.059 0.054 1 255 1803 50 GLU CB C 29.440 0.017 1 256 1803 50 GLU CG C 36.157 0.014 1 257 1803 50 GLU N N 115.667 0.016 1 258 1804 51 LYS H H 7.480 0.004 1 259 1804 51 LYS HA H 3.955 0.001 1 260 1804 51 LYS HB2 H 2.103 0.002 2 261 1804 51 LYS HB3 H 1.736 0.003 2 262 1804 51 LYS HD2 H 1.654 0.001 2 263 1804 51 LYS HD3 H 1.654 0.001 2 264 1804 51 LYS HE2 H 2.951 0.004 2 265 1804 51 LYS HE3 H 2.951 0.004 2 266 1804 51 LYS HG2 H 1.653 0.001 2 267 1804 51 LYS HG3 H 1.387 0.003 2 268 1804 51 LYS CA C 58.121 0.045 1 269 1804 51 LYS CB C 31.582 0.028 1 270 1804 51 LYS CD C 28.905 0.012 1 271 1804 51 LYS CE C 41.922 0.018 1 272 1804 51 LYS CG C 24.853 0.041 1 273 1804 51 LYS N N 115.567 0.013 1 274 1805 52 PHE H H 7.513 0.002 1 275 1805 52 PHE HA H 4.079 0.002 1 276 1805 52 PHE HB2 H 2.694 0.003 2 277 1805 52 PHE HB3 H 2.270 0.005 2 278 1805 52 PHE HD1 H 7.492 0.003 3 279 1805 52 PHE HD2 H 7.492 0.003 3 280 1805 52 PHE HE1 H 7.287 0.004 3 281 1805 52 PHE HE2 H 7.287 0.004 3 282 1805 52 PHE HZ H 7.033 0.005 1 283 1805 52 PHE CA C 58.710 0.019 1 284 1805 52 PHE CB C 39.886 0.030 1 285 1805 52 PHE CD1 C 132.013 0.034 3 286 1805 52 PHE CE1 C 131.187 0.058 3 287 1805 52 PHE CZ C 129.413 0.019 1 288 1805 52 PHE N N 116.335 0.007 1 289 1806 53 ASP H H 7.758 0.003 1 290 1806 53 ASP HA H 5.095 0.002 1 291 1806 53 ASP HB2 H 2.125 0.004 2 292 1806 53 ASP HB3 H 1.575 0.005 2 293 1806 53 ASP CA C 51.414 0.100 1 294 1806 53 ASP CB C 38.985 0.051 1 295 1806 53 ASP N N 120.001 0.007 1 296 1807 54 PRO HA H 4.550 0.003 1 297 1807 54 PRO HB2 H 2.317 0.003 2 298 1807 54 PRO HB3 H 1.992 0.003 2 299 1807 54 PRO HD2 H 3.701 0.003 2 300 1807 54 PRO HD3 H 3.101 0.007 2 301 1807 54 PRO HG2 H 1.956 0.002 2 302 1807 54 PRO HG3 H 1.873 0.004 2 303 1807 54 PRO CA C 64.842 0.035 1 304 1807 54 PRO CB C 31.452 0.042 1 305 1807 54 PRO CD C 50.387 0.012 1 306 1807 54 PRO CG C 26.983 0.009 1 307 1808 55 ASP H H 9.054 0.003 1 308 1808 55 ASP HA H 4.813 0.001 1 309 1808 55 ASP HB2 H 2.875 0.002 2 310 1808 55 ASP HB3 H 2.712 0.003 2 311 1808 55 ASP CB C 39.852 0.011 1 312 1808 55 ASP N N 117.653 0.019 1 313 1809 56 ALA H H 8.351 0.003 1 314 1809 56 ALA HA H 4.294 0.002 1 315 1809 56 ALA HB H 1.429 0.002 1 316 1809 56 ALA CA C 53.237 0.046 1 317 1809 56 ALA CB C 15.737 0.026 1 318 1809 56 ALA N N 122.448 0.025 1 319 1810 57 THR H H 9.798 0.004 1 320 1810 57 THR HA H 4.276 0.003 1 321 1810 57 THR HB H 4.492 0.003 1 322 1810 57 THR HG2 H 1.398 0.002 1 323 1810 57 THR CA C 64.182 0.019 1 324 1810 57 THR CB C 70.944 0.030 1 325 1810 57 THR CG2 C 21.924 0.023 1 326 1810 57 THR N N 113.932 0.018 1 327 1811 58 GLN H H 10.576 0.006 1 328 1811 58 GLN HA H 3.607 0.006 1 329 1811 58 GLN HB2 H 2.327 0.004 2 330 1811 58 GLN HB3 H 1.775 0.012 2 331 1811 58 GLN HE21 H 7.389 0.001 2 332 1811 58 GLN HE22 H 6.885 0.004 2 333 1811 58 GLN HG2 H 2.289 0.003 2 334 1811 58 GLN HG3 H 2.113 0.002 2 335 1811 58 GLN CA C 58.121 0.100 1 336 1811 58 GLN CB C 26.377 0.027 1 337 1811 58 GLN CG C 33.891 0.024 1 338 1811 58 GLN N N 113.856 0.016 1 339 1812 59 PHE H H 8.481 0.006 1 340 1812 59 PHE HA H 5.589 0.003 1 341 1812 59 PHE HB2 H 2.817 0.003 2 342 1812 59 PHE HB3 H 2.753 0.004 2 343 1812 59 PHE HD1 H 7.064 0.004 3 344 1812 59 PHE HD2 H 7.064 0.004 3 345 1812 59 PHE HE1 H 7.454 0.004 3 346 1812 59 PHE HE2 H 7.454 0.004 3 347 1812 59 PHE HZ H 7.473 0.001 1 348 1812 59 PHE CA C 56.564 0.027 1 349 1812 59 PHE CB C 44.293 0.021 1 350 1812 59 PHE CD1 C 132.458 0.033 3 351 1812 59 PHE CE1 C 131.222 0.049 3 352 1812 59 PHE CZ C 129.623 0.004 1 353 1812 59 PHE N N 116.866 0.022 1 354 1813 60 ILE H H 8.765 0.005 1 355 1813 60 ILE HA H 4.514 0.003 1 356 1813 60 ILE HB H 1.272 0.001 1 357 1813 60 ILE HD1 H 0.026 0.002 1 358 1813 60 ILE HG12 H 1.262 0.001 2 359 1813 60 ILE HG13 H 1.199 0.003 2 360 1813 60 ILE HG2 H 0.500 0.001 1 361 1813 60 ILE CA C 58.819 0.039 1 362 1813 60 ILE CB C 41.702 0.047 1 363 1813 60 ILE CD1 C 13.486 0.021 1 364 1813 60 ILE CG1 C 26.970 0.012 1 365 1813 60 ILE CG2 C 16.271 0.024 1 366 1813 60 ILE N N 114.917 0.021 1 367 1814 61 GLU H H 8.581 0.003 1 368 1814 61 GLU HA H 4.596 0.003 1 369 1814 61 GLU HB2 H 2.315 0.002 2 370 1814 61 GLU HB3 H 1.979 0.009 2 371 1814 61 GLU HG2 H 2.399 0.005 2 372 1814 61 GLU HG3 H 2.399 0.005 2 373 1814 61 GLU CA C 56.264 0.008 1 374 1814 61 GLU CB C 30.324 0.020 1 375 1814 61 GLU CG C 36.976 0.014 1 376 1814 61 GLU N N 124.143 0.015 1 377 1815 62 PHE H H 9.383 0.005 1 378 1815 62 PHE HA H 4.082 0.002 1 379 1815 62 PHE HB2 H 3.394 0.002 2 380 1815 62 PHE HB3 H 3.201 0.003 2 381 1815 62 PHE HD1 H 7.259 0.003 3 382 1815 62 PHE HD2 H 7.259 0.003 3 383 1815 62 PHE HE1 H 7.266 0.003 3 384 1815 62 PHE HE2 H 7.266 0.003 3 385 1815 62 PHE HZ H 7.144 0.004 1 386 1815 62 PHE CA C 61.570 0.017 1 387 1815 62 PHE CB C 38.714 0.027 1 388 1815 62 PHE CD1 C 131.888 0.052 3 389 1815 62 PHE CE1 C 130.802 0.047 3 390 1815 62 PHE CZ C 129.293 0.062 1 391 1815 62 PHE N N 125.029 0.026 1 392 1816 63 ALA H H 9.079 0.002 1 393 1816 63 ALA HA H 4.083 0.001 1 394 1816 63 ALA HB H 1.534 0.002 1 395 1816 63 ALA CA C 54.472 0.048 1 396 1816 63 ALA CB C 18.608 0.011 1 397 1816 63 ALA N N 118.190 0.005 1 398 1817 64 LYS H H 7.678 0.003 1 399 1817 64 LYS HA H 4.581 0.003 1 400 1817 64 LYS HB2 H 2.228 0.005 2 401 1817 64 LYS HB3 H 1.954 0.005 2 402 1817 64 LYS HD2 H 1.907 0.002 2 403 1817 64 LYS HD3 H 1.859 0.003 2 404 1817 64 LYS HE2 H 3.086 0.002 2 405 1817 64 LYS HE3 H 3.086 0.002 2 406 1817 64 LYS HG2 H 1.673 0.002 2 407 1817 64 LYS HG3 H 1.567 0.005 2 408 1817 64 LYS CA C 55.681 0.026 1 409 1817 64 LYS CB C 33.112 0.038 1 410 1817 64 LYS CD C 28.811 0.028 1 411 1817 64 LYS CE C 42.028 0.034 1 412 1817 64 LYS CG C 25.251 0.062 1 413 1817 64 LYS N N 115.651 0.009 1 414 1818 65 LEU H H 7.859 0.003 1 415 1818 65 LEU HA H 3.942 0.003 1 416 1818 65 LEU HB2 H 1.814 0.003 2 417 1818 65 LEU HB3 H 1.325 0.004 2 418 1818 65 LEU HD1 H 1.084 0.002 1 419 1818 65 LEU HD2 H 0.993 0.003 1 420 1818 65 LEU HG H 1.865 0.002 1 421 1818 65 LEU CA C 57.385 0.037 1 422 1818 65 LEU CB C 42.024 0.041 1 423 1818 65 LEU CD1 C 24.130 0.008 1 424 1818 65 LEU CD2 C 27.069 0.019 1 425 1818 65 LEU CG C 26.324 0.037 1 426 1818 65 LEU N N 121.984 0.024 1 427 1819 66 SER H H 8.072 0.004 1 428 1819 66 SER HA H 3.984 0.005 1 429 1819 66 SER HB2 H 3.883 0.003 2 430 1819 66 SER HB3 H 3.802 0.002 2 431 1819 66 SER CA C 60.866 0.033 1 432 1819 66 SER CB C 62.442 0.018 1 433 1819 66 SER N N 111.968 0.100 1 434 1820 67 ASP H H 7.792 0.001 1 435 1820 67 ASP HA H 4.251 0.003 1 436 1820 67 ASP HB2 H 2.954 0.005 2 437 1820 67 ASP HB3 H 2.866 0.004 2 438 1820 67 ASP CA C 56.992 0.024 1 439 1820 67 ASP CB C 40.028 0.025 1 440 1820 67 ASP N N 119.523 0.022 1 441 1821 68 PHE H H 7.867 0.002 1 442 1821 68 PHE HA H 3.033 0.004 1 443 1821 68 PHE HB2 H 2.581 0.004 2 444 1821 68 PHE HB3 H 1.787 0.002 2 445 1821 68 PHE HD1 H 6.531 0.003 3 446 1821 68 PHE HD2 H 6.531 0.003 3 447 1821 68 PHE HE1 H 6.737 0.004 3 448 1821 68 PHE HE2 H 6.737 0.004 3 449 1821 68 PHE HZ H 6.182 0.003 1 450 1821 68 PHE CA C 60.696 0.019 1 451 1821 68 PHE CB C 38.536 0.019 1 452 1821 68 PHE CD1 C 130.839 0.070 3 453 1821 68 PHE CE1 C 130.251 0.087 3 454 1821 68 PHE CZ C 130.110 0.001 1 455 1821 68 PHE N N 122.108 0.009 1 456 1822 69 ALA H H 8.648 0.003 1 457 1822 69 ALA HA H 3.695 0.005 1 458 1822 69 ALA HB H 1.521 0.002 1 459 1822 69 ALA CA C 54.411 0.034 1 460 1822 69 ALA CB C 18.664 0.025 1 461 1822 69 ALA N N 118.445 0.022 1 462 1823 70 ASP H H 6.838 0.003 1 463 1823 70 ASP HA H 4.457 0.002 1 464 1823 70 ASP HB2 H 2.563 0.004 2 465 1823 70 ASP HB3 H 2.508 0.007 2 466 1823 70 ASP CA C 54.692 0.033 1 467 1823 70 ASP CB C 44.941 0.027 1 468 1823 70 ASP N N 112.750 0.009 1 469 1824 71 ALA H H 7.303 0.005 1 470 1824 71 ALA HA H 4.356 0.005 1 471 1824 71 ALA HB H 1.503 0.002 1 472 1824 71 ALA CA C 51.321 0.039 1 473 1824 71 ALA CB C 19.495 0.009 1 474 1824 71 ALA N N 118.945 0.027 1 475 1825 72 LEU H H 6.314 0.004 1 476 1825 72 LEU HA H 4.114 0.004 1 477 1825 72 LEU HB2 H 1.338 0.006 2 478 1825 72 LEU HB3 H 1.338 0.006 2 479 1825 72 LEU HD1 H 0.758 0.002 1 480 1825 72 LEU HD2 H 0.538 0.002 1 481 1825 72 LEU HG H 1.365 0.008 1 482 1825 72 LEU CA C 53.855 0.024 1 483 1825 72 LEU CB C 43.576 0.037 1 484 1825 72 LEU CD1 C 26.930 0.023 1 485 1825 72 LEU CD2 C 23.732 0.015 1 486 1825 72 LEU CG C 25.414 0.028 1 487 1825 72 LEU N N 117.783 0.011 1 488 1826 73 ASP H H 8.000 0.004 1 489 1826 73 ASP HA H 5.061 0.004 1 490 1826 73 ASP HB2 H 2.833 0.005 2 491 1826 73 ASP HB3 H 2.367 0.002 2 492 1826 73 ASP CA C 52.241 0.021 1 493 1826 73 ASP CB C 39.694 0.009 1 494 1826 73 ASP N N 119.065 0.004 1 495 1827 74 PRO HA H 4.354 0.002 1 496 1827 74 PRO HB2 H 2.372 0.003 2 497 1827 74 PRO HB3 H 1.839 0.004 2 498 1827 74 PRO HD2 H 3.828 0.002 2 499 1827 74 PRO HD3 H 3.651 0.003 2 500 1827 74 PRO HG2 H 2.142 0.001 2 501 1827 74 PRO HG3 H 2.004 0.010 2 502 1827 74 PRO CA C 62.700 0.019 1 503 1827 74 PRO CB C 30.086 0.024 1 504 1827 74 PRO CD C 50.153 0.015 1 505 1827 74 PRO CG C 27.706 0.016 1 506 1828 75 PRO HA H 4.606 0.003 1 507 1828 75 PRO HB2 H 2.299 0.004 2 508 1828 75 PRO HB3 H 2.209 0.003 2 509 1828 75 PRO HD2 H 3.531 0.003 2 510 1828 75 PRO HD3 H 3.441 0.006 2 511 1828 75 PRO HG2 H 2.097 0.005 2 512 1828 75 PRO HG3 H 1.428 0.003 2 513 1828 75 PRO CA C 63.345 0.014 1 514 1828 75 PRO CB C 33.970 0.034 1 515 1828 75 PRO CD C 49.931 0.029 1 516 1828 75 PRO CG C 24.578 0.021 1 517 1829 76 LEU H H 7.720 0.004 1 518 1829 76 LEU HA H 4.073 0.001 1 519 1829 76 LEU HB2 H 1.838 0.004 2 520 1829 76 LEU HB3 H 1.557 0.004 2 521 1829 76 LEU HD1 H 0.871 0.002 1 522 1829 76 LEU HD2 H 0.783 0.004 1 523 1829 76 LEU HG H 1.485 0.003 1 524 1829 76 LEU CA C 56.536 0.024 1 525 1829 76 LEU CB C 43.598 0.054 1 526 1829 76 LEU CD1 C 25.802 0.024 1 527 1829 76 LEU CD2 C 23.427 0.042 1 528 1829 76 LEU CG C 27.577 0.100 1 529 1829 76 LEU N N 122.500 0.100 1 530 1830 77 LEU H H 6.341 0.003 1 531 1830 77 LEU HA H 3.761 0.004 1 532 1830 77 LEU HB2 H 1.287 0.003 2 533 1830 77 LEU HB3 H 1.152 0.003 2 534 1830 77 LEU HD1 H 0.982 0.002 1 535 1830 77 LEU HD2 H 0.856 0.002 1 536 1830 77 LEU HG H 1.281 0.003 1 537 1830 77 LEU CA C 55.851 0.012 1 538 1830 77 LEU CB C 42.753 0.055 1 539 1830 77 LEU CD1 C 22.232 0.013 1 540 1830 77 LEU CD2 C 26.225 0.034 1 541 1830 77 LEU CG C 26.855 0.020 1 542 1830 77 LEU N N 116.789 0.024 1 543 1831 78 ILE H H 7.282 0.004 1 544 1831 78 ILE HA H 3.966 0.003 1 545 1831 78 ILE HB H 1.532 0.006 1 546 1831 78 ILE HD1 H 0.005 0.002 1 547 1831 78 ILE HG12 H 1.491 0.004 2 548 1831 78 ILE HG13 H 0.443 0.003 2 549 1831 78 ILE HG2 H 0.611 0.002 1 550 1831 78 ILE CA C 60.881 0.022 1 551 1831 78 ILE CB C 37.521 0.027 1 552 1831 78 ILE CD1 C 13.909 0.032 1 553 1831 78 ILE CG1 C 25.761 0.027 1 554 1831 78 ILE CG2 C 18.351 0.011 1 555 1831 78 ILE N N 127.101 0.002 1 556 1832 79 ALA H H 8.467 0.004 1 557 1832 79 ALA HA H 4.586 0.002 1 558 1832 79 ALA HB H 1.296 0.002 1 559 1832 79 ALA CA C 51.877 0.034 1 560 1832 79 ALA CB C 18.770 0.100 1 561 1832 79 ALA N N 128.751 0.004 1 562 1833 80 LYS H H 8.571 0.004 1 563 1833 80 LYS HA H 3.914 0.004 1 564 1833 80 LYS HB2 H 1.786 0.004 2 565 1833 80 LYS HB3 H 1.507 0.004 2 566 1833 80 LYS HD2 H 1.635 0.005 2 567 1833 80 LYS HD3 H 1.580 0.010 2 568 1833 80 LYS HE2 H 2.944 0.003 2 569 1833 80 LYS HE3 H 2.848 0.001 2 570 1833 80 LYS HG2 H 1.327 0.004 2 571 1833 80 LYS HG3 H 1.327 0.004 2 572 1833 80 LYS CA C 55.907 0.036 1 573 1833 80 LYS CB C 31.938 0.017 1 574 1833 80 LYS CD C 29.868 0.040 1 575 1833 80 LYS CE C 42.056 0.033 1 576 1833 80 LYS CG C 26.844 0.037 1 577 1833 80 LYS N N 119.412 0.016 1 578 1834 81 PRO HA H 4.467 0.004 1 579 1834 81 PRO HB2 H 2.388 0.002 2 580 1834 81 PRO HB3 H 2.248 0.004 2 581 1834 81 PRO HD2 H 3.570 0.002 2 582 1834 81 PRO HD3 H 3.570 0.002 2 583 1834 81 PRO HG2 H 2.158 0.002 2 584 1834 81 PRO HG3 H 1.935 0.001 2 585 1834 81 PRO CA C 62.394 0.026 1 586 1834 81 PRO CB C 33.376 0.011 1 587 1834 81 PRO CD C 50.246 0.018 1 588 1834 81 PRO CG C 24.861 0.011 1 589 1835 82 ASN HA H 5.110 0.006 1 590 1835 82 ASN HB2 H 2.761 0.004 2 591 1835 82 ASN HB3 H 2.626 0.007 2 592 1835 82 ASN HD21 H 8.089 0.003 2 593 1835 82 ASN HD22 H 7.603 0.004 2 594 1835 82 ASN CA C 51.127 0.034 1 595 1835 82 ASN CB C 39.245 0.024 1 596 1836 83 LYS H H 7.864 0.005 1 597 1836 83 LYS HA H 3.861 0.002 1 598 1836 83 LYS HB2 H 2.007 0.003 2 599 1836 83 LYS HB3 H 1.918 0.003 2 600 1836 83 LYS HD2 H 1.769 0.004 2 601 1836 83 LYS HD3 H 1.769 0.004 2 602 1836 83 LYS HE2 H 3.017 0.002 2 603 1836 83 LYS HE3 H 3.017 0.002 2 604 1836 83 LYS HG2 H 1.673 0.001 2 605 1836 83 LYS HG3 H 1.494 0.002 2 606 1836 83 LYS CA C 60.887 0.039 1 607 1836 83 LYS CB C 32.290 0.022 1 608 1836 83 LYS CD C 29.089 0.047 1 609 1836 83 LYS CE C 41.715 0.026 1 610 1836 83 LYS CG C 25.207 0.025 1 611 1836 83 LYS N N 120.773 0.013 1 612 1837 84 VAL H H 8.349 0.004 1 613 1837 84 VAL HA H 3.585 0.002 1 614 1837 84 VAL HB H 1.996 0.002 1 615 1837 84 VAL HG1 H 0.928 0.001 1 616 1837 84 VAL HG2 H 1.050 0.004 1 617 1837 84 VAL CA C 66.547 0.039 1 618 1837 84 VAL CB C 31.184 0.021 1 619 1837 84 VAL CG1 C 20.661 0.012 1 620 1837 84 VAL CG2 C 22.265 0.019 1 621 1837 84 VAL N N 117.444 0.009 1 622 1838 85 GLN H H 8.612 0.006 1 623 1838 85 GLN HA H 3.974 0.004 1 624 1838 85 GLN HB2 H 1.993 0.001 2 625 1838 85 GLN HB3 H 1.822 0.002 2 626 1838 85 GLN HE21 H 7.585 0.001 2 627 1838 85 GLN HE22 H 6.971 0.004 2 628 1838 85 GLN HG2 H 2.424 0.018 2 629 1838 85 GLN HG3 H 2.364 0.002 2 630 1838 85 GLN CA C 59.362 0.018 1 631 1838 85 GLN CB C 28.269 0.014 1 632 1838 85 GLN CG C 34.664 0.021 1 633 1838 85 GLN N N 119.611 0.007 1 634 1839 86 LEU H H 7.917 0.003 1 635 1839 86 LEU HA H 4.417 0.003 1 636 1839 86 LEU HB2 H 2.043 0.002 2 637 1839 86 LEU HB3 H 1.399 0.005 2 638 1839 86 LEU HD1 H 0.610 0.002 1 639 1839 86 LEU HD2 H 0.926 0.001 1 640 1839 86 LEU HG H 1.927 0.002 1 641 1839 86 LEU CA C 57.367 0.073 1 642 1839 86 LEU CB C 41.383 0.022 1 643 1839 86 LEU CD1 C 24.748 0.026 1 644 1839 86 LEU CD2 C 22.837 0.009 1 645 1839 86 LEU CG C 26.607 0.002 1 646 1839 86 LEU N N 118.323 0.012 1 647 1840 87 ILE H H 8.702 0.003 1 648 1840 87 ILE HA H 3.852 0.004 1 649 1840 87 ILE HB H 2.015 0.002 1 650 1840 87 ILE HD1 H 0.930 0.001 1 651 1840 87 ILE HG12 H 1.933 0.002 2 652 1840 87 ILE HG13 H 1.331 0.004 2 653 1840 87 ILE HG2 H 0.976 0.001 1 654 1840 87 ILE CA C 64.799 0.019 1 655 1840 87 ILE CB C 37.738 0.014 1 656 1840 87 ILE CD1 C 13.183 0.006 1 657 1840 87 ILE CG1 C 29.536 0.042 1 658 1840 87 ILE CG2 C 16.858 0.004 1 659 1840 87 ILE N N 121.697 0.007 1 660 1841 88 ALA H H 7.740 0.004 1 661 1841 88 ALA HA H 4.216 0.003 1 662 1841 88 ALA HB H 1.509 0.003 1 663 1841 88 ALA CA C 53.482 0.009 1 664 1841 88 ALA CB C 17.939 0.028 1 665 1841 88 ALA N N 120.787 0.005 1 666 1842 89 MET H H 7.289 0.003 1 667 1842 89 MET HA H 4.091 0.002 1 668 1842 89 MET HB2 H 2.231 0.002 2 669 1842 89 MET HB3 H 2.079 0.004 2 670 1842 89 MET HE H 1.767 0.001 1 671 1842 89 MET HG2 H 3.183 0.005 2 672 1842 89 MET HG3 H 2.603 0.004 2 673 1842 89 MET CA C 57.946 0.029 1 674 1842 89 MET CB C 32.640 0.036 1 675 1842 89 MET CE C 18.128 0.009 1 676 1842 89 MET CG C 33.449 0.035 1 677 1842 89 MET N N 115.679 0.013 1 678 1843 90 ASP H H 7.954 0.004 1 679 1843 90 ASP HA H 4.341 0.001 1 680 1843 90 ASP HB2 H 3.025 0.002 2 681 1843 90 ASP HB3 H 2.332 0.002 2 682 1843 90 ASP CA C 54.069 0.024 1 683 1843 90 ASP CB C 38.901 0.100 1 684 1843 90 ASP N N 118.884 0.019 1 685 1844 91 LEU H H 9.111 0.004 1 686 1844 91 LEU HA H 4.307 0.003 1 687 1844 91 LEU HB2 H 1.804 0.003 2 688 1844 91 LEU HB3 H 1.261 0.003 2 689 1844 91 LEU HD1 H 1.096 0.003 1 690 1844 91 LEU HD2 H 0.939 0.001 1 691 1844 91 LEU HG H 1.694 0.002 1 692 1844 91 LEU CA C 53.248 0.031 1 693 1844 91 LEU CB C 41.047 0.027 1 694 1844 91 LEU CD1 C 26.615 0.038 1 695 1844 91 LEU CD2 C 24.154 0.017 1 696 1844 91 LEU CG C 27.278 0.100 1 697 1844 91 LEU N N 121.190 0.002 1 698 1845 92 PRO HA H 4.490 0.002 1 699 1845 92 PRO HB2 H 2.230 0.001 2 700 1845 92 PRO HB3 H 1.975 0.001 2 701 1845 92 PRO HD2 H 4.028 0.004 2 702 1845 92 PRO HD3 H 3.444 0.003 2 703 1845 92 PRO HG2 H 2.168 0.002 2 704 1845 92 PRO HG3 H 2.059 0.001 2 705 1845 92 PRO CA C 62.334 0.041 1 706 1845 92 PRO CB C 30.901 0.009 1 707 1845 92 PRO CD C 50.390 0.023 1 708 1845 92 PRO CG C 27.513 0.027 1 709 1846 93 MET H H 8.388 0.004 1 710 1846 93 MET HA H 5.248 0.003 1 711 1846 93 MET HB2 H 1.948 0.003 2 712 1846 93 MET HB3 H 1.901 0.002 2 713 1846 93 MET HE H 1.743 0.001 1 714 1846 93 MET HG2 H 2.506 0.002 2 715 1846 93 MET HG3 H 2.296 0.002 2 716 1846 93 MET CA C 54.155 0.029 1 717 1846 93 MET CB C 35.920 0.032 1 718 1846 93 MET CE C 16.856 0.005 1 719 1846 93 MET CG C 31.974 0.024 1 720 1846 93 MET N N 121.676 0.003 1 721 1847 94 VAL H H 9.098 0.004 1 722 1847 94 VAL HA H 4.627 0.004 1 723 1847 94 VAL HB H 2.285 0.002 1 724 1847 94 VAL HG1 H 1.020 0.002 1 725 1847 94 VAL HG2 H 0.783 0.002 1 726 1847 94 VAL CA C 59.669 0.017 1 727 1847 94 VAL CB C 33.495 0.017 1 728 1847 94 VAL CG1 C 21.392 0.014 1 729 1847 94 VAL CG2 C 19.694 0.021 1 730 1847 94 VAL N N 118.281 0.100 1 731 1848 95 SER H H 8.290 0.003 1 732 1848 95 SER HA H 4.144 0.002 1 733 1848 95 SER HB2 H 3.908 0.005 2 734 1848 95 SER HB3 H 3.845 0.004 2 735 1848 95 SER CA C 59.099 0.011 1 736 1848 95 SER CB C 62.695 0.025 1 737 1848 95 SER N N 114.662 0.006 1 738 1849 96 GLY H H 8.814 0.002 1 739 1849 96 GLY HA2 H 4.155 0.001 2 740 1849 96 GLY HA3 H 3.659 0.006 2 741 1849 96 GLY CA C 45.316 0.005 1 742 1849 96 GLY N N 111.469 0.009 1 743 1850 97 ASP H H 8.407 0.002 1 744 1850 97 ASP HA H 4.587 0.004 1 745 1850 97 ASP HB2 H 3.111 0.007 2 746 1850 97 ASP HB3 H 2.948 0.005 2 747 1850 97 ASP CA C 54.665 0.018 1 748 1850 97 ASP CB C 39.092 0.059 1 749 1850 97 ASP N N 118.956 0.005 1 750 1851 98 ARG H H 7.407 0.007 1 751 1851 98 ARG HA H 5.132 0.005 1 752 1851 98 ARG HB2 H 1.534 0.005 2 753 1851 98 ARG HB3 H 1.534 0.005 2 754 1851 98 ARG HD2 H 3.035 0.003 2 755 1851 98 ARG HD3 H 2.839 0.003 2 756 1851 98 ARG HE H 6.857 0.004 1 757 1851 98 ARG HG2 H 1.606 0.006 2 758 1851 98 ARG HG3 H 1.419 0.004 2 759 1851 98 ARG CA C 55.022 0.030 1 760 1851 98 ARG CB C 32.688 0.032 1 761 1851 98 ARG CD C 43.185 0.022 1 762 1851 98 ARG CG C 27.631 0.037 1 763 1851 98 ARG N N 117.108 0.023 1 764 1851 98 ARG NE N 83.882 0.017 1 765 1852 99 ILE H H 9.270 0.005 1 766 1852 99 ILE HA H 4.818 0.002 1 767 1852 99 ILE HB H 1.751 0.006 1 768 1852 99 ILE HD1 H 1.081 0.003 1 769 1852 99 ILE HG12 H 1.701 0.003 2 770 1852 99 ILE HG13 H 1.220 0.003 2 771 1852 99 ILE HG2 H 1.299 0.003 1 772 1852 99 ILE CB C 41.868 0.013 1 773 1852 99 ILE CD1 C 16.344 0.021 1 774 1852 99 ILE CG1 C 28.299 0.019 1 775 1852 99 ILE CG2 C 20.462 0.020 1 776 1852 99 ILE N N 120.060 0.008 1 777 1853 100 HIS H H 9.859 0.003 1 778 1853 100 HIS HA H 4.188 0.003 1 779 1853 100 HIS HB2 H 2.929 0.007 2 780 1853 100 HIS HB3 H 2.896 0.006 2 781 1853 100 HIS HD2 H 6.231 0.002 1 782 1853 100 HIS HE1 H 7.503 0.007 1 783 1853 100 HIS CA C 57.993 0.059 1 784 1853 100 HIS CB C 32.052 0.031 1 785 1853 100 HIS CD2 C 119.053 0.030 1 786 1853 100 HIS CE1 C 137.291 0.020 1 787 1853 100 HIS N N 128.886 0.008 1 788 1854 101 CYS H H 8.035 0.004 1 789 1854 101 CYS HA H 2.834 0.003 1 790 1854 101 CYS HB2 H 1.511 0.003 2 791 1854 101 CYS HB3 H 1.511 0.003 2 792 1854 101 CYS CA C 61.908 0.018 1 793 1854 101 CYS CB C 27.298 0.042 1 794 1854 101 CYS N N 126.190 0.013 1 795 1855 102 LEU H H 10.121 0.008 1 796 1855 102 LEU HA H 3.913 0.004 1 797 1855 102 LEU HB2 H 1.766 0.005 2 798 1855 102 LEU HB3 H 1.336 0.006 2 799 1855 102 LEU HD1 H 0.835 0.003 1 800 1855 102 LEU HD2 H 0.775 0.002 1 801 1855 102 LEU HG H 1.670 0.002 1 802 1855 102 LEU CA C 57.461 0.029 1 803 1855 102 LEU CB C 40.719 0.065 1 804 1855 102 LEU CD1 C 24.929 0.013 1 805 1855 102 LEU CD2 C 22.562 0.023 1 806 1855 102 LEU CG C 26.886 0.004 1 807 1856 103 ASP H H 7.326 0.004 1 808 1856 103 ASP HA H 4.662 0.005 1 809 1856 103 ASP HB2 H 2.957 0.005 2 810 1856 103 ASP HB3 H 2.643 0.006 2 811 1856 103 ASP CA C 57.482 0.018 1 812 1856 103 ASP CB C 40.319 0.018 1 813 1856 103 ASP N N 118.081 0.013 1 814 1857 104 ILE H H 7.524 0.003 1 815 1857 104 ILE HA H 3.523 0.003 1 816 1857 104 ILE HB H 1.914 0.003 1 817 1857 104 ILE HD1 H 0.801 0.002 1 818 1857 104 ILE HG12 H 1.655 0.003 2 819 1857 104 ILE HG13 H 0.963 0.007 2 820 1857 104 ILE HG2 H 0.338 0.003 1 821 1857 104 ILE CA C 64.183 0.011 1 822 1857 104 ILE CB C 36.785 0.029 1 823 1857 104 ILE CD1 C 15.031 0.024 1 824 1857 104 ILE CG1 C 29.447 0.028 1 825 1857 104 ILE CG2 C 16.774 0.012 1 826 1857 104 ILE N N 122.092 0.020 1 827 1858 105 LEU H H 8.678 0.003 1 828 1858 105 LEU HA H 3.388 0.004 1 829 1858 105 LEU HB2 H 1.463 0.004 2 830 1858 105 LEU HB3 H 0.891 0.005 2 831 1858 105 LEU HD1 H -0.294 0.002 1 832 1858 105 LEU HD2 H 0.458 0.002 1 833 1858 105 LEU HG H 1.014 0.004 1 834 1858 105 LEU CA C 58.056 0.032 1 835 1858 105 LEU CB C 40.499 0.043 1 836 1858 105 LEU CD1 C 19.717 0.018 1 837 1858 105 LEU CD2 C 25.029 0.017 1 838 1858 105 LEU CG C 25.858 0.043 1 839 1858 105 LEU N N 120.472 0.018 1 840 1859 106 PHE H H 8.301 0.003 1 841 1859 106 PHE HA H 4.178 0.002 1 842 1859 106 PHE HB2 H 3.340 0.002 2 843 1859 106 PHE HB3 H 3.183 0.004 2 844 1859 106 PHE HD1 H 7.289 0.003 3 845 1859 106 PHE HD2 H 7.289 0.003 3 846 1859 106 PHE CA C 61.192 0.023 1 847 1859 106 PHE CB C 38.465 0.033 1 848 1859 106 PHE CD1 C 131.445 0.015 3 849 1859 106 PHE N N 119.269 0.021 1 850 1860 107 ALA H H 7.948 0.003 1 851 1860 107 ALA HA H 4.110 0.003 1 852 1860 107 ALA HB H 1.856 0.003 1 853 1860 107 ALA CA C 55.156 0.058 1 854 1860 107 ALA CB C 19.702 0.014 1 855 1860 107 ALA N N 121.361 0.008 1 856 1861 108 PHE H H 9.626 0.004 1 857 1861 108 PHE HA H 4.385 0.002 1 858 1861 108 PHE HB2 H 3.456 0.006 2 859 1861 108 PHE HB3 H 3.010 0.004 2 860 1861 108 PHE HD1 H 7.325 0.002 3 861 1861 108 PHE HD2 H 7.325 0.002 3 862 1861 108 PHE HE1 H 7.220 0.003 3 863 1861 108 PHE HE2 H 7.220 0.003 3 864 1861 108 PHE HZ H 7.097 0.005 1 865 1861 108 PHE CA C 59.389 0.027 1 866 1861 108 PHE CB C 36.994 0.043 1 867 1861 108 PHE CD1 C 130.471 0.024 3 868 1861 108 PHE CE1 C 130.520 0.022 3 869 1861 108 PHE CZ C 128.596 0.045 1 870 1861 108 PHE N N 119.388 0.100 1 871 1862 109 THR H H 8.263 0.005 1 872 1862 109 THR HA H 3.813 0.004 1 873 1862 109 THR HB H 4.146 0.004 1 874 1862 109 THR HG2 H 1.132 0.003 1 875 1862 109 THR CA C 66.546 0.039 1 876 1862 109 THR CB C 67.934 0.031 1 877 1862 109 THR CG2 C 21.455 0.027 1 878 1862 109 THR N N 115.943 0.008 1 879 1863 110 LYS H H 8.171 0.002 1 880 1863 110 LYS HA H 3.828 0.002 1 881 1863 110 LYS HB2 H 1.750 0.003 2 882 1863 110 LYS HB3 H 1.653 0.002 2 883 1863 110 LYS HD2 H 1.564 0.002 2 884 1863 110 LYS HD3 H 1.564 0.002 2 885 1863 110 LYS HE2 H 2.882 0.001 2 886 1863 110 LYS HE3 H 2.825 0.001 2 887 1863 110 LYS HG2 H 1.276 0.005 2 888 1863 110 LYS HG3 H 1.276 0.005 2 889 1863 110 LYS CA C 59.176 0.021 1 890 1863 110 LYS CB C 31.594 0.016 1 891 1863 110 LYS CD C 29.097 0.024 1 892 1863 110 LYS CE C 41.731 0.004 1 893 1863 110 LYS CG C 24.526 0.022 1 894 1863 110 LYS N N 122.966 0.007 1 895 1864 111 ARG H H 7.439 0.003 1 896 1864 111 ARG HA H 4.008 0.004 1 897 1864 111 ARG HB2 H 1.851 0.010 2 898 1864 111 ARG HB3 H 1.777 0.002 2 899 1864 111 ARG HD2 H 3.040 0.007 2 900 1864 111 ARG HD3 H 3.005 0.008 2 901 1864 111 ARG HE H 7.599 0.001 1 902 1864 111 ARG HG2 H 1.622 0.004 2 903 1864 111 ARG HG3 H 1.424 0.003 2 904 1864 111 ARG CA C 58.491 0.026 1 905 1864 111 ARG CB C 29.420 0.007 1 906 1864 111 ARG CD C 42.526 0.019 1 907 1864 111 ARG CG C 27.050 0.011 1 908 1864 111 ARG N N 117.711 0.015 1 909 1864 111 ARG NE N 83.931 0.021 1 910 1865 112 VAL H H 7.156 0.003 1 911 1865 112 VAL HA H 3.806 0.002 1 912 1865 112 VAL HB H 2.196 0.004 1 913 1865 112 VAL HG1 H 0.900 0.003 1 914 1865 112 VAL HG2 H 1.013 0.003 1 915 1865 112 VAL CA C 64.538 0.009 1 916 1865 112 VAL CB C 31.998 0.005 1 917 1865 112 VAL CG1 C 21.153 0.019 1 918 1865 112 VAL CG2 C 22.226 0.024 1 919 1865 112 VAL N N 116.969 0.019 1 920 1866 113 LEU H H 8.079 0.005 1 921 1866 113 LEU HA H 4.175 0.002 1 922 1866 113 LEU HB2 H 1.738 0.006 2 923 1866 113 LEU HB3 H 1.546 0.003 2 924 1866 113 LEU HD1 H 0.846 0.002 1 925 1866 113 LEU HD2 H 0.850 0.001 1 926 1866 113 LEU HG H 1.724 0.001 1 927 1866 113 LEU CA C 56.036 0.013 1 928 1866 113 LEU CB C 42.112 0.100 1 929 1866 113 LEU CD1 C 25.195 0.029 1 930 1866 113 LEU CD2 C 22.523 0.020 1 931 1866 113 LEU CG C 26.602 0.014 1 932 1866 113 LEU N N 118.923 0.014 1 933 1867 114 GLY H H 8.107 0.006 1 934 1867 114 GLY HA2 H 4.024 0.005 2 935 1867 114 GLY HA3 H 3.926 0.001 2 936 1867 114 GLY CA C 45.235 0.037 1 937 1867 114 GLY N N 107.015 0.100 1 938 1868 115 GLU H H 8.230 0.003 1 939 1868 115 GLU HA H 4.314 0.003 1 940 1868 115 GLU HB2 H 2.116 0.003 2 941 1868 115 GLU HB3 H 1.953 0.002 2 942 1868 115 GLU HG2 H 2.271 0.009 2 943 1868 115 GLU HG3 H 2.271 0.009 2 944 1868 115 GLU CA C 56.509 0.100 1 945 1868 115 GLU CB C 29.815 0.100 1 946 1868 115 GLU N N 120.158 0.003 1 947 1869 116 SER H H 8.365 0.003 1 948 1869 116 SER HA H 4.489 0.001 1 949 1869 116 SER HB2 H 3.977 0.004 2 950 1869 116 SER HB3 H 3.911 0.003 2 951 1869 116 SER CA C 58.479 0.008 1 952 1869 116 SER CB C 63.691 0.032 1 953 1869 116 SER N N 116.025 0.006 1 954 1870 117 GLY H H 8.446 0.003 1 955 1870 117 GLY HA2 H 4.035 0.005 2 956 1870 117 GLY HA3 H 3.930 0.001 2 957 1870 117 GLY CA C 45.414 0.013 1 958 1870 117 GLY N N 110.527 0.011 1 959 1871 118 GLU H H 8.396 0.003 1 960 1871 118 GLU HA H 4.270 0.002 1 961 1871 118 GLU HB2 H 2.063 0.004 2 962 1871 118 GLU HB3 H 1.961 0.002 2 963 1871 118 GLU HG2 H 2.273 0.005 2 964 1871 118 GLU HG3 H 2.273 0.005 2 965 1871 118 GLU CA C 56.980 0.032 1 966 1871 118 GLU CB C 29.809 0.004 1 967 1871 118 GLU N N 120.846 0.001 1 968 1872 119 MET H H 8.379 0.003 1 969 1872 119 MET HA H 4.438 0.002 1 970 1872 119 MET HB2 H 2.112 0.002 2 971 1872 119 MET HB3 H 2.057 0.010 2 972 1872 119 MET HG2 H 2.603 0.001 2 973 1872 119 MET HG3 H 2.538 0.001 2 974 1872 119 MET CA C 55.844 0.028 1 975 1872 119 MET CB C 32.063 0.011 1 976 1872 119 MET CG C 31.947 0.013 1 977 1872 119 MET N N 120.335 0.005 1 978 1873 120 ASP H H 8.337 0.004 1 979 1873 120 ASP HA H 4.474 0.005 1 980 1873 120 ASP HB2 H 2.682 0.003 2 981 1873 120 ASP HB3 H 2.682 0.003 2 982 1873 120 ASP CA C 55.528 0.020 1 983 1873 120 ASP CB C 40.527 0.065 1 984 1873 120 ASP N N 121.151 0.015 1 985 1874 121 ALA H H 8.152 0.002 1 986 1874 121 ALA HA H 4.168 0.003 1 987 1874 121 ALA HB H 1.416 0.004 1 988 1874 121 ALA CA C 53.524 0.014 1 989 1874 121 ALA CB C 18.465 0.009 1 990 1874 121 ALA N N 122.507 0.008 1 991 1875 122 LEU H H 7.968 0.003 1 992 1875 122 LEU HA H 4.226 0.003 1 993 1875 122 LEU HB2 H 1.724 0.010 2 994 1875 122 LEU HB3 H 1.656 0.010 2 995 1875 122 LEU HD1 H 0.916 0.002 1 996 1875 122 LEU HD2 H 0.856 0.002 1 997 1875 122 LEU HG H 1.661 0.010 1 998 1875 122 LEU CA C 55.842 0.032 1 999 1875 122 LEU CB C 41.703 0.020 1 1000 1875 122 LEU CD1 C 24.554 0.030 1 1001 1875 122 LEU CD2 C 23.548 0.019 1 1002 1875 122 LEU CG C 26.839 0.100 1 1003 1875 122 LEU N N 119.132 0.002 1 1004 1876 123 ARG H H 8.014 0.005 1 1005 1876 123 ARG HA H 4.128 0.002 1 1006 1876 123 ARG HB2 H 1.866 0.002 2 1007 1876 123 ARG HB3 H 1.763 0.001 2 1008 1876 123 ARG HD2 H 3.141 0.002 2 1009 1876 123 ARG HD3 H 3.141 0.002 2 1010 1876 123 ARG HG3 H 1.522 0.010 2 1011 1876 123 ARG CA C 57.160 0.029 1 1012 1876 123 ARG CB C 29.885 0.030 1 1013 1876 123 ARG CD C 42.957 0.022 1 1014 1876 123 ARG CG C 27.007 0.100 1 1015 1876 123 ARG N N 120.385 0.014 1 1016 1877 124 ILE H H 7.933 0.003 1 1017 1877 124 ILE HA H 3.973 0.003 1 1018 1877 124 ILE HB H 1.839 0.002 1 1019 1877 124 ILE HD1 H 0.833 0.015 1 1020 1877 124 ILE HG12 H 1.511 0.002 2 1021 1877 124 ILE HG13 H 1.156 0.002 2 1022 1877 124 ILE HG2 H 0.873 0.001 1 1023 1877 124 ILE CA C 62.041 0.009 1 1024 1877 124 ILE CB C 38.201 0.007 1 1025 1877 124 ILE CD1 C 12.680 0.017 1 1026 1877 124 ILE CG1 C 27.666 0.017 1 1027 1877 124 ILE CG2 C 17.148 0.005 1 1028 1877 124 ILE N N 120.150 0.007 1 1029 1878 125 GLN H H 8.169 0.003 1 1030 1878 125 GLN HA H 4.237 0.002 1 1031 1878 125 GLN HB2 H 2.106 0.010 2 1032 1878 125 GLN HB3 H 2.039 0.001 2 1033 1878 125 GLN HE21 H 7.525 0.010 2 1034 1878 125 GLN HE22 H 6.841 0.010 2 1035 1878 125 GLN HG2 H 2.356 0.008 2 1036 1878 125 GLN HG3 H 2.356 0.008 2 1037 1878 125 GLN CA C 56.346 0.100 1 1038 1878 125 GLN CB C 28.925 0.009 1 1039 1878 125 GLN CG C 33.574 0.007 1 1040 1878 125 GLN N N 122.206 0.003 1 1041 1879 126 MET H H 8.295 0.003 1 1042 1879 126 MET HA H 4.367 0.003 1 1043 1879 126 MET HB2 H 2.090 0.003 2 1044 1879 126 MET HB3 H 2.029 0.010 2 1045 1879 126 MET HG2 H 2.612 0.001 2 1046 1879 126 MET HG3 H 2.503 0.003 2 1047 1879 126 MET CA C 55.741 0.036 1 1048 1879 126 MET CB C 32.695 0.021 1 1049 1879 126 MET CG C 31.910 0.005 1 1050 1879 126 MET N N 120.146 0.012 1 1051 1880 127 GLU H H 8.233 0.004 1 1052 1880 127 GLU HG2 H 2.330 0.010 2 1053 1880 127 GLU HG3 H 2.239 0.010 2 1054 1880 127 GLU N N 120.798 0.002 1 1055 1881 128 GLU H H 8.273 0.003 1 1056 1881 128 GLU HA H 4.279 0.002 1 1057 1881 128 GLU HB2 H 2.062 0.004 2 1058 1881 128 GLU HB3 H 1.928 0.012 2 1059 1881 128 GLU HG2 H 2.317 0.010 2 1060 1881 128 GLU HG3 H 2.229 0.010 2 1061 1881 128 GLU CA C 56.312 0.100 1 1062 1881 128 GLU CB C 29.900 0.100 1 1063 1881 128 GLU N N 121.872 0.012 1 1064 1882 129 ARG H H 7.924 0.003 1 1065 1882 129 ARG HA H 4.154 0.003 1 1066 1882 129 ARG HB2 H 1.831 0.002 2 1067 1882 129 ARG HB3 H 1.696 0.002 2 1068 1882 129 ARG HD2 H 3.092 0.002 2 1069 1882 129 ARG HD3 H 3.092 0.002 2 1070 1882 129 ARG HG2 H 1.563 0.003 2 1071 1882 129 ARG HG3 H 1.563 0.003 2 1072 1882 129 ARG CA C 57.149 0.013 1 1073 1882 129 ARG CB C 31.266 0.018 1 1074 1882 129 ARG CD C 43.109 0.100 1 1075 1882 129 ARG CG C 26.852 0.100 1 1076 1882 129 ARG N N 127.339 0.007 1 stop_ save_