data_18623 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of mutant (T170E) second CARD of human RIG-I ; _BMRB_accession_number 18623 _BMRB_flat_file_name bmr18623.str _Entry_type original _Submission_date 2012-07-27 _Accession_date 2012-07-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dutta Kaushik . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 559 "13C chemical shifts" 431 "15N chemical shifts" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-18 update BMRB 'update entry citation' 2012-10-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18622 'Solution structure of second CARD of human RIG-I.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23063562 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ferrage Fabien . . 2 Dutta Kaushik . . 3 Nistal-Villan Estanislao . . 4 Patel Jenish R. . 5 Sanchez-Aparicio Maria T. . 6 'De Ioannes' Pablo . . 7 Buku Angeliki . . 8 Aseguinolaza 'Gloria Gonzalez' . . 9 Garcia-Sastre Adolfo . . 10 Aggarwal Aneel K. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 20 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2048 _Page_last 2061 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'mutant (T170E) second CARD of human RIG-I' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'mutant (T170E) second CARD of human RIG-I' $card2_mutant 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_card2_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'mutant (T170E) second CARD of human RIG-I' _Molecular_mass 11397.522 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; GSHMKKIEKLEEYRLLLKRL QPEFKTRIIPTDIISDLSEC LINQECEEILQICSTKGMMA GAEKLVECLLRSDKENWPKE LKLALEKERNKFSELWIVEK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 91 GLY 2 92 SER 3 93 HIS 4 94 MET 5 95 LYS 6 96 LYS 7 97 ILE 8 98 GLU 9 99 LYS 10 100 LEU 11 101 GLU 12 102 GLU 13 103 TYR 14 104 ARG 15 105 LEU 16 106 LEU 17 107 LEU 18 108 LYS 19 109 ARG 20 110 LEU 21 111 GLN 22 112 PRO 23 113 GLU 24 114 PHE 25 115 LYS 26 116 THR 27 117 ARG 28 118 ILE 29 119 ILE 30 120 PRO 31 121 THR 32 122 ASP 33 123 ILE 34 124 ILE 35 125 SER 36 126 ASP 37 127 LEU 38 128 SER 39 129 GLU 40 130 CYS 41 131 LEU 42 132 ILE 43 133 ASN 44 134 GLN 45 135 GLU 46 136 CYS 47 137 GLU 48 138 GLU 49 139 ILE 50 140 LEU 51 141 GLN 52 142 ILE 53 143 CYS 54 144 SER 55 145 THR 56 146 LYS 57 147 GLY 58 148 MET 59 149 MET 60 150 ALA 61 151 GLY 62 152 ALA 63 153 GLU 64 154 LYS 65 155 LEU 66 156 VAL 67 157 GLU 68 158 CYS 69 159 LEU 70 160 LEU 71 161 ARG 72 162 SER 73 163 ASP 74 164 LYS 75 165 GLU 76 166 ASN 77 167 TRP 78 168 PRO 79 169 LYS 80 170 GLU 81 171 LEU 82 172 LYS 83 173 LEU 84 174 ALA 85 175 LEU 86 176 GLU 87 177 LYS 88 178 GLU 89 179 ARG 90 180 ASN 91 181 LYS 92 182 PHE 93 183 SER 94 184 GLU 95 185 LEU 96 186 TRP 97 187 ILE 98 188 VAL 99 189 GLU 100 190 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 18622 "second CARD of human RIG-I" 100.00 100 99.00 99.00 5.17e-62 PDB 2LWD "Solution Structure Of Second Card Of Human Rig-I" 100.00 100 99.00 99.00 5.17e-62 PDB 2LWE "Solution Structure Of Mutant (T170e) Second Card Of Human Rig-I" 100.00 100 100.00 100.00 1.20e-62 PDB 4NQK "Structure Of An Ubiquitin Complex" 97.00 203 97.94 97.94 1.72e-57 PDB 4P4H "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" 97.00 205 97.94 97.94 1.32e-57 DBJ BAG11006 "ATP-dependent RNA helicase DDX58 [synthetic construct]" 97.00 925 97.94 97.94 1.17e-53 DBJ BAG54273 "unnamed protein product [Homo sapiens]" 97.00 854 97.94 97.94 1.07e-53 EMBL CAI46068 "hypothetical protein [Homo sapiens]" 97.00 703 97.94 97.94 2.53e-54 GB AAD19826 "RNA helicase [Homo sapiens]" 97.00 925 97.94 97.94 1.34e-53 GB AAI07732 "DDX58 protein, partial [Homo sapiens]" 97.00 251 97.94 97.94 5.17e-57 GB AAI32787 "DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 [Homo sapiens]" 97.00 925 97.94 97.94 1.17e-53 GB AAI36611 "DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 [Homo sapiens]" 97.00 925 97.94 97.94 1.17e-53 GB EAW58547 "DEAD (Asp-Glu-Ala-Asp) box polypeptide 58, isoform CRA_a, partial [Homo sapiens]" 97.00 703 97.94 97.94 2.41e-54 REF NP_055129 "probable ATP-dependent RNA helicase DDX58 [Homo sapiens]" 97.00 925 97.94 97.94 1.17e-53 REF XP_001156662 "PREDICTED: probable ATP-dependent RNA helicase DDX58 [Pan troglodytes]" 97.00 925 97.94 97.94 1.17e-53 REF XP_002819761 "PREDICTED: probable ATP-dependent RNA helicase DDX58 isoform X1 [Pongo abelii]" 97.00 925 97.94 97.94 1.57e-53 REF XP_003830148 "PREDICTED: probable ATP-dependent RNA helicase DDX58 isoform X1 [Pan paniscus]" 97.00 925 97.94 97.94 1.11e-53 REF XP_004047964 "PREDICTED: probable ATP-dependent RNA helicase DDX58 [Gorilla gorilla gorilla]" 97.00 890 97.94 97.94 8.04e-54 SP O95786 "RecName: Full=Probable ATP-dependent RNA helicase DDX58; AltName: Full=DEAD box protein 58; AltName: Full=RIG-I-like receptor 1" 97.00 925 97.94 97.94 1.17e-53 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $card2_mutant Human 9606 Eukaryota Metazoa Homo sapiens 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 $card2_mutant 'recombinant technology' . Escherichia coli . pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '15N labeled sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $card2_mutant 300 uM '[U-100% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' Bis-Tris 50 mM 'natural abundance' 'sodium chloride' 250 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '13C-15N labeled sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $card2_mutant 300 uM '[U-100% 13C; U-100% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' Bis-Tris 50 mM 'natural abundance' 'sodium chloride' 250 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details '13C-15N labeled sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $card2_mutant 300 uM '[U-100% 13C; U-100% 15N]' D2O 100 % 'natural abundance' Bis-Tris 50 mM 'natural abundance' 'sodium chloride' 250 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 8.3 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'chemical shift assignment' 'chemical shift calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details CryoProbe save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details CryoProbe save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details CryoProbe save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_2 save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_aliphatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_3 save_ save_3D_1H-13C_NOESY_aromatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_3 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' 250 . mM pH 7.5 . pH pressure 1 . atm temperature 273 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D HBHA(CO)NH' '3D C(CO)NH' '3D H(CCO)NH' '3D 1H-13C NOESY aromatic' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'mutant (T170E) second CARD of human RIG-I' _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 93 3 HIS HA H 4.5960 0.03 1 2 93 3 HIS HB2 H 3.1080 0.04 2 3 93 3 HIS HB3 H 3.1770 0.04 2 4 93 3 HIS HD2 H 7.1885 0.04 1 5 93 3 HIS HE1 H 8.2922 0.04 1 6 93 3 HIS C C 175.2566 0.09 1 7 93 3 HIS CA C 56.5347 0.40 1 8 93 3 HIS CB C 30.1000 0.40 1 9 93 3 HIS CD2 C 119.8620 0.35 1 10 93 3 HIS CE1 C 137.1764 0.35 1 11 94 4 MET H H 8.3047 0.01 1 12 94 4 MET HA H 4.3530 0.03 1 13 94 4 MET HB2 H 1.9650 0.04 2 14 94 4 MET HG2 H 2.4900 0.04 2 15 94 4 MET HG3 H 2.4400 0.04 2 16 94 4 MET C C 176.2397 0.09 1 17 94 4 MET CA C 55.9042 0.40 1 18 94 4 MET CB C 32.9316 0.40 1 19 94 4 MET CG C 31.8750 0.35 1 20 94 4 MET N N 121.5950 0.05 1 21 95 5 LYS H H 8.3645 0.01 1 22 95 5 LYS HA H 4.2370 0.03 1 23 95 5 LYS HB2 H 1.7650 0.04 2 24 95 5 LYS HG2 H 1.4010 0.04 2 25 95 5 LYS HD2 H 1.7100 0.04 2 26 95 5 LYS HD3 H 1.6750 0.04 2 27 95 5 LYS HE2 H 2.9600 0.04 2 28 95 5 LYS C C 176.7985 0.09 1 29 95 5 LYS CA C 56.5111 0.40 1 30 95 5 LYS CB C 32.9464 0.40 1 31 95 5 LYS CG C 24.7590 0.35 1 32 95 5 LYS CD C 28.5010 0.35 1 33 95 5 LYS CE C 42.2290 0.35 1 34 95 5 LYS N N 123.0106 0.05 1 35 96 6 LYS H H 8.3524 0.01 1 36 96 6 LYS HA H 4.1960 0.03 1 37 96 6 LYS HB2 H 1.7700 0.04 2 38 96 6 LYS HG2 H 1.4180 0.04 2 39 96 6 LYS HG3 H 1.3500 0.04 2 40 96 6 LYS HD2 H 1.6670 0.04 2 41 96 6 LYS HE2 H 2.9500 0.04 2 42 96 6 LYS C C 177.0763 0.09 1 43 96 6 LYS CA C 57.2375 0.40 1 44 96 6 LYS CB C 32.7867 0.40 1 45 96 6 LYS CG C 24.7840 0.35 1 46 96 6 LYS N N 123.2688 0.05 1 47 97 7 ILE H H 8.2116 0.01 1 48 97 7 ILE HA H 4.0800 0.03 1 49 97 7 ILE HB H 1.8650 0.03 1 50 97 7 ILE HG12 H 1.5000 0.04 2 51 97 7 ILE HG13 H 1.2400 0.04 2 52 97 7 ILE HG2 H 0.8490 0.04 1 53 97 7 ILE HD1 H 0.8490 0.04 1 54 97 7 ILE C C 176.7273 0.09 1 55 97 7 ILE CA C 61.5384 0.40 1 56 97 7 ILE CB C 38.1712 0.40 1 57 97 7 ILE CG1 C 27.7090 0.35 1 58 97 7 ILE CG2 C 18.1780 0.35 1 59 97 7 ILE CD1 C 13.2570 0.35 1 60 97 7 ILE N N 122.2514 0.05 1 61 98 8 GLU H H 8.4891 0.01 1 62 98 8 GLU HA H 4.1950 0.03 1 63 98 8 GLU HB2 H 2.0150 0.04 2 64 98 8 GLU HG2 H 2.2780 0.04 2 65 98 8 GLU C C 178.0701 0.09 1 66 98 8 GLU CA C 57.9658 0.40 1 67 98 8 GLU CB C 29.9981 0.40 1 68 98 8 GLU CG C 36.5290 0.35 1 69 98 8 GLU N N 125.1970 0.05 1 70 99 9 LYS H H 8.4250 0.01 1 71 99 9 LYS HA H 4.1270 0.03 1 72 99 9 LYS HB2 H 1.8580 0.04 2 73 99 9 LYS HG2 H 1.4770 0.04 2 74 99 9 LYS HD2 H 1.6660 0.04 2 75 99 9 LYS C C 177.9372 0.09 1 76 99 9 LYS CA C 58.1450 0.40 1 77 99 9 LYS CB C 32.1914 0.40 1 78 99 9 LYS CG C 24.6930 0.35 1 79 99 9 LYS N N 121.5477 0.05 1 80 100 10 LEU H H 8.2351 0.01 1 81 100 10 LEU HA H 4.2980 0.03 1 82 100 10 LEU HB2 H 1.8240 0.04 2 83 100 10 LEU HB3 H 1.7300 0.04 2 84 100 10 LEU HG H 1.7330 0.04 1 85 100 10 LEU HD1 H 0.8800 0.04 2 86 100 10 LEU HD2 H 0.9500 0.04 2 87 100 10 LEU C C 179.1700 0.09 1 88 100 10 LEU CA C 57.7822 0.40 1 89 100 10 LEU CB C 42.7595 0.40 1 90 100 10 LEU CG C 26.9050 0.35 1 91 100 10 LEU CD1 C 23.8980 0.35 2 92 100 10 LEU N N 118.5855 0.05 1 93 101 11 GLU H H 8.1003 0.01 1 94 101 11 GLU HA H 4.1060 0.03 1 95 101 11 GLU HB2 H 2.1350 0.04 2 96 101 11 GLU HB3 H 2.0330 0.04 2 97 101 11 GLU HG2 H 2.3420 0.04 2 98 101 11 GLU C C 178.7038 0.09 1 99 101 11 GLU CA C 59.8520 0.40 1 100 101 11 GLU CB C 29.2474 0.40 1 101 101 11 GLU CG C 35.6600 0.35 1 102 101 11 GLU N N 119.0193 0.05 1 103 102 12 GLU H H 7.9927 0.01 1 104 102 12 GLU HA H 3.9110 0.03 1 105 102 12 GLU HB2 H 1.8460 0.04 2 106 102 12 GLU HB3 H 1.6600 0.04 2 107 102 12 GLU HG2 H 2.0000 0.04 2 108 102 12 GLU HG3 H 1.8800 0.04 2 109 102 12 GLU C C 179.4895 0.09 1 110 102 12 GLU CA C 59.6775 0.40 1 111 102 12 GLU CB C 29.2202 0.40 1 112 102 12 GLU CG C 36.0460 0.35 1 113 102 12 GLU N N 118.0184 0.05 1 114 103 13 TYR H H 7.5086 0.01 1 115 103 13 TYR HA H 4.2650 0.03 1 116 103 13 TYR HB2 H 2.9020 0.04 2 117 103 13 TYR HB3 H 2.5720 0.04 2 118 103 13 TYR HD1 H 6.6500 0.04 3 119 103 13 TYR HE1 H 6.5300 0.04 3 120 103 13 TYR C C 178.2356 0.09 1 121 103 13 TYR CA C 62.1462 0.40 1 122 103 13 TYR CB C 38.1334 0.40 1 123 103 13 TYR CD1 C 132.6128 0.35 3 124 103 13 TYR CE1 C 118.2587 0.35 3 125 103 13 TYR N N 118.9442 0.05 1 126 104 14 ARG H H 8.6835 0.01 1 127 104 14 ARG HA H 4.2160 0.03 1 128 104 14 ARG HB2 H 2.2030 0.04 2 129 104 14 ARG HB3 H 1.9860 0.04 2 130 104 14 ARG HG2 H 1.9100 0.04 2 131 104 14 ARG HD2 H 3.2300 0.04 2 132 104 14 ARG HD3 H 3.4200 0.04 2 133 104 14 ARG C C 178.3881 0.09 1 134 104 14 ARG CA C 60.7118 0.40 1 135 104 14 ARG CB C 30.6883 0.40 1 136 104 14 ARG CG C 29.1680 0.35 1 137 104 14 ARG N N 121.3366 0.05 1 138 105 15 LEU H H 8.0833 0.01 1 139 105 15 LEU HA H 4.0040 0.03 1 140 105 15 LEU HB2 H 1.8350 0.04 2 141 105 15 LEU HB3 H 1.5110 0.04 2 142 105 15 LEU HG H 1.5190 0.04 1 143 105 15 LEU HD1 H 0.8880 0.04 2 144 105 15 LEU HD2 H 0.8880 0.04 2 145 105 15 LEU C C 179.9421 0.09 1 146 105 15 LEU CA C 58.1808 0.40 1 147 105 15 LEU CB C 41.7325 0.40 1 148 105 15 LEU CD1 C 24.8130 0.35 2 149 105 15 LEU CD2 C 23.2440 0.35 2 150 105 15 LEU N N 118.3356 0.05 1 151 106 16 LEU H H 7.9114 0.01 1 152 106 16 LEU HA H 4.2030 0.03 1 153 106 16 LEU HB2 H 2.0970 0.04 2 154 106 16 LEU HB3 H 1.5600 0.04 2 155 106 16 LEU HG H 1.6160 0.04 1 156 106 16 LEU HD1 H 0.5220 0.04 2 157 106 16 LEU HD2 H 0.9440 0.04 2 158 106 16 LEU C C 178.1271 0.09 1 159 106 16 LEU CA C 58.1855 0.40 1 160 106 16 LEU CB C 42.1577 0.40 1 161 106 16 LEU CD1 C 25.3810 0.35 2 162 106 16 LEU CD2 C 22.8050 0.35 2 163 106 16 LEU N N 121.5184 0.05 1 164 107 17 LEU H H 8.7997 0.01 1 165 107 17 LEU HA H 4.3080 0.03 1 166 107 17 LEU HB2 H 2.1100 0.04 2 167 107 17 LEU HB3 H 2.1800 0.04 2 168 107 17 LEU HG H 1.3020 0.04 1 169 107 17 LEU HD1 H 0.4520 0.04 2 170 107 17 LEU HD2 H 0.2830 0.04 2 171 107 17 LEU C C 178.0314 0.09 1 172 107 17 LEU CA C 58.3318 0.40 1 173 107 17 LEU CB C 40.9651 0.40 1 174 107 17 LEU CG C 27.7490 0.35 1 175 107 17 LEU CD1 C 27.3150 0.35 2 176 107 17 LEU CD2 C 22.2580 0.35 2 177 107 17 LEU N N 119.0469 0.05 1 178 108 18 LYS H H 8.1992 0.01 1 179 108 18 LYS HA H 3.9050 0.03 1 180 108 18 LYS HB2 H 1.9310 0.04 2 181 108 18 LYS HG2 H 1.4110 0.04 2 182 108 18 LYS HG3 H 1.6300 0.04 2 183 108 18 LYS HD2 H 1.6220 0.04 2 184 108 18 LYS C C 180.3164 0.09 1 185 108 18 LYS CA C 59.9848 0.40 1 186 108 18 LYS CB C 32.2607 0.40 1 187 108 18 LYS CG C 25.8540 0.35 1 188 108 18 LYS CE C 42.2620 0.35 1 189 108 18 LYS N N 115.8733 0.05 1 190 109 19 ARG H H 8.1384 0.01 1 191 109 19 ARG HA H 4.1710 0.03 1 192 109 19 ARG HB2 H 2.1400 0.04 2 193 109 19 ARG HB3 H 2.3150 0.04 2 194 109 19 ARG HG2 H 1.8500 0.04 2 195 109 19 ARG HG3 H 1.9900 0.04 2 196 109 19 ARG HD2 H 3.2440 0.04 2 197 109 19 ARG HD3 H 3.4120 0.04 2 198 109 19 ARG C C 178.3683 0.09 1 199 109 19 ARG CA C 59.4429 0.40 1 200 109 19 ARG CB C 30.2467 0.40 1 201 109 19 ARG CG C 27.5360 0.35 1 202 109 19 ARG CD C 44.2600 0.35 1 203 109 19 ARG N N 119.8150 0.05 1 204 110 20 LEU H H 8.1633 0.01 1 205 110 20 LEU HA H 4.8180 0.03 1 206 110 20 LEU HB2 H 2.2070 0.04 2 207 110 20 LEU HB3 H 2.2300 0.04 2 208 110 20 LEU HG H 2.0900 0.04 1 209 110 20 LEU HD1 H 1.0850 0.04 2 210 110 20 LEU HD2 H 1.0160 0.04 2 211 110 20 LEU C C 177.0376 0.09 1 212 110 20 LEU CA C 54.1601 0.40 1 213 110 20 LEU CB C 43.2354 0.40 1 214 110 20 LEU CG C 27.0600 0.35 1 215 110 20 LEU CD1 C 27.0600 0.35 2 216 110 20 LEU CD2 C 22.5800 0.35 2 217 110 20 LEU N N 117.3939 0.05 1 218 111 21 GLN H H 7.6561 0.01 1 219 111 21 GLN HB2 H 2.2960 0.04 2 220 111 21 GLN HB3 H 2.3600 0.04 2 221 111 21 GLN HG2 H 2.4000 0.04 2 222 111 21 GLN CA C 62.2923 0.40 1 223 111 21 GLN CB C 26.8399 0.40 1 224 111 21 GLN N N 123.3497 0.05 1 225 112 22 PRO HA H 4.1970 0.03 1 226 112 22 PRO HB2 H 2.3700 0.04 2 227 112 22 PRO HB3 H 1.8930 0.04 2 228 112 22 PRO HG2 H 2.2170 0.04 2 229 112 22 PRO HG3 H 2.0070 0.04 2 230 112 22 PRO HD2 H 3.8020 0.04 2 231 112 22 PRO HD3 H 3.8600 0.04 2 232 112 22 PRO C C 179.4837 0.09 1 233 112 22 PRO CA C 66.7739 0.40 1 234 112 22 PRO CB C 31.1138 0.40 1 235 112 22 PRO CD C 50.4360 0.35 1 236 113 23 GLU H H 7.9262 0.01 1 237 113 23 GLU HA H 4.1640 0.03 1 238 113 23 GLU HB2 H 2.4300 0.04 2 239 113 23 GLU HB3 H 2.0200 0.04 2 240 113 23 GLU HG2 H 2.4230 0.04 2 241 113 23 GLU HG3 H 2.3630 0.04 2 242 113 23 GLU C C 178.0512 0.09 1 243 113 23 GLU CA C 59.1705 0.40 1 244 113 23 GLU CB C 29.5423 0.40 1 245 113 23 GLU CG C 36.0670 0.35 1 246 113 23 GLU N N 117.3386 0.05 1 247 114 24 PHE H H 8.8859 0.01 1 248 114 24 PHE HA H 3.0810 0.03 1 249 114 24 PHE HB2 H 2.9840 0.04 2 250 114 24 PHE HB3 H 2.4180 0.04 2 251 114 24 PHE HD1 H 6.2000 0.04 3 252 114 24 PHE HE1 H 6.7000 0.04 3 253 114 24 PHE HZ H 6.5580 0.04 1 254 114 24 PHE C C 177.1411 0.09 1 255 114 24 PHE CA C 60.9253 0.40 1 256 114 24 PHE CB C 39.6939 0.40 1 257 114 24 PHE CD1 C 132.5508 0.35 3 258 114 24 PHE CE1 C 129.8946 0.35 3 259 114 24 PHE CZ C 127.6898 0.35 1 260 114 24 PHE N N 122.3619 0.05 1 261 115 25 LYS H H 8.4484 0.01 1 262 115 25 LYS HA H 3.8690 0.03 1 263 115 25 LYS HB2 H 1.9530 0.04 2 264 115 25 LYS HB3 H 1.7500 0.04 2 265 115 25 LYS HG2 H 1.5710 0.04 2 266 115 25 LYS HD2 H 1.7190 0.04 2 267 115 25 LYS HE2 H 2.8900 0.04 2 268 115 25 LYS C C 176.0810 0.09 1 269 115 25 LYS CA C 59.0664 0.40 1 270 115 25 LYS CB C 32.4486 0.40 1 271 115 25 LYS CG C 24.9670 0.35 1 272 115 25 LYS CD C 30.8680 0.35 1 273 115 25 LYS N N 113.4833 0.05 1 274 116 26 THR H H 7.1558 0.01 1 275 116 26 THR HA H 4.2470 0.03 1 276 116 26 THR HB H 4.2470 0.03 1 277 116 26 THR HG2 H 1.2470 0.04 1 278 116 26 THR C C 176.0350 0.09 1 279 116 26 THR CA C 62.8735 0.40 1 280 116 26 THR CB C 69.7756 0.40 1 281 116 26 THR CG2 C 22.3260 0.35 1 282 116 26 THR N N 106.5949 0.05 1 283 117 27 ARG H H 7.4989 0.01 1 284 117 27 ARG HA H 4.3770 0.03 1 285 117 27 ARG HB2 H 2.0470 0.04 2 286 117 27 ARG HB3 H 1.5410 0.04 2 287 117 27 ARG HG2 H 1.7490 0.04 2 288 117 27 ARG HG3 H 1.5490 0.04 2 289 117 27 ARG HD2 H 3.0800 0.04 2 290 117 27 ARG C C 176.0001 0.09 1 291 117 27 ARG CA C 56.6215 0.40 1 292 117 27 ARG CB C 32.4559 0.40 1 293 117 27 ARG CG C 27.4310 0.35 1 294 117 27 ARG CD C 43.8700 0.35 1 295 117 27 ARG N N 118.3301 0.05 1 296 118 28 ILE H H 7.4868 0.01 1 297 118 28 ILE HA H 3.8300 0.03 1 298 118 28 ILE HB H 1.1120 0.03 1 299 118 28 ILE HG12 H 0.2000 0.04 2 300 118 28 ILE HG13 H -0.3200 0.04 2 301 118 28 ILE HG2 H 0.0800 0.04 1 302 118 28 ILE HD1 H -0.2550 0.04 1 303 118 28 ILE C C 174.0044 0.09 1 304 118 28 ILE CA C 59.3236 0.40 1 305 118 28 ILE CB C 36.7286 0.40 1 306 118 28 ILE CG1 C 26.9890 0.35 1 307 118 28 ILE CG2 C 17.3380 0.35 1 308 118 28 ILE CD1 C 12.0600 0.35 1 309 118 28 ILE N N 120.4282 0.05 1 310 119 29 ILE H H 8.5290 0.01 1 311 119 29 ILE HA H 4.4300 0.03 1 312 119 29 ILE HB H 2.1010 0.03 1 313 119 29 ILE HG12 H 1.4400 0.04 2 314 119 29 ILE HG13 H 1.2000 0.04 2 315 119 29 ILE HG2 H 0.8520 0.04 1 316 119 29 ILE HD1 H 0.7600 0.04 1 317 119 29 ILE CA C 56.8148 0.40 1 318 119 29 ILE CB C 36.3921 0.40 1 319 119 29 ILE CG1 C 26.6000 0.35 1 320 119 29 ILE CG2 C 17.7000 0.35 1 321 119 29 ILE CD1 C 11.3000 0.35 1 322 119 29 ILE N N 128.8932 0.05 1 323 120 30 PRO HA H 3.6860 0.03 1 324 120 30 PRO HB2 H 1.7720 0.04 2 325 120 30 PRO HB3 H 2.0300 0.04 2 326 120 30 PRO HG2 H 1.7840 0.04 2 327 120 30 PRO HG3 H 1.5400 0.04 2 328 120 30 PRO HD2 H 4.0480 0.04 2 329 120 30 PRO HD3 H 4.2300 0.04 2 330 120 30 PRO C C 176.6338 0.09 1 331 120 30 PRO CA C 65.6877 0.40 1 332 120 30 PRO CB C 32.5399 0.40 1 333 120 30 PRO CG C 27.5880 0.35 1 334 120 30 PRO CD C 51.5200 0.35 1 335 121 31 THR H H 6.7522 0.01 1 336 121 31 THR HA H 3.6860 0.03 1 337 121 31 THR HB H 4.1740 0.03 1 338 121 31 THR HG2 H 1.1660 0.04 1 339 121 31 THR C C 175.8754 0.09 1 340 121 31 THR CA C 64.2052 0.40 1 341 121 31 THR CB C 67.0474 0.40 1 342 121 31 THR CG2 C 23.0770 0.35 1 343 121 31 THR N N 128.2915 0.05 1 344 122 32 ASP H H 7.4512 0.01 1 345 122 32 ASP HA H 4.5710 0.03 1 346 122 32 ASP HB2 H 2.6630 0.04 2 347 122 32 ASP C C 176.9627 0.09 1 348 122 32 ASP CA C 56.1276 0.40 1 349 122 32 ASP CB C 41.0031 0.40 1 350 122 32 ASP N N 120.4355 0.05 1 351 123 33 ILE H H 6.8873 0.01 1 352 123 33 ILE HA H 4.7670 0.03 1 353 123 33 ILE HB H 1.7610 0.03 1 354 123 33 ILE HG12 H 1.3200 0.04 2 355 123 33 ILE HG13 H 1.3900 0.04 2 356 123 33 ILE HG2 H 0.6700 0.04 1 357 123 33 ILE HD1 H 0.5400 0.04 1 358 123 33 ILE C C 177.1889 0.09 1 359 123 33 ILE CA C 61.2388 0.40 1 360 123 33 ILE CB C 40.6858 0.40 1 361 123 33 ILE CG1 C 27.3360 0.35 1 362 123 33 ILE CG2 C 17.0600 0.35 1 363 123 33 ILE CD1 C 14.0580 0.35 1 364 123 33 ILE N N 111.1755 0.05 1 365 124 34 ILE H H 7.6074 0.01 1 366 124 34 ILE HA H 3.6850 0.03 1 367 124 34 ILE HB H 1.8670 0.03 1 368 124 34 ILE HG12 H 1.1900 0.04 2 369 124 34 ILE HG13 H 1.2400 0.04 2 370 124 34 ILE HG2 H 0.8710 0.04 1 371 124 34 ILE HD1 H 0.7400 0.04 1 372 124 34 ILE C C 177.4228 0.09 1 373 124 34 ILE CA C 64.2640 0.40 1 374 124 34 ILE CB C 37.6979 0.40 1 375 124 34 ILE CD1 C 14.6400 0.35 1 376 124 34 ILE N N 120.5857 0.05 1 377 125 35 SER H H 8.2438 0.01 1 378 125 35 SER HA H 4.1800 0.03 1 379 125 35 SER HB2 H 3.8500 0.04 2 380 125 35 SER C C 176.4901 0.09 1 381 125 35 SER CA C 61.3200 0.40 1 382 125 35 SER CB C 62.4050 0.40 1 383 125 35 SER N N 116.9435 0.05 1 384 126 36 ASP H H 7.6567 0.01 1 385 126 36 ASP HA H 4.7210 0.03 1 386 126 36 ASP HB2 H 2.8760 0.04 2 387 126 36 ASP HB3 H 2.6330 0.04 2 388 126 36 ASP C C 176.7328 0.09 1 389 126 36 ASP CA C 55.5658 0.40 1 390 126 36 ASP CB C 41.2493 0.40 1 391 126 36 ASP N N 119.8055 0.05 1 392 127 37 LEU H H 7.5166 0.01 1 393 127 37 LEU HA H 4.6420 0.03 1 394 127 37 LEU HB2 H 1.6130 0.04 2 395 127 37 LEU HB3 H 1.6700 0.04 2 396 127 37 LEU HG H 1.6720 0.04 1 397 127 37 LEU HD1 H 0.7060 0.04 2 398 127 37 LEU HD2 H 0.7060 0.04 2 399 127 37 LEU C C 177.5212 0.09 1 400 127 37 LEU CA C 53.9619 0.40 1 401 127 37 LEU CB C 41.9128 0.40 1 402 127 37 LEU CG C 26.7480 0.35 1 403 127 37 LEU CD1 C 26.7480 0.35 2 404 127 37 LEU CD2 C 22.4740 0.35 2 405 127 37 LEU N N 119.0068 0.05 1 406 128 38 SER H H 7.5657 0.01 1 407 128 38 SER HA H 3.9940 0.03 1 408 128 38 SER HB2 H 3.9940 0.04 2 409 128 38 SER C C 175.5145 0.09 1 410 128 38 SER CA C 62.1480 0.40 1 411 128 38 SER CB C 63.2487 0.40 1 412 128 38 SER N N 116.2015 0.05 1 413 129 39 GLU H H 8.6377 0.01 1 414 129 39 GLU HA H 4.3910 0.03 1 415 129 39 GLU HB2 H 2.1400 0.04 2 416 129 39 GLU HB3 H 1.8610 0.04 2 417 129 39 GLU HG2 H 2.3150 0.04 2 418 129 39 GLU HG3 H 2.1920 0.04 2 419 129 39 GLU C C 177.5278 0.09 1 420 129 39 GLU CA C 56.9974 0.40 1 421 129 39 GLU CB C 29.1401 0.40 1 422 129 39 GLU CG C 36.5470 0.35 1 423 129 39 GLU N N 118.3562 0.05 1 424 130 40 CYS H H 8.1002 0.01 1 425 130 40 CYS HA H 4.5360 0.03 1 426 130 40 CYS HB2 H 2.9470 0.04 2 427 130 40 CYS HB3 H 2.7950 0.04 2 428 130 40 CYS C C 172.9440 0.09 1 429 130 40 CYS CA C 59.5310 0.40 1 430 130 40 CYS CB C 29.4623 0.40 1 431 130 40 CYS N N 114.8884 0.05 1 432 131 41 LEU H H 7.3720 0.01 1 433 131 41 LEU HA H 4.6860 0.03 1 434 131 41 LEU HB2 H 1.4920 0.04 2 435 131 41 LEU HB3 H 1.4070 0.04 2 436 131 41 LEU HG H 1.4990 0.04 1 437 131 41 LEU HD1 H 0.5940 0.04 2 438 131 41 LEU HD2 H 0.5940 0.04 2 439 131 41 LEU C C 176.2178 0.09 1 440 131 41 LEU CA C 53.5894 0.40 1 441 131 41 LEU CB C 44.7969 0.40 1 442 131 41 LEU CG C 26.5370 0.35 1 443 131 41 LEU CD1 C 26.5370 0.35 2 444 131 41 LEU CD2 C 23.0130 0.35 2 445 131 41 LEU N N 121.4172 0.05 1 446 132 42 ILE H H 8.4452 0.01 1 447 132 42 ILE HA H 4.4890 0.03 1 448 132 42 ILE HB H 1.9980 0.03 1 449 132 42 ILE HG12 H 1.2800 0.04 2 450 132 42 ILE HG2 H 0.9700 0.04 1 451 132 42 ILE HD1 H 0.8847 0.04 1 452 132 42 ILE C C 178.1899 0.09 1 453 132 42 ILE CA C 60.6054 0.40 1 454 132 42 ILE CB C 39.5394 0.40 1 455 132 42 ILE CG1 C 26.3580 0.35 1 456 132 42 ILE CG2 C 17.6080 0.35 1 457 132 42 ILE CD1 C 12.9860 0.35 1 458 132 42 ILE N N 116.8662 0.05 1 459 133 43 ASN H H 9.0445 0.01 1 460 133 43 ASN HA H 4.2400 0.03 1 461 133 43 ASN HB2 H 2.8280 0.04 2 462 133 43 ASN HB3 H 2.7500 0.04 2 463 133 43 ASN C C 177.2228 0.09 1 464 133 43 ASN CA C 57.6794 0.40 1 465 133 43 ASN CB C 38.0652 0.40 1 466 133 43 ASN N N 123.7892 0.05 1 467 134 44 GLN H H 8.8326 0.01 1 468 134 44 GLN HA H 4.0970 0.03 1 469 134 44 GLN HB2 H 2.0030 0.04 2 470 134 44 GLN HG2 H 2.3740 0.04 2 471 134 44 GLN C C 178.2595 0.09 1 472 134 44 GLN CA C 58.8972 0.40 1 473 134 44 GLN CB C 28.4809 0.40 1 474 134 44 GLN CG C 34.2000 0.35 1 475 134 44 GLN N N 118.3680 0.05 1 476 135 45 GLU H H 7.2569 0.01 1 477 135 45 GLU HA H 4.0360 0.03 1 478 135 45 GLU HB2 H 2.3280 0.04 2 479 135 45 GLU HB3 H 2.0070 0.04 2 480 135 45 GLU HG2 H 2.2550 0.04 2 481 135 45 GLU HG3 H 2.3200 0.04 2 482 135 45 GLU C C 178.5911 0.09 1 483 135 45 GLU CA C 59.1817 0.40 1 484 135 45 GLU CB C 29.7143 0.40 1 485 135 45 GLU CG C 37.8150 0.35 1 486 135 45 GLU N N 118.5590 0.05 1 487 136 46 CYS H H 7.8330 0.01 1 488 136 46 CYS HA H 3.7820 0.03 1 489 136 46 CYS HB2 H 3.0980 0.04 2 490 136 46 CYS HB3 H 2.6620 0.04 2 491 136 46 CYS C C 176.2497 0.09 1 492 136 46 CYS CA C 63.9020 0.40 1 493 136 46 CYS CB C 26.3848 0.40 1 494 136 46 CYS N N 117.6492 0.05 1 495 137 47 GLU H H 8.1148 0.01 1 496 137 47 GLU HA H 3.8300 0.03 1 497 137 47 GLU HB2 H 1.9510 0.04 2 498 137 47 GLU HG2 H 2.2760 0.04 2 499 137 47 GLU HG3 H 2.1660 0.04 2 500 137 47 GLU C C 179.2121 0.09 1 501 137 47 GLU CA C 59.5820 0.40 1 502 137 47 GLU CB C 29.2659 0.40 1 503 137 47 GLU CG C 36.5360 0.35 1 504 137 47 GLU N N 117.7599 0.05 1 505 138 48 GLU H H 7.9412 0.01 1 506 138 48 GLU HA H 3.9770 0.03 1 507 138 48 GLU HB2 H 2.0900 0.04 2 508 138 48 GLU HB3 H 1.9840 0.04 2 509 138 48 GLU HG2 H 2.3600 0.04 2 510 138 48 GLU C C 179.0252 0.09 1 511 138 48 GLU CA C 59.7528 0.40 1 512 138 48 GLU CB C 29.7257 0.40 1 513 138 48 GLU CG C 36.4400 0.35 1 514 138 48 GLU N N 121.0882 0.05 1 515 139 49 ILE H H 8.3513 0.01 1 516 139 49 ILE HA H 3.3420 0.03 1 517 139 49 ILE HB H 1.8200 0.03 1 518 139 49 ILE HG12 H 0.8000 0.04 2 519 139 49 ILE HG13 H 1.0700 0.04 2 520 139 49 ILE HG2 H 0.6610 0.04 1 521 139 49 ILE HD1 H 0.7690 0.04 1 522 139 49 ILE C C 178.4871 0.09 1 523 139 49 ILE CA C 66.3944 0.40 1 524 139 49 ILE CB C 38.6564 0.40 1 525 139 49 ILE CG2 C 18.1370 0.35 1 526 139 49 ILE CD1 C 13.7700 0.35 1 527 139 49 ILE N N 119.5407 0.05 1 528 140 50 LEU H H 8.1709 0.01 1 529 140 50 LEU HA H 3.8320 0.03 1 530 140 50 LEU HB2 H 1.8250 0.04 2 531 140 50 LEU HB3 H 1.4350 0.04 2 532 140 50 LEU HG H 1.7770 0.04 1 533 140 50 LEU HD1 H 0.7840 0.04 2 534 140 50 LEU HD2 H 0.7840 0.04 2 535 140 50 LEU C C 179.8190 0.09 1 536 140 50 LEU CA C 58.7885 0.40 1 537 140 50 LEU CB C 41.0686 0.40 1 538 140 50 LEU CG C 26.6310 0.35 1 539 140 50 LEU CD1 C 24.5810 0.35 2 540 140 50 LEU CD2 C 23.6060 0.35 2 541 140 50 LEU N N 120.5964 0.05 1 542 141 51 GLN H H 8.2348 0.01 1 543 141 51 GLN HA H 4.0450 0.03 1 544 141 51 GLN HB2 H 2.1540 0.04 2 545 141 51 GLN HG2 H 2.3730 0.04 2 546 141 51 GLN HG3 H 2.4400 0.04 2 547 141 51 GLN C C 179.7721 0.09 1 548 141 51 GLN CA C 59.1598 0.40 1 549 141 51 GLN CB C 27.6421 0.40 1 550 141 51 GLN CG C 33.4140 0.35 1 551 141 51 GLN N N 121.4268 0.05 1 552 142 52 ILE H H 8.4988 0.01 1 553 142 52 ILE HA H 3.6110 0.03 1 554 142 52 ILE HB H 1.8640 0.03 1 555 142 52 ILE HG12 H 1.0800 0.04 2 556 142 52 ILE HG2 H 0.7600 0.04 1 557 142 52 ILE HD1 H 0.7600 0.04 1 558 142 52 ILE C C 178.8161 0.09 1 559 142 52 ILE CA C 65.2960 0.40 1 560 142 52 ILE CB C 38.0026 0.40 1 561 142 52 ILE CG1 C 29.1000 0.35 1 562 142 52 ILE CG2 C 17.5870 0.35 1 563 142 52 ILE N N 122.9648 0.05 1 564 143 53 CYS H H 8.5620 0.01 1 565 143 53 CYS HA H 4.0970 0.03 1 566 143 53 CYS HB2 H 3.1870 0.04 2 567 143 53 CYS HB3 H 2.8150 0.04 2 568 143 53 CYS C C 177.0165 0.09 1 569 143 53 CYS CA C 63.8416 0.40 1 570 143 53 CYS CB C 27.0738 0.40 1 571 143 53 CYS N N 118.8043 0.05 1 572 144 54 SER H H 7.6634 0.01 1 573 144 54 SER HA H 4.1960 0.03 1 574 144 54 SER HB2 H 3.9460 0.04 2 575 144 54 SER HB3 H 3.9600 0.04 2 576 144 54 SER C C 175.1121 0.09 1 577 144 54 SER CA C 60.9566 0.40 1 578 144 54 SER CB C 63.7021 0.40 1 579 144 54 SER N N 111.7616 0.05 1 580 145 55 THR H H 7.8782 0.01 1 581 145 55 THR HA H 4.3480 0.03 1 582 145 55 THR HB H 4.0960 0.03 1 583 145 55 THR HG2 H 1.2280 0.04 1 584 145 55 THR C C 175.8442 0.09 1 585 145 55 THR CA C 63.3913 0.40 1 586 145 55 THR CB C 70.3493 0.40 1 587 145 55 THR CG2 C 22.3430 0.35 1 588 145 55 THR N N 110.9687 0.05 1 589 146 56 LYS H H 8.8986 0.01 1 590 146 56 LYS HA H 4.5110 0.03 1 591 146 56 LYS HB2 H 1.8190 0.04 2 592 146 56 LYS HB3 H 1.7120 0.04 2 593 146 56 LYS HG2 H 1.3960 0.04 2 594 146 56 LYS HG3 H 1.5200 0.04 2 595 146 56 LYS HD2 H 1.6050 0.04 2 596 146 56 LYS HD3 H 1.5450 0.04 2 597 146 56 LYS HE2 H 2.9220 0.04 2 598 146 56 LYS C C 177.3980 0.09 1 599 146 56 LYS CA C 56.0746 0.40 1 600 146 56 LYS CB C 34.6074 0.40 1 601 146 56 LYS CG C 24.9340 0.35 1 602 146 56 LYS N N 121.5193 0.05 1 603 147 57 GLY H H 7.5400 0.01 1 604 147 57 GLY HA2 H 4.6660 0.04 2 605 147 57 GLY HA3 H 3.9700 0.04 2 606 147 57 GLY C C 174.3340 0.09 1 607 147 57 GLY CA C 44.7122 0.40 1 608 147 57 GLY N N 109.2144 0.05 1 609 148 58 MET H H 8.5992 0.01 1 610 148 58 MET HA H 4.2590 0.03 1 611 148 58 MET HB2 H 2.2160 0.04 2 612 148 58 MET HB3 H 1.9890 0.04 2 613 148 58 MET HG2 H 2.8560 0.04 2 614 148 58 MET HG3 H 2.8400 0.04 2 615 148 58 MET HE H 2.0400 0.04 1 616 148 58 MET C C 178.3333 0.09 1 617 148 58 MET CA C 58.1259 0.40 1 618 148 58 MET CB C 32.2762 0.40 1 619 148 58 MET CG C 33.4850 0.35 1 620 148 58 MET CE C 18.4800 0.35 1 621 148 58 MET N N 116.7954 0.05 1 622 149 59 MET H H 8.3529 0.01 1 623 149 59 MET HA H 4.2770 0.03 1 624 149 59 MET HB2 H 2.0800 0.04 2 625 149 59 MET HB3 H 1.8880 0.04 2 626 149 59 MET HG2 H 2.5920 0.04 2 627 149 59 MET HG3 H 2.5300 0.04 2 628 149 59 MET HE H 2.0500 0.04 1 629 149 59 MET C C 178.4221 0.09 1 630 149 59 MET CA C 59.7172 0.40 1 631 149 59 MET CB C 32.3281 0.40 1 632 149 59 MET CG C 32.0790 0.35 1 633 149 59 MET CE C 16.9500 0.35 1 634 149 59 MET N N 118.9043 0.05 1 635 150 60 ALA H H 8.0324 0.01 1 636 150 60 ALA HA H 4.1380 0.03 1 637 150 60 ALA HB H 1.2080 0.04 1 638 150 60 ALA C C 182.0974 0.09 1 639 150 60 ALA CA C 54.5848 0.40 1 640 150 60 ALA CB C 18.4486 0.40 1 641 150 60 ALA N N 122.2075 0.05 1 642 151 61 GLY H H 8.3164 0.01 1 643 151 61 GLY HA2 H 4.3040 0.04 2 644 151 61 GLY HA3 H 3.5210 0.04 2 645 151 61 GLY C C 174.9504 0.09 1 646 151 61 GLY CA C 47.7671 0.40 1 647 151 61 GLY N N 108.4879 0.05 1 648 152 62 ALA H H 8.9626 0.01 1 649 152 62 ALA HA H 3.8530 0.03 1 650 152 62 ALA HB H 1.5640 0.04 1 651 152 62 ALA C C 179.2294 0.09 1 652 152 62 ALA CA C 55.6654 0.40 1 653 152 62 ALA CB C 18.4045 0.40 1 654 152 62 ALA N N 126.5892 0.05 1 655 153 63 GLU H H 8.2882 0.01 1 656 153 63 GLU HA H 3.7500 0.03 1 657 153 63 GLU HB2 H 2.0760 0.04 2 658 153 63 GLU HG2 H 2.3930 0.04 2 659 153 63 GLU HG3 H 2.0760 0.04 2 660 153 63 GLU C C 178.8249 0.09 1 661 153 63 GLU CA C 60.1374 0.40 1 662 153 63 GLU CB C 29.7467 0.40 1 663 153 63 GLU CG C 37.4380 0.35 1 664 153 63 GLU N N 118.1969 0.05 1 665 154 64 LYS H H 7.6157 0.01 1 666 154 64 LYS HA H 4.1740 0.03 1 667 154 64 LYS HB2 H 1.7970 0.04 2 668 154 64 LYS HG2 H 1.5130 0.04 2 669 154 64 LYS HG3 H 1.2060 0.04 2 670 154 64 LYS HD2 H 1.8120 0.04 2 671 154 64 LYS HD3 H 1.5700 0.04 2 672 154 64 LYS HE2 H 2.5200 0.04 2 673 154 64 LYS HE3 H 2.7200 0.04 2 674 154 64 LYS C C 177.7816 0.09 1 675 154 64 LYS CA C 56.9292 0.40 1 676 154 64 LYS CB C 30.2816 0.40 1 677 154 64 LYS CG C 24.8140 0.35 1 678 154 64 LYS CD C 27.6390 0.35 1 679 154 64 LYS CE C 41.6900 0.35 1 680 154 64 LYS N N 120.3648 0.05 1 681 155 65 LEU H H 8.2789 0.01 1 682 155 65 LEU HA H 3.8620 0.03 1 683 155 65 LEU HB2 H 2.2600 0.04 2 684 155 65 LEU HB3 H 1.2840 0.04 2 685 155 65 LEU HG H 1.2900 0.04 1 686 155 65 LEU HD1 H 0.7470 0.04 2 687 155 65 LEU HD2 H 0.7470 0.04 2 688 155 65 LEU C C 177.3885 0.09 1 689 155 65 LEU CA C 58.5964 0.40 1 690 155 65 LEU CB C 41.1442 0.40 1 691 155 65 LEU CG C 26.2630 0.35 1 692 155 65 LEU CD1 C 26.2630 0.35 2 693 155 65 LEU CD2 C 23.7610 0.35 2 694 155 65 LEU N N 121.8275 0.05 1 695 156 66 VAL H H 7.9203 0.01 1 696 156 66 VAL HA H 2.8180 0.03 1 697 156 66 VAL HB H 1.9850 0.03 1 698 156 66 VAL HG1 H 0.5700 0.04 2 699 156 66 VAL HG2 H 0.2980 0.04 2 700 156 66 VAL C C 176.5240 0.09 1 701 156 66 VAL CA C 67.3213 0.40 1 702 156 66 VAL CB C 30.8933 0.40 1 703 156 66 VAL CG1 C 20.7100 0.35 2 704 156 66 VAL CG2 C 23.9800 0.35 2 705 156 66 VAL N N 118.7528 0.05 1 706 157 67 GLU H H 7.4680 0.01 1 707 157 67 GLU HA H 3.6900 0.03 1 708 157 67 GLU HB2 H 2.1580 0.04 2 709 157 67 GLU HG2 H 2.3500 0.04 2 710 157 67 GLU HG3 H 2.0290 0.04 2 711 157 67 GLU C C 179.3917 0.09 1 712 157 67 GLU CA C 59.9321 0.40 1 713 157 67 GLU CB C 29.4008 0.40 1 714 157 67 GLU CG C 36.2510 0.35 1 715 157 67 GLU N N 118.6443 0.05 1 716 158 68 CYS H H 8.0369 0.01 1 717 158 68 CYS HA H 3.8420 0.03 1 718 158 68 CYS HB2 H 2.7550 0.04 2 719 158 68 CYS HB3 H 2.6320 0.04 2 720 158 68 CYS C C 177.6978 0.09 1 721 158 68 CYS CA C 63.5761 0.40 1 722 158 68 CYS CB C 27.1778 0.40 1 723 158 68 CYS N N 116.1034 0.05 1 724 159 69 LEU H H 7.9841 0.01 1 725 159 69 LEU HA H 3.1380 0.03 1 726 159 69 LEU HB2 H 1.0320 0.04 2 727 159 69 LEU HB3 H -0.6360 0.04 2 728 159 69 LEU HG H 1.3520 0.04 1 729 159 69 LEU HD1 H 0.8710 0.04 2 730 159 69 LEU HD2 H 0.2960 0.04 2 731 159 69 LEU C C 178.4606 0.09 1 732 159 69 LEU CA C 57.3468 0.40 1 733 159 69 LEU CB C 39.5397 0.40 1 734 159 69 LEU CG C 25.4150 0.35 1 735 159 69 LEU CD1 C 25.4150 0.35 2 736 159 69 LEU CD2 C 25.4150 0.35 2 737 159 69 LEU N N 121.3827 0.05 1 738 160 70 LEU H H 8.2588 0.01 1 739 160 70 LEU HA H 3.7460 0.03 1 740 160 70 LEU HB2 H 1.7780 0.04 2 741 160 70 LEU HB3 H 1.3150 0.04 2 742 160 70 LEU HG H 1.7920 0.04 1 743 160 70 LEU HD1 H 0.7220 0.04 2 744 160 70 LEU HD2 H 0.9420 0.04 2 745 160 70 LEU C C 178.2220 0.09 1 746 160 70 LEU CA C 57.9147 0.40 1 747 160 70 LEU CB C 41.5079 0.40 1 748 160 70 LEU CG C 26.2210 0.35 1 749 160 70 LEU CD1 C 26.2210 0.35 2 750 160 70 LEU CD2 C 24.4450 0.35 2 751 160 70 LEU N N 117.0628 0.05 1 752 161 71 ARG H H 7.0047 0.01 1 753 161 71 ARG HA H 4.3150 0.03 1 754 161 71 ARG HB2 H 1.7400 0.04 2 755 161 71 ARG HB3 H 1.8200 0.04 2 756 161 71 ARG HG2 H 1.7000 0.04 2 757 161 71 ARG HD2 H 3.0890 0.04 2 758 161 71 ARG C C 176.2886 0.09 1 759 161 71 ARG CA C 55.7777 0.40 1 760 161 71 ARG CB C 31.1082 0.40 1 761 161 71 ARG CG C 27.3290 0.35 1 762 161 71 ARG N N 113.7379 0.05 1 763 162 72 SER H H 6.9796 0.01 1 764 162 72 SER HA H 4.1660 0.03 1 765 162 72 SER HB2 H 3.8250 0.04 2 766 162 72 SER HB3 H 3.6800 0.04 2 767 162 72 SER C C 176.2262 0.09 1 768 162 72 SER CA C 59.2025 0.40 1 769 162 72 SER CB C 63.4003 0.40 1 770 162 72 SER N N 114.6052 0.05 1 771 163 73 ASP H H 8.7993 0.01 1 772 163 73 ASP HA H 4.8020 0.03 1 773 163 73 ASP HB2 H 2.8270 0.04 2 774 163 73 ASP HB3 H 2.7100 0.04 2 775 163 73 ASP C C 176.0201 0.09 1 776 163 73 ASP CA C 53.4027 0.40 1 777 163 73 ASP CB C 40.9417 0.40 1 778 163 73 ASP N N 127.4927 0.05 1 779 164 74 LYS H H 8.4575 0.01 1 780 164 74 LYS HA H 4.3930 0.03 1 781 164 74 LYS HB2 H 2.0840 0.04 2 782 164 74 LYS HB3 H 2.1700 0.04 2 783 164 74 LYS HG2 H 1.5430 0.04 2 784 164 74 LYS HG3 H 1.6450 0.04 2 785 164 74 LYS HD2 H 1.7390 0.04 2 786 164 74 LYS C C 176.6802 0.09 1 787 164 74 LYS CA C 55.6751 0.40 1 788 164 74 LYS CB C 31.1570 0.40 1 789 164 74 LYS CG C 24.4840 0.35 1 790 164 74 LYS CD C 29.7740 0.35 1 791 164 74 LYS CE C 43.5780 0.35 1 792 164 74 LYS N N 121.9391 0.05 1 793 165 75 GLU H H 8.7464 0.01 1 794 165 75 GLU HA H 3.9420 0.03 1 795 165 75 GLU HB2 H 2.0430 0.04 2 796 165 75 GLU HG2 H 2.3010 0.04 2 797 165 75 GLU C C 175.2265 0.09 1 798 165 75 GLU CA C 58.7050 0.40 1 799 165 75 GLU CB C 29.7231 0.40 1 800 165 75 GLU CG C 36.0470 0.35 1 801 165 75 GLU N N 123.5916 0.05 1 802 166 76 ASN H H 8.5835 0.01 1 803 166 76 ASN HA H 4.7930 0.03 1 804 166 76 ASN HB2 H 2.9190 0.04 2 805 166 76 ASN HB3 H 2.8330 0.04 2 806 166 76 ASN C C 176.7689 0.09 1 807 166 76 ASN CA C 52.6875 0.40 1 808 166 76 ASN CB C 38.1632 0.40 1 809 166 76 ASN N N 112.4693 0.05 1 810 167 77 TRP H H 8.0718 0.01 1 811 167 77 TRP HA H 4.5700 0.03 1 812 167 77 TRP HB2 H 3.6000 0.04 2 813 167 77 TRP HB3 H 3.2500 0.04 2 814 167 77 TRP HD1 H 7.9688 0.04 1 815 167 77 TRP HE1 H 10.4800 0.04 1 816 167 77 TRP HZ2 H 7.1500 0.04 1 817 167 77 TRP HH2 H 7.1700 0.04 1 818 167 77 TRP CA C 62.1280 0.40 1 819 167 77 TRP CB C 28.8562 0.40 1 820 167 77 TRP CD1 C 130.3528 0.35 1 821 167 77 TRP CZ2 C 113.5506 0.35 1 822 167 77 TRP N N 122.6915 0.05 1 823 167 77 TRP NE1 N 133.5030 0.05 1 824 168 78 PRO HA H 3.9900 0.03 1 825 168 78 PRO HB2 H 0.9590 0.04 2 826 168 78 PRO HB3 H 0.8760 0.04 2 827 168 78 PRO HG2 H -0.6000 0.04 2 828 168 78 PRO HD2 H 2.9100 0.04 2 829 168 78 PRO HD3 H 2.1580 0.04 2 830 168 78 PRO C C 179.5633 0.09 1 831 168 78 PRO CA C 66.8755 0.40 1 832 168 78 PRO CB C 30.4750 0.40 1 833 168 78 PRO CG C 27.3150 0.35 1 834 168 78 PRO CD C 49.6570 0.35 1 835 169 79 LYS H H 7.2264 0.01 1 836 169 79 LYS HA H 3.9510 0.03 1 837 169 79 LYS HB2 H 1.8070 0.04 2 838 169 79 LYS HB3 H 1.8500 0.04 2 839 169 79 LYS HG2 H 1.6160 0.04 2 840 169 79 LYS HG3 H 1.3350 0.04 2 841 169 79 LYS HD2 H 1.8150 0.04 2 842 169 79 LYS HE2 H 2.8760 0.04 2 843 169 79 LYS C C 178.1697 0.09 1 844 169 79 LYS CA C 58.7360 0.40 1 845 169 79 LYS CB C 32.3176 0.40 1 846 169 79 LYS CG C 24.9660 0.35 1 847 169 79 LYS CD C 30.0480 0.35 1 848 169 79 LYS CE C 41.7300 0.35 1 849 169 79 LYS N N 117.9802 0.05 1 850 170 80 GLU H H 8.3483 0.01 1 851 170 80 GLU HA H 4.1010 0.03 1 852 170 80 GLU HB2 H 2.0870 0.04 2 853 170 80 GLU HB3 H 1.9690 0.04 2 854 170 80 GLU HG2 H 2.2660 0.04 2 855 170 80 GLU HG3 H 2.1280 0.04 2 856 170 80 GLU C C 180.2040 0.09 1 857 170 80 GLU CA C 59.0980 0.40 1 858 170 80 GLU CB C 29.2172 0.40 1 859 170 80 GLU CG C 35.9860 0.35 1 860 170 80 GLU N N 120.5329 0.05 1 861 171 81 LEU H H 9.0956 0.01 1 862 171 81 LEU HA H 4.0860 0.03 1 863 171 81 LEU HB2 H 2.1330 0.04 2 864 171 81 LEU HB3 H 1.4740 0.04 2 865 171 81 LEU HG H 1.1410 0.04 1 866 171 81 LEU HD1 H 0.1320 0.04 2 867 171 81 LEU HD2 H 0.7130 0.04 2 868 171 81 LEU C C 177.5085 0.09 1 869 171 81 LEU CA C 58.2543 0.40 1 870 171 81 LEU CB C 41.5567 0.40 1 871 171 81 LEU CG C 27.4510 0.35 1 872 171 81 LEU CD1 C 24.6650 0.35 2 873 171 81 LEU CD2 C 23.0770 0.35 2 874 171 81 LEU N N 119.7569 0.05 1 875 172 82 LYS H H 7.6994 0.01 1 876 172 82 LYS HA H 4.1320 0.03 1 877 172 82 LYS HB2 H 2.4750 0.04 2 878 172 82 LYS HB3 H 2.0080 0.04 2 879 172 82 LYS HG2 H 1.5100 0.04 2 880 172 82 LYS HD2 H 1.6000 0.04 2 881 172 82 LYS C C 177.4831 0.09 1 882 172 82 LYS CA C 59.2120 0.40 1 883 172 82 LYS CB C 32.8734 0.40 1 884 172 82 LYS CG C 23.9140 0.35 1 885 172 82 LYS N N 118.6872 0.05 1 886 173 83 LEU H H 8.3408 0.01 1 887 173 83 LEU HA H 4.0150 0.03 1 888 173 83 LEU HB2 H 1.8850 0.04 2 889 173 83 LEU HB3 H 1.5320 0.04 2 890 173 83 LEU HG H 1.8890 0.04 1 891 173 83 LEU HD1 H 0.8800 0.04 2 892 173 83 LEU HD2 H 0.8800 0.04 2 893 173 83 LEU C C 179.9781 0.09 1 894 173 83 LEU CA C 58.0843 0.40 1 895 173 83 LEU CB C 41.5100 0.40 1 896 173 83 LEU CG C 26.9050 0.35 1 897 173 83 LEU CD1 C 25.0640 0.35 2 898 173 83 LEU CD2 C 22.9540 0.35 2 899 173 83 LEU N N 117.6168 0.05 1 900 174 84 ALA H H 8.1256 0.01 1 901 174 84 ALA HA H 4.0830 0.03 1 902 174 84 ALA HB H 1.5080 0.04 1 903 174 84 ALA C C 179.7340 0.09 1 904 174 84 ALA CA C 55.2979 0.40 1 905 174 84 ALA CB C 18.7693 0.40 1 906 174 84 ALA N N 122.8049 0.05 1 907 175 85 LEU H H 8.3975 0.01 1 908 175 85 LEU HA H 3.9160 0.03 1 909 175 85 LEU HB2 H 2.2720 0.04 2 910 175 85 LEU HB3 H 1.4030 0.04 2 911 175 85 LEU HG H 2.1400 0.04 1 912 175 85 LEU HD1 H 0.8600 0.04 2 913 175 85 LEU HD2 H 0.7100 0.04 2 914 175 85 LEU C C 179.5480 0.09 1 915 175 85 LEU CA C 57.4320 0.40 1 916 175 85 LEU CB C 42.0079 0.40 1 917 175 85 LEU CD1 C 28.0200 0.35 2 918 175 85 LEU N N 116.7029 0.05 1 919 176 86 GLU H H 8.4630 0.01 1 920 176 86 GLU HA H 4.0790 0.03 1 921 176 86 GLU HB2 H 2.1620 0.04 2 922 176 86 GLU HB3 H 2.0520 0.04 2 923 176 86 GLU HG2 H 2.4760 0.04 2 924 176 86 GLU HG3 H 2.2730 0.04 2 925 176 86 GLU C C 180.3784 0.09 1 926 176 86 GLU CA C 58.8582 0.40 1 927 176 86 GLU CB C 30.0699 0.40 1 928 176 86 GLU CG C 36.7770 0.35 1 929 176 86 GLU N N 118.3978 0.05 1 930 177 87 LYS H H 8.2705 0.01 1 931 177 87 LYS HA H 4.0000 0.03 1 932 177 87 LYS HB2 H 1.9630 0.04 2 933 177 87 LYS HG2 H 1.3980 0.04 2 934 177 87 LYS HG3 H 1.5520 0.04 2 935 177 87 LYS HD2 H 1.7190 0.04 2 936 177 87 LYS HE2 H 3.1070 0.04 2 937 177 87 LYS HE3 H 2.9200 0.04 2 938 177 87 LYS C C 178.1929 0.09 1 939 177 87 LYS CA C 59.5418 0.40 1 940 177 87 LYS CB C 32.2644 0.40 1 941 177 87 LYS CG C 24.6230 0.35 1 942 177 87 LYS CE C 42.3400 0.35 1 943 177 87 LYS N N 122.5300 0.05 1 944 178 88 GLU H H 7.4744 0.01 1 945 178 88 GLU HA H 4.3400 0.03 1 946 178 88 GLU HB2 H 2.2600 0.04 2 947 178 88 GLU HB3 H 1.8060 0.04 2 948 178 88 GLU HG2 H 2.5300 0.04 2 949 178 88 GLU HG3 H 2.4900 0.04 2 950 178 88 GLU C C 175.4290 0.09 1 951 178 88 GLU CA C 55.0739 0.40 1 952 178 88 GLU CB C 29.0672 0.40 1 953 178 88 GLU CG C 34.5900 0.35 1 954 178 88 GLU N N 114.4480 0.05 1 955 179 89 ARG H H 7.9006 0.01 1 956 179 89 ARG HA H 3.8710 0.03 1 957 179 89 ARG HB2 H 1.8850 0.04 2 958 179 89 ARG HB3 H 2.0080 0.04 2 959 179 89 ARG HG2 H 1.5720 0.04 2 960 179 89 ARG HD2 H 3.2130 0.04 2 961 179 89 ARG C C 175.6252 0.09 1 962 179 89 ARG CA C 56.7866 0.40 1 963 179 89 ARG CB C 26.8388 0.40 1 964 179 89 ARG CG C 27.1100 0.35 1 965 179 89 ARG CD C 43.5900 0.35 1 966 179 89 ARG N N 118.3881 0.05 1 967 180 90 ASN H H 8.3148 0.01 1 968 180 90 ASN HA H 4.6330 0.03 1 969 180 90 ASN HB2 H 2.6850 0.04 2 970 180 90 ASN HB3 H 2.5630 0.04 2 971 180 90 ASN C C 178.1260 0.09 1 972 180 90 ASN CA C 54.0106 0.40 1 973 180 90 ASN N N 117.7612 0.05 1 974 181 91 LYS H H 9.2741 0.01 1 975 181 91 LYS HA H 4.1280 0.03 1 976 181 91 LYS HB2 H 1.8150 0.04 2 977 181 91 LYS HG2 H 1.5520 0.04 2 978 181 91 LYS HD2 H 1.6450 0.04 2 979 181 91 LYS HE2 H 2.9930 0.04 2 980 181 91 LYS C C 178.3058 0.09 1 981 181 91 LYS CA C 58.6875 0.40 1 982 181 91 LYS CB C 32.3676 0.40 1 983 181 91 LYS CG C 25.3450 0.35 1 984 181 91 LYS N N 129.4783 0.05 1 985 182 92 PHE H H 9.7393 0.01 1 986 182 92 PHE HA H 4.0650 0.03 1 987 182 92 PHE HB2 H 2.8100 0.04 2 988 182 92 PHE HB3 H 2.6850 0.04 2 989 182 92 PHE HD1 H 6.9747 0.04 3 990 182 92 PHE HE1 H 7.2000 0.04 3 991 182 92 PHE C C 176.5408 0.09 1 992 182 92 PHE CA C 61.0618 0.40 1 993 182 92 PHE CB C 39.5130 0.40 1 994 182 92 PHE CD1 C 132.4022 0.35 3 995 182 92 PHE CE1 C 130.4997 0.35 3 996 182 92 PHE N N 121.8967 0.05 1 997 183 93 SER H H 8.3669 0.01 1 998 183 93 SER HA H 3.9660 0.03 1 999 183 93 SER HB2 H 3.9660 0.04 2 1000 183 93 SER C C 176.5230 0.09 1 1001 183 93 SER CA C 61.5070 0.40 1 1002 183 93 SER CB C 63.5494 0.40 1 1003 183 93 SER N N 110.8135 0.05 1 1004 184 94 GLU H H 7.4179 0.01 1 1005 184 94 GLU HA H 3.9120 0.03 1 1006 184 94 GLU HB2 H 1.9400 0.04 2 1007 184 94 GLU HG2 H 2.2600 0.04 2 1008 184 94 GLU C C 177.2256 0.09 1 1009 184 94 GLU CA C 58.2548 0.40 1 1010 184 94 GLU CB C 29.5464 0.40 1 1011 184 94 GLU CG C 36.2100 0.35 1 1012 184 94 GLU N N 114.9185 0.05 1 1013 185 95 LEU H H 7.2308 0.01 1 1014 185 95 LEU HA H 4.1610 0.03 1 1015 185 95 LEU HB2 H 1.3810 0.04 2 1016 185 95 LEU HB3 H 1.0600 0.04 2 1017 185 95 LEU HG H 1.4360 0.04 1 1018 185 95 LEU HD1 H 0.7810 0.04 2 1019 185 95 LEU HD2 H 0.7810 0.04 2 1020 185 95 LEU C C 175.9456 0.09 1 1021 185 95 LEU CA C 54.2956 0.40 1 1022 185 95 LEU CB C 42.4015 0.40 1 1023 185 95 LEU CG C 25.8110 0.35 1 1024 185 95 LEU CD1 C 25.2870 0.35 2 1025 185 95 LEU CD2 C 22.2840 0.35 2 1026 185 95 LEU N N 115.4386 0.05 1 1027 186 96 TRP H H 7.3054 0.01 1 1028 186 96 TRP HA H 4.6440 0.03 1 1029 186 96 TRP HB2 H 3.2480 0.04 2 1030 186 96 TRP HB3 H 2.6720 0.04 2 1031 186 96 TRP HD1 H 6.8000 0.04 1 1032 186 96 TRP HE1 H 9.9700 0.04 1 1033 186 96 TRP HZ2 H 7.0430 0.04 1 1034 186 96 TRP HZ3 H 7.2597 0.04 1 1035 186 96 TRP HH2 H 7.8238 0.04 1 1036 186 96 TRP C C 172.5687 0.09 1 1037 186 96 TRP CA C 54.5336 0.40 1 1038 186 96 TRP CB C 29.4528 0.40 1 1039 186 96 TRP CD1 C 125.2318 0.35 1 1040 186 96 TRP CZ2 C 114.7838 0.35 1 1041 186 96 TRP CZ3 C 124.8481 0.35 1 1042 186 96 TRP CH2 C 124.9343 0.35 1 1043 186 96 TRP N N 121.8884 0.05 1 1044 186 96 TRP NE1 N 126.2500 0.05 1 1045 187 97 ILE H H 6.6411 0.01 1 1046 187 97 ILE HA H 3.9410 0.03 1 1047 187 97 ILE HB H 1.5790 0.03 1 1048 187 97 ILE HG12 H 1.2000 0.04 2 1049 187 97 ILE HG13 H 0.9700 0.04 2 1050 187 97 ILE HG2 H 0.6780 0.04 1 1051 187 97 ILE HD1 H 0.6780 0.04 1 1052 187 97 ILE C C 174.7208 0.09 1 1053 187 97 ILE CA C 59.9243 0.40 1 1054 187 97 ILE CB C 37.5867 0.40 1 1055 187 97 ILE CG1 C 27.4240 0.35 1 1056 187 97 ILE CG2 C 17.5700 0.35 1 1057 187 97 ILE CD1 C 11.8690 0.35 1 1058 187 97 ILE N N 126.0626 0.05 1 1059 188 98 VAL H H 7.8588 0.01 1 1060 188 98 VAL HA H 4.1630 0.03 1 1061 188 98 VAL HB H 1.6310 0.03 1 1062 188 98 VAL HG1 H 0.2970 0.04 2 1063 188 98 VAL HG2 H 0.3150 0.04 2 1064 188 98 VAL C C 175.2679 0.09 1 1065 188 98 VAL CA C 60.2596 0.40 1 1066 188 98 VAL CB C 33.5025 0.40 1 1067 188 98 VAL CG1 C 20.7910 0.35 2 1068 188 98 VAL CG2 C 19.9130 0.35 2 1069 188 98 VAL N N 123.4869 0.05 1 1070 189 99 GLU H H 7.9334 0.01 1 1071 189 99 GLU HA H 4.1880 0.03 1 1072 189 99 GLU HB2 H 1.9420 0.04 2 1073 189 99 GLU HB3 H 1.8060 0.04 2 1074 189 99 GLU HG2 H 2.1430 0.04 2 1075 189 99 GLU C C 175.1154 0.09 1 1076 189 99 GLU CA C 56.4754 0.40 1 1077 189 99 GLU CB C 30.6433 0.40 1 1078 189 99 GLU CG C 36.1910 0.35 1 1079 189 99 GLU N N 124.7303 0.05 1 1080 190 100 LYS H H 7.9347 0.01 1 1081 190 100 LYS HB2 H 1.6900 0.04 2 1082 190 100 LYS HG2 H 1.3600 0.04 2 1083 190 100 LYS HD2 H 1.6300 0.04 2 1084 190 100 LYS CA C 58.0489 0.40 1 1085 190 100 LYS CB C 33.4854 0.40 1 1086 190 100 LYS N N 127.3422 0.05 1 stop_ save_