data_5393 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific (1H, 15N, 13C) resonance assignment of the N-terminal domain of the Cyclase-associated Protein (CAP) from Dictyostelium discoideum ; _BMRB_accession_number 5393 _BMRB_flat_file_name bmr5393.str _Entry_type original _Submission_date 2002-06-12 _Accession_date 2002-06-13 _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 Rehm Till . . 2 Mavoungou Chrystelle . . 3 Israel Lars . . 4 Schleicher Michael . . 5 Holak Tad A . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 714 "13C chemical shifts" 542 "15N chemical shifts" 173 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-25 original author . stop_ _Original_release_date 2002-09-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific (1H, 15N, 13C) resonance assignment of the N-terminal domain of the Cyclase-associated Protein (CAP) from Dictyostelium discoideum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rehm Till . . 2 Mavoungou Chrystelle . . 3 Israel Lars . . 4 Schleicher Michael . . 5 Holak Tad A . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 337 _Page_last 338 _Year 2002 _Details . loop_ _Keyword 'adenylyl cyclase associated protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_CAP _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of the adenylyl cyclase associated Protein' _Abbreviation_common CAP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CAP N-terminus' $CAP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CAP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cyclase associated Protein' _Abbreviation_common CAP _Molecular_mass . _Mol_thiol_state 'not present' _Details ; The N-terminal domain of CAP described here is shorter by 39 residues than previously reported. ; ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; SVKEFQNLVDQHITPFVALS KKLAPEVGNQVEQLVKAIDA EKALINTASQSKKPSQETLL ELIKPLNNFAAEVGKIRDSN RSSKFFNNLSAISESIGFLS WVVVEPTPGPHVAEMRGSAE FYTNRILKEFKGVNQDQVDW VSNYVNFLKDLEKYIKQYHT TGLTWNPKGGDAKSAT ; loop_ _Residue_seq_code _Residue_label 1 SER 2 VAL 3 LYS 4 GLU 5 PHE 6 GLN 7 ASN 8 LEU 9 VAL 10 ASP 11 GLN 12 HIS 13 ILE 14 THR 15 PRO 16 PHE 17 VAL 18 ALA 19 LEU 20 SER 21 LYS 22 LYS 23 LEU 24 ALA 25 PRO 26 GLU 27 VAL 28 GLY 29 ASN 30 GLN 31 VAL 32 GLU 33 GLN 34 LEU 35 VAL 36 LYS 37 ALA 38 ILE 39 ASP 40 ALA 41 GLU 42 LYS 43 ALA 44 LEU 45 ILE 46 ASN 47 THR 48 ALA 49 SER 50 GLN 51 SER 52 LYS 53 LYS 54 PRO 55 SER 56 GLN 57 GLU 58 THR 59 LEU 60 LEU 61 GLU 62 LEU 63 ILE 64 LYS 65 PRO 66 LEU 67 ASN 68 ASN 69 PHE 70 ALA 71 ALA 72 GLU 73 VAL 74 GLY 75 LYS 76 ILE 77 ARG 78 ASP 79 SER 80 ASN 81 ARG 82 SER 83 SER 84 LYS 85 PHE 86 PHE 87 ASN 88 ASN 89 LEU 90 SER 91 ALA 92 ILE 93 SER 94 GLU 95 SER 96 ILE 97 GLY 98 PHE 99 LEU 100 SER 101 TRP 102 VAL 103 VAL 104 VAL 105 GLU 106 PRO 107 THR 108 PRO 109 GLY 110 PRO 111 HIS 112 VAL 113 ALA 114 GLU 115 MET 116 ARG 117 GLY 118 SER 119 ALA 120 GLU 121 PHE 122 TYR 123 THR 124 ASN 125 ARG 126 ILE 127 LEU 128 LYS 129 GLU 130 PHE 131 LYS 132 GLY 133 VAL 134 ASN 135 GLN 136 ASP 137 GLN 138 VAL 139 ASP 140 TRP 141 VAL 142 SER 143 ASN 144 TYR 145 VAL 146 ASN 147 PHE 148 LEU 149 LYS 150 ASP 151 LEU 152 GLU 153 LYS 154 TYR 155 ILE 156 LYS 157 GLN 158 TYR 159 HIS 160 THR 161 THR 162 GLY 163 LEU 164 THR 165 TRP 166 ASN 167 PRO 168 LYS 169 GLY 170 GLY 171 ASP 172 ALA 173 LYS 174 SER 175 ALA 176 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 1S0P "Structure Of The N-Terminal Domain Of The Adenylyl Cyclase- Associated Protein (Cap) From Dictyostelium Discoideum" 100.00 176 100.00 100.00 1.18e-124 PDB 1TJF "The Crystal Structure Of The N-Terminal Domain Of Cap Indicates Variable Oligomerisation" 100.00 186 100.00 100.00 1.28e-124 GB AAB09713 "cyclase associated protein [Dictyostelium discoideum AX3]" 100.00 464 100.00 100.00 2.81e-123 GB EAL63006 "cyclase associated protein [Dictyostelium discoideum AX4]" 100.00 464 100.00 100.00 2.81e-123 REF XP_636512 "cyclase associated protein [Dictyostelium discoideum AX4]" 100.00 464 100.00 100.00 2.81e-123 SP P54654 "RecName: Full=Adenylyl cyclase-associated protein; Short=CAP [Dictyostelium discoideum]" 100.00 464 100.00 100.00 2.81e-123 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CAP 'Dictyostelium discoideum' 44689 Eukaryota . Dictyostelium discoideum 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 $CAP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CAP . mM 0.8 1.2 [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CAP 0.9 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version . _Details . save_ save_Sparky _Saveframe_category software _Name Sparky _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_13C-1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _Sample_label . save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Exp-cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.3 0.1 n/a temperature 300 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 TSP H 1 methyl ppm 0.00 . direct . . . 1.0 TSP C 13 methyl ppm -0.2 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Exp-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CAP N-terminus' _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 . 3 LYS C C 178.355 0.1 1 2 . 3 LYS CA C 59.337 0.1 1 3 . 3 LYS CB C 28.034 0.3 1 4 . 4 GLU H H 8.034 0.02 1 5 . 4 GLU C C 176.826 0.1 1 6 . 4 GLU CA C 61.952 0.1 1 7 . 4 GLU N N 123.843 0.05 1 8 . 5 PHE H H 8.489 0.02 1 9 . 5 PHE C C 176.00 0.1 1 10 . 5 PHE CA C 58.111 0.1 1 11 . 5 PHE N N 119.60 0.05 1 12 . 6 GLN H H 8.167 0.02 1 13 . 6 GLN C C 178.320 0.1 1 14 . 6 GLN CA C 59.281 0.1 1 15 . 6 GLN CB C 32.00 0.3 1 16 . 6 GLN N N 118.525 0.05 1 17 . 7 ASN H H 8.169 0.02 1 18 . 7 ASN C C 177.530 0.1 1 19 . 7 ASN CA C 56.234 0.1 1 20 . 7 ASN CB C 37.636 0.3 1 21 . 7 ASN N N 118.851 0.05 1 22 . 8 LEU H H 7.354 0.02 1 23 . 8 LEU N N 120.373 0.05 1 24 . 8 LEU C C 178.512 0.1 1 25 . 8 LEU CA C 58.004 0.1 1 26 . 8 LEU CB C 42.148 0.3 1 27 . 9 VAL H H 7.397 0.02 1 28 . 9 VAL HA H 3.389 0.05 1 29 . 9 VAL HB H 2.293 0.05 1 30 . 9 VAL HG1 H 0.889 0.05 2 31 . 9 VAL HG2 H 0.723 0.05 2 32 . 9 VAL C C 178.009 0.1 1 33 . 9 VAL CA C 66.283 0.1 1 34 . 9 VAL CB C 31.320 0.3 1 35 . 9 VAL N N 122.06 0.05 1 36 . 10 ASP H H 8.749 0.02 1 37 . 10 ASP HA H 4.348 0.05 1 38 . 10 ASP HB2 H 2.736 0.05 2 39 . 10 ASP HB3 H 2.692 0.05 2 40 . 10 ASP C C 177.654 0.1 1 41 . 10 ASP CA C 57.309 0.1 1 42 . 10 ASP CB C 40.517 0.3 1 43 . 10 ASP N N 121.254 0.05 1 44 . 11 GLN H H 7.781 0.02 1 45 . 11 GLN HA H 3.881 0.05 1 46 . 11 GLN HB2 H 1.846 0.05 2 47 . 11 GLN HB3 H 1.468 0.05 2 48 . 11 GLN C C 176.592 0.1 1 49 . 11 GLN CA C 58.530 0.1 1 50 . 11 GLN CB C 28.957 0.3 1 51 . 11 GLN N N 116.680 0.05 1 52 . 12 HIS H H 7.480 0.02 1 53 . 12 HIS HA H 4.959 0.05 1 54 . 12 HIS HB2 H 3.359 0.05 2 55 . 12 HIS HB3 H 2.995 0.05 2 56 . 12 HIS C C 176.668 0.1 1 57 . 12 HIS CA C 56.908 0.1 1 58 . 12 HIS CB C 35.027 0.3 1 59 . 12 HIS N N 112.447 0.05 1 60 . 13 ILE H H 8.172 0.02 1 61 . 13 ILE HA H 4.095 0.05 1 62 . 13 ILE HB H 2.694 0.05 1 63 . 13 ILE HG12 H 1.189 0.05 2 64 . 13 ILE HG13 H 0.579 0.05 2 65 . 13 ILE HG2 H 0.838 0.05 1 66 . 13 ILE HD1 H -0.289 0.05 1 67 . 13 ILE C C 177.415 0.1 1 68 . 13 ILE CA C 59.928 0.1 1 69 . 13 ILE CB C 33.81 0.3 1 70 . 13 ILE CG1 C 27.638 0.1 1 71 . 13 ILE CG2 C 17.846 0.1 1 72 . 13 ILE CD1 C 5.715 0.1 1 73 . 13 ILE N N 119.564 0.05 1 74 . 14 THR H H 8.023 0.02 1 75 . 14 THR HA H 4.091 0.02 1 76 . 14 THR HB H 4.516 0.02 1 77 . 14 THR HG2 H 1.281 0.05 1 78 . 14 THR CA C 69.387 0.1 1 79 . 14 THR CB C 66.214 0.1 1 80 . 14 THR CG2 C 22.595 0.1 1 81 . 14 THR N N 119.258 0.05 1 82 . 15 PRO HA H 4.509 0.02 1 83 . 15 PRO HB2 H 2.339 0.02 1 84 . 15 PRO HB3 H 1.938 0.02 1 85 . 15 PRO C C 178.322 0.1 1 86 . 15 PRO CA C 65.484 0.1 1 87 . 15 PRO CB C 30.601 0.3 1 88 . 16 PHE H H 6.969 0.02 1 89 . 16 PHE HA H 4.411 0.05 1 90 . 16 PHE HB2 H 3.487 0.05 2 91 . 16 PHE HB3 H 3.302 0.05 2 92 . 16 PHE HD1 H 6.858 0.05 3 93 . 16 PHE HE1 H 5.755 0.05 3 94 . 16 PHE HZ H 5.949 0.05 1 95 . 16 PHE C C 178.815 0.1 1 96 . 16 PHE CA C 60.711 0.1 1 97 . 16 PHE CB C 40.022 0.3 1 98 . 16 PHE N N 121.835 0.05 1 99 . 17 VAL H H 8.895 0.02 1 100 . 17 VAL HA H 3.395 0.05 1 101 . 17 VAL HB H 2.221 0.05 1 102 . 17 VAL HG1 H 1.078 0.05 2 103 . 17 VAL HG2 H 0.975 0.05 2 104 . 17 VAL C C 176.905 0.1 1 105 . 17 VAL CA C 67.007 0.1 1 106 . 17 VAL CB C 31.664 0.3 1 107 . 17 VAL N N 126.060 0.05 1 108 . 18 ALA H H 6.876 0.02 1 109 . 18 ALA HA H 4.088 0.05 1 110 . 18 ALA HB H 1.517 0.05 1 111 . 18 ALA C C 175.548 0.1 1 112 . 18 ALA CA C 55.363 0.1 1 113 . 18 ALA CB C 17.691 0.3 1 114 . 18 ALA N N 122.452 0.05 1 115 . 19 LEU H H 7.964 0.02 1 116 . 19 LEU HA H 4.045 0.05 1 117 . 19 LEU HB2 H 1.642 0.05 2 118 . 19 LEU HB3 H 2.048 0.05 2 119 . 19 LEU HG H 1.540 0.05 1 120 . 19 LEU HD1 H 1.083 0.05 2 121 . 19 LEU HD2 H 1.167 0.05 2 122 . 19 LEU C C 177.882 0.1 1 123 . 19 LEU CA C 57.692 0.1 1 124 . 19 LEU CB C 43.611 0.3 1 125 . 19 LEU N N 119.362 0.05 1 126 . 20 SER H H 8.084 0.02 1 127 . 20 SER HA H 4.115 0.05 1 128 . 20 SER HB2 H 3.907 0.05 2 129 . 20 SER HB3 H 3.416 0.05 2 130 . 20 SER C C 174.415 0.1 1 131 . 20 SER CA C 63.514 0.1 1 132 . 20 SER N N 116.413 0.05 1 133 . 21 LYS H H 7.487 0.02 1 134 . 21 LYS HA H 3.721 0.05 1 135 . 21 LYS HB2 H 1.840 0.05 2 136 . 21 LYS HB3 H 1.634 0.05 2 137 . 21 LYS HG3 H 1.377 0.05 2 138 . 21 LYS C C 177.538 0.1 1 139 . 21 LYS CA C 58.844 0.1 1 140 . 21 LYS CB C 32.309 0.3 1 141 . 21 LYS N N 117.655 0.05 1 142 . 22 LYS H H 7.210 0.02 1 143 . 22 LYS HA H 3.975 0.05 1 144 . 22 LYS HB2 H 1.904 0.05 2 145 . 22 LYS HB3 H 1.725 0.05 2 146 . 22 LYS HG2 H 1.379 0.05 2 147 . 22 LYS HG3 H 1.523 0.05 2 148 . 22 LYS C C 177.654 0.1 1 149 . 22 LYS CA C 57.947 0.1 1 150 . 22 LYS CB C 32.867 0.3 1 151 . 22 LYS N N 118.722 0.05 1 152 . 23 LEU H H 7.364 0.02 1 153 . 23 LEU HA H 3.799 0.05 1 154 . 23 LEU HB2 H 1.588 0.05 2 155 . 23 LEU HB3 H 1.396 0.05 2 156 . 23 LEU HG H 0.674 0.05 1 157 . 23 LEU HD1 H 0.492 0.05 2 158 . 23 LEU HD2 H 0.139 0.05 2 159 . 23 LEU C C 176.250 0.1 1 160 . 23 LEU CA C 57.366 0.1 1 161 . 23 LEU CB C 41.935 0.3 1 162 . 23 LEU CG C 25.97 0.1 1 163 . 23 LEU CD1 C 22.799 0.1 2 164 . 23 LEU CD2 C 25.302 0.1 2 165 . 23 LEU N N 120.072 0.05 1 166 . 24 ALA H H 6.766 0.02 1 167 . 24 ALA HA H 4.331 0.05 1 168 . 24 ALA HB H 0.579 0.05 1 169 . 24 ALA CA C 50.754 0.1 1 170 . 24 ALA CB C 19.990 0.3 1 171 . 24 ALA N N 115.055 0.05 1 172 . 25 PRO HD2 H 3.766 0.05 2 173 . 25 PRO C C 178.468 0.1 1 174 . 25 PRO CA C 65.067 0.1 1 175 . 25 PRO CB C 31.772 0.3 1 176 . 26 GLU H H 10.698 0.02 1 177 . 26 GLU HA H 4.277 0.05 1 178 . 26 GLU HB2 H 1.789 0.05 2 179 . 26 GLU HB3 H 2.221 0.05 2 180 . 26 GLU HG2 H 2.899 0.05 2 181 . 26 GLU C C 177.504 0.1 1 182 . 26 GLU CA C 58.944 0.1 1 183 . 26 GLU CB C 27.066 0.3 1 184 . 26 GLU N N 118.558 0.05 1 185 . 27 VAL H H 6.476 0.02 1 186 . 27 VAL HA H 3.668 0.05 1 187 . 27 VAL HB H 2.011 0.05 1 188 . 27 VAL HG1 H 0.649 0.05 2 189 . 27 VAL HG2 H 0.949 0.05 2 190 . 27 VAL C C 177.554 0.1 1 191 . 27 VAL CA C 65.354 0.1 1 192 . 27 VAL CB C 30.525 0.3 1 193 . 27 VAL CG1 C 23.468 0.1 2 194 . 27 VAL CG2 C 21.231 0.1 2 195 . 27 VAL N N 121.888 0.05 1 196 . 28 GLY H H 8.016 0.02 1 197 . 28 GLY HA2 H 3.861 0.05 2 198 . 28 GLY HA3 H 3.284 0.05 2 199 . 28 GLY C C 175.662 0.1 1 200 . 28 GLY CA C 47.808 0.1 1 201 . 28 GLY N N 108.085 0.05 1 202 . 29 ASN H H 8.710 0.02 1 203 . 29 ASN HA H 4.501 0.05 1 204 . 29 ASN HB2 H 2.926 0.05 2 205 . 29 ASN HB3 H 2.843 0.05 2 206 . 29 ASN HD21 H 7.557 0.05 2 207 . 29 ASN C C 177.694 0.1 1 208 . 29 ASN CA C 55.678 0.1 1 209 . 29 ASN CB C 38.024 0.3 1 210 . 29 ASN N N 120.106 0.05 1 211 . 29 ASN ND2 N 111.968 0.05 1 212 . 30 GLN H H 7.909 0.02 1 213 . 30 GLN HA H 3.953 0.05 1 214 . 30 GLN HB2 H 2.171 0.05 2 215 . 30 GLN HB3 H 2.617 0.05 2 216 . 30 GLN HG2 H 2.456 0.05 2 217 . 30 GLN C C 178.382 0.1 1 218 . 30 GLN CA C 59.889 0.1 1 219 . 30 GLN CB C 29.376 0.3 1 220 . 30 GLN N N 121.957 0.05 1 221 . 31 VAL H H 8.614 0.02 1 222 . 31 VAL HA H 3.784 0.05 1 223 . 31 VAL HB H 2.180 0.05 1 224 . 31 VAL HG1 H 1.186 0.05 2 225 . 31 VAL HG2 H 0.972 0.05 2 226 . 31 VAL C C 178.242 0.1 1 227 . 31 VAL CA C 66.570 0.1 1 228 . 31 VAL CB C 31.653 0.3 1 229 . 31 VAL CG1 C 24.727 0.1 2 230 . 31 VAL N N 120.492 0.05 1 231 . 32 GLU H H 8.355 0.02 1 232 . 32 GLU HA H 4.491 0.05 1 233 . 32 GLU HB2 H 2.151 0.05 2 234 . 32 GLU HG2 H 2.349 0.05 2 235 . 32 GLU C C 178.990 0.1 1 236 . 32 GLU CA C 60.274 0.1 1 237 . 32 GLU CB C 29.311 0.3 1 238 . 32 GLU N N 122.738 0.05 1 239 . 33 GLN H H 7.154 0.02 1 240 . 33 GLN HA H 4.024 0.05 1 241 . 33 GLN HB2 H 2.261 0.05 2 242 . 33 GLN HG2 H 2.715 0.05 2 243 . 33 GLN HG3 H 2.483 0.05 2 244 . 33 GLN C C 177.396 0.1 1 245 . 33 GLN CA C 57.560 0.1 1 246 . 33 GLN CB C 27.38 0.3 1 247 . 33 GLN N N 116.783 0.05 1 248 . 34 LEU H H 7.578 0.02 1 249 . 34 LEU HA H 3.980 0.05 1 250 . 34 LEU HB2 H 1.728 0.05 2 251 . 34 LEU HG H 1.441 0.05 1 252 . 34 LEU C C 177.615 0.1 1 253 . 34 LEU CA C 58.372 0.1 1 254 . 34 LEU CB C 41.752 0.3 1 255 . 34 LEU N N 121.641 0.05 1 256 . 35 VAL H H 8.732 0.02 1 257 . 35 VAL HA H 3.438 0.05 1 258 . 35 VAL HB H 2.198 0.05 1 259 . 35 VAL HG1 H 0.989 0.05 2 260 . 35 VAL HG2 H 0.898 0.05 2 261 . 35 VAL C C 177.677 0.1 1 262 . 35 VAL CA C 67.421 0.1 1 263 . 35 VAL CB C 31.009 0.3 1 264 . 35 VAL N N 120.367 0.05 1 265 . 36 LYS H H 7.229 0.02 1 266 . 36 LYS HA H 3.836 0.05 1 267 . 36 LYS HB2 H 0.554 0.05 2 268 . 36 LYS HB3 H 1.144 0.05 2 269 . 36 LYS HG2 H 1.540 0.05 2 270 . 36 LYS HG3 H 1.282 0.05 2 271 . 36 LYS HD2 H 1.275 0.05 2 272 . 36 LYS HE2 H 2.659 0.05 2 273 . 36 LYS C C 179.008 0.1 1 274 . 36 LYS CA C 59.644 0.1 1 275 . 36 LYS CB C 30.729 0.3 1 276 . 36 LYS N N 120.521 0.05 1 277 . 37 ALA H H 7.740 0.02 1 278 . 37 ALA HA H 4.111 0.05 1 279 . 37 ALA HB H 1.722 0.05 1 280 . 37 ALA C C 178.454 0.1 1 281 . 37 ALA CA C 55.237 0.1 1 282 . 37 ALA CB C 18.654 0.3 1 283 . 37 ALA N N 123.933 0.05 1 284 . 38 ILE H H 8.668 0.02 1 285 . 38 ILE HA H 3.752 0.05 1 286 . 38 ILE HB H 2.188 0.05 1 287 . 38 ILE HG2 H 1.190 0.05 1 288 . 38 ILE HD1 H 0.845 0.05 1 289 . 38 ILE C C 177.720 0.1 1 290 . 38 ILE CA C 65.919 0.1 1 291 . 38 ILE CB C 37.519 0.3 1 292 . 38 ILE N N 121.456 0.05 1 293 . 39 ASP H H 8.529 0.02 1 294 . 39 ASP HA H 4.641 0.05 1 295 . 39 ASP HB2 H 2.689 0.05 2 296 . 39 ASP HB3 H 2.835 0.05 2 297 . 39 ASP C C 179.029 0.1 1 298 . 39 ASP CA C 57.664 0.1 1 299 . 39 ASP CB C 40.388 0.3 1 300 . 39 ASP N N 122.977 0.05 1 301 . 40 ALA H H 8.040 0.02 1 302 . 40 ALA HA H 4.349 0.05 1 303 . 40 ALA HB H 1.774 0.05 1 304 . 40 ALA C C 179.719 0.1 1 305 . 40 ALA CA C 54.793 0.1 1 306 . 40 ALA CB C 17.032 0.3 1 307 . 40 ALA N N 125.092 0.05 1 308 . 41 GLU H H 8.749 0.02 1 309 . 41 GLU HA H 3.929 0.05 1 310 . 41 GLU HB2 H 2.079 0.05 2 311 . 41 GLU HG2 H 2.781 0.05 2 312 . 41 GLU C C 176.689 0.1 1 313 . 41 GLU CA C 60.547 0.1 1 314 . 41 GLU CB C 28.097 0.3 1 315 . 41 GLU N N 123.601 0.05 1 316 . 42 LYS H H 8.725 0.02 1 317 . 42 LYS HA H 3.395 0.05 1 318 . 42 LYS HB2 H 2.158 0.05 2 319 . 42 LYS HB3 H 1.562 0.05 2 320 . 42 LYS HG2 H 1.568 0.05 2 321 . 42 LYS HE3 H 2.384 0.05 2 322 . 42 LYS C C 177.557 0.1 1 323 . 42 LYS CA C 60.387 0.1 1 324 . 42 LYS CB C 31.729 0.3 1 325 . 42 LYS N N 122.564 0.05 1 326 . 43 ALA H H 7.720 0.02 1 327 . 43 ALA HA H 4.196 0.05 1 328 . 43 ALA HB H 1.629 0.05 1 329 . 43 ALA C C 179.469 0.1 1 330 . 43 ALA CA C 54.847 0.1 1 331 . 43 ALA CB C 17.483 0.3 1 332 . 43 ALA N N 120.920 0.05 1 333 . 44 LEU H H 7.716 0.02 1 334 . 44 LEU HA H 4.091 0.05 1 335 . 44 LEU HB2 H 1.626 0.05 2 336 . 44 LEU HB3 H 1.845 0.05 2 337 . 44 LEU HG H 1.423 0.05 1 338 . 44 LEU HD1 H 0.721 0.05 2 339 . 44 LEU HD2 H 0.930 0.05 2 340 . 44 LEU C C 177.614 0.1 1 341 . 44 LEU CA C 57.926 0.1 1 342 . 44 LEU CB C 41.376 0.3 1 343 . 44 LEU CD1 C 26.189 0.1 2 344 . 44 LEU N N 122.384 0.05 1 345 . 45 ILE H H 8.091 0.02 1 346 . 45 ILE HA H 3.289 0.05 1 347 . 45 ILE HB H 1.514 0.05 1 348 . 45 ILE HG12 H 1.773 0.05 2 349 . 45 ILE HG13 H 0.930 0.05 2 350 . 45 ILE HG2 H 0.539 0.05 1 351 . 45 ILE HD1 H 0.327 0.05 1 352 . 45 ILE C C 178.470 0.1 1 353 . 45 ILE CA C 66.045 0.1 1 354 . 45 ILE CB C 38.110 0.3 1 355 . 45 ILE CG1 C 16.767 0.1 2 356 . 45 ILE CD1 C 14.119 0.1 1 357 . 45 ILE N N 121.725 0.05 1 358 . 46 ASN H H 8.238 0.02 1 359 . 46 ASN HA H 4.346 0.05 1 360 . 46 ASN HB2 H 2.733 0.05 2 361 . 46 ASN HB3 H 3.179 0.05 2 362 . 46 ASN C C 178.265 0.1 1 363 . 46 ASN CA C 56.948 0.1 1 364 . 46 ASN CB C 39.034 0.3 1 365 . 46 ASN N N 119.760 0.05 1 366 . 47 THR H H 8.989 0.02 1 367 . 47 THR HA H 3.832 0.05 1 368 . 47 THR HB H 4.400 0.05 1 369 . 47 THR HG2 H 1.374 0.05 1 370 . 47 THR C C 177.124 0.1 1 371 . 47 THR CA C 67.399 0.1 1 372 . 47 THR CB C 69.287 0.3 1 373 . 47 THR N N 122.728 0.05 1 374 . 48 ALA H H 8.646 0.02 1 375 . 48 ALA HA H 3.998 0.05 1 376 . 48 ALA HB H 0.007 0.05 1 377 . 48 ALA C C 177.406 0.1 1 378 . 48 ALA CA C 55.438 0.1 1 379 . 48 ALA CB C 15.463 0.3 1 380 . 48 ALA N N 128.647 0.05 1 381 . 49 SER H H 7.593 0.02 1 382 . 49 SER HA H 4.312 0.05 1 383 . 49 SER HB2 H 4.138 0.05 2 384 . 49 SER C C 175.645 0.1 1 385 . 49 SER CA C 60.907 0.1 1 386 . 49 SER CB C 63.486 0.3 1 387 . 49 SER N N 111.216 0.05 1 388 . 50 GLN H H 7.502 0.02 1 389 . 50 GLN HA H 4.831 0.05 1 390 . 50 GLN HB2 H 2.105 0.05 2 391 . 50 GLN HG2 H 2.473 0.05 2 392 . 50 GLN C C 176.312 0.1 1 393 . 50 GLN CA C 55.071 0.1 1 394 . 50 GLN CB C 32.148 0.3 1 395 . 50 GLN N N 118.997 0.05 1 396 . 51 SER H H 7.749 0.02 1 397 . 51 SER HA H 5.344 0.05 1 398 . 51 SER HB2 H 4.068 0.05 2 399 . 51 SER HB3 H 3.912 0.05 2 400 . 51 SER C C 172.390 0.1 1 401 . 51 SER CA C 58.328 0.1 1 402 . 51 SER CB C 66.612 0.3 1 403 . 51 SER N N 116.870 0.05 1 404 . 52 LYS H H 8.464 0.02 1 405 . 52 LYS HA H 4.386 0.05 1 406 . 52 LYS HG2 H 1.658 0.05 2 407 . 52 LYS HG3 H 1.352 0.05 2 408 . 52 LYS C C 176.781 0.1 1 409 . 52 LYS CA C 55.968 0.1 1 410 . 52 LYS CB C 33.190 0.3 1 411 . 52 LYS N N 124.416 0.05 1 412 . 53 LYS H H 8.654 0.02 1 413 . 53 LYS HA H 3.050 0.05 1 414 . 53 LYS HB2 H 1.793 0.05 2 415 . 53 LYS HB3 H 2.427 0.05 2 416 . 53 LYS HG2 H 1.112 0.05 2 417 . 53 LYS CA C 54.745 0.1 1 418 . 53 LYS CG C 24.152 0.1 1 419 . 53 LYS N N 126.401 0.05 1 420 . 54 PRO C C 175.630 0.1 1 421 . 54 PRO CA C 61.669 0.1 1 422 . 54 PRO CB C 32.244 0.3 1 423 . 55 SER H H 8.259 0.02 1 424 . 55 SER HA H 4.278 0.05 1 425 . 55 SER HB2 H 4.184 0.05 2 426 . 55 SER HB3 H 4.046 0.05 2 427 . 55 SER C C 174.948 0.1 1 428 . 55 SER CA C 57.501 0.1 1 429 . 55 SER CB C 64.581 0.3 1 430 . 55 SER N N 114.111 0.05 1 431 . 56 GLN H H 8.800 0.02 1 432 . 56 GLN HA H 3.939 0.05 1 433 . 56 GLN HB2 H 2.174 0.05 2 434 . 56 GLN HB3 H 2.025 0.05 2 435 . 56 GLN HG2 H 2.454 0.05 2 436 . 56 GLN C C 177.519 0.1 1 437 . 56 GLN CA C 59.362 0.1 1 438 . 56 GLN CB C 28.076 0.3 1 439 . 56 GLN N N 122.598 0.05 1 440 . 57 GLU H H 8.749 0.02 1 441 . 57 GLU HA H 3.974 0.05 1 442 . 57 GLU HB2 H 2.061 0.05 2 443 . 57 GLU C C 178.536 0.1 1 444 . 57 GLU CA C 60.325 0.1 1 445 . 57 GLU CB C 28.699 0.3 1 446 . 57 GLU N N 118.276 0.05 1 447 . 58 THR H H 7.650 0.02 1 448 . 58 THR HA H 4.025 0.05 1 449 . 58 THR HB H 4.145 0.05 1 450 . 58 THR HG2 H 1.204 0.05 1 451 . 58 THR C C 176.230 0.1 1 452 . 58 THR CA C 66.162 0.1 1 453 . 58 THR CB C 67.912 0.3 1 454 . 58 THR N N 119.528 0.05 1 455 . 59 LEU H H 8.427 0.02 1 456 . 59 LEU HA H 3.867 0.05 1 457 . 59 LEU HB2 H 2.193 0.05 2 458 . 59 LEU HB3 H 1.868 0.05 2 459 . 59 LEU HG H 1.471 0.05 1 460 . 59 LEU HD2 H 0.953 0.05 2 461 . 59 LEU C C 177.613 0.1 1 462 . 59 LEU CA C 58.759 0.1 1 463 . 59 LEU CB C 41.440 0.3 1 464 . 59 LEU N N 125.158 0.05 1 465 . 60 LEU H H 7.876 0.02 1 466 . 60 LEU HA H 3.995 0.05 1 467 . 60 LEU HB2 H 1.904 0.05 2 468 . 60 LEU HB3 H 1.511 0.05 2 469 . 60 LEU HD2 H 0.934 0.05 2 470 . 60 LEU C C 179.125 0.1 1 471 . 60 LEU CA C 57.604 0.1 1 472 . 60 LEU CB C 41.097 0.3 1 473 . 60 LEU CG C 26.233 0.1 1 474 . 60 LEU N N 116.841 0.05 1 475 . 61 GLU H H 7.264 0.02 1 476 . 61 GLU HA H 4.100 0.05 1 477 . 61 GLU HB2 H 2.221 0.05 2 478 . 61 GLU HB3 H 1.880 0.05 2 479 . 61 GLU HG2 H 2.246 0.05 2 480 . 61 GLU HG3 H 2.334 0.05 2 481 . 61 GLU C C 179.347 0.1 1 482 . 61 GLU CA C 58.886 0.1 1 483 . 61 GLU CB C 29.419 0.3 1 484 . 61 GLU N N 118.939 0.05 1 485 . 62 LEU H H 8.209 0.02 1 486 . 62 LEU HA H 4.161 0.05 1 487 . 62 LEU HB2 H 1.540 0.05 2 488 . 62 LEU HB3 H 2.171 0.05 2 489 . 62 LEU HG H 2.007 0.05 1 490 . 62 LEU HD2 H 0.933 0.05 2 491 . 62 LEU C C 178.487 0.1 1 492 . 62 LEU CA C 57.313 0.1 1 493 . 62 LEU CB C 41.902 0.3 1 494 . 62 LEU CG C 26.422 0.1 1 495 . 62 LEU N N 120.771 0.05 1 496 . 63 ILE H H 7.515 0.02 1 497 . 63 ILE HA H 4.420 0.05 1 498 . 63 ILE HB H 2.127 0.05 1 499 . 63 ILE HG12 H 1.584 0.05 2 500 . 63 ILE HG13 H 1.329 0.05 2 501 . 63 ILE HG2 H 0.931 0.05 1 502 . 63 ILE HD1 H 0.848 0.05 1 503 . 63 ILE C C 175.706 0.1 1 504 . 63 ILE CA C 61.152 0.1 1 505 . 63 ILE CB C 38.271 0.3 1 506 . 63 ILE CD1 C 17.473 0.1 1 507 . 63 ILE N N 109.825 0.05 1 508 . 64 LYS H H 7.321 0.02 1 509 . 64 LYS HA H 4.126 0.05 1 510 . 64 LYS HB2 H 2.053 0.05 2 511 . 64 LYS HB3 H 1.903 0.05 2 512 . 64 LYS HG2 H 1.435 0.05 2 513 . 64 LYS CA C 61.830 0.1 1 514 . 64 LYS N N 124.685 0.05 1 515 . 65 PRO HA H 4.116 0.05 1 516 . 65 PRO HB2 H 2.377 0.05 2 517 . 65 PRO HB3 H 1.861 0.05 2 518 . 65 PRO C C 178.141 0.1 1 519 . 65 PRO CA C 66.331 0.1 1 520 . 65 PRO CB C 30.686 0.3 1 521 . 66 LEU H H 7.312 0.02 1 522 . 66 LEU HA H 4.063 0.05 1 523 . 66 LEU HB3 H 1.915 0.05 2 524 . 66 LEU HG H 1.749 0.05 1 525 . 66 LEU HD1 H 0.900 0.05 2 526 . 66 LEU C C 178.011 0.1 1 527 . 66 LEU CA C 59.121 0.1 1 528 . 66 LEU CB C 41.602 0.3 1 529 . 66 LEU N N 117.001 0.05 1 530 . 67 ASN H H 7.930 0.02 1 531 . 67 ASN HA H 4.444 0.05 1 532 . 67 ASN HB2 H 2.805 0.05 2 533 . 67 ASN HB3 H 2.946 0.05 2 534 . 67 ASN HD21 H 7.502 0.05 2 535 . 67 ASN HD22 H 6.417 0.05 2 536 . 67 ASN C C 177.005 0.1 1 537 . 67 ASN CA C 55.293 0.1 1 538 . 67 ASN CB C 37.476 0.3 1 539 . 67 ASN N N 118.238 0.05 1 540 . 67 ASN ND2 N 110.380 0.05 1 541 . 68 ASN H H 8.372 0.02 1 542 . 68 ASN HA H 4.481 0.05 1 543 . 68 ASN HB2 H 2.670 0.05 2 544 . 68 ASN C C 177.994 0.1 1 545 . 68 ASN CA C 56.103 0.1 1 546 . 68 ASN CB C 37.498 0.3 1 547 . 68 ASN N N 122.745 0.05 1 548 . 69 PHE H H 7.988 0.02 1 549 . 69 PHE HA H 4.655 0.05 1 550 . 69 PHE HB2 H 2.922 0.05 2 551 . 69 PHE HB3 H 3.442 0.05 2 552 . 69 PHE C C 177.973 0.1 1 553 . 69 PHE CA C 61.358 0.1 1 554 . 69 PHE CB C 39.109 0.3 1 555 . 69 PHE N N 120.956 0.05 1 556 . 70 ALA H H 8.346 0.02 1 557 . 70 ALA HA H 3.948 0.05 1 558 . 70 ALA HB H 1.526 0.05 1 559 . 70 ALA C C 179.701 0.1 1 560 . 70 ALA CA C 55.594 0.1 1 561 . 70 ALA CB C 18.375 0.3 1 562 . 70 ALA N N 121.735 0.05 1 563 . 71 ALA H H 8.121 0.02 1 564 . 71 ALA HA H 3.953 0.05 1 565 . 71 ALA HB H 1.633 0.05 1 566 . 71 ALA C C 179.984 0.1 1 567 . 71 ALA CA C 54.817 0.1 1 568 . 71 ALA CB C 17.687 0.3 1 569 . 71 ALA N N 122.028 0.05 1 570 . 72 GLU H H 7.793 0.02 1 571 . 72 GLU HA H 4.197 0.05 1 572 . 72 GLU HB2 H 2.011 0.05 2 573 . 72 GLU HG2 H 2.431 0.05 2 574 . 72 GLU HG3 H 2.279 0.05 2 575 . 72 GLU C C 178.481 0.1 1 576 . 72 GLU CA C 58.905 0.1 1 577 . 72 GLU CB C 29.011 0.3 1 578 . 72 GLU N N 121.288 0.05 1 579 . 73 VAL H H 8.006 0.02 1 580 . 73 VAL HA H 3.681 0.05 1 581 . 73 VAL HB H 2.690 0.05 1 582 . 73 VAL HG1 H 0.961 0.05 2 583 . 73 VAL HG2 H 1.190 0.05 2 584 . 73 VAL C C 178.661 0.1 1 585 . 73 VAL CA C 67.274 0.1 1 586 . 73 VAL CB C 31.439 0.3 1 587 . 73 VAL CG1 C 22.595 0.1 2 588 . 73 VAL N N 119.742 0.05 1 589 . 74 GLY H H 7.693 0.02 1 590 . 74 GLY HA2 H 3.936 0.05 2 591 . 74 GLY HA3 H 4.135 0.05 2 592 . 74 GLY C C 175.551 0.1 1 593 . 74 GLY CA C 47.465 0.1 1 594 . 74 GLY N N 108.236 0.05 1 595 . 75 LYS H H 8.160 0.02 1 596 . 75 LYS HA H 4.163 0.05 1 597 . 75 LYS HB2 H 2.019 0.05 2 598 . 75 LYS HG2 H 1.493 0.05 2 599 . 75 LYS HD2 H 1.689 0.05 2 600 . 75 LYS C C 179.339 0.1 1 601 . 75 LYS CA C 59.703 0.1 1 602 . 75 LYS CB C 32.448 0.3 1 603 . 75 LYS N N 124.579 0.05 1 604 . 76 ILE H H 8.135 0.02 1 605 . 76 ILE HA H 3.754 0.05 1 606 . 76 ILE HB H 1.777 0.05 1 607 . 76 ILE HG12 H 1.166 0.05 2 608 . 76 ILE HG13 H 1.996 0.05 2 609 . 76 ILE HG2 H 0.997 0.05 1 610 . 76 ILE HD1 H 0.883 0.05 1 611 . 76 ILE C C 178.001 0.1 1 612 . 76 ILE CA C 65.319 0.1 1 613 . 76 ILE CB C 39.088 0.3 1 614 . 76 ILE CG2 C 17.846 0.1 2 615 . 76 ILE N N 120.580 0.05 1 616 . 77 ARG H H 7.095 0.02 1 617 . 77 ARG HA H 4.020 0.05 1 618 . 77 ARG HB2 H 2.128 0.05 2 619 . 77 ARG HB3 H 2.288 0.05 2 620 . 77 ARG C C 177.698 0.1 1 621 . 77 ARG CA C 60.897 0.1 1 622 . 77 ARG CB C 29.698 0.3 1 623 . 77 ARG N N 121.576 0.05 1 624 . 78 ASP H H 8.454 0.02 1 625 . 78 ASP HA H 4.466 0.05 1 626 . 78 ASP HB2 H 2.839 0.05 2 627 . 78 ASP C C 177.707 0.1 1 628 . 78 ASP CA C 57.554 0.1 1 629 . 78 ASP CB C 40.678 0.3 1 630 . 78 ASP N N 119.061 0.05 1 631 . 79 SER H H 7.941 0.02 1 632 . 79 SER HA H 4.601 0.05 1 633 . 79 SER HB2 H 4.068 0.05 2 634 . 79 SER C C 174.444 0.1 1 635 . 79 SER CA C 59.356 0.1 1 636 . 79 SER CB C 64.012 0.3 1 637 . 79 SER N N 113.311 0.05 1 638 . 80 ASN H H 7.671 0.02 1 639 . 80 ASN HA H 5.285 0.05 1 640 . 80 ASN HB2 H 2.630 0.05 2 641 . 80 ASN HB3 H 3.004 0.05 2 642 . 80 ASN C C 180.234 0.1 1 643 . 80 ASN CA C 53.534 0.1 1 644 . 80 ASN CB C 40.785 0.3 1 645 . 80 ASN N N 123.048 0.05 1 646 . 81 ARG H H 7.973 0.02 1 647 . 81 ARG HA H 3.894 0.05 1 648 . 81 ARG HG2 H 1.692 0.05 2 649 . 81 ARG C C 176.915 0.1 1 650 . 81 ARG CA C 59.247 0.1 1 651 . 81 ARG CB C 29.579 0.3 1 652 . 81 ARG N N 119.533 0.05 1 653 . 82 SER H H 8.206 0.02 1 654 . 82 SER HA H 4.478 0.05 1 655 . 82 SER HB2 H 4.140 0.05 2 656 . 82 SER C C 174.662 0.1 1 657 . 82 SER CA C 57.760 0.1 1 658 . 82 SER CB C 63.185 0.3 1 659 . 82 SER N N 111.962 0.05 1 660 . 83 SER H H 7.433 0.02 1 661 . 83 SER HA H 4.379 0.05 1 662 . 83 SER C C 177.698 0.1 1 663 . 83 SER CA C 58.363 0.1 1 664 . 83 SER CB C 64.001 0.3 1 665 . 83 SER N N 116.689 0.05 1 666 . 84 LYS H H 9.428 0.02 1 667 . 84 LYS HA H 4.281 0.05 1 668 . 84 LYS HB2 H 1.683 0.05 2 669 . 84 LYS HG2 H 1.420 0.05 2 670 . 84 LYS HG3 H 0.849 0.05 2 671 . 84 LYS C C 176.661 0.1 1 672 . 84 LYS CA C 58.177 0.1 1 673 . 84 LYS CB C 31.267 0.3 1 674 . 84 LYS N N 131.639 0.05 1 675 . 85 PHE H H 9.161 0.02 1 676 . 85 PHE HA H 4.606 0.05 1 677 . 85 PHE HB2 H 3.161 0.05 2 678 . 85 PHE HB3 H 2.408 0.05 2 679 . 85 PHE C C 175.821 0.1 1 680 . 85 PHE CA C 56.983 0.1 1 681 . 85 PHE CB C 38.056 0.3 1 682 . 85 PHE N N 119.699 0.05 1 683 . 86 PHE H H 7.691 0.02 1 684 . 86 PHE HA H 4.188 0.05 1 685 . 86 PHE HB2 H 3.133 0.05 2 686 . 86 PHE HB3 H 3.059 0.05 2 687 . 86 PHE C C 178.256 0.1 1 688 . 86 PHE CA C 63.017 0.1 1 689 . 86 PHE CB C 39.131 0.3 1 690 . 86 PHE N N 124.183 0.05 1 691 . 87 ASN H H 9.777 0.02 1 692 . 87 ASN HA H 4.593 0.05 1 693 . 87 ASN HB2 H 2.630 0.05 2 694 . 87 ASN HD21 H 7.119 0.05 2 695 . 87 ASN HD22 H 8.533 0.05 2 696 . 87 ASN C C 177.218 0.1 1 697 . 87 ASN CA C 56.867 0.1 1 698 . 87 ASN CB C 37.562 0.3 1 699 . 87 ASN N N 120.323 0.05 1 700 . 87 ASN ND2 N 115.252 0.05 1 701 . 88 ASN H H 7.489 0.02 1 702 . 88 ASN HA H 4.149 0.05 1 703 . 88 ASN HB2 H 1.936 0.05 2 704 . 88 ASN HB3 H 2.759 0.05 2 705 . 88 ASN C C 175.929 0.1 1 706 . 88 ASN CA C 57.602 0.1 1 707 . 88 ASN CB C 38.336 0.3 1 708 . 88 ASN N N 119.005 0.05 1 709 . 89 LEU H H 7.870 0.02 1 710 . 89 LEU HA H 4.993 0.05 1 711 . 89 LEU HB2 H 1.181 0.05 2 712 . 89 LEU HB3 H 1.797 0.05 2 713 . 89 LEU HD1 H 0.672 0.05 2 714 . 89 LEU HD2 H 1.025 0.05 2 715 . 89 LEU CA C 55.691 0.1 1 716 . 89 LEU CB C 42.599 0.1 1 717 . 89 LEU CD1 C 23.468 0.1 2 718 . 89 LEU CD2 C 27.979 0.1 2 719 . 89 LEU N N 116.308 0.05 1 720 . 90 SER C C 174.488 0.1 1 721 . 90 SER CA C 60.380 0.1 1 722 . 90 SER CB C 61.649 0.3 1 723 . 91 ALA H H 7.940 0.02 1 724 . 91 ALA HA H 4.256 0.05 1 725 . 91 ALA HB H 1.844 0.05 1 726 . 91 ALA C C 178.298 0.1 1 727 . 91 ALA CA C 55.876 0.1 1 728 . 91 ALA CB C 18.074 0.3 1 729 . 91 ALA N N 125.059 0.05 1 730 . 92 ILE H H 6.904 0.02 1 731 . 92 ILE HA H 3.810 0.05 1 732 . 92 ILE HB H 2.147 0.05 1 733 . 92 ILE HG12 H 1.517 0.05 2 734 . 92 ILE HG13 H 1.164 0.05 2 735 . 92 ILE HG2 H 0.879 0.05 1 736 . 92 ILE HD1 H 0.506 0.05 1 737 . 92 ILE C C 177.902 0.1 1 738 . 92 ILE CA C 62.669 0.1 1 739 . 92 ILE CB C 36.391 0.3 1 740 . 92 ILE CG1 C 26.801 0.1 2 741 . 92 ILE CG2 C 17.846 0.1 2 742 . 92 ILE CD1 C 10.728 0.1 1 743 . 92 ILE N N 113.418 0.05 1 744 . 93 SER H H 8.652 0.02 1 745 . 93 SER HA H 3.838 0.05 1 746 . 93 SER HB2 H 4.107 0.05 2 747 . 93 SER HB3 H 3.553 0.05 2 748 . 93 SER C C 177.569 0.1 1 749 . 93 SER CA C 63.732 0.1 1 750 . 93 SER CB C 62.025 0.3 1 751 . 93 SER N N 116.879 0.05 1 752 . 94 GLU H H 8.818 0.02 1 753 . 94 GLU HA H 4.422 0.05 2 754 . 94 GLU HB2 H 2.081 0.05 2 755 . 94 GLU HB3 H 2.479 0.05 2 756 . 94 GLU HG2 H 2.404 0.05 2 757 . 94 GLU C C 176.329 0.1 1 758 . 94 GLU CA C 56.995 0.1 1 759 . 94 GLU CB C 28.097 0.3 1 760 . 94 GLU N N 118.807 0.05 1 761 . 95 SER H H 7.594 0.02 1 762 . 95 SER HA H 5.167 0.05 1 763 . 95 SER HB2 H 4.374 0.05 2 764 . 95 SER HB3 H 3.981 0.05 2 765 . 95 SER C C 176.192 0.1 1 766 . 95 SER CA C 57.358 0.1 1 767 . 95 SER CB C 67.611 0.3 1 768 . 95 SER N N 110.303 0.05 1 769 . 96 ILE H H 7.422 0.02 1 770 . 96 ILE HA H 4.526 0.05 1 771 . 96 ILE HB H 2.353 0.05 1 772 . 96 ILE HG12 H 1.471 0.05 2 773 . 96 ILE HG13 H 1.703 0.05 2 774 . 96 ILE HG2 H 1.098 0.05 1 775 . 96 ILE HD1 H 0.861 0.05 1 776 . 96 ILE C C 175.575 0.1 1 777 . 96 ILE CA C 60.151 0.1 1 778 . 96 ILE CB C 38.798 0.3 1 779 . 96 ILE CG2 C 16.389 0.1 2 780 . 96 ILE N N 126.717 0.05 1 781 . 97 GLY H H 8.903 0.02 1 782 . 97 GLY HA2 H 4.333 0.05 2 783 . 97 GLY HA3 H 4.209 0.05 2 784 . 97 GLY C C 177.606 0.1 1 785 . 97 GLY CA C 46.630 0.1 1 786 . 97 GLY N N 112.164 0.05 1 787 . 98 PHE H H 9.599 0.02 1 788 . 98 PHE HA H 4.397 0.05 1 789 . 98 PHE HB2 H 3.328 0.05 2 790 . 98 PHE HB3 H 3.428 0.05 2 791 . 98 PHE C C 176.249 0.1 1 792 . 98 PHE CA C 61.648 0.1 1 793 . 98 PHE CB C 36.434 0.3 1 794 . 98 PHE N N 126.161 0.05 1 795 . 99 LEU H H 7.071 0.02 1 796 . 99 LEU HA H 4.071 0.05 1 797 . 99 LEU HB2 H 1.398 0.05 2 798 . 99 LEU HB3 H 1.699 0.05 2 799 . 99 LEU HD2 H 0.773 0.05 2 800 . 99 LEU C C 178.874 0.1 1 801 . 99 LEU CA C 56.413 0.1 1 802 . 99 LEU CB C 43.234 0.3 1 803 . 99 LEU CD2 C 23.468 0.1 2 804 . 99 LEU N N 121.449 0.05 1 805 . 100 SER H H 7.885 0.02 1 806 . 100 SER HA H 4.130 0.05 1 807 . 100 SER HB2 H 4.022 0.05 2 808 . 100 SER HB3 H 4.130 0.05 2 809 . 100 SER C C 174.439 0.1 1 810 . 100 SER CA C 59.486 0.1 1 811 . 100 SER CB C 62.347 0.3 1 812 . 100 SER N N 113.382 0.05 1 813 . 101 TRP H H 8.173 0.02 1 814 . 101 TRP HA H 4.042 0.05 1 815 . 101 TRP HB2 H 3.495 0.05 2 816 . 101 TRP HB3 H 3.687 0.05 2 817 . 101 TRP HE1 H 8.953 0.05 1 818 . 101 TRP C C 176.430 0.1 1 819 . 101 TRP CA C 59.988 0.1 1 820 . 101 TRP CB C 27.775 0.3 1 821 . 101 TRP N N 122.914 0.05 1 822 . 101 TRP NE1 N 127.740 0.05 1 823 . 102 VAL H H 5.549 0.02 1 824 . 102 VAL HA H 3.072 0.05 1 825 . 102 VAL HB H 1.862 0.05 1 826 . 102 VAL HG1 H -0.636 0.05 2 827 . 102 VAL HG2 H 0.587 0.05 2 828 . 102 VAL C C 175.063 0.1 1 829 . 102 VAL CA C 63.524 0.1 1 830 . 102 VAL CB C 30.289 0.3 1 831 . 102 VAL CG1 C 19.619 0.1 2 832 . 102 VAL CG2 C 16.476 0.1 2 833 . 102 VAL N N 110.547 0.05 1 834 . 103 VAL H H 7.512 0.02 1 835 . 103 VAL HA H 4.712 0.05 1 836 . 103 VAL HB H 2.574 0.05 1 837 . 103 VAL HG2 H 0.866 0.05 2 838 . 103 VAL C C 175.871 0.1 1 839 . 103 VAL CA C 60.527 0.1 1 840 . 103 VAL CB C 31.922 0.3 1 841 . 103 VAL CG2 C 18.870 0.1 2 842 . 103 VAL N N 111.830 0.05 1 843 . 104 VAL H H 7.467 0.02 1 844 . 104 VAL HA H 4.057 0.05 1 845 . 104 VAL HB H 1.957 0.05 1 846 . 104 VAL HG1 H 0.461 0.05 2 847 . 104 VAL HG2 H 0.758 0.05 2 848 . 104 VAL C C 175.254 0.1 1 849 . 104 VAL CA C 63.259 0.1 1 850 . 104 VAL CB C 32.545 0.3 1 851 . 104 VAL CG1 C 20.543 0.1 2 852 . 104 VAL CG2 C 21.910 0.1 2 853 . 104 VAL N N 125.832 0.05 1 854 . 105 GLU H H 8.293 0.02 1 855 . 105 GLU CA C 53.206 0.1 1 856 . 105 GLU N N 126.035 0.05 1 857 . 106 PRO HA H 4.588 0.05 1 858 . 106 PRO HB2 H 2.104 0.05 2 859 . 106 PRO HB3 H 2.486 0.05 2 860 . 106 PRO C C 175.702 0.1 1 861 . 106 PRO CA C 64.175 0.1 1 862 . 106 PRO CB C 32.620 0.3 1 863 . 107 THR H H 7.267 0.02 1 864 . 107 THR HA H 5.028 0.05 1 865 . 107 THR HB H 4.514 0.05 1 866 . 107 THR HG2 H 1.163 0.05 1 867 . 107 THR CA C 58.659 0.1 1 868 . 107 THR CB C 67.858 0.1 1 869 . 107 THR CG2 C 21.344 0.1 1 870 . 107 THR N N 107.264 0.05 1 871 . 108 PRO C C 177.508 0.1 1 872 . 108 PRO CA C 65.925 0.1 1 873 . 108 PRO CB C 31.890 0.3 1 874 . 109 GLY H H 9.056 0.02 1 875 . 109 GLY HA2 H 3.884 0.05 2 876 . 109 GLY HA3 H 3.691 0.05 2 877 . 109 GLY CA C 48.547 0.1 1 878 . 109 GLY N N 109.064 0.05 1 879 . 110 PRO C C 174.425 0.1 1 880 . 110 PRO CA C 64.937 0.1 1 881 . 111 HIS H H 7.503 0.02 1 882 . 111 HIS C C 177.050 0.1 1 883 . 111 HIS CA C 60.755 0.1 1 884 . 111 HIS CB C 30.966 0.3 1 885 . 111 HIS N N 117.987 0.05 1 886 . 112 VAL H H 7.726 0.02 1 887 . 112 VAL HA H 3.389 0.05 1 888 . 112 VAL HB H 2.267 0.05 1 889 . 112 VAL HG1 H 0.936 0.05 2 890 . 112 VAL HG2 H 1.351 0.05 2 891 . 112 VAL C C 177.1 0.1 1 892 . 112 VAL CA C 68.371 0.1 1 893 . 112 VAL CB C 31.073 0.3 1 894 . 112 VAL CG1 C 22.595 0.1 2 895 . 112 VAL CG2 C 25.054 0.1 2 896 . 112 VAL N N 120.181 0.05 1 897 . 113 ALA H H 8.038 0.02 1 898 . 113 ALA HA H 3.998 0.05 1 899 . 113 ALA HB H 1.470 0.05 1 900 . 113 ALA C C 180.1 0.1 1 901 . 113 ALA CA C 55.671 0.1 1 902 . 113 ALA CB C 17.816 0.3 1 903 . 113 ALA N N 123.629 0.05 1 904 . 114 GLU H H 8.312 0.02 1 905 . 114 GLU HA H 4.081 0.05 1 906 . 114 GLU HB2 H 2.245 0.05 2 907 . 114 GLU HB3 H 2.398 0.05 2 908 . 114 GLU C C 179.421 0.1 1 909 . 114 GLU CA C 59.267 0.1 1 910 . 114 GLU CB C 29.011 0.3 1 911 . 114 GLU N N 122.183 0.05 1 912 . 115 MET H H 7.811 0.02 1 913 . 115 MET HA H 4.598 0.05 1 914 . 115 MET HB3 H 2.399 0.05 2 915 . 115 MET C C 178.461 0.1 1 916 . 115 MET CA C 56.863 0.1 1 917 . 115 MET CB C 32.889 0.3 1 918 . 115 MET N N 121.498 0.05 1 919 . 116 ARG H H 8.967 0.02 1 920 . 116 ARG HA H 3.893 0.05 1 921 . 116 ARG C C 177.857 0.1 1 922 . 116 ARG CA C 59.662 0.1 1 923 . 116 ARG CB C 28.753 0.3 1 924 . 116 ARG N N 122.638 0.05 1 925 . 117 GLY H H 8.043 0.02 1 926 . 117 GLY HA2 H 4.049 0.05 2 927 . 117 GLY C C 176.981 0.1 1 928 . 117 GLY CA C 47.410 0.1 1 929 . 117 GLY N N 108.279 0.05 1 930 . 118 SER H H 7.828 0.02 1 931 . 118 SER HA H 4.499 0.05 1 932 . 118 SER HB2 H 4.299 0.05 2 933 . 118 SER HB3 H 4.090 0.05 2 934 . 118 SER C C 176.975 0.1 1 935 . 118 SER CA C 62.226 0.1 1 936 . 118 SER CB C 63.464 0.3 1 937 . 118 SER N N 119.707 0.05 1 938 . 119 ALA H H 8.059 0.02 1 939 . 119 ALA HA H 4.677 0.05 2 940 . 119 ALA HB H 1.847 0.05 1 941 . 119 ALA C C 180.071 0.1 1 942 . 119 ALA CA C 55.562 0.1 1 943 . 119 ALA CB C 18.214 0.3 1 944 . 119 ALA N N 123.232 0.05 1 945 . 120 GLU H H 8.740 0.02 1 946 . 120 GLU HA H 5.453 0.05 1 947 . 120 GLU HB2 H 2.028 0.05 2 948 . 120 GLU HG2 H 2.582 0.05 2 949 . 120 GLU HG3 H 2.226 0.05 2 950 . 120 GLU C C 178.166 0.1 1 951 . 120 GLU CA C 57.530 0.1 1 952 . 120 GLU CB C 29.451 0.3 1 953 . 120 GLU CG C 38.020 0.1 1 954 . 120 GLU N N 119.193 0.05 1 955 . 121 PHE H H 7.498 0.02 1 956 . 121 PHE HA H 4.126 0.05 1 957 . 121 PHE HB2 H 3.249 0.05 2 958 . 121 PHE HB3 H 2.936 0.05 2 959 . 121 PHE HE1 H 6.485 0.05 3 960 . 121 PHE C C 177.255 0.1 1 961 . 121 PHE CA C 61.791 0.1 1 962 . 121 PHE CB C 39.356 0.3 1 963 . 121 PHE N N 120.925 0.05 1 964 . 122 TYR H H 7.413 0.02 1 965 . 122 TYR HA H 4.188 0.05 1 966 . 122 TYR HB2 H 3.495 0.05 2 967 . 122 TYR HB3 H 2.948 0.05 2 968 . 122 TYR C C 178.898 0.1 1 969 . 122 TYR CA C 61.970 0.1 1 970 . 122 TYR CB C 39.915 0.3 1 971 . 122 TYR N N 114.936 0.05 1 972 . 123 THR H H 9.730 0.02 1 973 . 123 THR HA H 4.210 0.05 1 974 . 123 THR HB H 4.732 0.05 1 975 . 123 THR HG2 H 1.470 0.05 1 976 . 123 THR C C 177.902 0.1 1 977 . 123 THR CA C 66.916 0.1 1 978 . 123 THR CB C 66.480 0.1 1 979 . 123 THR CG2 C 22.595 0.1 1 980 . 123 THR N N 115.420 0.05 1 981 . 124 ASN H H 9.013 0.02 1 982 . 124 ASN HA H 4.644 0.05 1 983 . 124 ASN HB2 H 2.711 0.05 2 984 . 124 ASN HB3 H 2.955 0.05 2 985 . 124 ASN HD21 H 7.161 0.05 2 986 . 124 ASN HD22 H 7.476 0.05 2 987 . 124 ASN C C 178.456 0.1 1 988 . 124 ASN CA C 56.135 0.1 1 989 . 124 ASN CB C 37.401 0.3 1 990 . 124 ASN N N 121.920 0.05 1 991 . 124 ASN ND2 N 113.801 0.05 1 992 . 125 ARG H H 6.904 0.02 1 993 . 125 ARG HA H 4.020 0.05 1 994 . 125 ARG HB2 H 1.961 0.05 2 995 . 125 ARG HB3 H 2.149 0.05 2 996 . 125 ARG HG2 H 1.537 0.05 2 997 . 125 ARG HG3 H 1.753 0.05 2 998 . 125 ARG C C 178.409 0.1 1 999 . 125 ARG CA C 59.574 0.1 1 1000 . 125 ARG CB C 30.3 0.3 1 1001 . 125 ARG N N 120.64 0.05 1 1002 . 126 ILE H H 7.644 0.02 1 1003 . 126 ILE HA H 4.282 0.05 1 1004 . 126 ILE HB H 2.244 0.05 1 1005 . 126 ILE HG2 H 1.093 0.05 1 1006 . 126 ILE HD1 H 0.828 0.05 1 1007 . 126 ILE C C 178.20 0.1 1 1008 . 126 ILE CA C 65.083 0.1 1 1009 . 126 ILE CB C 38.679 0.3 1 1010 . 126 ILE CG2 C 19.139 0.1 2 1011 . 126 ILE N N 123.198 0.05 1 1012 . 127 LEU H H 8.490 0.02 1 1013 . 127 LEU HA H 3.777 0.05 1 1014 . 127 LEU HB2 H 2.291 0.05 2 1015 . 127 LEU C C 178.717 0.1 1 1016 . 127 LEU CA C 58.124 0.1 1 1017 . 127 LEU CB C 41.666 0.3 1 1018 . 127 LEU N N 119.405 0.05 1 1019 . 128 LYS H H 7.712 0.02 1 1020 . 128 LYS HA H 4.010 0.05 1 1021 . 128 LYS HB2 H 1.944 0.05 2 1022 . 128 LYS HG2 H 1.539 0.05 2 1023 . 128 LYS HE2 H 3.013 0.05 2 1024 . 128 LYS C C 177.910 0.1 1 1025 . 128 LYS CA C 59.165 0.1 1 1026 . 128 LYS CB C 32.223 0.3 1 1027 . 128 LYS N N 119.161 0.05 1 1028 . 129 GLU H H 7.533 0.02 1 1029 . 129 GLU HA H 3.892 0.05 1 1030 . 129 GLU HB2 H 1.515 0.05 2 1031 . 129 GLU HB3 H 1.773 0.05 2 1032 . 129 GLU C C 177.864 0.1 1 1033 . 129 GLU CA C 58.673 0.1 1 1034 . 129 GLU CB C 30.332 0.3 1 1035 . 129 GLU N N 118.213 0.05 1 1036 . 130 PHE H H 8.368 0.02 1 1037 . 130 PHE HA H 4.894 0.05 1 1038 . 130 PHE HB2 H 2.847 0.05 2 1039 . 130 PHE HB3 H 3.621 0.05 2 1040 . 130 PHE C C 176.985 0.1 1 1041 . 130 PHE CA C 59.674 0.1 1 1042 . 130 PHE CB C 40.645 0.3 1 1043 . 130 PHE N N 112.505 0.05 1 1044 . 131 LYS H H 8.674 0.02 1 1045 . 131 LYS HA H 4.111 0.05 1 1046 . 131 LYS HB2 H 1.548 0.05 2 1047 . 131 LYS HB3 H 2.031 0.05 2 1048 . 131 LYS C C 177.421 0.1 1 1049 . 131 LYS CA C 59.684 0.1 1 1050 . 131 LYS CB C 31.406 0.3 1 1051 . 131 LYS N N 126.084 0.05 1 1052 . 132 GLY H H 8.939 0.02 1 1053 . 132 GLY HA2 H 4.279 0.05 2 1054 . 132 GLY HA3 H 3.837 0.05 2 1055 . 132 GLY C C 174.229 0.1 1 1056 . 132 GLY CA C 45.743 0.1 1 1057 . 132 GLY N N 116.744 0.05 1 1058 . 133 VAL H H 8.179 0.02 1 1059 . 133 VAL HA H 4.377 0.05 1 1060 . 133 VAL HB H 2.122 0.05 1 1061 . 133 VAL HG1 H 1.000 0.05 2 1062 . 133 VAL HG2 H 1.189 0.05 2 1063 . 133 VAL C C 175.801 0.1 1 1064 . 133 VAL CA C 63.638 0.1 1 1065 . 133 VAL CB C 35.220 0.3 1 1066 . 133 VAL N N 119.830 0.05 1 1067 . 134 ASN H H 8.543 0.02 1 1068 . 134 ASN HA H 5.065 0.05 1 1069 . 134 ASN HB3 H 2.932 0.05 2 1070 . 134 ASN C C 174.745 0.1 1 1071 . 134 ASN CA C 52.457 0.1 1 1072 . 134 ASN CB C 40.388 0.3 1 1073 . 134 ASN N N 118.614 0.05 1 1074 . 135 GLN H H 9.018 0.02 1 1075 . 135 GLN HA H 3.930 0.05 1 1076 . 135 GLN HB2 H 2.291 0.05 2 1077 . 135 GLN HB3 H 2.747 0.05 2 1078 . 135 GLN C C 176.762 0.1 1 1079 . 135 GLN CA C 57.330 0.1 1 1080 . 135 GLN CB C 28.463 0.3 1 1081 . 135 GLN N N 127.879 0.05 1 1082 . 136 ASP H H 7.984 0.02 1 1083 . 136 ASP HA H 4.383 0.05 1 1084 . 136 ASP HB2 H 2.425 0.05 2 1085 . 136 ASP HB3 H 2.945 0.05 2 1086 . 136 ASP C C 178.318 0.1 1 1087 . 136 ASP CA C 57.848 0.1 1 1088 . 136 ASP CB C 39.593 0.3 1 1089 . 136 ASP N N 119.727 0.05 1 1090 . 137 GLN H H 7.201 0.02 1 1091 . 137 GLN HA H 4.367 0.05 1 1092 . 137 GLN HB2 H 1.844 0.05 2 1093 . 137 GLN HB3 H 1.674 0.05 2 1094 . 137 GLN HE21 H 6.073 0.05 2 1095 . 137 GLN C C 177.606 0.1 1 1096 . 137 GLN CA C 59.004 0.1 1 1097 . 137 GLN CB C 28.688 0.3 1 1098 . 137 GLN N N 117.279 0.05 1 1099 . 137 GLN NE2 N 106.538 0.05 1 1100 . 138 VAL H H 6.907 0.02 1 1101 . 138 VAL HA H 3.565 0.05 1 1102 . 138 VAL HB H 2.301 0.05 1 1103 . 138 VAL HG1 H 1.096 0.05 2 1104 . 138 VAL HG2 H 1.163 0.05 2 1105 . 138 VAL C C 178.261 0.1 1 1106 . 138 VAL CA C 66.636 0.1 1 1107 . 138 VAL CB C 31.481 0.3 1 1108 . 138 VAL N N 119.102 0.05 1 1109 . 139 ASP H H 8.888 0.02 1 1110 . 139 ASP HA H 4.490 0.05 1 1111 . 139 ASP HB2 H 2.755 0.05 2 1112 . 139 ASP HB3 H 2.916 0.05 2 1113 . 139 ASP C C 177.704 0.1 1 1114 . 139 ASP CA C 57.321 0.1 1 1115 . 139 ASP CB C 40.345 0.3 1 1116 . 139 ASP N N 122.560 0.05 1 1117 . 140 TRP H H 8.574 0.02 1 1118 . 140 TRP HA H 4.093 0.05 1 1119 . 140 TRP HB2 H 3.906 0.05 2 1120 . 140 TRP HB3 H 3.417 0.05 2 1121 . 140 TRP HE1 H 9.107 0.05 1 1122 . 140 TRP C C 177.147 0.1 1 1123 . 140 TRP CA C 63.988 0.1 1 1124 . 140 TRP CB C 29.344 0.3 1 1125 . 140 TRP N N 125.972 0.05 1 1126 . 140 TRP NE1 N 132.523 0.05 1 1127 . 141 VAL H H 8.220 0.02 1 1128 . 141 VAL HA H 3.571 0.05 1 1129 . 141 VAL HB H 2.673 0.05 1 1130 . 141 VAL HG1 H 1.191 0.05 2 1131 . 141 VAL HG2 H 1.634 0.05 2 1132 . 141 VAL C C 177.209 0.1 1 1133 . 141 VAL CA C 67.780 0.1 1 1134 . 141 VAL CB C 32.072 0.3 1 1135 . 141 VAL CG1 C 22.595 0.1 2 1136 . 141 VAL CG2 C 24.293 0.1 2 1137 . 141 VAL N N 117.702 0.05 1 1138 . 142 SER H H 8.313 0.02 1 1139 . 142 SER HA H 4.098 0.05 1 1140 . 142 SER HB3 H 4.001 0.05 2 1141 . 142 SER C C 177.554 0.1 1 1142 . 142 SER CA C 61.740 0.1 1 1143 . 142 SER CB C 63.421 0.3 1 1144 . 142 SER N N 113.762 0.05 1 1145 . 143 ASN H H 8.157 0.02 1 1146 . 143 ASN HA H 4.628 0.05 1 1147 . 143 ASN HB2 H 2.732 0.05 2 1148 . 143 ASN HB3 H 3.145 0.05 2 1149 . 143 ASN C C 176.361 0.1 1 1150 . 143 ASN CA C 56.738 0.1 1 1151 . 143 ASN CB C 39.808 0.3 1 1152 . 143 ASN N N 118.388 0.05 1 1153 . 144 TYR H H 7.287 0.02 1 1154 . 144 TYR HA H 3.413 0.05 1 1155 . 144 TYR HB2 H 2.202 0.05 2 1156 . 144 TYR HB3 H 2.101 0.05 2 1157 . 144 TYR HE1 H 6.132 0.05 3 1158 . 144 TYR C C 176.792 0.1 1 1159 . 144 TYR CA C 61.613 0.1 1 1160 . 144 TYR CB C 38.024 0.3 1 1161 . 144 TYR N N 119.866 0.05 1 1162 . 145 VAL H H 8.417 0.02 1 1163 . 145 VAL HA H 3.084 0.05 1 1164 . 145 VAL HB H 2.034 0.05 1 1165 . 145 VAL HG1 H 0.884 0.05 2 1166 . 145 VAL HG2 H 1.092 0.05 2 1167 . 145 VAL C C 177.862 0.1 1 1168 . 145 VAL CA C 67.454 0.1 1 1169 . 145 VAL CB C 31.234 0.3 1 1170 . 145 VAL N N 117.103 0.05 1 1171 . 146 ASN H H 8.357 0.02 1 1172 . 146 ASN HA H 4.164 0.05 1 1173 . 146 ASN HB2 H 2.850 0.05 2 1174 . 146 ASN HB3 H 2.251 0.05 2 1175 . 146 ASN HD21 H 7.692 0.05 2 1176 . 146 ASN C C 177.290 0.1 1 1177 . 146 ASN CA C 55.689 0.1 1 1178 . 146 ASN CB C 37.122 0.3 1 1179 . 146 ASN N N 118.276 0.05 1 1180 . 146 ASN ND2 N 112.775 0.05 1 1181 . 147 PHE H H 7.429 0.02 1 1182 . 147 PHE HA H 3.485 0.05 1 1183 . 147 PHE HB2 H 2.779 0.05 2 1184 . 147 PHE HB3 H 2.889 0.05 2 1185 . 147 PHE C C 175.795 0.1 1 1186 . 147 PHE CA C 61.557 0.1 1 1187 . 147 PHE CB C 37.423 0.3 1 1188 . 147 PHE N N 121.987 0.05 1 1189 . 148 LEU H H 7.235 0.02 1 1190 . 148 LEU HA H 3.201 0.05 1 1191 . 148 LEU HB2 H 0.761 0.05 2 1192 . 148 LEU HB3 H 1.516 0.05 2 1193 . 148 LEU HG H 0.931 0.05 1 1194 . 148 LEU HD1 H -0.266 0.05 2 1195 . 148 LEU HD2 H 0.295 0.05 2 1196 . 148 LEU C C 177.3 0.1 1 1197 . 148 LEU CA C 57.542 0.1 1 1198 . 148 LEU CB C 41.784 0.3 1 1199 . 148 LEU CD1 C 20.827 0.1 2 1200 . 148 LEU CD2 C 25.054 0.1 2 1201 . 148 LEU N N 118.175 0.05 1 1202 . 149 LYS H H 8.308 0.02 1 1203 . 149 LYS HA H 4.425 0.05 1 1204 . 149 LYS C C 178.880 0.1 1 1205 . 149 LYS CA C 60.441 0.1 1 1206 . 149 LYS CB C 32.438 0.3 1 1207 . 149 LYS N N 122.049 0.05 1 1208 . 150 ASP H H 8.286 0.02 1 1209 . 150 ASP HA H 4.556 0.05 1 1210 . 150 ASP HB2 H 2.624 0.05 2 1211 . 150 ASP HB3 H 1.989 0.05 2 1212 . 150 ASP C C 178.835 0.1 1 1213 . 150 ASP CA C 56.584 0.1 1 1214 . 150 ASP CB C 39.249 0.3 1 1215 . 150 ASP N N 122.986 0.05 1 1216 . 151 LEU H H 8.852 0.02 1 1217 . 151 LEU HA H 3.938 0.05 1 1218 . 151 LEU HG H 1.523 0.05 1 1219 . 151 LEU HD1 H 0.623 0.05 2 1220 . 151 LEU HD2 H 0.977 0.05 2 1221 . 151 LEU C C 177.6 0.1 1 1222 . 151 LEU CA C 57.441 0.1 1 1223 . 151 LEU CB C 40.205 0.3 1 1224 . 151 LEU CD1 C 25.753 0.1 2 1225 . 151 LEU N N 126.639 0.05 1 1226 . 152 GLU H H 7.51 0.02 1 1227 . 152 GLU HA H 3.610 0.05 1 1228 . 152 GLU HB2 H 1.902 0.05 2 1229 . 152 GLU HB3 H 2.105 0.05 2 1230 . 152 GLU HG2 H 2.309 0.05 2 1231 . 152 GLU C C 177.425 0.1 1 1232 . 152 GLU CA C 60.348 0.1 1 1233 . 152 GLU CB C 29.440 0.3 1 1234 . 152 GLU N N 121.179 0.05 1 1235 . 153 LYS H H 7.238 0.02 1 1236 . 153 LYS HA H 3.896 0.05 1 1237 . 153 LYS HB2 H 1.656 0.05 2 1238 . 153 LYS HB3 H 1.988 0.05 2 1239 . 153 LYS HG2 H 1.429 0.05 2 1240 . 153 LYS HD2 H 1.669 0.05 2 1241 . 153 LYS C C 177.939 0.1 1 1242 . 153 LYS CA C 60.212 0.1 1 1243 . 153 LYS CB C 32.470 0.3 1 1244 . 153 LYS N N 119.686 0.05 1 1245 . 154 TYR H H 8.322 0.02 1 1246 . 154 TYR HA H 4.420 0.05 1 1247 . 154 TYR HB3 H 3.432 0.05 2 1248 . 154 TYR C C 176.936 0.1 1 1249 . 154 TYR CA C 61.271 0.1 1 1250 . 154 TYR CB C 38.357 0.3 1 1251 . 154 TYR N N 124.041 0.05 1 1252 . 155 ILE H H 8.475 0.02 1 1253 . 155 ILE HA H 2.984 0.05 1 1254 . 155 ILE HB H 1.561 0.05 1 1255 . 155 ILE HG12 H -0.804 0.05 2 1256 . 155 ILE HG13 H 1.253 0.05 2 1257 . 155 ILE HG2 H 0.577 0.05 1 1258 . 155 ILE HD1 H -0.108 0.05 1 1259 . 155 ILE C C 177.556 0.1 1 1260 . 155 ILE CA C 65.533 0.1 1 1261 . 155 ILE CB C 38.615 0.3 1 1262 . 155 ILE CG1 C 28.933 0.1 2 1263 . 155 ILE CG2 C 17.846 0.1 2 1264 . 155 ILE CD1 C 16.767 0.1 1 1265 . 155 ILE N N 123.426 0.05 1 1266 . 156 LYS H H 7.979 0.02 1 1267 . 156 LYS HA H 3.843 0.05 1 1268 . 156 LYS HB2 H 1.920 0.05 2 1269 . 156 LYS HG2 H 1.471 0.05 2 1270 . 156 LYS HD2 H 1.662 0.05 2 1271 . 156 LYS C C 177.964 0.1 1 1272 . 156 LYS CA C 60.050 0.1 1 1273 . 156 LYS CB C 31.782 0.3 1 1274 . 156 LYS N N 118.659 0.05 1 1275 . 157 GLN H H 7.666 0.02 1 1276 . 157 GLN HA H 3.971 0.05 1 1277 . 157 GLN C C 176.987 0.1 1 1278 . 157 GLN CA C 58.162 0.1 1 1279 . 157 GLN CB C 28.946 0.3 1 1280 . 157 GLN N N 119.245 0.05 1 1281 . 158 TYR H H 7.940 0.02 1 1282 . 158 TYR HA H 4.233 0.05 1 1283 . 158 TYR HB2 H 2.318 0.05 2 1284 . 158 TYR HB3 H 1.716 0.05 2 1285 . 158 TYR C C 175.640 0.1 1 1286 . 158 TYR CA C 60.130 0.1 1 1287 . 158 TYR CB C 39.990 0.3 1 1288 . 158 TYR N N 115.134 0.05 1 1289 . 159 HIS H H 8.534 0.02 1 1290 . 159 HIS HA H 4.985 0.05 1 1291 . 159 HIS HB2 H 3.507 0.05 2 1292 . 159 HIS HB3 H 2.570 0.05 2 1293 . 159 HIS C C 176.615 0.1 1 1294 . 159 HIS CA C 54.178 0.1 1 1295 . 159 HIS CB C 32.943 0.3 1 1296 . 159 HIS N N 121.458 0.05 1 1297 . 160 THR H H 7.284 0.02 1 1298 . 160 THR HA H 3.694 0.05 1 1299 . 160 THR HB H 4.036 0.05 1 1300 . 160 THR HG2 H 1.446 0.05 1 1301 . 160 THR C C 176.155 0.1 1 1302 . 160 THR CA C 68.492 0.1 1 1303 . 160 THR CB C 70.114 0.3 1 1304 . 160 THR N N 113.903 0.05 1 1305 . 161 THR H H 8.161 0.02 1 1306 . 161 THR HA H 5.278 0.05 1 1307 . 161 THR HB H 4.863 0.05 1 1308 . 161 THR HG2 H 1.330 0.05 1 1309 . 161 THR C C 174.601 0.1 1 1310 . 161 THR CA C 60.122 0.1 1 1311 . 161 THR CB C 68.524 0.3 1 1312 . 161 THR CG2 C 21.904 0.1 1 1313 . 161 THR N N 107.226 0.05 1 1314 . 162 GLY H H 7.674 0.02 1 1315 . 162 GLY HA2 H 4.703 0.05 2 1316 . 162 GLY HA3 H 3.945 0.05 2 1317 . 162 GLY C C 173.474 0.1 1 1318 . 162 GLY CA C 43.994 0.1 1 1319 . 162 GLY N N 111.699 0.05 1 1320 . 163 LEU H H 8.894 0.02 1 1321 . 163 LEU HA H 4.245 0.05 1 1322 . 163 LEU HB2 H 1.898 0.05 2 1323 . 163 LEU HB3 H 1.117 0.05 2 1324 . 163 LEU HG H 0.671 0.05 1 1325 . 163 LEU HD1 H 0.347 0.05 2 1326 . 163 LEU HD2 H 0.322 0.05 2 1327 . 163 LEU C C 176.467 0.1 1 1328 . 163 LEU CA C 56.194 0.1 1 1329 . 163 LEU CB C 42.354 0.3 1 1330 . 163 LEU CD1 C 24.520 0.3 1 1331 . 163 LEU N N 124.062 0.05 1 1332 . 164 THR H H 10.375 0.02 1 1333 . 164 THR HA H 4.164 0.05 1 1334 . 164 THR HB H 4.298 0.05 1 1335 . 164 THR HG2 H 1.400 0.05 1 1336 . 164 THR C C 174.340 0.1 1 1337 . 164 THR CA C 64.671 0.1 1 1338 . 164 THR CB C 69.212 0.3 1 1339 . 164 THR N N 129.322 0.05 1 1340 . 165 TRP H H 8.158 0.02 1 1341 . 165 TRP HA H 5.125 0.05 1 1342 . 165 TRP HB2 H 3.719 0.05 2 1343 . 165 TRP HB3 H 2.938 0.05 2 1344 . 165 TRP HE1 H 10.360 0.05 1 1345 . 165 TRP C C 175.853 0.1 1 1346 . 165 TRP CA C 56.780 0.1 1 1347 . 165 TRP CB C 29.677 0.3 1 1348 . 165 TRP N N 130.840 0.05 1 1349 . 165 TRP NE1 N 130.786 0.05 1 1350 . 166 ASN H H 8.777 0.02 1 1351 . 166 ASN HA H 5.245 0.05 1 1352 . 166 ASN HB2 H 2.874 0.05 2 1353 . 166 ASN HB3 H 2.710 0.05 2 1354 . 166 ASN CA C 49.653 0.1 1 1355 . 166 ASN CB C 39.403 0.1 1 1356 . 166 ASN N N 121.099 0.05 1 1357 . 167 PRO HA H 5.242 0.05 1 1358 . 167 PRO HB2 H 2.357 0.05 2 1359 . 167 PRO HB3 H 2.570 0.05 2 1360 . 167 PRO HG3 H 2.198 0.05 2 1361 . 167 PRO C C 177.480 0.1 1 1362 . 167 PRO CA C 64.399 0.1 1 1363 . 167 PRO CB C 32.298 0.3 1 1364 . 168 LYS H H 7.716 0.02 1 1365 . 168 LYS HA H 4.555 0.05 1 1366 . 168 LYS HB2 H 2.149 0.05 2 1367 . 168 LYS HB3 H 1.753 0.05 2 1368 . 168 LYS HG2 H 1.459 0.05 2 1369 . 168 LYS C C 176.938 0.1 1 1370 . 168 LYS CA C 55.176 0.1 1 1371 . 168 LYS CB C 31.847 0.3 1 1372 . 168 LYS N N 117.196 0.05 1 1373 . 169 GLY H H 7.976 0.02 1 1374 . 169 GLY HA2 H 3.573 0.05 2 1375 . 169 GLY HA3 H 4.253 0.05 2 1376 . 169 GLY C C 173.879 0.1 1 1377 . 169 GLY CA C 44.400 0.1 1 1378 . 169 GLY N N 109.825 0.05 1 1379 . 170 GLY H H 7.984 0.02 1 1380 . 170 GLY HA2 H 3.887 0.05 2 1381 . 170 GLY HA3 H 4.514 0.05 2 1382 . 170 GLY C C 173.963 0.1 1 1383 . 170 GLY CA C 44.314 0.1 1 1384 . 170 GLY N N 106.896 0.05 1 1385 . 171 ASP H H 8.343 0.02 1 1386 . 171 ASP HA H 4.806 0.05 1 1387 . 171 ASP HB2 H 2.739 0.05 2 1388 . 171 ASP HB3 H 2.569 0.05 2 1389 . 171 ASP C C 177.287 0.1 1 1390 . 171 ASP CA C 54.040 0.1 1 1391 . 171 ASP CB C 41.902 0.3 1 1392 . 171 ASP N N 120.195 0.05 1 1393 . 172 ALA H H 9.461 0.02 1 1394 . 172 ALA HA H 4.372 0.05 1 1395 . 172 ALA HB H 1.468 0.05 1 1396 . 172 ALA C C 177.346 0.1 1 1397 . 172 ALA CA C 53.495 0.1 1 1398 . 172 ALA CB C 18.869 0.3 1 1399 . 172 ALA N N 130.180 0.05 1 1400 . 173 LYS H H 8.273 0.02 1 1401 . 173 LYS HA H 4.324 0.05 1 1402 . 173 LYS HB2 H 1.785 0.05 2 1403 . 173 LYS HB3 H 1.922 0.05 2 1404 . 173 LYS HG2 H 0.936 0.05 2 1405 . 173 LYS HG3 H 1.164 0.05 2 1406 . 173 LYS C C 180.379 0.1 1 1407 . 173 LYS CA C 56.451 0.1 1 1408 . 173 LYS CB C 33.157 0.3 1 1409 . 173 LYS N N 118.737 0.05 1 1410 . 174 SER H H 8.173 0.02 1 1411 . 174 SER HA H 4.469 0.05 1 1412 . 174 SER HB2 H 4.328 0.05 2 1413 . 174 SER HB3 H 3.952 0.05 2 1414 . 174 SER C C 174.517 0.1 1 1415 . 174 SER CA C 58.338 0.1 1 1416 . 174 SER CB C 63.776 0.3 1 1417 . 174 SER N N 117.133 0.05 1 1418 . 175 ALA H H 8.072 0.02 1 1419 . 175 ALA HA H 4.451 0.05 1 1420 . 175 ALA HB H 1.485 0.05 1 1421 . 175 ALA C C 176.862 0.1 1 1422 . 175 ALA CA C 52.623 0.1 1 1423 . 175 ALA CB C 19.385 0.3 1 1424 . 175 ALA N N 127.342 0.05 1 1425 . 176 THR H H 7.765 0.02 1 1426 . 176 THR HA H 4.196 0.05 1 1427 . 176 THR HG2 H 1.212 0.05 1 1428 . 176 THR CA C 63.099 0.1 1 1429 . 176 THR N N 119.501 0.05 1 stop_ save_