data_5704 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N assignment of mth677 protein from Methanobacterium Thermoautotrophicum ; _BMRB_accession_number 5704 _BMRB_flat_file_name bmr5704.str _Entry_type original _Submission_date 2003-02-17 _Accession_date 2003-02-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Assignment of the hypothetical protein mth677, part of an archaeal conserved region and a target within the pilot project on structural genomics. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blanco Francisco J . 2 Campos-Olivas Ramon . . 3 Yee Adelinda . . 4 Arrowsmith Cheryl H . 5 Rico Manuel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 487 "13C chemical shifts" 414 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-09 original author . stop_ _Original_release_date 2003-06-09 save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 15N and 13C resonance assignment of the hypothetical protein mth677from Mthanobacterium thermoautotrophicum ; _Citation_status 'in preparation' _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 Blanco Francisco J . 2 Campos-Olivas Ramon . . 3 Yee Adelinda . . 4 Arrowsmith Cheryl H . 5 Rico Manuel . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name mth677 _Abbreviation_common mth677 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label mth677 $mth677 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_mth677 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mth677 _Abbreviation_common mth677 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; GSHMSLRKLTEGDLDEISSF LHNTISDFILKRVSAKEIVD IDITVLVEYTDELKVDISAE LYLDELSDADPGIVDEAVDA AYRSLESFLDGFRE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 SER 6 3 LEU 7 4 ARG 8 5 LYS 9 6 LEU 10 7 THR 11 8 GLU 12 9 GLY 13 10 ASP 14 11 LEU 15 12 ASP 16 13 GLU 17 14 ILE 18 15 SER 19 16 SER 20 17 PHE 21 18 LEU 22 19 HIS 23 20 ASN 24 21 THR 25 22 ILE 26 23 SER 27 24 ASP 28 25 PHE 29 26 ILE 30 27 LEU 31 28 LYS 32 29 ARG 33 30 VAL 34 31 SER 35 32 ALA 36 33 LYS 37 34 GLU 38 35 ILE 39 36 VAL 40 37 ASP 41 38 ILE 42 39 ASP 43 40 ILE 44 41 THR 45 42 VAL 46 43 LEU 47 44 VAL 48 45 GLU 49 46 TYR 50 47 THR 51 48 ASP 52 49 GLU 53 50 LEU 54 51 LYS 55 52 VAL 56 53 ASP 57 54 ILE 58 55 SER 59 56 ALA 60 57 GLU 61 58 LEU 62 59 TYR 63 60 LEU 64 61 ASP 65 62 GLU 66 63 LEU 67 64 SER 68 65 ASP 69 66 ALA 70 67 ASP 71 68 PRO 72 69 GLY 73 70 ILE 74 71 VAL 75 72 ASP 76 73 GLU 77 74 ALA 78 75 VAL 79 76 ASP 80 77 ALA 81 78 ALA 82 79 TYR 83 80 ARG 84 81 SER 85 82 LEU 86 83 GLU 87 84 SER 88 85 PHE 89 86 LEU 90 87 ASP 91 88 GLY 92 89 PHE 93 90 ARG 94 91 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1PU1 "Solution Structure Of The Hypothetical Protein Mth677 From Methanothermobacter Thermautotrophicus" 100.00 94 100.00 100.00 8.09e-57 DBJ BAM69854 "conserved hypothetical protein [Methanothermobacter thermautotrophicus CaT2]" 96.81 91 100.00 100.00 4.94e-54 GB AAB85182 "unknown [Methanothermobacter thermautotrophicus str. Delta H]" 96.81 91 100.00 100.00 4.94e-54 REF NP_275819 "hypothetical protein MTH677 [Methanothermobacter thermautotrophicus str. Delta H]" 96.81 91 100.00 100.00 4.94e-54 REF WP_010876315 "hypothetical protein [Methanothermobacter thermautotrophicus]" 96.81 91 100.00 100.00 4.94e-54 SP O26773 "RecName: Full=Uncharacterized protein MTH_677 [Methanothermobacter thermautotrophicus str. Delta H]" 96.81 91 100.00 100.00 4.94e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $mth677 'Methanobacterium thermoautotrophicum' 187420 Archaea Euryarchaeota Methanothermobacter thermoautotrophicus 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 $mth677 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Uniformly 15N enrichment, and with protease inhibitor mixture.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mth677 1.2 mM [U-15N] 'Sodium phosphate' 25 mM . 'Sodim chloride' 450 mM . DTT 10 mM . benzamidine 1 mM . H2O 90 '% v/v' . D2O 10 '% v/v' . 'Zinc chloride' 20 uM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Uniformly 15N and 13C enrichment, and with protease inhibitor mixture.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mth677 1 mM '[U-15N; U-13C]' 'Sodium phosphate' 25 mM . 'Sodim chloride' 450 mM . DTT 10 mM . benzamidine 1 mM . H2O 90 '% v/v' . D2O 10 '% v/v' . 'Zinc chloride' 20 uM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details 'Uniformly 15N and 13C enrichment, and with protease inhibitor mixture.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mth677 1 mM '[U-15N; U-13C]' 'Sodium phosphate' 25 mM . 'Sodim chloride' 450 mM . DTT 10 mM . benzamidine 1 mM . D2O 100 '% v/v' . 'Zinc chloride' 20 uM . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.1 loop_ _Vendor _Address _Electronic_address Bruker . www.bruker.de stop_ loop_ _Task acquisition plotting processing stop_ _Details . save_ save_nmrPipe _Saveframe_category software _Name NMRPipe _Version 97.027.12.56 loop_ _Task 'data processing' stop_ _Details . save_ save_nmrDraw _Saveframe_category software _Name NMRDraw _Version 2.2 loop_ _Task 'processing and analysis' 'spectral visualization' stop_ _Details . save_ save_nmrview _Saveframe_category software _Name NMRView _Version 5.0.3 loop_ _Task 'spectra analysis' 'spectra visualization' stop_ _Details . save_ save_cyana _Saveframe_category software _Name CYANA _Version 1.0.5 loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.0 0.1 n/a temperature 298 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 C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.101329118 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 TSP N 15 'methyl protons' ppm 0.00 internal indirect . . . 0.251449530 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name mth677 _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 . 1 GLY CA C 46.258 0.1 1 2 . 1 GLY HA2 H 3.770 0.04 2 3 . 2 SER CA C 57.567 0.1 1 4 . 2 SER HA H 4.230 0.04 1 5 . 2 SER CB C 63.605 0.1 1 6 . 2 SER HB3 H 3.976 0.04 2 7 . 2 SER HB2 H 4.063 0.04 2 8 . 3 HIS CA C 55.787 0.1 1 9 . 3 HIS HA H 4.567 0.04 1 10 . 3 HIS CB C 30.248 0.1 1 11 . 3 HIS HB3 H 3.204 0.04 2 12 . 3 HIS HB2 H 3.262 0.04 2 13 . 3 HIS CD2 C 119.997 0.1 1 14 . 3 HIS HD2 H 7.211 0.04 1 15 . 3 HIS CE1 C 137.381 0.1 1 16 . 3 HIS HE1 H 8.297 0.04 1 17 . 3 HIS C C 172.181 0.1 1 18 . 4 MET N N 120.419 0.05 1 19 . 4 MET H H 8.487 0.04 1 20 . 4 MET CA C 55.752 0.1 1 21 . 4 MET HA H 4.569 0.04 1 22 . 4 MET CB C 33.765 0.1 1 23 . 4 MET HB3 H 2.012 0.04 2 24 . 4 MET HB2 H 2.079 0.04 2 25 . 4 MET CG C 32.513 0.1 1 26 . 4 MET HG3 H 2.488 0.04 2 27 . 4 MET HG2 H 2.520 0.04 2 28 . 4 MET CE C 16.907 0.1 1 29 . 4 MET HE H 2.141 0.04 1 30 . 4 MET C C 173.225 0.1 1 31 . 5 SER H H 8.555 0.04 1 32 . 5 SER CA C 58.166 0.1 1 33 . 5 SER HA H 4.550 0.04 1 34 . 5 SER CB C 63.726 0.1 1 35 . 5 SER HB2 H 3.940 0.04 2 36 . 5 SER C C 171.354 0.1 1 37 . 6 LEU N N 122.638 0.05 1 38 . 6 LEU H H 8.313 0.04 1 39 . 6 LEU CA C 55.362 0.1 1 40 . 6 LEU HA H 4.588 0.04 1 41 . 6 LEU CB C 43.294 0.1 1 42 . 6 LEU HB2 H 1.736 0.04 2 43 . 6 LEU CG C 27.220 0.1 1 44 . 6 LEU HG H 1.858 0.04 1 45 . 6 LEU CD1 C 26.597 0.1 2 46 . 6 LEU HD1 H 1.022 0.04 2 47 . 6 LEU CD2 C 24.977 0.1 2 48 . 6 LEU HD2 H 0.916 0.04 2 49 . 6 LEU C C 175.336 0.1 1 50 . 7 ARG N N 119.956 0.05 1 51 . 7 ARG H H 8.314 0.04 1 52 . 7 ARG CA C 55.727 0.1 1 53 . 7 ARG HA H 4.367 0.04 1 54 . 7 ARG CB C 30.723 0.1 1 55 . 7 ARG HB3 H 1.699 0.04 2 56 . 7 ARG HB2 H 1.854 0.04 2 57 . 7 ARG CG C 26.568 0.1 1 58 . 7 ARG HG2 H 1.397 0.04 2 59 . 7 ARG CD C 43.919 0.1 1 60 . 7 ARG HD2 H 3.091 0.04 2 61 . 7 ARG NE N 83.941 0.05 1 62 . 7 ARG HE H 7.511 0.04 1 63 . 7 ARG CZ C 156.738 0.1 1 64 . 7 ARG C C 171.359 0.1 1 65 . 8 LYS N N 117.435 0.05 1 66 . 8 LYS H H 8.046 0.04 1 67 . 8 LYS CA C 57.326 0.1 1 68 . 8 LYS HA H 4.023 0.04 1 69 . 8 LYS CB C 31.694 0.1 1 70 . 8 LYS HB2 H 1.767 0.04 2 71 . 8 LYS CG C 24.967 0.1 1 72 . 8 LYS HG3 H 1.440 0.04 2 73 . 8 LYS HG2 H 1.527 0.04 2 74 . 8 LYS CD C 29.237 0.1 1 75 . 8 LYS HD2 H 1.755 0.04 2 76 . 8 LYS CE C 42.227 0.1 1 77 . 8 LYS HE2 H 3.063 0.04 2 78 . 8 LYS C C 174.228 0.1 1 79 . 9 LEU N N 126.045 0.05 1 80 . 9 LEU H H 6.766 0.04 1 81 . 9 LEU CA C 53.911 0.1 1 82 . 9 LEU HA H 4.656 0.04 1 83 . 9 LEU CB C 42.532 0.1 1 84 . 9 LEU HB3 H 0.967 0.04 2 85 . 9 LEU HB2 H 1.044 0.04 2 86 . 9 LEU CG C 26.129 0.1 1 87 . 9 LEU HG H 1.528 0.04 1 88 . 9 LEU CD1 C 23.237 0.1 2 89 . 9 LEU HD1 H 0.522 0.04 2 90 . 9 LEU CD2 C 27.156 0.1 2 91 . 9 LEU HD2 H 0.454 0.04 2 92 . 9 LEU C C 174.636 0.1 1 93 . 10 THR N N 113.725 0.05 1 94 . 10 THR H H 9.381 0.04 1 95 . 10 THR CA C 60.018 0.1 1 96 . 10 THR HA H 4.564 0.04 1 97 . 10 THR CB C 72.218 0.1 1 98 . 10 THR HB H 4.706 0.04 1 99 . 10 THR CG2 C 21.858 0.1 1 100 . 10 THR HG2 H 1.317 0.04 1 101 . 10 THR C C 172.927 0.1 1 102 . 11 GLU N N 119.047 0.05 1 103 . 11 GLU H H 9.042 0.04 1 104 . 11 GLU CA C 60.576 0.1 1 105 . 11 GLU HA H 3.976 0.04 1 106 . 11 GLU CB C 29.441 0.1 1 107 . 11 GLU HB2 H 2.119 0.04 2 108 . 11 GLU CG C 36.838 0.1 1 109 . 11 GLU HG3 H 2.399 0.04 2 110 . 11 GLU HG2 H 2.433 0.04 2 111 . 11 GLU C C 176.462 0.1 1 112 . 12 GLY N N 106.035 0.05 1 113 . 12 GLY H H 8.446 0.04 1 114 . 12 GLY CA C 47.029 0.1 1 115 . 12 GLY HA3 H 3.933 0.04 2 116 . 12 GLY HA2 H 3.946 0.04 2 117 . 12 GLY C C 174.343 0.1 1 118 . 13 ASP N N 122.462 0.05 1 119 . 13 ASP H H 7.751 0.04 1 120 . 13 ASP CA C 57.650 0.1 1 121 . 13 ASP HA H 4.494 0.04 1 122 . 13 ASP CB C 42.147 0.1 1 123 . 13 ASP HB3 H 2.621 0.04 1 124 . 13 ASP HB2 H 3.030 0.04 1 125 . 13 ASP C C 175.679 0.1 1 126 . 14 LEU N N 117.421 0.05 1 127 . 14 LEU H H 7.997 0.04 1 128 . 14 LEU CA C 58.440 0.1 1 129 . 14 LEU HA H 3.926 0.04 1 130 . 14 LEU CB C 40.100 0.1 1 131 . 14 LEU HB3 H 1.422 0.04 1 132 . 14 LEU HB2 H 2.049 0.04 1 133 . 14 LEU CG C 26.781 0.1 1 134 . 14 LEU HG H 1.790 0.04 1 135 . 14 LEU CD1 C 25.976 0.1 2 136 . 14 LEU HD1 H 0.905 0.04 2 137 . 14 LEU CD2 C 23.316 0.1 2 138 . 14 LEU HD2 H 0.562 0.04 2 139 . 14 LEU C C 177.138 0.1 1 140 . 15 ASP N N 119.656 0.05 1 141 . 15 ASP H H 8.120 0.04 1 142 . 15 ASP CA C 57.593 0.1 1 143 . 15 ASP HA H 4.501 0.04 1 144 . 15 ASP CB C 40.906 0.1 1 145 . 15 ASP HB3 H 2.811 0.04 2 146 . 15 ASP HB2 H 2.885 0.04 2 147 . 15 ASP C C 176.415 0.1 1 148 . 16 GLU N N 121.166 0.05 1 149 . 16 GLU H H 8.089 0.04 1 150 . 16 GLU CA C 60.090 0.1 1 151 . 16 GLU HA H 4.221 0.04 1 152 . 16 GLU CB C 29.722 0.1 1 153 . 16 GLU HB3 H 2.484 0.04 2 154 . 16 GLU HB2 H 2.534 0.04 2 155 . 16 GLU CG C 36.761 0.1 1 156 . 16 GLU HG3 H 2.639 0.04 2 157 . 16 GLU HG2 H 2.672 0.04 2 158 . 16 GLU C C 177.494 0.1 1 159 . 17 ILE N N 120.395 0.05 1 160 . 17 ILE H H 8.421 0.04 1 161 . 17 ILE CA C 66.169 0.1 1 162 . 17 ILE HA H 3.678 0.04 1 163 . 17 ILE CB C 38.807 0.1 1 164 . 17 ILE HB H 1.913 0.04 1 165 . 17 ILE CG1 C 30.604 0.1 1 166 . 17 ILE HG12 H 1.875 0.04 2 167 . 17 ILE CD1 C 14.417 0.1 1 168 . 17 ILE HD1 H 0.451 0.04 1 169 . 17 ILE CG2 C 17.832 0.1 1 170 . 17 ILE HG2 H 0.841 0.04 1 171 . 17 ILE C C 174.693 0.1 1 172 . 18 SER N N 113.338 0.05 1 173 . 18 SER H H 8.506 0.04 1 174 . 18 SER CA C 62.477 0.1 1 175 . 18 SER HA H 4.075 0.04 1 176 . 18 SER CB C 62.962 0.1 1 177 . 18 SER HB2 H 4.207 0.04 2 178 . 18 SER C C 174.715 0.1 1 179 . 19 SER N N 115.786 0.05 1 180 . 19 SER H H 8.523 0.04 1 181 . 19 SER CA C 62.042 0.1 1 182 . 19 SER HA H 4.231 0.04 1 183 . 19 SER CB C 63.106 0.1 1 184 . 19 SER HB3 H 3.973 0.04 2 185 . 19 SER HB2 H 4.048 0.04 2 186 . 19 SER C C 173.555 0.1 1 187 . 20 PHE N N 121.645 0.05 1 188 . 20 PHE H H 8.247 0.04 1 189 . 20 PHE CA C 61.449 0.1 1 190 . 20 PHE HA H 4.152 0.04 1 191 . 20 PHE CB C 39.020 0.1 1 192 . 20 PHE HB3 H 2.707 0.04 2 193 . 20 PHE HB2 H 2.798 0.04 2 194 . 20 PHE CD1 C 131.776 0.1 3 195 . 20 PHE HD1 H 6.673 0.04 3 196 . 20 PHE CE1 C 130.674 0.1 3 197 . 20 PHE HE1 H 6.993 0.04 3 198 . 20 PHE CZ C 133.457 0.1 1 199 . 20 PHE HZ H 7.140 0.04 1 200 . 20 PHE C C 176.619 0.1 1 201 . 21 LEU N N 121.225 0.05 1 202 . 21 LEU H H 8.223 0.04 1 203 . 21 LEU CA C 58.194 0.1 1 204 . 21 LEU HA H 3.572 0.04 1 205 . 21 LEU CB C 42.514 0.1 1 206 . 21 LEU HB3 H 0.970 0.04 1 207 . 21 LEU HB2 H 2.128 0.04 1 208 . 21 LEU CG C 27.100 0.1 1 209 . 21 LEU HG H 2.035 0.04 1 210 . 21 LEU CD1 C 27.538 0.1 2 211 . 21 LEU HD1 H 0.780 0.04 2 212 . 21 LEU CD2 C 23.654 0.1 2 213 . 21 LEU HD2 H 0.740 0.04 2 214 . 21 LEU C C 175.321 0.1 1 215 . 22 HIS N N 117.203 0.05 1 216 . 22 HIS H H 8.443 0.04 1 217 . 22 HIS CA C 61.237 0.1 1 218 . 22 HIS HA H 3.742 0.04 1 219 . 22 HIS CB C 30.240 0.1 1 220 . 22 HIS HB2 H 3.277 0.04 2 221 . 22 HIS CD2 C 120.723 0.1 1 222 . 22 HIS HD2 H 7.136 0.04 1 223 . 22 HIS CE1 C 137.875 0.1 1 224 . 22 HIS HE1 H 8.117 0.04 1 225 . 22 HIS C C 174.945 0.1 1 226 . 23 ASN N N 116.016 0.05 1 227 . 23 ASN H H 8.543 0.04 1 228 . 23 ASN CA C 56.099 0.1 1 229 . 23 ASN HA H 4.393 0.04 1 230 . 23 ASN CB C 38.055 0.1 1 231 . 23 ASN HB2 H 2.817 0.04 2 232 . 23 ASN CG C 174.227 0.1 1 233 . 23 ASN ND2 N 112.178 0.05 1 234 . 23 ASN HD21 H 6.969 0.04 2 235 . 23 ASN HD22 H 7.612 0.04 2 236 . 23 ASN C C 174.275 0.1 1 237 . 24 THR N N 116.175 0.05 1 238 . 24 THR H H 8.088 0.04 1 239 . 24 THR CA C 67.297 0.1 1 240 . 24 THR HA H 3.762 0.04 1 241 . 24 THR CB C 68.462 0.1 1 242 . 24 THR HB H 3.638 0.04 1 243 . 24 THR CG2 C 20.547 0.1 1 244 . 24 THR HG2 H 1.020 0.04 1 245 . 24 THR C C 174.282 0.1 1 246 . 25 ILE N N 121.425 0.05 1 247 . 25 ILE H H 7.655 0.04 1 248 . 25 ILE CA C 65.872 0.1 1 249 . 25 ILE HA H 3.475 0.04 1 250 . 25 ILE CB C 38.328 0.1 1 251 . 25 ILE HB H 1.627 0.04 1 252 . 25 ILE CG1 C 30.451 0.1 1 253 . 25 ILE HG13 H 0.532 0.04 2 254 . 25 ILE HG12 H 1.659 0.04 2 255 . 25 ILE CD1 C 14.892 0.1 1 256 . 25 ILE HD1 H 0.497 0.04 1 257 . 25 ILE CG2 C 17.016 0.1 1 258 . 25 ILE HG2 H 0.575 0.04 1 259 . 25 ILE C C 174.097 0.1 1 260 . 26 SER N N 112.338 0.05 1 261 . 26 SER H H 7.839 0.04 1 262 . 26 SER CA C 62.748 0.1 1 263 . 26 SER HA H 3.828 0.04 1 264 . 26 SER CB C 64.088 0.1 1 265 . 26 SER HB2 H 3.827 0.04 2 266 . 26 SER C C 173.231 0.1 1 267 . 27 ASP N N 117.802 0.05 1 268 . 27 ASP H H 8.538 0.04 1 269 . 27 ASP CA C 57.586 0.1 1 270 . 27 ASP HA H 4.298 0.04 1 271 . 27 ASP CB C 41.236 0.1 1 272 . 27 ASP HB3 H 2.609 0.04 1 273 . 27 ASP HB2 H 2.780 0.04 1 274 . 27 ASP C C 175.245 0.1 1 275 . 28 PHE N N 117.850 0.05 1 276 . 28 PHE H H 7.661 0.04 1 277 . 28 PHE CA C 61.382 0.1 1 278 . 28 PHE HA H 3.846 0.04 1 279 . 28 PHE CB C 39.831 0.1 1 280 . 28 PHE HB3 H 3.208 0.04 1 281 . 28 PHE HB2 H 3.333 0.04 1 282 . 28 PHE CD1 C 131.890 0.1 3 283 . 28 PHE HD1 H 7.032 0.04 3 284 . 28 PHE CE1 C 132.146 0.1 3 285 . 28 PHE HE1 H 7.179 0.04 3 286 . 28 PHE CZ C 130.540 0.1 1 287 . 28 PHE HZ H 7.101 0.04 1 288 . 28 PHE C C 176.140 0.1 1 289 . 29 ILE N N 116.500 0.05 1 290 . 29 ILE H H 7.832 0.04 1 291 . 29 ILE CA C 65.845 0.1 1 292 . 29 ILE HA H 3.568 0.04 1 293 . 29 ILE CB C 38.708 0.1 1 294 . 29 ILE HB H 1.972 0.04 1 295 . 29 ILE CG1 C 29.978 0.1 1 296 . 29 ILE HG13 H 0.920 0.04 2 297 . 29 ILE HG12 H 2.074 0.04 2 298 . 29 ILE CD1 C 14.495 0.1 1 299 . 29 ILE HD1 H 0.781 0.04 1 300 . 29 ILE CG2 C 17.751 0.1 1 301 . 29 ILE HG2 H 0.847 0.04 1 302 . 29 ILE C C 175.211 0.1 1 303 . 30 LEU N N 118.419 0.05 1 304 . 30 LEU H H 8.589 0.04 1 305 . 30 LEU CA C 57.222 0.1 1 306 . 30 LEU HA H 4.445 0.04 1 307 . 30 LEU CB C 41.409 0.1 1 308 . 30 LEU HB3 H 1.542 0.04 2 309 . 30 LEU HB2 H 1.855 0.04 2 310 . 30 LEU CG C 28.103 0.1 1 311 . 30 LEU HG H 1.778 0.04 1 312 . 30 LEU CD1 C 25.254 0.1 2 313 . 30 LEU HD1 H 0.885 0.04 2 314 . 30 LEU CD2 C 23.111 0.1 2 315 . 30 LEU HD2 H 0.884 0.04 2 316 . 30 LEU C C 176.403 0.1 1 317 . 31 LYS N N 115.969 0.05 1 318 . 31 LYS H H 7.502 0.04 1 319 . 31 LYS CA C 57.722 0.1 1 320 . 31 LYS HA H 4.152 0.04 1 321 . 31 LYS CB C 33.100 0.1 1 322 . 31 LYS HB2 H 1.729 0.04 2 323 . 31 LYS CG C 25.824 0.1 1 324 . 31 LYS HG3 H 1.405 0.04 2 325 . 31 LYS HG2 H 1.494 0.04 2 326 . 31 LYS CD C 28.974 0.1 1 327 . 31 LYS HD2 H 1.556 0.04 2 328 . 31 LYS CE C 42.154 0.1 1 329 . 31 LYS HE2 H 2.913 0.04 2 330 . 31 LYS C C 175.059 0.1 1 331 . 32 ARG N N 116.763 0.05 1 332 . 32 ARG H H 7.463 0.04 1 333 . 32 ARG CA C 56.633 0.1 1 334 . 32 ARG HA H 4.291 0.04 1 335 . 32 ARG CB C 33.153 0.1 1 336 . 32 ARG HB3 H 1.550 0.04 2 337 . 32 ARG HB2 H 1.954 0.04 2 338 . 32 ARG CG C 27.822 0.1 1 339 . 32 ARG HG2 H 1.433 0.04 2 340 . 32 ARG CD C 42.609 0.1 1 341 . 32 ARG HD3 H 2.711 0.04 2 342 . 32 ARG HD2 H 2.965 0.04 2 343 . 32 ARG NE N 83.829 0.05 1 344 . 32 ARG HE H 7.166 0.04 1 345 . 32 ARG CZ C 156.489 0.1 1 346 . 32 ARG C C 172.639 0.1 1 347 . 33 VAL N N 121.102 0.05 1 348 . 33 VAL H H 8.203 0.04 1 349 . 33 VAL CA C 61.012 0.1 1 350 . 33 VAL HA H 4.164 0.04 1 351 . 33 VAL CB C 34.637 0.1 1 352 . 33 VAL HB H 1.845 0.04 1 353 . 33 VAL CG2 C 22.033 0.1 2 354 . 33 VAL HG2 H 0.841 0.04 2 355 . 33 VAL CG1 C 21.933 0.1 2 356 . 33 VAL HG1 H 0.835 0.04 2 357 . 33 VAL C C 171.113 0.1 1 358 . 34 SER N N 117.797 0.05 1 359 . 34 SER H H 8.305 0.04 1 360 . 34 SER CA C 58.421 0.1 1 361 . 34 SER HA H 4.322 0.04 1 362 . 34 SER CB C 64.172 0.1 1 363 . 34 SER HB3 H 3.806 0.04 2 364 . 34 SER HB2 H 4.006 0.04 2 365 . 34 SER C C 173.842 0.1 1 366 . 35 ALA N N 127.458 0.05 1 367 . 35 ALA H H 8.704 0.04 1 368 . 35 ALA CA C 55.540 0.1 1 369 . 35 ALA HA H 3.914 0.04 1 370 . 35 ALA CB C 18.478 0.1 1 371 . 35 ALA HB H 1.491 0.04 1 372 . 35 ALA C C 177.619 0.1 1 373 . 36 LYS N N 113.309 0.05 1 374 . 36 LYS H H 7.987 0.04 1 375 . 36 LYS CA C 57.952 0.1 1 376 . 36 LYS HA H 4.168 0.04 1 377 . 36 LYS CB C 32.301 0.1 1 378 . 36 LYS HB2 H 1.857 0.04 2 379 . 36 LYS CG C 24.949 0.1 1 380 . 36 LYS HG3 H 1.425 0.04 2 381 . 36 LYS HG2 H 1.490 0.04 2 382 . 36 LYS CD C 29.161 0.1 1 383 . 36 LYS HD2 H 1.696 0.04 2 384 . 36 LYS CE C 42.064 0.1 1 385 . 36 LYS HE2 H 3.017 0.04 2 386 . 36 LYS C C 175.122 0.1 1 387 . 37 GLU N N 116.277 0.05 1 388 . 37 GLU H H 7.833 0.04 1 389 . 37 GLU CA C 56.633 0.1 1 390 . 37 GLU HA H 4.266 0.04 1 391 . 37 GLU CB C 30.606 0.1 1 392 . 37 GLU HB2 H 2.149 0.04 2 393 . 37 GLU CG C 37.586 0.1 1 394 . 37 GLU HG3 H 2.186 0.04 2 395 . 37 GLU HG2 H 2.322 0.04 2 396 . 37 GLU C C 172.008 0.1 1 397 . 38 ILE N N 118.800 0.05 1 398 . 38 ILE H H 7.284 0.04 1 399 . 38 ILE CA C 62.249 0.1 1 400 . 38 ILE HA H 4.004 0.04 1 401 . 38 ILE CB C 37.028 0.1 1 402 . 38 ILE HB H 1.857 0.04 1 403 . 38 ILE CG1 C 27.871 0.1 1 404 . 38 ILE HG13 H 0.622 0.04 2 405 . 38 ILE HG12 H 1.761 0.04 2 406 . 38 ILE CD1 C 14.220 0.1 1 407 . 38 ILE HD1 H 0.701 0.04 1 408 . 38 ILE CG2 C 17.495 0.1 1 409 . 38 ILE HG2 H 0.706 0.04 1 410 . 38 ILE C C 173.270 0.1 1 411 . 39 VAL N N 128.672 0.05 1 412 . 39 VAL H H 9.002 0.04 1 413 . 39 VAL CA C 64.833 0.1 1 414 . 39 VAL HA H 3.938 0.04 1 415 . 39 VAL CB C 32.430 0.1 1 416 . 39 VAL HB H 1.744 0.04 1 417 . 39 VAL CG2 C 20.838 0.1 2 418 . 39 VAL HG2 H 0.882 0.04 2 419 . 39 VAL CG1 C 21.112 0.1 2 420 . 39 VAL HG1 H 0.880 0.04 2 421 . 39 VAL C C 173.949 0.1 1 422 . 40 ASP N N 115.663 0.05 1 423 . 40 ASP H H 8.070 0.04 1 424 . 40 ASP CA C 54.384 0.1 1 425 . 40 ASP HA H 4.823 0.04 1 426 . 40 ASP CB C 44.619 0.1 1 427 . 40 ASP HB3 H 2.447 0.04 2 428 . 40 ASP HB2 H 2.697 0.04 2 429 . 40 ASP C C 171.002 0.1 1 430 . 41 ILE N N 120.345 0.05 1 431 . 41 ILE H H 8.391 0.04 1 432 . 41 ILE CA C 60.866 0.1 1 433 . 41 ILE HA H 4.665 0.04 1 434 . 41 ILE CB C 40.482 0.1 1 435 . 41 ILE HB H 1.801 0.04 1 436 . 41 ILE CG1 C 28.109 0.1 1 437 . 41 ILE HG13 H 0.887 0.04 2 438 . 41 ILE HG12 H 1.638 0.04 2 439 . 41 ILE CD1 C 14.126 0.1 1 440 . 41 ILE HD1 H 0.873 0.04 1 441 . 41 ILE CG2 C 16.961 0.1 1 442 . 41 ILE HG2 H 0.810 0.04 1 443 . 41 ILE C C 171.108 0.1 1 444 . 42 ASP N N 127.222 0.05 1 445 . 42 ASP H H 8.906 0.04 1 446 . 42 ASP CA C 53.409 0.1 1 447 . 42 ASP HA H 5.016 0.04 1 448 . 42 ASP CB C 43.264 0.1 1 449 . 42 ASP HB3 H 2.572 0.04 1 450 . 42 ASP HB2 H 2.840 0.04 1 451 . 42 ASP C C 172.600 0.1 1 452 . 43 ILE N N 126.151 0.05 1 453 . 43 ILE H H 8.623 0.04 1 454 . 43 ILE CA C 61.070 0.1 1 455 . 43 ILE HA H 4.452 0.04 1 456 . 43 ILE CB C 40.796 0.1 1 457 . 43 ILE HB H 1.502 0.04 1 458 . 43 ILE CG1 C 28.026 0.1 1 459 . 43 ILE HG13 H 0.573 0.04 2 460 . 43 ILE HG12 H 1.469 0.04 2 461 . 43 ILE CD1 C 14.410 0.1 1 462 . 43 ILE HD1 H 0.570 0.04 1 463 . 43 ILE CG2 C 18.505 0.1 1 464 . 43 ILE HG2 H 0.530 0.04 1 465 . 43 ILE C C 172.462 0.1 1 466 . 44 THR N N 124.304 0.05 1 467 . 44 THR H H 9.099 0.04 1 468 . 44 THR CA C 62.394 0.1 1 469 . 44 THR HA H 4.515 0.04 1 470 . 44 THR CB C 70.376 0.1 1 471 . 44 THR HB H 3.989 0.04 1 472 . 44 THR CG2 C 21.354 0.1 1 473 . 44 THR HG2 H 1.126 0.04 1 474 . 44 THR C C 170.277 0.1 1 475 . 45 VAL N N 126.323 0.05 1 476 . 45 VAL H H 8.803 0.04 1 477 . 45 VAL CA C 61.267 0.1 1 478 . 45 VAL HA H 4.497 0.04 1 479 . 45 VAL CB C 33.888 0.1 1 480 . 45 VAL HB H 2.063 0.04 1 481 . 45 VAL CG2 C 20.963 0.1 2 482 . 45 VAL HG2 H 0.695 0.04 2 483 . 45 VAL CG1 C 22.898 0.1 2 484 . 45 VAL HG1 H 0.871 0.04 2 485 . 45 VAL C C 171.692 0.1 1 486 . 46 LEU N N 129.723 0.05 1 487 . 46 LEU H H 9.012 0.04 1 488 . 46 LEU CA C 54.055 0.1 1 489 . 46 LEU HA H 4.806 0.04 1 490 . 46 LEU CB C 43.483 0.1 1 491 . 46 LEU HB2 H 1.674 0.04 2 492 . 46 LEU CG C 27.378 0.1 1 493 . 46 LEU HG H 1.488 0.04 1 494 . 46 LEU CD1 C 24.907 0.1 2 495 . 46 LEU HD1 H 0.878 0.04 2 496 . 46 LEU CD2 C 24.267 0.1 2 497 . 46 LEU HD2 H 0.861 0.04 2 498 . 46 LEU C C 172.847 0.1 1 499 . 47 VAL N N 122.862 0.05 1 500 . 47 VAL H H 8.575 0.04 1 501 . 47 VAL CA C 60.692 0.1 1 502 . 47 VAL HA H 4.989 0.04 1 503 . 47 VAL CB C 34.218 0.1 1 504 . 47 VAL HB H 1.999 0.04 1 505 . 47 VAL CG2 C 21.850 0.1 2 506 . 47 VAL HG2 H 0.905 0.04 2 507 . 47 VAL CG1 C 23.095 0.1 2 508 . 47 VAL HG1 H 1.389 0.04 2 509 . 47 VAL C C 171.851 0.1 1 510 . 48 GLU N N 124.364 0.05 1 511 . 48 GLU H H 8.980 0.04 1 512 . 48 GLU CA C 55.025 0.1 1 513 . 48 GLU HA H 4.698 0.04 1 514 . 48 GLU CB C 34.175 0.1 1 515 . 48 GLU HB3 H 1.920 0.04 2 516 . 48 GLU HB2 H 2.050 0.04 2 517 . 48 GLU CG C 36.645 0.1 1 518 . 48 GLU HG2 H 2.171 0.04 2 519 . 48 GLU C C 171.303 0.1 1 520 . 49 TYR N N 123.801 0.05 1 521 . 49 TYR H H 9.135 0.04 1 522 . 49 TYR CA C 57.377 0.1 1 523 . 49 TYR HA H 5.494 0.04 1 524 . 49 TYR CB C 41.802 0.1 1 525 . 49 TYR HB3 H 2.636 0.04 1 526 . 49 TYR HB2 H 3.048 0.04 1 527 . 49 TYR CD1 C 133.055 0.1 3 528 . 49 TYR HD1 H 6.858 0.04 3 529 . 49 TYR CE1 C 118.200 0.1 3 530 . 49 TYR HE1 H 6.739 0.04 3 531 . 49 TYR C C 172.011 0.1 1 532 . 50 THR N N 119.542 0.05 1 533 . 50 THR H H 7.648 0.04 1 534 . 50 THR CA C 60.239 0.1 1 535 . 50 THR HA H 4.387 0.04 1 536 . 50 THR CB C 68.163 0.1 1 537 . 50 THR HB H 4.290 0.04 1 538 . 50 THR CG2 C 22.324 0.1 1 539 . 50 THR HG2 H 1.161 0.04 1 540 . 50 THR C C 170.775 0.1 1 541 . 51 ASP N N 119.275 0.05 1 542 . 51 ASP H H 8.820 0.04 1 543 . 51 ASP CA C 54.372 0.1 1 544 . 51 ASP HA H 4.398 0.04 1 545 . 51 ASP CB C 40.678 0.1 1 546 . 51 ASP HB3 H 2.635 0.04 2 547 . 51 ASP HB2 H 2.798 0.04 2 548 . 51 ASP C C 172.078 0.1 1 549 . 52 GLU N N 114.941 0.05 1 550 . 52 GLU H H 6.832 0.04 1 551 . 52 GLU CA C 54.143 0.1 1 552 . 52 GLU HA H 4.443 0.04 1 553 . 52 GLU CB C 32.570 0.1 1 554 . 52 GLU HB3 H 2.631 0.04 2 555 . 52 GLU HB2 H 1.938 0.04 2 556 . 52 GLU CG C 35.043 0.1 1 557 . 52 GLU HG3 H 1.970 0.04 2 558 . 52 GLU HG2 H 2.135 0.04 2 559 . 52 GLU C C 171.501 0.1 1 560 . 53 LEU N N 122.418 0.05 1 561 . 53 LEU H H 8.872 0.04 1 562 . 53 LEU CA C 55.393 0.1 1 563 . 53 LEU HA H 4.868 0.04 1 564 . 53 LEU CB C 43.413 0.1 1 565 . 53 LEU HB3 H 1.347 0.04 2 566 . 53 LEU HB2 H 1.968 0.04 2 567 . 53 LEU CG C 27.495 0.1 1 568 . 53 LEU HG H 1.475 0.04 1 569 . 53 LEU CD1 C 27.199 0.1 2 570 . 53 LEU HD1 H 0.828 0.04 2 571 . 53 LEU CD2 C 24.313 0.1 2 572 . 53 LEU HD2 H 0.817 0.04 2 573 . 53 LEU C C 172.750 0.1 1 574 . 54 LYS N N 128.734 0.05 1 575 . 54 LYS H H 9.239 0.04 1 576 . 54 LYS CA C 55.535 0.1 1 577 . 54 LYS HA H 4.743 0.04 1 578 . 54 LYS CB C 34.873 0.1 1 579 . 54 LYS HB3 H 1.742 0.04 2 580 . 54 LYS HB2 H 1.832 0.04 2 581 . 54 LYS CG C 24.745 0.1 1 582 . 54 LYS HG3 H 1.334 0.04 2 583 . 54 LYS HG2 H 1.417 0.04 2 584 . 54 LYS CD C 29.127 0.1 1 585 . 54 LYS HD2 H 1.645 0.04 2 586 . 54 LYS CE C 42.160 0.1 1 587 . 54 LYS HE2 H 2.920 0.04 2 588 . 54 LYS C C 172.136 0.1 1 589 . 55 VAL N N 122.371 0.05 1 590 . 55 VAL H H 8.564 0.04 1 591 . 55 VAL CA C 60.815 0.1 1 592 . 55 VAL HA H 5.014 0.04 1 593 . 55 VAL CB C 35.091 0.1 1 594 . 55 VAL HB H 2.078 0.04 1 595 . 55 VAL CG2 C 22.092 0.1 2 596 . 55 VAL HG2 H 0.814 0.04 2 597 . 55 VAL CG1 C 21.255 0.1 2 598 . 55 VAL HG1 H 0.923 0.04 2 599 . 55 VAL C C 171.881 0.1 1 600 . 56 ASP N N 127.199 0.05 1 601 . 56 ASP H H 9.067 0.04 1 602 . 56 ASP CA C 54.028 0.1 1 603 . 56 ASP HA H 5.092 0.04 1 604 . 56 ASP CB C 44.626 0.1 1 605 . 56 ASP HB3 H 2.542 0.04 2 606 . 56 ASP HB2 H 2.710 0.04 2 607 . 56 ASP C C 172.012 0.1 1 608 . 57 ILE N N 122.258 0.05 1 609 . 57 ILE H H 7.969 0.04 1 610 . 57 ILE CA C 60.514 0.1 1 611 . 57 ILE HA H 4.800 0.04 1 612 . 57 ILE CB C 41.186 0.1 1 613 . 57 ILE HB H 1.467 0.04 1 614 . 57 ILE CG1 C 27.576 0.1 1 615 . 57 ILE HG13 H 0.692 0.04 2 616 . 57 ILE HG12 H 1.429 0.04 2 617 . 57 ILE CD1 C 14.198 0.1 1 618 . 57 ILE HD1 H 0.189 0.04 1 619 . 57 ILE CG2 C 18.988 0.1 1 620 . 57 ILE HG2 H 0.157 0.04 1 621 . 57 ILE C C 172.086 0.1 1 622 . 58 SER N N 120.138 0.05 1 623 . 58 SER H H 8.802 0.04 1 624 . 58 SER CA C 57.260 0.1 1 625 . 58 SER HA H 4.676 0.04 1 626 . 58 SER CB C 65.357 0.1 1 627 . 58 SER HB3 H 3.756 0.04 2 628 . 58 SER HB2 H 3.788 0.04 2 629 . 58 SER C C 169.380 0.1 1 630 . 59 ALA N N 123.569 0.05 1 631 . 59 ALA H H 8.564 0.04 1 632 . 59 ALA CA C 51.249 0.1 1 633 . 59 ALA HA H 5.257 0.04 1 634 . 59 ALA CB C 22.192 0.1 1 635 . 59 ALA HB H 0.990 0.04 1 636 . 59 ALA C C 171.941 0.1 1 637 . 60 GLU N N 118.539 0.05 1 638 . 60 GLU H H 8.643 0.04 1 639 . 60 GLU CA C 55.209 0.1 1 640 . 60 GLU HA H 4.472 0.04 1 641 . 60 GLU CB C 33.789 0.1 1 642 . 60 GLU HB2 H 1.826 0.04 2 643 . 60 GLU CG C 36.034 0.1 1 644 . 60 GLU HG2 H 2.093 0.04 2 645 . 60 GLU C C 170.590 0.1 1 646 . 61 LEU N N 124.305 0.05 1 647 . 61 LEU H H 8.581 0.04 1 648 . 61 LEU CA C 53.531 0.1 1 649 . 61 LEU HA H 4.709 0.04 1 650 . 61 LEU CB C 46.341 0.1 1 651 . 61 LEU HB3 H 1.824 0.04 2 652 . 61 LEU HB2 H 1.816 0.04 2 653 . 61 LEU CG C 27.204 0.1 1 654 . 61 LEU HG H 1.383 0.04 1 655 . 61 LEU CD1 C 25.079 0.1 2 656 . 61 LEU HD1 H 0.943 0.04 2 657 . 61 LEU CD2 C 27.040 0.1 2 658 . 61 LEU HD2 H 0.834 0.04 2 659 . 61 LEU C C 170.992 0.1 1 660 . 62 TYR N N 125.157 0.05 1 661 . 62 TYR H H 8.735 0.04 1 662 . 62 TYR CA C 56.923 0.1 1 663 . 62 TYR HA H 4.793 0.04 1 664 . 62 TYR CB C 38.491 0.1 1 665 . 62 TYR HB3 H 2.835 0.04 1 666 . 62 TYR HB2 H 3.079 0.04 1 667 . 62 TYR CD1 C 133.274 0.1 3 668 . 62 TYR HD1 H 7.062 0.04 3 669 . 62 TYR CE1 C 118.379 0.1 3 670 . 62 TYR HE1 H 6.778 0.04 3 671 . 62 TYR C C 172.467 0.1 1 672 . 63 LEU N N 124.506 0.05 1 673 . 63 LEU H H 8.907 0.04 1 674 . 63 LEU CA C 53.443 0.1 1 675 . 63 LEU HA H 5.098 0.04 1 676 . 63 LEU CB C 45.147 0.1 1 677 . 63 LEU HB3 H 1.672 0.04 1 678 . 63 LEU HB2 H 1.834 0.04 1 679 . 63 LEU CG C 27.709 0.1 1 680 . 63 LEU HG H 1.517 0.04 1 681 . 63 LEU CD1 C 24.370 0.1 2 682 . 63 LEU HD1 H 0.852 0.04 2 683 . 63 LEU CD2 C 26.270 0.1 2 684 . 63 LEU HD2 H 0.820 0.04 2 685 . 63 LEU C C 174.566 0.1 1 686 . 64 ASP N N 120.847 0.05 1 687 . 64 ASP H H 8.703 0.04 1 688 . 64 ASP CA C 54.967 0.1 1 689 . 64 ASP HA H 4.321 0.04 1 690 . 64 ASP CB C 43.641 0.1 1 691 . 64 ASP HB3 H 2.456 0.04 2 692 . 64 ASP HB2 H 2.572 0.04 2 693 . 64 ASP C C 174.807 0.1 1 694 . 65 GLU N N 124.355 0.05 1 695 . 65 GLU H H 8.768 0.04 1 696 . 65 GLU CA C 59.309 0.1 1 697 . 65 GLU HA H 4.144 0.04 1 698 . 65 GLU CB C 29.905 0.1 1 699 . 65 GLU HB3 H 2.065 0.04 2 700 . 65 GLU HB2 H 2.108 0.04 2 701 . 65 GLU CG C 36.389 0.1 1 702 . 65 GLU HG2 H 2.360 0.04 2 703 . 65 GLU C C 174.433 0.1 1 704 . 66 LEU N N 116.897 0.05 1 705 . 66 LEU H H 8.547 0.04 1 706 . 66 LEU CA C 54.716 0.1 1 707 . 66 LEU HA H 4.415 0.04 1 708 . 66 LEU CB C 45.857 0.1 1 709 . 66 LEU HB3 H 1.651 0.04 2 710 . 66 LEU HB2 H 1.676 0.04 2 711 . 66 LEU CG C 27.317 0.1 1 712 . 66 LEU HG H 1.647 0.04 1 713 . 66 LEU CD1 C 24.111 0.1 2 714 . 66 LEU HD1 H 0.876 0.04 2 715 . 66 LEU CD2 C 23.005 0.1 2 716 . 66 LEU HD2 H 0.856 0.04 2 717 . 66 LEU C C 175.274 0.1 1 718 . 67 SER N N 112.987 0.05 1 719 . 67 SER H H 7.722 0.04 1 720 . 67 SER CA C 59.325 0.1 1 721 . 67 SER HA H 4.225 0.04 1 722 . 67 SER CB C 64.872 0.1 1 723 . 67 SER HB2 H 3.988 0.04 2 724 . 67 SER C C 173.404 0.1 1 725 . 68 ASP N N 126.707 0.05 1 726 . 68 ASP H H 8.817 0.04 1 727 . 68 ASP CA C 53.685 0.1 1 728 . 68 ASP HA H 4.911 0.04 1 729 . 68 ASP CB C 41.429 0.1 1 730 . 68 ASP HB3 H 2.724 0.04 2 731 . 68 ASP HB2 H 2.789 0.04 2 732 . 68 ASP C C 173.457 0.1 1 733 . 69 ALA N N 123.255 0.05 1 734 . 69 ALA H H 8.316 0.04 1 735 . 69 ALA CA C 52.434 0.1 1 736 . 69 ALA HA H 4.193 0.04 1 737 . 69 ALA CB C 19.602 0.1 1 738 . 69 ALA HB H 1.344 0.04 1 739 . 69 ALA C C 173.299 0.1 1 740 . 70 ASP N N 120.295 0.05 1 741 . 70 ASP H H 8.292 0.04 1 742 . 70 ASP CA C 51.173 0.1 1 743 . 70 ASP HA H 4.874 0.04 1 744 . 70 ASP CB C 42.614 0.1 1 745 . 70 ASP HB3 H 2.687 0.04 1 746 . 70 ASP HB2 H 2.884 0.04 1 747 . 70 ASP C C 173.299 0.1 1 748 . 71 PRO CA C 64.721 0.1 1 749 . 71 PRO HA H 4.274 0.04 1 750 . 71 PRO CB C 31.992 0.1 1 751 . 71 PRO HB3 H 2.082 0.04 2 752 . 71 PRO HB2 H 2.378 0.04 2 753 . 71 PRO CG C 27.585 0.1 1 754 . 71 PRO HG3 H 2.050 0.04 2 755 . 71 PRO HG2 H 2.096 0.04 2 756 . 71 PRO CD C 51.187 0.1 1 757 . 71 PRO HD3 H 3.974 0.04 2 758 . 71 PRO HD2 H 4.091 0.04 2 759 . 71 PRO C C 175.816 0.1 1 760 . 72 GLY N N 106.749 0.05 1 761 . 72 GLY H H 8.904 0.04 1 762 . 72 GLY CA C 46.407 0.1 1 763 . 72 GLY HA3 H 3.888 0.04 2 764 . 72 GLY HA2 H 4.194 0.04 2 765 . 72 GLY C C 173.264 0.1 1 766 . 73 ILE N N 120.646 0.05 1 767 . 73 ILE H H 7.947 0.04 1 768 . 73 ILE CA C 64.032 0.1 1 769 . 73 ILE HA H 4.158 0.04 1 770 . 73 ILE CB C 38.435 0.1 1 771 . 73 ILE HB H 2.018 0.04 1 772 . 73 ILE CG1 C 29.236 0.1 1 773 . 73 ILE HG13 H 1.398 0.04 2 774 . 73 ILE HG12 H 1.727 0.04 2 775 . 73 ILE CD1 C 15.338 0.1 1 776 . 73 ILE HD1 H 0.988 0.04 1 777 . 73 ILE CG2 C 18.222 0.1 1 778 . 73 ILE HG2 H 0.997 0.04 1 779 . 73 ILE C C 174.323 0.1 1 780 . 74 VAL N N 117.657 0.05 1 781 . 74 VAL H H 7.489 0.04 1 782 . 74 VAL CA C 65.829 0.1 1 783 . 74 VAL HA H 3.615 0.04 1 784 . 74 VAL CB C 31.694 0.1 1 785 . 74 VAL HB H 2.029 0.04 1 786 . 74 VAL CG2 C 23.012 0.1 2 787 . 74 VAL HG2 H 0.951 0.04 2 788 . 74 VAL CG1 C 21.656 0.1 2 789 . 74 VAL HG1 H 0.954 0.04 2 790 . 74 VAL C C 173.342 0.1 1 791 . 75 ASP N N 119.990 0.05 1 792 . 75 ASP H H 7.395 0.04 1 793 . 75 ASP CA C 57.502 0.1 1 794 . 75 ASP HA H 4.408 0.04 1 795 . 75 ASP CB C 40.389 0.1 1 796 . 75 ASP HB2 H 2.757 0.04 2 797 . 75 ASP C C 176.657 0.1 1 798 . 76 GLU N N 118.814 0.05 1 799 . 76 GLU H H 7.366 0.04 1 800 . 76 GLU CA C 59.041 0.1 1 801 . 76 GLU HA H 4.001 0.04 1 802 . 76 GLU CB C 30.097 0.1 1 803 . 76 GLU HB3 H 2.194 0.04 2 804 . 76 GLU HB2 H 2.199 0.04 2 805 . 76 GLU CG C 36.904 0.1 1 806 . 76 GLU HG3 H 2.286 0.04 2 807 . 76 GLU HG2 H 2.433 0.04 2 808 . 76 GLU C C 176.090 0.1 1 809 . 77 ALA N N 122.800 0.05 1 810 . 77 ALA H H 8.043 0.04 1 811 . 77 ALA CA C 54.225 0.1 1 812 . 77 ALA HA H 2.493 0.04 1 813 . 77 ALA CB C 19.856 0.1 1 814 . 77 ALA HB H 1.405 0.04 1 815 . 77 ALA C C 176.505 0.1 1 816 . 78 VAL N N 118.307 0.05 1 817 . 78 VAL H H 7.991 0.04 1 818 . 78 VAL CA C 67.494 0.1 1 819 . 78 VAL HA H 3.210 0.04 1 820 . 78 VAL CB C 32.013 0.1 1 821 . 78 VAL HB H 2.167 0.04 1 822 . 78 VAL CG2 C 23.558 0.1 2 823 . 78 VAL HG2 H 0.954 0.04 2 824 . 78 VAL CG1 C 22.198 0.1 2 825 . 78 VAL HG1 H 0.971 0.04 2 826 . 78 VAL C C 174.678 0.1 1 827 . 79 ASP N N 117.974 0.05 1 828 . 79 ASP H H 7.669 0.04 1 829 . 79 ASP CA C 58.083 0.1 1 830 . 79 ASP HA H 4.560 0.04 1 831 . 79 ASP CB C 41.451 0.1 1 832 . 79 ASP HB3 H 2.625 0.04 2 833 . 79 ASP HB2 H 2.746 0.04 2 834 . 79 ASP C C 176.439 0.1 1 835 . 80 ALA N N 119.815 0.05 1 836 . 80 ALA H H 7.961 0.04 1 837 . 80 ALA CA C 55.143 0.1 1 838 . 80 ALA HA H 3.982 0.04 1 839 . 80 ALA CB C 18.309 0.1 1 840 . 80 ALA HB H 1.238 0.04 1 841 . 80 ALA C C 177.796 0.1 1 842 . 81 ALA N N 122.473 0.05 1 843 . 81 ALA H H 8.034 0.04 1 844 . 81 ALA CA C 55.119 0.1 1 845 . 81 ALA HA H 3.907 0.04 1 846 . 81 ALA CB C 18.044 0.1 1 847 . 81 ALA HB H 1.283 0.04 1 848 . 81 ALA C C 176.861 0.1 1 849 . 82 TYR N N 115.649 0.05 1 850 . 82 TYR H H 8.163 0.04 1 851 . 82 TYR CA C 63.366 0.1 1 852 . 82 TYR HA H 4.195 0.04 1 853 . 82 TYR CB C 38.140 0.1 1 854 . 82 TYR HB3 H 3.064 0.04 2 855 . 82 TYR HB2 H 3.138 0.04 2 856 . 82 TYR CD1 C 133.304 0.1 3 857 . 82 TYR HD1 H 7.250 0.04 3 858 . 82 TYR CE1 C 118.370 0.1 3 859 . 82 TYR HE1 H 6.758 0.04 3 860 . 82 TYR CZ C 157.091 0.1 1 861 . 82 TYR C C 177.266 0.1 1 862 . 83 ARG N N 118.151 0.05 1 863 . 83 ARG H H 8.089 0.04 1 864 . 83 ARG CA C 59.728 0.1 1 865 . 83 ARG HA H 4.287 0.04 1 866 . 83 ARG CB C 30.271 0.1 1 867 . 83 ARG HB3 H 2.006 0.04 2 868 . 83 ARG HB2 H 2.022 0.04 2 869 . 83 ARG CG C 28.211 0.1 1 870 . 83 ARG HG3 H 1.727 0.04 2 871 . 83 ARG HG2 H 1.890 0.04 2 872 . 83 ARG CD C 43.514 0.1 1 873 . 83 ARG HD3 H 3.258 0.04 2 874 . 83 ARG HD2 H 3.327 0.04 2 875 . 83 ARG NE N 83.988 0.05 1 876 . 83 ARG HE H 7.445 0.04 1 877 . 83 ARG CZ C 157.091 0.1 1 878 . 83 ARG C C 177.293 0.1 1 879 . 84 SER H H 8.547 0.04 1 880 . 84 SER CA C 61.829 0.1 1 881 . 84 SER HA H 4.515 0.04 1 882 . 84 SER CB C 63.368 0.1 1 883 . 84 SER HB3 H 1.854 0.04 2 884 . 84 SER HB2 H 4.221 0.04 2 885 . 84 SER C C 173.833 0.1 1 886 . 85 LEU N N 122.307 0.05 1 887 . 85 LEU H H 8.401 0.04 1 888 . 85 LEU CA C 58.003 0.1 1 889 . 85 LEU HA H 4.199 0.04 1 890 . 85 LEU CB C 41.730 0.1 1 891 . 85 LEU HB3 H 1.856 0.04 2 892 . 85 LEU HB2 H 2.299 0.04 2 893 . 85 LEU CG C 26.873 0.1 1 894 . 85 LEU HG H 1.825 0.04 1 895 . 85 LEU CD1 C 26.277 0.1 2 896 . 85 LEU HD1 H 1.056 0.04 2 897 . 85 LEU CD2 C 23.826 0.1 2 898 . 85 LEU HD2 H 1.035 0.04 2 899 . 85 LEU C C 174.493 0.1 1 900 . 86 GLU N N 115.485 0.05 1 901 . 86 GLU H H 7.597 0.04 1 902 . 86 GLU CA C 60.144 0.1 1 903 . 86 GLU HA H 4.053 0.04 1 904 . 86 GLU CB C 29.461 0.1 1 905 . 86 GLU HB2 H 2.214 0.04 2 906 . 86 GLU CG C 36.152 0.1 1 907 . 86 GLU HG2 H 2.416 0.04 2 908 . 86 GLU C C 175.823 0.1 1 909 . 87 SER N N 109.949 0.05 1 910 . 87 SER H H 7.542 0.04 1 911 . 87 SER CA C 60.621 0.1 1 912 . 87 SER HA H 4.465 0.04 1 913 . 87 SER CB C 63.116 0.1 1 914 . 87 SER HB2 H 4.018 0.04 2 915 . 87 SER C C 174.712 0.1 1 916 . 88 PHE N N 124.506 0.05 1 917 . 88 PHE H H 7.997 0.04 1 918 . 88 PHE CA C 61.650 0.1 1 919 . 88 PHE HA H 4.089 0.04 1 920 . 88 PHE CB C 40.213 0.1 1 921 . 88 PHE HB2 H 2.662 0.04 2 922 . 88 PHE CD1 C 131.467 0.1 3 923 . 88 PHE HD1 H 6.576 0.04 3 924 . 88 PHE CE1 C 131.014 0.1 3 925 . 88 PHE HE1 H 7.030 0.04 3 926 . 88 PHE CZ C 129.289 0.1 1 927 . 88 PHE HZ H 7.221 0.04 1 928 . 88 PHE C C 175.977 0.1 1 929 . 89 LEU N N 115.077 0.05 1 930 . 89 LEU H H 8.491 0.04 1 931 . 89 LEU CA C 56.871 0.1 1 932 . 89 LEU HA H 4.093 0.04 1 933 . 89 LEU CB C 41.365 0.1 1 934 . 89 LEU HB3 H 1.515 0.04 2 935 . 89 LEU HB2 H 1.774 0.04 2 936 . 89 LEU CG C 26.845 0.1 1 937 . 89 LEU HG H 2.020 0.04 1 938 . 89 LEU CD1 C 26.200 0.1 2 939 . 89 LEU HD1 H 0.881 0.04 2 940 . 89 LEU CD2 C 22.287 0.1 2 941 . 89 LEU HD2 H 0.680 0.04 2 942 . 89 LEU C C 175.675 0.1 1 943 . 90 ASP N N 119.255 0.05 1 944 . 90 ASP H H 7.584 0.04 1 945 . 90 ASP CA C 57.861 0.1 1 946 . 90 ASP HA H 4.431 0.04 1 947 . 90 ASP CB C 40.167 0.1 1 948 . 90 ASP HB3 H 2.659 0.04 2 949 . 90 ASP HB2 H 2.884 0.04 2 950 . 90 ASP C C 176.045 0.1 1 951 . 91 GLY N N 103.705 0.05 1 952 . 91 GLY H H 7.636 0.04 1 953 . 91 GLY CA C 45.800 0.1 1 954 . 91 GLY HA3 H 3.471 0.04 2 955 . 91 GLY HA2 H 3.931 0.04 2 956 . 91 GLY C C 171.374 0.1 1 957 . 92 PHE N N 117.752 0.05 1 958 . 92 PHE H H 7.916 0.04 1 959 . 92 PHE CA C 57.236 0.1 1 960 . 92 PHE HA H 4.490 0.04 1 961 . 92 PHE CB C 39.894 0.1 1 962 . 92 PHE HB3 H 2.791 0.04 2 963 . 92 PHE HB2 H 3.255 0.04 2 964 . 92 PHE HD1 H 6.901 0.04 3 965 . 92 PHE CE1 C 129.366 0.1 3 966 . 92 PHE HE1 H 7.114 0.04 3 967 . 92 PHE HZ H 6.885 0.04 1 968 . 92 PHE C C 171.471 0.1 1 969 . 93 ARG N N 118.530 0.05 1 970 . 93 ARG H H 7.217 0.04 1 971 . 93 ARG CA C 56.660 0.1 1 972 . 93 ARG HA H 4.657 0.04 1 973 . 93 ARG CB C 31.902 0.1 1 974 . 93 ARG HB3 H 1.836 0.04 2 975 . 93 ARG HB2 H 1.964 0.04 2 976 . 93 ARG CG C 28.608 0.1 1 977 . 93 ARG HG3 H 1.593 0.04 2 978 . 93 ARG HG2 H 1.880 0.04 2 979 . 93 ARG CD C 43.469 0.1 1 980 . 93 ARG HD2 H 3.240 0.04 2 981 . 93 ARG NE N 84.452 0.05 1 982 . 93 ARG HE H 7.398 0.04 1 983 . 93 ARG CZ C 156.841 0.1 1 984 . 93 ARG C C 173.047 0.1 1 985 . 94 GLU N N 124.829 0.05 1 986 . 94 GLU H H 8.257 0.04 1 987 . 94 GLU CA C 58.196 0.1 1 988 . 94 GLU HA H 4.128 0.04 1 989 . 94 GLU CB C 31.507 0.1 1 990 . 94 GLU HB3 H 1.878 0.04 2 991 . 94 GLU HB2 H 1.859 0.04 2 992 . 94 GLU CG C 36.720 0.1 1 993 . 94 GLU HG2 H 2.152 0.04 2 994 . 94 GLU C C 173.047 0.1 1 stop_ save_