data_5760 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein titin ; _BMRB_accession_number 5760 _BMRB_flat_file_name bmr5760.str _Entry_type original _Submission_date 2003-04-01 _Accession_date 2003-04-07 _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 Edlich Christian . . 2 Muhle-Goll Claudia . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 179 "13C chemical shifts" 374 "15N chemical shifts" 179 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-05 original author . stop_ _Original_release_date 2003-09-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C, and 15N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein titin ; _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 Edlich Christian . . 2 Muhle-Goll Claudia . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 283 _Page_last 284 _Year 2003 _Details . loop_ _Keyword 'Ig domain' 'NMR assignment' t-cap titin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40. ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_titin_Z1Z2 _Saveframe_category molecular_system _Mol_system_name Z1Z2 _Abbreviation_common 'titin Z1Z2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Z1Z2 $Z1Z2 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_Z1Z2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'titin Z1Z2' _Abbreviation_common 'titin Z1Z2' _Molecular_mass 21924 _Mol_thiol_state 'not present' _Details ; A N-terminal sequence tag has been added: MKHHHHHHP. Met on position 1 of the native sequence thus becomes Met-10 in this deposition. Residue Thr-2 has been replaced by an Ala in the molecule studied (Ala-11 in this deposition.) ; ############################## # Polymer residue sequence # ############################## _Residue_count 204 _Mol_residue_sequence ; MKHHHHHHPMATQAPTFTQP LQSVVVLEGSTATFEAHISG FPVPEVSWFRDGQVISTSTL PGVQISFSDGRAKLTIPAVT KANSGRYSLKATNGSGQATS TAELLVKAETAPPNFVQRLQ SMTVRQGSQVRLQVRVTGIP TPVVKFYRDGAEIQSSLDFQ ISQEGDLYSLLIAEAYPEDS GTYSVNATNSVGRATSTAEL LVQG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 PRO 10 MET 11 ALA 12 THR 13 GLN 14 ALA 15 PRO 16 THR 17 PHE 18 THR 19 GLN 20 PRO 21 LEU 22 GLN 23 SER 24 VAL 25 VAL 26 VAL 27 LEU 28 GLU 29 GLY 30 SER 31 THR 32 ALA 33 THR 34 PHE 35 GLU 36 ALA 37 HIS 38 ILE 39 SER 40 GLY 41 PHE 42 PRO 43 VAL 44 PRO 45 GLU 46 VAL 47 SER 48 TRP 49 PHE 50 ARG 51 ASP 52 GLY 53 GLN 54 VAL 55 ILE 56 SER 57 THR 58 SER 59 THR 60 LEU 61 PRO 62 GLY 63 VAL 64 GLN 65 ILE 66 SER 67 PHE 68 SER 69 ASP 70 GLY 71 ARG 72 ALA 73 LYS 74 LEU 75 THR 76 ILE 77 PRO 78 ALA 79 VAL 80 THR 81 LYS 82 ALA 83 ASN 84 SER 85 GLY 86 ARG 87 TYR 88 SER 89 LEU 90 LYS 91 ALA 92 THR 93 ASN 94 GLY 95 SER 96 GLY 97 GLN 98 ALA 99 THR 100 SER 101 THR 102 ALA 103 GLU 104 LEU 105 LEU 106 VAL 107 LYS 108 ALA 109 GLU 110 THR 111 ALA 112 PRO 113 PRO 114 ASN 115 PHE 116 VAL 117 GLN 118 ARG 119 LEU 120 GLN 121 SER 122 MET 123 THR 124 VAL 125 ARG 126 GLN 127 GLY 128 SER 129 GLN 130 VAL 131 ARG 132 LEU 133 GLN 134 VAL 135 ARG 136 VAL 137 THR 138 GLY 139 ILE 140 PRO 141 THR 142 PRO 143 VAL 144 VAL 145 LYS 146 PHE 147 TYR 148 ARG 149 ASP 150 GLY 151 ALA 152 GLU 153 ILE 154 GLN 155 SER 156 SER 157 LEU 158 ASP 159 PHE 160 GLN 161 ILE 162 SER 163 GLN 164 GLU 165 GLY 166 ASP 167 LEU 168 TYR 169 SER 170 LEU 171 LEU 172 ILE 173 ALA 174 GLU 175 ALA 176 TYR 177 PRO 178 GLU 179 ASP 180 SER 181 GLY 182 THR 183 TYR 184 SER 185 VAL 186 ASN 187 ALA 188 THR 189 ASN 190 SER 191 VAL 192 GLY 193 ARG 194 ALA 195 THR 196 SER 197 THR 198 ALA 199 GLU 200 LEU 201 LEU 202 VAL 203 GLN 204 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2A38 "Crystal Structure Of The N-Terminus Of Titin" 95.10 194 99.48 99.48 8.02e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue $Z1Z2 Human 9606 Eukaryota Metazoa Homo sapiens 'heart, skeletal' muscle 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 $Z1Z2 '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 _Isotopic_labeling $Z1Z2 1.0 mM '[U-100% 15N; U-100% 13C; U-70% 2H]' 'sodium acetate' 10 mM . (NH4)2SO4 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.02 M pH 5.7 0.2 n/a temperature 310 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 DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external parallel 1.0 DSS N 15 'methyl protons' ppm 0.00 external 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 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Z1Z2 _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 . 9 PRO CA C 62.533 0.10 1 2 . 9 PRO CB C 31.462 0.20 1 3 . 10 MET H H 8.317 0.02 1 4 . 10 MET CA C 54.272 0.10 1 5 . 10 MET CB C 32.489 0.20 1 6 . 10 MET N N 120.396 0.20 1 7 . 11 ALA H H 8.037 0.02 1 8 . 11 ALA CA C 51.232 0.10 1 9 . 11 ALA CB C 19.368 0.20 1 10 . 11 ALA N N 124.787 0.20 1 11 . 12 THR H H 7.967 0.02 1 12 . 12 THR CA C 60.998 0.10 1 13 . 12 THR CB C 69.699 0.20 1 14 . 12 THR N N 111.864 0.20 1 15 . 13 GLN H H 9.114 0.02 1 16 . 13 GLN CA C 54.802 0.10 1 17 . 13 GLN CB C 32.230 0.20 1 18 . 13 GLN N N 122.075 0.20 1 19 . 14 ALA H H 8.780 0.02 1 20 . 14 ALA CA C 50.208 0.10 1 21 . 14 ALA CB C 16.684 0.20 1 22 . 14 ALA N N 128.971 0.20 1 23 . 15 PRO CA C 61.293 0.10 1 24 . 15 PRO CB C 31.470 0.20 1 25 . 16 THR H H 8.186 0.02 1 26 . 16 THR CA C 59.465 0.10 1 27 . 16 THR CB C 71.554 0.20 1 28 . 16 THR N N 114.215 0.20 1 29 . 17 PHE H H 8.895 0.02 1 30 . 17 PHE CA C 56.968 0.10 1 31 . 17 PHE CB C 38.393 0.20 1 32 . 17 PHE N N 121.815 0.20 1 33 . 18 THR H H 8.301 0.02 1 34 . 18 THR CA C 62.843 0.10 1 35 . 18 THR CB C 67.493 0.20 1 36 . 18 THR N N 119.533 0.20 1 37 . 19 GLN H H 7.764 0.02 1 38 . 19 GLN CA C 53.190 0.10 1 39 . 19 GLN CB C 31.462 0.20 1 40 . 19 GLN N N 119.389 0.20 1 41 . 20 PRO CA C 61.167 0.10 1 42 . 20 PRO CB C 32.324 0.20 1 43 . 21 LEU H H 7.686 0.02 1 44 . 21 LEU CA C 54.944 0.10 1 45 . 21 LEU CB C 43.711 0.20 1 46 . 21 LEU N N 115.459 0.20 1 47 . 22 GLN H H 8.413 0.02 1 48 . 22 GLN CA C 53.130 0.10 1 49 . 22 GLN CB C 31.727 0.20 1 50 . 22 GLN N N 119.450 0.20 1 51 . 23 SER H H 8.677 0.02 1 52 . 23 SER CA C 59.469 0.10 1 53 . 23 SER CB C 63.712 0.20 1 54 . 23 SER N N 118.257 0.20 1 55 . 24 VAL H H 8.748 0.02 1 56 . 24 VAL CA C 60.403 0.10 1 57 . 24 VAL CB C 36.035 0.20 1 58 . 24 VAL N N 121.671 0.20 1 59 . 25 VAL H H 8.253 0.02 1 60 . 25 VAL CA C 59.887 0.10 1 61 . 25 VAL CB C 32.568 0.20 1 62 . 25 VAL N N 126.686 0.20 1 63 . 26 VAL H H 8.582 0.02 1 64 . 26 VAL CA C 57.839 0.10 1 65 . 26 VAL CB C 35.860 0.20 1 66 . 26 VAL N N 121.126 0.20 1 67 . 27 LEU H H 8.131 0.02 1 68 . 27 LEU CA C 53.163 0.10 1 69 . 27 LEU CB C 42.595 0.20 1 70 . 27 LEU N N 122.437 0.20 1 71 . 28 GLU H H 8.396 0.02 1 72 . 28 GLU CA C 57.859 0.10 1 73 . 28 GLU CB C 29.360 0.20 1 74 . 28 GLU N N 122.506 0.20 1 75 . 29 GLY H H 9.279 0.02 1 76 . 29 GLY CA C 44.184 0.10 1 77 . 29 GLY N N 113.931 0.20 1 78 . 30 SER H H 7.957 0.02 1 79 . 30 SER CA C 57.558 0.10 1 80 . 30 SER CB C 64.368 0.20 1 81 . 30 SER N N 116.771 0.20 1 82 . 31 THR H H 8.233 0.02 1 83 . 31 THR CA C 61.312 0.10 1 84 . 31 THR CB C 69.700 0.20 1 85 . 31 THR N N 116.668 0.20 1 86 . 32 ALA H H 8.432 0.02 1 87 . 32 ALA CA C 49.503 0.10 1 88 . 32 ALA CB C 23.066 0.20 1 89 . 32 ALA N N 128.296 0.20 1 90 . 33 THR H H 8.019 0.02 1 91 . 33 THR CA C 60.314 0.10 1 92 . 33 THR CB C 71.405 0.20 1 93 . 33 THR N N 116.875 0.20 1 94 . 34 PHE H H 9.215 0.02 1 95 . 34 PHE CA C 56.564 0.10 1 96 . 34 PHE CB C 43.092 0.20 1 97 . 34 PHE N N 124.652 0.20 1 98 . 35 GLU H H 8.529 0.02 1 99 . 35 GLU CA C 54.380 0.10 1 100 . 35 GLU CB C 33.328 0.20 1 101 . 35 GLU N N 120.502 0.20 1 102 . 36 ALA H H 9.259 0.02 1 103 . 36 ALA CA C 49.629 0.10 1 104 . 36 ALA CB C 24.126 0.20 1 105 . 36 ALA N N 125.443 0.20 1 106 . 37 HIS H H 9.258 0.02 1 107 . 37 HIS CA C 53.287 0.10 1 108 . 37 HIS CB C 31.959 0.20 1 109 . 37 HIS N N 119.948 0.20 1 110 . 38 ILE H H 9.214 0.02 1 111 . 38 ILE CA C 59.260 0.10 1 112 . 38 ILE CB C 41.769 0.20 1 113 . 38 ILE N N 125.028 0.20 1 114 . 39 SER H H 8.974 0.02 1 115 . 39 SER CA C 55.570 0.10 1 116 . 39 SER CB C 65.292 0.20 1 117 . 39 SER N N 122.057 0.20 1 118 . 40 GLY H H 7.805 0.02 1 119 . 40 GLY CA C 44.296 0.10 1 120 . 40 GLY N N 108.337 0.20 1 121 . 41 PHE H H 8.488 0.02 1 122 . 41 PHE CA C 56.443 0.10 1 123 . 41 PHE CB C 42.728 0.20 1 124 . 41 PHE N N 120.882 0.20 1 125 . 42 PRO CA C 62.175 0.10 1 126 . 42 PRO CB C 33.450 0.20 1 127 . 43 VAL H H 8.222 0.02 1 128 . 43 VAL CA C 60.751 0.10 1 129 . 43 VAL CB C 31.926 0.20 1 130 . 43 VAL N N 122.895 0.20 1 131 . 44 PRO CA C 61.785 0.10 1 132 . 44 PRO CB C 32.324 0.20 1 133 . 45 GLU H H 8.549 0.02 1 134 . 45 GLU CA C 54.960 0.10 1 135 . 45 GLU CB C 30.501 0.20 1 136 . 45 GLU N N 119.051 0.20 1 137 . 46 VAL H H 8.322 0.02 1 138 . 46 VAL CA C 58.853 0.10 1 139 . 46 VAL CB C 33.980 0.20 1 140 . 46 VAL N N 119.360 0.20 1 141 . 47 SER H H 8.444 0.02 1 142 . 47 SER CA C 56.821 0.10 1 143 . 47 SER CB C 66.407 0.20 1 144 . 47 SER N N 118.445 0.20 1 145 . 48 TRP H H 8.688 0.02 1 146 . 48 TRP CA C 55.479 0.10 1 147 . 48 TRP CB C 32.451 0.20 1 148 . 48 TRP N N 123.957 0.20 1 149 . 49 PHE H H 9.549 0.02 1 150 . 49 PHE CA C 55.868 0.10 1 151 . 49 PHE CB C 43.542 0.20 1 152 . 49 PHE N N 117.773 0.20 1 153 . 50 ARG H H 8.914 0.02 1 154 . 50 ARG CA C 53.902 0.10 1 155 . 50 ARG CB C 31.133 0.20 1 156 . 50 ARG N N 119.673 0.20 1 157 . 51 ASP H H 9.672 0.02 1 158 . 51 ASP CA C 55.118 0.10 1 159 . 51 ASP CB C 39.432 0.20 1 160 . 51 ASP N N 129.362 0.20 1 161 . 52 GLY H H 8.389 0.02 1 162 . 52 GLY CA C 45.399 0.10 1 163 . 52 GLY N N 102.331 0.20 1 164 . 53 GLN H H 8.201 0.02 1 165 . 53 GLN CA C 53.280 0.10 1 166 . 53 GLN CB C 30.373 0.20 1 167 . 53 GLN N N 120.952 0.20 1 168 . 54 VAL H H 8.688 0.02 1 169 . 54 VAL CA C 62.347 0.10 1 170 . 54 VAL CB C 31.904 0.20 1 171 . 54 VAL N N 126.306 0.20 1 172 . 55 ILE H H 8.411 0.02 1 173 . 55 ILE CA C 60.858 0.10 1 174 . 55 ILE CB C 38.139 0.20 1 175 . 55 ILE N N 127.792 0.20 1 176 . 56 SER H H 8.109 0.02 1 177 . 56 SER CA C 55.208 0.10 1 178 . 56 SER CB C 66.717 0.20 1 179 . 56 SER N N 121.279 0.20 1 180 . 57 THR CA C 63.465 0.10 1 181 . 57 THR CB C 68.108 0.20 1 182 . 58 SER H H 7.976 0.02 1 183 . 58 SER CA C 59.604 0.10 1 184 . 58 SER CB C 63.138 0.20 1 185 . 58 SER N N 113.524 0.20 1 186 . 59 THR H H 7.449 0.02 1 187 . 59 THR CA C 61.576 0.10 1 188 . 59 THR CB C 69.301 0.20 1 189 . 59 THR N N 111.289 0.20 1 190 . 60 LEU H H 7.900 0.02 1 191 . 60 LEU CA C 52.196 0.10 1 192 . 60 LEU CB C 42.396 0.20 1 193 . 60 LEU N N 125.650 0.20 1 194 . 61 PRO CA C 63.574 0.10 1 195 . 61 PRO CB C 31.131 0.20 1 196 . 62 GLY H H 8.656 0.02 1 197 . 62 GLY CA C 44.977 0.10 1 198 . 62 GLY N N 111.213 0.20 1 199 . 63 VAL H H 7.771 0.02 1 200 . 63 VAL CA C 61.383 0.10 1 201 . 63 VAL CB C 31.470 0.20 1 202 . 63 VAL N N 118.775 0.20 1 203 . 64 GLN H H 8.541 0.02 1 204 . 64 GLN CA C 53.532 0.10 1 205 . 64 GLN CB C 30.037 0.20 1 206 . 64 GLN N N 124.382 0.20 1 207 . 65 ILE H H 8.550 0.02 1 208 . 65 ILE CA C 59.967 0.10 1 209 . 65 ILE CB C 40.841 0.20 1 210 . 65 ILE N N 126.375 0.20 1 211 . 66 SER H H 9.251 0.02 1 212 . 66 SER CA C 56.503 0.10 1 213 . 66 SER CB C 66.385 0.20 1 214 . 66 SER N N 120.330 0.20 1 215 . 67 PHE CA C 55.841 0.10 1 216 . 67 PHE CB C 40.342 0.20 1 217 . 68 SER H H 8.076 0.02 1 218 . 68 SER CA C 56.783 0.10 1 219 . 68 SER CB C 64.463 0.20 1 220 . 68 SER N N 120.712 0.20 1 221 . 69 ASP CA C 54.659 0.10 1 222 . 69 ASP CB C 39.878 0.20 1 223 . 70 GLY H H 7.670 0.02 1 224 . 70 GLY CA C 45.653 0.10 1 225 . 70 GLY N N 102.892 0.20 1 226 . 71 ARG H H 7.894 0.02 1 227 . 71 ARG CA C 54.395 0.10 1 228 . 71 ARG CB C 30.120 0.20 1 229 . 71 ARG N N 120.744 0.20 1 230 . 72 ALA H H 9.414 0.02 1 231 . 72 ALA CA C 50.176 0.10 1 232 . 72 ALA CB C 21.873 0.20 1 233 . 72 ALA N N 133.416 0.20 1 234 . 73 LYS H H 9.068 0.02 1 235 . 73 LYS CA C 54.648 0.10 1 236 . 73 LYS CB C 37.194 0.20 1 237 . 73 LYS N N 122.921 0.20 1 238 . 74 LEU H H 8.476 0.02 1 239 . 74 LEU CA C 53.602 0.10 1 240 . 74 LEU CB C 42.107 0.20 1 241 . 74 LEU N N 126.938 0.20 1 242 . 75 THR H H 8.929 0.02 1 243 . 75 THR CA C 60.494 0.10 1 244 . 75 THR CB C 70.941 0.20 1 245 . 75 THR N N 122.679 0.20 1 246 . 76 ILE H H 9.178 0.02 1 247 . 76 ILE CA C 57.407 0.10 1 248 . 76 ILE CB C 39.490 0.20 1 249 . 76 ILE N N 127.239 0.20 1 250 . 77 PRO CA C 63.151 0.10 1 251 . 77 PRO CB C 32.058 0.20 1 252 . 78 ALA H H 7.748 0.02 1 253 . 78 ALA CA C 50.585 0.10 1 254 . 78 ALA CB C 18.374 0.20 1 255 . 78 ALA N N 120.734 0.20 1 256 . 79 VAL H H 8.441 0.02 1 257 . 79 VAL CA C 61.638 0.10 1 258 . 79 VAL CB C 32.990 0.20 1 259 . 79 VAL N N 117.635 0.20 1 260 . 80 THR H H 8.548 0.02 1 261 . 80 THR CA C 58.620 0.10 1 262 . 80 THR CB C 72.025 0.20 1 263 . 80 THR N N 113.938 0.20 1 264 . 81 LYS H H 9.248 0.02 1 265 . 81 LYS CA C 59.500 0.10 1 266 . 81 LYS CB C 31.495 0.20 1 267 . 81 LYS N N 121.813 0.20 1 268 . 82 ALA H H 8.043 0.02 1 269 . 82 ALA CA C 53.145 0.10 1 270 . 82 ALA CB C 18.076 0.20 1 271 . 82 ALA N N 120.172 0.20 1 272 . 83 ASN H H 8.168 0.02 1 273 . 83 ASN CA C 53.617 0.10 1 274 . 83 ASN CB C 39.680 0.20 1 275 . 83 ASN N N 112.670 0.20 1 276 . 84 SER H H 7.838 0.02 1 277 . 84 SER CA C 59.546 0.10 1 278 . 84 SER CB C 64.066 0.20 1 279 . 84 SER N N 116.555 0.20 1 280 . 85 GLY H H 8.840 0.02 1 281 . 85 GLY CA C 44.893 0.10 1 282 . 85 GLY N N 110.484 0.20 1 283 . 86 ARG H H 8.874 0.02 1 284 . 86 ARG CA C 55.288 0.10 1 285 . 86 ARG CB C 30.501 0.20 1 286 . 86 ARG N N 121.090 0.20 1 287 . 87 TYR H H 9.449 0.02 1 288 . 87 TYR CA C 56.462 0.10 1 289 . 87 TYR CB C 40.419 0.20 1 290 . 87 TYR N N 129.346 0.20 1 291 . 88 SER H H 9.267 0.02 1 292 . 88 SER CA C 55.509 0.10 1 293 . 88 SER CB C 66.484 0.20 1 294 . 88 SER N N 114.215 0.20 1 295 . 89 LEU H H 8.672 0.02 1 296 . 89 LEU CA C 52.459 0.10 1 297 . 89 LEU CB C 44.583 0.20 1 298 . 89 LEU N N 124.130 0.20 1 299 . 90 LYS H H 8.983 0.02 1 300 . 90 LYS CA C 53.883 0.10 1 301 . 90 LYS CB C 35.438 0.20 1 302 . 90 LYS N N 125.063 0.20 1 303 . 91 ALA H H 9.254 0.02 1 304 . 91 ALA CA C 48.611 0.10 1 305 . 91 ALA CB C 22.100 0.20 1 306 . 91 ALA N N 128.828 0.20 1 307 . 92 THR H H 8.900 0.02 1 308 . 92 THR CA C 60.811 0.10 1 309 . 92 THR CB C 71.328 0.20 1 310 . 92 THR N N 116.426 0.20 1 311 . 93 ASN H H 9.097 0.02 1 312 . 93 ASN CA C 51.363 0.10 1 313 . 93 ASN CB C 39.944 0.20 1 314 . 93 ASN N N 123.163 0.20 1 315 . 94 GLY H H 8.654 0.02 1 316 . 94 GLY CA C 46.122 0.10 1 317 . 94 GLY N N 103.735 0.20 1 318 . 95 SER H H 7.993 0.02 1 319 . 95 SER CA C 58.770 0.10 1 320 . 95 SER CB C 64.065 0.20 1 321 . 95 SER N N 113.721 0.20 1 322 . 96 GLY H H 7.794 0.02 1 323 . 96 GLY CA C 45.399 0.10 1 324 . 96 GLY N N 108.068 0.20 1 325 . 97 GLN H H 8.308 0.02 1 326 . 97 GLN CA C 52.904 0.10 1 327 . 97 GLN CB C 33.029 0.20 1 328 . 97 GLN N N 115.643 0.20 1 329 . 98 ALA H H 9.012 0.02 1 330 . 98 ALA CA C 50.925 0.10 1 331 . 98 ALA CB C 23.136 0.20 1 332 . 98 ALA N N 125.404 0.20 1 333 . 99 THR H H 8.652 0.02 1 334 . 99 THR CA C 60.269 0.10 1 335 . 99 THR CB C 72.283 0.20 1 336 . 99 THR N N 115.148 0.20 1 337 . 100 SER H H 8.368 0.02 1 338 . 100 SER CA C 64.478 0.10 1 339 . 100 SER CB C 64.265 0.20 1 340 . 100 SER N N 119.608 0.20 1 341 . 101 THR H H 8.016 0.02 1 342 . 101 THR CA C 60.310 0.10 1 343 . 101 THR CB C 71.355 0.20 1 344 . 101 THR N N 121.055 0.20 1 345 . 102 ALA H H 9.353 0.02 1 346 . 102 ALA CA C 50.770 0.10 1 347 . 102 ALA CB C 23.620 0.20 1 348 . 102 ALA N N 127.688 0.20 1 349 . 103 GLU H H 8.702 0.02 1 350 . 103 GLU CA C 54.835 0.10 1 351 . 103 GLU CB C 32.589 0.20 1 352 . 103 GLU N N 118.360 0.20 1 353 . 104 LEU H H 9.270 0.02 1 354 . 104 LEU CA C 53.115 0.10 1 355 . 104 LEU CB C 44.318 0.20 1 356 . 104 LEU N N 122.817 0.20 1 357 . 105 LEU H H 9.027 0.02 1 358 . 105 LEU CA C 53.506 0.10 1 359 . 105 LEU CB C 43.795 0.20 1 360 . 105 LEU N N 130.050 0.20 1 361 . 106 VAL H H 7.958 0.02 1 362 . 106 VAL CA C 59.920 0.10 1 363 . 106 VAL CB C 32.423 0.20 1 364 . 106 VAL N N 123.370 0.20 1 365 . 107 LYS H H 8.767 0.02 1 366 . 107 LYS CA C 53.711 0.10 1 367 . 107 LYS CB C 34.047 0.20 1 368 . 107 LYS N N 127.081 0.20 1 369 . 108 ALA H H 8.466 0.02 1 370 . 108 ALA CA C 50.916 0.10 1 371 . 108 ALA CB C 20.528 0.20 1 372 . 108 ALA N N 124.303 0.20 1 373 . 109 GLU H H 8.250 0.02 1 374 . 109 GLU CA C 55.460 0.10 1 375 . 109 GLU CB C 30.711 0.20 1 376 . 109 GLU N N 119.794 0.20 1 377 . 110 THR H H 7.726 0.02 1 378 . 110 THR CA C 59.620 0.10 1 379 . 110 THR CB C 71.223 0.20 1 380 . 110 THR N N 110.276 0.20 1 381 . 111 ALA H H 9.798 0.02 1 382 . 111 ALA CA C 49.726 0.10 1 383 . 111 ALA CB C 20.660 0.20 1 384 . 111 ALA N N 122.763 0.20 1 385 . 113 PRO CA C 60.906 0.10 1 386 . 113 PRO CB C 31.893 0.20 1 387 . 114 ASN H H 8.166 0.02 1 388 . 114 ASN CA C 51.101 0.10 1 389 . 114 ASN CB C 42.014 0.20 1 390 . 114 ASN N N 118.445 0.20 1 391 . 115 PHE H H 8.683 0.02 1 392 . 115 PHE CA C 57.263 0.10 1 393 . 115 PHE CB C 38.838 0.20 1 394 . 115 PHE N N 121.683 0.20 1 395 . 116 VAL H H 8.234 0.02 1 396 . 116 VAL CA C 63.156 0.10 1 397 . 116 VAL CB C 32.079 0.20 1 398 . 116 VAL N N 126.062 0.20 1 399 . 117 GLN H H 7.824 0.02 1 400 . 117 GLN CA C 55.227 0.10 1 401 . 117 GLN CB C 31.065 0.20 1 402 . 117 GLN N N 118.586 0.20 1 403 . 118 ARG H H 8.749 0.02 1 404 . 118 ARG CA C 54.477 0.10 1 405 . 118 ARG CB C 32.091 0.20 1 406 . 118 ARG N N 124.652 0.20 1 407 . 119 LEU H H 7.575 0.02 1 408 . 119 LEU CA C 54.663 0.10 1 409 . 119 LEU CB C 43.490 0.20 1 410 . 119 LEU N N 118.175 0.20 1 411 . 120 GLN H H 8.388 0.02 1 412 . 120 GLN CA C 53.303 0.10 1 413 . 120 GLN CB C 31.515 0.20 1 414 . 120 GLN N N 120.813 0.20 1 415 . 121 SER H H 8.574 0.02 1 416 . 121 SER CA C 58.993 0.10 1 417 . 121 SER CB C 63.550 0.20 1 418 . 121 SER N N 119.086 0.20 1 419 . 122 MET H H 8.419 0.02 1 420 . 122 MET CA C 54.677 0.10 1 421 . 122 MET CB C 37.318 0.20 1 422 . 122 MET N N 119.907 0.20 1 423 . 123 THR H H 8.450 0.02 1 424 . 123 THR CA C 60.404 0.10 1 425 . 123 THR CB C 69.911 0.20 1 426 . 123 THR N N 119.956 0.20 1 427 . 124 VAL H H 8.982 0.02 1 428 . 124 VAL CA C 57.678 0.10 1 429 . 124 VAL CB C 35.607 0.20 1 430 . 124 VAL N N 119.224 0.20 1 431 . 125 ARG H H 8.396 0.02 1 432 . 125 ARG CA C 54.242 0.10 1 433 . 125 ARG CB C 30.733 0.20 1 434 . 125 ARG N N 120.181 0.20 1 435 . 126 GLN H H 8.515 0.02 1 436 . 126 GLN CA C 56.037 0.10 1 437 . 126 GLN CB C 28.181 0.20 1 438 . 126 GLN N N 122.358 0.20 1 439 . 127 GLY H H 9.573 0.02 1 440 . 127 GLY CA C 43.709 0.10 1 441 . 127 GLY N N 113.419 0.20 1 442 . 128 SER H H 7.517 0.02 1 443 . 128 SER CA C 58.229 0.10 1 444 . 128 SER CB C 64.596 0.20 1 445 . 128 SER N N 115.354 0.20 1 446 . 129 GLN H H 8.337 0.02 1 447 . 129 GLN CA C 54.711 0.10 1 448 . 129 GLN CB C 30.204 0.20 1 449 . 129 GLN N N 121.781 0.20 1 450 . 130 VAL H H 8.564 0.02 1 451 . 130 VAL CA C 60.507 0.10 1 452 . 130 VAL CB C 34.842 0.20 1 453 . 130 VAL N N 124.890 0.20 1 454 . 131 ARG H H 8.448 0.02 1 455 . 131 ARG CA C 53.652 0.10 1 456 . 131 ARG CB C 31.904 0.20 1 457 . 131 ARG N N 127.216 0.20 1 458 . 132 LEU H H 9.191 0.02 1 459 . 132 LEU CA C 53.486 0.10 1 460 . 132 LEU CB C 41.938 0.20 1 461 . 132 LEU N N 128.161 0.20 1 462 . 133 GLN H H 8.364 0.02 1 463 . 133 GLN CA C 53.804 0.10 1 464 . 133 GLN CB C 33.285 0.20 1 465 . 133 GLN N N 120.433 0.20 1 466 . 134 VAL H H 8.998 0.02 1 467 . 134 VAL CA C 58.117 0.10 1 468 . 134 VAL CB C 35.723 0.20 1 469 . 134 VAL N N 112.095 0.20 1 470 . 135 ARG H H 8.404 0.02 1 471 . 135 ARG CA C 54.553 0.10 1 472 . 135 ARG CB C 33.781 0.20 1 473 . 135 ARG N N 120.601 0.20 1 474 . 136 VAL H H 8.939 0.02 1 475 . 136 VAL CA C 59.075 0.10 1 476 . 136 VAL CB C 35.185 0.20 1 477 . 136 VAL N N 125.535 0.20 1 478 . 137 THR H H 8.551 0.02 1 479 . 137 THR CA C 58.431 0.10 1 480 . 137 THR CB C 70.891 0.20 1 481 . 137 THR N N 116.219 0.20 1 482 . 138 GLY H H 7.847 0.02 1 483 . 138 GLY CA C 45.315 0.10 1 484 . 138 GLY N N 106.338 0.20 1 485 . 139 ILE H H 8.310 0.02 1 486 . 139 ILE CA C 58.341 0.10 1 487 . 139 ILE CB C 41.866 0.20 1 488 . 139 ILE N N 121.193 0.20 1 489 . 140 PRO CA C 61.805 0.10 1 490 . 140 PRO CB C 34.974 0.20 1 491 . 141 THR H H 8.513 0.02 1 492 . 141 THR CA C 61.263 0.10 1 493 . 141 THR N N 118.605 0.20 1 494 . 142 PRO CA C 61.481 0.10 1 495 . 142 PRO CB C 36.035 0.20 1 496 . 143 VAL H H 8.759 0.02 1 497 . 143 VAL CA C 61.760 0.10 1 498 . 143 VAL CB C 32.158 0.20 1 499 . 143 VAL N N 121.781 0.20 1 500 . 144 VAL H H 8.595 0.02 1 501 . 144 VAL CA C 60.966 0.10 1 502 . 144 VAL CB C 33.159 0.20 1 503 . 144 VAL N N 130.803 0.20 1 504 . 145 LYS H H 8.405 0.02 1 505 . 145 LYS CA C 54.079 0.10 1 506 . 145 LYS CB C 37.956 0.20 1 507 . 145 LYS N N 125.732 0.20 1 508 . 146 PHE H H 8.977 0.02 1 509 . 146 PHE CA C 56.524 0.10 1 510 . 146 PHE CB C 42.959 0.20 1 511 . 146 PHE N N 120.606 0.20 1 512 . 147 TYR H H 9.516 0.02 1 513 . 147 TYR CA C 56.196 0.10 1 514 . 147 TYR CB C 42.230 0.20 1 515 . 147 TYR N N 117.506 0.20 1 516 . 148 ARG H H 8.763 0.02 1 517 . 148 ARG CA C 53.913 0.10 1 518 . 148 ARG CB C 31.323 0.20 1 519 . 148 ARG N N 119.086 0.20 1 520 . 149 ASP H H 9.646 0.02 1 521 . 149 ASP CA C 54.944 0.10 1 522 . 149 ASP CB C 39.547 0.20 1 523 . 149 ASP N N 129.103 0.20 1 524 . 150 GLY H H 8.332 0.02 1 525 . 150 GLY CA C 45.484 0.10 1 526 . 150 GLY N N 101.881 0.20 1 527 . 151 ALA H H 8.143 0.02 1 528 . 151 ALA CA C 49.868 0.10 1 529 . 151 ALA CB C 20.594 0.20 1 530 . 151 ALA N N 124.924 0.20 1 531 . 152 GLU H H 8.821 0.02 1 532 . 152 GLU CA C 56.264 0.10 1 533 . 152 GLU CB C 29.607 0.20 1 534 . 152 GLU N N 125.546 0.20 1 535 . 153 ILE H H 8.551 0.02 1 536 . 153 ILE CA C 60.373 0.10 1 537 . 153 ILE CB C 38.477 0.20 1 538 . 153 ILE N N 127.965 0.20 1 539 . 154 GLN H H 8.251 0.02 1 540 . 154 GLN CA C 53.225 0.10 1 541 . 154 GLN CB C 29.507 0.20 1 542 . 154 GLN N N 125.867 0.20 1 543 . 155 SER H H 8.572 0.02 1 544 . 155 SER CA C 58.560 0.10 1 545 . 155 SER CB C 63.271 0.20 1 546 . 155 SER N N 117.704 0.20 1 547 . 156 SER H H 9.184 0.02 1 548 . 156 SER CA C 56.642 0.10 1 549 . 156 SER CB C 65.954 0.20 1 550 . 156 SER N N 122.933 0.20 1 551 . 157 LEU H H 8.404 0.02 1 552 . 157 LEU CA C 56.978 0.10 1 553 . 157 LEU CB C 41.005 0.20 1 554 . 157 LEU N N 118.588 0.20 1 555 . 158 ASP H H 7.933 0.02 1 556 . 158 ASP CA C 55.008 0.10 1 557 . 158 ASP CB C 41.634 0.20 1 558 . 158 ASP N N 114.936 0.20 1 559 . 159 PHE H H 7.324 0.02 1 560 . 159 PHE CA C 55.553 0.10 1 561 . 159 PHE CB C 40.010 0.20 1 562 . 159 PHE N N 121.366 0.20 1 563 . 160 GLN H H 8.545 0.02 1 564 . 160 GLN CA C 54.945 0.10 1 565 . 160 GLN CB C 30.568 0.20 1 566 . 160 GLN N N 121.297 0.20 1 567 . 161 ILE H H 8.604 0.02 1 568 . 161 ILE CA C 59.683 0.10 1 569 . 161 ILE CB C 38.983 0.20 1 570 . 161 ILE N N 128.940 0.20 1 571 . 162 SER H H 9.261 0.02 1 572 . 162 SER CA C 56.232 0.10 1 573 . 162 SER CB C 66.285 0.20 1 574 . 162 SER N N 122.560 0.20 1 575 . 163 GLN H H 8.436 0.02 1 576 . 163 GLN CA C 53.492 0.10 1 577 . 163 GLN CB C 30.402 0.20 1 578 . 163 GLN N N 122.195 0.20 1 579 . 164 GLU H H 8.942 0.02 1 580 . 164 GLU CA C 54.305 0.10 1 581 . 164 GLU CB C 30.830 0.20 1 582 . 164 GLU N N 127.861 0.20 1 583 . 165 GLY H H 8.315 0.02 1 584 . 165 GLY CA C 46.947 0.10 1 585 . 165 GLY N N 117.505 0.20 1 586 . 166 ASP H H 8.280 0.02 1 587 . 166 ASP CA C 52.787 0.10 1 588 . 166 ASP CB C 40.011 0.20 1 589 . 166 ASP N N 127.010 0.20 1 590 . 167 LEU H H 7.786 0.02 1 591 . 167 LEU CA C 53.356 0.10 1 592 . 167 LEU CB C 43.656 0.20 1 593 . 167 LEU N N 121.055 0.20 1 594 . 168 TYR H H 9.310 0.02 1 595 . 168 TYR CA C 56.306 0.10 1 596 . 168 TYR CB C 40.773 0.20 1 597 . 168 TYR N N 126.514 0.20 1 598 . 169 SER H H 9.025 0.02 1 599 . 169 SER CA C 56.116 0.10 1 600 . 169 SER CB C 66.166 0.20 1 601 . 169 SER N N 115.320 0.20 1 602 . 170 LEU H H 8.803 0.02 1 603 . 170 LEU CA C 52.377 0.10 1 604 . 170 LEU CB C 42.856 0.20 1 605 . 170 LEU N N 125.484 0.20 1 606 . 171 LEU H H 9.132 0.02 1 607 . 171 LEU CA C 52.449 0.10 1 608 . 171 LEU CB C 43.711 0.20 1 609 . 171 LEU N N 128.566 0.20 1 610 . 172 ILE H H 9.133 0.02 1 611 . 172 ILE CA C 59.934 0.10 1 612 . 172 ILE CB C 37.856 0.20 1 613 . 172 ILE N N 128.966 0.20 1 614 . 173 ALA H H 7.823 0.02 1 615 . 173 ALA CA C 55.215 0.10 1 616 . 173 ALA CB C 18.698 0.20 1 617 . 173 ALA N N 129.049 0.20 1 618 . 174 GLU H H 7.978 0.02 1 619 . 174 GLU CA C 54.862 0.10 1 620 . 174 GLU CB C 31.369 0.20 1 621 . 174 GLU N N 115.476 0.20 1 622 . 175 ALA H H 8.434 0.02 1 623 . 175 ALA CA C 51.428 0.10 1 624 . 175 ALA CB C 19.534 0.20 1 625 . 175 ALA N N 126.365 0.20 1 626 . 176 TYR H H 9.661 0.02 1 627 . 176 TYR CA C 56.202 0.10 1 628 . 176 TYR CB C 39.282 0.20 1 629 . 176 TYR N N 123.429 0.20 1 630 . 177 PRO CA C 66.046 0.10 1 631 . 177 PRO CB C 31.595 0.20 1 632 . 178 GLU H H 9.628 0.02 1 633 . 178 GLU CA C 57.964 0.10 1 634 . 178 GLU CB C 27.851 0.20 1 635 . 178 GLU N N 116.426 0.20 1 636 . 179 ASP H H 8.827 0.02 1 637 . 179 ASP CA C 54.820 0.10 1 638 . 179 ASP CB C 40.872 0.20 1 639 . 179 ASP N N 119.017 0.20 1 640 . 180 SER H H 8.054 0.02 1 641 . 180 SER CA C 59.605 0.10 1 642 . 180 SER CB C 64.265 0.20 1 643 . 180 SER N N 116.668 0.20 1 644 . 181 GLY H H 9.196 0.02 1 645 . 181 GLY CA C 44.727 0.10 1 646 . 181 GLY N N 110.967 0.20 1 647 . 182 THR H H 9.005 0.02 1 648 . 182 THR CA C 61.940 0.10 1 649 . 182 THR CB C 68.307 0.20 1 650 . 182 THR N N 118.741 0.20 1 651 . 183 TYR H H 9.612 0.02 1 652 . 183 TYR CA C 56.403 0.10 1 653 . 183 TYR CB C 40.574 0.20 1 654 . 183 TYR N N 132.072 0.20 1 655 . 184 SER H H 9.215 0.02 1 656 . 184 SER CA C 55.404 0.10 1 657 . 184 SER CB C 66.786 0.20 1 658 . 184 SER N N 113.599 0.20 1 659 . 185 VAL H H 8.978 0.02 1 660 . 185 VAL CA C 58.668 0.10 1 661 . 185 VAL CB C 34.278 0.20 1 662 . 185 VAL N N 119.929 0.20 1 663 . 186 ASN H H 8.897 0.02 1 664 . 186 ASN CA C 50.539 0.10 1 665 . 186 ASN CB C 41.681 0.20 1 666 . 186 ASN N N 123.232 0.20 1 667 . 187 ALA H H 9.236 0.02 1 668 . 187 ALA CA C 48.889 0.10 1 669 . 187 ALA CB C 23.089 0.20 1 670 . 187 ALA N N 126.375 0.20 1 671 . 188 THR H H 8.712 0.02 1 672 . 188 THR CA C 60.608 0.10 1 673 . 188 THR CB C 71.560 0.20 1 674 . 188 THR N N 115.856 0.20 1 675 . 189 ASN H H 9.156 0.02 1 676 . 189 ASN CA C 51.021 0.10 1 677 . 189 ASN CB C 40.419 0.20 1 678 . 189 ASN N N 123.612 0.20 1 679 . 190 SER CA C 59.800 0.10 1 680 . 190 SER CB C 62.873 0.20 1 681 . 191 VAL H H 7.596 0.02 1 682 . 191 VAL CA C 60.670 0.10 1 683 . 191 VAL CB C 32.399 0.20 1 684 . 191 VAL N N 113.628 0.20 1 685 . 192 GLY H H 7.781 0.02 1 686 . 192 GLY CA C 45.509 0.10 1 687 . 192 GLY N N 107.784 0.20 1 688 . 193 ARG H H 8.307 0.02 1 689 . 193 ARG CA C 53.627 0.10 1 690 . 193 ARG CB C 34.087 0.20 1 691 . 193 ARG N N 117.186 0.20 1 692 . 194 ALA H H 9.095 0.02 1 693 . 194 ALA CA C 50.801 0.10 1 694 . 194 ALA CB C 23.179 0.20 1 695 . 194 ALA N N 125.327 0.20 1 696 . 195 THR H H 8.717 0.02 1 697 . 195 THR CA C 60.340 0.10 1 698 . 195 THR CB C 71.488 0.20 1 699 . 195 THR N N 115.821 0.20 1 700 . 196 SER H H 8.422 0.02 1 701 . 196 SER CA C 55.678 0.10 1 702 . 196 SER CB C 64.588 0.20 1 703 . 196 SER N N 120.433 0.20 1 704 . 197 THR H H 8.124 0.02 1 705 . 197 THR CA C 60.479 0.10 1 706 . 197 THR CB C 71.156 0.20 1 707 . 197 THR N N 121.412 0.20 1 708 . 198 ALA H H 9.501 0.02 1 709 . 198 ALA CA C 51.120 0.10 1 710 . 198 ALA CB C 23.675 0.20 1 711 . 198 ALA N N 126.894 0.20 1 712 . 199 GLU H H 8.570 0.02 1 713 . 199 GLU CA C 54.521 0.10 1 714 . 199 GLU CB C 31.197 0.20 1 715 . 199 GLU N N 118.894 0.20 1 716 . 200 LEU H H 9.237 0.02 1 717 . 200 LEU CA C 52.753 0.10 1 718 . 200 LEU CB C 44.716 0.20 1 719 . 200 LEU N N 125.754 0.20 1 720 . 201 LEU H H 8.818 0.02 1 721 . 201 LEU CA C 53.311 0.10 1 722 . 201 LEU CB C 43.854 0.20 1 723 . 201 LEU N N 130.253 0.20 1 724 . 202 VAL CA C 59.475 0.10 1 725 . 202 VAL CB C 31.133 0.20 1 726 . 203 GLN H H 8.902 0.02 1 727 . 203 GLN CA C 54.546 0.10 1 728 . 203 GLN CB C 30.833 0.20 1 729 . 203 GLN N N 125.615 0.20 1 730 . 204 GLY H H 8.317 0.02 1 731 . 204 GLY CA C 45.268 0.10 1 732 . 204 GLY N N 117.500 0.20 1 stop_ save_