data_5816 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignment of The Dimer Yeast Peroxiredoxin YLR109w ; _BMRB_accession_number 5816 _BMRB_flat_file_name bmr5816.str _Entry_type original _Submission_date 2003-06-04 _Accession_date 2003-06-04 _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 Trivelli Xavier . . 2 Krimm Isabelle . . 3 Tsan Pascale . . 4 Lancelin Jean-Marc . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 513 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-12-18 original author . stop_ _Original_release_date 2003-12-18 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 resonance assignments of the dimeric yeast peroxiredoxin YLR109w ; _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 Trivelli Xavier . . 2 Krimm Isabelle . . 3 Verdoucq Lionel . . 4 Chartier Yvette . . 5 Tsan Pascale . . 6 Meyer Yves . . 7 Lancelin Jean-Marc . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 95 _Page_last 96 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem. 1999 Jul 9;274(28):19714-22. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10391912 _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_YLR109w _Saveframe_category molecular_system _Mol_system_name 'YLR109w dimer' _Abbreviation_common YLR109w _Enzyme_commission_number 1.6.4.- loop_ _Mol_system_component_name _Mol_label 'YLR109w subunit 1' $YLR109w 'YLR109w subunit 2' $YLR109w stop_ _System_molecular_weight . _System_physical_state reduced _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'YLR109w subunit 1' 1 'YLR109w subunit 2' stop_ loop_ _Biological_function 'alkyl hydroperoxyde reductase' peroxydase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YLR109w _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YLR109w _Name_variant Ahp1 _Abbreviation_common YLR109w _Molecular_mass 19115 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; MSDLVNKKFPAGDYKFQYIA ISQSDADSESCKMPQTVEWS KLISENKKVIITGAPAAFSP TCTVSHIPGYINYLDELVKE KEVDQVIVVTVDNPFANQAW AKSLGVKDTTHIKFASDPGC AFTKSIGFELAVGDGVYWSG RWAMVVENGIVTYAAKETNP GTDVTVSSVESVLAHL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ASP 4 LEU 5 VAL 6 ASN 7 LYS 8 LYS 9 PHE 10 PRO 11 ALA 12 GLY 13 ASP 14 TYR 15 LYS 16 PHE 17 GLN 18 TYR 19 ILE 20 ALA 21 ILE 22 SER 23 GLN 24 SER 25 ASP 26 ALA 27 ASP 28 SER 29 GLU 30 SER 31 CYS 32 LYS 33 MET 34 PRO 35 GLN 36 THR 37 VAL 38 GLU 39 TRP 40 SER 41 LYS 42 LEU 43 ILE 44 SER 45 GLU 46 ASN 47 LYS 48 LYS 49 VAL 50 ILE 51 ILE 52 THR 53 GLY 54 ALA 55 PRO 56 ALA 57 ALA 58 PHE 59 SER 60 PRO 61 THR 62 CYS 63 THR 64 VAL 65 SER 66 HIS 67 ILE 68 PRO 69 GLY 70 TYR 71 ILE 72 ASN 73 TYR 74 LEU 75 ASP 76 GLU 77 LEU 78 VAL 79 LYS 80 GLU 81 LYS 82 GLU 83 VAL 84 ASP 85 GLN 86 VAL 87 ILE 88 VAL 89 VAL 90 THR 91 VAL 92 ASP 93 ASN 94 PRO 95 PHE 96 ALA 97 ASN 98 GLN 99 ALA 100 TRP 101 ALA 102 LYS 103 SER 104 LEU 105 GLY 106 VAL 107 LYS 108 ASP 109 THR 110 THR 111 HIS 112 ILE 113 LYS 114 PHE 115 ALA 116 SER 117 ASP 118 PRO 119 GLY 120 CYS 121 ALA 122 PHE 123 THR 124 LYS 125 SER 126 ILE 127 GLY 128 PHE 129 GLU 130 LEU 131 ALA 132 VAL 133 GLY 134 ASP 135 GLY 136 VAL 137 TYR 138 TRP 139 SER 140 GLY 141 ARG 142 TRP 143 ALA 144 MET 145 VAL 146 VAL 147 GLU 148 ASN 149 GLY 150 ILE 151 VAL 152 THR 153 TYR 154 ALA 155 ALA 156 LYS 157 GLU 158 THR 159 ASN 160 PRO 161 GLY 162 THR 163 ASP 164 VAL 165 THR 166 VAL 167 SER 168 SER 169 VAL 170 GLU 171 SER 172 VAL 173 LEU 174 ALA 175 HIS 176 LEU 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 4DSQ "Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Oxidized Form" 100.00 184 100.00 100.00 4.40e-125 PDB 4DSR "Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Reduced Form" 100.00 184 100.00 100.00 4.40e-125 PDB 4DSS "Crystal Structure Of Peroxiredoxin Ahp1 From Saccharomyces Cerevisiae In Complex With Thioredoxin Trx2" 100.00 176 99.43 99.43 8.56e-124 PDB 4H86 "Crystal Structure Of Ahp1 From Saccharomyces Cerevisiae In Reduced Form" 100.00 199 100.00 100.00 2.23e-125 DBJ GAA24996 "K7_Ahp1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 176 100.00 100.00 3.67e-125 EMBL CAA61687 "L2916 [Saccharomyces cerevisiae]" 100.00 176 100.00 100.00 3.67e-125 EMBL CAA97676 "unnamed protein product [Saccharomyces cerevisiae]" 100.00 176 100.00 100.00 3.67e-125 EMBL CAY81346 "Ahp1p [Saccharomyces cerevisiae EC1118]" 100.00 176 100.00 100.00 3.67e-125 GB AAB67554 "Ylr109wp [Saccharomyces cerevisiae]" 100.00 176 100.00 100.00 3.67e-125 GB AHY78511 "Ahp1p [Saccharomyces cerevisiae YJM993]" 100.00 176 100.00 100.00 3.67e-125 GB EDN59654 "alkyl hydroperoxide reductase [Saccharomyces cerevisiae YJM789]" 100.00 176 100.00 100.00 3.67e-125 GB EDV09411 "alkyl hydroperoxide reductase [Saccharomyces cerevisiae RM11-1a]" 100.00 176 100.00 100.00 3.67e-125 GB EDZ70648 "YLR109Wp-like protein [Saccharomyces cerevisiae AWRI1631]" 100.00 176 100.00 100.00 3.67e-125 REF NP_013210 "Ahp1p [Saccharomyces cerevisiae S288c]" 100.00 176 100.00 100.00 3.67e-125 SP P38013 "RecName: Full=Peroxiredoxin type-2; AltName: Full=AHPC1; AltName: Full=Cytoplasmic thiol peroxidase 3; Short=cTPx 3; AltName: F" 100.00 176 100.00 100.00 3.67e-125 TPG DAA09425 "TPA: Ahp1p [Saccharomyces cerevisiae S288c]" 100.00 176 100.00 100.00 3.67e-125 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $YLR109w 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae cytoplasm 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 $YLR109w '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 $YLR109w 2.0 mM '[U-50% 2H; U-13C; U-15N]' DTT 5.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YLR109w 2.0 mM [U-15N] DTT 5.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_PIPP_suite _Saveframe_category software _Name PIPP _Version . loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA_Unity+ _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA_Unity+ _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_MQ-HNCOCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name MQ-HNCOCA _Sample_label . save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label . save_ save_HN(CA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label . save_ save_(H)C(CCO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CCO)NH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name MQ-HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details 'The sample was reduced by 5 DTT equvalents.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.2 n/a temperature 311 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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal 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 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'YLR109w subunit 1' _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 MET H H 8.28 0.02 1 2 . 1 MET C C 176.0 0.1 1 3 . 1 MET CA C 55.4 0.2 1 4 . 1 MET CB C 32.4 0.3 1 5 . 1 MET CG C 31.6 0.4 1 6 . 1 MET N N 121.8 0.1 1 7 . 2 SER H H 8.12 0.02 1 8 . 2 SER C C 174.9 0.1 1 9 . 2 SER CA C 58.1 0.2 1 10 . 2 SER CB C 64.0 0.3 1 11 . 2 SER N N 115.91 0.1 1 12 . 3 ASP H H 8.41 0.02 1 13 . 3 ASP C C 176.0 0.1 1 14 . 3 ASP CA C 54.8 0.2 1 15 . 3 ASP CB C 40.3 0.3 1 16 . 3 ASP N N 123.9 0.1 1 17 . 4 LEU H H 7.92 0.02 1 18 . 4 LEU C C 177.4 0.1 1 19 . 4 LEU CA C 55.6 0.2 1 20 . 4 LEU CB C 43.5 0.3 1 21 . 4 LEU N N 118.5 0.1 1 22 . 5 VAL H H 7.11 0.02 1 23 . 5 VAL C C 176.2 0.1 1 24 . 5 VAL CA C 64.3 0.2 1 25 . 5 VAL CB C 30.8 0.3 1 26 . 5 VAL N N 117.4 0.1 1 27 . 6 ASN H H 9.43 0.02 1 28 . 6 ASN C C 174.2 0.1 1 29 . 6 ASN CA C 55.0 0.2 1 30 . 6 ASN CB C 36.7 0.3 1 31 . 6 ASN CG C 178.2 0.1 1 32 . 6 ASN N N 117.8 0.1 1 33 . 6 ASN ND2 N 112.2 0.1 1 34 . 6 ASN HD21 H 7.55 0.02 1 35 . 6 ASN HD22 H 6.86 0.02 1 36 . 7 LYS H H 7.74 0.02 1 37 . 7 LYS C C 175.9 0.1 1 38 . 7 LYS CA C 54.0 0.2 1 39 . 7 LYS CB C 34.5 0.3 1 40 . 7 LYS N N 117.6 0.1 1 41 . 8 LYS H H 8.38 0.02 1 42 . 8 LYS C C 177.4 0.1 1 43 . 8 LYS CA C 56.5 0.2 1 44 . 8 LYS CB C 32.1 0.3 1 45 . 8 LYS N N 119.9 0.1 1 46 . 9 PHE H H 8.65 0.02 1 47 . 9 PHE C C 174.4 0.1 1 48 . 9 PHE CA C 55.6 0.2 1 49 . 9 PHE CB C 39.9 0.3 1 50 . 9 PHE N N 125.0 0.1 1 51 . 10 PRO C C 173.9 0.1 1 52 . 10 PRO CA C 61.2 0.2 1 53 . 10 PRO CB C 27.5 0.3 1 54 . 11 ALA H H 7.63 0.02 1 55 . 11 ALA C C 177.3 0.1 1 56 . 11 ALA CA C 53.8 0.2 1 57 . 11 ALA CB C 19.1 0.3 1 58 . 11 ALA N N 125.3 0.1 1 59 . 12 GLY H H 8.17 0.02 1 60 . 12 GLY C C 174.3 0.1 1 61 . 12 GLY CA C 46.4 0.2 1 62 . 12 GLY N N 101.5 0.1 1 63 . 13 ASP H H 8.14 0.02 1 64 . 13 ASP C C 176.7 0.1 1 65 . 13 ASP CA C 52.6 0.2 1 66 . 13 ASP CB C 40.2 0.3 1 67 . 13 ASP N N 125.3 0.1 1 68 . 14 TYR H H 8.04 0.02 1 69 . 14 TYR C C 176.8 0.1 1 70 . 14 TYR CA C 60.3 0.2 1 71 . 14 TYR CB C 39.6 0.3 1 72 . 14 TYR N N 118.0 0.1 1 73 . 15 LYS H H 9.56 0.02 1 74 . 15 LYS C C 175.5 0.1 1 75 . 15 LYS CA C 54.9 0.2 1 76 . 15 LYS CB C 35.7 0.3 1 77 . 15 LYS N N 122.5 0.1 1 78 . 16 PHE H H 8.91 0.02 1 79 . 16 PHE C C 173.6 0.1 1 80 . 16 PHE CA C 54.6 0.2 1 81 . 16 PHE CB C 41.7 0.3 1 82 . 16 PHE N N 119.2 0.1 1 83 . 17 GLN H H 8.36 0.02 1 84 . 17 GLN C C 176.4 0.1 1 85 . 17 GLN CA C 53.3 0.2 1 86 . 17 GLN CB C 33.4 0.3 1 87 . 17 GLN N N 114.9 0.1 1 88 . 18 TYR H H 9.01 0.02 1 89 . 18 TYR C C 171.1 0.1 1 90 . 18 TYR CA C 56.1 0.2 1 91 . 18 TYR CB C 42.0 0.3 1 92 . 18 TYR N N 119.8 0.1 1 93 . 19 ILE H H 8.33 0.02 1 94 . 19 ILE C C 174.3 0.1 1 95 . 19 ILE CA C 60.0 0.2 1 96 . 19 ILE CB C 37.9 0.3 1 97 . 19 ILE N N 120.6 0.1 1 98 . 20 ALA H H 7.93 0.02 1 99 . 20 ALA C C 176.1 0.1 1 100 . 20 ALA CA C 51.9 0.2 1 101 . 20 ALA CB C 19.3 0.3 1 102 . 20 ALA N N 129.3 0.1 1 103 . 21 ILE H H 8.49 0.02 1 104 . 21 ILE C C 175.0 0.1 1 105 . 21 ILE CA C 61.2 0.2 1 106 . 21 ILE CB C 41.4 0.3 1 107 . 21 ILE CG2 C 16.9 0.4 1 108 . 21 ILE N N 118.9 0.1 1 109 . 22 SER H H 8.19 0.02 1 110 . 22 SER C C 174.7 0.1 1 111 . 22 SER CA C 56.2 0.2 1 112 . 22 SER CB C 65.2 0.3 1 113 . 22 SER N N 121.0 0.1 1 114 . 23 GLN H H 9.01 0.02 1 115 . 23 GLN C C 176.6 0.1 1 116 . 23 GLN CA C 56.4 0.2 1 117 . 23 GLN CB C 28.6 0.3 1 118 . 23 GLN CG C 33.8 0.4 1 119 . 23 GLN CD C 180.5 0.1 1 120 . 23 GLN N N 123.6 0.1 1 121 . 23 GLN NE2 N 112.7 0.1 1 122 . 23 GLN HE21 H 7.75 0.02 1 123 . 23 GLN HE22 H 6.92 0.02 1 124 . 24 SER H H 8.23 0.02 1 125 . 24 SER C C 175.0 0.1 1 126 . 24 SER CA C 57.9 0.2 1 127 . 24 SER CB C 63.8 0.3 1 128 . 24 SER N N 114.0 0.1 1 129 . 25 ASP H H 8.25 0.02 1 130 . 25 ASP C C 176.6 0.1 1 131 . 25 ASP CA C 54.5 0.2 1 132 . 25 ASP CB C 40.3 0.3 1 133 . 25 ASP N N 124.5 0.1 1 134 . 26 ALA H H 8.03 0.02 1 135 . 26 ALA C C 178.0 0.1 1 136 . 26 ALA CA C 53.4 0.2 1 137 . 26 ALA CB C 18.6 0.3 1 138 . 26 ALA N N 122.7 0.1 1 139 . 27 ASP H H 8.02 0.02 1 140 . 27 ASP C C 176.5 0.1 1 141 . 27 ASP CA C 53.9 0.2 1 142 . 27 ASP CB C 40.8 0.3 1 143 . 27 ASP N N 116.6 0.1 1 144 . 28 SER H H 7.73 0.02 1 145 . 28 SER C C 176.1 0.1 1 146 . 28 SER CA C 59.2 0.2 1 147 . 28 SER CB C 63.8 0.3 1 148 . 28 SER N N 115.4 0.1 1 149 . 29 GLU H H 8.68 0.02 1 150 . 29 GLU C C 178.3 0.1 1 151 . 29 GLU CA C 58.3 0.2 1 152 . 29 GLU CB C 28.8 0.3 1 153 . 29 GLU CG C 35.9 0.4 1 154 . 29 GLU N N 122.6 0.1 1 155 . 30 SER H H 8.11 0.02 1 156 . 30 SER C C 174.7 0.1 1 157 . 30 SER CA C 63.3 0.2 1 158 . 30 SER CB C 59.8 0.3 1 159 . 30 SER N N 114.1 0.1 1 160 . 31 CYS H H 7.65 0.02 1 161 . 31 CYS C C 174.3 0.1 1 162 . 31 CYS CA C 58.4 0.2 1 163 . 31 CYS CB C 27.9 0.3 1 164 . 31 CYS N N 117.9 0.1 1 165 . 32 LYS H H 7.79 0.02 1 166 . 32 LYS C C 175.4 0.1 1 167 . 32 LYS CA C 56.5 0.2 1 168 . 32 LYS CB C 34.31 0.3 1 169 . 32 LYS CG C 24.4 0.4 1 170 . 32 LYS CD C 28.9 0.4 1 171 . 32 LYS N N 119.8 0.1 1 172 . 33 MET H H 7.85 0.02 1 173 . 33 MET C C 173.8 0.1 1 174 . 33 MET CA C 51.3 0.2 1 175 . 33 MET CB C 33.0 0.3 1 176 . 33 MET N N 116.9 0.1 1 177 . 34 PRO C C 175.8 0.1 1 178 . 34 PRO CA C 62.4 0.2 1 179 . 34 PRO CB C 31.2 0.3 1 180 . 35 GLN H H 8.89 0.02 1 181 . 35 GLN C C 174.9 0.1 1 182 . 35 GLN CA C 53.5 0.2 1 183 . 35 GLN CB C 31.0 0.3 1 184 . 35 GLN CG C 33.7 0.4 1 185 . 35 GLN CD C 180.4 0.1 1 186 . 35 GLN N N 122.5 0.1 1 187 . 35 GLN NE2 N 112.5 0.1 1 188 . 35 GLN HE21 H 7.38 0.02 1 189 . 35 GLN HE22 H 6.83 0.02 1 190 . 36 THR H H 8.51 0.02 1 191 . 36 THR C C 173.9 0.1 1 192 . 36 THR CA C 61.9 0.2 1 193 . 36 THR CB C 69.2 0.3 1 194 . 36 THR CG2 C 21.9 0.4 1 195 . 36 THR N N 118.7 0.1 1 196 . 37 VAL H H 8.80 0.02 1 197 . 37 VAL C C 174.3 0.1 1 198 . 37 VAL CA C 59.9 0.2 1 199 . 37 VAL CB C 33.4 0.3 1 200 . 37 VAL N N 128.8 0.1 1 201 . 38 GLU H H 8.73 0.02 1 202 . 38 GLU C C 177.6 0.1 1 203 . 38 GLU CA C 56.2 0.2 1 204 . 38 GLU CB C 29.1 0.3 1 205 . 38 GLU CG C 36.5 0.4 1 206 . 38 GLU N N 124.7 0.1 1 207 . 39 TRP H H 8.47 0.02 1 208 . 39 TRP C C 178.2 0.1 1 209 . 39 TRP CA C 61.9 0.2 1 210 . 39 TRP CB C 29.3 0.3 1 211 . 39 TRP N N 126.6 0.1 1 212 . 40 SER H H 9.50 0.02 1 213 . 40 SER C C 178.2 0.1 1 214 . 40 SER CA C 60.6 0.2 1 215 . 40 SER CB C 62.0 0.3 1 216 . 40 SER N N 117.7 0.1 1 217 . 41 LYS H H 6.84 0.02 1 218 . 41 LYS C C 177.7 0.1 1 219 . 41 LYS CA C 58.1 0.2 1 220 . 41 LYS CB C 31.9 0.3 1 221 . 41 LYS CG C 24.3 0.4 1 222 . 41 LYS N N 123.7 0.1 1 223 . 42 LEU H H 7.49 0.02 1 224 . 42 LEU C C 179.8 0.1 1 225 . 42 LEU CA C 57.8 0.2 1 226 . 42 LEU CB C 40.9 0.3 1 227 . 42 LEU N N 119.6 0.1 1 228 . 43 ILE H H 7.94 0.02 1 229 . 43 ILE C C 176.6 0.1 1 230 . 43 ILE CA C 60.8 0.2 1 231 . 43 ILE CB C 35.6 0.3 1 232 . 43 ILE N N 115.2 0.1 1 233 . 44 SER H H 7.69 0.02 1 234 . 44 SER C C 176.4 0.1 1 235 . 44 SER CA C 60.6 0.2 1 236 . 44 SER CB C 63.5 0.3 1 237 . 44 SER N N 113.6 0.1 1 238 . 45 GLU H H 7.64 0.02 1 239 . 45 GLU C C 175.5 0.1 1 240 . 45 GLU CA C 56.4 0.2 1 241 . 45 GLU CB C 30.1 0.3 1 242 . 45 GLU CG C 36.3 0.4 1 243 . 45 GLU N N 117.35 0.1 1 244 . 46 ASN H H 7.12 0.02 1 245 . 46 ASN C C 172.2 0.1 1 246 . 46 ASN CA C 52.2 0.2 1 247 . 46 ASN CB C 42.0 0.3 1 248 . 46 ASN N N 116.9 0.1 1 249 . 47 LYS H H 8.24 0.02 1 250 . 47 LYS C C 177.5 0.1 1 251 . 47 LYS CA C 59.3 0.2 1 252 . 47 LYS CB C 32.2 0.3 1 253 . 47 LYS N N 122.0 0.1 1 254 . 48 LYS H H 9.24 0.02 1 255 . 48 LYS C C 174.8 0.1 1 256 . 48 LYS CA C 56.3 0.2 1 257 . 48 LYS CB C 34.1 0.3 1 258 . 48 LYS N N 122.0 0.1 1 259 . 49 VAL H H 9.24 0.02 1 260 . 49 VAL CA C 60.0 0.2 1 261 . 49 VAL CB C 35.9 0.3 1 262 . 49 VAL N N 126.5 0.1 1 263 . 50 ILE C C 173.8 0.1 1 264 . 50 ILE CA C 58.9 0.2 1 265 . 50 ILE CB C 39.9 0.3 1 266 . 51 ILE H H 9.15 0.02 1 267 . 51 ILE C C 174.1 0.1 1 268 . 51 ILE CA C 58.9 0.2 1 269 . 51 ILE CB C 41.4 0.3 1 270 . 51 ILE N N 126.9 0.1 1 271 . 52 THR H H 9.07 0.02 1 272 . 52 THR C C 170.0 0.1 1 273 . 52 THR CA C 57.6 0.2 1 274 . 52 THR N N 121.8 0.1 1 275 . 53 GLY H H 6.62 0.02 1 276 . 53 GLY C C 180.8 0.1 1 277 . 53 GLY CA C 42.9 0.2 1 278 . 53 GLY N N 115.4 0.1 1 279 . 54 ALA H H 8.53 0.02 1 280 . 54 ALA C C 176.3 0.1 1 281 . 54 ALA CA C 57.2 0.2 1 282 . 54 ALA CB C 21.1 0.3 1 283 . 54 ALA N N 122.8 0.1 1 284 . 55 PRO C C 177.7 0.1 1 285 . 55 PRO CA C 64.6 0.2 1 286 . 55 PRO CB C 33.0 0.3 1 287 . 56 ALA H H 8.18 0.02 1 288 . 56 ALA C C 174.0 0.1 1 289 . 56 ALA CA C 52.1 0.2 1 290 . 56 ALA CB C 19.3 0.3 1 291 . 56 ALA N N 119.6 0.1 1 292 . 57 ALA H H 9.02 0.02 1 293 . 57 ALA C C 176.5 0.1 1 294 . 57 ALA CA C 52.4 0.2 1 295 . 57 ALA CB C 17.0 0.3 1 296 . 57 ALA N N 129.1 0.1 1 297 . 58 PHE H H 7.88 0.02 1 298 . 58 PHE C C 179.4 0.1 1 299 . 58 PHE CA C 54.9 0.2 1 300 . 58 PHE CB C 40.8 0.3 1 301 . 58 PHE N N 123.2 0.1 1 302 . 60 PRO C C 177.7 0.1 1 303 . 61 THR H H 8.18 0.02 1 304 . 61 THR CA C 66.4 0.2 1 305 . 61 THR CB C 69.9 0.3 1 306 . 61 THR N N 111.8 0.1 1 307 . 62 CYS C C 178.2 0.1 1 308 . 62 CYS CA C 66.6 0.2 1 309 . 62 CYS CB C 31.4 0.3 1 310 . 63 THR H H 8.49 0.02 1 311 . 63 THR C C 173.5 0.1 1 312 . 63 THR CA C 66.6 0.2 1 313 . 63 THR CB C 67.8 0.3 1 314 . 63 THR N N 116.2 0.1 1 315 . 64 VAL H H 8.55 0.02 1 316 . 64 VAL C C 177.9 0.1 1 317 . 64 VAL CA C 63.9 0.2 1 318 . 64 VAL CB C 32.1 0.3 1 319 . 64 VAL N N 116.3 0.1 1 320 . 68 PRO C C 177.8 0.1 1 321 . 68 PRO CA C 66.6 0.2 1 322 . 68 PRO CB C 29.9 0.3 1 323 . 69 GLY H H 7.62 0.02 1 324 . 69 GLY C C 175.8 0.1 1 325 . 69 GLY CA C 47.8 0.2 1 326 . 69 GLY N N 102.5 0.1 1 327 . 70 TYR H H 7.45 0.02 1 328 . 70 TYR C C 175.9 0.1 1 329 . 70 TYR CA C 63.0 0.2 1 330 . 70 TYR CB C 37.7 0.3 1 331 . 70 TYR N N 118.8 0.1 1 332 . 71 ILE H H 6.95 0.02 1 333 . 71 ILE C C 179.4 0.1 1 334 . 71 ILE CA C 64.0 0.2 1 335 . 71 ILE CB C 37.3 0.3 1 336 . 71 ILE N N 115.2 0.1 1 337 . 72 ASN H H 8.91 0.02 1 338 . 72 ASN C C 177.4 0.1 1 339 . 72 ASN CA C 55.4 0.2 1 340 . 72 ASN CB C 37.7 0.3 1 341 . 72 ASN CG C 175.8 0.1 1 342 . 72 ASN N N 118.6 0.1 1 343 . 72 ASN ND2 N 110.8 0.1 1 344 . 72 ASN HD21 H 7.11 0.02 1 345 . 72 ASN HD22 H 6.76 0.20 1 346 . 73 TYR H H 7.61 0.02 1 347 . 73 TYR C C 175.6 0.1 1 348 . 73 TYR CA C 58.5 0.2 1 349 . 73 TYR CB C 37.7 0.3 1 350 . 73 TYR N N 115.2 0.1 1 351 . 74 LEU H H 7.23 0.02 1 352 . 74 LEU C C 177.4 0.1 1 353 . 74 LEU CA C 59.2 0.2 1 354 . 74 LEU CB C 41.4 0.3 1 355 . 74 LEU N N 123.2 0.1 1 356 . 75 ASP H H 8.44 0.02 1 357 . 75 ASP C C 178.2 0.1 1 358 . 75 ASP CA C 57.6 0.2 1 359 . 75 ASP CB C 39.7 0.3 1 360 . 75 ASP N N 115.8 0.1 1 361 . 76 GLU H H 7.85 0.02 1 362 . 76 GLU C C 179.2 0.1 1 363 . 76 GLU CA C 59.3 0.2 1 364 . 76 GLU CB C 28.4 0.3 1 365 . 76 GLU CG C 35.0 0.4 1 366 . 76 GLU N N 120.6 0.1 1 367 . 77 LEU H H 8.72 0.02 1 368 . 77 LEU C C 178.1 0.1 1 369 . 77 LEU CA C 57.8 0.2 1 370 . 77 LEU CB C 40.1 0.3 1 371 . 77 LEU N N 119.1 0.1 1 372 . 78 VAL H H 8.34 0.02 1 373 . 78 VAL C C 178.6 0.1 1 374 . 78 VAL CA C 64.1 0.2 1 375 . 78 VAL CB C 32.0 0.3 1 376 . 78 VAL CG1 C 20.73 0.4 1 377 . 78 VAL CG2 C 20.73 0.4 1 378 . 78 VAL N N 117.6 0.1 1 379 . 79 LYS H H 8.44 0.02 1 380 . 79 LYS C C 178.4 0.1 1 381 . 79 LYS CA C 58.5 0.2 1 382 . 79 LYS CB C 32.2 0.3 1 383 . 79 LYS N N 116.4 0.1 1 384 . 80 GLU H H 8.12 0.02 1 385 . 80 GLU C C 178.3 0.1 1 386 . 80 GLU CA C 57.0 0.2 1 387 . 80 GLU CB C 29.7 0.3 1 388 . 80 GLU CG C 35.7 0.4 1 389 . 80 GLU N N 114.9 0.1 1 390 . 81 LYS H H 7.22 0.02 1 391 . 81 LYS C C 175.2 0.1 1 392 . 81 LYS CA C 53.1 0.2 1 393 . 81 LYS CB C 31.1 0.3 1 394 . 81 LYS N N 113.4 0.1 1 395 . 82 GLU H H 7.03 0.02 1 396 . 82 GLU C C 174.6 0.1 1 397 . 82 GLU CA C 56.8 0.2 1 398 . 82 GLU CB C 26.4 0.3 1 399 . 82 GLU N N 112.0 0.1 1 400 . 83 VAL H H 8.15 0.02 1 401 . 83 VAL C C 175.4 0.1 1 402 . 83 VAL CA C 63.4 0.2 1 403 . 83 VAL CB C 31.1 0.3 1 404 . 83 VAL N N 118.6 0.1 1 405 . 84 ASP H H 8.96 0.02 1 406 . 84 ASP C C 177.6 0.1 1 407 . 84 ASP CA C 57.1 0.2 1 408 . 84 ASP CB C 44.2 0.3 1 409 . 84 ASP N N 124.5 0.1 1 410 . 85 GLN H H 7.17 0.02 1 411 . 85 GLN C C 173.1 0.1 1 412 . 85 GLN CA C 53.7 0.2 1 413 . 85 GLN CB C 33.2 0.3 1 414 . 85 GLN N N 113.6 0.1 1 415 . 86 VAL H H 8.49 0.02 1 416 . 86 VAL C C 174.3 0.1 1 417 . 86 VAL CA C 60.6 0.2 1 418 . 86 VAL CB C 32.4 0.3 1 419 . 86 VAL N N 122.9 0.1 1 420 . 87 ILE H H 8.37 0.02 1 421 . 87 ILE C C 174.9 0.1 1 422 . 87 ILE CA C 56.8 0.2 1 423 . 87 ILE CB C 31.4 0.3 1 424 . 87 ILE N N 128.4 0.1 1 425 . 88 VAL H H 9.36 0.02 1 426 . 88 VAL C C 174.3 0.1 1 427 . 88 VAL CA C 60.6 0.2 1 428 . 88 VAL N N 128.9 0.1 1 429 . 90 THR C C 174.5 0.1 1 430 . 90 THR CA C 58.6 0.2 1 431 . 91 VAL H H 8.51 0.02 1 432 . 91 VAL C C 176.8 0.1 1 433 . 91 VAL CA C 60.4 0.2 1 434 . 91 VAL CB C 30.7 0.3 1 435 . 91 VAL N N 108.8 0.1 1 436 . 92 ASP H H 8.23 0.02 1 437 . 92 ASP C C 175.5 0.1 1 438 . 92 ASP CA C 54.4 0.2 1 439 . 92 ASP CB C 41.8 0.3 1 440 . 92 ASP N N 120.5 0.1 1 441 . 93 ASN H H 9.17 0.02 1 442 . 93 ASN C C 173.1 0.1 1 443 . 93 ASN CA C 52.8 0.2 1 444 . 93 ASN CB C 36.6 0.3 1 445 . 93 ASN N N 121.1 0.1 1 446 . 94 PRO C C 179.0 0.1 1 447 . 94 PRO CA C 65.5 0.2 1 448 . 95 PHE H H 8.75 0.02 1 449 . 95 PHE C C 179.1 0.1 1 450 . 95 PHE CA C 60.0 0.2 1 451 . 95 PHE CB C 36.0 0.3 1 452 . 95 PHE N N 120.8 0.1 1 453 . 96 ALA H H 8.22 0.02 1 454 . 96 ALA C C 179.2 0.1 1 455 . 96 ALA CA C 54.0 0.2 1 456 . 96 ALA CB C 16.8 0.3 1 457 . 96 ALA N N 126.0 0.1 1 458 . 97 ASN H H 7.97 0.02 1 459 . 97 ASN C C 177.5 0.1 1 460 . 97 ASN CA C 55.0 0.2 1 461 . 97 ASN CB C 37.6 0.3 1 462 . 97 ASN N N 116.0 0.1 1 463 . 98 GLN H H 7.80 0.02 1 464 . 98 GLN C C 177.4 0.1 1 465 . 98 GLN CA C 58.7 0.2 1 466 . 98 GLN CB C 27.3 0.3 1 467 . 98 GLN N N 120.5 0.1 1 468 . 99 ALA H H 7.95 0.02 1 469 . 99 ALA C C 180.7 0.1 1 470 . 99 ALA CA C 55.0 0.2 1 471 . 99 ALA N N 122.0 0.1 1 472 . 100 TRP C C 178.3 0.1 1 473 . 100 TRP CA C 55.51 0.2 1 474 . 100 TRP CB C 26.7 0.3 1 475 . 101 ALA H H 7.96 0.02 1 476 . 101 ALA C C 180.0 0.1 1 477 . 101 ALA CA C 55.2 0.2 1 478 . 101 ALA N N 122.1 0.1 1 479 . 102 LYS H H 8.15 0.02 1 480 . 102 LYS C C 181.2 0.1 1 481 . 102 LYS CA C 59.8 0.2 1 482 . 102 LYS CB C 31.4 0.3 1 483 . 102 LYS N N 116.7 0.1 1 484 . 103 SER H H 8.13 0.02 1 485 . 103 SER C C 175.2 0.1 1 486 . 103 SER CA C 61.3 0.2 1 487 . 103 SER CB C 62.6 0.3 1 488 . 103 SER N N 118.6 0.1 1 489 . 104 LEU H H 7.27 0.02 1 490 . 104 LEU C C 176.5 0.1 1 491 . 104 LEU CA C 54.5 0.2 1 492 . 104 LEU CB C 42.0 0.3 1 493 . 104 LEU N N 122.0 0.1 1 494 . 105 GLY H H 7.55 0.02 1 495 . 105 GLY C C 174.8 0.1 1 496 . 105 GLY CA C 44.7 0.2 1 497 . 105 GLY N N 104.7 0.1 1 498 . 106 VAL H H 7.70 0.02 1 499 . 106 VAL C C 175.7 0.1 1 500 . 106 VAL CA C 64.0 0.2 1 501 . 106 VAL CB C 30.3 0.3 1 502 . 106 VAL CG1 C 21.9 0.4 1 503 . 106 VAL CG2 C 21.9 0.4 1 504 . 106 VAL N N 121.2 0.1 1 505 . 107 LYS H H 8.30 0.02 1 506 . 107 LYS C C 175.4 0.1 1 507 . 107 LYS CA C 55.3 0.2 1 508 . 107 LYS CB C 33.8 0.3 1 509 . 107 LYS N N 125.3 0.1 1 510 . 108 ASP H H 7.11 0.02 1 511 . 108 ASP C C 177.1 0.1 1 512 . 108 ASP CA C 53.4 0.2 1 513 . 108 ASP CB C 43.7 0.3 1 514 . 108 ASP N N 116.3 0.1 1 515 . 109 THR H H 8.33 0.02 1 516 . 109 THR C C 175.1 0.1 1 517 . 109 THR CA C 60.6 0.2 1 518 . 109 THR CB C 68.8 0.3 1 519 . 109 THR CG2 C 20.6 0.4 1 520 . 109 THR N N 113.5 0.1 1 521 . 110 THR H H 8.9 0.02 1 522 . 110 THR C C 175.5 0.1 1 523 . 110 THR CA C 68.3 0.2 1 524 . 110 THR CB C 67.5 0.3 1 525 . 110 THR CG2 C 20.1 0.4 1 526 . 110 THR N N 121.7 0.1 1 527 . 111 HIS H H 9.41 0.02 1 528 . 111 HIS C C 172.1 0.1 1 529 . 111 HIS CA C 55.0 0.2 1 530 . 111 HIS CB C 30.1 0.3 1 531 . 111 HIS N N 112.9 0.1 1 532 . 112 ILE H H 6.79 0.02 1 533 . 112 ILE C C 171.5 0.1 1 534 . 112 ILE CA C 57.5 0.2 1 535 . 112 ILE CB C 39.7 0.3 1 536 . 112 ILE N N 117.7 0.1 1 537 . 113 LYS H H 8.14 0.02 1 538 . 113 LYS CA C 53.8 0.2 1 539 . 113 LYS CB C 36.1 0.3 1 540 . 113 LYS N N 120.5 0.1 1 541 . 115 ALA C C 174.1 0.1 1 542 . 115 ALA CA C 59.0 0.2 1 543 . 116 SER H H 9.07 0.02 1 544 . 116 SER C C 174.0 0.1 1 545 . 116 SER CA C 57.6 0.2 1 546 . 116 SER N N 121.8 0.1 1 547 . 117 ASP H H 9.12 0.02 1 548 . 117 ASP C C 174.6 0.1 1 549 . 117 ASP CA C 50.3 0.2 1 550 . 117 ASP CB C 41.9 0.3 1 551 . 117 ASP N N 126.3 0.1 1 552 . 118 PRO C C 180.7 0.1 1 553 . 118 PRO CA C 63.5 0.2 1 554 . 118 PRO CB C 31.2 0.3 1 555 . 119 GLY H H 9.81 0.02 1 556 . 119 GLY C C 175.2 0.1 1 557 . 119 GLY CA C 46.1 0.2 1 558 . 119 GLY N N 114.7 0.1 1 559 . 120 CYS H H 9.20 0.02 1 560 . 120 CYS C C 176.5 0.1 1 561 . 120 CYS CA C 60.3 0.2 1 562 . 120 CYS CB C 28.8 0.3 1 563 . 120 CYS N N 121.1 0.1 1 564 . 121 ALA H H 6.92 0.02 1 565 . 121 ALA C C 180.0 0.1 1 566 . 121 ALA CA C 56.4 0.2 1 567 . 121 ALA CB C 19.1 0.3 1 568 . 121 ALA N N 121.2 0.1 1 569 . 122 PHE H H 10.76 0.02 1 570 . 122 PHE C C 179.2 0.1 1 571 . 122 PHE CA C 60.3 0.2 1 572 . 122 PHE CB C 38.9 0.3 1 573 . 122 PHE N N 123.1 0.1 1 574 . 123 THR H H 10.07 0.02 1 575 . 123 THR C C 176.9 0.1 1 576 . 123 THR CA C 61.3 0.2 1 577 . 123 THR N N 123.2 0.1 1 578 . 124 LYS H H 8.33 0.02 1 579 . 124 LYS C C 180.0 0.1 1 580 . 124 LYS CA C 58.0 0.2 1 581 . 124 LYS CB C 32.0 0.3 1 582 . 124 LYS N N 118.5 0.1 1 583 . 125 SER H H 7.25 0.02 1 584 . 125 SER C C 175.6 0.1 1 585 . 125 SER CA C 61.5 0.2 1 586 . 125 SER CB C 62.2 0.3 1 587 . 125 SER N N 119.1 0.1 1 588 . 126 ILE H H 6.18 0.02 1 589 . 126 ILE C C 174.8 0.1 1 590 . 126 ILE CA C 60.2 0.2 1 591 . 126 ILE CB C 36.6 0.3 1 592 . 126 ILE N N 112.4 0.1 1 593 . 127 GLY H H 7.17 0.02 1 594 . 127 GLY C C 176.8 0.1 1 595 . 127 GLY CA C 46.2 0.2 1 596 . 127 GLY N N 107.6 0.1 1 597 . 128 PHE H H 7.36 0.02 1 598 . 128 PHE C C 174.1 0.1 1 599 . 128 PHE CA C 53.1 0.2 1 600 . 128 PHE CB C 36.1 0.3 1 601 . 128 PHE N N 120.5 0.1 1 602 . 129 GLU H H 10.13 0.02 1 603 . 129 GLU C C 173.7 0.1 1 604 . 129 GLU CA C 56.6 0.2 1 605 . 129 GLU CB C 30.3 0.3 1 606 . 129 GLU N N 122.6 0.1 1 607 . 130 LEU H H 9.21 0.02 1 608 . 130 LEU C C 174.6 0.1 1 609 . 130 LEU CA C 53.7 0.2 1 610 . 130 LEU CB C 44.4 0.3 1 611 . 130 LEU N N 124.0 0.1 1 612 . 131 ALA H H 8.92 0.02 1 613 . 131 ALA C C 177.7 0.1 1 614 . 131 ALA CA C 52.0 0.2 1 615 . 131 ALA CB C 17.8 0.3 1 616 . 131 ALA N N 130.3 0.1 1 617 . 132 VAL H H 7.69 0.02 1 618 . 132 VAL C C 175.6 0.1 1 619 . 132 VAL CA C 61.2 0.2 1 620 . 132 VAL CB C 30.9 0.3 1 621 . 132 VAL CG1 C 19.9 0.4 2 622 . 132 VAL CG2 C 17.4 0.4 2 623 . 132 VAL N N 118.7 0.1 1 624 . 133 GLY H H 7.63 0.02 1 625 . 133 GLY C C 173.8 0.1 1 626 . 133 GLY CA C 44.0 0.2 1 627 . 133 GLY N N 110.0 0.1 1 628 . 134 ASP H H 8.71 0.02 1 629 . 134 ASP C C 175.9 0.1 1 630 . 134 ASP CA C 55.1 0.2 1 631 . 134 ASP CB C 39.4 0.3 1 632 . 134 ASP N N 120.0 0.1 1 633 . 135 GLY H H 8.26 0.02 1 634 . 135 GLY C C 173.4 0.1 1 635 . 135 GLY CA C 45.5 0.2 1 636 . 135 GLY N N 108.5 0.1 1 637 . 136 VAL H H 7.23 0.02 1 638 . 136 VAL C C 174.5 0.1 1 639 . 136 VAL CA C 61.7 0.2 1 640 . 136 VAL CB C 32.0 0.3 1 641 . 136 VAL CG1 C 21.1 0.4 1 642 . 136 VAL CG2 C 21.1 0.4 1 643 . 136 VAL N N 120.9 0.1 1 644 . 137 TYR H H 8.52 0.02 1 645 . 137 TYR C C 175.1 0.1 1 646 . 137 TYR CA C 56.9 0.2 1 647 . 137 TYR CB C 40.6 0.3 1 648 . 137 TYR N N 124.9 0.1 1 649 . 138 TRP H H 9.28 0.02 1 650 . 138 TRP C C 176.8 0.1 1 651 . 138 TRP CA C 52.9 0.2 1 652 . 138 TRP CB C 32.2 0.3 1 653 . 138 TRP N N 124.2 0.1 1 654 . 138 TRP NE1 N 127.4 0.1 1 655 . 138 TRP HE1 H 9.95 0.02 1 656 . 139 SER H H 8.66 0.02 1 657 . 139 SER C C 175.3 0.1 1 658 . 139 SER CA C 60.4 0.2 1 659 . 139 SER CB C 62.8 0.3 1 660 . 139 SER N N 115.5 0.1 1 661 . 140 GLY H H 8.04 0.02 1 662 . 140 GLY C C 172.3 0.1 1 663 . 140 GLY CA C 44.6 0.2 1 664 . 140 GLY N N 107.8 0.1 1 665 . 141 ARG H H 8.75 0.02 1 666 . 141 ARG C C 174.0 0.1 1 667 . 141 ARG CA C 54.9 0.2 1 668 . 141 ARG CB C 31.1 0.3 1 669 . 141 ARG N N 121.5 0.1 1 670 . 142 TRP H H 8.00 0.02 1 671 . 142 TRP C C 175.3 0.1 1 672 . 142 TRP CA C 54.5 0.2 1 673 . 142 TRP N N 123.3 0.1 1 674 . 143 ALA H H 9.28 0.02 1 675 . 143 ALA C C 175.0 0.1 1 676 . 143 ALA CA C 52.2 0.2 1 677 . 143 ALA CB C 23.5 0.3 1 678 . 143 ALA N N 121.6 0.1 1 679 . 144 MET H H 9.78 0.02 1 680 . 144 MET C C 173.9 0.1 1 681 . 144 MET CA C 54.5 0.2 1 682 . 144 MET N N 119.5 0.1 1 683 . 145 VAL H H 8.87 0.02 1 684 . 145 VAL C C 174.5 0.1 1 685 . 145 VAL CA C 61.4 0.2 1 686 . 145 VAL N N 123.3 0.1 1 687 . 146 VAL H H 9.29 0.02 1 688 . 146 VAL C C 174.7 0.1 1 689 . 146 VAL CA C 60.3 0.2 1 690 . 146 VAL CB C 33.4 0.3 1 691 . 146 VAL N N 127.5 0.1 1 692 . 147 GLU H H 9.33 0.02 1 693 . 147 GLU C C 177.0 0.1 1 694 . 147 GLU CA C 54.2 0.2 1 695 . 147 GLU CB C 32.6 0.3 1 696 . 147 GLU CG C 36.6 0.4 1 697 . 147 GLU N N 125.7 0.1 1 698 . 148 ASN H H 10.38 0.02 1 699 . 148 ASN C C 175.9 0.1 1 700 . 148 ASN CA C 54.1 0.2 1 701 . 148 ASN CB C 37.4 0.3 1 702 . 148 ASN CG C 178.2 0.1 1 703 . 148 ASN N N 126.9 0.1 1 704 . 148 ASN ND2 N 112.7 0.1 1 705 . 148 ASN HD21 H 7.58 0.02 1 706 . 148 ASN HD22 H 6.85 0.02 1 707 . 149 GLY H H 8.75 0.02 1 708 . 149 GLY C C 172.8 0.1 1 709 . 149 GLY CA C 45.5 0.2 1 710 . 149 GLY N N 101.6 0.1 1 711 . 150 ILE H H 7.93 0.02 1 712 . 150 ILE C C 175.1 0.1 1 713 . 150 ILE CA C 58.2 0.2 1 714 . 150 ILE CB C 38.3 0.3 1 715 . 150 ILE N N 122.9 0.1 1 716 . 151 VAL H H 8.49 0.02 1 717 . 151 VAL C C 176.3 0.1 1 718 . 151 VAL CA C 62.7 0.2 1 719 . 151 VAL CB C 30.6 0.3 1 720 . 151 VAL N N 126.8 0.1 1 721 . 152 THR H H 9.14 0.02 1 722 . 152 THR C C 175.4 0.1 1 723 . 152 THR CA C 61.8 0.2 1 724 . 152 THR CB C 68.5 0.3 1 725 . 152 THR N N 120.4 0.1 1 726 . 153 TYR H H 7.67 0.02 1 727 . 153 TYR C C 173.6 0.1 1 728 . 153 TYR CA C 57.8 0.2 1 729 . 153 TYR CB C 41.4 0.3 1 730 . 153 TYR N N 122.1 0.1 1 731 . 154 ALA H H 7.45 0.02 1 732 . 154 ALA C C 174.1 0.1 1 733 . 154 ALA CA C 51.9 0.2 1 734 . 154 ALA CB C 21.0 0.3 1 735 . 154 ALA N N 127.8 0.1 1 736 . 155 ALA H H 8.57 0.02 1 737 . 155 ALA C C 173.6 0.1 1 738 . 155 ALA CA C 51.8 0.2 1 739 . 155 ALA CB C 22.8 0.3 1 740 . 155 ALA N N 123.9 0.1 1 741 . 156 LYS H H 8.30 0.02 1 742 . 156 LYS C C 175.1 0.1 1 743 . 156 LYS CA C 53.0 0.2 1 744 . 156 LYS CB C 35.3 0.3 1 745 . 156 LYS N N 118.0 0.1 1 746 . 157 GLU H H 8.71 0.02 1 747 . 157 GLU C C 178.0 0.1 1 748 . 157 GLU CA C 54.6 0.2 1 749 . 157 GLU CB C 28.1 0.3 1 750 . 157 GLU N N 118.9 0.1 1 751 . 158 THR H H 8.70 0.02 1 752 . 158 THR C C 174.6 0.1 1 753 . 158 THR CA C 64.5 0.2 1 754 . 158 THR CB C 68.6 0.3 1 755 . 158 THR CG2 C 21.6 0.4 1 756 . 158 THR N N 118.9 0.1 1 757 . 159 ASN H H 8.29 0.02 1 758 . 159 ASN C C 172.8 0.1 1 759 . 159 ASN CA C 50.0 0.2 1 760 . 159 ASN CB C 37.9 0.3 1 761 . 159 ASN CG C 177.7 0.1 1 762 . 159 ASN N N 118.3 0.1 1 763 . 159 ASN ND2 N 113.8 0.1 1 764 . 159 ASN HD21 H 7.62 0.02 1 765 . 159 ASN HD22 H 6.81 0.02 1 766 . 160 PRO C C 177.1 0.1 1 767 . 160 PRO CA C 64.1 0.2 1 768 . 160 PRO CB C 32.7 0.3 1 769 . 161 GLY H H 8.92 0.02 1 770 . 161 GLY C C 174.9 0.1 1 771 . 161 GLY CA C 46.5 0.2 1 772 . 161 GLY N N 105.4 0.1 1 773 . 162 THR H H 7.08 0.02 1 774 . 162 THR C C 173.7 0.1 1 775 . 162 THR CA C 61.6 0.2 1 776 . 162 THR CB C 70.9 0.3 1 777 . 162 THR CG2 C 20.7 0.4 1 778 . 162 THR N N 106.5 0.1 1 779 . 163 ASP H H 7.84 0.02 1 780 . 163 ASP C C 173.7 0.1 1 781 . 163 ASP CA C 54.3 0.2 1 782 . 163 ASP CB C 41.9 0.3 1 783 . 163 ASP N N 123.0 0.1 1 784 . 164 VAL H H 8.06 0.02 1 785 . 164 VAL C C 175.7 0.1 1 786 . 164 VAL CA C 61.6 0.2 1 787 . 164 VAL N N 119.8 0.1 1 788 . 165 THR H H 10.87 0.02 1 789 . 165 THR C C 176.9 0.1 1 790 . 165 THR CA C 58.7 0.2 1 791 . 165 THR CB C 70.2 0.3 1 792 . 165 THR N N 120.3 0.1 1 793 . 166 VAL H H 9.80 0.02 1 794 . 166 VAL C C 176.0 0.1 1 795 . 166 VAL CA C 62.6 0.2 1 796 . 166 VAL CB C 29.9 0.3 1 797 . 166 VAL N N 123.2 0.1 1 798 . 167 SER C C 174.4 0.1 1 799 . 167 SER CA C 58.5 0.2 1 800 . 167 SER CB C 63.5 0.3 1 801 . 168 SER H H 7.74 0.02 1 802 . 168 SER CA C 57.2 0.2 1 803 . 168 SER CB C 65.6 0.3 1 804 . 168 SER N N 120.1 0.1 1 805 . 169 VAL C C 175.8 0.1 1 806 . 169 VAL CA C 56.0 0.2 1 807 . 169 VAL CB C 29.6 0.3 1 808 . 170 GLU H H 8.37 0.02 1 809 . 170 GLU C C 179.7 0.1 1 810 . 170 GLU CA C 60.7 0.2 1 811 . 170 GLU CB C 27.2 0.3 1 812 . 170 GLU CG C 37.2 0.4 1 813 . 170 GLU N N 120.7 0.1 1 814 . 171 SER H H 7.89 0.02 1 815 . 171 SER C C 176.5 0.1 1 816 . 171 SER CA C 61.5 0.2 1 817 . 171 SER CB C 62.7 0.3 1 818 . 171 SER N N 117.7 0.1 1 819 . 172 VAL H H 7.62 0.02 1 820 . 172 VAL C C 178.2 0.1 1 821 . 172 VAL CA C 66.8 0.2 1 822 . 172 VAL CB C 30.7 0.3 1 823 . 172 VAL N N 122.9 0.1 1 824 . 173 LEU H H 8.66 0.02 1 825 . 173 LEU C C 178.6 0.1 1 826 . 173 LEU CA C 57.9 0.2 1 827 . 173 LEU CB C 41.5 0.3 1 828 . 173 LEU N N 120.0 0.1 1 829 . 174 ALA H H 6.97 0.02 1 830 . 174 ALA C C 177.7 0.1 1 831 . 174 ALA CA C 53.0 0.2 1 832 . 174 ALA CB C 17.5 0.3 1 833 . 174 ALA N N 117.3 0.1 1 834 . 175 HIS H H 7.88 0.02 1 835 . 175 HIS C C 172.8 0.1 1 836 . 175 HIS CA C 56.0 0.2 1 837 . 175 HIS CB C 28.5 0.3 1 838 . 175 HIS N N 115.7 0.1 1 839 . 176 LEU H H 6.99 0.02 1 840 . 176 LEU C C 181.6 0.1 1 841 . 176 LEU CA C 55.5 0.2 1 842 . 176 LEU CB C 43.7 0.3 1 843 . 176 LEU N N 125.0 0.1 1 stop_ save_