data_4567 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C resonance assignments for the catalytic domain of the yeast E2, UBC1 ; _BMRB_accession_number 4567 _BMRB_flat_file_name bmr4567.str _Entry_type original _Submission_date 1999-12-22 _Accession_date 1999-12-22 _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 Hamilton Katherine S. . 2 Ellison Michael J. . 3 Shaw Gary S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 466 "13C chemical shifts" 463 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-03 original author . stop_ _Original_release_date 2000-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Hamilton, K.S., Ellison, M.J., and Shaw, G.S., "Letter to the Editor: 1H, 15N and 13C Resonance Assignments for the Catalytic Domain of the Yeast E2, UBC1," J. Biomol. NMR 16, 351-352 (2000). ; _Citation_title ; Letter to the Editor: 1H, 15N and 13C Resonance Assignments for the Catalytic Domain of the Yeast E2, UBC1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20285165 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hamilton Katherine S. . 2 Ellison Michael J. . 3 Shaw Gary S. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 16 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 351 _Page_last 352 _Year 2000 _Details . loop_ _Keyword 'yeast UBC1' 'conjugating enzyme' 'resonance assignments' 'ubiquitin system' stop_ save_ ################################## # Molecular system description # ################################## save_yUBC1 _Saveframe_category molecular_system _Mol_system_name 'catalytic domain of yUBC1' _Abbreviation_common yUBC1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label yUBC1D450(K93R) $yUBC1D450(K93R) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'conjugatin enzyme in ubiquitin system' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_yUBC1D450(K93R) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'yeast UBC1 (catalytic domain)' _Name_variant yUBC1D450(K93R) _Abbreviation_common yUBC1D450(K93R) _Molecular_mass 16821 _Mol_thiol_state 'all free' _Details ; Yeast UBC1 enzyme lacking the C-terminal 'tail', with a mutation at position 93(K to R) and a 1 residue insertion at position 3(a Ser), due to cloning procedures. Will support thiol ester chain formation in invitro reaction with E1 and ubiquitin. ; ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; MSSRAKRIMKEIQAVKDDPA AHITLEFVSESDIHHLKGTF LGPPGTPYEGGKFVVDIEVP MEYPFKPPKMQFDTKVYHPN ISSVTGAICLDILRNAWSPV ITLKSALISLQALLQSPEPN DPQDAEVAQHYLRDRESFNK TAALWTRLYAS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 SER 4 ARG 5 ALA 6 LYS 7 ARG 8 ILE 9 MET 10 LYS 11 GLU 12 ILE 13 GLN 14 ALA 15 VAL 16 LYS 17 ASP 18 ASP 19 PRO 20 ALA 21 ALA 22 HIS 23 ILE 24 THR 25 LEU 26 GLU 27 PHE 28 VAL 29 SER 30 GLU 31 SER 32 ASP 33 ILE 34 HIS 35 HIS 36 LEU 37 LYS 38 GLY 39 THR 40 PHE 41 LEU 42 GLY 43 PRO 44 PRO 45 GLY 46 THR 47 PRO 48 TYR 49 GLU 50 GLY 51 GLY 52 LYS 53 PHE 54 VAL 55 VAL 56 ASP 57 ILE 58 GLU 59 VAL 60 PRO 61 MET 62 GLU 63 TYR 64 PRO 65 PHE 66 LYS 67 PRO 68 PRO 69 LYS 70 MET 71 GLN 72 PHE 73 ASP 74 THR 75 LYS 76 VAL 77 TYR 78 HIS 79 PRO 80 ASN 81 ILE 82 SER 83 SER 84 VAL 85 THR 86 GLY 87 ALA 88 ILE 89 CYS 90 LEU 91 ASP 92 ILE 93 LEU 94 ARG 95 ASN 96 ALA 97 TRP 98 SER 99 PRO 100 VAL 101 ILE 102 THR 103 LEU 104 LYS 105 SER 106 ALA 107 LEU 108 ILE 109 SER 110 LEU 111 GLN 112 ALA 113 LEU 114 LEU 115 GLN 116 SER 117 PRO 118 GLU 119 PRO 120 ASN 121 ASP 122 PRO 123 GLN 124 ASP 125 ALA 126 GLU 127 VAL 128 ALA 129 GLN 130 HIS 131 TYR 132 LEU 133 ARG 134 ASP 135 ARG 136 GLU 137 SER 138 PHE 139 ASN 140 LYS 141 THR 142 ALA 143 ALA 144 LEU 145 TRP 146 THR 147 ARG 148 LEU 149 TYR 150 ALA 151 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 1FXT "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" 98.68 149 99.33 100.00 2.96e-105 PDB 1FZY "Crystal Structure Of Saccharomyces Cerevisiae Ubiquitin Conjugating Enzyme 1" 98.68 149 99.33 100.00 2.96e-105 PDB 1TTE "The Structure Of A Class Ii Ubiquitin-Conjugating Enzyme, Ubc1" 99.34 215 100.00 100.00 2.83e-106 DBJ GAA22407 "K7_Ubc1p [Saccharomyces cerevisiae Kyokai no. 7]" 98.68 215 99.33 100.00 3.77e-105 EMBL CAA39812 "UBC1 ubiquitin-conjugating enzyme [Saccharomyces cerevisiae]" 98.68 215 99.33 100.00 3.77e-105 EMBL CAA86682 "Ubc1p [Saccharomyces cerevisiae]" 98.68 215 99.33 100.00 3.77e-105 EMBL CAY78679 "Ubc1p [Saccharomyces cerevisiae EC1118]" 98.68 215 99.33 100.00 3.77e-105 GB AAS56001 "YDR177W [Saccharomyces cerevisiae]" 98.68 215 99.33 100.00 3.77e-105 GB AHY75163 "Ubc1p [Saccharomyces cerevisiae YJM993]" 98.68 215 98.66 100.00 1.20e-104 GB AJP37891 "Ubc1p [Saccharomyces cerevisiae YJM1078]" 98.68 215 98.66 99.33 3.42e-104 GB AJU58013 "Ubc1p [Saccharomyces cerevisiae YJM189]" 98.68 215 99.33 100.00 3.77e-105 GB AJU58708 "Ubc1p [Saccharomyces cerevisiae YJM193]" 98.68 215 99.33 100.00 3.77e-105 REF NP_010462 "E2 ubiquitin-conjugating protein UBC1 [Saccharomyces cerevisiae S288c]" 98.68 215 99.33 100.00 3.77e-105 SP P21734 "RecName: Full=Ubiquitin-conjugating enzyme E2 1; AltName: Full=E2 ubiquitin-conjugating enzyme 1; AltName: Full=Ubiquitin carri" 98.68 215 99.33 100.00 3.77e-105 TPG DAA12019 "TPA: E2 ubiquitin-conjugating protein UBC1 [Saccharomyces cerevisiae S288c]" 98.68 215 99.33 100.00 3.77e-105 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $yUBC1D450(K93R) 'baker's yeast' 4932 Eukaryota . Saccharomyces cerevisiae ubc1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $yUBC1D450(K93R) 'recombinant technology' E.coli . . BL21DE3pLysS plasmid pET3A 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 $yUBC1D450(K93R) 0.7 mM '[U-95% 13C; U-95% 15N]' HEPES 40 mM . NaCl 400 mM . DTT 1.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $yUBC1D450(K93R) . mM 0.8 0.9 '[U-95% 15N]' HEPES 40 mM . . . NaCl 400 mM . . . DTT 1.0 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_15N-edited_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_15N-edited_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCACOCANH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCACOCANH _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 '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _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 CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCACOCANH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.03 na 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name yUBC1D450(K93R) _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 . 2 SER C C 173.64 0.10 1 2 . 3 SER H H 8.43 0.02 1 3 . 3 SER HA H 4.64 0.03 1 4 . 3 SER C C 174.79 0.10 1 5 . 3 SER CA C 54.75 0.20 1 6 . 3 SER N N 119.41 0.20 1 7 . 4 ARG H H 9.75 0.02 1 8 . 4 ARG CA C 59.67 0.20 1 9 . 4 ARG CB C 30.37 0.20 1 10 . 4 ARG N N 124.97 0.20 1 11 . 5 ALA H H 8.18 0.02 1 12 . 5 ALA HA H 4.05 0.03 1 13 . 5 ALA HB H 1.52 0.03 1 14 . 5 ALA C C 179.56 0.10 1 15 . 5 ALA CA C 55.63 0.20 1 16 . 5 ALA CB C 18.58 0.20 1 17 . 5 ALA N N 121.36 0.20 1 18 . 6 LYS H H 7.99 0.02 1 19 . 6 LYS HA H 4.05 0.03 1 20 . 6 LYS HB3 H 1.97 0.03 2 21 . 6 LYS C C 179.39 0.10 1 22 . 6 LYS CA C 59.43 0.20 1 23 . 6 LYS CB C 32.28 0.20 1 24 . 6 LYS N N 117.09 0.20 1 25 . 7 ARG H H 7.97 0.02 1 26 . 7 ARG HA H 4.27 0.03 1 27 . 7 ARG C C 178.32 0.10 1 28 . 7 ARG CA C 58.80 0.20 1 29 . 7 ARG CB C 28.77 0.20 1 30 . 7 ARG N N 120.10 0.20 1 31 . 8 ILE H H 8.45 0.02 1 32 . 8 ILE HA H 3.73 0.03 1 33 . 8 ILE HB H 2.05 0.03 1 34 . 8 ILE HG2 H 1.10 0.03 1 35 . 8 ILE CA C 64.91 0.20 1 36 . 8 ILE CB C 37.27 0.20 1 37 . 8 ILE CG2 C 17.65 0.20 1 38 . 8 ILE N N 119.55 0.20 1 39 . 9 MET C C 179.83 0.10 1 40 . 10 LYS H H 8.00 0.02 1 41 . 10 LYS HA H 4.17 0.03 1 42 . 10 LYS C C 179.68 0.10 1 43 . 10 LYS CA C 59.53 0.20 1 44 . 10 LYS CB C 32.34 0.20 1 45 . 10 LYS N N 121.00 0.20 1 46 . 11 GLU H H 8.42 0.02 1 47 . 11 GLU HA H 4.16 0.03 1 48 . 11 GLU HB3 H 1.77 0.03 2 49 . 11 GLU C C 179.58 0.10 1 50 . 11 GLU CA C 60.10 0.20 1 51 . 11 GLU CB C 29.55 0.20 1 52 . 11 GLU N N 121.47 0.20 1 53 . 12 ILE H H 8.23 0.02 1 54 . 12 ILE HA H 3.67 0.03 1 55 . 12 ILE HB H 2.00 0.03 1 56 . 12 ILE HD1 H 0.41 0.03 1 57 . 12 ILE HG2 H 0.91 0.03 1 58 . 12 ILE C C 178.89 0.10 1 59 . 12 ILE CA C 64.53 0.20 1 60 . 12 ILE CB C 37.72 0.20 1 61 . 12 ILE CD1 C 13.14 0.20 1 62 . 12 ILE CG2 C 17.20 0.20 1 63 . 12 ILE N N 119.10 0.20 1 64 . 13 GLN H H 8.03 0.02 1 65 . 13 GLN HA H 3.87 0.03 1 66 . 13 GLN HB2 H 2.27 0.03 2 67 . 13 GLN HB3 H 2.21 0.03 2 68 . 13 GLN HG2 H 2.48 0.03 2 69 . 13 GLN HG3 H 2.56 0.03 2 70 . 13 GLN HE21 H 6.91 0.03 2 71 . 13 GLN HE22 H 7.92 0.03 2 72 . 13 GLN C C 176.27 0.10 1 73 . 13 GLN CA C 58.67 0.20 1 74 . 13 GLN CB C 28.01 0.20 1 75 . 13 GLN CG C 33.38 0.20 1 76 . 13 GLN CD C 180.38 0.20 1 77 . 13 GLN N N 120.96 0.20 1 78 . 13 GLN NE2 N 114.84 0.20 1 79 . 14 ALA H H 8.07 0.02 1 80 . 14 ALA HA H 4.25 0.03 1 81 . 14 ALA HB H 1.60 0.03 1 82 . 14 ALA C C 181.14 0.10 1 83 . 14 ALA CA C 54.79 0.20 1 84 . 14 ALA CB C 18.54 0.20 1 85 . 14 ALA N N 119.65 0.20 1 86 . 15 VAL H H 7.45 0.02 1 87 . 15 VAL HA H 3.77 0.03 1 88 . 15 VAL HB H 2.35 0.03 2 89 . 15 VAL HG1 H 1.07 0.03 2 90 . 15 VAL HG2 H 0.92 0.03 2 91 . 15 VAL C C 178.35 0.10 1 92 . 15 VAL CA C 66.04 0.20 1 93 . 15 VAL CB C 31.35 0.20 1 94 . 15 VAL CG1 C 22.92 0.20 1 95 . 15 VAL CG2 C 22.48 0.20 1 96 . 15 VAL N N 116.43 0.20 1 97 . 16 LYS H H 7.80 0.02 1 98 . 16 LYS HA H 4.05 0.03 1 99 . 16 LYS HB3 H 1.97 0.03 2 100 . 16 LYS C C 178.32 0.10 1 101 . 16 LYS CA C 58.91 0.20 1 102 . 16 LYS CB C 32.31 0.20 1 103 . 16 LYS N N 121.31 0.20 1 104 . 17 ASP H H 8.01 0.02 1 105 . 17 ASP HA H 4.62 0.03 1 106 . 17 ASP HB2 H 2.69 0.03 2 107 . 17 ASP HB3 H 2.86 0.03 2 108 . 17 ASP C C 174.98 0.10 1 109 . 17 ASP CA C 54.95 0.20 1 110 . 17 ASP CB C 40.96 0.20 1 111 . 17 ASP N N 116.14 0.20 1 112 . 18 ASP H H 7.26 0.02 1 113 . 18 ASP HA H 5.21 0.03 1 114 . 18 ASP HB2 H 2.93 0.03 2 115 . 18 ASP HB3 H 2.50 0.03 2 116 . 18 ASP C C 175.15 0.10 1 117 . 18 ASP CA C 50.80 0.20 1 118 . 18 ASP CB C 41.21 0.20 1 119 . 18 ASP N N 118.37 0.20 1 120 . 19 PRO C C 178.44 0.10 1 121 . 19 PRO CA C 64.42 0.20 1 122 . 19 PRO CB C 31.69 0.20 1 123 . 20 ALA H H 8.11 0.02 1 124 . 20 ALA HA H 4.07 0.03 1 125 . 20 ALA HB H 1.41 0.03 1 126 . 20 ALA C C 177.81 0.10 1 127 . 20 ALA CA C 53.44 0.20 1 128 . 20 ALA CB C 18.40 0.20 1 129 . 20 ALA N N 120.58 0.20 1 130 . 21 ALA H H 7.32 0.02 1 131 . 21 ALA HA H 4.21 0.03 1 132 . 21 ALA HB H 1.49 0.03 1 133 . 21 ALA C C 177.52 0.10 1 134 . 21 ALA CA C 52.96 0.20 1 135 . 21 ALA CB C 18.24 0.20 1 136 . 21 ALA N N 118.95 0.20 1 137 . 22 HIS HA H 4.28 0.03 1 138 . 22 HIS HB3 H 3.35 0.03 2 139 . 22 HIS C C 176.26 0.10 1 140 . 22 HIS CA C 57.19 0.20 1 141 . 22 HIS CB C 27.86 0.20 1 142 . 23 ILE H H 8.01 0.02 1 143 . 23 ILE HA H 5.15 0.03 1 144 . 23 ILE HB H 1.70 0.03 1 145 . 23 ILE HG13 H 1.26 0.03 2 146 . 23 ILE HD1 H 0.87 0.03 1 147 . 23 ILE HG2 H 0.98 0.03 1 148 . 23 ILE C C 175.98 0.10 1 149 . 23 ILE CA C 58.89 0.20 1 150 . 23 ILE CB C 40.79 0.20 1 151 . 23 ILE CG1 C 27.33 0.20 1 152 . 23 ILE CD1 C 13.71 0.20 1 153 . 23 ILE CG2 C 18.69 0.20 1 154 . 23 ILE N N 119.38 0.20 1 155 . 24 THR H H 8.34 0.02 1 156 . 24 THR HA H 4.73 0.03 1 157 . 24 THR HB H 4.21 0.03 1 158 . 24 THR HG2 H 1.07 0.03 1 159 . 24 THR C C 172.78 0.10 1 160 . 24 THR CA C 60.01 0.20 1 161 . 24 THR CB C 71.51 0.20 1 162 . 24 THR N N 115.68 0.20 1 163 . 25 LEU H H 8.24 0.02 1 164 . 25 LEU HA H 5.06 0.03 1 165 . 25 LEU HB3 H 1.35 0.03 2 166 . 25 LEU HD1 H 0.73 0.03 1 167 . 25 LEU C C 174.10 0.10 1 168 . 25 LEU CA C 54.38 0.20 1 169 . 25 LEU CB C 46.52 0.20 1 170 . 25 LEU CD1 C 25.76 0.20 2 171 . 25 LEU N N 122.37 0.20 1 172 . 26 GLU H H 8.33 0.02 1 173 . 26 GLU HA H 4.61 0.03 1 174 . 26 GLU HB3 H 1.75 0.03 2 175 . 26 GLU C C 175.32 0.10 1 176 . 26 GLU CA C 53.87 0.20 1 177 . 26 GLU CB C 34.28 0.20 1 178 . 26 GLU N N 120.80 0.20 1 179 . 27 PHE H H 8.50 0.02 1 180 . 27 PHE HA H 4.39 0.03 1 181 . 27 PHE HB2 H 2.82 0.03 2 182 . 27 PHE HB3 H 2.75 0.03 2 183 . 27 PHE C C 177.05 0.10 1 184 . 27 PHE CA C 58.19 0.20 1 185 . 27 PHE CB C 39.26 0.20 1 186 . 27 PHE N N 120.36 0.20 1 187 . 28 VAL H H 8.15 0.02 1 188 . 28 VAL HA H 3.76 0.03 1 189 . 28 VAL HB H 1.73 0.03 1 190 . 28 VAL HG1 H 0.41 0.03 2 191 . 28 VAL HG2 H 0.81 0.03 2 192 . 28 VAL C C 176.21 0.10 1 193 . 28 VAL CA C 65.09 0.20 1 194 . 28 VAL CB C 31.63 0.20 1 195 . 28 VAL CG1 C 21.78 0.20 1 196 . 28 VAL CG2 C 20.99 0.20 1 197 . 28 VAL N N 123.05 0.20 1 198 . 29 SER H H 8.97 0.02 1 199 . 29 SER HA H 4.73 0.03 1 200 . 29 SER HB2 H 3.80 0.03 2 201 . 29 SER HB3 H 3.97 0.03 2 202 . 29 SER CA C 56.51 0.20 1 203 . 29 SER CB C 65.00 0.20 1 204 . 29 SER N N 114.43 0.20 1 205 . 30 GLU H H 8.30 0.02 1 206 . 30 GLU HA H 4.41 0.03 1 207 . 30 GLU C C 176.21 0.10 1 208 . 30 GLU CA C 58.41 0.20 1 209 . 30 GLU CB C 29.51 0.20 1 210 . 30 GLU N N 116.66 0.20 1 211 . 31 SER H H 7.94 0.02 1 212 . 31 SER HA H 4.30 0.03 1 213 . 31 SER HB2 H 3.85 0.03 2 214 . 31 SER HB3 H 3.92 0.03 2 215 . 31 SER C C 173.56 0.10 1 216 . 31 SER CA C 58.83 0.20 1 217 . 31 SER CB C 63.52 0.20 1 218 . 31 SER N N 112.03 0.20 1 219 . 32 ASP H H 7.50 0.02 1 220 . 32 ASP HA H 4.98 0.03 1 221 . 32 ASP HB2 H 2.91 0.03 2 222 . 32 ASP HB3 H 2.59 0.03 2 223 . 32 ASP C C 175.90 0.10 1 224 . 32 ASP CA C 53.14 0.20 1 225 . 32 ASP CB C 42.39 0.20 1 226 . 32 ASP N N 121.51 0.20 1 227 . 33 ILE H H 8.02 0.02 1 228 . 33 ILE HA H 4.15 0.03 1 229 . 33 ILE HB H 1.98 0.03 1 230 . 33 ILE HG12 H 1.06 0.03 2 231 . 33 ILE HG13 H 1.12 0.03 2 232 . 33 ILE HD1 H 0.77 0.03 1 233 . 33 ILE HG2 H 0.57 0.03 1 234 . 33 ILE CA C 61.43 0.20 1 235 . 33 ILE CB C 38.34 0.20 1 236 . 33 ILE CG1 C 26.28 0.20 1 237 . 33 ILE CD1 C 14.63 0.20 1 238 . 33 ILE CG2 C 17.32 0.20 1 239 . 33 ILE N N 118.13 0.20 1 240 . 34 HIS H H 7.99 0.02 1 241 . 34 HIS HA H 4.49 0.03 1 242 . 34 HIS HB3 H 3.30 0.03 2 243 . 34 HIS CA C 56.60 0.20 1 244 . 34 HIS CB C 30.51 0.20 1 245 . 34 HIS N N 112.83 0.20 1 246 . 35 HIS H H 7.23 0.02 1 247 . 35 HIS HA H 5.72 0.03 1 248 . 35 HIS HB2 H 2.77 0.03 2 249 . 35 HIS HB3 H 3.30 0.03 2 250 . 35 HIS C C 173.93 0.10 1 251 . 35 HIS CA C 53.81 0.20 1 252 . 35 HIS CB C 30.80 0.20 1 253 . 35 HIS N N 118.61 0.20 1 254 . 36 LEU H H 9.70 0.02 1 255 . 36 LEU HA H 5.31 0.03 1 256 . 36 LEU HB3 H 1.22 0.03 2 257 . 36 LEU C C 174.85 0.10 1 258 . 36 LEU CA C 54.28 0.20 1 259 . 36 LEU CB C 46.77 0.20 1 260 . 36 LEU N N 128.26 0.20 1 261 . 37 LYS H H 8.63 0.02 1 262 . 37 LYS HA H 5.24 0.03 1 263 . 37 LYS HB3 H 1.61 0.03 2 264 . 37 LYS C C 177.37 0.10 1 265 . 37 LYS CA C 53.73 0.20 1 266 . 37 LYS CB C 34.92 0.20 1 267 . 37 LYS N N 115.69 0.20 1 268 . 38 GLY H H 9.65 0.02 1 269 . 38 GLY HA2 H 5.58 0.03 2 270 . 38 GLY HA3 H 3.28 0.03 2 271 . 38 GLY C C 171.73 0.10 1 272 . 38 GLY CA C 44.02 0.20 1 273 . 38 GLY N N 113.72 0.20 1 274 . 39 THR H H 8.70 0.02 1 275 . 39 THR HA H 5.93 0.03 1 276 . 39 THR HB H 3.94 0.03 1 277 . 39 THR HG2 H 1.07 0.03 1 278 . 39 THR C C 173.03 0.10 1 279 . 39 THR CA C 60.09 0.20 1 280 . 39 THR CB C 72.02 0.20 1 281 . 39 THR N N 114.75 0.20 1 282 . 40 PHE H H 8.40 0.02 1 283 . 40 PHE HA H 5.33 0.03 1 284 . 40 PHE HB2 H 3.05 0.03 2 285 . 40 PHE HB3 H 3.37 0.03 2 286 . 40 PHE C C 172.65 0.10 1 287 . 40 PHE CA C 55.66 0.20 1 288 . 40 PHE CB C 41.58 0.20 1 289 . 40 PHE N N 116.24 0.20 1 290 . 41 LEU H H 9.17 0.02 1 291 . 41 LEU HA H 5.49 0.03 1 292 . 41 LEU HB3 H 1.96 0.03 2 293 . 41 LEU HD1 H 0.87 0.03 2 294 . 41 LEU C C 179.22 0.10 1 295 . 41 LEU CA C 52.97 0.20 1 296 . 41 LEU CB C 42.44 0.20 1 297 . 41 LEU CD1 C 25.09 0.20 1 298 . 41 LEU N N 119.64 0.20 1 299 . 42 GLY H H 9.30 0.02 1 300 . 42 GLY CA C 44.33 0.20 1 301 . 42 GLY N N 108.26 0.20 1 302 . 44 PRO C C 177.57 0.10 1 303 . 44 PRO CA C 62.80 0.20 1 304 . 44 PRO CB C 32.16 0.20 1 305 . 45 GLY H H 9.36 0.02 1 306 . 45 GLY HA2 H 4.73 0.03 2 307 . 45 GLY HA3 H 4.18 0.03 2 308 . 45 GLY C C 173.97 0.10 1 309 . 45 GLY CA C 45.95 0.20 1 310 . 45 GLY N N 109.73 0.20 1 311 . 46 THR H H 7.36 0.02 1 312 . 46 THR HA H 5.16 0.03 1 313 . 46 THR HB H 3.11 0.03 1 314 . 46 THR HG2 H 1.38 0.03 1 315 . 46 THR C C 174.59 0.10 1 316 . 46 THR CA C 59.17 0.20 1 317 . 46 THR CB C 70.60 0.20 1 318 . 46 THR CG2 C 21.71 0.20 1 319 . 46 THR N N 107.90 0.20 1 320 . 47 PRO C C 175.11 0.10 1 321 . 47 PRO CA C 63.92 0.20 1 322 . 47 PRO CB C 32.64 0.20 1 323 . 48 TYR H H 7.20 0.02 1 324 . 48 TYR HA H 5.28 0.03 1 325 . 48 TYR HB2 H 2.40 0.03 2 326 . 48 TYR HB3 H 2.47 0.03 2 327 . 48 TYR C C 175.60 0.10 1 328 . 48 TYR CA C 56.15 0.20 1 329 . 48 TYR CB C 38.48 0.20 1 330 . 48 TYR N N 116.75 0.20 1 331 . 49 GLU H H 7.54 0.02 1 332 . 49 GLU HA H 3.67 0.03 1 333 . 49 GLU C C 177.01 0.10 1 334 . 49 GLU CA C 58.00 0.20 1 335 . 49 GLU CB C 30.02 0.20 1 336 . 49 GLU N N 122.78 0.20 1 337 . 50 GLY H H 9.36 0.02 1 338 . 50 GLY HA2 H 4.35 0.03 2 339 . 50 GLY HA3 H 3.72 0.03 2 340 . 50 GLY C C 174.77 0.10 1 341 . 50 GLY CA C 45.01 0.20 1 342 . 50 GLY N N 115.75 0.20 1 343 . 51 GLY H H 8.30 0.02 1 344 . 51 GLY HA2 H 3.31 0.03 2 345 . 51 GLY HA3 H 4.21 0.03 2 346 . 51 GLY C C 171.71 0.10 1 347 . 51 GLY CA C 45.16 0.20 1 348 . 51 GLY N N 107.32 0.20 1 349 . 52 LYS H H 8.70 0.02 1 350 . 52 LYS HA H 4.62 0.03 1 351 . 52 LYS HB3 H 1.47 0.03 2 352 . 52 LYS C C 173.60 0.10 1 353 . 52 LYS CA C 55.51 0.20 1 354 . 52 LYS CB C 33.45 0.20 1 355 . 52 LYS N N 125.46 0.20 1 356 . 53 PHE H H 8.69 0.02 1 357 . 53 PHE HA H 4.42 0.03 1 358 . 53 PHE HB2 H 2.40 0.03 2 359 . 53 PHE HB3 H 2.35 0.03 2 360 . 53 PHE C C 173.54 0.10 1 361 . 53 PHE CA C 57.47 0.20 1 362 . 53 PHE CB C 41.16 0.20 1 363 . 53 PHE N N 125.06 0.20 1 364 . 54 VAL H H 8.86 0.02 1 365 . 54 VAL HA H 4.65 0.03 1 366 . 54 VAL HB H 1.97 0.03 1 367 . 54 VAL C C 175.58 0.10 1 368 . 54 VAL CA C 60.87 0.20 1 369 . 54 VAL N N 120.87 0.20 1 370 . 55 VAL H H 9.65 0.02 1 371 . 55 VAL HA H 4.20 0.03 1 372 . 55 VAL HB H 1.57 0.03 1 373 . 55 VAL HG1 H 0.43 0.03 2 374 . 55 VAL HG2 H 0.26 0.03 2 375 . 55 VAL C C 173.96 0.10 1 376 . 55 VAL CA C 60.64 0.20 1 377 . 55 VAL CB C 34.94 0.20 1 378 . 55 VAL CG1 C 21.12 0.20 1 379 . 55 VAL CG2 C 20.95 0.20 1 380 . 55 VAL N N 128.01 0.20 1 381 . 56 ASP H H 9.28 0.02 1 382 . 56 ASP HA H 4.80 0.03 1 383 . 56 ASP HB3 H 2.71 0.03 2 384 . 56 ASP C C 175.37 0.10 1 385 . 56 ASP CA C 55.44 0.20 1 386 . 56 ASP CB C 44.08 0.20 1 387 . 56 ASP N N 128.35 0.20 1 388 . 57 ILE H H 8.82 0.02 1 389 . 57 ILE HA H 4.93 0.03 1 390 . 57 ILE HB H 1.59 0.03 1 391 . 57 ILE HG2 H 0.62 0.03 1 392 . 57 ILE C C 174.29 0.10 1 393 . 57 ILE CA C 60.41 0.20 1 394 . 57 ILE CB C 41.09 0.20 1 395 . 57 ILE CG2 C 17.66 0.20 1 396 . 57 ILE N N 124.66 0.20 1 397 . 58 GLU H H 9.02 0.02 1 398 . 58 GLU HA H 5.22 0.03 1 399 . 58 GLU HB3 H 1.86 0.03 2 400 . 58 GLU HG2 H 2.05 0.03 2 401 . 58 GLU HG3 H 1.77 0.03 2 402 . 58 GLU C C 175.82 0.10 1 403 . 58 GLU CA C 54.32 0.20 1 404 . 58 GLU CB C 32.28 0.20 1 405 . 58 GLU CG C 36.35 0.20 1 406 . 58 GLU N N 128.21 0.20 1 407 . 59 VAL H H 9.24 0.02 1 408 . 59 VAL HA H 4.10 0.03 1 409 . 59 VAL HB H 1.97 0.03 1 410 . 59 VAL HG1 H 0.65 0.03 2 411 . 59 VAL HG2 H 0.48 0.03 2 412 . 59 VAL C C 173.93 0.10 1 413 . 59 VAL CA C 59.48 0.20 1 414 . 59 VAL CB C 32.49 0.20 1 415 . 59 VAL CG1 C 21.38 0.20 1 416 . 59 VAL CG2 C 21.74 0.20 1 417 . 59 VAL N N 127.40 0.20 1 418 . 61 MET HA H 4.15 0.03 1 419 . 61 MET HB2 H 2.70 0.03 2 420 . 61 MET HB3 H 2.59 0.03 2 421 . 61 MET HG3 H 2.11 0.03 1 422 . 61 MET C C 177.90 0.10 1 423 . 61 MET CA C 58.05 0.20 1 424 . 61 MET CB C 31.92 0.20 1 425 . 61 MET CG C 31.50 0.20 1 426 . 62 GLU H H 8.74 0.02 1 427 . 62 GLU HA H 4.41 0.03 1 428 . 62 GLU HB2 H 2.48 0.03 2 429 . 62 GLU HB3 H 2.31 0.03 2 430 . 62 GLU HG2 H 2.49 0.03 2 431 . 62 GLU HG3 H 2.27 0.03 2 432 . 62 GLU C C 176.51 0.10 1 433 . 62 GLU CA C 57.08 0.20 1 434 . 62 GLU CB C 29.38 0.20 1 435 . 62 GLU CG C 37.04 0.20 1 436 . 62 GLU N N 113.73 0.20 1 437 . 63 TYR H H 7.67 0.02 1 438 . 63 TYR HA H 4.54 0.03 1 439 . 63 TYR C C 174.59 0.10 1 440 . 63 TYR CA C 57.99 0.20 1 441 . 63 TYR CB C 41.02 0.20 1 442 . 63 TYR N N 123.10 0.20 1 443 . 64 PRO C C 174.50 0.10 1 444 . 64 PRO CA C 63.62 0.20 1 445 . 64 PRO CB C 33.24 0.20 1 446 . 65 PHE H H 9.07 0.02 1 447 . 65 PHE HA H 4.41 0.03 1 448 . 65 PHE HB2 H 3.43 0.03 2 449 . 65 PHE HB3 H 3.13 0.03 2 450 . 65 PHE C C 175.37 0.10 1 451 . 65 PHE CA C 60.24 0.20 1 452 . 65 PHE CB C 38.30 0.20 1 453 . 65 PHE N N 125.05 0.20 1 454 . 66 LYS H H 7.00 0.02 1 455 . 66 LYS HA H 4.46 0.03 1 456 . 66 LYS HB3 H 1.67 0.03 2 457 . 66 LYS HG3 H 1.48 0.03 2 458 . 66 LYS HD3 H 1.78 0.03 2 459 . 66 LYS HE3 H 3.02 0.03 2 460 . 66 LYS C C 171.44 0.10 1 461 . 66 LYS CA C 52.33 0.20 1 462 . 66 LYS CB C 35.49 0.20 1 463 . 66 LYS CG C 25.13 0.20 1 464 . 66 LYS CD C 28.91 0.20 1 465 . 66 LYS N N 118.69 0.20 1 466 . 68 PRO C C 176.28 0.10 1 467 . 69 LYS H H 8.82 0.02 1 468 . 69 LYS HA H 5.59 0.03 1 469 . 69 LYS HB3 H 2.22 0.03 2 470 . 69 LYS CA C 54.92 0.20 1 471 . 69 LYS CB C 36.50 0.20 1 472 . 69 LYS N N 124.78 0.20 1 473 . 70 MET C C 175.10 0.10 1 474 . 71 GLN H H 9.01 0.02 1 475 . 71 GLN HA H 4.97 0.03 1 476 . 71 GLN C C 173.44 0.10 1 477 . 71 GLN N N 120.58 0.20 1 478 . 72 PHE C C 176.88 0.10 1 479 . 72 PHE CA C 61.61 0.20 1 480 . 72 PHE CB C 38.25 0.20 1 481 . 73 ASP H H 9.27 0.02 1 482 . 73 ASP HA H 4.71 0.03 1 483 . 73 ASP HB2 H 2.60 0.03 2 484 . 73 ASP HB3 H 2.44 0.03 2 485 . 73 ASP C C 177.61 0.10 1 486 . 73 ASP CA C 55.38 0.20 1 487 . 73 ASP CB C 40.89 0.20 1 488 . 73 ASP N N 125.60 0.20 1 489 . 74 THR H H 7.48 0.02 1 490 . 74 THR HA H 4.21 0.03 1 491 . 74 THR HB H 3.98 0.03 1 492 . 74 THR HG2 H 1.55 0.03 1 493 . 74 THR C C 173.43 0.10 1 494 . 74 THR CA C 63.24 0.20 1 495 . 74 THR CB C 71.11 0.20 1 496 . 74 THR CG2 C 22.49 0.20 1 497 . 74 THR N N 117.56 0.20 1 498 . 75 LYS H H 8.13 0.02 1 499 . 75 LYS HA H 4.31 0.03 1 500 . 75 LYS HB3 H 1.24 0.03 2 501 . 75 LYS HG3 H 0.95 0.03 2 502 . 75 LYS HD3 H 1.11 0.03 2 503 . 75 LYS C C 175.17 0.10 1 504 . 75 LYS CA C 57.02 0.20 1 505 . 75 LYS CB C 32.41 0.20 1 506 . 75 LYS CG C 20.64 0.20 1 507 . 75 LYS CD C 32.96 0.20 1 508 . 75 LYS N N 128.30 0.20 1 509 . 76 VAL H H 8.67 0.02 1 510 . 76 VAL HA H 4.53 0.03 1 511 . 76 VAL HB H 1.59 0.03 1 512 . 76 VAL HG1 H 0.62 0.03 2 513 . 76 VAL HG2 H 0.51 0.03 2 514 . 76 VAL C C 172.42 0.10 1 515 . 76 VAL CA C 61.23 0.20 1 516 . 76 VAL CB C 35.34 0.20 1 517 . 76 VAL CG1 C 22.10 0.20 1 518 . 76 VAL CG2 C 22.00 0.20 1 519 . 76 VAL N N 124.08 0.20 1 520 . 77 TYR H H 8.70 0.02 1 521 . 77 TYR HA H 4.22 0.03 1 522 . 77 TYR HB2 H 2.70 0.03 2 523 . 77 TYR HB3 H 2.69 0.03 2 524 . 77 TYR CA C 57.59 0.20 1 525 . 77 TYR CB C 37.93 0.20 1 526 . 77 TYR N N 130.60 0.20 1 527 . 79 PRO C C 176.49 0.10 1 528 . 79 PRO CA C 65.30 0.20 1 529 . 79 PRO CB C 32.36 0.20 1 530 . 80 ASN H H 11.49 0.02 1 531 . 80 ASN HA H 4.69 0.03 1 532 . 80 ASN C C 171.44 0.10 1 533 . 80 ASN CA C 55.41 0.20 1 534 . 80 ASN CB C 41.15 0.20 1 535 . 80 ASN N N 117.72 0.20 1 536 . 81 ILE H H 7.65 0.02 1 537 . 81 ILE HA H 4.91 0.03 1 538 . 81 ILE C C 174.87 0.10 1 539 . 81 ILE CA C 59.29 0.20 1 540 . 81 ILE CB C 42.90 0.20 1 541 . 81 ILE N N 120.97 0.20 1 542 . 82 SER H H 9.09 0.02 1 543 . 82 SER HA H 4.68 0.03 1 544 . 82 SER CA C 58.32 0.20 1 545 . 82 SER CB C 63.15 0.20 1 546 . 82 SER N N 119.05 0.20 1 547 . 83 SER H H 9.98 0.02 1 548 . 83 SER HA H 4.51 0.03 1 549 . 83 SER HB2 H 4.16 0.03 2 550 . 83 SER HB3 H 4.06 0.03 2 551 . 83 SER C C 173.89 0.10 1 552 . 83 SER CA C 61.19 0.20 1 553 . 83 SER CB C 63.23 0.20 1 554 . 83 SER N N 128.97 0.20 1 555 . 84 VAL H H 8.12 0.02 1 556 . 84 VAL HA H 4.18 0.03 1 557 . 84 VAL HB H 2.03 0.03 1 558 . 84 VAL HG1 H 1.04 0.03 2 559 . 84 VAL HG2 H 1.10 0.03 2 560 . 84 VAL C C 177.92 0.10 1 561 . 84 VAL CA C 64.58 0.20 1 562 . 84 VAL CB C 33.76 0.20 1 563 . 84 VAL CG1 C 21.32 0.20 1 564 . 84 VAL CG2 C 21.72 0.20 1 565 . 84 VAL N N 121.11 0.20 1 566 . 85 THR H H 8.10 0.02 1 567 . 85 THR HA H 4.60 0.03 1 568 . 85 THR HG2 H 1.30 0.03 1 569 . 85 THR C C 176.47 0.10 1 570 . 85 THR CA C 61.72 0.20 1 571 . 85 THR CB C 71.25 0.20 1 572 . 85 THR CG2 C 21.12 0.20 1 573 . 85 THR N N 106.24 0.20 1 574 . 86 GLY H H 7.86 0.02 1 575 . 86 GLY HA2 H 3.90 0.03 2 576 . 86 GLY HA3 H 5.03 0.03 2 577 . 86 GLY C C 174.31 0.10 1 578 . 86 GLY CA C 46.41 0.20 1 579 . 86 GLY N N 109.44 0.20 1 580 . 87 ALA H H 7.87 0.02 1 581 . 87 ALA HA H 4.49 0.03 1 582 . 87 ALA HB H 1.41 0.03 1 583 . 87 ALA C C 176.27 0.10 1 584 . 87 ALA CA C 53.16 0.20 1 585 . 87 ALA CB C 19.44 0.20 1 586 . 87 ALA N N 122.18 0.20 1 587 . 88 ILE H H 8.76 0.02 1 588 . 88 ILE HA H 4.59 0.03 1 589 . 88 ILE HB H 1.56 0.03 1 590 . 88 ILE CA C 60.54 0.20 1 591 . 88 ILE CB C 42.72 0.20 1 592 . 88 ILE N N 118.84 0.20 1 593 . 89 CYS H H 8.86 0.02 1 594 . 89 CYS HA H 4.59 0.03 1 595 . 89 CYS HB3 H 2.93 0.03 2 596 . 89 CYS CA C 57.60 0.20 1 597 . 89 CYS CB C 26.84 0.20 1 598 . 89 CYS N N 126.89 0.20 1 599 . 90 LEU H H 7.60 0.02 1 600 . 90 LEU HA H 4.67 0.03 1 601 . 90 LEU HB3 H 1.53 0.03 2 602 . 90 LEU CA C 54.42 0.20 1 603 . 90 LEU CB C 45.19 0.20 1 604 . 90 LEU N N 125.67 0.20 1 605 . 91 ASP CA C 58.51 0.20 1 606 . 91 ASP CB C 39.29 0.20 1 607 . 92 ILE H H 8.40 0.02 1 608 . 92 ILE HA H 3.79 0.03 1 609 . 92 ILE HB H 2.08 0.03 1 610 . 92 ILE HG2 H 0.99 0.03 1 611 . 92 ILE C C 173.65 0.10 1 612 . 92 ILE CA C 64.29 0.20 1 613 . 92 ILE CB C 38.74 0.20 1 614 . 92 ILE CG2 C 18.40 0.20 1 615 . 92 ILE N N 117.11 0.20 1 616 . 93 LEU H H 7.20 0.02 1 617 . 93 LEU HA H 4.63 0.03 1 618 . 93 LEU HB3 H 1.89 0.03 2 619 . 93 LEU C C 178.28 0.10 1 620 . 93 LEU CA C 54.10 0.20 1 621 . 93 LEU CB C 41.23 0.20 1 622 . 93 LEU N N 113.62 0.20 1 623 . 94 ARG H H 8.03 0.02 1 624 . 94 ARG HA H 4.56 0.03 1 625 . 94 ARG HB2 H 1.92 0.03 2 626 . 94 ARG HB3 H 2.00 0.03 2 627 . 94 ARG HD3 H 3.29 0.03 2 628 . 94 ARG C C 179.91 0.10 1 629 . 94 ARG CA C 56.23 0.20 1 630 . 94 ARG CB C 31.43 0.20 1 631 . 94 ARG CD C 43.67 0.20 1 632 . 94 ARG N N 121.36 0.20 1 633 . 95 ASN H H 8.46 0.02 1 634 . 95 ASN HA H 4.84 0.03 1 635 . 95 ASN HB2 H 2.93 0.03 2 636 . 95 ASN HB3 H 3.00 0.03 2 637 . 95 ASN C C 175.47 0.10 1 638 . 95 ASN CA C 54.83 0.20 1 639 . 95 ASN CB C 38.88 0.20 1 640 . 95 ASN N N 118.07 0.20 1 641 . 96 ALA H H 7.93 0.02 1 642 . 96 ALA HA H 4.71 0.03 1 643 . 96 ALA HB H 1.19 0.03 1 644 . 96 ALA C C 175.67 0.10 1 645 . 96 ALA CA C 51.06 0.20 1 646 . 96 ALA CB C 18.61 0.20 1 647 . 96 ALA N N 121.03 0.20 1 648 . 97 TRP H H 7.48 0.02 1 649 . 97 TRP HA H 4.36 0.03 1 650 . 97 TRP C C 176.03 0.10 1 651 . 97 TRP CA C 59.11 0.20 1 652 . 97 TRP CB C 30.12 0.20 1 653 . 97 TRP N N 120.92 0.20 1 654 . 98 SER H H 5.62 0.02 1 655 . 98 SER HA H 4.66 0.03 1 656 . 98 SER HB2 H 3.32 0.03 2 657 . 98 SER HB3 H 3.86 0.03 2 658 . 98 SER C C 171.44 0.10 1 659 . 98 SER CA C 54.31 0.20 1 660 . 98 SER CB C 64.42 0.20 1 661 . 98 SER N N 121.01 0.20 1 662 . 99 PRO C C 176.18 0.10 1 663 . 99 PRO CA C 63.97 0.20 1 664 . 99 PRO CB C 31.89 0.20 1 665 . 100 VAL H H 6.82 0.02 1 666 . 100 VAL HA H 3.94 0.03 1 667 . 100 VAL HB H 2.04 0.03 1 668 . 100 VAL HG1 H 0.74 0.03 2 669 . 100 VAL HG2 H 0.81 0.03 2 670 . 100 VAL C C 176.47 0.10 1 671 . 100 VAL CA C 62.17 0.20 1 672 . 100 VAL CB C 31.58 0.20 1 673 . 100 VAL CG1 C 19.58 0.20 1 674 . 100 VAL CG2 C 20.86 0.20 1 675 . 100 VAL N N 112.34 0.20 1 676 . 101 ILE H H 7.36 0.02 1 677 . 101 ILE HA H 3.53 0.03 1 678 . 101 ILE HB H 1.27 0.03 1 679 . 101 ILE HD1 H 0.83 0.03 1 680 . 101 ILE HG2 H 0.75 0.03 1 681 . 101 ILE C C 173.23 0.10 1 682 . 101 ILE CA C 62.20 0.20 1 683 . 101 ILE CB C 35.69 0.20 1 684 . 101 ILE CD1 C 18.03 0.20 1 685 . 101 ILE CG2 C 22.43 0.20 1 686 . 101 ILE N N 125.04 0.20 1 687 . 102 THR H H 6.81 0.02 1 688 . 102 THR HA H 4.90 0.03 1 689 . 102 THR HB H 3.46 0.03 1 690 . 102 THR HG2 H 1.21 0.03 1 691 . 102 THR CA C 58.70 0.20 1 692 . 102 THR CB C 72.07 0.20 1 693 . 102 THR CG2 C 21.74 0.20 1 694 . 102 THR N N 111.41 0.20 1 695 . 103 LEU H H 9.96 0.02 1 696 . 103 LEU C C 179.25 0.10 1 697 . 103 LEU CA C 58.76 0.20 1 698 . 103 LEU CB C 41.11 0.20 1 699 . 103 LEU N N 121.86 0.20 1 700 . 104 LYS H H 8.77 0.02 1 701 . 104 LYS C C 177.36 0.10 1 702 . 104 LYS CA C 60.54 0.20 1 703 . 104 LYS CB C 32.50 0.20 1 704 . 104 LYS N N 117.48 0.20 1 705 . 105 SER H H 7.90 0.02 1 706 . 105 SER HA H 4.11 0.03 1 707 . 105 SER HB2 H 4.05 0.03 2 708 . 105 SER HB3 H 4.00 0.03 2 709 . 105 SER C C 177.59 0.10 1 710 . 105 SER CA C 61.30 0.20 1 711 . 105 SER CB C 62.87 0.20 1 712 . 105 SER N N 113.56 0.20 1 713 . 106 ALA H H 8.81 0.02 1 714 . 106 ALA HA H 4.02 0.03 1 715 . 106 ALA HB H 1.52 0.03 1 716 . 106 ALA C C 178.95 0.10 1 717 . 106 ALA CA C 55.50 0.20 1 718 . 106 ALA CB C 17.47 0.20 1 719 . 106 ALA N N 125.71 0.20 1 720 . 107 LEU H H 8.17 0.02 1 721 . 107 LEU HA H 3.81 0.03 1 722 . 107 LEU C C 178.80 0.10 1 723 . 107 LEU CA C 58.44 0.20 1 724 . 107 LEU CB C 41.21 0.20 1 725 . 107 LEU N N 118.46 0.20 1 726 . 108 ILE H H 8.25 0.02 1 727 . 108 ILE HA H 3.60 0.03 1 728 . 108 ILE HB H 1.94 0.03 1 729 . 108 ILE HG13 H 0.79 0.03 2 730 . 108 ILE HD1 H 1.08 0.03 1 731 . 108 ILE HG2 H 0.93 0.03 1 732 . 108 ILE C C 179.41 0.10 1 733 . 108 ILE CA C 65.16 0.20 1 734 . 108 ILE CB C 37.23 0.20 1 735 . 108 ILE CG1 C 25.51 0.20 1 736 . 108 ILE CD1 C 16.74 0.20 1 737 . 108 ILE CG2 C 17.17 0.20 1 738 . 108 ILE N N 121.14 0.20 1 739 . 109 SER H H 8.36 0.02 1 740 . 109 SER HA H 4.23 0.03 1 741 . 109 SER C C 176.88 0.10 1 742 . 109 SER CA C 62.54 0.20 1 743 . 109 SER N N 118.68 0.20 1 744 . 110 LEU H H 7.83 0.02 1 745 . 110 LEU HA H 3.97 0.03 1 746 . 110 LEU HB3 H 1.74 0.03 2 747 . 110 LEU C C 177.61 0.10 1 748 . 110 LEU CA C 57.37 0.20 1 749 . 110 LEU CB C 41.39 0.20 1 750 . 110 LEU N N 124.60 0.20 1 751 . 111 GLN H H 7.42 0.02 1 752 . 111 GLN HA H 3.37 0.03 1 753 . 111 GLN HG2 H 2.23 0.03 2 754 . 111 GLN HG3 H 2.08 0.03 2 755 . 111 GLN C C 177.85 0.10 1 756 . 111 GLN CA C 59.64 0.20 1 757 . 111 GLN CB C 29.41 0.20 1 758 . 111 GLN CG C 34.47 0.20 1 759 . 111 GLN N N 120.65 0.20 1 760 . 112 ALA H H 8.10 0.02 1 761 . 112 ALA HA H 4.18 0.03 1 762 . 112 ALA HB H 1.51 0.03 1 763 . 112 ALA C C 180.17 0.10 1 764 . 112 ALA CA C 54.47 0.20 1 765 . 112 ALA CB C 17.66 0.20 1 766 . 112 ALA N N 120.58 0.20 1 767 . 113 LEU H H 7.77 0.02 1 768 . 113 LEU HA H 4.11 0.03 1 769 . 113 LEU C C 180.09 0.10 1 770 . 113 LEU CA C 56.65 0.20 1 771 . 113 LEU CB C 42.23 0.20 1 772 . 113 LEU N N 122.34 0.20 1 773 . 114 LEU H H 7.53 0.02 1 774 . 114 LEU HA H 3.63 0.03 1 775 . 114 LEU HB3 H 1.82 0.03 2 776 . 114 LEU C C 177.12 0.10 1 777 . 114 LEU CA C 58.30 0.20 1 778 . 114 LEU CB C 39.60 0.20 1 779 . 114 LEU N N 118.47 0.20 1 780 . 115 GLN H H 7.24 0.02 1 781 . 115 GLN HA H 4.26 0.03 1 782 . 115 GLN HB3 H 2.38 0.03 2 783 . 115 GLN HG3 H 2.46 0.03 2 784 . 115 GLN C C 175.80 0.10 1 785 . 115 GLN CA C 57.82 0.20 1 786 . 115 GLN CB C 29.79 0.20 1 787 . 115 GLN CG C 34.40 0.20 1 788 . 115 GLN N N 114.90 0.20 1 789 . 116 SER H H 7.94 0.02 1 790 . 116 SER HA H 4.93 0.03 1 791 . 116 SER HB2 H 3.93 0.03 2 792 . 116 SER HB3 H 3.69 0.03 2 793 . 116 SER CA C 54.52 0.20 1 794 . 116 SER CB C 63.28 0.20 1 795 . 116 SER N N 114.45 0.20 1 796 . 117 PRO C C 174.99 0.10 1 797 . 117 PRO CA C 61.21 0.20 1 798 . 117 PRO CB C 31.90 0.20 1 799 . 118 GLU H H 8.50 0.02 1 800 . 118 GLU HA H 4.49 0.03 1 801 . 118 GLU HB3 H 1.80 0.03 2 802 . 118 GLU C C 176.27 0.10 1 803 . 118 GLU CA C 54.99 0.20 1 804 . 118 GLU CB C 32.54 0.20 1 805 . 118 GLU N N 121.16 0.20 1 806 . 119 PRO C C 175.04 0.10 1 807 . 119 PRO CA C 64.35 0.20 1 808 . 119 PRO CB C 32.10 0.20 1 809 . 120 ASN H H 8.74 0.02 1 810 . 120 ASN HA H 4.61 0.03 1 811 . 120 ASN HB2 H 2.83 0.03 2 812 . 120 ASN HB3 H 2.75 0.03 2 813 . 120 ASN C C 174.60 0.10 1 814 . 120 ASN CA C 53.95 0.20 1 815 . 120 ASN CB C 38.05 0.20 1 816 . 120 ASN N N 115.92 0.20 1 817 . 121 ASP H H 7.20 0.02 1 818 . 121 ASP HA H 4.98 0.03 1 819 . 121 ASP HB2 H 2.23 0.03 2 820 . 121 ASP HB3 H 2.71 0.03 2 821 . 121 ASP C C 171.75 0.10 1 822 . 121 ASP CA C 51.54 0.20 1 823 . 121 ASP CB C 41.10 0.20 1 824 . 121 ASP N N 119.02 0.20 1 825 . 123 GLN HE21 H 6.86 0.03 2 826 . 123 GLN HE22 H 7.54 0.03 2 827 . 123 GLN CA C 55.79 0.20 1 828 . 123 GLN CB C 29.63 0.20 1 829 . 123 GLN CG C 34.00 0.20 1 830 . 123 GLN CD C 179.80 0.10 1 831 . 123 GLN NE2 N 111.28 0.20 1 832 . 124 ASP H H 7.37 0.02 1 833 . 124 ASP HA H 4.89 0.03 1 834 . 124 ASP HB2 H 2.60 0.03 2 835 . 124 ASP HB3 H 2.99 0.03 2 836 . 124 ASP C C 175.84 0.10 1 837 . 124 ASP CA C 53.00 0.20 1 838 . 124 ASP CB C 42.77 0.20 1 839 . 124 ASP N N 118.44 0.20 1 840 . 125 ALA HA H 3.93 0.03 1 841 . 125 ALA HB H 1.52 0.03 1 842 . 125 ALA C C 175.81 0.10 1 843 . 125 ALA CA C 55.60 0.20 1 844 . 125 ALA CB C 18.44 0.20 1 845 . 126 GLU H H 8.57 0.02 1 846 . 126 GLU HA H 4.12 0.03 1 847 . 126 GLU HB3 H 2.22 0.03 2 848 . 126 GLU C C 179.77 0.10 1 849 . 126 GLU CA C 59.70 0.20 1 850 . 126 GLU CB C 29.23 0.20 1 851 . 126 GLU N N 118.00 0.20 1 852 . 127 VAL H H 7.84 0.02 1 853 . 127 VAL HA H 3.68 0.03 1 854 . 127 VAL HB H 1.83 0.03 1 855 . 127 VAL HG1 H 0.28 0.03 2 856 . 127 VAL HG2 H 0.73 0.03 2 857 . 127 VAL C C 177.27 0.10 1 858 . 127 VAL CA C 66.35 0.20 1 859 . 127 VAL CB C 31.95 0.20 1 860 . 127 VAL CG1 C 21.38 0.20 1 861 . 127 VAL CG2 C 21.89 0.20 1 862 . 127 VAL N N 122.75 0.20 1 863 . 128 ALA H H 8.21 0.02 1 864 . 128 ALA HA H 3.73 0.03 1 865 . 128 ALA HB H 1.52 0.03 1 866 . 128 ALA C C 178.40 0.10 1 867 . 128 ALA CA C 55.63 0.20 1 868 . 128 ALA CB C 18.58 0.20 1 869 . 128 ALA N N 121.36 0.20 1 870 . 129 GLN H H 8.14 0.02 1 871 . 129 GLN HA H 4.04 0.03 1 872 . 129 GLN HB2 H 2.25 0.03 2 873 . 129 GLN HB3 H 2.22 0.03 2 874 . 129 GLN HE21 H 6.89 0.02 2 875 . 129 GLN HE22 H 7.50 0.02 2 876 . 129 GLN C C 178.17 0.10 1 877 . 129 GLN CA C 58.85 0.20 1 878 . 129 GLN CB C 28.46 0.20 1 879 . 129 GLN CD C 180.26 0.20 1 880 . 129 GLN N N 115.31 0.20 1 881 . 129 GLN NE2 N 111.87 0.20 1 882 . 130 HIS H H 7.89 0.02 1 883 . 130 HIS HA H 4.52 0.03 1 884 . 130 HIS C C 176.17 0.10 1 885 . 130 HIS CA C 57.88 0.20 1 886 . 130 HIS CB C 32.24 0.20 1 887 . 130 HIS N N 121.82 0.20 1 888 . 131 TYR H H 8.19 0.02 1 889 . 131 TYR HA H 4.38 0.03 1 890 . 131 TYR HB3 H 2.99 0.03 2 891 . 131 TYR C C 176.55 0.10 1 892 . 131 TYR CA C 61.79 0.20 1 893 . 131 TYR CB C 38.59 0.20 1 894 . 131 TYR N N 117.21 0.20 1 895 . 132 LEU H H 7.88 0.02 1 896 . 132 LEU HA H 3.96 0.03 1 897 . 132 LEU HB2 H 1.87 0.03 2 898 . 132 LEU HB3 H 1.83 0.03 2 899 . 132 LEU HG H 1.58 0.03 1 900 . 132 LEU HD1 H 0.80 0.03 2 901 . 132 LEU C C 179.02 0.10 1 902 . 132 LEU CA C 56.51 0.20 1 903 . 132 LEU CB C 43.15 0.20 1 904 . 132 LEU CG C 27.72 0.20 1 905 . 132 LEU CD1 C 25.08 0.20 1 906 . 132 LEU N N 115.20 0.20 1 907 . 133 ARG H H 8.44 0.02 1 908 . 133 ARG HA H 4.20 0.03 1 909 . 133 ARG HB2 H 1.97 0.03 2 910 . 133 ARG HB3 H 2.04 0.03 2 911 . 133 ARG HG3 H 1.78 0.03 2 912 . 133 ARG HD2 H 3.29 0.03 2 913 . 133 ARG HD3 H 3.26 0.03 2 914 . 133 ARG C C 177.27 0.10 1 915 . 133 ARG CA C 58.20 0.20 1 916 . 133 ARG CB C 31.07 0.20 1 917 . 133 ARG CG C 27.60 0.20 1 918 . 133 ARG CD C 42.96 0.20 1 919 . 133 ARG N N 119.60 0.20 1 920 . 134 ASP H H 8.10 0.02 1 921 . 134 ASP HA H 4.71 0.03 1 922 . 134 ASP HB2 H 2.67 0.03 2 923 . 134 ASP HB3 H 2.98 0.03 2 924 . 134 ASP C C 174.02 0.10 1 925 . 134 ASP CA C 53.23 0.20 1 926 . 134 ASP CB C 41.06 0.20 1 927 . 134 ASP N N 117.90 0.20 1 928 . 135 ARG H H 8.73 0.02 1 929 . 135 ARG HA H 3.74 0.03 1 930 . 135 ARG HB3 H 1.76 0.03 2 931 . 135 ARG HG3 H 1.20 0.03 2 932 . 135 ARG HD3 H 2.64 0.03 2 933 . 135 ARG C C 177.89 0.10 1 934 . 135 ARG CA C 57.75 0.20 1 935 . 135 ARG CB C 29.03 0.20 1 936 . 135 ARG CG C 26.60 0.20 1 937 . 135 ARG N N 127.34 0.20 1 938 . 136 GLU H H 8.30 0.02 1 939 . 136 GLU HA H 4.14 0.03 1 940 . 136 GLU HB3 H 2.10 0.03 2 941 . 136 GLU HG2 H 2.32 0.03 2 942 . 136 GLU HG3 H 2.38 0.03 2 943 . 136 GLU C C 179.34 0.10 1 944 . 136 GLU CA C 59.39 0.20 1 945 . 136 GLU CB C 29.15 0.20 1 946 . 136 GLU CG C 36.66 0.20 1 947 . 136 GLU N N 117.06 0.20 1 948 . 137 SER H H 7.72 0.02 1 949 . 137 SER HA H 4.29 0.03 1 950 . 137 SER HB2 H 4.12 0.03 2 951 . 137 SER HB3 H 4.09 0.03 2 952 . 137 SER C C 178.32 0.10 1 953 . 137 SER CA C 60.12 0.20 1 954 . 137 SER CB C 62.21 0.20 1 955 . 137 SER N N 114.94 0.20 1 956 . 138 PHE H H 8.70 0.02 1 957 . 138 PHE C C 176.05 0.10 1 958 . 138 PHE CA C 62.79 0.20 1 959 . 138 PHE CB C 38.30 0.20 1 960 . 138 PHE N N 125.37 0.20 1 961 . 139 ASN H H 8.97 0.02 1 962 . 139 ASN HA H 4.16 0.03 1 963 . 139 ASN HB3 H 3.16 0.03 2 964 . 139 ASN C C 178.19 0.10 1 965 . 139 ASN CA C 55.57 0.20 1 966 . 139 ASN CB C 37.30 0.20 1 967 . 139 ASN N N 120.52 0.20 1 968 . 140 LYS H H 7.82 0.02 1 969 . 140 LYS HA H 4.06 0.03 1 970 . 140 LYS HB3 H 1.97 0.03 2 971 . 140 LYS HG3 H 1.53 0.03 2 972 . 140 LYS HD3 H 1.70 0.03 2 973 . 140 LYS HE3 H 3.03 0.03 2 974 . 140 LYS C C 179.89 0.10 1 975 . 140 LYS CA C 59.62 0.20 1 976 . 140 LYS CB C 32.44 0.20 1 977 . 140 LYS CG C 25.47 0.20 1 978 . 140 LYS CD C 29.32 0.20 1 979 . 140 LYS CE C 42.13 0.20 1 980 . 140 LYS N N 120.55 0.20 1 981 . 141 THR H H 7.82 0.02 1 982 . 141 THR HA H 3.77 0.03 1 983 . 141 THR HB H 3.49 0.03 1 984 . 141 THR HG2 H -0.04 0.03 1 985 . 141 THR C C 174.76 0.10 1 986 . 141 THR CA C 67.32 0.20 1 987 . 141 THR CB C 68.70 0.20 1 988 . 141 THR CG2 C 19.87 0.20 1 989 . 141 THR N N 119.45 0.20 1 990 . 142 ALA H H 8.73 0.02 1 991 . 142 ALA HA H 3.94 0.03 1 992 . 142 ALA HB H 1.05 0.03 1 993 . 142 ALA C C 180.83 0.10 1 994 . 142 ALA CA C 55.58 0.20 1 995 . 142 ALA CB C 17.45 0.20 1 996 . 142 ALA N N 124.03 0.20 1 997 . 143 ALA H H 8.39 0.02 1 998 . 143 ALA HA H 4.59 0.03 1 999 . 143 ALA HB H 1.53 0.03 1 1000 . 143 ALA C C 180.10 0.10 1 1001 . 143 ALA CA C 54.94 0.20 1 1002 . 143 ALA CB C 17.89 0.20 1 1003 . 143 ALA N N 122.34 0.20 1 1004 . 144 LEU H H 7.89 0.02 1 1005 . 144 LEU HA H 4.22 0.03 1 1006 . 144 LEU C C 178.88 0.10 1 1007 . 144 LEU CA C 58.43 0.20 1 1008 . 144 LEU CB C 41.19 0.20 1 1009 . 144 LEU N N 123.18 0.20 1 1010 . 145 TRP H H 9.19 0.02 1 1011 . 145 TRP HA H 4.31 0.03 1 1012 . 145 TRP C C 180.82 0.10 1 1013 . 145 TRP CA C 61.46 0.20 1 1014 . 145 TRP CB C 28.41 0.20 1 1015 . 145 TRP N N 119.18 0.20 1 1016 . 146 THR H H 8.51 0.02 1 1017 . 146 THR HA H 4.16 0.03 1 1018 . 146 THR HG2 H 1.20 0.03 1 1019 . 146 THR C C 176.44 0.10 1 1020 . 146 THR CA C 68.06 0.20 1 1021 . 146 THR CG2 C 22.11 0.20 1 1022 . 146 THR N N 123.27 0.20 1 1023 . 147 ARG H H 7.91 0.02 1 1024 . 147 ARG HA H 3.99 0.03 1 1025 . 147 ARG HB3 H 1.92 0.03 2 1026 . 147 ARG C C 178.70 0.10 1 1027 . 147 ARG CA C 59.14 0.20 1 1028 . 147 ARG CB C 30.11 0.20 1 1029 . 147 ARG N N 122.61 0.20 1 1030 . 148 LEU H H 8.56 0.02 1 1031 . 148 LEU HA H 3.82 0.03 1 1032 . 148 LEU HD1 H 0.73 0.03 2 1033 . 148 LEU HD2 H 0.27 0.03 2 1034 . 148 LEU C C 180.00 0.10 1 1035 . 148 LEU CA C 57.02 0.20 1 1036 . 148 LEU CB C 41.87 0.20 1 1037 . 148 LEU N N 116.77 0.20 1 1038 . 149 TYR H H 8.12 0.02 1 1039 . 149 TYR HA H 5.06 0.03 1 1040 . 149 TYR HB3 H 3.63 0.03 2 1041 . 149 TYR C C 176.20 0.10 1 1042 . 149 TYR CA C 57.30 0.20 1 1043 . 149 TYR CB C 39.99 0.20 1 1044 . 149 TYR N N 113.40 0.20 1 1045 . 150 ALA H H 7.85 0.02 1 1046 . 150 ALA HA H 4.87 0.03 1 1047 . 150 ALA HB H 1.07 0.03 1 1048 . 150 ALA C C 176.24 0.10 1 1049 . 150 ALA CA C 50.87 0.20 1 1050 . 150 ALA CB C 20.31 0.20 1 1051 . 150 ALA N N 124.27 0.20 1 1052 . 151 SER H H 7.48 0.02 1 1053 . 151 SER HA H 4.47 0.03 1 1054 . 151 SER HB2 H 3.91 0.03 1 1055 . 151 SER HB3 H 3.91 0.03 1 1056 . 151 SER C C 178.93 0.10 1 1057 . 151 SER CA C 59.63 0.20 1 1058 . 151 SER CB C 65.03 0.20 1 1059 . 151 SER N N 119.61 0.20 1 stop_ save_