data_5300 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Resonance Assignments for the 20.8 KDa C.elegans gene product ORF C32E8.3. Northeast Structural Genomics Consortium Target WR33. ; _BMRB_accession_number 5300 _BMRB_flat_file_name bmr5300.str _Entry_type original _Submission_date 2002-02-22 _Accession_date 2002-02-25 _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 Monleon Daniel . . 2 YiWen Chiang . . 3 Aramini James . . 4 Swapna G.V.T. . . 5 Kim Seho . . 6 Szyperski Thomas . . 7 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 331 "13C chemical shifts" 496 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-27 original author . stop_ _Original_release_date 2002-06-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C assignments for the 21 kDa Caenorhabditis elegans homologue of 'brain-specific' protein ; _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 Monleon Daniel . . 2 YiWen Chiang . . 3 Aramini James M. . 4 Swapna G.V.T. . . 5 Macapagal Daphne . . 6 Gunsalus Kristin C. . 7 Kim Seho . . 8 Szyperski Thomas . . 9 Montelione Gaetano T. . 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 91 _Page_last 92 _Year 2004 _Details . loop_ _Keyword 'structural genomics' 'Northeast Structural Genomics Consortium' WR33 nematode stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T. J. Mol. Biol. 269, 592-610, (1997). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9217263 _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_wr33 _Saveframe_category molecular_system _Mol_system_name 'ORF C32E8.3' _Abbreviation_common 'ORF C32E8.3' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C.elegans ORF C32E8.3' $WR33 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_WR33 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ORF C32E8.3' _Abbreviation_common 'ORF C32E8.3' _Molecular_mass 20800 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 190 _Mol_residue_sequence ; MGHHHHHHSHMAAAAGFNWD DADVKKRWDAFTKFGAATAT EMTGKNFDKWLKDAGVLDNK AITGTMTGIAFSKVTGPKKK ATFDETKKVLAFVAEDRARQ SKKPIQDELDAITEKLAKLE APSVGGAAKANAAGVYSRLT DHTKYTGAHKERFDAEGKGK GKSGRADTTENTGYVGAYKN KDSYDKTHGK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 SER 10 HIS 11 MET 12 ALA 13 ALA 14 ALA 15 ALA 16 GLY 17 PHE 18 ASN 19 TRP 20 ASP 21 ASP 22 ALA 23 ASP 24 VAL 25 LYS 26 LYS 27 ARG 28 TRP 29 ASP 30 ALA 31 PHE 32 THR 33 LYS 34 PHE 35 GLY 36 ALA 37 ALA 38 THR 39 ALA 40 THR 41 GLU 42 MET 43 THR 44 GLY 45 LYS 46 ASN 47 PHE 48 ASP 49 LYS 50 TRP 51 LEU 52 LYS 53 ASP 54 ALA 55 GLY 56 VAL 57 LEU 58 ASP 59 ASN 60 LYS 61 ALA 62 ILE 63 THR 64 GLY 65 THR 66 MET 67 THR 68 GLY 69 ILE 70 ALA 71 PHE 72 SER 73 LYS 74 VAL 75 THR 76 GLY 77 PRO 78 LYS 79 LYS 80 LYS 81 ALA 82 THR 83 PHE 84 ASP 85 GLU 86 THR 87 LYS 88 LYS 89 VAL 90 LEU 91 ALA 92 PHE 93 VAL 94 ALA 95 GLU 96 ASP 97 ARG 98 ALA 99 ARG 100 GLN 101 SER 102 LYS 103 LYS 104 PRO 105 ILE 106 GLN 107 ASP 108 GLU 109 LEU 110 ASP 111 ALA 112 ILE 113 THR 114 GLU 115 LYS 116 LEU 117 ALA 118 LYS 119 LEU 120 GLU 121 ALA 122 PRO 123 SER 124 VAL 125 GLY 126 GLY 127 ALA 128 ALA 129 LYS 130 ALA 131 ASN 132 ALA 133 ALA 134 GLY 135 VAL 136 TYR 137 SER 138 ARG 139 LEU 140 THR 141 ASP 142 HIS 143 THR 144 LYS 145 TYR 146 THR 147 GLY 148 ALA 149 HIS 150 LYS 151 GLU 152 ARG 153 PHE 154 ASP 155 ALA 156 GLU 157 GLY 158 LYS 159 GLY 160 LYS 161 GLY 162 LYS 163 SER 164 GLY 165 ARG 166 ALA 167 ASP 168 THR 169 THR 170 GLU 171 ASN 172 THR 173 GLY 174 TYR 175 VAL 176 GLY 177 ALA 178 TYR 179 LYS 180 ASN 181 LYS 182 ASP 183 SER 184 TYR 185 ASP 186 LYS 187 THR 188 HIS 189 GLY 190 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-07-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1PUL "Solution Structure For The 21kda Caenorhabditis Elegans Protein Ce32e8.3. Northeast Structural Genomics Consortium Target Wr33" 65.79 125 100.00 100.00 2.82e-83 EMBL CCD66401 "Protein C32E8.3 [Caenorhabditis elegans]" 94.74 180 100.00 100.00 2.63e-123 REF NP_491219 "Protein C32E8.3 [Caenorhabditis elegans]" 94.74 180 100.00 100.00 2.63e-123 SP P91127 "RecName: Full=TPPP family protein C32E8.3 [Caenorhabditis elegans]" 94.74 180 100.00 100.00 2.63e-123 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WR33 C.elegans. 6239 Eubacteria . Caenorhabditis elegans 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 _Details $WR33 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pET15b ; C.elegans ORF C32E8.3 (WR33) gene was cloned into expression plasmid pET15b, generating plasmid pETWR33 E.coli strain BL21(DE3) cell cultures transformed with pETWR33 were grown at 37 C in MJ minimal media containing U15N-(NH4)2SO4 and 13C-glucose as sole nitrogen and carbon sources. ; 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 $WR33 1.4 mM '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WR33 0.5 mM '[U-13C; U-15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type Bi-cell _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WR33 0.5 mM '[U-13C; U-15N]' DMPC:DHCP:CTAB(30:10:1) 4.5 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2000 loop_ _Task 'data processing' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.91 loop_ _Task 'peak picking' stop_ _Details . save_ save_AUTOASSIGN _Saveframe_category software _Name AUTOASSIGN _Version 1.8.0 loop_ _Task 'automated analysis of backbone 1H, 13C and 15N assignments' stop_ _Details 'In-house developed software for automating the peak assignment process.' _Citation_label $ref-1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_(HA)CA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CA(CO)NH _Sample_label . save_ save_HA(CA)(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)(CO)NH _Sample_label . save_ save_(HA)CANH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CANH _Sample_label . save_ save_HA(CA)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)NH _Sample_label . save_ save_(H)CC(CO)NH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _Sample_label . save_ save_13C-edited_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label . save_ save_15N-edited_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_RD-HNCA,HA_12 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HNCA,HA _Sample_label . save_ save_RD-HA,CA(CO)NH_13 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HA,CA(CO)NH _Sample_label . save_ save_RDC-JHC_COUPLED_(HA)CANH_14 _Saveframe_category NMR_applied_experiment _Experiment_name 'RDC-JHC COUPLED (HA)CANH' _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 HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)CANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HNCA,HA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HA,CA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name 'RDC-JHC COUPLED (HA)CANH' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details ; The sample stability was tested by recording a 1H-15N HSQC spectrum every 3 days during the global data collection period. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.50 0.05 n/a temperature 298 0.5 K stop_ save_ save_condition_2 _Saveframe_category sample_conditions _Details ; This sample was put in DMPC:DMHC:CTAB bicelle 30:10:1 4.5% for alignment purposes. Aligned sample at T=32C. Unaligned sample at T=25C. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.50 0.05 n/a temperature 298 0.5 K stop_ save_ save_condition_3 _Saveframe_category sample_conditions _Details ; This sample was put in DMPC:DMHC:CTAB bicelle 30:10:1 4.5% for alignment purposes. Aligned sample at T=32C. Unaligned sample at T=25C. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.50 0.05 n/a temperature 305 0.5 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'C.elegans ORF C32E8.3' _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 C C 177.6 0.2 1 2 . 1 MET CA C 57.1 0.2 1 3 . 1 MET CB C 33.4 0.2 1 4 . 2 GLY HA2 H 4.22 0.01 1 5 . 2 GLY C C 174.4 0.2 1 6 . 2 GLY H H 8.50 0.01 1 7 . 2 GLY HA3 H 3.97 0.01 1 8 . 2 GLY CA C 45.9 0.2 1 9 . 2 GLY N N 109.9 0.2 1 10 . 3 HIS H H 7.84 0.01 1 11 . 3 HIS HA H 4.02 0.05 1 12 . 3 HIS CA C 63.1 0.2 1 13 . 3 HIS CB C 33.0 0.2 1 14 . 3 HIS N N 119.6 0.2 1 15 . 4 HIS H H 8.29 0.01 1 16 . 4 HIS CA C 54.6 0.2 1 17 . 4 HIS CB C 33.3 0.2 1 18 . 4 HIS N N 122.3 0.2 1 19 . 8 HIS C C 176.8 0.2 1 20 . 9 SER C C 177.9 0.2 1 21 . 9 SER H H 7.57 0.01 1 22 . 9 SER CA C 61.8 0.2 1 23 . 9 SER N N 121.0 0.2 1 24 . 10 HIS C C 179.1 0.2 1 25 . 10 HIS H H 7.10 0.01 1 26 . 10 HIS CA C 60.2 0.2 1 27 . 10 HIS CB C 32.5 0.2 1 28 . 10 HIS N N 119.1 0.2 1 29 . 11 MET C C 176.7 0.2 1 30 . 11 MET H H 8.26 0.01 1 31 . 11 MET CA C 56.7 0.2 1 32 . 11 MET CB C 33.6 0.2 1 33 . 11 MET N N 119.9 0.2 1 34 . 12 ALA C C 177.9 0.2 1 35 . 12 ALA H H 8.26 0.01 1 36 . 12 ALA CA C 53.1 0.2 1 37 . 12 ALA CB C 19.6 0.2 1 38 . 12 ALA N N 125.2 0.2 1 39 . 13 ALA C C 177.5 0.2 1 40 . 13 ALA H H 8.24 0.01 1 41 . 13 ALA HA H 4.35 0.05 1 42 . 13 ALA CA C 58.4 0.2 1 43 . 13 ALA CB C 19.7 0.2 1 44 . 13 ALA N N 123.3 0.2 1 45 . 14 ALA C C 177.2 0.2 1 46 . 14 ALA H H 8.06 0.01 1 47 . 14 ALA HA H 4.28 0.05 1 48 . 14 ALA CA C 52.6 0.2 1 49 . 14 ALA CB C 19.7 0.2 1 50 . 14 ALA N N 123.0 0.2 1 51 . 15 ALA C C 177.0 0.2 1 52 . 15 ALA H H 7.92 0.01 1 53 . 15 ALA HA H 4.20 0.05 1 54 . 15 ALA CA C 52.5 0.2 1 55 . 15 ALA CB C 19.7 0.2 1 56 . 15 ALA N N 123.4 0.2 1 57 . 16 GLY HA2 H 3.61 0.01 1 58 . 16 GLY C C 172.7 0.2 1 59 . 16 GLY H H 8.73 0.01 1 60 . 16 GLY CA C 44.7 0.2 1 61 . 16 GLY N N 109.5 0.2 1 62 . 17 PHE C C 175.8 0.2 1 63 . 17 PHE H H 8.47 0.01 1 64 . 17 PHE HA H 3.72 0.05 1 65 . 17 PHE CA C 58.3 0.2 1 66 . 17 PHE CB C 39.2 0.2 1 67 . 17 PHE N N 120.5 0.2 1 68 . 18 ASN C C 174.3 0.2 1 69 . 18 ASN H H 9.15 0.01 1 70 . 18 ASN HA H 4.92 0.05 1 71 . 18 ASN CA C 53.3 0.2 1 72 . 18 ASN CB C 37.9 0.2 1 73 . 18 ASN N N 126.3 0.2 1 74 . 19 TRP C C 174.9 0.2 1 75 . 19 TRP H H 7.93 0.01 1 76 . 19 TRP HA H 5.00 0.05 1 77 . 19 TRP CA C 53.7 0.2 1 78 . 19 TRP CB C 30.6 0.2 1 79 . 19 TRP N N 118.1 0.2 1 80 . 20 ASP C C 175.3 0.2 1 81 . 20 ASP H H 9.25 0.01 1 82 . 20 ASP HA H 5.01 0.05 1 83 . 20 ASP CA C 53.4 0.2 1 84 . 20 ASP CB C 41.1 0.2 1 85 . 20 ASP N N 121.1 0.2 1 86 . 21 ASP C C 177.3 0.2 1 87 . 21 ASP H H 8.69 0.01 1 88 . 21 ASP HA H 4.05 0.05 1 89 . 21 ASP CA C 59.2 0.2 1 90 . 21 ASP CB C 43.8 0.2 1 91 . 21 ASP N N 127.8 0.2 1 92 . 22 ALA H H 8.08 0.01 1 93 . 22 ALA HA H 3.98 0.05 1 94 . 22 ALA CA C 55.6 0.2 1 95 . 22 ALA CB C 18.6 0.2 1 96 . 22 ALA N N 118.5 0.2 1 97 . 23 ASP C C 176.8 0.2 1 98 . 23 ASP H H 7.60 0.01 1 99 . 23 ASP HA H 4.37 0.05 1 100 . 23 ASP CA C 57.8 0.2 1 101 . 23 ASP CB C 43.5 0.2 1 102 . 23 ASP N N 119.7 0.2 1 103 . 24 VAL C C 177.2 0.2 1 104 . 24 VAL H H 8.54 0.01 1 105 . 24 VAL HA H 3.40 0.05 1 106 . 24 VAL CA C 67.6 0.2 1 107 . 24 VAL CB C 31.1 0.2 1 108 . 24 VAL N N 119.0 0.2 1 109 . 25 LYS C C 178.3 0.2 1 110 . 25 LYS H H 8.37 0.01 1 111 . 25 LYS HA H 3.08 0.05 1 112 . 25 LYS CA C 57.3 0.2 1 113 . 25 LYS CB C 29.6 0.2 1 114 . 25 LYS N N 122.3 0.2 1 115 . 26 LYS H H 6.97 0.01 1 116 . 26 LYS HA H 4.14 0.05 1 117 . 26 LYS CA C 60.3 0.2 1 118 . 26 LYS CB C 32.7 0.2 1 119 . 26 LYS N N 117.1 0.2 1 120 . 27 ARG C C 178.3 0.2 1 121 . 27 ARG H H 7.44 0.01 1 122 . 27 ARG HA H 4.14 0.05 1 123 . 27 ARG CA C 60.2 0.2 1 124 . 27 ARG CB C 30.6 0.2 1 125 . 27 ARG N N 121.8 0.2 1 126 . 28 TRP C C 179.0 0.2 1 127 . 28 TRP H H 9.44 0.01 1 128 . 28 TRP HA H 3.15 0.05 1 129 . 28 TRP CA C 62.4 0.2 1 130 . 28 TRP CB C 29.7 0.2 1 131 . 28 TRP N N 121.3 0.2 1 132 . 29 ASP C C 177.4 0.2 1 133 . 29 ASP H H 8.91 0.01 1 134 . 29 ASP HA H 3.84 0.05 1 135 . 29 ASP CA C 58.3 0.2 1 136 . 29 ASP CB C 42.0 0.2 1 137 . 29 ASP N N 121.5 0.2 1 138 . 30 ALA H H 7.16 0.01 1 139 . 30 ALA HA H 3.97 0.05 1 140 . 30 ALA CA C 55.2 0.2 1 141 . 30 ALA CB C 19.0 0.2 1 142 . 30 ALA N N 119.7 0.2 1 143 . 31 PHE C C 175.8 0.2 1 144 . 31 PHE H H 7.65 0.01 1 145 . 31 PHE HA H 3.98 0.05 1 146 . 31 PHE CA C 63.3 0.2 1 147 . 31 PHE CB C 39.4 0.2 1 148 . 31 PHE N N 116.5 0.2 1 149 . 32 THR C C 175.0 0.2 1 150 . 32 THR H H 8.16 0.01 1 151 . 32 THR HA H 4.83 0.05 1 152 . 32 THR CA C 62.8 0.2 1 153 . 32 THR CB C 70.2 0.2 1 154 . 32 THR N N 114.3 0.2 1 155 . 33 LYS C C 176.4 0.2 1 156 . 33 LYS H H 8.41 0.01 1 157 . 33 LYS HA H 4.34 0.05 1 158 . 33 LYS CA C 57.0 0.2 1 159 . 33 LYS CB C 30.7 0.2 1 160 . 33 LYS N N 123.3 0.2 1 161 . 34 PHE C C 175.7 0.2 1 162 . 34 PHE H H 8.50 0.01 1 163 . 34 PHE HA H 4.19 0.05 1 164 . 34 PHE CA C 53.7 0.2 1 165 . 34 PHE CB C 39.3 0.2 1 166 . 34 PHE N N 120.2 0.2 1 167 . 35 GLY C C 173.9 0.2 1 168 . 35 GLY H H 8.32 0.01 1 169 . 35 GLY CA C 46.6 0.2 1 170 . 35 GLY N N 122.3 0.2 1 171 . 36 ALA C C 176.0 0.2 1 172 . 36 ALA H H 7.83 0.01 1 173 . 36 ALA HA H 4.50 0.05 1 174 . 36 ALA CA C 52.6 0.2 1 175 . 36 ALA CB C 18.8 0.2 1 176 . 36 ALA N N 125.4 0.2 1 177 . 37 ALA C C 178.7 0.2 1 178 . 37 ALA H H 8.44 0.01 1 179 . 37 ALA HA H 4.09 0.05 1 180 . 37 ALA CA C 56.1 0.2 1 181 . 37 ALA CB C 19.6 0.2 1 182 . 37 ALA N N 123.3 0.2 1 183 . 38 THR C C 175.4 0.2 1 184 . 38 THR H H 7.75 0.01 1 185 . 38 THR HA H 4.38 0.05 1 186 . 38 THR CA C 60.9 0.2 1 187 . 38 THR CB C 69.8 0.2 1 188 . 38 THR N N 103.7 0.2 1 189 . 39 ALA C C 177.6 0.2 1 190 . 39 ALA H H 7.96 0.01 1 191 . 39 ALA HA H 4.20 0.05 1 192 . 39 ALA CA C 54.3 0.2 1 193 . 39 ALA CB C 20.7 0.2 1 194 . 39 ALA N N 127.4 0.2 1 195 . 40 THR C C 174.8 0.2 1 196 . 40 THR H H 8.53 0.01 1 197 . 40 THR HA H 4.51 0.05 1 198 . 40 THR CA C 61.5 0.2 1 199 . 40 THR CB C 70.7 0.2 1 200 . 40 THR N N 108.5 0.2 1 201 . 41 GLU C C 175.2 0.2 1 202 . 41 GLU H H 7.62 0.01 1 203 . 41 GLU HA H 4.84 0.05 1 204 . 41 GLU CA C 56.0 0.2 1 205 . 41 GLU CB C 34.7 0.2 1 206 . 41 GLU N N 121.6 0.2 1 207 . 42 MET H H 9.57 0.01 1 208 . 42 MET HA H 4.42 0.05 1 209 . 42 MET CA C 57.3 0.2 1 210 . 42 MET CB C 37.5 0.2 1 211 . 42 MET N N 126.5 0.2 1 212 . 43 THR C C 175.1 0.2 1 213 . 43 THR H H 8.19 0.01 1 214 . 43 THR CA C 59.0 0.2 1 215 . 43 THR CB C 70.3 0.2 1 216 . 43 THR N N 122.3 0.2 1 217 . 44 GLY HA2 H 4.42 0.01 1 218 . 44 GLY C C 177.8 0.2 1 219 . 44 GLY H H 8.79 0.01 1 220 . 44 GLY CA C 46.9 0.2 1 221 . 44 GLY N N 111.3 0.2 1 222 . 45 LYS C C 179.6 0.2 1 223 . 45 LYS H H 7.84 0.01 1 224 . 45 LYS HA H 4.21 0.05 1 225 . 45 LYS CA C 59.5 0.2 1 226 . 45 LYS CB C 33.3 0.2 1 227 . 45 LYS N N 117.3 0.2 1 228 . 46 ASN C C 177.3 0.2 1 229 . 46 ASN H H 7.54 0.01 1 230 . 46 ASN HA H 4.75 0.05 1 231 . 46 ASN CA C 56.1 0.2 1 232 . 46 ASN CB C 38.1 0.2 1 233 . 46 ASN N N 122.1 0.2 1 234 . 47 PHE C C 176.6 0.2 1 235 . 47 PHE H H 8.58 0.01 1 236 . 47 PHE HA H 5.02 0.05 1 237 . 47 PHE CA C 62.8 0.2 1 238 . 47 PHE CB C 39.9 0.2 1 239 . 47 PHE N N 126.1 0.2 1 240 . 48 ASP C C 178.8 0.2 1 241 . 48 ASP H H 8.11 0.01 1 242 . 48 ASP HA H 4.25 0.05 1 243 . 48 ASP CA C 57.8 0.2 1 244 . 48 ASP CB C 39.9 0.2 1 245 . 48 ASP N N 120.1 0.2 1 246 . 49 LYS C C 177.1 0.2 1 247 . 49 LYS H H 7.77 0.01 1 248 . 49 LYS HA H 3.97 0.05 1 249 . 49 LYS CA C 60.4 0.2 1 250 . 49 LYS CB C 32.8 0.2 1 251 . 49 LYS N N 119.9 0.2 1 252 . 50 TRP C C 176.9 0.2 1 253 . 50 TRP H H 7.96 0.01 1 254 . 50 TRP HA H 3.84 0.05 1 255 . 50 TRP CA C 58.9 0.2 1 256 . 50 TRP CB C 29.2 0.2 1 257 . 50 TRP N N 121.2 0.2 1 258 . 51 LEU H H 7.75 0.01 1 259 . 51 LEU HA H 3.39 0.05 1 260 . 51 LEU CA C 59.3 0.2 1 261 . 51 LEU CB C 42.5 0.2 1 262 . 51 LEU N N 114.1 0.2 1 263 . 52 LYS H H 9.32 0.01 1 264 . 52 LYS HA H 4.13 0.05 1 265 . 52 LYS CA C 60.6 0.2 1 266 . 52 LYS CB C 33.1 0.2 1 267 . 52 LYS N N 126.6 0.2 1 268 . 53 ASP C C 178.4 0.2 1 269 . 53 ASP H H 9.44 0.01 1 270 . 53 ASP HA H 4.32 0.05 1 271 . 53 ASP CA C 57.9 0.2 1 272 . 53 ASP CB C 40.0 0.2 1 273 . 53 ASP N N 125.1 0.2 1 274 . 54 ALA C C 177.6 0.2 1 275 . 54 ALA H H 7.54 0.01 1 276 . 54 ALA HA H 4.15 0.05 1 277 . 54 ALA CA C 52.9 0.2 1 278 . 54 ALA CB C 20.9 0.2 1 279 . 54 ALA N N 117.8 0.2 1 280 . 55 GLY HA2 H 3.79 0.01 1 281 . 55 GLY C C 174.7 0.2 1 282 . 55 GLY H H 7.79 0.01 1 283 . 55 GLY CA C 45.5 0.2 1 284 . 55 GLY N N 105.3 0.2 1 285 . 56 VAL C C 175.8 0.2 1 286 . 56 VAL H H 7.92 0.01 1 287 . 56 VAL HA H 3.79 0.05 1 288 . 56 VAL CA C 64.3 0.2 1 289 . 56 VAL CB C 33.4 0.2 1 290 . 56 VAL N N 119.0 0.2 1 291 . 57 LEU C C 174.7 0.2 1 292 . 57 LEU H H 6.62 0.01 1 293 . 57 LEU HA H 3.81 0.05 1 294 . 57 LEU CA C 55.2 0.2 1 295 . 57 LEU CB C 42.4 0.2 1 296 . 57 LEU N N 119.9 0.2 1 297 . 58 ASP C C 176.9 0.2 1 298 . 58 ASP H H 8.30 0.01 1 299 . 58 ASP HA H 4.59 0.05 1 300 . 58 ASP CA C 53.3 0.2 1 301 . 58 ASP CB C 42.1 0.2 1 302 . 58 ASP N N 127.0 0.2 1 303 . 59 ASN C C 173.9 0.2 1 304 . 59 ASN H H 8.59 0.01 1 305 . 59 ASN HA H 4.24 0.05 1 306 . 59 ASN CA C 56.1 0.2 1 307 . 59 ASN CB C 38.3 0.2 1 308 . 59 ASN N N 114.8 0.2 1 309 . 60 LYS C C 175.0 0.2 1 310 . 60 LYS H H 8.24 0.01 1 311 . 60 LYS HA H 4.33 0.05 1 312 . 60 LYS CA C 58.2 0.2 1 313 . 60 LYS CB C 35.0 0.2 1 314 . 60 LYS N N 119.4 0.2 1 315 . 61 ALA C C 177.3 0.2 1 316 . 61 ALA H H 9.02 0.01 1 317 . 61 ALA HA H 4.22 0.05 1 318 . 61 ALA CA C 54.7 0.2 1 319 . 61 ALA CB C 20.1 0.2 1 320 . 61 ALA N N 126.0 0.2 1 321 . 62 ILE C C 175.5 0.2 1 322 . 62 ILE H H 7.91 0.01 1 323 . 62 ILE HA H 4.63 0.05 1 324 . 62 ILE CA C 61.1 0.2 1 325 . 62 ILE CB C 38.8 0.2 1 326 . 62 ILE N N 116.0 0.2 1 327 . 63 THR C C 175.5 0.2 1 328 . 63 THR H H 7.60 0.01 1 329 . 63 THR HA H 4.83 0.05 1 330 . 63 THR CA C 59.3 0.2 1 331 . 63 THR CB C 72.7 0.2 1 332 . 63 THR N N 117.0 0.2 1 333 . 64 GLY C C 177.9 0.2 1 334 . 64 GLY H H 9.11 0.01 1 335 . 64 GLY CA C 46.2 0.2 1 336 . 64 GLY N N 108.3 0.2 1 337 . 65 THR C C 176.5 0.2 1 338 . 65 THR H H 7.82 0.01 1 339 . 65 THR CA C 66.5 0.2 1 340 . 65 THR CB C 69.2 0.2 1 341 . 65 THR N N 118.5 0.2 1 342 . 66 MET H H 7.43 0.01 1 343 . 66 MET HA H 4.09 0.05 1 344 . 66 MET CA C 59.9 0.2 1 345 . 66 MET CB C 35.5 0.2 1 346 . 66 MET N N 120.5 0.2 1 347 . 67 THR C C 173.1 0.2 1 348 . 67 THR H H 8.66 0.01 1 349 . 67 THR CA C 66.9 0.2 1 350 . 67 THR CB C 67.0 0.2 1 351 . 67 THR N N 111.8 0.2 1 352 . 68 GLY HA2 H 4.03 0.01 1 353 . 68 GLY C C 177.8 0.2 1 354 . 68 GLY H H 8.30 0.01 1 355 . 68 GLY HA3 H 4.03 0.01 1 356 . 68 GLY CA C 47.9 0.2 1 357 . 68 GLY N N 111.1 0.2 1 358 . 69 ILE C C 178.6 0.2 1 359 . 69 ILE H H 7.95 0.01 1 360 . 69 ILE HA H 3.86 0.05 1 361 . 69 ILE CA C 65.3 0.2 1 362 . 69 ILE CB C 38.8 0.2 1 363 . 69 ILE N N 123.7 0.2 1 364 . 70 ALA C C 178.4 0.2 1 365 . 70 ALA H H 7.53 0.01 1 366 . 70 ALA HA H 3.84 0.05 1 367 . 70 ALA CA C 55.9 0.2 1 368 . 70 ALA CB C 21.1 0.2 1 369 . 70 ALA N N 122.9 0.2 1 370 . 71 PHE H H 8.82 0.01 1 371 . 71 PHE HA H 3.81 0.05 1 372 . 71 PHE CA C 62.8 0.2 1 373 . 71 PHE CB C 40.6 0.2 1 374 . 71 PHE N N 118.0 0.2 1 375 . 72 SER C C 177.6 0.2 1 376 . 72 SER H H 8.34 0.01 1 377 . 72 SER HA H 4.04 0.05 1 378 . 72 SER CA C 62.0 0.2 1 379 . 72 SER N N 116.5 0.2 1 380 . 73 LYS C C 178.7 0.2 1 381 . 73 LYS H H 8.13 0.01 1 382 . 73 LYS HA H 4.45 0.05 1 383 . 73 LYS CA C 58.4 0.2 1 384 . 73 LYS CB C 33.1 0.2 1 385 . 73 LYS N N 122.8 0.2 1 386 . 74 VAL C C 177.8 0.2 1 387 . 74 VAL H H 7.18 0.01 1 388 . 74 VAL HA H 3.86 0.05 1 389 . 74 VAL CA C 65.6 0.2 1 390 . 74 VAL CB C 33.3 0.2 1 391 . 74 VAL N N 115.7 0.2 1 392 . 75 THR C C 176.5 0.2 1 393 . 75 THR H H 7.72 0.01 1 394 . 75 THR HA H 4.05 0.05 1 395 . 75 THR CA C 64.3 0.2 1 396 . 75 THR CB C 71.3 0.2 1 397 . 75 THR N N 107.3 0.2 1 398 . 76 GLY H H 8.09 0.01 1 399 . 76 GLY CA C 46.0 0.2 1 400 . 76 GLY N N 111.9 0.2 1 401 . 77 PRO C C 177.8 0.2 1 402 . 77 PRO HA H 4.47 0.05 1 403 . 77 PRO CA C 64.7 0.2 1 404 . 77 PRO CB C 32.6 0.2 1 405 . 78 LYS C C 178.3 0.2 1 406 . 78 LYS H H 7.84 0.01 1 407 . 78 LYS HA H 4.27 0.05 1 408 . 78 LYS CA C 59.5 0.2 1 409 . 78 LYS CB C 33.3 0.2 1 410 . 78 LYS N N 117.3 0.2 1 411 . 79 LYS C C 174.7 0.2 1 412 . 79 LYS H H 7.51 0.01 1 413 . 79 LYS HA H 4.16 0.05 1 414 . 79 LYS CA C 58.5 0.2 1 415 . 79 LYS CB C 30.8 0.2 1 416 . 79 LYS N N 109.9 0.2 1 417 . 80 LYS C C 173.9 0.2 1 418 . 80 LYS H H 7.20 0.01 1 419 . 80 LYS HA H 5.34 0.05 1 420 . 80 LYS CA C 55.9 0.2 1 421 . 80 LYS CB C 35.9 0.2 1 422 . 80 LYS N N 114.7 0.2 1 423 . 81 ALA C C 179.6 0.2 1 424 . 81 ALA H H 9.22 0.01 1 425 . 81 ALA CA C 50.9 0.2 1 426 . 81 ALA CB C 24.5 0.2 1 427 . 81 ALA N N 123.8 0.2 1 428 . 82 THR C C 177.0 0.2 1 429 . 82 THR H H 7.56 0.01 1 430 . 82 THR CA C 62.0 0.2 1 431 . 82 THR CB C 71.8 0.2 1 432 . 82 THR N N 122.3 0.2 1 433 . 83 PHE C C 177.0 0.2 1 434 . 83 PHE H H 9.38 0.01 1 435 . 83 PHE HA H 3.21 0.05 1 436 . 83 PHE CA C 62.5 0.2 1 437 . 83 PHE CB C 38.3 0.2 1 438 . 83 PHE N N 128.4 0.2 1 439 . 84 ASP H H 8.26 0.01 1 440 . 84 ASP HA H 3.99 0.05 1 441 . 84 ASP CA C 58.2 0.2 1 442 . 84 ASP CB C 41.1 0.2 1 443 . 84 ASP N N 118.2 0.2 1 444 . 85 GLU C C 178.3 0.2 1 445 . 85 GLU H H 7.69 0.01 1 446 . 85 GLU HA H 3.73 0.05 1 447 . 85 GLU CA C 59.5 0.2 1 448 . 85 GLU CB C 30.2 0.2 1 449 . 85 GLU N N 119.2 0.2 1 450 . 86 THR C C 178.9 0.2 1 451 . 86 THR H H 8.58 0.01 1 452 . 86 THR HA H 3.52 0.05 1 453 . 86 THR CA C 67.7 0.2 1 454 . 86 THR CB C 67.7 0.2 1 455 . 86 THR N N 119.2 0.2 1 456 . 87 LYS C C 176.0 0.2 1 457 . 87 LYS H H 8.46 0.01 1 458 . 87 LYS HA H 4.10 0.05 1 459 . 87 LYS CA C 59.0 0.2 1 460 . 87 LYS CB C 31.3 0.2 1 461 . 87 LYS N N 118.9 0.2 1 462 . 88 LYS C C 177.2 0.2 1 463 . 88 LYS H H 8.28 0.01 1 464 . 88 LYS CA C 59.1 0.2 1 465 . 88 LYS CB C 31.4 0.2 1 466 . 88 LYS N N 121.8 0.2 1 467 . 89 VAL C C 179.1 0.2 1 468 . 89 VAL H H 6.97 0.01 1 469 . 89 VAL HA H 4.19 0.05 1 470 . 89 VAL CA C 60.3 0.2 1 471 . 89 VAL CB C 32.7 0.2 1 472 . 89 VAL N N 117.1 0.2 1 473 . 90 LEU C C 173.9 0.2 1 474 . 90 LEU H H 8.26 0.01 1 475 . 90 LEU HA H 4.75 0.05 1 476 . 90 LEU CA C 52.9 0.2 1 477 . 90 LEU CB C 45.8 0.2 1 478 . 90 LEU N N 119.9 0.2 1 479 . 91 ALA C C 177.8 0.2 1 480 . 91 ALA H H 8.14 0.01 1 481 . 91 ALA HA H 4.30 0.05 1 482 . 91 ALA CA C 52.9 0.2 1 483 . 91 ALA CB C 19.7 0.2 1 484 . 91 ALA N N 123.6 0.2 1 485 . 92 PHE C C 179.8 0.2 1 486 . 92 PHE H H 8.10 0.01 1 487 . 92 PHE HA H 4.63 0.05 1 488 . 92 PHE CA C 58.4 0.2 1 489 . 92 PHE CB C 38.8 0.2 1 490 . 92 PHE N N 119.6 0.2 1 491 . 93 VAL C C 177.7 0.2 1 492 . 93 VAL H H 8.79 0.01 1 493 . 93 VAL HA H 3.92 0.05 1 494 . 93 VAL CA C 67.3 0.2 1 495 . 93 VAL CB C 31.9 0.2 1 496 . 93 VAL N N 123.1 0.2 1 497 . 94 ALA C C 178.9 0.2 1 498 . 94 ALA H H 8.44 0.01 1 499 . 94 ALA HA H 3.80 0.05 1 500 . 94 ALA CA C 56.0 0.2 1 501 . 94 ALA CB C 18.8 0.2 1 502 . 94 ALA N N 121.5 0.2 1 503 . 95 GLU C C 174.0 0.2 1 504 . 95 GLU H H 8.18 0.01 1 505 . 95 GLU HA H 3.90 0.05 1 506 . 95 GLU CA C 60.3 0.2 1 507 . 95 GLU CB C 30.2 0.2 1 508 . 95 GLU N N 118.2 0.2 1 509 . 96 ASP C C 176.0 0.2 1 510 . 96 ASP H H 8.01 0.01 1 511 . 96 ASP HA H 4.61 0.05 1 512 . 96 ASP CA C 58.5 0.2 1 513 . 96 ASP CB C 39.3 0.2 1 514 . 96 ASP N N 120.7 0.2 1 515 . 97 ARG C C 178.6 0.2 1 516 . 97 ARG H H 8.12 0.01 1 517 . 97 ARG CA C 58.4 0.2 1 518 . 97 ARG CB C 29.3 0.2 1 519 . 97 ARG N N 123.2 0.2 1 520 . 98 ALA H H 8.77 0.01 1 521 . 98 ALA HA H 4.58 0.05 1 522 . 98 ALA CA C 54.9 0.2 1 523 . 98 ALA CB C 18.8 0.2 1 524 . 98 ALA N N 122.7 0.2 1 525 . 99 ARG C C 178.6 0.2 1 526 . 99 ARG H H 7.91 0.01 1 527 . 99 ARG HA H 4.12 0.05 1 528 . 99 ARG CA C 60.0 0.2 1 529 . 99 ARG CB C 30.5 0.2 1 530 . 99 ARG N N 118.8 0.2 1 531 . 100 GLN C C 178.3 0.2 1 532 . 100 GLN H H 7.51 0.01 1 533 . 100 GLN HA H 4.37 0.05 1 534 . 100 GLN CA C 57.8 0.2 1 535 . 100 GLN CB C 30.0 0.2 1 536 . 100 GLN N N 115.9 0.2 1 537 . 101 SER C C 176.2 0.2 1 538 . 101 SER H H 9.23 0.01 1 539 . 101 SER HA H 4.25 0.05 1 540 . 101 SER CA C 59.8 0.2 1 541 . 101 SER CB C 64.8 0.2 1 542 . 101 SER N N 116.7 0.2 1 543 . 102 LYS C C 176.3 0.2 1 544 . 102 LYS H H 8.45 0.01 1 545 . 102 LYS HA H 4.00 0.05 1 546 . 102 LYS CA C 58.2 0.2 1 547 . 102 LYS CB C 29.2 0.2 1 548 . 102 LYS N N 116.3 0.2 1 549 . 103 LYS H H 7.99 0.01 1 550 . 103 LYS HA H 4.67 0.05 1 551 . 103 LYS CA C 55.2 0.2 1 552 . 103 LYS CB C 32.6 0.2 1 553 . 103 LYS N N 121.3 0.2 1 554 . 104 PRO C C 177.9 0.2 1 555 . 104 PRO CA C 63.1 0.2 1 556 . 104 PRO CB C 33.1 0.2 1 557 . 105 ILE C C 178.1 0.2 1 558 . 105 ILE H H 8.26 0.01 1 559 . 105 ILE HA H 3.30 0.05 1 560 . 105 ILE CA C 66.5 0.2 1 561 . 105 ILE CB C 38.3 0.2 1 562 . 105 ILE N N 123.4 0.2 1 563 . 106 GLN C C 177.2 0.2 1 564 . 106 GLN H H 8.82 0.01 1 565 . 106 GLN HA H 3.62 0.05 1 566 . 106 GLN CA C 58.5 0.2 1 567 . 106 GLN CB C 29.7 0.2 1 568 . 106 GLN N N 117.7 0.2 1 569 . 107 ASP H H 6.99 0.01 1 570 . 107 ASP HA H 4.34 0.05 1 571 . 107 ASP CA C 57.8 0.2 1 572 . 107 ASP CB C 40.6 0.2 1 573 . 107 ASP N N 117.0 0.2 1 574 . 108 GLU C C 179.9 0.2 1 575 . 108 GLU H H 7.34 0.01 1 576 . 108 GLU HA H 4.79 0.05 1 577 . 108 GLU CA C 57.8 0.2 1 578 . 108 GLU CB C 29.1 0.2 1 579 . 108 GLU N N 118.6 0.2 1 580 . 109 LEU C C 178.5 0.2 1 581 . 109 LEU H H 8.73 0.01 1 582 . 109 LEU HA H 3.96 0.05 1 583 . 109 LEU CA C 58.1 0.2 1 584 . 109 LEU CB C 41.6 0.2 1 585 . 109 LEU N N 122.2 0.2 1 586 . 110 ASP C C 178.0 0.2 1 587 . 110 ASP H H 8.65 0.01 1 588 . 110 ASP HA H 4.32 0.05 1 589 . 110 ASP CA C 57.3 0.2 1 590 . 110 ASP CB C 40.2 0.2 1 591 . 110 ASP N N 120.5 0.2 1 592 . 111 ALA H H 7.30 0.01 1 593 . 111 ALA HA H 4.18 0.05 1 594 . 111 ALA CA C 55.2 0.2 1 595 . 111 ALA CB C 18.6 0.2 1 596 . 111 ALA N N 120.2 0.2 1 597 . 112 ILE C C 178.3 0.2 1 598 . 112 ILE H H 7.38 0.01 1 599 . 112 ILE HA H 3.64 0.05 1 600 . 112 ILE CA C 65.5 0.2 1 601 . 112 ILE CB C 39.7 0.2 1 602 . 112 ILE N N 118.0 0.2 1 603 . 113 THR C C 175.5 0.2 1 604 . 113 THR H H 9.28 0.01 1 605 . 113 THR HA H 3.90 0.05 1 606 . 113 THR CA C 66.2 0.2 1 607 . 113 THR CB C 68.9 0.2 1 608 . 113 THR N N 112.3 0.2 1 609 . 114 GLU C C 179.1 0.2 1 610 . 114 GLU H H 8.39 0.01 1 611 . 114 GLU HA H 4.13 0.05 1 612 . 114 GLU CA C 59.8 0.2 1 613 . 114 GLU CB C 29.7 0.2 1 614 . 114 GLU N N 122.2 0.2 1 615 . 115 LYS H H 6.75 0.01 1 616 . 115 LYS HA H 4.07 0.05 1 617 . 115 LYS CA C 59.5 0.2 1 618 . 115 LYS CB C 33.5 0.2 1 619 . 115 LYS N N 116.0 0.2 1 620 . 116 LEU C C 179.1 0.2 1 621 . 116 LEU H H 7.75 0.01 1 622 . 116 LEU HA H 3.70 0.05 1 623 . 116 LEU CA C 57.9 0.2 1 624 . 116 LEU CB C 42.3 0.2 1 625 . 116 LEU N N 119.0 0.2 1 626 . 117 ALA C C 178.1 0.2 1 627 . 117 ALA H H 8.59 0.01 1 628 . 117 ALA HA H 4.08 0.05 1 629 . 117 ALA CA C 54.7 0.2 1 630 . 117 ALA CB C 19.7 0.2 1 631 . 117 ALA N N 118.7 0.2 1 632 . 118 LYS C C 176.6 0.2 1 633 . 118 LYS H H 6.84 0.01 1 634 . 118 LYS HA H 4.43 0.05 1 635 . 118 LYS CA C 56.2 0.2 1 636 . 118 LYS CB C 34.2 0.2 1 637 . 118 LYS N N 111.6 0.2 1 638 . 119 LEU C C 177.7 0.2 1 639 . 119 LEU H H 6.98 0.01 1 640 . 119 LEU HA H 4.48 0.05 1 641 . 119 LEU CA C 56.0 0.2 1 642 . 119 LEU CB C 42.8 0.2 1 643 . 119 LEU N N 123.1 0.2 1 644 . 120 GLU C C 175.5 0.2 1 645 . 120 GLU H H 9.04 0.01 1 646 . 120 GLU HA H 4.29 0.05 1 647 . 120 GLU CA C 57.4 0.2 1 648 . 120 GLU CB C 31.2 0.2 1 649 . 120 GLU N N 130.7 0.2 1 650 . 121 ALA H H 8.39 0.01 1 651 . 121 ALA CA C 50.8 0.2 1 652 . 121 ALA CB C 19.8 0.2 1 653 . 121 ALA N N 122.3 0.2 1 654 . 122 PRO C C 177.6 0.2 1 655 . 122 PRO HA H 5.72 0.05 1 656 . 123 SER C C 175.2 0.2 1 657 . 123 SER H H 8.13 0.01 1 658 . 123 SER HA H 4.40 0.05 1 659 . 123 SER CA C 62.1 0.2 1 660 . 123 SER CB C 65.8 0.2 1 661 . 123 SER N N 122.8 0.2 1 662 . 124 VAL C C 175.0 0.2 1 663 . 124 VAL H H 8.24 0.01 1 664 . 124 VAL HA H 4.31 0.05 1 665 . 124 VAL CA C 62.8 0.2 1 666 . 124 VAL CB C 33.8 0.2 1 667 . 124 VAL N N 116.3 0.2 1 668 . 125 GLY HA2 H 3.97 0.01 1 669 . 125 GLY C C 175.0 0.2 1 670 . 125 GLY H H 8.41 0.01 1 671 . 125 GLY CA C 46.0 0.2 1 672 . 125 GLY N N 123.3 0.2 1 673 . 126 GLY HA2 H 4.23 0.01 1 674 . 126 GLY C C 173.9 0.2 1 675 . 126 GLY H H 8.27 0.01 1 676 . 126 GLY HA3 H 3.94 0.01 1 677 . 126 GLY CA C 46.0 0.2 1 678 . 126 GLY N N 109.3 0.2 1 679 . 127 ALA C C 178.2 0.2 1 680 . 127 ALA H H 8.05 0.01 1 681 . 127 ALA HA H 4.25 0.05 1 682 . 127 ALA CA C 53.0 0.2 1 683 . 127 ALA CB C 19.7 0.2 1 684 . 127 ALA N N 123.7 0.2 1 685 . 128 ALA C C 174.8 0.2 1 686 . 128 ALA H H 8.35 0.01 1 687 . 128 ALA HA H 4.20 0.05 1 688 . 128 ALA CA C 53.2 0.2 1 689 . 128 ALA CB C 19.7 0.2 1 690 . 128 ALA N N 118.7 0.2 1 691 . 129 LYS C C 177.5 0.2 1 692 . 129 LYS H H 8.19 0.01 1 693 . 129 LYS HA H 4.29 0.05 1 694 . 129 LYS CA C 57.0 0.2 1 695 . 129 LYS CB C 33.4 0.2 1 696 . 129 LYS N N 120.8 0.2 1 697 . 130 ALA H H 8.48 0.01 1 698 . 130 ALA CA C 45.8 0.2 1 699 . 130 ALA N N 110.2 0.2 1 700 . 131 ASN CA C 56.2 0.2 1 701 . 131 ASN CB C 39.9 0.2 1 702 . 132 ALA C C 174.4 0.2 1 703 . 132 ALA H H 8.12 0.01 1 704 . 132 ALA HA H 4.49 0.05 1 705 . 132 ALA CA C 53.0 0.2 1 706 . 132 ALA CB C 19.6 0.2 1 707 . 132 ALA N N 119.6 0.2 1 708 . 133 ALA C C 176.0 0.2 1 709 . 133 ALA H H 8.18 0.01 1 710 . 133 ALA HA H 2.31 0.05 1 711 . 133 ALA CA C 53.1 0.2 1 712 . 133 ALA CB C 19.7 0.2 1 713 . 133 ALA N N 122.8 0.2 1 714 . 134 GLY HA2 H 4.40 0.01 1 715 . 134 GLY H H 8.13 0.01 1 716 . 134 GLY CA C 45.9 0.2 1 717 . 134 GLY N N 123.0 0.2 1 718 . 135 VAL C C 175.1 0.2 1 719 . 135 VAL H H 7.75 0.01 1 720 . 135 VAL HA H 4.07 0.05 1 721 . 135 VAL CA C 62.8 0.2 1 722 . 135 VAL CB C 33.1 0.2 1 723 . 135 VAL N N 119.7 0.2 1 724 . 136 TYR H H 7.76 0.01 1 725 . 136 TYR CA C 59.6 0.2 1 726 . 136 TYR CB C 40.2 0.2 1 727 . 136 TYR N N 128.9 0.2 1 728 . 137 SER C C 174.4 0.2 1 729 . 137 SER HA H 3.81 0.05 1 730 . 137 SER CA C 59.2 0.2 1 731 . 137 SER CB C 62.1 0.2 1 732 . 138 ARG C C 175.4 0.2 1 733 . 138 ARG H H 8.18 0.01 1 734 . 138 ARG HA H 5.07 0.05 1 735 . 138 ARG CA C 53.3 0.2 1 736 . 138 ARG CB C 31.1 0.2 1 737 . 138 ARG N N 122.8 0.2 1 738 . 139 LEU C C 177.9 0.2 1 739 . 139 LEU H H 8.21 0.01 1 740 . 139 LEU HA H 4.30 0.05 1 741 . 139 LEU CA C 56.1 0.2 1 742 . 139 LEU CB C 42.7 0.2 1 743 . 139 LEU N N 122.8 0.2 1 744 . 140 THR H H 7.99 0.01 1 745 . 140 THR HA H 4.28 0.05 1 746 . 140 THR CA C 62.3 0.2 1 747 . 140 THR CB C 70.2 0.2 1 748 . 140 THR N N 113.8 0.2 1 749 . 141 ASP CA C 54.7 0.2 1 750 . 141 ASP CB C 41.6 0.2 1 751 . 142 HIS C C 176.0 0.2 1 752 . 142 HIS H H 8.40 0.01 1 753 . 142 HIS HA H 4.63 0.05 1 754 . 142 HIS CA C 57.0 0.2 1 755 . 142 HIS CB C 30.3 0.2 1 756 . 142 HIS N N 120.8 0.2 1 757 . 143 THR C C 175.0 0.2 1 758 . 143 THR H H 8.17 0.01 1 759 . 143 THR CA C 63.5 0.2 1 760 . 143 THR CB C 70.1 0.2 1 761 . 143 THR N N 115.0 0.2 1 762 . 144 LYS C C 176.4 0.2 1 763 . 144 LYS H H 8.09 0.01 1 764 . 144 LYS HA H 3.22 0.05 1 765 . 144 LYS CA C 56.9 0.2 1 766 . 144 LYS CB C 33.3 0.2 1 767 . 144 LYS N N 123.2 0.2 1 768 . 145 TYR C C 177.1 0.2 1 769 . 145 TYR H H 8.14 0.01 1 770 . 145 TYR HA H 4.47 0.05 1 771 . 145 TYR CA C 58.4 0.2 1 772 . 145 TYR CB C 33.3 0.2 1 773 . 145 TYR N N 121.5 0.2 1 774 . 146 THR H H 8.43 0.01 1 775 . 146 THR HA H 4.45 0.05 1 776 . 146 THR CA C 59.0 0.2 1 777 . 146 THR CB C 64.4 0.2 1 778 . 146 THR N N 117.1 0.2 1 779 . 147 GLY H H 8.43 0.01 1 780 . 147 GLY CA C 45.8 0.2 1 781 . 147 GLY N N 111.1 0.2 1 782 . 148 ALA C C 177.5 0.2 1 783 . 148 ALA HA H 3.76 0.05 1 784 . 148 ALA CA C 52.6 0.2 1 785 . 148 ALA CB C 19.8 0.2 1 786 . 149 HIS C C 176.0 0.2 1 787 . 149 HIS H H 8.06 0.01 1 788 . 149 HIS HA H 4.23 0.05 1 789 . 149 HIS CA C 56.7 0.2 1 790 . 149 HIS CB C 33.3 0.2 1 791 . 149 HIS N N 123.0 0.2 1 792 . 150 LYS H H 8.29 0.01 1 793 . 150 LYS CA C 56.7 0.2 1 794 . 150 LYS CB C 39.5 0.2 1 795 . 150 LYS N N 119.8 0.2 1 796 . 151 GLU C C 178.7 0.2 1 797 . 151 GLU HA H 5.34 0.05 1 798 . 151 GLU CA C 51.1 0.2 1 799 . 152 ARG H H 9.26 0.01 1 800 . 152 ARG HA H 4.87 0.05 1 801 . 152 ARG CA C 61.9 0.2 1 802 . 152 ARG CB C 24.5 0.2 1 803 . 152 ARG N N 113.7 0.2 1 804 . 153 PHE H H 8.14 0.01 1 805 . 153 PHE CA C 55.4 0.2 1 806 . 153 PHE CB C 41.5 0.2 1 807 . 153 PHE N N 126.3 0.2 1 808 . 154 ASP C C 176.3 0.2 1 809 . 154 ASP CA C 54.5 0.2 1 810 . 154 ASP CB C 41.5 0.2 1 811 . 155 ALA C C 178.5 0.2 1 812 . 155 ALA H H 8.18 0.01 1 813 . 155 ALA HA H 4.29 0.05 1 814 . 155 ALA CA C 53.6 0.2 1 815 . 155 ALA CB C 19.7 0.2 1 816 . 155 ALA N N 124.6 0.2 1 817 . 156 GLU C C 175.4 0.2 1 818 . 156 GLU H H 8.33 0.01 1 819 . 156 GLU HA H 4.25 0.05 1 820 . 156 GLU CA C 56.7 0.2 1 821 . 156 GLU CB C 30.5 0.2 1 822 . 156 GLU N N 118.9 0.2 1 823 . 157 GLY HA2 H 2.77 0.01 1 824 . 157 GLY H H 8.23 0.01 1 825 . 157 GLY HA3 H 2.76 0.01 1 826 . 157 GLY CA C 45.7 0.2 1 827 . 157 GLY N N 121.6 0.2 1 828 . 158 LYS H H 8.40 0.01 1 829 . 158 LYS CA C 57.0 0.2 1 830 . 158 LYS CB C 30.3 0.2 1 831 . 158 LYS N N 120.8 0.2 1 832 . 159 GLY H H 8.31 0.01 1 833 . 159 GLY CA C 46.0 0.2 1 834 . 159 GLY N N 111.1 0.2 1 835 . 160 LYS H H 7.82 0.01 1 836 . 160 LYS CA C 57.9 0.2 1 837 . 160 LYS CB C 34.3 0.2 1 838 . 160 LYS N N 127.2 0.2 1 839 . 161 GLY HA2 H 4.03 0.01 1 840 . 161 GLY C C 176.0 0.2 1 841 . 161 GLY CA C 45.8 0.2 1 842 . 162 LYS C C 176.8 0.2 1 843 . 162 LYS H H 8.12 0.01 1 844 . 162 LYS HA H 4.44 0.05 1 845 . 162 LYS CA C 56.9 0.2 1 846 . 162 LYS CB C 33.3 0.2 1 847 . 162 LYS N N 123.2 0.2 1 848 . 163 SER C C 176.0 0.2 1 849 . 163 SER H H 8.47 0.01 1 850 . 163 SER HA H 4.44 0.05 1 851 . 163 SER CA C 58.5 0.2 1 852 . 163 SER CB C 63.1 0.2 1 853 . 163 SER N N 117.2 0.2 1 854 . 164 GLY C C 176.0 0.2 1 855 . 164 GLY H H 8.44 0.01 1 856 . 164 GLY CA C 45.7 0.2 1 857 . 164 GLY N N 123.3 0.2 1 858 . 165 ARG C C 176.3 0.2 1 859 . 165 ARG H H 8.27 0.01 1 860 . 165 ARG HA H 4.34 0.05 1 861 . 165 ARG CA C 56.6 0.2 1 862 . 165 ARG CB C 31.4 0.2 1 863 . 165 ARG N N 121.6 0.2 1 864 . 166 ALA C C 177.6 0.2 1 865 . 166 ALA H H 8.44 0.01 1 866 . 166 ALA HA H 4.34 0.05 1 867 . 166 ALA CA C 52.9 0.2 1 868 . 166 ALA CB C 19.7 0.2 1 869 . 166 ALA N N 125.7 0.2 1 870 . 167 ASP C C 176.8 0.2 1 871 . 167 ASP H H 8.36 0.01 1 872 . 167 ASP HA H 4.69 0.05 1 873 . 167 ASP CA C 54.7 0.2 1 874 . 167 ASP CB C 41.6 0.2 1 875 . 167 ASP N N 119.9 0.2 1 876 . 168 THR C C 176.4 0.2 1 877 . 168 THR H H 8.11 0.01 1 878 . 168 THR HA H 4.66 0.05 1 879 . 168 THR CA C 62.2 0.2 1 880 . 168 THR CB C 70.3 0.2 1 881 . 168 THR N N 114.1 0.2 1 882 . 169 THR C C 176.6 0.2 1 883 . 169 THR H H 8.13 0.01 1 884 . 169 THR CA C 62.3 0.2 1 885 . 169 THR CB C 70.4 0.2 1 886 . 169 THR N N 116.1 0.2 1 887 . 170 GLU C C 176.4 0.2 1 888 . 170 GLU H H 8.50 0.01 1 889 . 170 GLU HA H 4.29 0.05 1 890 . 170 GLU CA C 57.1 0.2 1 891 . 170 GLU CB C 30.7 0.2 1 892 . 170 GLU N N 122.1 0.2 1 893 . 171 ASN C C 175.8 0.2 1 894 . 171 ASN H H 8.50 0.01 1 895 . 171 ASN HA H 4.81 0.05 1 896 . 171 ASN CA C 53.7 0.2 1 897 . 171 ASN CB C 39.3 0.2 1 898 . 171 ASN N N 120.2 0.2 1 899 . 172 THR C C 175.5 0.2 1 900 . 172 THR H H 8.16 0.01 1 901 . 172 THR HA H 4.78 0.05 1 902 . 172 THR CA C 62.8 0.2 1 903 . 172 THR CB C 70.2 0.2 1 904 . 172 THR N N 114.3 0.2 1 905 . 173 GLY HA2 H 4.28 0.01 1 906 . 173 GLY C C 177.6 0.2 1 907 . 173 GLY H H 8.39 0.01 1 908 . 173 GLY HA3 H 3.93 0.01 1 909 . 173 GLY CA C 45.8 0.2 1 910 . 173 GLY N N 111.0 0.2 1 911 . 174 TYR C C 176.1 0.2 1 912 . 174 TYR H H 8.16 0.01 1 913 . 174 TYR HA H 3.75 0.05 1 914 . 174 TYR CA C 53.1 0.2 1 915 . 174 TYR CB C 39.0 0.2 1 916 . 174 TYR N N 122.8 0.2 1 917 . 175 VAL C C 176.4 0.2 1 918 . 175 VAL H H 8.05 0.01 1 919 . 175 VAL HA H 4.04 0.05 1 920 . 175 VAL CA C 62.9 0.2 1 921 . 175 VAL CB C 33.3 0.2 1 922 . 175 VAL N N 123.3 0.2 1 923 . 176 GLY HA2 H 4.04 0.01 1 924 . 176 GLY C C 173.9 0.2 1 925 . 176 GLY H H 7.94 0.01 1 926 . 176 GLY HA3 H 3.83 0.01 1 927 . 176 GLY CA C 45.7 0.2 1 928 . 176 GLY N N 112.0 0.2 1 929 . 177 ALA C C 177.9 0.2 1 930 . 177 ALA H H 8.14 0.01 1 931 . 177 ALA HA H 4.25 0.05 1 932 . 177 ALA CA C 52.9 0.2 1 933 . 177 ALA CB C 19.7 0.2 1 934 . 177 ALA N N 123.6 0.2 1 935 . 178 TYR H H 8.36 0.01 1 936 . 178 TYR HA H 4.66 0.05 1 937 . 178 TYR CA C 53.7 0.2 1 938 . 178 TYR CB C 39.2 0.2 1 939 . 178 TYR N N 118.2 0.2 1 940 . 179 LYS C C 177.9 0.2 1 941 . 179 LYS H H 8.31 0.01 1 942 . 179 LYS HA H 4.82 0.05 1 943 . 179 LYS CB C 33.3 0.2 1 944 . 179 LYS N N 122.0 0.2 1 945 . 180 ASN C C 177.6 0.2 1 946 . 180 ASN H H 8.26 0.01 1 947 . 180 ASN HA H 3.30 0.05 1 948 . 180 ASN CA C 58.4 0.2 1 949 . 180 ASN CB C 39.2 0.2 1 950 . 180 ASN N N 123.4 0.2 1 951 . 181 LYS C C 176.7 0.2 1 952 . 181 LYS H H 8.13 0.01 1 953 . 181 LYS CA C 57.5 0.2 1 954 . 181 LYS CB C 33.3 0.2 1 955 . 181 LYS N N 122.8 0.2 1 956 . 182 ASP C C 176.7 0.2 1 957 . 182 ASP H H 8.33 0.01 1 958 . 182 ASP HA H 4.61 0.05 1 959 . 182 ASP CA C 55.3 0.2 1 960 . 182 ASP CB C 41.7 0.2 1 961 . 182 ASP N N 121.1 0.2 1 962 . 183 SER C C 174.8 0.2 1 963 . 183 SER H H 8.10 0.01 1 964 . 183 SER HA H 4.36 0.05 1 965 . 183 SER CA C 59.2 0.2 1 966 . 183 SER CB C 64.2 0.2 1 967 . 183 SER N N 115.5 0.2 1 968 . 184 TYR C C 176.3 0.2 1 969 . 184 TYR H H 8.15 0.01 1 970 . 184 TYR HA H 5.13 0.05 1 971 . 184 TYR CA C 53.1 0.2 1 972 . 184 TYR CB C 33.1 0.2 1 973 . 184 TYR N N 122.5 0.2 1 974 . 185 ASP C C 176.0 0.2 1 975 . 185 ASP H H 8.26 0.01 1 976 . 185 ASP HA H 3.30 0.05 1 977 . 185 ASP CA C 58.4 0.2 1 978 . 185 ASP CB C 39.2 0.2 1 979 . 185 ASP N N 123.7 0.2 1 980 . 186 LYS C C 176.1 0.2 1 981 . 186 LYS H H 8.28 0.01 1 982 . 186 LYS HA H 4.47 0.05 1 983 . 186 LYS CA C 58.3 0.2 1 984 . 186 LYS CB C 39.1 0.2 1 985 . 186 LYS N N 121.8 0.2 1 986 . 187 THR C C 174.5 0.2 1 987 . 187 THR H H 8.10 0.01 1 988 . 187 THR HA H 4.41 0.05 1 989 . 187 THR CA C 58.6 0.2 1 990 . 187 THR CB C 64.4 0.2 1 991 . 187 THR N N 117.9 0.2 1 992 . 188 HIS H H 8.30 0.01 1 993 . 188 HIS CA C 56.7 0.2 1 994 . 188 HIS CB C 31.1 0.2 1 995 . 188 HIS N N 123.2 0.2 1 996 . 189 GLY H H 8.31 0.01 1 997 . 189 GLY CA C 46.0 0.2 1 998 . 189 GLY N N 111.1 0.2 1 999 . 190 LYS H H 7.82 0.01 1 1000 . 190 LYS CA C 57.9 0.2 1 1001 . 190 LYS CB C 34.3 0.2 1 1002 . 190 LYS N N 127.2 0.2 1 stop_ save_