data_4834 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone (1H, 15N, 13C) Resonance Assignments of a 21 kDa construct of S. aureus Peptide Deformylase ; _BMRB_accession_number 4834 _BMRB_flat_file_name bmr4834.str _Entry_type original _Submission_date 2000-09-18 _Accession_date 2000-09-19 _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 Scahill Terrence A. . 2 Kloosterman David A. . 3 Cialdella Joyce I. . 4 Deibel Martin R. Jr. 5 Marshall Vincent P. . 6 Yem Anthony W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 610 "13C chemical shifts" 509 "15N chemical shifts" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-14 original author . stop_ _Original_release_date 2001-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone (1H, 15N, 13C) resonance assignments of a 21 kDa construct of S. aureus peptide deformylase ; _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 Scahill Terrence A. . 2 Kloosterman David A. . 3 Cialdella Joyce I. . 4 Deibel Martin R. Jr. 5 Marshall Vincent P. . 6 Yem Anthony W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 81 _Page_last 82 _Year 2001 _Details . loop_ _Keyword antibiotics 'drug discovery' 'peptide deformylase' pdf 'NMR assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_pdf _Saveframe_category molecular_system _Mol_system_name 'S. aureus peptide deformylase' _Abbreviation_common pdf _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label pdf $pdf 'ZN 2+' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'peptide deformylase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_pdf _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Staphylococcal aureus peptide deformylase' _Abbreviation_common 'S. aureus pdf' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; MLTMKDIIRDGHPTLRQKAA ELELPLTKEEKETLIAMREF LVNSQDEEIAKRYGLRSGVG LAAPQINISKRMIAVLIPDD GSGKSYDYMLVNPKIVSHSV QEAYLPTGEGCLSVDDNVAG LVHRHNRITIKAKDIEGNDI QLRLKGYPAIVFQHEIDHLN GVMFYDHIDKDHPLQPHTDA VEVHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 THR 4 MET 5 LYS 6 ASP 7 ILE 8 ILE 9 ARG 10 ASP 11 GLY 12 HIS 13 PRO 14 THR 15 LEU 16 ARG 17 GLN 18 LYS 19 ALA 20 ALA 21 GLU 22 LEU 23 GLU 24 LEU 25 PRO 26 LEU 27 THR 28 LYS 29 GLU 30 GLU 31 LYS 32 GLU 33 THR 34 LEU 35 ILE 36 ALA 37 MET 38 ARG 39 GLU 40 PHE 41 LEU 42 VAL 43 ASN 44 SER 45 GLN 46 ASP 47 GLU 48 GLU 49 ILE 50 ALA 51 LYS 52 ARG 53 TYR 54 GLY 55 LEU 56 ARG 57 SER 58 GLY 59 VAL 60 GLY 61 LEU 62 ALA 63 ALA 64 PRO 65 GLN 66 ILE 67 ASN 68 ILE 69 SER 70 LYS 71 ARG 72 MET 73 ILE 74 ALA 75 VAL 76 LEU 77 ILE 78 PRO 79 ASP 80 ASP 81 GLY 82 SER 83 GLY 84 LYS 85 SER 86 TYR 87 ASP 88 TYR 89 MET 90 LEU 91 VAL 92 ASN 93 PRO 94 LYS 95 ILE 96 VAL 97 SER 98 HIS 99 SER 100 VAL 101 GLN 102 GLU 103 ALA 104 TYR 105 LEU 106 PRO 107 THR 108 GLY 109 GLU 110 GLY 111 CYS 112 LEU 113 SER 114 VAL 115 ASP 116 ASP 117 ASN 118 VAL 119 ALA 120 GLY 121 LEU 122 VAL 123 HIS 124 ARG 125 HIS 126 ASN 127 ARG 128 ILE 129 THR 130 ILE 131 LYS 132 ALA 133 LYS 134 ASP 135 ILE 136 GLU 137 GLY 138 ASN 139 ASP 140 ILE 141 GLN 142 LEU 143 ARG 144 LEU 145 LYS 146 GLY 147 TYR 148 PRO 149 ALA 150 ILE 151 VAL 152 PHE 153 GLN 154 HIS 155 GLU 156 ILE 157 ASP 158 HIS 159 LEU 160 ASN 161 GLY 162 VAL 163 MET 164 PHE 165 TYR 166 ASP 167 HIS 168 ILE 169 ASP 170 LYS 171 ASP 172 HIS 173 PRO 174 LEU 175 GLN 176 PRO 177 HIS 178 THR 179 ASP 180 ALA 181 VAL 182 GLU 183 VAL 184 HIS 185 HIS 186 HIS 187 HIS 188 HIS 189 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1LM4 "Structure Of Peptide Deformylase From Staphylococcus Aureus At 1.45 A" 96.83 194 98.91 99.45 1.43e-126 PDB 1LQW "Crystal Structure Of S.Aureus Peptide Deformylase" 96.83 183 99.45 100.00 4.50e-129 PDB 1Q1Y "Crystal Structures Of Peptide Deformylase From Staphylococcus Aureus Complexed With Actinonin" 101.06 191 98.43 98.43 5.18e-131 PDB 2AI9 "S.Aureus Polypeptide Deformylase" 96.83 183 99.45 100.00 4.50e-129 PDB 3U7K "Crystal Structures Of The Staphylococcus Aureus Peptide Deformylase In Complex With Two Classes Of New Inhibitors" 101.06 191 98.43 98.43 5.18e-131 PDB 3U7L "Crystal Structures Of The Staphylococcus Aureus Peptide Deformylase In Complex With Two Classes Of New Inhibitors" 101.06 191 98.43 98.43 5.18e-131 PDB 3U7M "Crystal Structures Of The Staphylococcus Aureus Peptide Deformylase In Complex With Two Classes Of New Inhibitors" 101.06 191 98.43 98.43 5.18e-131 PDB 3U7N "Crystal Structures Of The Staphylococcus Aureus Peptide Deformylase In Complex With Two Classes Of New Inhibitors" 101.06 191 98.43 98.43 5.18e-131 DBJ BAB42188 "pdf1 [Staphylococcus aureus subsp. aureus N315]" 96.83 183 99.45 100.00 4.50e-129 DBJ BAB57253 "formylmethionine deformylase homolog [Staphylococcus aureus subsp. aureus Mu50]" 96.83 183 99.45 100.00 4.50e-129 DBJ BAB94839 "pdf1 [Staphylococcus aureus subsp. aureus MW2]" 96.83 183 100.00 100.00 1.15e-129 DBJ BAF67229 "polypeptide deformylase 2 [Staphylococcus aureus subsp. aureus str. Newman]" 96.83 183 100.00 100.00 1.15e-129 DBJ BAF77966 "formylmethionine deformylase homolog [Staphylococcus aureus subsp. aureus Mu3]" 96.83 183 99.45 100.00 4.50e-129 EMBL CAG40067 "putative polypeptide deformylase 2 [Staphylococcus aureus subsp. aureus MRSA252]" 96.83 183 100.00 100.00 1.15e-129 EMBL CAG42800 "putative polypeptide deformylase 2 [Staphylococcus aureus subsp. aureus MSSA476]" 96.83 183 100.00 100.00 1.15e-129 EMBL CAI80645 "peptide deformylase [Staphylococcus aureus RF122]" 96.83 183 100.00 100.00 1.15e-129 EMBL CAQ49513 "peptide deformylase [Staphylococcus aureus subsp. aureus ST398]" 96.83 183 99.45 99.45 3.31e-129 EMBL CBI48965 "putative polypeptide deformylase 2 [Staphylococcus aureus subsp. aureus TW20]" 96.83 183 100.00 100.00 1.15e-129 GB AAG02249 "peptide deformylase Pdf1 [Staphylococcus aureus]" 96.83 183 99.45 100.00 4.50e-129 GB AAW37980 "polypeptide deformylase [Staphylococcus aureus subsp. aureus COL]" 96.83 183 100.00 100.00 1.15e-129 GB ABD21929 "peptide deformylase [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 96.83 183 100.00 100.00 1.15e-129 GB ABD30158 "polypeptide deformylase [Staphylococcus aureus subsp. aureus NCTC 8325]" 96.83 183 100.00 100.00 1.15e-129 GB ABQ48951 "peptide deformylase [Staphylococcus aureus subsp. aureus JH9]" 96.83 183 99.45 100.00 4.50e-129 REF NP_371615 "peptide deformylase [Staphylococcus aureus subsp. aureus Mu50]" 96.83 183 99.45 100.00 4.50e-129 REF NP_374210 "peptide deformylase [Staphylococcus aureus subsp. aureus N315]" 96.83 183 99.45 100.00 4.50e-129 REF NP_645791 "peptide deformylase [Staphylococcus aureus subsp. aureus MW2]" 96.83 183 100.00 100.00 1.15e-129 REF WP_000957034 "peptide deformylase [Staphylococcus aureus]" 96.83 183 99.45 99.45 3.31e-129 REF WP_000957036 "peptide deformylase [Staphylococcus aureus]" 96.83 183 100.00 100.00 1.15e-129 SP P68825 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase [Staphylococcus aureus subsp. aureus Mu50]" 96.83 183 99.45 100.00 4.50e-129 SP P68826 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase [Staphylococcus aureus]" 96.83 183 99.45 100.00 4.50e-129 SP P99077 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase [Staphylococcus aureus subsp. aureus N315]" 96.83 183 99.45 100.00 4.50e-129 SP Q5HGZ3 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase [Staphylococcus aureus subsp. aureus COL]" 96.83 183 100.00 100.00 1.15e-129 SP Q6GAC3 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase [Staphylococcus aureus subsp. aureus MSSA47" 96.83 183 100.00 100.00 1.15e-129 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:20:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $pdf . 1280 Bacteria . Staphylococcus aureus 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 $pdf 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $pdf . mM 0.3 1.0 '[95% 13C; 90% 15N]' $ZN . mM 0.6 2.0 . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'visualization and resonance assignments' stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Task 'visualization and resonance assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CBCACONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_NHCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name NHCACB _Sample_label $sample_1 save_ save_HBHACONH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name NHCACB _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _BMRB_pulse_sequence_accession_number . _Details 'The HNCA, HNCOCA, CBCACONH, HNCACB, HBHACONH were gradient-enhanced experiments' save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.4 0.2 n/a temperature 310 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_ _Experiment_label '1H-15N HSQC' '1H-15N NOESY' HNCA HN(CO)CA HNCO CBCACONH NHCACB HBHACONH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name pdf _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 HA H 3.85 0.02 1 2 . 1 MET HB2 H 1.89 0.02 1 3 . 1 MET HB3 H 1.89 0.02 1 4 . 1 MET C C 173.8 0.10 1 5 . 1 MET CA C 55.6 0.10 1 6 . 1 MET CB C 34.4 0.10 1 7 . 2 LEU H H 8.75 0.02 1 8 . 2 LEU HA H 4.74 0.02 1 9 . 2 LEU HB2 H 1.88 0.02 2 10 . 2 LEU HB3 H 1.26 0.02 2 11 . 2 LEU C C 176.5 0.10 1 12 . 2 LEU CA C 54.9 0.10 1 13 . 2 LEU CB C 43.6 0.10 1 14 . 2 LEU N N 125.1 0.10 1 15 . 3 THR H H 9.46 0.02 1 16 . 3 THR HA H 4.83 0.02 1 17 . 3 THR C C 175.6 0.10 1 18 . 3 THR CA C 60.6 0.10 1 19 . 3 THR CB C 71.5 0.10 1 20 . 3 THR N N 111.5 0.10 1 21 . 4 MET H H 8.62 0.02 1 22 . 4 MET HA H 4.64 0.02 1 23 . 4 MET HB2 H 2.32 0.02 1 24 . 4 MET HB3 H 2.32 0.02 1 25 . 4 MET C C 179.7 0.10 1 26 . 4 MET CA C 56.8 0.10 1 27 . 4 MET CB C 29.1 0.10 1 28 . 4 MET N N 114.6 0.10 1 29 . 5 LYS H H 7.83 0.02 1 30 . 5 LYS HA H 4.18 0.02 1 31 . 5 LYS HB2 H 1.83 0.02 1 32 . 5 LYS HB3 H 1.83 0.02 1 33 . 5 LYS C C 177.5 0.10 1 34 . 5 LYS CA C 58.3 0.10 1 35 . 5 LYS CB C 32.2 0.10 1 36 . 5 LYS N N 116.6 0.10 1 37 . 6 ASP H H 7.69 0.02 1 38 . 6 ASP HA H 4.50 0.02 1 39 . 6 ASP HB2 H 2.72 0.02 1 40 . 6 ASP HB3 H 2.72 0.02 1 41 . 6 ASP C C 174.7 0.10 1 42 . 6 ASP CA C 55.5 0.10 1 43 . 6 ASP CB C 44.1 0.10 1 44 . 6 ASP N N 116.9 0.10 1 45 . 7 ILE H H 7.16 0.02 1 46 . 7 ILE HA H 4.57 0.02 1 47 . 7 ILE HB H 2.02 0.02 1 48 . 7 ILE C C 177.9 0.10 1 49 . 7 ILE CA C 59.1 0.10 1 50 . 7 ILE CB C 37.1 0.10 1 51 . 7 ILE N N 118.9 0.10 1 52 . 8 ILE H H 8.85 0.02 1 53 . 8 ILE HA H 4.43 0.02 1 54 . 8 ILE HB H 1.84 0.02 1 55 . 8 ILE C C 174.8 0.10 1 56 . 8 ILE CA C 61.7 0.10 1 57 . 8 ILE CB C 37.9 0.10 1 58 . 8 ILE N N 126.4 0.10 1 59 . 9 ARG H H 8.66 0.02 1 60 . 9 ARG HA H 5.20 0.02 1 61 . 9 ARG HB2 H 2.11 0.02 2 62 . 9 ARG HB3 H 1.91 0.02 2 63 . 9 ARG C C 176.3 0.10 1 64 . 9 ARG CA C 52.6 0.10 1 65 . 9 ARG CB C 32.7 0.10 1 66 . 9 ARG N N 118.6 0.10 1 67 . 10 ASP H H 8.35 0.02 1 68 . 10 ASP HA H 4.36 0.02 1 69 . 10 ASP HB2 H 2.87 0.02 2 70 . 10 ASP HB3 H 2.72 0.02 2 71 . 10 ASP C C 175.4 0.10 1 72 . 10 ASP CA C 57.3 0.10 1 73 . 10 ASP CB C 42.8 0.10 1 74 . 10 ASP N N 118.4 0.10 1 75 . 11 GLY H H 8.45 0.02 1 76 . 11 GLY HA2 H 4.64 0.02 2 77 . 11 GLY HA3 H 3.57 0.02 2 78 . 11 GLY C C 175.1 0.10 1 79 . 11 GLY CA C 44.9 0.10 1 80 . 11 GLY N N 116.9 0.10 1 81 . 12 HIS H H 8.62 0.10 1 82 . 12 HIS CA C 56.0 0.10 1 83 . 12 HIS CB C 32.7 0.10 1 84 . 12 HIS N N 125.1 0.10 1 85 . 13 PRO HA H 4.37 0.02 1 86 . 13 PRO HB2 H 2.42 0.02 2 87 . 13 PRO HB3 H 2.03 0.02 2 88 . 13 PRO C C 180.2 0.10 1 89 . 13 PRO CA C 65.1 0.10 1 90 . 13 PRO CB C 32.2 0.10 1 91 . 14 THR H H 11.39 0.02 1 92 . 14 THR HA H 3.92 0.02 2 93 . 14 THR HB H 4.11 0.02 2 94 . 14 THR C C 176.9 0.10 1 95 . 14 THR CA C 66.7 0.10 1 96 . 14 THR CB C 67.7 0.10 1 97 . 14 THR N N 121.3 0.10 1 98 . 15 LEU H H 7.64 0.02 1 99 . 15 LEU HA H 4.18 0.02 1 100 . 15 LEU HB2 H 2.03 0.02 2 101 . 15 LEU HB3 H 1.90 0.02 2 102 . 15 LEU C C 177.1 0.10 1 103 . 15 LEU CA C 56.1 0.10 1 104 . 15 LEU CB C 41.8 0.10 1 105 . 15 LEU N N 117.3 0.10 1 106 . 16 ARG H H 7.35 0.02 1 107 . 16 ARG HA H 4.70 0.02 1 108 . 16 ARG HB2 H 2.29 0.02 2 109 . 16 ARG HB3 H 1.71 0.02 2 110 . 16 ARG C C 175.8 0.10 1 111 . 16 ARG CA C 53.2 0.10 1 112 . 16 ARG CB C 31.7 0.10 1 113 . 16 ARG N N 113.8 0.10 1 114 . 17 GLN H H 7.01 0.02 1 115 . 17 GLN HA H 4.50 0.02 1 116 . 17 GLN HB2 H 2.10 0.02 1 117 . 17 GLN HB3 H 1.90 0.02 1 118 . 17 GLN C C 174.8 0.10 1 119 . 17 GLN CA C 54.5 0.10 1 120 . 17 GLN CB C 30.2 0.10 1 121 . 17 GLN N N 119.5 0.10 1 122 . 18 LYS H H 8.47 0.02 1 123 . 18 LYS HA H 4.24 0.02 1 124 . 18 LYS HB2 H 1.77 0.02 1 125 . 18 LYS HB3 H 1.77 0.02 1 126 . 18 LYS C C 175.6 0.10 1 127 . 18 LYS CA C 56.1 0.10 1 128 . 18 LYS CB C 32.0 0.10 1 129 . 18 LYS N N 121.7 0.10 1 130 . 19 ALA H H 8.48 0.02 1 131 . 19 ALA HA H 4.37 0.02 1 132 . 19 ALA HB H 1.25 0.02 1 133 . 19 ALA C C 177.3 0.10 1 134 . 19 ALA CA C 51.6 0.10 1 135 . 19 ALA CB C 20.6 0.10 1 136 . 19 ALA N N 128.4 0.10 1 137 . 20 ALA H H 7.76 0.02 1 138 . 20 ALA HA H 4.50 0.02 1 139 . 20 ALA HB H 1.58 0.02 1 140 . 20 ALA C C 178.3 0.10 1 141 . 20 ALA CA C 52.5 0.10 1 142 . 20 ALA CB C 20.6 0.10 1 143 . 20 ALA N N 125.5 0.10 1 144 . 21 GLU H H 8.76 0.02 1 145 . 21 GLU HA H 4.05 0.02 1 146 . 21 GLU HB2 H 1.97 0.02 1 147 . 21 GLU HB3 H 1.97 0.02 1 148 . 21 GLU C C 176.2 0.10 1 149 . 21 GLU CA C 57.1 0.10 1 150 . 21 GLU CB C 30.5 0.10 1 151 . 21 GLU N N 123.1 0.10 1 152 . 22 LEU H H 9.84 0.02 1 153 . 22 LEU HA H 4.50 0.02 1 154 . 22 LEU HB2 H 2.03 0.02 2 155 . 22 LEU HB3 H 1.90 0.02 2 156 . 22 LEU C C 178.2 0.10 1 157 . 22 LEU CA C 53.5 0.10 1 158 . 22 LEU CB C 41.1 0.10 1 159 . 22 LEU N N 127.7 0.10 1 160 . 23 GLU H H 8.47 0.02 1 161 . 23 GLU HA H 4.31 0.02 1 162 . 23 GLU HB2 H 1.97 0.02 2 163 . 23 GLU HB3 H 1.90 0.02 2 164 . 23 GLU C C 174.3 0.10 1 165 . 23 GLU CA C 55.6 0.10 1 166 . 23 GLU CB C 30.2 0.10 1 167 . 23 GLU N N 122.2 0.10 1 168 . 24 LEU H H 8.14 0.02 1 169 . 24 LEU CA C 51.2 0.10 1 170 . 24 LEU CB C 41.1 0.10 1 171 . 24 LEU N N 122.2 0.10 1 172 . 25 PRO HA H 4.44 0.02 1 173 . 25 PRO HB2 H 2.49 0.02 2 174 . 25 PRO HB3 H 2.10 0.02 2 175 . 25 PRO C C 175.6 0.10 1 176 . 25 PRO CA C 62.0 0.10 1 177 . 25 PRO CB C 34.6 0.10 1 178 . 26 LEU H H 8.47 0.02 1 179 . 26 LEU HA H 4.50 0.02 1 180 . 26 LEU HB2 H 1.90 0.02 2 181 . 26 LEU HB3 H 1.64 0.02 2 182 . 26 LEU C C 179.0 0.10 1 183 . 26 LEU CA C 55.0 0.10 1 184 . 26 LEU CB C 43.4 0.10 1 185 . 26 LEU N N 119.7 0.10 1 186 . 27 THR H H 9.06 0.02 1 187 . 27 THR HA H 4.96 0.02 1 188 . 27 THR HB H 3.40 0.02 1 189 . 27 THR C C 175.4 0.10 1 190 . 27 THR CA C 60.7 0.10 1 191 . 27 THR CB C 71.3 0.10 1 192 . 27 THR N N 112.4 0.10 1 193 . 28 LYS H H 8.79 0.02 1 194 . 28 LYS HA H 3.97 0.02 1 195 . 28 LYS HB2 H 1.97 0.02 2 196 . 28 LYS HB3 H 1.81 0.02 2 197 . 28 LYS C C 178.3 0.10 1 198 . 28 LYS CA C 60.2 0.10 1 199 . 28 LYS CB C 32.2 0.10 1 200 . 28 LYS N N 121.3 0.10 1 201 . 29 GLU H H 8.53 0.02 1 202 . 29 GLU HA H 4.11 0.02 1 203 . 29 GLU HB2 H 2.10 0.02 2 204 . 29 GLU HB3 H 1.96 0.02 2 205 . 29 GLU C C 180.2 0.10 1 206 . 29 GLU CA C 60.1 0.10 1 207 . 29 GLU CB C 29.3 0.10 1 208 . 29 GLU N N 116.4 0.10 1 209 . 30 GLU H H 7.97 0.02 1 210 . 30 GLU HA H 5.22 0.02 1 211 . 30 GLU HB2 H 2.10 0.02 2 212 . 30 GLU HB3 H 1.90 0.02 2 213 . 30 GLU C C 178.2 0.10 1 214 . 30 GLU CA C 59.4 0.10 1 215 . 30 GLU CB C 29.7 0.10 1 216 . 30 GLU N N 122.4 0.10 1 217 . 31 LYS H H 8.38 0.02 1 218 . 31 LYS HA H 3.85 0.02 1 219 . 31 LYS HB2 H 1.84 0.02 1 220 . 31 LYS HB3 H 1.84 0.02 1 221 . 31 LYS C C 178.2 0.10 1 222 . 31 LYS CA C 60.7 0.10 1 223 . 31 LYS CB C 32.3 0.10 1 224 . 31 LYS N N 118.4 0.10 1 225 . 32 GLU H H 8.44 0.02 1 226 . 32 GLU HA H 3.85 0.02 1 227 . 32 GLU HB2 H 2.16 0.02 2 228 . 32 GLU HB3 H 1.97 0.02 2 229 . 32 GLU C C 179.9 0.10 1 230 . 32 GLU CA C 59.4 0.10 1 231 . 32 GLU CB C 28.6 0.10 1 232 . 32 GLU N N 115.3 0.10 1 233 . 33 THR H H 8.06 0.02 1 234 . 33 THR HA H 3.85 0.02 1 235 . 33 THR C C 174.8 0.10 1 236 . 33 THR CA C 66.9 0.10 1 237 . 33 THR CB C 68.2 0.10 1 238 . 33 THR N N 118.2 0.10 1 239 . 34 LEU H H 7.76 0.02 1 240 . 34 LEU HA H 4.37 0.02 1 241 . 34 LEU HB2 H 1.90 0.02 2 242 . 34 LEU HB3 H 1.84 0.02 2 243 . 34 LEU C C 178.6 0.10 1 244 . 34 LEU CA C 58.1 0.10 1 245 . 34 LEU CB C 41.3 0.10 1 246 . 34 LEU N N 124.6 0.10 1 247 . 35 ILE H H 8.14 0.02 1 248 . 35 ILE HA H 3.92 0.02 1 249 . 35 ILE HB H 1.77 0.02 1 250 . 35 ILE C C 179.2 0.10 1 251 . 35 ILE CA C 65.1 0.10 1 252 . 35 ILE CB C 37.8 0.10 1 253 . 35 ILE N N 118.6 0.10 1 254 . 36 ALA H H 8.11 0.02 1 255 . 36 ALA HA H 4.24 0.02 1 256 . 36 ALA HB H 1.58 0.02 1 257 . 36 ALA C C 181.2 0.10 1 258 . 36 ALA CA C 54.8 0.10 1 259 . 36 ALA CB C 17.9 0.10 1 260 . 36 ALA N N 122.8 0.10 1 261 . 37 MET H H 8.47 0.02 1 262 . 37 MET HA H 3.79 0.02 1 263 . 37 MET HB2 H 1.90 0.02 1 264 . 37 MET HB3 H 1.90 0.02 1 265 . 37 MET C C 176.8 0.10 1 266 . 37 MET CA C 59.4 0.10 1 267 . 37 MET CB C 33.3 0.10 1 268 . 37 MET N N 121.3 0.10 1 269 . 38 ARG H H 7.79 0.02 1 270 . 38 ARG HA H 3.79 0.02 1 271 . 38 ARG HB2 H 1.97 0.02 2 272 . 38 ARG HB3 H 1.71 0.02 2 273 . 38 ARG C C 177.5 0.10 1 274 . 38 ARG CA C 60.1 0.10 1 275 . 38 ARG CB C 29.2 0.10 1 276 . 38 ARG N N 118.9 0.10 1 277 . 39 GLU H H 8.63 0.02 1 278 . 39 GLU HA H 3.79 0.02 1 279 . 39 GLU HB2 H 2.16 0.02 1 280 . 39 GLU HB3 H 2.16 0.02 1 281 . 39 GLU C C 177.5 0.10 1 282 . 39 GLU CA C 59.2 0.10 1 283 . 39 GLU CB C 30.3 0.10 1 284 . 39 GLU N N 119.0 0.10 1 285 . 40 PHE H H 7.99 0.02 1 286 . 40 PHE HA H 4.50 0.02 1 287 . 40 PHE HB2 H 3.40 0.02 2 288 . 40 PHE HB3 H 2.98 0.02 2 289 . 40 PHE C C 176.9 0.10 1 290 . 40 PHE CA C 61.4 0.10 1 291 . 40 PHE CB C 38.5 0.10 1 292 . 40 PHE N N 118.9 0.10 1 293 . 41 LEU H H 7.55 0.02 1 294 . 41 LEU HA H 3.91 0.02 1 295 . 41 LEU HB2 H 2.17 0.02 2 296 . 41 LEU HB3 H 1.25 0.02 2 297 . 41 LEU C C 179.9 0.10 1 298 . 41 LEU CA C 57.7 0.10 1 299 . 41 LEU CB C 41.3 0.10 1 300 . 41 LEU N N 119.8 0.10 1 301 . 42 VAL H H 8.37 0.02 1 302 . 42 VAL HA H 3.20 0.02 1 303 . 42 VAL HB H 2.09 0.02 1 304 . 42 VAL C C 179.4 0.10 1 305 . 42 VAL CA C 66.4 0.10 1 306 . 42 VAL CB C 32.3 0.10 1 307 . 42 VAL N N 120.2 0.10 1 308 . 43 ASN H H 8.55 0.02 1 309 . 43 ASN HA H 4.25 0.02 1 310 . 43 ASN HB2 H 2.75 0.02 2 311 . 43 ASN HB3 H 2.18 0.02 2 312 . 43 ASN C C 176.9 0.10 1 313 . 43 ASN CA C 55.5 0.10 1 314 . 43 ASN CB C 37.6 0.10 1 315 . 43 ASN N N 119.0 0.10 1 316 . 44 SER H H 8.72 0.02 1 317 . 44 SER HA H 4.11 0.02 1 318 . 44 SER HB2 H 3.60 0.02 2 319 . 44 SER HB3 H 3.33 0.02 2 320 . 44 SER C C 174.1 0.10 1 321 . 44 SER CA C 61.4 0.10 1 322 . 44 SER N N 114.7 0.10 1 323 . 45 GLN H H 7.20 0.02 1 324 . 45 GLN HA H 4.76 0.02 1 325 . 45 GLN HB2 H 2.39 0.02 2 326 . 45 GLN HB3 H 1.74 0.02 2 327 . 45 GLN C C 175.3 0.10 1 328 . 45 GLN CA C 56.0 0.10 1 329 . 45 GLN CB C 29.1 0.10 1 330 . 45 GLN N N 119.7 0.10 1 331 . 46 ASP H H 7.41 0.02 1 332 . 46 ASP HA H 4.76 0.02 1 333 . 46 ASP HB2 H 3.20 0.02 2 334 . 46 ASP HB3 H 2.55 0.02 2 335 . 46 ASP C C 175.1 0.10 1 336 . 46 ASP CA C 53.1 0.10 1 337 . 46 ASP CB C 42.4 0.10 1 338 . 46 ASP N N 123.8 0.10 1 339 . 47 GLU H H 8.78 0.02 1 340 . 47 GLU HA H 4.18 0.02 1 341 . 47 GLU HB2 H 1.97 0.02 1 342 . 47 GLU HB3 H 1.97 0.02 1 343 . 47 GLU C C 179.2 0.10 1 344 . 47 GLU CA C 60.3 0.10 1 345 . 47 GLU CB C 30.3 0.10 1 346 . 47 GLU N N 125.6 0.10 1 347 . 48 GLU H H 7.76 0.02 1 348 . 48 GLU HA H 4.18 0.02 1 349 . 48 GLU HB2 H 2.10 0.02 2 350 . 48 GLU HB3 H 1.77 0.02 2 351 . 48 GLU C C 175.7 0.10 1 352 . 48 GLU CA C 59.1 0.10 1 353 . 48 GLU CB C 29.6 0.10 1 354 . 48 GLU N N 120.2 0.10 1 355 . 49 ILE H H 8.26 0.02 1 356 . 49 ILE HA H 3.66 0.02 1 357 . 49 ILE HB H 2.23 0.02 1 358 . 49 ILE C C 178.1 0.10 1 359 . 49 ILE CA C 64.6 0.10 1 360 . 49 ILE CB C 36.7 0.10 1 361 . 49 ILE N N 123.1 0.10 1 362 . 50 ALA H H 9.29 0.02 1 363 . 50 ALA HA H 4.18 0.02 1 364 . 50 ALA HB H 1.77 0.02 1 365 . 50 ALA C C 181.5 0.10 1 366 . 50 ALA CA C 56.1 0.10 1 367 . 50 ALA CB C 18.2 0.10 1 368 . 50 ALA N N 122.4 0.10 1 369 . 51 LYS H H 7.70 0.02 1 370 . 51 LYS HA H 3.98 0.02 1 371 . 51 LYS HB2 H 2.10 0.02 2 372 . 51 LYS HB3 H 1.84 0.02 2 373 . 51 LYS C C 178.5 0.10 1 374 . 51 LYS CA C 58.9 0.10 1 375 . 51 LYS CB C 32.3 0.10 1 376 . 51 LYS N N 115.6 0.10 1 377 . 52 ARG H H 8.09 0.02 1 378 . 52 ARG HA H 3.92 0.02 1 379 . 52 ARG HB2 H 1.84 0.02 2 380 . 52 ARG HB3 H 1.64 0.02 2 381 . 52 ARG C C 178.2 0.10 1 382 . 52 ARG CA C 58.9 0.10 1 383 . 52 ARG CB C 29.9 0.10 1 384 . 52 ARG N N 116.9 0.10 1 385 . 53 TYR H H 7.83 0.02 1 386 . 53 TYR HA H 4.77 0.02 1 387 . 53 TYR HB2 H 3.40 0.02 2 388 . 53 TYR HB3 H 2.49 0.02 2 389 . 53 TYR C C 175.5 0.10 1 390 . 53 TYR CA C 57.6 0.10 1 391 . 53 TYR CB C 38.7 0.10 1 392 . 53 TYR N N 112.2 0.10 1 393 . 54 GLY H H 7.88 0.02 1 394 . 54 GLY HA2 H 4.05 0.02 1 395 . 54 GLY HA3 H 4.05 0.02 1 396 . 54 GLY C C 175.5 0.10 1 397 . 54 GLY CA C 47.3 0.10 1 398 . 54 GLY N N 112.0 0.10 1 399 . 55 LEU H H 8.79 0.02 1 400 . 55 LEU HA H 4.37 0.02 1 401 . 55 LEU HB2 H 1.51 0.02 2 402 . 55 LEU HB3 H 1.12 0.02 2 403 . 55 LEU C C 175.9 0.10 1 404 . 55 LEU CA C 53.0 0.10 1 405 . 55 LEU CB C 41.6 0.10 1 406 . 55 LEU N N 116.4 0.10 1 407 . 56 ARG H H 7.24 0.02 1 408 . 56 ARG HA H 4.50 0.02 1 409 . 56 ARG HB2 H 1.84 0.02 1 410 . 56 ARG HB3 H 1.84 0.02 1 411 . 56 ARG C C 174.0 0.10 1 412 . 56 ARG CA C 54.8 0.10 1 413 . 56 ARG CB C 32.3 0.10 1 414 . 56 ARG N N 123.3 0.10 1 415 . 57 SER H H 8.03 0.02 1 416 . 57 SER HA H 4.05 0.02 1 417 . 57 SER HB2 H 3.79 0.02 1 418 . 57 SER HB3 H 3.79 0.02 1 419 . 57 SER C C 174.9 0.10 1 420 . 57 SER CA C 58.9 0.10 1 421 . 57 SER CB C 64.1 0.10 1 422 . 57 SER N N 115.5 0.10 1 423 . 58 GLY H H 8.11 0.02 1 424 . 58 GLY HA2 H 4.63 0.02 2 425 . 58 GLY HA3 H 3.72 0.02 2 426 . 58 GLY C C 171.7 0.10 1 427 . 58 GLY CA C 44.5 0.10 1 428 . 58 GLY N N 111.1 0.10 1 429 . 59 VAL H H 8.03 0.02 1 430 . 59 VAL HA H 4.70 0.02 1 431 . 59 VAL HB H 2.36 0.02 1 432 . 59 VAL C C 173.9 0.10 1 433 . 59 VAL CA C 60.7 0.10 1 434 . 59 VAL CB C 32.3 0.10 1 435 . 59 VAL N N 108.2 0.10 1 436 . 60 GLY H H 7.33 0.02 1 437 . 60 GLY HA2 H 4.96 0.02 1 438 . 60 GLY HA3 H 3.40 0.02 1 439 . 60 GLY C C 170.5 0.10 1 440 . 60 GLY CA C 44.2 0.10 1 441 . 60 GLY N N 108.0 0.10 1 442 . 61 LEU H H 8.69 0.02 1 443 . 61 LEU HA H 4.50 0.02 1 444 . 61 LEU HB2 H 2.03 0.02 2 445 . 61 LEU HB3 H 1.38 0.02 2 446 . 61 LEU C C 173.3 0.10 1 447 . 61 LEU CA C 54.8 0.10 1 448 . 61 LEU CB C 47.5 0.10 1 449 . 61 LEU N N 121.1 0.10 1 450 . 62 ALA H H 8.28 0.02 1 451 . 62 ALA HA H 5.22 0.02 1 452 . 62 ALA HB H 1.77 0.02 1 453 . 62 ALA C C 178.5 0.10 1 454 . 62 ALA CA C 49.3 0.10 1 455 . 62 ALA CB C 22.9 0.10 1 456 . 62 ALA N N 126.4 0.10 1 457 . 63 ALA H H 8.32 0.02 1 458 . 63 ALA CA C 56.9 0.10 1 459 . 63 ALA CB C 15.9 0.10 1 460 . 63 ALA N N 124.8 0.10 1 461 . 64 PRO HA H 3.79 0.02 1 462 . 64 PRO HB2 H 2.55 0.02 2 463 . 64 PRO HB3 H 1.32 0.02 2 464 . 64 PRO C C 177.4 0.10 1 465 . 64 PRO CA C 67.0 0.10 1 466 . 64 PRO CB C 32.2 0.10 1 467 . 65 GLN H H 8.08 0.02 1 468 . 65 GLN HA H 3.83 0.02 1 469 . 65 GLN HB2 H 2.04 0.02 1 470 . 65 GLN HB3 H 2.04 0.02 1 471 . 65 GLN C C 176.2 0.10 1 472 . 65 GLN CA C 58.7 0.10 1 473 . 65 GLN CB C 31.7 0.10 1 474 . 65 GLN N N 108.5 0.10 1 475 . 66 ILE H H 7.97 0.02 1 476 . 66 ILE HA H 5.20 0.02 1 477 . 66 ILE HB H 2.10 0.02 1 478 . 66 ILE C C 175.7 0.10 1 479 . 66 ILE CA C 59.9 0.10 1 480 . 66 ILE CB C 36.4 0.10 1 481 . 66 ILE N N 111.1 0.10 1 482 . 67 ASN H H 7.95 0.02 1 483 . 67 ASN HA H 4.31 0.02 1 484 . 67 ASN HB2 H 3.57 0.02 1 485 . 67 ASN HB3 H 2.09 0.02 1 486 . 67 ASN C C 174.2 0.10 1 487 . 67 ASN CA C 53.0 0.10 1 488 . 67 ASN CB C 38.2 0.10 1 489 . 67 ASN N N 116.6 0.10 1 490 . 68 ILE H H 7.42 0.02 1 491 . 68 ILE HA H 3.81 0.02 1 492 . 68 ILE CA C 59.9 0.10 1 493 . 68 ILE CB C 39.0 0.10 1 494 . 68 ILE N N 118.6 0.10 1 495 . 69 SER HA H 4.44 0.02 1 496 . 69 SER HB2 H 4.11 0.02 1 497 . 69 SER C C 175.7 0.10 1 498 . 69 SER CA C 56.8 0.10 1 499 . 69 SER CB C 61.5 0.10 1 500 . 70 LYS H H 8.37 0.02 1 501 . 70 LYS HA H 5.42 0.02 1 502 . 70 LYS HB2 H 1.97 0.02 2 503 . 70 LYS HB3 H 1.32 0.02 2 504 . 70 LYS C C 177.0 0.10 1 505 . 70 LYS CA C 54.5 0.10 1 506 . 70 LYS CB C 38.2 0.10 1 507 . 70 LYS N N 122.8 0.10 1 508 . 71 ARG H H 7.91 0.02 1 509 . 71 ARG HA H 4.37 0.02 1 510 . 71 ARG HB2 H 1.97 0.02 1 511 . 71 ARG HB3 H 1.97 0.02 1 512 . 71 ARG C C 172.4 0.10 1 513 . 71 ARG CA C 56.9 0.10 1 514 . 71 ARG CB C 28.6 0.10 1 515 . 71 ARG N N 120.6 0.10 1 516 . 72 MET H H 8.09 0.02 1 517 . 72 MET HA H 5.61 0.02 1 518 . 72 MET HB2 H 1.97 0.02 1 519 . 72 MET HB3 H 1.97 0.02 1 520 . 72 MET C C 174.8 0.10 1 521 . 72 MET CA C 54.3 0.10 1 522 . 72 MET CB C 36.1 0.10 1 523 . 72 MET N N 121.7 0.10 1 524 . 73 ILE H H 8.93 0.02 1 525 . 73 ILE HA H 5.22 0.02 1 526 . 73 ILE HB H 1.77 0.02 1 527 . 73 ILE C C 171.4 0.10 1 528 . 73 ILE CA C 59.2 0.10 1 529 . 73 ILE CB C 42.6 0.10 1 530 . 73 ILE N N 114.6 0.10 1 531 . 74 ALA H H 9.09 0.02 1 532 . 74 ALA HA H 5.48 0.02 1 533 . 74 ALA HB H 1.19 0.02 1 534 . 74 ALA C C 174.4 0.10 1 535 . 74 ALA CA C 50.4 0.10 1 536 . 74 ALA CB C 21.4 0.10 1 537 . 74 ALA N N 124.2 0.10 1 538 . 75 VAL H H 8.76 0.02 1 539 . 75 VAL HA H 4.50 0.02 1 540 . 75 VAL HB H 1.45 0.02 1 541 . 75 VAL C C 173.1 0.10 1 542 . 75 VAL CA C 61.4 0.10 1 543 . 75 VAL CB C 36.8 0.10 1 544 . 75 VAL N N 120.2 0.10 1 545 . 76 LEU H H 8.88 0.02 1 546 . 76 LEU HA H 5.29 0.02 1 547 . 76 LEU HB2 H 1.86 0.02 2 548 . 76 LEU HB3 H 1.18 0.02 2 549 . 76 LEU C C 175.0 0.10 1 550 . 76 LEU CA C 54.2 0.10 1 551 . 76 LEU CB C 44.6 0.10 1 552 . 76 LEU N N 129.9 0.10 1 553 . 77 ILE H H 9.30 0.02 1 554 . 77 ILE HA H 4.80 0.02 1 555 . 77 ILE HB H 2.09 0.02 1 556 . 77 ILE CA C 57.9 0.10 1 557 . 77 ILE CB C 41.8 0.10 1 558 . 77 ILE N N 125.3 0.10 1 559 . 78 PRO HA H 4.50 0.02 1 560 . 78 PRO HB2 H 2.42 0.02 2 561 . 78 PRO HB3 H 2.03 0.02 2 562 . 78 PRO C C 176.1 0.10 1 563 . 78 PRO CA C 63.3 0.10 1 564 . 78 PRO CB C 32.3 0.10 1 565 . 79 ASP H H 7.81 0.02 1 566 . 79 ASP HA H 4.77 0.02 1 567 . 79 ASP HB2 H 2.75 0.02 2 568 . 79 ASP HB3 H 2.62 0.02 2 569 . 79 ASP C C 176.4 0.10 1 570 . 79 ASP CA C 54.5 0.10 1 571 . 79 ASP CB C 41.6 0.10 1 572 . 79 ASP N N 116.2 0.10 1 573 . 80 ASP H H 8.88 0.02 1 574 . 80 ASP HA H 4.57 0.02 1 575 . 80 ASP HB2 H 3.27 0.02 1 576 . 80 ASP HB3 H 2.75 0.02 1 577 . 80 ASP C C 176.5 0.10 1 578 . 80 ASP CA C 53.7 0.10 1 579 . 80 ASP CB C 40.8 0.10 1 580 . 80 ASP N N 127.7 0.10 1 581 . 81 GLY H H 9.46 0.02 1 582 . 81 GLY HA2 H 4.57 0.02 2 583 . 81 GLY HA3 H 3.59 0.02 2 584 . 81 GLY C C 175.0 0.10 1 585 . 81 GLY CA C 44.9 0.10 1 586 . 81 GLY N N 111.1 0.10 1 587 . 82 SER H H 8.93 0.02 1 588 . 82 SER HA H 4.63 0.02 1 589 . 82 SER HB2 H 4.11 0.02 2 590 . 82 SER HB3 H 3.98 0.02 2 591 . 82 SER C C 175.5 0.10 1 592 . 82 SER CA C 58.4 0.10 1 593 . 82 SER CB C 65.1 0.10 1 594 . 82 SER N N 117.1 0.10 1 595 . 83 GLY H H 9.51 0.02 1 596 . 83 GLY HA2 H 4.37 0.02 2 597 . 83 GLY HA3 H 3.85 0.02 2 598 . 83 GLY C C 174.2 0.10 1 599 . 83 GLY CA C 45.2 0.10 1 600 . 83 GLY N N 113.3 0.10 1 601 . 84 LYS H H 7.63 0.02 1 602 . 84 LYS HA H 4.63 0.02 1 603 . 84 LYS HB2 H 1.77 0.02 2 604 . 84 LYS HB3 H 1.71 0.02 2 605 . 84 LYS C C 174.1 0.10 1 606 . 84 LYS CA C 55.0 0.10 1 607 . 84 LYS CB C 33.6 0.10 1 608 . 84 LYS N N 120.8 0.10 1 609 . 85 SER H H 7.89 0.02 1 610 . 85 SER HA H 4.83 0.02 1 611 . 85 SER HB2 H 4.11 0.02 2 612 . 85 SER HB3 H 3.98 0.02 2 613 . 85 SER C C 173.3 0.10 1 614 . 85 SER CA C 56.1 0.10 1 615 . 85 SER CB C 65.9 0.10 1 616 . 85 SER N N 116.2 0.10 1 617 . 86 TYR H H 8.84 0.02 1 618 . 86 TYR HA H 4.70 0.02 1 619 . 86 TYR HB2 H 3.14 0.02 2 620 . 86 TYR HB3 H 3.01 0.02 2 621 . 86 TYR C C 173.0 0.10 1 622 . 86 TYR CA C 57.4 0.10 1 623 . 86 TYR CB C 40.3 0.10 1 624 . 86 TYR N N 118.2 0.10 1 625 . 87 ASP H H 7.78 0.02 1 626 . 87 ASP HA H 5.29 0.02 1 627 . 87 ASP HB2 H 2.68 0.02 2 628 . 87 ASP HB3 H 2.29 0.02 2 629 . 87 ASP C C 175.1 0.10 1 630 . 87 ASP CA C 52.2 0.10 1 631 . 87 ASP CB C 40.8 0.10 1 632 . 87 ASP N N 126.6 0.10 1 633 . 88 TYR H H 9.06 0.02 1 634 . 88 TYR HA H 5.09 0.02 1 635 . 88 TYR HB2 H 3.01 0.02 2 636 . 88 TYR HB3 H 2.62 0.02 2 637 . 88 TYR C C 174.5 0.10 1 638 . 88 TYR CA C 57.9 0.10 1 639 . 88 TYR CB C 44.2 0.10 1 640 . 88 TYR N N 118.6 0.10 1 641 . 89 MET H H 8.45 0.02 1 642 . 89 MET HA H 5.03 0.02 1 643 . 89 MET HB2 H 2.49 0.02 2 644 . 89 MET HB3 H 1.84 0.02 2 645 . 89 MET C C 175.1 0.10 1 646 . 89 MET CA C 55.3 0.10 1 647 . 89 MET CB C 34.3 0.10 1 648 . 89 MET N N 122.6 0.10 1 649 . 90 LEU H H 8.98 0.02 1 650 . 90 LEU HA H 5.42 0.02 1 651 . 90 LEU HB2 H 1.64 0.02 2 652 . 90 LEU HB3 H 1.25 0.02 2 653 . 90 LEU C C 174.8 0.10 1 654 . 90 LEU CA C 53.0 0.10 1 655 . 90 LEU CB C 46.5 0.10 1 656 . 90 LEU N N 118.4 0.10 1 657 . 91 VAL H H 9.32 0.02 1 658 . 91 VAL HA H 5.35 0.02 1 659 . 91 VAL HB H 2.29 0.02 1 660 . 91 VAL C C 174.3 0.10 1 661 . 91 VAL CA C 59.7 0.10 1 662 . 91 VAL CB C 33.8 0.10 1 663 . 91 VAL N N 118.4 0.10 1 664 . 92 ASN H H 9.06 0.02 1 665 . 92 ASN HA H 5.09 0.02 1 666 . 92 ASN HB2 H 3.42 0.02 2 667 . 92 ASN HB3 H 2.33 0.02 2 668 . 92 ASN CA C 57.8 0.10 1 669 . 92 ASN CB C 44.2 0.10 1 670 . 92 ASN N N 118.6 0.10 1 671 . 93 PRO HA H 5.09 0.02 1 672 . 93 PRO HB2 H 1.71 0.02 1 673 . 93 PRO HB3 H 1.71 0.02 1 674 . 93 PRO C C 177.1 0.10 1 675 . 93 PRO CA C 63.2 0.10 1 676 . 93 PRO CB C 32.4 0.10 1 677 . 94 LYS H H 9.22 0.02 1 678 . 94 LYS HA H 4.58 0.02 1 679 . 94 LYS HB2 H 2.28 0.02 1 680 . 94 LYS HB3 H 2.28 0.02 1 681 . 94 LYS C C 174.7 0.10 1 682 . 94 LYS CA C 55.7 0.10 1 683 . 94 LYS CB C 36.6 0.10 1 684 . 94 LYS N N 120.8 0.10 1 685 . 95 ILE H H 8.95 0.02 1 686 . 95 ILE HA H 4.44 0.02 1 687 . 95 ILE HB H 1.90 0.02 1 688 . 95 ILE C C 176.6 0.10 1 689 . 95 ILE CA C 62.5 0.10 1 690 . 95 ILE CB C 38.1 0.10 1 691 . 95 ILE N N 124.0 0.10 1 692 . 96 VAL H H 8.67 0.02 1 693 . 96 VAL HA H 4.45 0.02 1 694 . 96 VAL HB H 2.28 0.02 1 695 . 96 VAL C C 175.8 0.10 1 696 . 96 VAL CA C 62.2 0.10 1 697 . 96 VAL CB C 32.7 0.10 1 698 . 96 VAL N N 122.2 0.10 1 699 . 97 SER H H 7.61 0.02 1 700 . 97 SER HA H 5.24 0.02 1 701 . 97 SER HB2 H 3.86 0.02 2 702 . 97 SER HB3 H 3.66 0.02 2 703 . 97 SER CA C 57.8 0.10 1 704 . 97 SER CB C 65.3 0.10 1 705 . 97 SER N N 114.2 0.10 1 706 . 101 GLN HA H 4.37 0.02 1 707 . 101 GLN HB2 H 2.16 0.02 1 708 . 101 GLN HB3 H 2.16 0.02 1 709 . 101 GLN C C 176.4 0.10 1 710 . 101 GLN CA C 57.5 0.10 1 711 . 101 GLN CB C 30.1 0.10 1 712 . 102 GLU H H 9.10 0.02 1 713 . 102 GLU HA H 5.42 0.02 1 714 . 102 GLU HB2 H 2.23 0.02 1 715 . 102 GLU HB3 H 2.23 0.02 1 716 . 102 GLU C C 175.6 0.10 1 717 . 102 GLU CA C 55.7 0.10 1 718 . 102 GLU CB C 35.0 0.10 1 719 . 102 GLU N N 127.7 0.10 1 720 . 103 ALA H H 9.38 0.02 1 721 . 103 ALA HA H 5.68 0.02 1 722 . 103 ALA HB H 1.19 0.02 1 723 . 103 ALA C C 175.4 0.10 1 724 . 103 ALA CA C 50.8 0.10 1 725 . 103 ALA CB C 24.4 0.10 1 726 . 103 ALA N N 122.0 0.10 1 727 . 104 TYR H H 8.14 0.02 1 728 . 104 TYR HA H 4.55 0.02 1 729 . 104 TYR HB2 H 3.32 0.02 2 730 . 104 TYR HB3 H 2.38 0.02 2 731 . 104 TYR CA C 56.8 0.10 1 732 . 104 TYR CB C 41.2 0.10 1 733 . 104 TYR N N 112.9 0.10 1 734 . 106 PRO HA H 4.50 0.02 1 735 . 106 PRO HB2 H 2.49 0.02 2 736 . 106 PRO HB3 H 2.23 0.02 2 737 . 106 PRO C C 176.3 0.10 1 738 . 106 PRO CA C 65.2 0.10 1 739 . 106 PRO CB C 32.2 0.10 1 740 . 107 THR H H 7.29 0.02 1 741 . 107 THR HA H 4.57 0.02 1 742 . 107 THR HB H 4.37 0.02 1 743 . 107 THR C C 175.5 0.10 1 744 . 107 THR CA C 61.2 0.10 1 745 . 107 THR CB C 69.4 0.10 1 746 . 107 THR N N 104.5 0.10 1 747 . 108 GLY H H 7.36 0.02 1 748 . 108 GLY HA2 H 4.70 0.02 2 749 . 108 GLY HA3 H 4.37 0.02 2 750 . 108 GLY C C 173.5 0.10 1 751 . 108 GLY CA C 45.4 0.10 1 752 . 108 GLY N N 109.3 0.10 1 753 . 109 GLU H H 8.65 0.02 1 754 . 109 GLU HA H 4.44 0.02 1 755 . 109 GLU HB2 H 1.77 0.02 1 756 . 109 GLU HB3 H 1.77 0.02 1 757 . 109 GLU C C 174.5 0.10 1 758 . 109 GLU CA C 55.7 0.10 1 759 . 109 GLU CB C 33.7 0.10 1 760 . 109 GLU N N 117.1 0.10 1 761 . 110 GLY H H 7.41 0.02 1 762 . 110 GLY HA2 H 4.05 0.02 2 763 . 110 GLY HA3 H 3.59 0.02 2 764 . 110 GLY C C 172.6 0.10 1 765 . 110 GLY CA C 43.6 0.10 1 766 . 110 GLY N N 104.2 0.10 1 767 . 111 CYS H H 9.04 0.02 1 768 . 111 CYS HA H 4.50 0.02 1 769 . 111 CYS HB2 H 2.94 0.02 1 770 . 111 CYS HB3 H 2.94 0.02 1 771 . 111 CYS C C 176.0 0.10 1 772 . 111 CYS CA C 61.3 0.10 1 773 . 111 CYS CB C 32.0 0.10 1 774 . 111 CYS N N 120.0 0.10 1 775 . 112 LEU H H 9.50 0.02 1 776 . 112 LEU HA H 4.24 0.02 1 777 . 112 LEU HB2 H 1.64 0.02 1 778 . 112 LEU HB3 H 1.64 0.02 1 779 . 112 LEU C C 176.7 0.10 1 780 . 112 LEU CA C 58.7 0.10 1 781 . 112 LEU CB C 42.8 0.10 1 782 . 112 LEU N N 131.0 0.10 1 783 . 113 SER H H 8.35 0.02 1 784 . 113 SER HA H 4.70 0.02 1 785 . 113 SER HB2 H 4.11 0.02 1 786 . 113 SER HB3 H 4.11 0.02 1 787 . 113 SER C C 171.9 0.10 1 788 . 113 SER CA C 60.7 0.10 1 789 . 113 SER CB C 65.5 0.10 1 790 . 113 SER N N 110.4 0.10 1 791 . 114 VAL H H 8.22 0.02 1 792 . 114 VAL HA H 4.37 0.02 1 793 . 114 VAL HB H 2.16 0.02 1 794 . 114 VAL C C 174.8 0.10 1 795 . 114 VAL CA C 61.8 0.10 1 796 . 114 VAL CB C 34.1 0.10 1 797 . 114 VAL N N 121.7 0.10 1 798 . 115 ASP H H 9.10 0.02 1 799 . 115 ASP HA H 4.70 0.02 1 800 . 115 ASP HB2 H 2.81 0.02 2 801 . 115 ASP HB3 H 2.55 0.02 2 802 . 115 ASP C C 176.1 0.02 1 803 . 115 ASP CA C 56.3 0.10 1 804 . 115 ASP CB C 41.8 0.10 1 805 . 115 ASP N N 128.2 0.10 1 806 . 116 ASP H H 7.70 0.02 1 807 . 116 ASP HA H 4.77 0.02 1 808 . 116 ASP HB2 H 2.62 0.02 2 809 . 116 ASP HB3 H 2.49 0.02 2 810 . 116 ASP C C 174.7 0.10 1 811 . 116 ASP CA C 53.2 0.10 1 812 . 116 ASP CB C 42.1 0.10 1 813 . 116 ASP N N 118.2 0.10 1 814 . 117 ASN H H 8.51 0.02 1 815 . 117 ASN HA H 4.77 0.02 1 816 . 117 ASN HB2 H 2.75 0.02 1 817 . 117 ASN HB3 H 2.75 0.02 1 818 . 117 ASN C C 174.8 0.10 1 819 . 117 ASN CA C 53.2 0.10 1 820 . 117 ASN CB C 38.7 0.10 1 821 . 117 ASN N N 118.6 0.10 1 822 . 118 VAL H H 8.38 0.02 1 823 . 118 VAL HA H 4.11 0.02 1 824 . 118 VAL HB H 2.23 0.02 1 825 . 118 VAL C C 174.9 0.10 1 826 . 118 VAL CA C 62.3 0.10 1 827 . 118 VAL CB C 33.0 0.10 1 828 . 118 VAL N N 125.3 0.10 1 829 . 119 ALA H H 8.53 0.02 1 830 . 119 ALA HA H 4.57 0.02 1 831 . 119 ALA HB H 1.32 0.02 1 832 . 119 ALA C C 176.9 0.10 1 833 . 119 ALA CA C 51.4 0.10 1 834 . 119 ALA CB C 20.0 0.10 1 835 . 119 ALA N N 130.6 0.10 1 836 . 120 GLY H H 8.22 0.02 1 837 . 120 GLY HA2 H 4.50 0.02 2 838 . 120 GLY HA3 H 3.53 0.02 2 839 . 120 GLY C C 171.9 0.10 1 840 . 120 GLY CA C 44.6 0.10 1 841 . 120 GLY N N 106.9 0.10 1 842 . 121 LEU H H 8.11 0.02 1 843 . 121 LEU HA H 4.37 0.02 1 844 . 121 LEU HB2 H 1.90 0.02 2 845 . 121 LEU HB3 H 1.38 0.02 2 846 . 121 LEU C C 176.3 0.10 1 847 . 121 LEU CA C 54.2 0.10 1 848 . 121 LEU CB C 43.0 0.10 1 849 . 121 LEU N N 117.3 0.10 1 850 . 122 VAL H H 9.21 0.02 1 851 . 122 VAL HA H 3.92 0.02 1 852 . 122 VAL HB H 2.10 0.02 1 853 . 122 VAL C C 175.2 0.10 1 854 . 122 VAL CA C 61.4 0.10 1 855 . 122 VAL CB C 32.4 0.10 1 856 . 122 VAL N N 123.7 0.10 1 857 . 123 HIS H H 8.79 0.02 1 858 . 123 HIS HA H 4.57 0.02 1 859 . 123 HIS HB2 H 2.81 0.02 1 860 . 123 HIS HB3 H 2.81 0.02 1 861 . 123 HIS C C 175.2 0.10 1 862 . 123 HIS CA C 59.3 0.10 1 863 . 123 HIS CB C 28.5 0.10 1 864 . 123 HIS N N 125.5 0.10 1 865 . 124 ARG H H 9.03 0.02 1 866 . 124 ARG HA H 4.50 0.02 1 867 . 124 ARG HB2 H 1.64 0.02 2 868 . 124 ARG HB3 H 1.32 0.02 2 869 . 124 ARG C C 175.2 0.10 1 870 . 124 ARG CA C 53.1 0.10 1 871 . 124 ARG CB C 33.6 0.10 1 872 . 124 ARG N N 122.8 0.10 1 873 . 125 HIS H H 8.29 0.02 1 874 . 125 HIS HA H 4.77 0.02 1 875 . 125 HIS HB2 H 2.68 0.02 1 876 . 125 HIS HB3 H 2.68 0.02 1 877 . 125 HIS C C 176.7 0.10 1 878 . 125 HIS CA C 57.8 0.10 1 879 . 125 HIS CB C 30.1 0.10 1 880 . 125 HIS N N 118.7 0.10 1 881 . 126 ASN H H 8.68 0.02 1 882 . 126 ASN HA H 4.44 0.02 1 883 . 126 ASN HB2 H 2.49 0.02 2 884 . 126 ASN HB3 H 2.29 0.02 2 885 . 126 ASN C C 173.4 0.10 1 886 . 126 ASN CA C 55.7 0.10 1 887 . 126 ASN CB C 39.7 0.10 1 888 . 126 ASN N N 119.1 0.10 1 889 . 127 ARG H H 8.13 0.02 1 890 . 127 ARG HA H 5.35 0.02 1 891 . 127 ARG HB2 H 1.90 0.02 1 892 . 127 ARG HB3 H 1.90 0.02 1 893 . 127 ARG C C 176.3 0.10 1 894 . 127 ARG CA C 54.2 0.10 1 895 . 127 ARG CB C 33.7 0.10 1 896 . 127 ARG N N 112.2 0.10 1 897 . 128 ILE H H 8.35 0.02 1 898 . 128 ILE HA H 5.22 0.02 1 899 . 128 ILE HB H 1.90 0.02 1 900 . 128 ILE C C 174.2 0.10 1 901 . 128 ILE CA C 59.6 0.10 1 902 . 128 ILE CB C 43.6 0.10 1 903 . 128 ILE N N 112.4 0.10 1 904 . 129 THR H H 8.28 0.02 1 905 . 129 THR HA H 5.29 0.02 1 906 . 129 THR HB H 3.85 0.02 1 907 . 129 THR C C 174.2 0.10 1 908 . 129 THR CA C 61.3 0.10 1 909 . 129 THR CB C 70.1 0.10 1 910 . 129 THR N N 117.5 0.10 1 911 . 130 ILE H H 9.23 0.02 1 912 . 130 ILE HA H 5.22 0.02 1 913 . 130 ILE HB H 1.45 0.02 1 914 . 130 ILE C C 174.8 0.10 1 915 . 130 ILE CA C 57.9 0.10 1 916 . 130 ILE CB C 41.3 0.10 1 917 . 130 ILE N N 124.6 0.10 1 918 . 131 LYS H H 8.84 0.02 1 919 . 131 LYS HA H 5.29 0.02 1 920 . 131 LYS HB2 H 1.90 0.02 2 921 . 131 LYS HB3 H 1.64 0.02 2 922 . 131 LYS C C 175.0 0.10 1 923 . 131 LYS CA C 55.0 0.10 1 924 . 131 LYS CB C 35.6 0.10 1 925 . 131 LYS N N 124.2 0.10 1 926 . 132 ALA H H 9.06 0.02 1 927 . 132 ALA HA H 4.83 0.02 1 928 . 132 ALA HB H 1.32 0.02 1 929 . 132 ALA C C 175.1 0.10 1 930 . 132 ALA CA C 50.6 0.10 1 931 . 132 ALA CB C 24.5 0.10 1 932 . 132 ALA N N 125.1 0.10 1 933 . 133 LYS H H 8.66 0.02 1 934 . 133 LYS HA H 5.68 0.02 1 935 . 133 LYS HB2 H 1.77 0.02 2 936 . 133 LYS HB3 H 1.71 0.02 2 937 . 133 LYS C C 175.7 0.10 1 938 . 133 LYS CA C 53.3 0.10 1 939 . 133 LYS CB C 35.9 0.10 1 940 . 133 LYS N N 118.9 0.10 1 941 . 134 ASP H H 8.56 0.02 1 942 . 134 ASP HA H 5.29 0.02 1 943 . 134 ASP HB2 H 3.98 0.02 2 944 . 134 ASP HB3 H 2.68 0.02 2 945 . 134 ASP C C 177.8 0.10 1 946 . 134 ASP CA C 51.6 0.10 1 947 . 134 ASP CB C 41.3 0.10 1 948 . 134 ASP N N 120.2 0.10 1 949 . 135 ILE H H 8.54 0.02 1 950 . 135 ILE HA H 3.85 0.02 1 951 . 135 ILE HB H 1.90 0.02 1 952 . 135 ILE C C 175.6 0.10 1 953 . 135 ILE CA C 64.6 0.10 1 954 . 135 ILE CB C 39.3 0.10 1 955 . 135 ILE N N 113.8 0.10 1 956 . 136 GLU H H 7.66 0.02 1 957 . 136 GLU HA H 4.50 0.02 1 958 . 136 GLU HB2 H 2.36 0.02 2 959 . 136 GLU HB3 H 1.90 0.02 2 960 . 136 GLU C C 177.3 0.10 1 961 . 136 GLU CA C 54.8 0.10 1 962 . 136 GLU CB C 29.7 0.10 1 963 . 136 GLU N N 117.5 0.10 1 964 . 137 GLY H H 8.56 0.02 1 965 . 137 GLY HA2 H 4.31 0.02 2 966 . 137 GLY HA3 H 3.46 0.02 2 967 . 137 GLY C C 174.1 0.10 1 968 . 137 GLY CA C 45.5 0.10 1 969 . 137 GLY N N 108.2 0.10 1 970 . 138 ASN H H 8.97 0.02 1 971 . 138 ASN HA H 4.77 0.02 1 972 . 138 ASN HB2 H 2.88 0.02 2 973 . 138 ASN HB3 H 2.68 0.02 2 974 . 138 ASN C C 175.3 0.10 1 975 . 138 ASN CA C 53.0 0.10 1 976 . 138 ASN CB C 38.7 0.10 1 977 . 138 ASN N N 120.4 0.10 1 978 . 139 ASP H H 8.70 0.02 1 979 . 139 ASP HA H 4.90 0.02 1 980 . 139 ASP HB2 H 2.62 0.02 1 981 . 139 ASP HB3 H 2.62 0.02 1 982 . 139 ASP C C 175.6 0.10 1 983 . 139 ASP CA C 55.8 0.10 1 984 . 139 ASP CB C 42.1 0.10 1 985 . 139 ASP N N 120.4 0.10 1 986 . 140 ILE H H 8.72 0.02 1 987 . 140 ILE HA H 4.57 0.02 1 988 . 140 ILE HB H 1.64 0.02 1 989 . 140 ILE C C 173.9 0.10 1 990 . 140 ILE CA C 58.9 0.10 1 991 . 140 ILE CB C 41.1 0.10 1 992 . 140 ILE N N 122.2 0.10 1 993 . 141 GLN H H 8.38 0.02 1 994 . 141 GLN HA H 4.96 0.02 1 995 . 141 GLN HB2 H 1.77 0.02 1 996 . 141 GLN HB3 H 1.77 0.02 1 997 . 141 GLN C C 174.6 0.10 1 998 . 141 GLN CA C 55.3 0.10 1 999 . 141 GLN CB C 31.5 0.10 1 1000 . 141 GLN N N 125.7 0.10 1 1001 . 142 LEU H H 8.66 0.02 1 1002 . 142 LEU HA H 4.77 0.02 1 1003 . 142 LEU HB2 H 1.05 0.02 2 1004 . 142 LEU C C 174.6 0.10 1 1005 . 142 LEU CA C 53.2 0.10 1 1006 . 142 LEU CB C 46.0 0.10 1 1007 . 142 LEU N N 124.0 0.10 1 1008 . 143 ARG H H 8.63 0.02 1 1009 . 143 ARG HA H 4.96 0.02 1 1010 . 143 ARG HB2 H 1.77 0.02 1 1011 . 143 ARG HB3 H 1.77 0.02 1 1012 . 143 ARG C C 175.3 0.10 1 1013 . 143 ARG CA C 55.3 0.10 1 1014 . 143 ARG CB C 30.5 0.10 1 1015 . 143 ARG N N 124.4 0.10 1 1016 . 144 LEU H H 8.70 0.02 1 1017 . 144 LEU HA H 5.61 0.02 1 1018 . 144 LEU HB2 H 1.71 0.02 1 1019 . 144 LEU HB3 H 1.71 0.02 1 1020 . 144 LEU C C 175.4 0.10 1 1021 . 144 LEU CA C 53.4 0.10 1 1022 . 144 LEU CB C 47.2 0.10 1 1023 . 144 LEU N N 123.7 0.10 1 1024 . 145 LYS H H 8.53 0.02 1 1025 . 145 LYS HA H 5.74 0.02 1 1026 . 145 LYS HB2 H 1.71 0.02 1 1027 . 145 LYS HB3 H 1.71 0.02 1 1028 . 145 LYS C C 176.9 0.10 1 1029 . 145 LYS CA C 54.2 0.10 1 1030 . 145 LYS CB C 37.2 0.10 1 1031 . 145 LYS N N 120.4 0.10 1 1032 . 146 GLY H H 8.81 0.02 1 1033 . 146 GLY HA2 H 4.05 0.02 2 1034 . 146 GLY HA3 H 3.53 0.02 2 1035 . 146 GLY C C 175.0 0.10 1 1036 . 146 GLY CA C 46.3 0.10 1 1037 . 146 GLY N N 110.4 0.10 1 1038 . 147 TYR H H 9.71 0.02 1 1039 . 147 TYR HA H 4.35 0.02 1 1040 . 147 TYR HB2 H 3.81 0.02 2 1041 . 147 TYR HB3 H 3.12 0.02 2 1042 . 147 TYR CA C 63.2 0.10 1 1043 . 147 TYR CB C 36.0 0.10 1 1044 . 147 TYR N N 125.5 0.10 1 1045 . 148 PRO HA H 3.66 0.02 1 1046 . 148 PRO HB2 H 1.38 0.02 2 1047 . 148 PRO HB3 H 1.12 0.02 2 1048 . 148 PRO C C 178.2 0.10 1 1049 . 148 PRO CA C 65.9 0.10 1 1050 . 148 PRO CB C 30.4 0.10 1 1051 . 149 ALA H H 6.54 0.02 1 1052 . 149 ALA HA H 3.72 0.02 1 1053 . 149 ALA HB H 1.19 0.02 1 1054 . 149 ALA C C 181.0 0.10 1 1055 . 149 ALA CA C 55.3 0.10 1 1056 . 149 ALA CB C 17.4 0.10 1 1057 . 149 ALA N N 116.6 0.10 1 1058 . 150 ILE H H 8.13 0.02 1 1059 . 150 ILE HA H 3.40 0.02 1 1060 . 150 ILE HB H 1.84 0.02 1 1061 . 150 ILE C C 176.6 0.10 1 1062 . 150 ILE CA C 66.4 0.10 1 1063 . 150 ILE CB C 37.2 0.10 1 1064 . 150 ILE N N 123.7 0.10 1 1065 . 151 VAL H H 7.73 0.02 1 1066 . 151 VAL HA H 3.40 0.02 1 1067 . 151 VAL HB H 1.64 0.02 1 1068 . 151 VAL C C 178.8 0.10 1 1069 . 151 VAL CA C 66.7 0.10 1 1070 . 151 VAL CB C 32.0 0.10 1 1071 . 151 VAL N N 119.5 0.10 1 1072 . 152 PHE H H 8.26 0.02 1 1073 . 152 PHE HA H 3.79 0.02 1 1074 . 152 PHE HB2 H 2.94 0.02 2 1075 . 152 PHE HB3 H 2.49 0.02 2 1076 . 152 PHE C C 178.7 0.10 1 1077 . 152 PHE CA C 63.3 0.10 1 1078 . 152 PHE CB C 39.3 0.10 1 1079 . 152 PHE N N 114.9 0.10 1 1080 . 153 GLN H H 7.91 0.02 1 1081 . 153 GLN HA H 3.92 0.02 1 1082 . 153 GLN HB2 H 2.29 0.02 2 1083 . 153 GLN HB3 H 2.16 0.02 2 1084 . 153 GLN C C 177.2 0.10 1 1085 . 153 GLN CA C 60.2 0.10 1 1086 . 153 GLN CB C 30.7 0.10 1 1087 . 153 GLN N N 116.4 0.10 1 1088 . 154 HIS H H 8.39 0.02 1 1089 . 154 HIS HA H 4.05 0.02 1 1090 . 154 HIS HB2 H 3.66 0.02 1 1091 . 154 HIS HB3 H 3.14 0.02 1 1092 . 154 HIS C C 178.2 0.10 1 1093 . 154 HIS CA C 59.6 0.10 1 1094 . 154 HIS CB C 28.0 0.10 1 1095 . 154 HIS N N 119.7 0.10 1 1096 . 155 GLU H H 8.31 0.02 1 1097 . 155 GLU HA H 4.70 0.02 1 1098 . 155 GLU C C 179.1 0.10 1 1099 . 155 GLU CA C 59.1 0.10 1 1100 . 155 GLU CB C 29.3 0.10 1 1101 . 155 GLU N N 117.5 0.10 1 1102 . 156 ILE H H 8.75 0.02 1 1103 . 156 ILE HA H 3.53 0.02 1 1104 . 156 ILE HB H 1.90 0.02 1 1105 . 156 ILE C C 178.8 0.10 1 1106 . 156 ILE CA C 66.9 0.10 1 1107 . 156 ILE CB C 37.6 0.10 1 1108 . 156 ILE N N 120.0 0.10 1 1109 . 157 ASP H H 8.35 0.02 1 1110 . 157 ASP HA H 4.46 0.02 1 1111 . 157 ASP HB2 H 3.06 0.02 2 1112 . 157 ASP HB3 H 2.42 0.02 2 1113 . 157 ASP C C 180.7 0.10 1 1114 . 157 ASP CA C 57.2 0.10 1 1115 . 157 ASP CB C 38.9 0.10 1 1116 . 157 ASP N N 120.3 0.10 1 1117 . 158 HIS H H 7.38 0.02 1 1118 . 158 HIS HA H 4.78 0.02 1 1119 . 158 HIS HB2 H 2.62 0.02 1 1120 . 158 HIS HB3 H 2.62 0.02 1 1121 . 158 HIS C C 180.2 0.10 1 1122 . 158 HIS CA C 59.2 0.10 1 1123 . 158 HIS CB C 29.4 0.10 1 1124 . 158 HIS N N 114.4 0.10 1 1125 . 159 LEU H H 8.17 0.02 1 1126 . 159 LEU HA H 4.11 0.02 1 1127 . 159 LEU HB2 H 1.43 0.02 1 1128 . 159 LEU HB3 H 1.43 0.02 1 1129 . 159 LEU C C 176.0 0.10 1 1130 . 159 LEU CA C 56.2 0.10 1 1131 . 159 LEU CB C 40.2 0.10 1 1132 . 159 LEU N N 116.2 0.10 1 1133 . 160 ASN H H 7.69 0.10 1 1134 . 160 ASN HA H 5.16 0.10 1 1135 . 160 ASN HB2 H 3.27 0.02 2 1136 . 160 ASN HB3 H 2.75 0.02 2 1137 . 160 ASN C C 174.5 0.02 1 1138 . 160 ASN CA C 51.8 0.10 1 1139 . 160 ASN CB C 39.9 0.10 1 1140 . 160 ASN N N 115.8 0.10 1 1141 . 161 GLY H H 7.63 0.02 1 1142 . 161 GLY HA2 H 4.11 0.02 2 1143 . 161 GLY HA3 H 3.59 0.02 2 1144 . 161 GLY C C 173.2 0.10 1 1145 . 161 GLY CA C 46.9 0.10 1 1146 . 161 GLY N N 108.7 0.10 1 1147 . 162 VAL H H 7.64 0.02 1 1148 . 162 VAL HA H 3.72 0.02 1 1149 . 162 VAL HB H 1.63 0.02 1 1150 . 162 VAL C C 175.0 0.10 1 1151 . 162 VAL CA C 62.5 0.10 1 1152 . 162 VAL CB C 34.2 0.10 1 1153 . 162 VAL N N 120.6 0.10 1 1154 . 163 MET H H 7.51 0.02 1 1155 . 163 MET C C 178.8 0.10 1 1156 . 163 MET CA C 51.3 0.10 1 1157 . 163 MET CB C 33.5 0.10 1 1158 . 163 MET N N 124.4 0.10 1 1159 . 164 PHE H H 8.39 0.02 1 1160 . 164 PHE C C 175.4 0.10 1 1161 . 164 PHE CA C 60.6 0.10 1 1162 . 164 PHE CB C 33.5 0.10 1 1163 . 164 PHE N N 118.0 0.10 1 1164 . 165 TYR H H 5.06 0.02 1 1165 . 165 TYR HA H 3.98 0.02 1 1166 . 165 TYR HB2 H 3.01 0.02 1 1167 . 165 TYR HB3 H 3.01 0.02 1 1168 . 165 TYR C C 177.1 0.10 1 1169 . 165 TYR CA C 56.0 0.10 1 1170 . 165 TYR N N 112.2 0.10 1 1171 . 166 ASP H H 7.58 0.02 1 1172 . 166 ASP HA H 4.18 0.02 1 1173 . 166 ASP HB2 H 2.49 0.02 1 1174 . 166 ASP HB3 H 2.49 0.02 1 1175 . 166 ASP C C 177.3 0.10 1 1176 . 166 ASP CA C 56.5 0.10 1 1177 . 166 ASP CB C 40.2 0.10 1 1178 . 166 ASP N N 126.6 0.10 1 1179 . 167 HIS H H 7.19 0.02 1 1180 . 167 HIS HA H 4.57 0.02 1 1181 . 167 HIS HB2 H 3.46 0.02 1 1182 . 167 HIS HB3 H 3.46 0.02 1 1183 . 167 HIS C C 176.2 0.10 1 1184 . 167 HIS CA C 55.7 0.10 1 1185 . 167 HIS CB C 33.2 0.10 1 1186 . 167 HIS N N 113.3 0.10 1 1187 . 168 ILE H H 7.20 0.02 1 1188 . 168 ILE HA H 3.98 0.02 1 1189 . 168 ILE HB H 1.77 0.02 1 1190 . 168 ILE C C 176.2 0.10 1 1191 . 168 ILE CA C 62.5 0.10 1 1192 . 168 ILE CB C 39.0 0.10 1 1193 . 168 ILE N N 121.3 0.10 1 1194 . 169 ASP H H 9.21 0.02 1 1195 . 169 ASP HA H 4.50 0.02 1 1196 . 169 ASP HB2 H 2.81 0.02 1 1197 . 169 ASP HB3 H 2.68 0.02 1 1198 . 169 ASP C C 176.2 0.10 1 1199 . 169 ASP CA C 54.5 0.10 1 1200 . 169 ASP CB C 42.1 0.10 1 1201 . 169 ASP N N 131.0 0.10 1 1202 . 170 LYS H H 8.38 0.02 1 1203 . 170 LYS HA H 3.98 0.02 1 1204 . 170 LYS HB2 H 1.84 0.02 1 1205 . 170 LYS HB3 H 1.84 0.02 1 1206 . 170 LYS C C 177.6 0.10 1 1207 . 170 LYS CA C 58.4 0.10 1 1208 . 170 LYS CB C 32.3 0.10 1 1209 . 170 LYS N N 123.5 0.10 1 1210 . 171 ASP H H 8.10 0.02 1 1211 . 171 ASP HA H 4.57 0.02 1 1212 . 171 ASP HB2 H 2.49 0.02 2 1213 . 171 ASP HB3 H 2.16 0.02 2 1214 . 171 ASP C C 176.3 0.10 1 1215 . 171 ASP CA C 56.0 0.10 1 1216 . 171 ASP CB C 41.8 0.10 1 1217 . 171 ASP N N 117.1 0.10 1 1218 . 172 HIS H H 8.08 0.02 1 1219 . 172 HIS CA C 53.3 0.10 1 1220 . 172 HIS CB C 29.2 0.10 1 1221 . 172 HIS N N 116.2 0.10 1 1222 . 173 PRO HA H 4.64 0.02 1 1223 . 173 PRO HB2 H 2.48 0.02 1 1224 . 173 PRO HB3 H 2.48 0.02 1 1225 . 173 PRO C C 177.3 0.10 1 1226 . 173 PRO CA C 65.7 0.10 1 1227 . 173 PRO CB C 32.6 0.10 1 1228 . 174 LEU H H 8.45 0.02 1 1229 . 174 LEU HA H 4.70 0.02 1 1230 . 174 LEU HB2 H 2.29 0.02 2 1231 . 174 LEU HB3 H 1.70 0.02 2 1232 . 174 LEU C C 175.8 0.10 1 1233 . 174 LEU CA C 53.3 0.10 1 1234 . 174 LEU CB C 41.5 0.10 1 1235 . 174 LEU N N 116.0 0.10 1 1236 . 175 GLN H H 7.11 0.02 1 1237 . 175 GLN CA C 52.7 0.10 1 1238 . 175 GLN CB C 30.8 0.10 1 1239 . 175 GLN N N 121.1 0.10 1 1240 . 176 PRO HA H 4.44 0.02 1 1241 . 176 PRO HB2 H 1.77 0.02 2 1242 . 176 PRO C C 178.1 0.10 1 1243 . 176 PRO CA C 61.5 0.10 1 1244 . 176 PRO CB C 32.5 0.10 1 1245 . 177 HIS H H 10.13 0.02 1 1246 . 177 HIS CA C 53.3 0.10 1 1247 . 177 HIS CB C 28.6 0.10 1 1248 . 177 HIS N N 124.4 0.10 1 1249 . 178 THR HA H 3.98 0.02 1 1250 . 178 THR C C 173.9 0.10 1 1251 . 179 ASP H H 8.94 0.02 1 1252 . 179 ASP HA H 4.63 0.02 1 1253 . 179 ASP HB2 H 3.01 0.02 2 1254 . 179 ASP HB3 H 2.88 0.02 2 1255 . 179 ASP C C 175.2 0.10 1 1256 . 179 ASP CA C 55.6 0.10 1 1257 . 179 ASP CB C 39.8 0.10 1 1258 . 179 ASP N N 120.2 0.10 1 1259 . 180 ALA H H 7.73 0.02 1 1260 . 180 ALA HA H 4.77 0.02 1 1261 . 180 ALA HB H 1.64 0.02 1 1262 . 180 ALA C C 177.1 0.10 1 1263 . 180 ALA CA C 51.4 0.10 1 1264 . 180 ALA CB C 21.6 0.10 1 1265 . 180 ALA N N 122.2 0.10 1 1266 . 181 VAL H H 8.93 0.02 1 1267 . 181 VAL HA H 4.18 0.02 1 1268 . 181 VAL HB H 2.05 0.02 1 1269 . 181 VAL C C 174.0 0.10 1 1270 . 181 VAL CA C 61.5 0.10 1 1271 . 181 VAL CB C 33.6 0.10 1 1272 . 181 VAL N N 121.7 0.10 1 1273 . 182 GLU H H 8.29 0.02 1 1274 . 182 GLU HA H 3.30 0.02 1 1275 . 182 GLU HB2 H 1.87 0.02 1 1276 . 182 GLU HB3 H 1.87 0.02 1 1277 . 182 GLU C C 175.9 0.02 1 1278 . 182 GLU CA C 55.3 0.02 1 1279 . 182 GLU CB C 30.5 0.02 1 1280 . 182 GLU N N 126.6 0.10 1 1281 . 183 VAL H H 8.01 0.02 1 1282 . 183 VAL C C 179.3 0.10 1 1283 . 183 VAL CA C 61.6 0.10 1 1284 . 183 VAL CB C 32.8 0.10 1 1285 . 183 VAL N N 126.7 0.10 1 stop_ save_