data_6433 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific 1HN, 13C and 15N resonance assignments of a novel calcium binding protein from Entamoeba histolytica ; _BMRB_accession_number 6433 _BMRB_flat_file_name bmr6433.str _Entry_type original _Submission_date 2004-12-16 _Accession_date 2004-12-16 _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 Bansal-Mutalik Ritu . . 2 Mustafi Sourajit Mitra . 3 Bhattacharya Alok . . 4 Chary 'V. R.' Kandala . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 479 "13C chemical shifts" 373 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-26 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence specific 1HN, 13C and 15N resonance assignments of a novel calcium-binding protein from Entamoeba histolytica. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15929013 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bansal-Mutalik Ritu . . 2 Mustafi Sourajit Mitra . 3 Bhattacharya Alok . . 4 Chary Kandala V.R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 379 _Page_last 380 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_system_EhCaBP2 _Saveframe_category molecular_system _Mol_system_name 'Entamoeba histolytica calcium binding protein 2' _Abbreviation_common EhCaBP2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EhCaBP2 $EhCaBP2 'CALCIUM (II) ION' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'calcium binding' 'signal transduction' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EhCaBP2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Entamoeba histolytica calcium binding protein' _Abbreviation_common EhCaBP2 _Molecular_mass 14944 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; MAEALFKQLDANGDGSVSYE EVKAFVSSKRPIKNEQLLQL IFKAIDIDGNGEIDLAEFTK FAAAVKEQDLSDEKVGLKIL YKLMDADGDGKLTKEEVTTF FKKFGYEKVVDQIMKADANG DGYITLEEFLAFNL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 GLU 4 ALA 5 LEU 6 PHE 7 LYS 8 GLN 9 LEU 10 ASP 11 ALA 12 ASN 13 GLY 14 ASP 15 GLY 16 SER 17 VAL 18 SER 19 TYR 20 GLU 21 GLU 22 VAL 23 LYS 24 ALA 25 PHE 26 VAL 27 SER 28 SER 29 LYS 30 ARG 31 PRO 32 ILE 33 LYS 34 ASN 35 GLU 36 GLN 37 LEU 38 LEU 39 GLN 40 LEU 41 ILE 42 PHE 43 LYS 44 ALA 45 ILE 46 ASP 47 ILE 48 ASP 49 GLY 50 ASN 51 GLY 52 GLU 53 ILE 54 ASP 55 LEU 56 ALA 57 GLU 58 PHE 59 THR 60 LYS 61 PHE 62 ALA 63 ALA 64 ALA 65 VAL 66 LYS 67 GLU 68 GLN 69 ASP 70 LEU 71 SER 72 ASP 73 GLU 74 LYS 75 VAL 76 GLY 77 LEU 78 LYS 79 ILE 80 LEU 81 TYR 82 LYS 83 LEU 84 MET 85 ASP 86 ALA 87 ASP 88 GLY 89 ASP 90 GLY 91 LYS 92 LEU 93 THR 94 LYS 95 GLU 96 GLU 97 VAL 98 THR 99 THR 100 PHE 101 PHE 102 LYS 103 LYS 104 PHE 105 GLY 106 TYR 107 GLU 108 LYS 109 VAL 110 VAL 111 ASP 112 GLN 113 ILE 114 MET 115 LYS 116 ALA 117 ASP 118 ALA 119 ASN 120 GLY 121 ASP 122 GLY 123 TYR 124 ILE 125 THR 126 LEU 127 GLU 128 GLU 129 PHE 130 LEU 131 ALA 132 PHE 133 ASN 134 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 2JNX "Nmr Derived Solution Structure Of An Ef-Hand Calcium Binding Protein From Entamoeba Histolytica" 100.00 134 100.00 100.00 5.65e-87 DBJ BAA22013 "calmodulin [Entamoeba histolytica]" 64.18 86 98.84 98.84 6.86e-50 GB AAR97975 "calcium binding protein 2 [Entamoeba histolytica]" 100.00 134 100.00 100.00 5.65e-87 GB EAL51694 "calmodulin, putative [Entamoeba histolytica HM-1:IMSS]" 100.00 134 100.00 100.00 5.65e-87 GB EDR27146 "calcium-binding protein, putative [Entamoeba dispar SAW760]" 100.00 134 97.76 99.25 2.47e-85 GB EKE36904 "calmodulin, putative [Entamoeba nuttalli P19]" 100.00 134 97.01 99.25 9.99e-85 GB EMD43571 "EF-Hand calcium binding protein, putative [Entamoeba histolytica KU27]" 100.00 134 100.00 100.00 5.65e-87 REF XP_001736602 "calcium-binding protein [Entamoeba dispar SAW760]" 100.00 134 97.76 99.25 2.47e-85 REF XP_008860769 "calmodulin, putative [Entamoeba nuttalli P19]" 100.00 134 97.01 99.25 9.99e-85 REF XP_657080 "calmodulin [Entamoeba histolytica HM-1:IMSS]" 100.00 134 100.00 100.00 5.65e-87 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _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 15:31:50 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 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 $EhCaBP2 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $EhCaBP2 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EhCaBP2 1.5 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Task 'Data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model . _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_N15_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 HSQC' _Sample_label $sample_1 save_ save_CBCANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 0.1 pH temperature 308 0.2 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 $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name EhCaBP2 _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 . 4 ALA CA C 54.20 0.1 1 2 . 4 ALA CB C 17.03 0.1 1 3 . 4 ALA C C 180.46 0.1 1 4 . 5 LEU N N 119.74 0.1 1 5 . 5 LEU H H 8.03 0.02 1 6 . 5 LEU CA C 56.48 0.1 1 7 . 5 LEU CB C 45.88 0.1 1 8 . 5 LEU C C 174.02 0.1 1 9 . 6 PHE N N 118.81 0.1 1 10 . 6 PHE H H 7.93 0.02 1 11 . 6 PHE CA C 54.32 0.1 1 12 . 6 PHE CB C 45.88 0.1 1 13 . 6 PHE C C 174.05 0.1 1 14 . 7 LYS CA C 58.55 0.1 1 15 . 7 LYS HA H 4.09 0.02 1 16 . 7 LYS CB C 31.90 0.1 1 17 . 7 LYS HB2 H 1.85 0.02 2 18 . 7 LYS HG2 H 1.48 0.02 2 19 . 7 LYS HE2 H 2.99 0.02 2 20 . 7 LYS C C 178.27 0.1 1 21 . 8 GLN N N 116.84 0.1 1 22 . 8 GLN H H 7.30 0.02 1 23 . 8 GLN CA C 57.23 0.1 1 24 . 8 GLN HA H 3.87 0.02 1 25 . 8 GLN CB C 28.04 0.1 1 26 . 8 GLN HB2 H 2.1 0.02 2 27 . 8 GLN HG2 H 2.47 0.02 2 28 . 8 GLN C C 177.65 0.1 1 29 . 9 LEU N N 118.68 0.1 1 30 . 9 LEU H H 7.52 0.02 1 31 . 9 LEU CA C 56.34 0.1 1 32 . 9 LEU HA H 3.57 0.02 1 33 . 9 LEU CB C 42.63 0.1 1 34 . 9 LEU HB2 H 1.27 0.02 2 35 . 9 LEU HG H 1.27 0.02 1 36 . 9 LEU HD1 H 0.86 0.02 2 37 . 9 LEU HD2 H 0.18 0.02 2 38 . 9 LEU C C 178.27 0.1 1 39 . 10 ASP N N 116.73 0.1 1 40 . 10 ASP H H 7.42 0.02 1 41 . 10 ASP CA C 51.56 0.1 1 42 . 10 ASP HA H 4.35 0.02 1 43 . 10 ASP CB C 36.97 0.1 1 44 . 10 ASP HB2 H 2.47 0.02 2 45 . 10 ASP C C 176.45 0.1 1 46 . 11 ALA N N 130.00 0.1 1 47 . 11 ALA H H 7.79 0.02 1 48 . 11 ALA CA C 53.66 0.1 1 49 . 11 ALA HA H 4.34 0.02 1 50 . 11 ALA CB C 18.51 0.1 1 51 . 11 ALA HB H 1.45 0.02 1 52 . 11 ALA C C 178.89 0.1 1 53 . 12 ASN N N 111.34 0.1 1 54 . 12 ASN H H 7.97 0.02 1 55 . 12 ASN CA C 50.81 0.1 1 56 . 12 ASN HA H 4.71 0.02 1 57 . 12 ASN CB C 36.38 0.1 1 58 . 12 ASN HB2 H 2.83 0.02 2 59 . 12 ASN HB3 H 3.25 0.02 2 60 . 12 ASN HD21 H 7.42 0.1 2 61 . 12 ASN C C 176.52 0.1 1 62 . 13 GLY N N 109.44 0.1 1 63 . 13 GLY H H 7.69 0.02 1 64 . 13 GLY CA C 46.60 0.1 1 65 . 13 GLY HA2 H 3.77 0.02 2 66 . 13 GLY C C 174.81 0.1 1 67 . 14 ASP N N 119.01 0.1 1 68 . 14 ASP H H 8.07 0.02 1 69 . 14 ASP CA C 52.69 0.1 1 70 . 14 ASP HA H 4.50 0.02 1 71 . 14 ASP CB C 39.66 0.1 1 72 . 14 ASP HB2 H 3.10 0.02 2 73 . 14 ASP HB3 H 2.36 0.02 2 74 . 14 ASP C C 177.93 0.1 1 75 . 15 GLY N N 114.04 0.1 1 76 . 15 GLY H H 10.53 0.02 1 77 . 15 GLY CA C 45.95 0.1 1 78 . 15 GLY HA2 H 4.30 0.02 2 79 . 15 GLY HA3 H 3.62 0.02 2 80 . 15 GLY C C 173.27 0.1 1 81 . 16 SER N N 114.46 0.1 1 82 . 16 SER H H 7.93 0.02 1 83 . 16 SER CA C 56.20 0.1 1 84 . 16 SER HA H 5.07 0.02 1 85 . 16 SER CB C 65.56 0.1 1 86 . 16 SER HB2 H 3.57 0.02 2 87 . 16 SER C C 172.48 0.1 1 88 . 17 VAL N N 128.09 0.1 1 89 . 17 VAL H H 9.63 0.02 1 90 . 17 VAL CA C 60.42 0.1 1 91 . 17 VAL HA H 4.92 0.02 1 92 . 17 VAL CB C 32.81 0.1 1 93 . 17 VAL HB H 1.85 0.02 1 94 . 17 VAL HG1 H 0.81 0.02 2 95 . 17 VAL C C 175.21 0.1 1 96 . 18 SER N N 125.46 0.1 1 97 . 18 SER H H 9.07 0.02 1 98 . 18 SER CA C 55.48 0.1 1 99 . 18 SER HA H 4.92 0.02 1 100 . 18 SER CB C 65.27 0.1 1 101 . 18 SER HB2 H 2.47 0.02 2 102 . 18 SER C C 175.17 0.1 1 103 . 19 TYR N N 123.07 0.1 1 104 . 19 TYR H H 9.20 0.02 1 105 . 19 TYR CA C 61.68 0.1 1 106 . 19 TYR HA H 3.98 0.02 1 107 . 19 TYR CB C 36.68 0.1 1 108 . 19 TYR HB2 H 2.36 0.02 2 109 . 19 TYR HB3 H 3.36 0.02 2 110 . 19 TYR HD1 H 7.00 0.02 3 111 . 19 TYR HE1 H 6.43 0.02 3 112 . 19 TYR C C 177.08 0.1 1 113 . 20 GLU N N 117.20 0.1 1 114 . 20 GLU H H 8.48 0.02 1 115 . 20 GLU CA C 59.01 0.1 1 116 . 20 GLU HA H 4.03 0.02 1 117 . 20 GLU CB C 27.74 0.1 1 118 . 20 GLU HB2 H 1.95 0.02 2 119 . 20 GLU HG2 H 2.37 0.02 2 120 . 20 GLU HG3 H 2.16 0.02 2 121 . 20 GLU C C 179.81 0.1 1 122 . 21 GLU N N 120.44 0.1 1 123 . 21 GLU H H 7.75 0.02 1 124 . 21 GLU CA C 58.81 0.1 1 125 . 21 GLU HA H 3.98 0.02 1 126 . 21 GLU CB C 27.74 0.1 1 127 . 21 GLU HB2 H 2.48 0.02 2 128 . 21 GLU HB3 H 2.51 0.02 2 129 . 21 GLU HG2 H 1.48 0.02 2 130 . 21 GLU C C 180.45 0.1 1 131 . 22 VAL N N 121.98 0.1 1 132 . 22 VAL H H 8.06 0.02 1 133 . 22 VAL CA C 66.51 0.1 1 134 . 22 VAL HA H 3.51 0.02 1 135 . 22 VAL CB C 31.90 0.1 1 136 . 22 VAL HB H 2.16 0.02 1 137 . 22 VAL HG1 H 0.91 0.02 2 138 . 22 VAL C C 176.99 0.1 1 139 . 23 LYS N N 120.54 0.1 1 140 . 23 LYS H H 8.60 0.02 1 141 . 23 LYS CA C 58.78 0.1 1 142 . 23 LYS HA H 4.60 0.02 1 143 . 23 LYS CB C 31.62 0.1 1 144 . 23 LYS HB2 H 1.48 0.02 2 145 . 23 LYS HG2 H 1.07 0.02 2 146 . 23 LYS HE2 H 3.51 0.02 2 147 . 23 LYS C C 178.77 0.1 1 148 . 24 ALA N N 121.87 0.1 1 149 . 24 ALA H H 8.21 0.02 1 150 . 24 ALA CA C 54.33 0.1 1 151 . 24 ALA HA H 3.98 0.02 1 152 . 24 ALA CB C 17.92 0.1 1 153 . 24 ALA HB H 1.43 0.02 1 154 . 24 ALA C C 179.72 0.1 1 155 . 25 PHE N N 118.41 0.1 1 156 . 25 PHE H H 7.70 0.02 1 157 . 25 PHE CA C 58.58 0.1 1 158 . 25 PHE HA H 4.19 0.02 1 159 . 25 PHE CB C 39.68 0.1 1 160 . 25 PHE HB2 H 3.06 0.02 2 161 . 25 PHE HB3 H 3.36 0.02 2 162 . 25 PHE C C 180.45 0.1 1 163 . 26 VAL N N 122.23 0.1 1 164 . 26 VAL H H 8.03 0.02 1 165 . 26 VAL CA C 66.51 0.1 1 166 . 26 VAL CB C 29.98 0.1 1 167 . 26 VAL C C 177.70 0.1 1 168 . 27 SER N N 112.79 0.1 1 169 . 27 SER H H 8.40 0.02 1 170 . 27 SER CA C 59.90 0.1 1 171 . 27 SER HA H 4.76 0.02 1 172 . 27 SER CB C 61.99 0.1 1 173 . 27 SER HB2 H 3.93 0.02 2 174 . 27 SER HB3 H 4.29 0.02 2 175 . 27 SER C C 175.36 0.1 1 176 . 28 SER N N 115.66 0.1 1 177 . 28 SER H H 7.34 0.02 1 178 . 28 SER CA C 59.31 0.1 1 179 . 28 SER HA H 4.20 0.02 1 180 . 28 SER CB C 61.99 0.1 1 181 . 28 SER HB2 H 3.88 0.02 2 182 . 28 SER HB3 H 3.51 0.02 2 183 . 28 SER C C 174.54 0.1 1 184 . 29 LYS N N 120.08 0.1 1 185 . 29 LYS H H 7.59 0.02 1 186 . 29 LYS CA C 54.80 0.1 1 187 . 29 LYS HA H 4.29 0.02 1 188 . 29 LYS CB C 32.51 0.1 1 189 . 29 LYS HB2 H 1.69 0.02 2 190 . 29 LYS HG2 H 1.43 0.02 2 191 . 29 LYS C C 176.24 0.1 1 192 . 30 ARG N N 118.27 0.1 1 193 . 30 ARG H H 8.30 0.02 1 194 . 30 ARG CA C 53.05 0.1 1 195 . 30 ARG HA H 4.66 0.02 1 196 . 30 ARG CB C 28.63 0.1 1 197 . 30 ARG HB2 H 1.95 0.02 2 198 . 30 ARG HG2 H 1.70 0.02 2 199 . 30 ARG HD2 H 2.94 0.02 2 200 . 30 ARG C C 176.48 0.1 1 201 . 31 PRO CA C 61.36 0.1 1 202 . 31 PRO CB C 31.35 0.1 1 203 . 31 PRO C C 177.36 0.1 1 204 . 32 ILE N N 123.54 0.1 1 205 . 32 ILE H H 8.58 0.02 1 206 . 32 ILE CA C 59.95 0.1 1 207 . 32 ILE HA H 4.03 0.02 1 208 . 32 ILE CB C 36.68 0.1 1 209 . 32 ILE HB H 1.85 0.02 2 210 . 32 ILE HG12 H 1.59 0.02 2 211 . 32 ILE HG2 H 0.81 0.02 4 212 . 32 ILE HD1 H 0.96 0.02 4 213 . 32 ILE C C 176.05 0.1 1 214 . 33 LYS N N 129.00 0.1 1 215 . 33 LYS H H 9.19 0.02 1 216 . 33 LYS CA C 56.20 0.1 1 217 . 33 LYS CB C 32.51 0.1 1 218 . 33 LYS C C 176.77 0.1 1 219 . 34 ASN N N 119.49 0.1 1 220 . 34 ASN H H 8.56 0.02 1 221 . 34 ASN CA C 50.57 0.1 1 222 . 34 ASN CB C 38.15 0.1 1 223 . 34 ASN C C 174.83 0.1 1 224 . 35 GLU N N 125.50 0.1 1 225 . 35 GLU H H 8.99 0.02 1 226 . 35 GLU CA C 58.54 0.1 1 227 . 35 GLU HA H 4.61 0.02 1 228 . 35 GLU CB C 28.05 0.1 1 229 . 35 GLU HB2 H 2.00 0.02 2 230 . 35 GLU HG2 H 3.77 0.02 2 231 . 35 GLU C C 177.58 0.1 1 232 . 36 GLN N N 118.50 0.1 1 233 . 36 GLN H H 8.38 0.02 1 234 . 36 GLN CA C 58.71 0.1 1 235 . 36 GLN HA H 4.04 0.02 1 236 . 36 GLN CB C 28.04 0.1 1 237 . 36 GLN HB2 H 2.36 0.02 2 238 . 36 GLN HG2 H 2.06 0.02 2 239 . 36 GLN C C 178.58 0.1 1 240 . 37 LEU N N 119.48 0.1 1 241 . 37 LEU H H 7.48 0.02 1 242 . 37 LEU CA C 56.93 0.1 1 243 . 37 LEU HA H 4.04 0.02 1 244 . 37 LEU CB C 40.85 0.1 1 245 . 37 LEU HB2 H 1.53 0.02 2 246 . 37 LEU HG H 1.53 0.02 1 247 . 37 LEU HD1 H 0.91 0.02 2 248 . 37 LEU C C 177.83 0.1 1 249 . 38 LEU N N 119.12 0.1 1 250 . 38 LEU H H 7.15 0.02 1 251 . 38 LEU CA C 56.93 0.1 1 252 . 38 LEU HA H 4.08 0.02 1 253 . 38 LEU CB C 40.85 0.1 1 254 . 38 LEU HB2 H 2.36 0.02 2 255 . 38 LEU HG H 1.90 0.02 1 256 . 38 LEU HD1 H 0.91 0.02 2 257 . 38 LEU C C 178.08 0.1 1 258 . 39 GLN N N 117.32 0.1 1 259 . 39 GLN H H 8.47 0.02 1 260 . 39 GLN CA C 59.00 0.1 1 261 . 39 GLN HA H 3.57 0.02 1 262 . 39 GLN CB C 27.74 0.1 1 263 . 39 GLN HB2 H 1.95 0.02 2 264 . 39 GLN HG2 H 2.36 0.02 2 265 . 39 GLN HE21 H 6.40 0.1 2 266 . 39 GLN C C 178.23 0.1 1 267 . 40 LEU N N 120.08 0.1 1 268 . 40 LEU H H 7.89 0.02 1 269 . 40 LEU CA C 57.22 0.1 1 270 . 40 LEU HA H 3.82 0.02 1 271 . 40 LEU CB C 41.44 0.1 1 272 . 40 LEU HB2 H 1.74 0.02 2 273 . 40 LEU HG H 1.48 0.02 1 274 . 40 LEU HD1 H 0.86 0.02 2 275 . 40 LEU C C 177.75 0.1 1 276 . 41 ILE N N 117.57 0.1 1 277 . 41 ILE H H 8.08 0.02 1 278 . 41 ILE CA C 65.11 0.1 1 279 . 41 ILE CB C 37.58 0.1 1 280 . 41 ILE HB H 1.95 0.02 1 281 . 41 ILE HG2 H 0.81 0.02 4 282 . 41 ILE HD1 H 0.81 0.02 4 283 . 41 ILE C C 176.55 0.1 1 284 . 42 PHE N N 118.52 0.1 1 285 . 42 PHE H H 8.47 0.02 1 286 . 42 PHE CA C 62.29 0.1 1 287 . 42 PHE HA H 4.14 0.02 1 288 . 42 PHE CB C 39.96 0.1 1 289 . 42 PHE C C 176.71 0.1 1 290 . 43 LYS N N 116.38 0.1 1 291 . 43 LYS H H 8.09 0.02 1 292 . 43 LYS CA C 58.31 0.1 1 293 . 43 LYS HA H 4.20 0.02 1 294 . 43 LYS CB C 31.90 0.1 1 295 . 43 LYS HB2 H 2.11 0.02 2 296 . 43 LYS HG2 H 1.48 0.02 2 297 . 43 LYS HG3 H 1.12 0.02 2 298 . 43 LYS HD2 H 1.60 0.02 2 299 . 43 LYS C C 176.81 0.1 1 300 . 44 ALA N N 119.24 0.1 1 301 . 44 ALA H H 7.78 0.02 1 302 . 44 ALA CA C 52.92 0.1 1 303 . 44 ALA HA H 3.67 0.02 1 304 . 44 ALA CB C 18.81 0.1 1 305 . 44 ALA HB H 1.43 0.02 1 306 . 44 ALA C C 178.31 0.1 1 307 . 45 ILE N N 117.13 0.1 1 308 . 45 ILE H H 7.52 0.02 1 309 . 45 ILE CA C 57.14 0.1 1 310 . 45 ILE CB C 40.48 0.1 1 311 . 45 ILE C C 178.91 0.1 1 312 . 46 ASP N N 120.20 0.1 1 313 . 46 ASP H H 7.37 0.02 1 314 . 46 ASP CA C 51.78 0.1 1 315 . 46 ASP HA H 4.30 0.02 1 316 . 46 ASP CB C 37.88 0.1 1 317 . 46 ASP HB2 H 2.88 0.02 2 318 . 46 ASP HB3 H 3.25 0.02 2 319 . 46 ASP C C 176.48 0.1 1 320 . 47 ILE N N 125.70 0.1 1 321 . 47 ILE H H 7.92 0.02 1 322 . 47 ILE CA C 63.48 0.1 1 323 . 47 ILE HA H 3.72 0.02 1 324 . 47 ILE CB C 37.27 0.1 1 325 . 47 ILE HB H 1.95 0.02 1 326 . 47 ILE HG12 H 1.64 0.02 2 327 . 47 ILE HG13 H 1.38 0.02 2 328 . 47 ILE HG2 H 0.91 0.02 4 329 . 47 ILE HD1 H 0.91 0.02 4 330 . 47 ILE C C 178.17 0.1 1 331 . 48 ASP N N 115.42 0.1 1 332 . 48 ASP H H 8.13 0.02 1 333 . 48 ASP CA C 52.69 0.1 1 334 . 48 ASP HA H 4.50 0.02 1 335 . 48 ASP CB C 38.77 0.1 1 336 . 48 ASP HB2 H 3.05 0.02 2 337 . 48 ASP HB3 H 2.63 0.02 2 338 . 48 ASP C C 177.93 0.1 1 339 . 49 GLY N N 108.84 0.1 1 340 . 49 GLY H H 7.89 0.02 1 341 . 49 GLY CA C 46.12 0.1 1 342 . 49 GLY HA2 H 3.83 0.02 2 343 . 49 GLY C C 175.11 0.1 1 344 . 50 ASN N N 118.88 0.1 1 345 . 50 ASN H H 8.21 0.02 1 346 . 50 ASN CA C 51.78 0.1 1 347 . 50 ASN HA H 4.61 0.02 1 348 . 50 ASN CB C 36.68 0.1 1 349 . 50 ASN HB2 H 2.62 0.02 2 350 . 50 ASN HB3 H 3.31 0.02 2 351 . 50 ASN HD21 H 6.95 0.1 2 352 . 50 ASN C C 176.46 0.1 1 353 . 51 GLY N N 113.50 0.1 1 354 . 51 GLY H H 10.75 0.02 1 355 . 51 GLY CA C 44.72 0.1 1 356 . 51 GLY HA2 H 3.67 0.02 2 357 . 51 GLY HA3 H 4.30 0.02 2 358 . 51 GLY C C 173.09 0.1 1 359 . 52 GLU N N 115.82 0.1 1 360 . 52 GLU H H 7.62 0.02 1 361 . 52 GLU CA C 52.45 0.1 1 362 . 52 GLU HA H 4.97 0.02 1 363 . 52 GLU CB C 31.62 0.1 1 364 . 52 GLU HB2 H 2.21 0.02 2 365 . 52 GLU HG2 H 1.74 0.02 2 366 . 52 GLU HG3 H 1.84 0.02 2 367 . 52 GLU C C 174.24 0.1 1 368 . 53 ILE N N 127.13 0.1 1 369 . 53 ILE H H 9.81 0.02 1 370 . 53 ILE CA C 59.31 0.1 1 371 . 53 ILE HA H 3.77 0.02 1 372 . 53 ILE CB C 41.62 0.1 1 373 . 53 ILE HB H 1.95 0.02 1 374 . 53 ILE HG12 H 1.07 0.02 2 375 . 53 ILE HG2 H 1.07 0.02 4 376 . 53 ILE HD1 H 0.28 0.02 4 377 . 53 ILE C C 175.86 0.1 1 378 . 54 ASP N N 128.32 0.1 1 379 . 54 ASP H H 8.78 0.02 1 380 . 54 ASP CA C 51.04 0.1 1 381 . 54 ASP HA H 5.23 0.02 1 382 . 54 ASP CB C 41.44 0.1 1 383 . 54 ASP HB2 H 2.21 0.02 2 384 . 54 ASP HB3 H 2.52 0.02 2 385 . 54 ASP C C 176.20 0.1 1 386 . 55 LEU N N 120.43 0.1 1 387 . 55 LEU H H 8.47 0.02 1 388 . 55 LEU CA C 57.37 0.1 1 389 . 55 LEU HA H 3.25 0.02 1 390 . 55 LEU CB C 40.23 0.1 1 391 . 55 LEU HB2 H 2.73 0.02 2 392 . 55 LEU HG H 1.38 0.02 1 393 . 55 LEU HD1 H 1.17 0.02 2 394 . 55 LEU HD2 H 0.70 0.02 2 395 . 55 LEU C C 179.35 0.1 1 396 . 56 ALA N N 124.99 0.1 1 397 . 56 ALA H H 8.25 0.02 1 398 . 56 ALA CA C 54.84 0.1 1 399 . 56 ALA HA H 4.03 0.02 1 400 . 56 ALA CB C 17.62 0.1 1 401 . 56 ALA HB H 1.43 0.02 1 402 . 56 ALA C C 181.43 0.1 1 403 . 57 GLU N N 120.19 0.1 1 404 . 57 GLU H H 8.78 0.02 1 405 . 57 GLU CA C 58.08 0.1 1 406 . 57 GLU HA H 3.98 0.02 2 407 . 57 GLU CB C 28.94 0.1 1 408 . 57 GLU HB2 H 2.26 0.02 2 409 . 57 GLU HG2 H 2.94 0.02 2 410 . 57 GLU C C 177.59 0.1 1 411 . 58 PHE N N 117.09 0.1 1 412 . 58 PHE H H 8.75 0.02 1 413 . 58 PHE CA C 54.38 0.1 1 414 . 58 PHE CB C 42.04 0.1 1 415 . 58 PHE C C 178.37 0.1 1 416 . 59 THR N N 116.85 0.1 1 417 . 59 THR H H 8.76 0.02 1 418 . 59 THR CA C 59.08 0.1 1 419 . 59 THR CB C 64.98 0.1 1 420 . 59 THR C C 176.08 0.1 1 421 . 61 PHE CA C 62.36 0.1 1 422 . 61 PHE CB C 37.28 0.1 1 423 . 61 PHE C C 177.28 0.1 1 424 . 62 ALA N N 118.76 0.1 1 425 . 62 ALA H H 7.32 0.02 1 426 . 62 ALA CA C 52.92 0.1 1 427 . 62 ALA HA H 4.20 0.02 1 428 . 62 ALA CB C 18.21 0.1 1 429 . 62 ALA HB H 1.38 0.02 1 430 . 62 ALA C C 178.68 0.1 1 431 . 63 ALA N N 118.77 0.1 1 432 . 63 ALA H H 7.31 0.02 1 433 . 63 ALA CA C 52.76 0.1 1 434 . 63 ALA HA H 4.20 0.02 1 435 . 63 ALA CB C 18.21 0.1 1 436 . 63 ALA HB H 1.38 0.02 1 437 . 63 ALA C C 179.25 0.1 1 438 . 64 ALA N N 116.86 0.1 1 439 . 64 ALA H H 7.58 0.02 1 440 . 64 ALA CA C 62.06 0.1 1 441 . 64 ALA CB C 18.81 0.1 1 442 . 64 ALA C C 176.72 0.1 1 443 . 65 VAL N N 114.94 0.1 1 444 . 65 VAL H H 8.87 0.02 1 445 . 65 VAL CA C 66.51 0.1 1 446 . 65 VAL HA H 3.61 0.02 1 447 . 65 VAL HB H 2.23 0.02 1 448 . 65 VAL HG1 H 1.17 0.02 2 449 . 65 VAL C C 176.42 0.1 1 450 . 66 LYS N N 122.09 0.1 1 451 . 66 LYS H H 7.57 0.02 1 452 . 66 LYS CA C 58.71 0.1 1 453 . 66 LYS HA H 3.98 0.02 1 454 . 66 LYS CB C 31.91 0.1 1 455 . 66 LYS HB2 H 1.89 0.02 2 456 . 66 LYS HG2 H 1.53 0.02 2 457 . 66 LYS HG3 H 1.38 0.02 2 458 . 66 LYS HE2 H 2.94 0.02 2 459 . 66 LYS C C 176.08 0.1 1 460 . 69 ASP N N 123.50 0.1 1 461 . 69 ASP H H 8.40 0.02 1 462 . 69 ASP CA C 54.55 0.1 1 463 . 69 ASP HA H 4.35 0.02 1 464 . 69 ASP CB C 45.88 0.1 1 465 . 69 ASP HB2 H 2.15 0.02 2 466 . 69 ASP C C 175.21 0.1 1 467 . 70 LEU N N 119.74 0.1 1 468 . 70 LEU H H 8.03 0.02 1 469 . 70 LEU CA C 56.48 0.1 1 470 . 70 LEU CB C 39.68 0.1 1 471 . 70 LEU C C 176.40 0.1 1 472 . 71 SER N N 112.76 0.1 1 473 . 71 SER H H 8.43 0.02 1 474 . 71 SER CA C 58.54 0.1 1 475 . 71 SER HA H 4.35 0.02 1 476 . 71 SER CB C 62.29 0.1 1 477 . 71 SER HB2 H 3.93 0.02 2 478 . 71 SER C C 174.22 0.1 1 479 . 72 ASP N N 123.42 0.1 1 480 . 72 ASP H H 7.40 0.02 1 481 . 72 ASP CA C 52.92 0.1 1 482 . 72 ASP HA H 4.45 0.02 1 483 . 72 ASP CB C 40.80 0.1 1 484 . 72 ASP HB2 H 2.99 0.02 2 485 . 72 ASP HB3 H 2.63 0.02 2 486 . 72 ASP C C 175.81 0.1 1 487 . 73 GLU CA C 58.82 0.1 1 488 . 73 GLU CB C 28.64 0.1 1 489 . 73 GLU C C 175.41 0.1 1 490 . 74 LYS N N 118.44 0.1 1 491 . 74 LYS H H 7.43 0.02 1 492 . 74 LYS CA C 59.08 0.1 1 493 . 74 LYS CB C 31.38 0.1 1 494 . 74 LYS C C 176.77 0.1 1 495 . 75 VAL N N 120.20 0.1 1 496 . 75 VAL H H 7.65 0.02 1 497 . 75 VAL CA C 64.68 0.1 1 498 . 75 VAL CB C 38.18 0.1 1 499 . 75 VAL C C 175.81 0.1 1 500 . 76 GLY N N 108.48 0.1 1 501 . 76 GLY H H 8.76 0.02 1 502 . 76 GLY CA C 47.06 0.1 1 503 . 76 GLY HA2 H 3.67 0.02 2 504 . 76 GLY C C 174.59 0.1 1 505 . 77 LEU N N 120.20 0.1 1 506 . 77 LEU H H 7.73 0.02 1 507 . 77 LEU CA C 56.68 0.1 1 508 . 77 LEU HA H 3.83 0.02 1 509 . 77 LEU CB C 41.74 0.1 1 510 . 77 LEU HB2 H 1.95 0.02 2 511 . 77 LEU HG H 1.69 0.02 1 512 . 77 LEU HD1 H 0.96 0.02 2 513 . 77 LEU C C 174.02 0.1 1 514 . 78 LYS N N 118.77 0.1 1 515 . 78 LYS H H 7.95 0.02 1 516 . 78 LYS CA C 59.95 0.1 1 517 . 78 LYS CB C 33.08 0.1 1 518 . 78 LYS C C 179.31 0.1 1 519 . 79 ILE N N 118.52 0.1 1 520 . 79 ILE H H 8.50 0.02 1 521 . 79 ILE CA C 65.38 0.1 1 522 . 79 ILE CB C 31.02 0.1 1 523 . 79 ILE C C 176.87 0.1 1 524 . 80 LEU N N 119.24 0.1 1 525 . 80 LEU H H 8.20 0.02 1 526 . 80 LEU CA C 57.61 0.1 1 527 . 80 LEU HA H 3.83 0.02 1 528 . 80 LEU CB C 41.15 0.1 1 529 . 80 LEU HB2 H 1.95 0.02 2 530 . 80 LEU HG H 1.69 0.02 1 531 . 80 LEU HD1 H 0.96 0.02 2 532 . 80 LEU C C 177.57 0.1 1 533 . 81 TYR N N 117.81 0.1 1 534 . 81 TYR H H 8.42 0.02 1 535 . 81 TYR CA C 62.06 0.1 1 536 . 81 TYR HA H 3.88 0.02 1 537 . 81 TYR CB C 37.87 0.1 1 538 . 81 TYR HB2 H 2.99 0.02 2 539 . 81 TYR HD1 H 7.00 0.02 3 540 . 81 TYR HE1 H 6.22 0.02 3 541 . 81 TYR C C 176.61 0.1 1 542 . 82 LYS N N 115.89 0.1 1 543 . 82 LYS H H 7.57 0.02 1 544 . 82 LYS CA C 57.55 0.1 1 545 . 82 LYS HA H 4.12 0.02 1 546 . 82 LYS CB C 31.62 0.1 1 547 . 82 LYS HB2 H 1.89 0.02 2 548 . 82 LYS HG2 H 1.64 0.02 2 549 . 82 LYS HE2 H 3.38 0.02 2 550 . 82 LYS C C 179.02 0.1 1 551 . 83 LEU N N 116.61 0.1 1 552 . 83 LEU H H 7.86 0.02 1 553 . 83 LEU CA C 55.73 0.1 1 554 . 83 LEU HA H 3.93 0.02 1 555 . 83 LEU CB C 40.84 0.1 1 556 . 83 LEU HB2 H 1.90 0.02 2 557 . 83 LEU HG H 1.80 0.02 1 558 . 83 LEU HD1 H 1.33 0.02 2 559 . 83 LEU HD2 H 0.86 0.02 2 560 . 83 LEU C C 178.16 0.1 1 561 . 84 MET N N 116.25 0.1 1 562 . 84 MET H H 7.40 0.02 1 563 . 84 MET CA C 57.22 0.1 1 564 . 84 MET HA H 3.46 0.02 1 565 . 84 MET CB C 34.88 0.1 1 566 . 84 MET HB2 H 1.84 0.02 2 567 . 84 MET C C 177.03 0.1 1 568 . 85 ASP N N 118.52 0.1 1 569 . 85 ASP H H 7.64 0.02 1 570 . 85 ASP CA C 52.22 0.1 1 571 . 85 ASP HA H 4.35 0.02 1 572 . 85 ASP CB C 37.27 0.1 1 573 . 85 ASP HB2 H 2.52 0.02 2 574 . 85 ASP C C 177.25 0.1 1 575 . 86 ALA N N 129.28 0.1 1 576 . 86 ALA H H 7.56 0.02 1 577 . 86 ALA CA C 54.47 0.1 1 578 . 86 ALA HA H 4.35 0.02 1 579 . 86 ALA CB C 18.21 0.1 1 580 . 86 ALA HB H 1.43 0.02 1 581 . 86 ALA C C 178.55 0.1 1 582 . 87 ASP N N 113.03 0.1 1 583 . 87 ASP H H 7.79 0.02 1 584 . 87 ASP CA C 51.75 0.1 1 585 . 87 ASP HA H 4.60 0.02 1 586 . 87 ASP CB C 38.77 0.1 1 587 . 87 ASP HB2 H 2.99 0.02 2 588 . 87 ASP HB3 H 2.63 0.02 2 589 . 87 ASP C C 177.70 0.1 1 590 . 88 GLY N N 108.36 0.1 1 591 . 88 GLY H H 7.89 0.02 1 592 . 88 GLY CA C 45.43 0.1 1 593 . 88 GLY HA2 H 3.82 0.02 2 594 . 88 GLY C C 174.85 0.1 1 595 . 89 ASP N N 118.23 0.1 1 596 . 89 ASP H H 8.00 0.02 1 597 . 89 ASP CA C 52.45 0.1 1 598 . 89 ASP HA H 4.40 0.02 1 599 . 89 ASP CB C 39.06 0.1 1 600 . 89 ASP HB2 H 2.36 0.02 2 601 . 89 ASP HB3 H 2.90 0.02 2 602 . 89 ASP C C 177.64 0.1 1 603 . 90 GLY N N 114.04 0.1 1 604 . 90 GLY H H 10.59 0.02 1 605 . 90 GLY CA C 45.66 0.1 1 606 . 90 GLY HA2 H 3.67 0.02 2 607 . 90 GLY HA3 H 3.98 0.02 2 608 . 90 GLY C C 174.07 0.1 1 609 . 91 LYS N N 119.23 0.1 1 610 . 91 LYS H H 7.94 0.02 1 611 . 91 LYS CA C 54.33 0.1 1 612 . 91 LYS HA H 4.24 0.02 1 613 . 91 LYS CB C 33.11 0.1 1 614 . 91 LYS HB2 H 1.64 0.02 2 615 . 91 LYS HG2 H 0.86 0.02 2 616 . 91 LYS HG3 H 0.55 0.02 2 617 . 91 LYS HE2 H 2.32 0.02 2 618 . 91 LYS HZ H 6.27 0.1 1 619 . 91 LYS C C 174.13 0.1 1 620 . 92 LEU N N 127.13 0.1 1 621 . 92 LEU H H 8.47 0.02 1 622 . 92 LEU CA C 52.92 0.1 1 623 . 92 LEU HA H 5.18 0.02 1 624 . 92 LEU CB C 41.74 0.1 1 625 . 92 LEU HB2 H 2.58 0.02 2 626 . 92 LEU HG H 2.58 0.02 1 627 . 92 LEU HD1 H 1.17 0.02 2 628 . 92 LEU C C 176.82 0.1 1 629 . 93 THR N N 116.97 0.1 1 630 . 93 THR H H 8.75 0.02 1 631 . 93 THR CA C 59.01 0.1 1 632 . 93 THR HA H 4.66 0.02 1 633 . 93 THR CB C 70.33 0.1 1 634 . 93 THR HB H 4.66 0.02 1 635 . 93 THR HG2 H 1.27 0.02 4 636 . 93 THR C C 175.13 0.1 1 637 . 94 LYS N N 121.39 0.1 1 638 . 94 LYS H H 9.21 0.02 1 639 . 94 LYS CA C 59.25 0.1 1 640 . 94 LYS HA H 4.20 0.02 1 641 . 94 LYS CB C 31.61 0.1 1 642 . 94 LYS HB2 H 1.85 0.02 2 643 . 94 LYS HG2 H 1.27 0.02 2 644 . 94 LYS HD2 H 1.64 0.02 2 645 . 94 LYS HE2 H 2.73 0.02 2 646 . 94 LYS C C 179.91 0.1 1 647 . 95 GLU N N 121.27 0.1 1 648 . 95 GLU H H 8.73 0.02 1 649 . 95 GLU CA C 59.55 0.1 1 650 . 95 GLU HA H 4.09 0.02 1 651 . 95 GLU CB C 28.05 0.1 1 652 . 95 GLU HB2 H 2.11 0.02 2 653 . 95 GLU HG2 H 2.36 0.02 2 654 . 95 GLU C C 179.08 0.1 1 655 . 96 GLU N N 121.63 0.1 1 656 . 96 GLU H H 7.85 0.02 1 657 . 96 GLU CA C 58.71 0.1 1 658 . 96 GLU HA H 3.98 0.02 1 659 . 96 GLU CB C 28.93 0.1 1 660 . 96 GLU HB2 H 2.47 0.02 2 661 . 96 GLU HG2 H 2.16 0.02 2 662 . 96 GLU C C 180.42 0.1 1 663 . 97 VAL N N 120.91 0.1 1 664 . 97 VAL H H 8.42 0.02 1 665 . 97 VAL CA C 66.28 0.1 1 666 . 97 VAL HA H 3.61 0.02 1 667 . 97 VAL CB C 31.32 0.1 1 668 . 97 VAL HB H 2.20 0.02 1 669 . 97 VAL HG1 H 1.01 0.02 2 670 . 97 VAL C C 177.58 0.1 1 671 . 98 THR N N 115.65 0.1 1 672 . 98 THR H H 8.71 0.02 1 673 . 98 THR CA C 66.51 0.1 1 674 . 98 THR HA H 4.30 0.02 1 675 . 98 THR CB C 67.95 0.1 1 676 . 98 THR HB H 3.93 0.02 1 677 . 98 THR HG2 H 1.22 0.02 4 678 . 98 THR C C 176.08 0.1 1 679 . 99 THR N N 117.08 0.1 1 680 . 99 THR H H 8.42 0.02 1 681 . 99 THR CA C 66.05 0.1 1 682 . 99 THR HA H 4.20 0.02 1 683 . 99 THR CB C 68.24 0.1 1 684 . 99 THR HB H 3.70 0.02 1 685 . 99 THR HG2 H 1.22 0.02 4 686 . 99 THR C C 175.73 0.1 1 687 . 100 PHE N N 120.67 0.1 1 688 . 100 PHE H H 7.65 0.02 1 689 . 100 PHE CA C 60.88 0.1 1 690 . 100 PHE HA H 4.04 0.02 1 691 . 100 PHE CB C 38.17 0.1 1 692 . 100 PHE HB2 H 2.94 0.02 2 693 . 100 PHE HB3 H 2.47 0.02 2 694 . 100 PHE HD1 H 6.48 0.02 3 695 . 100 PHE C C 175.99 0.1 1 696 . 101 PHE N N 113.03 0.1 1 697 . 101 PHE H H 8.14 0.02 1 698 . 101 PHE CA C 61.10 0.1 1 699 . 101 PHE HA H 3.88 0.02 1 700 . 101 PHE CB C 37.87 0.1 1 701 . 101 PHE HB2 H 2.00 0.02 2 702 . 101 PHE C C 179.12 0.1 1 703 . 102 LYS N N 120.91 0.1 1 704 . 102 LYS H H 8.65 0.02 1 705 . 102 LYS CA C 58.71 0.1 1 706 . 102 LYS HA H 4.09 0.02 1 707 . 102 LYS CB C 31.36 0.1 1 708 . 102 LYS HB2 H 1.90 0.02 2 709 . 102 LYS HG2 H 1.53 0.02 2 710 . 102 LYS C C 179.11 0.1 1 711 . 103 LYS N N 118.14 0.1 1 712 . 103 LYS H H 7.07 0.02 1 713 . 103 LYS CA C 57.82 0.1 1 714 . 103 LYS HA H 3.83 0.02 1 715 . 103 LYS CB C 31.31 0.1 1 716 . 103 LYS HB2 H 1.27 0.02 2 717 . 103 LYS HG2 H 1.07 0.02 2 718 . 103 LYS HG3 H 0.85 0.02 2 719 . 103 LYS HD2 H 1.85 0.02 2 720 . 103 LYS HE2 H 3.25 0.02 2 721 . 103 LYS C C 176.97 0.1 1 722 . 104 PHE N N 113.26 0.1 1 723 . 104 PHE H H 6.72 0.02 1 724 . 104 PHE CA C 55.14 0.1 1 725 . 104 PHE HA H 4.76 0.02 1 726 . 104 PHE CB C 39.06 0.1 1 727 . 104 PHE HB2 H 2.42 0.02 2 728 . 104 PHE HB3 H 3.14 0.02 2 729 . 104 PHE HD1 H 7.10 0.02 3 730 . 104 PHE C C 175.56 0.1 1 731 . 105 GLY N N 106.81 0.1 1 732 . 105 GLY H H 7.68 0.02 1 733 . 105 GLY CA C 45.90 0.1 1 734 . 105 GLY HA2 H 4.09 0.02 2 735 . 105 GLY C C 175.25 0.1 1 736 . 106 TYR N N 120.21 0.1 1 737 . 106 TYR H H 8.00 0.02 1 738 . 106 TYR CA C 55.26 0.1 1 739 . 106 TYR HA H 4.92 0.02 1 740 . 106 TYR CB C 37.87 0.1 1 741 . 106 TYR HB2 H 2.89 0.02 2 742 . 106 TYR HB3 H 3.41 0.02 2 743 . 106 TYR HD1 H 7.06 0.02 3 744 . 106 TYR HE1 H 6.69 0.02 3 745 . 106 TYR C C 176.09 0.1 1 746 . 107 GLU N N 120.91 0.1 1 747 . 107 GLU H H 9.03 0.02 1 748 . 107 GLU CA C 59.25 0.1 1 749 . 107 GLU HA H 3.98 0.02 1 750 . 107 GLU CB C 28.08 0.1 1 751 . 107 GLU HB2 H 2.06 0.02 2 752 . 107 GLU HG2 H 2.32 0.02 2 753 . 107 GLU C C 177.77 0.1 1 754 . 108 LYS N N 118.44 0.1 1 755 . 108 LYS H H 8.47 0.02 1 756 . 108 LYS CA C 57.81 0.1 1 757 . 108 LYS HA H 4.20 0.02 1 758 . 108 LYS CB C 31.31 0.1 1 759 . 108 LYS HB2 H 1.79 0.02 2 760 . 108 LYS HG2 H 1.38 0.02 2 761 . 108 LYS C C 177.56 0.1 1 762 . 109 VAL N N 115.89 0.1 1 763 . 109 VAL H H 7.54 0.02 1 764 . 109 VAL CA C 61.60 0.1 1 765 . 109 VAL HA H 4.09 0.02 1 766 . 109 VAL CB C 31.32 0.1 1 767 . 109 VAL HB H 1.90 0.02 1 768 . 109 VAL HG1 H 0.70 0.02 2 769 . 109 VAL C C 176.74 0.1 1 770 . 110 VAL N N 120.91 0.1 1 771 . 110 VAL H H 7.40 0.02 1 772 . 110 VAL CA C 66.28 0.1 1 773 . 110 VAL HA H 3.15 0.02 1 774 . 110 VAL CB C 31.02 0.1 1 775 . 110 VAL HB H 2.11 0.02 1 776 . 110 VAL HG1 H 0.86 0.02 2 777 . 110 VAL C C 176.98 0.1 1 778 . 111 ASP N N 116.37 0.1 1 779 . 111 ASP H H 8.04 0.02 1 780 . 111 ASP CA C 56.43 0.1 1 781 . 111 ASP HA H 4.26 0.02 1 782 . 111 ASP CB C 39.30 0.1 1 783 . 111 ASP HB2 H 2.57 0.02 2 784 . 111 ASP C C 178.28 0.1 1 785 . 112 GLN N N 117.33 0.1 1 786 . 112 GLN H H 7.44 0.02 1 787 . 112 GLN CA C 57.38 0.1 1 788 . 112 GLN HA H 4.14 0.02 1 789 . 112 GLN CB C 27.74 0.1 1 790 . 112 GLN HB2 H 2.16 0.02 2 791 . 112 GLN HG2 H 2.42 0.02 2 792 . 112 GLN C C 178.19 0.1 1 793 . 113 ILE N N 119.24 0.1 1 794 . 113 ILE H H 7.78 0.02 1 795 . 113 ILE CA C 62.06 0.1 1 796 . 113 ILE HA H 3.67 0.02 1 797 . 113 ILE CB C 35.18 0.1 1 798 . 113 ILE HB H 1.95 0.02 1 799 . 113 ILE HG12 H 1.43 0.02 2 800 . 113 ILE HG13 H 1.12 0.02 2 801 . 113 ILE HG2 H 0.86 0.02 4 802 . 113 ILE HD1 H 0.86 0.02 4 803 . 113 ILE C C 177.70 0.1 1 804 . 114 MET N N 113.86 0.1 1 805 . 114 MET H H 7.91 0.02 1 806 . 114 MET CA C 54.54 0.1 1 807 . 114 MET HA H 4.40 0.02 1 808 . 114 MET CB C 28.04 0.1 1 809 . 114 MET HB2 H 2.16 0.02 2 810 . 114 MET HG2 H 2.68 0.02 2 811 . 114 MET C C 179.51 0.1 1 812 . 115 LYS N N 119.96 0.1 1 813 . 115 LYS H H 7.34 0.02 1 814 . 115 LYS CA C 56.92 0.1 1 815 . 115 LYS HA H 3.98 0.02 1 816 . 115 LYS CB C 31.02 0.1 1 817 . 115 LYS HB2 H 1.9 0.02 2 818 . 115 LYS HB3 H 1.74 0.02 2 819 . 115 LYS HG2 H 1.43 0.02 2 820 . 115 LYS C C 176.75 0.1 1 821 . 116 ALA N N 119.48 0.1 1 822 . 116 ALA H H 7.81 0.02 1 823 . 116 ALA CA C 52.22 0.1 1 824 . 116 ALA HA H 3.67 0.02 1 825 . 116 ALA CB C 17.62 0.1 1 826 . 116 ALA HB H 1.12 0.02 1 827 . 116 ALA C C 178.06 0.1 1 828 . 117 ASP N N 115.42 0.1 1 829 . 117 ASP H H 7.29 0.02 1 830 . 117 ASP CA C 51.98 0.1 1 831 . 117 ASP HA H 4.50 0.02 1 832 . 117 ASP CB C 37.57 0.1 1 833 . 117 ASP HB2 H 2.90 0.02 2 834 . 117 ASP HB3 H 2.10 0.02 2 835 . 117 ASP C C 175.81 0.1 1 836 . 118 ALA N N 131.91 0.1 1 837 . 118 ALA H H 7.78 0.02 1 838 . 118 ALA CA C 53.62 0.1 1 839 . 118 ALA HA H 4.09 0.02 1 840 . 118 ALA CB C 18.78 0.1 1 841 . 118 ALA HB H 1.48 0.02 1 842 . 118 ALA C C 178.33 0.1 1 843 . 119 ASN N N 111.59 0.1 1 844 . 119 ASN H H 7.91 0.02 1 845 . 119 ASN CA C 50.81 0.1 1 846 . 119 ASN HA H 4.71 0.02 1 847 . 119 ASN CB C 36.38 0.1 1 848 . 119 ASN HB2 H 2.84 0.02 2 849 . 119 ASN HB3 H 3.20 0.02 2 850 . 119 ASN C C 176.43 0.1 1 851 . 120 GLY N N 109.20 0.1 1 852 . 120 GLY H H 7.46 0.02 1 853 . 120 GLY CA C 46.60 0.1 1 854 . 120 GLY HA2 H 3.77 0.02 2 855 . 120 GLY C C 174.85 0.1 1 856 . 121 ASP N N 118.74 0.1 1 857 . 121 ASP H H 7.90 0.02 1 858 . 121 ASP CA C 52.92 0.1 1 859 . 121 ASP HA H 4.40 0.02 1 860 . 121 ASP CB C 39.36 0.1 1 861 . 121 ASP HB2 H 2.32 0.02 2 862 . 121 ASP HB3 H 2.99 0.02 2 863 . 121 ASP C C 176.61 0.1 1 864 . 122 GLY N N 110.64 0.1 1 865 . 122 GLY H H 9.80 0.02 1 866 . 122 GLY CA C 44.25 0.1 1 867 . 122 GLY HA2 H 4.13 0.02 2 868 . 122 GLY HA3 H 3.35 0.02 2 869 . 122 GLY C C 173.11 0.1 1 870 . 123 TYR N N 115.66 0.1 1 871 . 123 TYR H H 7.61 0.02 1 872 . 123 TYR CA C 53.86 0.1 1 873 . 123 TYR HA H 5.23 0.02 1 874 . 123 TYR CB C 40.25 0.1 1 875 . 123 TYR HB2 H 2.62 0.02 2 876 . 123 TYR HB3 H 2.52 0.02 2 877 . 123 TYR HD1 H 7.06 0.02 3 878 . 123 TYR HE1 H 6.64 0.02 3 879 . 123 TYR C C 174.69 0.1 1 880 . 124 ILE N N 124.74 0.1 1 881 . 124 ILE H H 9.74 0.02 1 882 . 124 ILE CA C 58.54 0.1 1 883 . 124 ILE HA H 5.23 0.02 1 884 . 124 ILE CB C 39.96 0.1 1 885 . 124 ILE HB H 1.90 0.02 1 886 . 124 ILE HG12 H 1.48 0.02 2 887 . 124 ILE HG13 H 1.17 0.02 2 888 . 124 ILE HG2 H 0.86 0.02 4 889 . 124 ILE HD1 H 0.60 0.02 4 890 . 124 ILE C C 178.48 0.1 1 891 . 125 THR N N 124.50 0.1 1 892 . 125 THR H H 9.62 0.02 1 893 . 125 THR CA C 60.19 0.1 1 894 . 125 THR HA H 4.61 0.02 1 895 . 125 THR CB C 69.44 0.1 1 896 . 125 THR HB H 4.82 0.02 1 897 . 125 THR HG1 H 1.48 0.02 1 898 . 125 THR HG2 H 1.17 0.02 1 899 . 125 THR C C 174.93 0.1 1 900 . 126 LEU N N 125.45 0.1 1 901 . 126 LEU H H 9.39 0.02 1 902 . 126 LEU CA C 57.82 0.1 1 903 . 126 LEU HA H 4.24 0.02 1 904 . 126 LEU CB C 40.66 0.1 1 905 . 126 LEU HB2 H 1.48 0.02 2 906 . 126 LEU HG H 1.48 0.02 1 907 . 126 LEU HD1 H 0.75 0.02 2 908 . 126 LEU HD2 H 0.55 0.02 2 909 . 126 LEU C C 178.02 0.1 1 910 . 127 GLU N N 115.89 0.1 1 911 . 127 GLU H H 8.40 0.02 1 912 . 127 GLU CA C 59.72 0.1 1 913 . 127 GLU HA H 3.77 0.02 1 914 . 127 GLU CB C 28.04 0.1 1 915 . 127 GLU HB2 H 2.00 0.02 2 916 . 127 GLU HG2 H 2.32 0.02 2 917 . 127 GLU C C 180.17 0.1 1 918 . 128 GLU N N 119.00 0.1 1 919 . 128 GLU H H 7.76 0.02 1 920 . 128 GLU CA C 58.31 0.1 1 921 . 128 GLU HA H 4.03 0.02 1 922 . 128 GLU CB C 28.93 0.1 1 923 . 128 GLU HB2 H 2.57 0.02 2 924 . 128 GLU HG2 H 1.90 0.02 2 925 . 128 GLU C C 179.62 0.1 1 926 . 129 PHE N N 122.11 0.1 1 927 . 129 PHE H H 8.76 0.02 1 928 . 129 PHE CA C 60.90 0.1 1 929 . 129 PHE HA H 4.09 0.02 1 930 . 129 PHE CB C 39.66 0.1 1 931 . 129 PHE HB2 H 3.15 0.02 2 932 . 129 PHE HD1 H 7.00 0.02 3 933 . 129 PHE HE1 H 6.30 0.02 3 934 . 129 PHE C C 176.97 0.1 1 935 . 130 LEU N N 114.17 0.1 1 936 . 130 LEU H H 8.57 0.02 1 937 . 130 LEU CA C 55.73 0.1 1 938 . 130 LEU HA H 3.98 0.02 1 939 . 130 LEU CB C 40.24 0.1 1 940 . 130 LEU HB2 H 2.00 0.02 2 941 . 130 LEU HG H 1.79 0.02 1 942 . 130 LEU HD1 H 0.81 0.02 2 943 . 130 LEU C C 177.88 0.1 1 944 . 131 ALA N N 120.20 0.1 1 945 . 131 ALA H H 7.39 0.02 1 946 . 131 ALA CA C 51.58 0.1 1 947 . 131 ALA HA H 4.24 0.02 1 948 . 131 ALA CB C 18.51 0.1 1 949 . 131 ALA HB H 1.48 0.02 1 950 . 131 ALA C C 177.49 0.1 1 951 . 132 PHE N N 119.71 0.1 1 952 . 132 PHE H H 7.56 0.02 1 953 . 132 PHE CA C 57.14 0.1 1 954 . 132 PHE HA H 4.35 0.02 1 955 . 132 PHE CB C 39.36 0.1 1 956 . 132 PHE HB2 H 3.10 0.02 2 957 . 132 PHE HB3 H 2.89 0.02 2 958 . 132 PHE C C 174.18 0.1 1 959 . 133 ASN N N 119.95 0.1 1 960 . 133 ASN H H 7.23 0.02 1 961 . 133 ASN CA C 51.75 0.1 1 962 . 133 ASN HA H 4.40 0.02 1 963 . 133 ASN CB C 38.76 0.1 1 964 . 133 ASN HB2 H 2.57 0.02 2 965 . 133 ASN HB3 H 2.31 0.02 2 966 . 133 ASN C C 172.71 0.1 1 967 . 134 LEU N N 128.02 0.1 1 968 . 134 LEU H H 7.43 0.02 1 969 . 134 LEU CA C 56.20 0.1 1 970 . 134 LEU HA H 3.88 0.02 1 971 . 134 LEU CB C 42.63 0.1 1 972 . 134 LEU HB2 H 1.43 0.02 2 973 . 134 LEU HG H 1.50 0.02 1 974 . 134 LEU HD1 H 0.81 0.02 2 975 . 134 LEU C C 180.93 0.1 1 stop_ save_