data_5456 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N resonances assignment for the von Willebrand factor A3 domain ; _BMRB_accession_number 5456 _BMRB_flat_file_name bmr5456.str _Entry_type original _Submission_date 2002-07-08 _Accession_date 2002-07-08 _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 Nishida Noritaka . . 2 Miyazawa Mayumi . . 3 Sumikawa Hiromi . . 4 Sakakura Masayoshi . . 5 Shimba Nobuhisa . . 6 Takahashi Hideo . . 7 Terasawa Hiroaki . . 8 Suzuki Ei-ichiro . . 9 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 183 "13C chemical shifts" 366 "15N chemical shifts" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-23 original BMRB . stop_ _Original_release_date 2002-07-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of the von Willebrand factor A3 domain ; _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 Nishida Noritaka . . 2 Miyazawa Mayumi . . 3 Sumikawa Hiromi . . 4 Sakakura Masayoshi . . 5 Shimba Nobuhisa . . 6 Takahashi Hideo . . 7 Terasawa Hiroaki . . 8 Suzuki Ei-ichiro . . 9 Shimada Ichio . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 357 _Page_last 358 _Year 2002 _Details . loop_ _Keyword 'collagen-binding protein' 'platelet adhesion' 'resonance assignment' 'von Willebrand factor' stop_ save_ ################################## # Molecular system description # ################################## save_system_vWF_A3_domain _Saveframe_category molecular_system _Mol_system_name 'von Willebrand factor-A3 domain' _Abbreviation_common 'vWF-A3 domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'A3 domain' $A3_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'collagen binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_A3_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'von Willebrand factor-A3 domain' _Abbreviation_common 'vWF-A3 domain' _Molecular_mass 20861 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 197 _Mol_residue_sequence ; GSMDIAPDCSQPLDVILLLD GSSSFPASYFDEMKSFAKAF ISKANIGPRLTQVSVLQYGS ITTIDVPWNVVPEKAHLLSL VDVMQREGGPSQIGDALGFA VRYLTSEMHGARPGASKAVV ILVTDVSVDSVDAAADAARS NRVTVFPIGIGDRYDAAQLR ILAGPAGDSNVVKLQRIEDL PTMVTLGNSFLHKLCSG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 MET 4 ASP 5 ILE 6 ALA 7 PRO 8 ASP 9 CYS 10 SER 11 GLN 12 PRO 13 LEU 14 ASP 15 VAL 16 ILE 17 LEU 18 LEU 19 LEU 20 ASP 21 GLY 22 SER 23 SER 24 SER 25 PHE 26 PRO 27 ALA 28 SER 29 TYR 30 PHE 31 ASP 32 GLU 33 MET 34 LYS 35 SER 36 PHE 37 ALA 38 LYS 39 ALA 40 PHE 41 ILE 42 SER 43 LYS 44 ALA 45 ASN 46 ILE 47 GLY 48 PRO 49 ARG 50 LEU 51 THR 52 GLN 53 VAL 54 SER 55 VAL 56 LEU 57 GLN 58 TYR 59 GLY 60 SER 61 ILE 62 THR 63 THR 64 ILE 65 ASP 66 VAL 67 PRO 68 TRP 69 ASN 70 VAL 71 VAL 72 PRO 73 GLU 74 LYS 75 ALA 76 HIS 77 LEU 78 LEU 79 SER 80 LEU 81 VAL 82 ASP 83 VAL 84 MET 85 GLN 86 ARG 87 GLU 88 GLY 89 GLY 90 PRO 91 SER 92 GLN 93 ILE 94 GLY 95 ASP 96 ALA 97 LEU 98 GLY 99 PHE 100 ALA 101 VAL 102 ARG 103 TYR 104 LEU 105 THR 106 SER 107 GLU 108 MET 109 HIS 110 GLY 111 ALA 112 ARG 113 PRO 114 GLY 115 ALA 116 SER 117 LYS 118 ALA 119 VAL 120 VAL 121 ILE 122 LEU 123 VAL 124 THR 125 ASP 126 VAL 127 SER 128 VAL 129 ASP 130 SER 131 VAL 132 ASP 133 ALA 134 ALA 135 ALA 136 ASP 137 ALA 138 ALA 139 ARG 140 SER 141 ASN 142 ARG 143 VAL 144 THR 145 VAL 146 PHE 147 PRO 148 ILE 149 GLY 150 ILE 151 GLY 152 ASP 153 ARG 154 TYR 155 ASP 156 ALA 157 ALA 158 GLN 159 LEU 160 ARG 161 ILE 162 LEU 163 ALA 164 GLY 165 PRO 166 ALA 167 GLY 168 ASP 169 SER 170 ASN 171 VAL 172 VAL 173 LYS 174 LEU 175 GLN 176 ARG 177 ILE 178 GLU 179 ASP 180 LEU 181 PRO 182 THR 183 MET 184 VAL 185 THR 186 LEU 187 GLY 188 ASN 189 SER 190 PHE 191 LEU 192 HIS 193 LYS 194 LEU 195 CYS 196 SER 197 GLY stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1AO3 'A3 Domain Of Von Willebrand Factor' 94.92 187 100.00 100.00 6.13e-104 PDB 1ATZ 'Human Von Willebrand Factor A3 Domain' 95.94 189 100.00 100.00 4.21e-105 PDB 2ADF ; Crystal Structure And Paratope Determination Of 82d6a3, An Antithrombotic Antibody Directed Against The Von Willebrand Factor A3-Domain ; 97.97 196 99.48 100.00 4.57e-107 DBJ BAG59985 'unnamed protein product [Homo sapiens]' 83.76 1104 100.00 100.00 1.15e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $A3_domain Human 9606 Eukaryota Metazoa Homo sapiens 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 $A3_domain 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) . 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 $A3_domain . mM 0.5 0.8 '[U-98% 13C; U-98% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $A3_domain 0.8 mM '[U-98% 2H; U-98% 13C; U-98% 15N]' stop_ 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 . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'A3 domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 SER CA C 58.8 0.1 1 2 . 2 SER CB C 63.4 0.1 1 3 . 3 MET H H 8.50 0.02 1 4 . 3 MET CA C 55.2 0.1 1 5 . 3 MET CB C 32.0 0.1 1 6 . 3 MET N N 121.34 0.05 1 7 . 4 ASP H H 8.14 0.02 1 8 . 4 ASP CA C 54.3 0.1 1 9 . 4 ASP CB C 40.8 0.1 1 10 . 4 ASP N N 121.41 0.05 1 11 . 5 ILE H H 7.91 0.02 1 12 . 5 ILE CA C 60.5 0.1 1 13 . 5 ILE CB C 38.4 0.1 1 14 . 5 ILE N N 120.08 0.05 1 15 . 6 ALA H H 8.21 0.02 1 16 . 6 ALA CA C 50.1 0.1 1 17 . 6 ALA CB C 17.9 0.1 1 18 . 6 ALA N N 128.63 0.05 1 19 . 7 PRO CA C 62.8 0.1 1 20 . 7 PRO CB C 31.4 0.1 1 21 . 8 ASP H H 8.31 0.02 1 22 . 8 ASP CA C 53.9 0.1 1 23 . 8 ASP CB C 40.8 0.1 1 24 . 8 ASP N N 120.3 0.05 1 25 . 9 CYS H H 8.58 0.02 1 26 . 9 CYS CA C 55.5 0.1 1 27 . 9 CYS CB C 40.2 0.1 1 28 . 9 CYS N N 119.77 0.05 1 29 . 10 SER H H 8.73 0.02 1 30 . 10 SER CA C 58.9 0.1 1 31 . 10 SER CB C 63.6 0.1 1 32 . 10 SER N N 119.26 0.05 1 33 . 11 GLN H H 7.79 0.02 1 34 . 11 GLN CA C 52.8 0.1 1 35 . 11 GLN CB C 29.7 0.1 1 36 . 11 GLN N N 121.63 0.05 1 37 . 12 PRO CA C 63.4 0.1 1 38 . 12 PRO CB C 31.2 0.1 1 39 . 13 LEU H H 7.30 0.02 1 40 . 13 LEU CA C 54.3 0.1 1 41 . 13 LEU CB C 44.4 0.1 1 42 . 13 LEU N N 128.27 0.05 1 43 . 14 ASP H H 9.36 0.02 1 44 . 14 ASP CA C 53.4 0.1 1 45 . 14 ASP CB C 41.7 0.1 1 46 . 14 ASP N N 130.51 0.05 1 47 . 15 VAL H H 9.22 0.02 1 48 . 15 VAL CA C 58.6 0.1 1 49 . 15 VAL CB C 34.7 0.1 1 50 . 15 VAL N N 120.73 0.05 1 51 . 16 ILE H H 8.54 0.02 1 52 . 16 ILE CA C 59.3 0.1 1 53 . 16 ILE CB C 41.4 0.1 1 54 . 16 ILE N N 124.74 0.05 1 55 . 17 LEU H H 8.78 0.02 1 56 . 17 LEU CA C 53.3 0.1 1 57 . 17 LEU CB C 41.7 0.1 1 58 . 17 LEU N N 126.77 0.05 1 59 . 18 LEU H H 9.46 0.02 1 60 . 18 LEU CA C 53.0 0.1 1 61 . 18 LEU CB C 42.7 0.1 1 62 . 18 LEU N N 128.66 0.05 1 63 . 19 LEU H H 9.10 0.02 1 64 . 19 LEU CA C 55.1 0.1 1 65 . 19 LEU CB C 41.2 0.1 1 66 . 19 LEU N N 124.74 0.05 1 67 . 20 ASP H H 5.89 0.02 1 68 . 20 ASP CA C 53.7 0.1 1 69 . 20 ASP CB C 40.8 0.1 1 70 . 20 ASP N N 119.92 0.05 1 71 . 21 GLY H H 7.79 0.02 1 72 . 21 GLY CA C 45.2 0.1 1 73 . 21 GLY N N 116.31 0.05 1 74 . 22 SER H H 8.52 0.02 1 75 . 22 SER CA C 59.2 0.1 1 76 . 22 SER CB C 64.5 0.1 1 77 . 22 SER N N 116.0 0.05 1 78 . 23 SER H H 8.90 0.02 1 79 . 23 SER CA C 59.3 0.1 1 80 . 23 SER CB C 63.2 0.1 1 81 . 23 SER N N 119.92 0.05 1 82 . 24 SER H H 7.71 0.02 1 83 . 24 SER CA C 61.2 0.1 1 84 . 24 SER CB C 62.6 0.1 1 85 . 24 SER N N 115.5 0.05 1 86 . 25 PHE H H 7.20 0.02 1 87 . 25 PHE CA C 55.4 0.1 1 88 . 25 PHE CB C 37.6 0.1 1 89 . 25 PHE N N 118.11 0.05 1 90 . 26 PRO CA C 63.0 0.1 1 91 . 26 PRO CB C 31.9 0.1 1 92 . 27 ALA H H 8.75 0.02 1 93 . 27 ALA CA C 55.5 0.1 1 94 . 27 ALA CB C 17.7 0.1 1 95 . 27 ALA N N 125.35 0.05 1 96 . 28 SER H H 8.38 0.02 1 97 . 28 SER CA C 60.9 0.1 1 98 . 28 SER CB C 62.1 0.1 1 99 . 28 SER N N 113.77 0.05 1 100 . 29 TYR H H 8.84 0.02 1 101 . 29 TYR CA C 60.0 0.1 1 102 . 29 TYR CB C 36.8 0.1 1 103 . 29 TYR N N 124.01 0.05 1 104 . 30 PHE H H 8.01 0.02 1 105 . 30 PHE CA C 61.5 0.1 1 106 . 30 PHE CB C 38.8 0.1 1 107 . 30 PHE N N 121.63 0.05 1 108 . 31 ASP H H 7.70 0.02 1 109 . 31 ASP CA C 58.0 0.1 1 110 . 31 ASP CB C 39.7 0.1 1 111 . 31 ASP N N 118.44 0.05 1 112 . 32 GLU H H 7.38 0.02 1 113 . 32 GLU CA C 58.0 0.1 1 114 . 32 GLU CB C 28.6 0.1 1 115 . 32 GLU N N 119.16 0.05 1 116 . 33 MET H H 7.79 0.02 1 117 . 33 MET CA C 59.9 0.1 1 118 . 33 MET CB C 31.1 0.1 1 119 . 33 MET N N 119.97 0.05 1 120 . 34 LYS H H 8.14 0.02 1 121 . 34 LYS CA C 60.4 0.1 1 122 . 34 LYS CB C 31.0 0.1 1 123 . 34 LYS N N 120.03 0.05 1 124 . 35 SER H H 8.07 0.02 1 125 . 35 SER CA C 62.1 0.1 1 126 . 35 SER N N 115.59 0.05 1 127 . 36 PHE H H 8.34 0.02 1 128 . 36 PHE CA C 60.8 0.1 1 129 . 36 PHE CB C 38.2 0.1 1 130 . 36 PHE N N 123.09 0.05 1 131 . 37 ALA H H 8.25 0.02 1 132 . 37 ALA CA C 54.8 0.1 1 133 . 37 ALA CB C 17.2 0.1 1 134 . 37 ALA N N 122.89 0.05 1 135 . 38 LYS H H 8.41 0.02 1 136 . 38 LYS CA C 60.4 0.1 1 137 . 38 LYS CB C 31.7 0.1 1 138 . 38 LYS N N 115.79 0.05 1 139 . 39 ALA H H 8.25 0.02 1 140 . 39 ALA CA C 54.8 0.1 1 141 . 39 ALA CB C 17.6 0.1 1 142 . 39 ALA N N 123.37 0.05 1 143 . 40 PHE H H 8.55 0.02 1 144 . 40 PHE CA C 61.9 0.1 1 145 . 40 PHE CB C 38.7 0.1 1 146 . 40 PHE N N 118.95 0.05 1 147 . 41 ILE H H 8.29 0.02 1 148 . 41 ILE CA C 65.7 0.1 1 149 . 41 ILE CB C 38.7 0.1 1 150 . 41 ILE N N 118.60 0.05 1 151 . 42 SER H H 8.29 0.02 1 152 . 42 SER CA C 62.7 0.1 1 153 . 42 SER CB C 64.2 0.1 1 154 . 42 SER N N 112.19 0.05 1 155 . 43 LYS H H 7.42 0.02 1 156 . 43 LYS CA C 56.1 0.1 1 157 . 43 LYS CB C 32.8 0.1 1 158 . 43 LYS N N 119.90 0.05 1 159 . 44 ALA H H 7.56 0.02 1 160 . 44 ALA CA C 51.9 0.1 1 161 . 44 ALA CB C 18.2 0.1 1 162 . 44 ALA N N 122.79 0.05 1 163 . 45 ASN H H 9.00 0.02 1 164 . 45 ASN CA C 50.9 0.1 1 165 . 45 ASN CB C 36.8 0.1 1 166 . 45 ASN N N 121.68 0.05 1 167 . 46 ILE H H 7.40 0.02 1 168 . 46 ILE CA C 59.3 0.1 1 169 . 46 ILE CB C 38.4 0.1 1 170 . 46 ILE N N 121.73 0.05 1 171 . 47 GLY H H 8.20 0.02 1 172 . 47 GLY CA C 45.2 0.1 1 173 . 47 GLY N N 113.82 0.05 1 174 . 49 ARG H H 8.42 0.02 1 175 . 49 ARG CA C 61.3 0.1 1 176 . 49 ARG N N 116.86 0.05 1 177 . 50 LEU H H 7.40 0.02 1 178 . 50 LEU CA C 53.4 0.1 1 179 . 50 LEU CB C 41.0 0.1 1 180 . 50 LEU N N 122.29 0.05 1 181 . 51 THR H H 9.01 0.02 1 182 . 51 THR CA C 63.4 0.1 1 183 . 51 THR CB C 68.5 0.1 1 184 . 51 THR N N 126.02 0.05 1 185 . 52 GLN H H 9.13 0.02 1 186 . 52 GLN CA C 55.2 0.1 1 187 . 52 GLN CB C 31.5 0.1 1 188 . 52 GLN N N 124.68 0.05 1 189 . 53 VAL H H 8.76 0.02 1 190 . 53 VAL CA C 59.8 0.1 1 191 . 53 VAL CB C 34.7 0.1 1 192 . 53 VAL N N 122.49 0.05 1 193 . 54 SER H H 8.56 0.02 1 194 . 54 SER CA C 55.5 0.1 1 195 . 54 SER CB C 64.9 0.1 1 196 . 54 SER N N 120.15 0.05 1 197 . 55 VAL H H 8.49 0.02 1 198 . 55 VAL CA C 61.4 0.1 1 199 . 55 VAL CB C 32.7 0.1 1 200 . 55 VAL N N 121.11 0.05 1 201 . 56 LEU H H 9.22 0.02 1 202 . 56 LEU CA C 53.3 0.1 1 203 . 56 LEU CB C 45.5 0.1 1 204 . 56 LEU N N 132.79 0.05 1 205 . 57 GLN H H 8.47 0.02 1 206 . 57 GLN CA C 54.3 0.1 1 207 . 57 GLN CB C 32.5 0.1 1 208 . 57 GLN N N 114.47 0.05 1 209 . 58 TYR H H 7.99 0.02 1 210 . 58 TYR CA C 54.4 0.1 1 211 . 58 TYR CB C 42.5 0.1 1 212 . 58 TYR N N 116.15 0.05 1 213 . 59 GLY H H 6.97 0.02 1 214 . 59 GLY CA C 45.5 0.1 1 215 . 59 GLY N N 106.04 0.05 1 216 . 60 SER H H 8.96 0.02 1 217 . 60 SER CA C 63.0 0.1 1 218 . 60 SER CB C 62.3 0.1 1 219 . 60 SER N N 124.87 0.05 1 220 . 61 ILE H H 7.65 0.02 1 221 . 61 ILE CA C 59.3 0.1 1 222 . 61 ILE CB C 41.6 0.1 1 223 . 61 ILE N N 112.58 0.05 1 224 . 62 THR H H 8.25 0.02 1 225 . 62 THR CA C 62.8 0.1 1 226 . 62 THR CB C 67.4 0.1 1 227 . 62 THR N N 122.89 0.05 1 228 . 63 THR H H 8.66 0.02 1 229 . 63 THR CA C 59.8 0.1 1 230 . 63 THR CB C 70.6 0.1 1 231 . 63 THR N N 119.05 0.05 1 232 . 64 ILE H H 8.30 0.02 1 233 . 64 ILE CA C 60.5 0.1 1 234 . 64 ILE CB C 37.6 0.1 1 235 . 64 ILE N N 122.30 0.05 1 236 . 65 ASP H H 8.08 0.02 1 237 . 65 ASP CA C 56.4 0.1 1 238 . 65 ASP CB C 42.6 0.1 1 239 . 65 ASP N N 129.36 0.05 1 240 . 66 VAL H H 8.37 0.02 1 241 . 66 VAL CA C 59.5 0.1 1 242 . 66 VAL CB C 33.2 0.1 1 243 . 66 VAL N N 119.78 0.05 1 244 . 67 PRO CA C 62.1 0.1 1 245 . 67 PRO CB C 33.4 0.1 1 246 . 68 TRP H H 7.62 0.02 1 247 . 68 TRP CA C 57.1 0.1 1 248 . 68 TRP CB C 30.7 0.1 1 249 . 68 TRP N N 114.27 0.05 1 250 . 69 ASN H H 8.58 0.02 1 251 . 69 ASN N N 114.67 0.05 1 252 . 70 VAL H H 7.63 0.02 1 253 . 70 VAL CA C 61.6 0.1 1 254 . 70 VAL CB C 32.5 0.1 1 255 . 70 VAL N N 117.92 0.05 1 256 . 71 VAL H H 7.97 0.02 1 257 . 71 VAL CA C 60.2 0.1 1 258 . 71 VAL CB C 31.7 0.1 1 259 . 71 VAL N N 122.91 0.05 1 260 . 72 PRO CA C 62.5 0.1 1 261 . 72 PRO CB C 28.9 0.1 1 262 . 73 GLU H H 8.22 0.02 1 263 . 73 GLU CA C 54.6 0.1 1 264 . 73 GLU CB C 31.2 0.1 1 265 . 73 GLU N N 123.68 0.05 1 266 . 74 LYS H H 9.08 0.02 1 267 . 74 LYS CA C 61.7 0.1 1 268 . 74 LYS CB C 31.7 0.1 1 269 . 74 LYS N N 126.85 0.05 1 270 . 75 ALA H H 8.94 0.02 1 271 . 75 ALA CA C 55.6 0.1 1 272 . 75 ALA CB C 17.5 0.1 1 273 . 75 ALA N N 119.04 0.05 1 274 . 76 HIS H H 7.59 0.02 1 275 . 76 HIS CA C 58.4 0.1 1 276 . 76 HIS CB C 29.7 0.1 1 277 . 76 HIS N N 116.62 0.05 1 278 . 77 LEU H H 7.91 0.02 1 279 . 77 LEU CA C 58.7 0.1 1 280 . 77 LEU CB C 42.0 0.1 1 281 . 77 LEU N N 119.6 0.05 1 282 . 78 LEU H H 8.46 0.02 1 283 . 78 LEU CA C 58.8 0.1 1 284 . 78 LEU CB C 40.1 0.1 1 285 . 78 LEU N N 117.2 0.05 1 286 . 79 SER H H 7.55 0.02 1 287 . 79 SER CA C 61.5 0.1 1 288 . 79 SER CB C 62.7 0.1 1 289 . 79 SER N N 114.42 0.05 1 290 . 80 LEU H H 7.51 0.02 1 291 . 80 LEU CA C 56.8 0.1 1 292 . 80 LEU CB C 41.7 0.1 1 293 . 80 LEU N N 121.43 0.05 1 294 . 81 VAL H H 7.7 0.02 1 295 . 81 VAL CA C 65.5 0.1 1 296 . 81 VAL CB C 30.6 0.1 1 297 . 81 VAL N N 119.59 0.05 1 298 . 82 ASP H H 7.89 0.02 1 299 . 82 ASP CA C 58.0 0.1 1 300 . 82 ASP CB C 41.2 0.1 1 301 . 82 ASP N N 117.35 0.05 1 302 . 83 VAL H H 6.85 0.02 1 303 . 83 VAL CA C 61.7 0.1 1 304 . 83 VAL CB C 31.2 0.1 1 305 . 83 VAL N N 108.7 0.05 1 306 . 84 MET H H 7.68 0.02 1 307 . 84 MET CA C 57.7 0.1 1 308 . 84 MET CB C 34.2 0.1 1 309 . 84 MET N N 121.54 0.05 1 310 . 85 GLN H H 8.70 0.02 1 311 . 85 GLN CA C 53.1 0.1 1 312 . 85 GLN CB C 31.3 0.1 1 313 . 85 GLN N N 120.78 0.05 1 314 . 86 ARG H H 8.41 0.02 1 315 . 86 ARG CA C 56.7 0.1 1 316 . 86 ARG CB C 29.0 0.1 1 317 . 86 ARG N N 126.26 0.05 1 318 . 87 GLU H H 9.15 0.02 1 319 . 87 GLU CA C 58.2 0.1 1 320 . 87 GLU CB C 28.5 0.1 1 321 . 87 GLU N N 129.14 0.05 1 322 . 88 GLY H H 8.53 0.02 1 323 . 88 GLY CA C 44.4 0.1 1 324 . 88 GLY N N 110.33 0.05 1 325 . 89 GLY H H 8.25 0.02 1 326 . 89 GLY CA C 44 0.1 1 327 . 89 GLY N N 104.05 0.05 1 328 . 90 PRO CA C 61.7 0.1 1 329 . 90 PRO CB C 32.7 0.1 1 330 . 91 SER H H 8.35 0.02 1 331 . 91 SER CA C 57.3 0.1 1 332 . 91 SER CB C 62.7 0.1 1 333 . 91 SER N N 112.44 0.05 1 334 . 92 GLN H H 8.08 0.02 1 335 . 92 GLN CA C 54.1 0.1 1 336 . 92 GLN CB C 27.2 0.1 1 337 . 92 GLN N N 129.36 0.05 1 338 . 93 ILE H H 7.74 0.02 1 339 . 93 ILE CA C 65.1 0.1 1 340 . 93 ILE CB C 36.9 0.1 1 341 . 93 ILE N N 122.40 0.05 1 342 . 94 GLY H H 10.39 0.02 1 343 . 94 GLY CA C 47.4 0.1 1 344 . 94 GLY N N 114.37 0.05 1 345 . 95 ASP H H 9.07 0.02 1 346 . 95 ASP CA C 57.3 0.1 1 347 . 95 ASP CB C 42.2 0.1 1 348 . 95 ASP N N 125.18 0.05 1 349 . 96 ALA H H 7.59 0.02 1 350 . 96 ALA CA C 54.4 0.1 1 351 . 96 ALA CB C 20.5 0.1 1 352 . 96 ALA N N 120.59 0.05 1 353 . 97 LEU H H 8.89 0.02 1 354 . 97 LEU CA C 57.0 0.1 1 355 . 97 LEU CB C 39.6 0.1 1 356 . 97 LEU N N 118.42 0.05 1 357 . 98 GLY H H 8.45 0.02 1 358 . 98 GLY CA C 47.0 0.1 1 359 . 98 GLY N N 107.01 0.05 1 360 . 99 PHE H H 8.31 0.02 1 361 . 99 PHE CA C 61.3 0.1 1 362 . 99 PHE CB C 38.4 0.1 1 363 . 99 PHE N N 123.74 0.05 1 364 . 100 ALA H H 8.89 0.02 1 365 . 100 ALA CA C 55.2 0.1 1 366 . 100 ALA CB C 18.2 0.1 1 367 . 100 ALA N N 122.70 0.05 1 368 . 101 VAL H H 8.69 0.02 1 369 . 101 VAL CA C 67.5 0.1 1 370 . 101 VAL CB C 30.7 0.1 1 371 . 101 VAL N N 117.05 0.05 1 372 . 102 ARG H H 7.52 0.02 1 373 . 102 ARG CA C 59.8 0.1 1 374 . 102 ARG CB C 29.1 0.1 1 375 . 102 ARG N N 119.98 0.05 1 376 . 103 TYR H H 8.43 0.02 1 377 . 103 TYR CA C 60.9 0.1 1 378 . 103 TYR CB C 37.3 0.1 1 379 . 103 TYR N N 122.18 0.05 1 380 . 104 LEU H H 8.32 0.02 1 381 . 104 LEU CA C 56.7 0.1 1 382 . 104 LEU CB C 43.7 0.1 1 383 . 104 LEU N N 117.45 0.05 1 384 . 105 THR H H 7.42 0.02 1 385 . 105 THR CA C 60.5 0.1 1 386 . 105 THR CB C 69.9 0.1 1 387 . 105 THR N N 105.34 0.05 1 388 . 106 SER H H 7.31 0.02 1 389 . 106 SER CA C 56.9 0.1 1 390 . 106 SER CB C 62.2 0.1 1 391 . 106 SER N N 116.40 0.05 1 392 . 107 GLU H H 9.02 0.02 1 393 . 107 GLU CA C 58.1 0.1 1 394 . 107 GLU CB C 28.8 0.1 1 395 . 107 GLU N N 130.56 0.05 1 396 . 108 MET H H 8.41 0.02 1 397 . 108 MET CA C 57.3 0.1 1 398 . 108 MET CB C 31.7 0.1 1 399 . 108 MET N N 117.83 0.05 1 400 . 109 HIS H H 7.32 0.02 1 401 . 109 HIS CA C 57.2 0.1 1 402 . 109 HIS CB C 31.4 0.1 1 403 . 109 HIS N N 115.13 0.05 1 404 . 110 GLY H H 7.78 0.02 1 405 . 110 GLY CA C 45.0 0.1 1 406 . 110 GLY N N 106.08 0.05 1 407 . 111 ALA H H 7.38 0.02 1 408 . 111 ALA CA C 51.4 0.1 1 409 . 111 ALA CB C 17.2 0.1 1 410 . 111 ALA N N 124.25 0.05 1 411 . 112 ARG H H 9.01 0.02 1 412 . 112 ARG CA C 53.8 0.1 1 413 . 112 ARG CB C 29.8 0.1 1 414 . 112 ARG N N 122.65 0.05 1 415 . 113 PRO CA C 63.7 0.1 1 416 . 113 PRO CB C 31.2 0.1 1 417 . 114 GLY H H 8.69 0.02 1 418 . 114 GLY CA C 44.8 0.1 1 419 . 114 GLY N N 108.71 0.05 1 420 . 115 ALA H H 7.11 0.02 1 421 . 115 ALA CA C 51.4 0.1 1 422 . 115 ALA CB C 19.1 0.1 1 423 . 115 ALA N N 122.12 0.05 1 424 . 116 SER H H 8.32 0.02 1 425 . 116 SER CA C 59.8 0.1 1 426 . 116 SER CB C 63.5 0.1 1 427 . 116 SER N N 117.59 0.05 1 428 . 117 LYS H H 8.68 0.02 1 429 . 117 LYS CA C 54.0 0.1 1 430 . 117 LYS CB C 35.7 0.1 1 431 . 117 LYS N N 121.85 0.05 1 432 . 118 ALA H H 8.97 0.02 1 433 . 118 ALA CA C 50.8 0.1 1 434 . 118 ALA CB C 23.2 0.1 1 435 . 118 ALA N N 125.63 0.05 1 436 . 119 VAL H H 8.83 0.02 1 437 . 119 VAL CA C 59.8 0.1 1 438 . 119 VAL CB C 35.2 0.1 1 439 . 119 VAL N N 118.22 0.05 1 440 . 120 VAL H H 9.21 0.02 1 441 . 120 VAL CA C 60.7 0.1 1 442 . 120 VAL CB C 32.3 0.1 1 443 . 120 VAL N N 129.48 0.05 1 444 . 121 ILE H H 8.41 0.02 1 445 . 121 ILE CA C 57.7 0.1 1 446 . 121 ILE CB C 41.2 0.1 1 447 . 121 ILE N N 124.41 0.05 1 448 . 122 LEU H H 8.31 0.02 1 449 . 122 LEU CA C 53.7 0.1 1 450 . 122 LEU CB C 41.5 0.1 1 451 . 122 LEU N N 128.19 0.05 1 452 . 123 VAL H H 9.15 0.02 1 453 . 123 VAL CA C 63.4 0.1 1 454 . 123 VAL CB C 34.7 0.1 1 455 . 123 VAL N N 124.01 0.05 1 456 . 124 THR H H 8.43 0.02 1 457 . 124 THR CA C 61.2 0.1 1 458 . 124 THR CB C 70.4 0.1 1 459 . 124 THR N N 114.48 0.05 1 460 . 125 ASP H H 8.18 0.02 1 461 . 125 ASP CA C 51.7 0.1 1 462 . 125 ASP CB C 44.6 0.1 1 463 . 125 ASP N N 125.43 0.05 1 464 . 126 VAL H H 9.36 0.02 1 465 . 126 VAL CA C 62.1 0.1 1 466 . 126 VAL CB C 32.4 0.1 1 467 . 126 VAL N N 120.74 0.05 1 468 . 127 SER H H 8.96 0.02 1 469 . 127 SER CA C 58.7 0.1 1 470 . 127 SER CB C 62.7 0.1 1 471 . 127 SER N N 120.11 0.05 1 472 . 128 VAL H H 8.85 0.02 1 473 . 128 VAL CA C 62.7 0.1 1 474 . 128 VAL CB C 31.2 0.1 1 475 . 128 VAL N N 122.69 0.05 1 476 . 129 ASP H H 8.39 0.02 1 477 . 129 ASP CA C 50.7 0.1 1 478 . 129 ASP CB C 42.0 0.1 1 479 . 129 ASP N N 120.19 0.05 1 480 . 130 SER H H 8.2 0.02 1 481 . 130 SER CA C 57.7 0.1 1 482 . 130 SER CB C 63.2 0.1 1 483 . 130 SER N N 113.82 0.05 1 484 . 131 VAL H H 8.72 0.02 1 485 . 131 VAL CA C 61.3 0.1 1 486 . 131 VAL CB C 31.7 0.1 1 487 . 131 VAL N N 117.62 0.05 1 488 . 132 ASP H H 8.17 0.02 1 489 . 132 ASP CA C 57.8 0.1 1 490 . 132 ASP CB C 39.8 0.1 1 491 . 132 ASP N N 120.69 0.05 1 492 . 133 ALA H H 8.49 0.02 1 493 . 133 ALA CA C 55.0 0.1 1 494 . 133 ALA CB C 17.0 0.1 1 495 . 133 ALA N N 122.51 0.05 1 496 . 134 ALA H H 8.62 0.02 1 497 . 134 ALA CA C 54.6 0.1 1 498 . 134 ALA CB C 19.0 0.1 1 499 . 134 ALA N N 124.22 0.05 1 500 . 135 ALA H H 8.16 0.02 1 501 . 135 ALA CA C 55.0 0.1 1 502 . 135 ALA CB C 18.6 0.1 1 503 . 135 ALA N N 120.24 0.05 1 504 . 136 ASP H H 8.12 0.02 1 505 . 136 ASP CA C 57.1 0.1 1 506 . 136 ASP CB C 40.7 0.1 1 507 . 136 ASP N N 120.07 0.05 1 508 . 137 ALA H H 8.34 0.02 1 509 . 137 ALA CA C 54.7 0.1 1 510 . 137 ALA CB C 16.7 0.1 1 511 . 137 ALA N N 124.69 0.05 1 512 . 138 ALA H H 8.37 0.02 1 513 . 138 ALA CA C 55.7 0.1 1 514 . 138 ALA CB C 16.2 0.1 1 515 . 138 ALA N N 121.49 0.05 1 516 . 139 ARG H H 7.76 0.02 1 517 . 139 ARG CA C 59.4 0.1 1 518 . 139 ARG CB C 29.2 0.1 1 519 . 139 ARG N N 119.15 0.05 1 520 . 140 SER H H 8.84 0.02 1 521 . 140 SER CA C 61.4 0.1 1 522 . 140 SER CB C 62.7 0.1 1 523 . 140 SER N N 116.25 0.05 1 524 . 141 ASN H H 7.48 0.02 1 525 . 141 ASN CA C 53.8 0.1 1 526 . 141 ASN CB C 39.9 0.1 1 527 . 141 ASN N N 117.08 0.05 1 528 . 142 ARG H H 7.89 0.02 1 529 . 142 ARG CA C 57.3 0.1 1 530 . 142 ARG CB C 26.2 0.1 1 531 . 142 ARG N N 114.28 0.05 1 532 . 143 VAL H H 8.39 0.02 1 533 . 143 VAL CA C 61.2 0.1 1 534 . 143 VAL CB C 32.0 0.1 1 535 . 143 VAL N N 119.23 0.05 1 536 . 144 THR H H 8.28 0.02 1 537 . 144 THR CA C 63.2 0.1 1 538 . 144 THR CB C 68.5 0.1 1 539 . 144 THR N N 126.34 0.05 1 540 . 145 VAL H H 8.44 0.02 1 541 . 145 VAL CA C 61.0 0.1 1 542 . 145 VAL CB C 32.8 0.1 1 543 . 145 VAL N N 128.13 0.05 1 544 . 146 PHE H H 9.24 0.02 1 545 . 146 PHE CA C 54.7 0.1 1 546 . 146 PHE N N 126.42 0.05 1 547 . 147 PRO CA C 60.5 0.1 1 548 . 147 PRO CB C 32.2 0.1 1 549 . 148 ILE H H 9.04 0.02 1 550 . 148 ILE CA C 59.1 0.1 1 551 . 148 ILE CB C 37.7 0.1 1 552 . 148 ILE N N 125.25 0.05 1 553 . 149 GLY H H 8.98 0.02 1 554 . 149 GLY CA C 44.3 0.1 1 555 . 149 GLY N N 114.26 0.05 1 556 . 150 ILE H H 8.11 0.02 1 557 . 150 ILE CA C 59.7 0.1 1 558 . 150 ILE CB C 40.2 0.1 1 559 . 150 ILE N N 124.43 0.05 1 560 . 151 GLY H H 8.57 0.02 1 561 . 151 GLY CA C 45.3 0.1 1 562 . 151 GLY N N 114.35 0.05 1 563 . 152 ASP H H 8.18 0.02 1 564 . 152 ASP CA C 53.4 0.1 1 565 . 152 ASP CB C 41.6 0.1 1 566 . 152 ASP N N 118.44 0.05 1 567 . 153 ARG H H 9.38 0.02 1 568 . 153 ARG CA C 56.3 0.1 1 569 . 153 ARG CB C 31.2 0.1 1 570 . 153 ARG N N 119.24 0.05 1 571 . 154 TYR H H 6.29 0.02 1 572 . 154 TYR CA C 56.0 0.1 1 573 . 154 TYR CB C 31.8 0.1 1 574 . 154 TYR N N 112.25 0.05 1 575 . 155 ASP H H 9.19 0.02 1 576 . 155 ASP CA C 52.3 0.1 1 577 . 155 ASP CB C 42.7 0.1 1 578 . 155 ASP N N 121.27 0.05 1 579 . 156 ALA H H 9.16 0.02 1 580 . 156 ALA CA C 55.5 0.1 1 581 . 156 ALA CB C 18.0 0.1 1 582 . 156 ALA N N 130.19 0.05 1 583 . 157 ALA H H 8.40 0.02 1 584 . 157 ALA CA C 55.0 0.1 1 585 . 157 ALA CB C 17.5 0.1 1 586 . 157 ALA N N 120.81 0.05 1 587 . 158 GLN H H 7.87 0.02 1 588 . 158 GLN CA C 59.1 0.1 1 589 . 158 GLN CB C 28.0 0.1 1 590 . 158 GLN N N 118.45 0.05 1 591 . 159 LEU H H 7.69 0.02 1 592 . 159 LEU CA C 58.4 0.1 1 593 . 159 LEU CB C 40.1 0.1 1 594 . 159 LEU N N 116.17 0.05 1 595 . 160 ARG H H 7.40 0.02 1 596 . 160 ARG CA C 59.5 0.1 1 597 . 160 ARG CB C 29.4 0.1 1 598 . 160 ARG N N 116.29 0.05 1 599 . 161 ILE H H 7.68 0.02 1 600 . 161 ILE CA C 64.4 0.1 1 601 . 161 ILE CB C 37.2 0.1 1 602 . 161 ILE N N 120.43 0.05 1 603 . 162 LEU H H 7.87 0.02 1 604 . 162 LEU CA C 57.9 0.1 1 605 . 162 LEU CB C 41.9 0.1 1 606 . 162 LEU N N 118.45 0.05 1 607 . 163 ALA H H 7.23 0.02 1 608 . 163 ALA CA C 52.7 0.1 1 609 . 163 ALA CB C 19.5 0.1 1 610 . 163 ALA N N 115.85 0.05 1 611 . 164 GLY H H 7.67 0.02 1 612 . 164 GLY CA C 44.8 0.1 1 613 . 164 GLY N N 107.2 0.05 1 614 . 165 PRO CA C 64.6 0.1 1 615 . 165 PRO CB C 31.2 0.1 1 616 . 166 ALA H H 7.88 0.02 1 617 . 166 ALA CA C 52.9 0.1 1 618 . 166 ALA CB C 18.7 0.1 1 619 . 166 ALA N N 119.54 0.05 1 620 . 167 GLY H H 7.72 0.02 1 621 . 167 GLY CA C 45.7 0.1 1 622 . 167 GLY N N 105.54 0.05 1 623 . 168 ASP H H 8.59 0.02 1 624 . 168 ASP CA C 57.0 0.1 1 625 . 168 ASP CB C 40.7 0.1 1 626 . 168 ASP N N 121.41 0.05 1 627 . 169 SER H H 9.16 0.02 1 628 . 169 SER CA C 61.0 0.1 1 629 . 169 SER CB C 62.8 0.1 1 630 . 169 SER N N 113.79 0.05 1 631 . 170 ASN H H 7.72 0.02 1 632 . 170 ASN CA C 52.0 0.1 1 633 . 170 ASN CB C 39.2 0.1 1 634 . 170 ASN N N 119.46 0.05 1 635 . 171 VAL H H 7.13 0.02 1 636 . 171 VAL CA C 62.0 0.1 1 637 . 171 VAL CB C 32.6 0.1 1 638 . 171 VAL N N 118.49 0.05 1 639 . 172 VAL H H 8.38 0.02 1 640 . 172 VAL CA C 61.3 0.1 1 641 . 172 VAL CB C 33.7 0.1 1 642 . 172 VAL N N 129.64 0.05 1 643 . 173 LYS H H 8.38 0.02 1 644 . 173 LYS CA C 55.0 0.1 1 645 . 173 LYS CB C 33.0 0.1 1 646 . 173 LYS N N 126.31 0.05 1 647 . 174 LEU H H 9.04 0.02 1 648 . 174 LEU CA C 52.7 0.1 1 649 . 174 LEU CB C 43.4 0.1 1 650 . 174 LEU N N 123.52 0.05 1 651 . 175 GLN H H 9.23 0.02 1 652 . 175 GLN CA C 58.3 0.1 1 653 . 175 GLN CB C 29.1 0.1 1 654 . 175 GLN N N 124.51 0.05 1 655 . 176 ARG H H 7.68 0.02 1 656 . 176 ARG CA C 53.5 0.1 1 657 . 176 ARG CB C 31.7 0.1 1 658 . 176 ARG N N 113.82 0.05 1 659 . 177 ILE H H 8.49 0.02 1 660 . 177 ILE CA C 60.7 0.1 1 661 . 177 ILE CB C 37.2 0.1 1 662 . 177 ILE N N 123.49 0.05 1 663 . 178 GLU H H 9.36 0.02 1 664 . 178 GLU CA C 59.5 0.1 1 665 . 178 GLU CB C 27.5 0.1 1 666 . 178 GLU N N 121.12 0.05 1 667 . 179 ASP H H 7.40 0.02 1 668 . 179 ASP CA C 54.7 0.1 1 669 . 179 ASP CB C 41.1 0.1 1 670 . 179 ASP N N 116.29 0.05 1 671 . 180 LEU H H 7.95 0.02 1 672 . 180 LEU CA C 59.2 0.1 1 673 . 180 LEU CB C 38.9 0.1 1 674 . 180 LEU N N 121.25 0.05 1 675 . 181 PRO CA C 66.5 0.1 1 676 . 181 PRO CB C 29.9 0.1 1 677 . 182 THR H H 6.91 0.02 1 678 . 182 THR CA C 63.4 0.1 1 679 . 182 THR CB C 68.5 0.1 1 680 . 182 THR N N 107.38 0.05 1 681 . 183 MET H H 7.75 0.02 1 682 . 183 MET CA C 58.1 0.1 1 683 . 183 MET CB C 32.5 0.1 1 684 . 183 MET N N 120.14 0.05 1 685 . 184 VAL H H 7.47 0.02 1 686 . 184 VAL CA C 62.5 0.1 1 687 . 184 VAL CB C 31.8 0.1 1 688 . 184 VAL N N 112.1 0.05 1 689 . 185 THR H H 7.78 0.02 1 690 . 185 THR CA C 63.5 0.1 1 691 . 185 THR CB C 69.2 0.1 1 692 . 185 THR N N 111.36 0.05 1 693 . 186 LEU H H 7.88 0.02 1 694 . 186 LEU CA C 55.3 0.1 1 695 . 186 LEU CB C 41.2 0.1 1 696 . 186 LEU N N 122.03 0.05 1 697 . 187 GLY H H 7.90 0.02 1 698 . 187 GLY CA C 45.2 0.1 1 699 . 187 GLY N N 108.85 0.05 1 700 . 188 ASN H H 8.80 0.02 1 701 . 188 ASN N N 114.67 0.05 1 702 . 190 PHE H H 8.58 0.02 1 703 . 190 PHE CA C 61.0 0.1 1 704 . 190 PHE CB C 38.7 0.1 1 705 . 190 PHE N N 123.27 0.05 1 706 . 191 LEU H H 7.82 0.02 1 707 . 191 LEU CA C 57.6 0.1 1 708 . 191 LEU CB C 40.2 0.1 1 709 . 191 LEU N N 118.04 0.05 1 710 . 192 HIS H H 7.99 0.02 1 711 . 192 HIS CA C 58.4 0.1 1 712 . 192 HIS CB C 28.8 0.1 1 713 . 192 HIS N N 116.15 0.05 1 714 . 193 LYS H H 7.74 0.02 1 715 . 193 LYS CA C 58.6 0.1 1 716 . 193 LYS CB C 31.7 0.1 1 717 . 193 LYS N N 119.79 0.05 1 718 . 194 LEU H H 7.16 0.02 1 719 . 194 LEU CA C 56.0 0.1 1 720 . 194 LEU CB C 41.0 0.1 1 721 . 194 LEU N N 118.05 0.05 1 722 . 195 CYS H H 7.75 0.02 1 723 . 195 CYS CA C 55.4 0.1 1 724 . 195 CYS CB C 41.4 0.1 1 725 . 195 CYS N N 112.4 0.05 1 726 . 196 SER H H 7.86 0.02 1 727 . 196 SER CA C 58.6 0.1 1 728 . 196 SER CB C 64.2 0.1 1 729 . 196 SER N N 115.39 0.05 1 730 . 197 GLY H H 7.83 0.02 1 731 . 197 GLY CA C 46.2 0.1 1 732 . 197 GLY N N 116.42 0.05 1 stop_ save_