data_25199 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone (HN, NH, CO and CA) Chemical Shift Assignments for Ca(2+)-bound Myristoylated GCAP-2 in the Presence of 10 mM CHAPS ; _BMRB_accession_number 25199 _BMRB_flat_file_name bmr25199.str _Entry_type original _Submission_date 2014-09-04 _Accession_date 2014-09-04 _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 Margetic Aleksandra . . 2 Nannemann David . . 3 Meiler Jens . . 4 Huster Daniel . . 5 Theisgen Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 167 "13C chemical shifts" 356 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-10-07 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4492 'Unmyristoylated GCAP-2 with three calcium ions bound' stop_ _Original_release_date 2014-10-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Guanylate Cyclase-Activating Protein-2 Undergoes Structural Changes upon Binding to Detergent Micelles and Bicelles ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25051529 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Margetic Aleksandra . . 2 Nannemann David . . 3 Meiler Jens . . 4 Huster Daniel . . 5 Theisgen Stephan . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta - Biomembranes' _Journal_volume 1838 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2767 _Page_last 2777 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name myrGCAP2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label myrGCAP-2 $myrGCAP2 'Ca2+ - 1' $entity_CA 'Ca2+ - 2' $entity_CA 'Ca2+ - 3' $entity_CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_myrGCAP2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common myrGCAP2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 203 _Mol_residue_sequence ; GQQFSWEEAEENGAVGAADA AQLQEWYKKFLEECPSGTLF MHEFKRFFKVPDNEEATQYV EAMFRAFDTNGDNTIDFLEY VAALNLVLRGTLEHKLKWTF KIYDKDRNGCIDRQELLDIV ESIYKLKKACSVEVEAEQQG KLLTPEEVVDRIFLLVDENG DGQLSLNEFVEGARRDKWVM KMLQMDLNPSSWISQQRRKS AMF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 GLY 2 3 GLN 3 4 GLN 4 5 PHE 5 6 SER 6 7 TRP 7 8 GLU 8 9 GLU 9 10 ALA 10 11 GLU 11 12 GLU 12 13 ASN 13 14 GLY 14 15 ALA 15 16 VAL 16 17 GLY 17 18 ALA 18 19 ALA 19 20 ASP 20 21 ALA 21 22 ALA 22 23 GLN 23 24 LEU 24 25 GLN 25 26 GLU 26 27 TRP 27 28 TYR 28 29 LYS 29 30 LYS 30 31 PHE 31 32 LEU 32 33 GLU 33 34 GLU 34 35 CYS 35 36 PRO 36 37 SER 37 38 GLY 38 39 THR 39 40 LEU 40 41 PHE 41 42 MET 42 43 HIS 43 44 GLU 44 45 PHE 45 46 LYS 46 47 ARG 47 48 PHE 48 49 PHE 49 50 LYS 50 51 VAL 51 52 PRO 52 53 ASP 53 54 ASN 54 55 GLU 55 56 GLU 56 57 ALA 57 58 THR 58 59 GLN 59 60 TYR 60 61 VAL 61 62 GLU 62 63 ALA 63 64 MET 64 65 PHE 65 66 ARG 66 67 ALA 67 68 PHE 68 69 ASP 69 70 THR 70 71 ASN 71 72 GLY 72 73 ASP 73 74 ASN 74 75 THR 75 76 ILE 76 77 ASP 77 78 PHE 78 79 LEU 79 80 GLU 80 81 TYR 81 82 VAL 82 83 ALA 83 84 ALA 84 85 LEU 85 86 ASN 86 87 LEU 87 88 VAL 88 89 LEU 89 90 ARG 90 91 GLY 91 92 THR 92 93 LEU 93 94 GLU 94 95 HIS 95 96 LYS 96 97 LEU 97 98 LYS 98 99 TRP 99 100 THR 100 101 PHE 101 102 LYS 102 103 ILE 103 104 TYR 104 105 ASP 105 106 LYS 106 107 ASP 107 108 ARG 108 109 ASN 109 110 GLY 110 111 CYS 111 112 ILE 112 113 ASP 113 114 ARG 114 115 GLN 115 116 GLU 116 117 LEU 117 118 LEU 118 119 ASP 119 120 ILE 120 121 VAL 121 122 GLU 122 123 SER 123 124 ILE 124 125 TYR 125 126 LYS 126 127 LEU 127 128 LYS 128 129 LYS 129 130 ALA 130 131 CYS 131 132 SER 132 133 VAL 133 134 GLU 134 135 VAL 135 136 GLU 136 137 ALA 137 138 GLU 138 139 GLN 139 140 GLN 140 141 GLY 141 142 LYS 142 143 LEU 143 144 LEU 144 145 THR 145 146 PRO 146 147 GLU 147 148 GLU 148 149 VAL 149 150 VAL 150 151 ASP 151 152 ARG 152 153 ILE 153 154 PHE 154 155 LEU 155 156 LEU 156 157 VAL 157 158 ASP 158 159 GLU 159 160 ASN 160 161 GLY 161 162 ASP 162 163 GLY 163 164 GLN 164 165 LEU 165 166 SER 166 167 LEU 167 168 ASN 168 169 GLU 169 170 PHE 170 171 VAL 171 172 GLU 172 173 GLY 173 174 ALA 174 175 ARG 175 176 ARG 176 177 ASP 177 178 LYS 178 179 TRP 179 180 VAL 180 181 MET 181 182 LYS 182 183 MET 183 184 LEU 184 185 GLN 185 186 MET 186 187 ASP 187 188 LEU 188 189 ASN 189 190 PRO 190 191 SER 191 192 SER 192 193 TRP 193 194 ILE 194 195 SER 195 196 GLN 196 197 GLN 197 198 ARG 198 199 ARG 199 200 LYS 200 201 SER 201 202 ALA 202 203 MET 203 204 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 BMRB 4492 "guanylate cyclase activating protein 2" 100.00 204 100.00 100.00 2.96e-147 PDB 1JBA "Unmyristoylated Gcap-2 With Three Calcium Ions Bound" 100.00 204 100.00 100.00 2.96e-147 GB AAA83214 "guanylyl cyclase-activating protein 2 [Bos taurus]" 100.00 204 100.00 100.00 2.96e-147 GB AAC48478 "retinal guanylyl cyclase activator protein p24 [Bos taurus]" 100.00 204 100.00 100.00 2.96e-147 GB ELR53264 "Guanylyl cyclase-activating protein 2 [Bos mutus]" 100.00 204 99.51 99.51 1.49e-146 REF NP_777211 "guanylyl cyclase-activating protein 2 [Bos taurus]" 100.00 204 100.00 100.00 2.96e-147 REF XP_005900200 "PREDICTED: guanylyl cyclase-activating protein 2 [Bos mutus]" 100.00 204 99.51 99.51 1.49e-146 REF XP_006069256 "PREDICTED: guanylyl cyclase-activating protein 2 [Bubalus bubalis]" 100.00 204 97.54 99.01 2.07e-144 REF XP_010816471 "PREDICTED: guanylyl cyclase-activating protein 2 isoform X1 [Bos taurus]" 80.79 181 98.78 98.78 1.52e-113 REF XP_010861473 "PREDICTED: guanylyl cyclase-activating protein 2 [Bison bison bison]" 100.00 204 99.01 99.51 7.88e-146 SP P51177 "RecName: Full=Guanylyl cyclase-activating protein 2; Short=GCAP 2; AltName: Full=Guanylate cyclase activator 1B; AltName: Full=" 100.00 204 100.00 100.00 2.96e-147 TPG DAA16519 "TPA: guanylyl cyclase-activating protein 2 [Bos taurus]" 100.00 204 99.51 99.51 1.49e-146 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . 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 $myrGCAP2 'domestic cow' 9913 Eukaryota Metazoa Bos taurus 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 $myrGCAP2 'recombinant technology' . Escherichia coli . pET11a 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 $myrGCAP2 . mM 0.2 0.5 '[U-100% 13C; U-100% 15N]' CaCl2 10 mM . . 'natural abundance' CHAPS 10 mM . . 'natural abundance' MES 20 mM . . 'natural abundance' TCEP 2 mM . . 'natural abundance' H2O 95 % . . 'natural abundance' D2O 5 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 323 . K pH 6.0 . pH pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name myrGCAP-2 _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 1 GLY H H 7.86 0.02 1 2 2 1 GLY C C 174.53 0.10 1 3 2 1 GLY CA C 45.43 0.30 1 4 2 1 GLY N N 111.07 0.40 1 5 3 2 GLN H H 8.21 0.02 1 6 3 2 GLN C C 176.99 0.10 1 7 3 2 GLN CA C 56.93 0.30 1 8 3 2 GLN N N 118.99 0.40 1 9 4 3 GLN H H 8.2 0.02 1 10 4 3 GLN C C 176.5 0.10 1 11 4 3 GLN CA C 57.18 0.30 1 12 4 3 GLN N N 120.62 0.40 1 13 5 4 PHE H H 8.19 0.02 1 14 5 4 PHE CA C 57.17 0.30 1 15 5 4 PHE N N 118.38 0.40 1 16 6 5 SER C C 174.16 0.10 1 17 6 5 SER CA C 57.42 0.30 1 18 7 6 TRP H H 8.08 0.02 1 19 7 6 TRP C C 176.17 0.10 1 20 7 6 TRP CA C 57.92 0.30 1 21 7 6 TRP N N 123.45 0.40 1 22 8 7 GLU H H 8.18 0.02 1 23 8 7 GLU C C 176.61 0.10 1 24 8 7 GLU CA C 57.2 0.30 1 25 8 7 GLU N N 120.41 0.40 1 26 9 8 GLU H H 8.01 0.02 1 27 9 8 GLU C C 176.41 0.10 1 28 9 8 GLU CA C 56.94 0.30 1 29 9 8 GLU N N 120.41 0.40 1 30 10 9 ALA H H 7.97 0.02 1 31 10 9 ALA C C 177.81 0.10 1 32 10 9 ALA CA C 52.93 0.30 1 33 10 9 ALA N N 123.67 0.40 1 34 11 10 GLU H H 8.12 0.02 1 35 11 10 GLU CA C 56.43 0.30 1 36 11 10 GLU N N 118.99 0.40 1 37 12 11 GLU H H 8.1 0.02 1 38 12 11 GLU C C 175.17 0.10 1 39 12 11 GLU CA C 56.43 0.30 1 40 12 11 GLU N N 121.37 0.40 1 41 13 12 ASN H H 7.87 0.02 1 42 13 12 ASN C C 175.73 0.10 1 43 13 12 ASN CA C 53.68 0.30 1 44 13 12 ASN N N 124.88 0.40 1 45 14 13 GLY H H 8.15 0.02 1 46 14 13 GLY C C 173.9 0.10 1 47 14 13 GLY CA C 45.67 0.30 1 48 14 13 GLY N N 108.63 0.40 1 49 15 14 ALA H H 7.95 0.02 1 50 15 14 ALA C C 177.63 0.10 1 51 15 14 ALA CA C 52.68 0.30 1 52 15 14 ALA N N 123.07 0.40 1 53 16 15 VAL H H 7.83 0.02 1 54 16 15 VAL C C 176.5 0.10 1 55 16 15 VAL CA C 62.68 0.30 1 56 16 15 VAL N N 117.72 0.40 1 57 17 16 GLY H H 8.31 0.02 1 58 17 16 GLY C C 173.9 0.10 1 59 17 16 GLY CA C 45.45 0.30 1 60 17 16 GLY N N 111.62 0.40 1 61 18 17 ALA H H 7.96 0.02 1 62 18 17 ALA C C 177.91 0.10 1 63 18 17 ALA CA C 52.93 0.30 1 64 18 17 ALA N N 123.24 0.40 1 65 19 18 ALA H H 8.1 0.02 1 66 19 18 ALA C C 177.67 0.10 1 67 19 18 ALA CA C 52.94 0.30 1 68 19 18 ALA N N 121.69 0.40 1 69 20 19 ASP H H 7.88 0.02 1 70 20 19 ASP C C 176.75 0.10 1 71 20 19 ASP CA C 54.43 0.30 1 72 20 19 ASP N N 118.9 0.40 1 73 21 20 ALA H H 8.19 0.02 1 74 21 20 ALA C C 179.1 0.10 1 75 21 20 ALA CA C 54.93 0.30 1 76 21 20 ALA N N 123.26 0.40 1 77 22 21 ALA H H 8.01 0.02 1 78 22 21 ALA C C 180.05 0.10 1 79 22 21 ALA CA C 54.7 0.30 1 80 22 21 ALA N N 120.21 0.40 1 81 23 22 GLN H H 7.83 0.02 1 82 23 22 GLN C C 177.63 0.10 1 83 23 22 GLN CA C 58.17 0.30 1 84 23 22 GLN N N 117.85 0.40 1 85 24 23 LEU H H 7.83 0.02 1 86 24 23 LEU N N 117.88 0.40 1 87 25 24 GLN C C 178.37 0.10 1 88 25 24 GLN CA C 59.69 0.30 1 89 26 25 GLU H H 7.69 0.02 1 90 26 25 GLU C C 179.25 0.10 1 91 26 25 GLU CA C 59.43 0.30 1 92 26 25 GLU N N 119.02 0.40 1 93 27 26 TRP H H 8.16 0.02 1 94 27 26 TRP C C 180.16 0.10 1 95 27 26 TRP CA C 59.68 0.30 1 96 27 26 TRP N N 120.31 0.40 1 97 28 27 TYR H H 8.66 0.02 1 98 28 27 TYR C C 176.94 0.10 1 99 28 27 TYR CA C 60.18 0.30 1 100 28 27 TYR N N 122.43 0.40 1 101 29 28 LYS H H 8.01 0.02 1 102 29 28 LYS C C 178.86 0.10 1 103 29 28 LYS CA C 60.01 0.30 1 104 29 28 LYS N N 118.06 0.40 1 105 31 30 PHE C C 176.49 0.10 1 106 31 30 PHE CA C 61.68 0.30 1 107 32 31 LEU H H 7.64 0.02 1 108 32 31 LEU C C 178.76 0.10 1 109 32 31 LEU CA C 56.68 0.30 1 110 32 31 LEU N N 116.75 0.40 1 111 33 32 GLU H H 7.74 0.02 1 112 33 32 GLU C C 178.35 0.10 1 113 33 32 GLU CA C 58.69 0.30 1 114 33 32 GLU N N 116.76 0.40 1 115 34 33 GLU H H 7.48 0.02 1 116 34 33 GLU C C 176.68 0.10 1 117 34 33 GLU CA C 57.18 0.30 1 118 34 33 GLU N N 115.74 0.40 1 119 35 34 CYS H H 7.99 0.02 1 120 35 34 CYS CA C 55.68 0.30 1 121 35 34 CYS N N 117.98 0.40 1 122 36 35 PRO C C 177.98 0.10 1 123 36 35 PRO CA C 64.93 0.30 1 124 37 36 SER H H 8.09 0.02 1 125 37 36 SER C C 175.94 0.10 1 126 37 36 SER CA C 59.18 0.30 1 127 37 36 SER N N 111.27 0.40 1 128 38 37 GLY H H 8.56 0.02 1 129 38 37 GLY C C 172.4 0.10 1 130 38 37 GLY CA C 45.93 0.30 1 131 38 37 GLY N N 109.85 0.40 1 132 39 38 THR H H 7.33 0.02 1 133 39 38 THR CA C 60.18 0.30 1 134 39 38 THR N N 110.26 0.40 1 135 40 39 LEU C C 178.77 0.10 1 136 40 39 LEU CA C 56.91 0.30 1 137 41 40 PHE H H 8.13 0.02 1 138 41 40 PHE C C 178.46 0.10 1 139 41 40 PHE CA C 60.68 0.30 1 140 41 40 PHE N N 119.4 0.40 1 141 43 42 HIS C C 177.2 0.10 1 142 43 42 HIS CA C 59.45 0.30 1 143 44 43 GLU H H 7.07 0.02 1 144 44 43 GLU C C 178.08 0.10 1 145 44 43 GLU CA C 58.67 0.30 1 146 44 43 GLU N N 119.4 0.40 1 147 45 44 PHE H H 8.23 0.02 1 148 45 44 PHE C C 176.71 0.10 1 149 45 44 PHE CA C 61.68 0.30 1 150 45 44 PHE N N 121.61 0.40 1 151 46 45 LYS H H 8.27 0.02 1 152 46 45 LYS C C 178.12 0.10 1 153 46 45 LYS CA C 60.18 0.30 1 154 46 45 LYS N N 115.32 0.40 1 155 47 46 ARG H H 7.4 0.02 1 156 47 46 ARG C C 178.61 0.10 1 157 47 46 ARG CA C 58.68 0.30 1 158 47 46 ARG N N 117.16 0.40 1 159 52 51 PRO C C 175.9 0.10 1 160 52 51 PRO CA C 62.93 0.30 1 161 53 52 ASP H H 8.16 0.02 1 162 53 52 ASP C C 175.72 0.10 1 163 53 52 ASP CA C 54.58 0.30 1 164 53 52 ASP N N 118.79 0.40 1 165 54 53 ASN H H 7.83 0.02 1 166 54 53 ASN CA C 52.98 0.30 1 167 54 53 ASN N N 117.47 0.40 1 168 55 54 GLU C C 177.98 0.10 1 169 55 54 GLU CA C 58.71 0.30 1 170 56 55 GLU H H 8.88 0.02 1 171 56 55 GLU C C 178.16 0.10 1 172 56 55 GLU CA C 59.18 0.30 1 173 56 55 GLU N N 120.21 0.40 1 174 57 56 ALA H H 8.27 0.02 1 175 57 56 ALA C C 178.64 0.10 1 176 57 56 ALA CA C 54.18 0.30 1 177 57 56 ALA N N 121 0.40 1 178 58 57 THR H H 7.85 0.02 1 179 58 57 THR C C 175.96 0.10 1 180 58 57 THR CA C 66.55 0.30 1 181 58 57 THR N N 112.92 0.40 1 182 59 58 GLN H H 8.21 0.02 1 183 59 58 GLN C C 178.75 0.10 1 184 59 58 GLN CA C 59.39 0.30 1 185 59 58 GLN N N 119.75 0.40 1 186 60 59 TYR H H 7.92 0.02 1 187 60 59 TYR C C 176.08 0.10 1 188 60 59 TYR CA C 62.57 0.30 1 189 60 59 TYR N N 119.79 0.40 1 190 61 60 VAL C C 178.01 0.10 1 191 61 60 VAL CA C 66.95 0.30 1 192 62 61 GLU H H 8.3 0.02 1 193 62 61 GLU CA C 60.18 0.30 1 194 62 61 GLU N N 118.99 0.40 1 195 63 62 ALA C C 179.88 0.10 1 196 63 62 ALA CA C 55.09 0.30 1 197 64 63 MET H H 7.88 0.02 1 198 64 63 MET C C 177.05 0.10 1 199 64 63 MET CA C 58.93 0.30 1 200 64 63 MET N N 116.93 0.40 1 201 65 64 PHE C C 177.2 0.10 1 202 65 64 PHE CA C 61.93 0.30 1 203 66 65 ARG H H 7.98 0.02 1 204 66 65 ARG C C 178 0.10 1 205 66 65 ARG CA C 59.18 0.30 1 206 66 65 ARG N N 115.92 0.40 1 207 67 66 ALA H H 7.44 0.02 1 208 67 66 ALA C C 178.82 0.10 1 209 67 66 ALA CA C 54.18 0.30 1 210 67 66 ALA N N 119.51 0.40 1 211 68 67 PHE H H 7.46 0.02 1 212 68 67 PHE CA C 58.43 0.30 1 213 68 67 PHE N N 114.32 0.40 1 214 70 69 THR C C 176.22 0.10 1 215 70 69 THR CA C 65.18 0.30 1 216 71 70 ASN H H 8.05 0.02 1 217 71 70 ASN C C 176.66 0.10 1 218 71 70 ASN CA C 52.17 0.30 1 219 71 70 ASN N N 115.75 0.40 1 220 72 71 GLY H H 7.63 0.02 1 221 72 71 GLY C C 174.55 0.10 1 222 72 71 GLY CA C 47.68 0.30 1 223 72 71 GLY N N 109.04 0.40 1 224 73 72 ASP H H 8.15 0.02 1 225 73 72 ASP C C 177.03 0.10 1 226 73 72 ASP CA C 53.19 0.30 1 227 73 72 ASP N N 119.59 0.40 1 228 74 73 ASN H H 10.23 0.02 1 229 74 73 ASN C C 173.66 0.10 1 230 74 73 ASN CA C 55.18 0.30 1 231 74 73 ASN N N 116.83 0.40 1 232 75 74 THR H H 8.01 0.02 1 233 75 74 THR C C 173.13 0.10 1 234 75 74 THR CA C 60.68 0.30 1 235 75 74 THR N N 110.05 0.40 1 236 76 75 ILE H H 9.12 0.02 1 237 76 75 ILE C C 175.04 0.10 1 238 76 75 ILE CA C 59.68 0.30 1 239 76 75 ILE N N 128.14 0.40 1 240 77 76 ASP H H 8.78 0.02 1 241 77 76 ASP C C 176.5 0.10 1 242 77 76 ASP CA C 52.18 0.30 1 243 77 76 ASP N N 127.31 0.40 1 244 78 77 PHE H H 8.37 0.02 1 245 78 77 PHE C C 176.54 0.10 1 246 78 77 PHE CA C 61.43 0.30 1 247 78 77 PHE N N 116.16 0.40 1 248 79 78 LEU H H 7.9 0.02 1 249 79 78 LEU C C 180.27 0.10 1 250 79 78 LEU CA C 57.93 0.30 1 251 79 78 LEU N N 116.56 0.40 1 252 80 79 GLU H H 8.4 0.02 1 253 80 79 GLU C C 180.09 0.10 1 254 80 79 GLU CA C 58.93 0.30 1 255 80 79 GLU N N 121.74 0.40 1 256 81 80 TYR H H 8.52 0.02 1 257 81 80 TYR CA C 61.43 0.30 1 258 81 80 TYR N N 122.84 0.40 1 259 82 81 VAL H H 8.11 0.02 1 260 82 81 VAL C C 178.57 0.10 1 261 82 81 VAL CA C 66.44 0.30 1 262 82 81 VAL N N 117.98 0.40 1 263 83 82 ALA H H 7.97 0.02 1 264 83 82 ALA C C 179.95 0.10 1 265 83 82 ALA CA C 55.18 0.30 1 266 83 82 ALA N N 121.43 0.40 1 267 84 83 ALA H H 7.69 0.02 1 268 84 83 ALA C C 178.89 0.10 1 269 84 83 ALA CA C 54.93 0.30 1 270 84 83 ALA N N 121.22 0.40 1 271 85 84 LEU H H 7.82 0.02 1 272 85 84 LEU C C 178.86 0.10 1 273 85 84 LEU CA C 57.93 0.30 1 274 85 84 LEU N N 116.56 0.40 1 275 86 85 ASN H H 7.87 0.02 1 276 86 85 ASN C C 176.92 0.10 1 277 86 85 ASN CA C 56.95 0.30 1 278 86 85 ASN N N 115.54 0.40 1 279 87 86 LEU H H 7.61 0.02 1 280 87 86 LEU C C 178.58 0.10 1 281 87 86 LEU CA C 58.43 0.30 1 282 87 86 LEU N N 120.22 0.40 1 283 88 87 VAL H H 7.8 0.02 1 284 88 87 VAL C C 177.46 0.10 1 285 88 87 VAL CA C 65.93 0.30 1 286 88 87 VAL N N 115.14 0.40 1 287 90 89 ARG C C 176.71 0.10 1 288 90 89 ARG CA C 55.43 0.30 1 289 91 90 GLY H H 7.74 0.02 1 290 91 90 GLY C C 174.46 0.10 1 291 91 90 GLY CA C 45.94 0.30 1 292 91 90 GLY N N 108.23 0.40 1 293 93 92 LEU C C 178.54 0.10 1 294 93 92 LEU CA C 58.93 0.30 1 295 94 93 GLU H H 8.58 0.02 1 296 94 93 GLU C C 178.28 0.10 1 297 94 93 GLU CA C 60.93 0.30 1 298 94 93 GLU N N 116.94 0.40 1 299 95 94 HIS H H 7.55 0.02 1 300 95 94 HIS C C 178.67 0.10 1 301 95 94 HIS CA C 59.68 0.30 1 302 95 94 HIS N N 117.88 0.40 1 303 96 95 LYS H H 8.39 0.02 1 304 96 95 LYS C C 180.12 0.10 1 305 96 95 LYS CA C 60.68 0.30 1 306 96 95 LYS N N 119.35 0.40 1 307 97 96 LEU H H 8.73 0.02 1 308 97 96 LEU C C 178.78 0.10 1 309 97 96 LEU CA C 58.43 0.30 1 310 97 96 LEU N N 121.35 0.40 1 311 98 97 LYS H H 8.14 0.02 1 312 98 97 LYS C C 178.44 0.10 1 313 98 97 LYS CA C 60.44 0.30 1 314 98 97 LYS N N 119.25 0.40 1 315 99 98 TRP H H 7.98 0.02 1 316 99 98 TRP C C 177.37 0.10 1 317 99 98 TRP CA C 61.68 0.30 1 318 99 98 TRP N N 120.42 0.40 1 319 100 99 THR H H 8.21 0.02 1 320 100 99 THR C C 175.44 0.10 1 321 100 99 THR CA C 67.18 0.30 1 322 100 99 THR N N 114.73 0.40 1 323 101 100 PHE H H 8.03 0.02 1 324 101 100 PHE C C 176.12 0.10 1 325 101 100 PHE CA C 61.93 0.30 1 326 101 100 PHE N N 121.03 0.40 1 327 102 101 LYS H H 7.23 0.02 1 328 102 101 LYS C C 178.68 0.10 1 329 102 101 LYS CA C 58.91 0.30 1 330 102 101 LYS N N 113.7 0.40 1 331 103 102 ILE H H 7.33 0.02 1 332 103 102 ILE C C 176.6 0.10 1 333 103 102 ILE CA C 63.72 0.30 1 334 103 102 ILE N N 118.18 0.40 1 335 104 103 TYR C C 176.5 0.10 1 336 104 103 TYR CA C 58.67 0.30 1 337 105 104 ASP H H 7.27 0.02 1 338 105 104 ASP C C 177.17 0.10 1 339 105 104 ASP CA C 52.68 0.30 1 340 105 104 ASP N N 116.36 0.40 1 341 106 105 LYS H H 7.66 0.02 1 342 106 105 LYS C C 177.42 0.10 1 343 106 105 LYS CA C 59.93 0.30 1 344 106 105 LYS N N 128.13 0.40 1 345 107 106 ASP H H 8.13 0.02 1 346 107 106 ASP C C 176.22 0.10 1 347 107 106 ASP CA C 53.18 0.30 1 348 107 106 ASP N N 113.71 0.40 1 349 108 107 ARG H H 7.72 0.02 1 350 108 107 ARG C C 175.97 0.10 1 351 108 107 ARG CA C 57.43 0.30 1 352 108 107 ARG N N 113.71 0.40 1 353 109 108 ASN H H 8.36 0.02 1 354 109 108 ASN C C 177.1 0.10 1 355 109 108 ASN CA C 52.67 0.30 1 356 109 108 ASN N N 118.17 0.40 1 357 110 109 GLY H H 10.47 0.02 1 358 110 109 GLY C C 173.51 0.10 1 359 110 109 GLY CA C 45.68 0.30 1 360 110 109 GLY N N 112.9 0.40 1 361 111 110 CYS H H 7.75 0.02 1 362 111 110 CYS C C 173.26 0.10 1 363 111 110 CYS CA C 56.18 0.30 1 364 111 110 CYS N N 115.33 0.40 1 365 112 111 ILE H H 9.41 0.02 1 366 112 111 ILE C C 175.97 0.10 1 367 112 111 ILE CA C 60.15 0.30 1 368 112 111 ILE N N 126.91 0.40 1 369 113 112 ASP H H 9.05 0.02 1 370 113 112 ASP C C 176.09 0.10 1 371 113 112 ASP CA C 52.66 0.30 1 372 113 112 ASP N N 128.95 0.40 1 373 114 113 ARG H H 8.33 0.02 1 374 114 113 ARG C C 178.09 0.10 1 375 114 113 ARG CA C 60.68 0.30 1 376 114 113 ARG N N 117.8 0.40 1 377 115 114 GLN H H 8.09 0.02 1 378 115 114 GLN C C 178.37 0.10 1 379 115 114 GLN CA C 58.68 0.30 1 380 115 114 GLN N N 117.76 0.40 1 381 116 115 GLU H H 8.43 0.02 1 382 116 115 GLU C C 179.58 0.10 1 383 116 115 GLU CA C 59.46 0.30 1 384 116 115 GLU N N 120.22 0.40 1 385 117 116 LEU H H 7.96 0.02 1 386 117 116 LEU C C 178.3 0.10 1 387 117 116 LEU CA C 57.68 0.30 1 388 117 116 LEU N N 117.86 0.40 1 389 118 117 LEU H H 8.45 0.02 1 390 118 117 LEU C C 177.85 0.10 1 391 118 117 LEU CA C 58.67 0.30 1 392 118 117 LEU N N 119.6 0.40 1 393 119 118 ASP H H 8.35 0.02 1 394 119 118 ASP C C 179.63 0.10 1 395 119 118 ASP CA C 57.68 0.30 1 396 119 118 ASP N N 117.57 0.40 1 397 120 119 ILE H H 7.39 0.02 1 398 120 119 ILE C C 178.01 0.10 1 399 120 119 ILE CA C 62.68 0.30 1 400 120 119 ILE N N 118.38 0.40 1 401 121 120 VAL H H 8.67 0.02 1 402 121 120 VAL C C 178.49 0.10 1 403 121 120 VAL CA C 67.68 0.30 1 404 121 120 VAL N N 121.51 0.40 1 405 122 121 GLU H H 9.21 0.02 1 406 122 121 GLU C C 179.12 0.10 1 407 122 121 GLU CA C 60.43 0.30 1 408 122 121 GLU N N 118.58 0.40 1 409 123 122 SER H H 7.63 0.02 1 410 123 122 SER C C 176.42 0.10 1 411 123 122 SER CA C 62.69 0.30 1 412 123 122 SER N N 114.93 0.40 1 413 124 123 ILE H H 8.37 0.02 1 414 124 123 ILE C C 178.03 0.10 1 415 124 123 ILE CA C 64.93 0.30 1 416 124 123 ILE N N 122.64 0.40 1 417 125 124 TYR H H 8.67 0.02 1 418 125 124 TYR C C 178.84 0.10 1 419 125 124 TYR CA C 61.93 0.30 1 420 125 124 TYR N N 121.44 0.40 1 421 126 125 LYS H H 8.07 0.02 1 422 126 125 LYS C C 179.32 0.10 1 423 126 125 LYS CA C 59.93 0.30 1 424 126 125 LYS N N 118.59 0.40 1 425 127 126 LEU H H 8.02 0.02 1 426 127 126 LEU C C 178.5 0.10 1 427 127 126 LEU CA C 57.93 0.30 1 428 127 126 LEU N N 121.22 0.40 1 429 128 127 LYS H H 8.35 0.02 1 430 128 127 LYS C C 178.61 0.10 1 431 128 127 LYS CA C 59.44 0.30 1 432 128 127 LYS N N 119 0.40 1 433 129 128 LYS H H 7.67 0.02 1 434 129 128 LYS C C 178.47 0.10 1 435 129 128 LYS CA C 58.43 0.30 1 436 129 128 LYS N N 118.18 0.40 1 437 130 129 ALA H H 7.81 0.02 1 438 130 129 ALA C C 178.68 0.10 1 439 130 129 ALA CA C 53.93 0.30 1 440 130 129 ALA N N 121.22 0.40 1 441 131 130 CYS H H 7.77 0.02 1 442 131 130 CYS C C 174.04 0.10 1 443 131 130 CYS CA C 59.43 0.30 1 444 131 130 CYS N N 113.92 0.40 1 445 132 131 SER H H 7.86 0.02 1 446 132 131 SER C C 174.1 0.10 1 447 132 131 SER CA C 58.68 0.30 1 448 132 131 SER N N 115.13 0.40 1 449 133 132 VAL H H 7.85 0.02 1 450 133 132 VAL C C 175.82 0.10 1 451 133 132 VAL CA C 62.19 0.30 1 452 133 132 VAL N N 119.39 0.40 1 453 134 133 GLU H H 8.22 0.02 1 454 134 133 GLU C C 176.36 0.10 1 455 134 133 GLU CA C 56.68 0.30 1 456 134 133 GLU N N 123.36 0.40 1 457 135 134 VAL H H 7.92 0.02 1 458 135 134 VAL C C 176.08 0.10 1 459 135 134 VAL CA C 62.67 0.30 1 460 135 134 VAL N N 120.21 0.40 1 461 136 135 GLU H H 8.31 0.02 1 462 136 135 GLU C C 176.5 0.10 1 463 136 135 GLU CA C 57.18 0.30 1 464 136 135 GLU N N 123.46 0.40 1 465 137 136 ALA H H 8.08 0.02 1 466 137 136 ALA C C 177.95 0.10 1 467 137 136 ALA CA C 53.18 0.30 1 468 137 136 ALA N N 123.87 0.40 1 469 138 137 GLU H H 8.19 0.02 1 470 138 137 GLU C C 176.87 0.10 1 471 138 137 GLU CA C 57.18 0.30 1 472 138 137 GLU N N 118.58 0.40 1 473 139 138 GLN H H 8.1 0.02 1 474 139 138 GLN C C 176.13 0.10 1 475 139 138 GLN CA C 56.43 0.30 1 476 139 138 GLN N N 119.39 0.40 1 477 140 139 GLN H H 8.21 0.02 1 478 140 139 GLN C C 176.38 0.10 1 479 140 139 GLN CA C 56.68 0.30 1 480 140 139 GLN N N 119.8 0.40 1 481 141 140 GLY H H 8.18 0.02 1 482 141 140 GLY C C 173.65 0.10 1 483 141 140 GLY CA C 45.43 0.30 1 484 141 140 GLY N N 108.63 0.40 1 485 142 141 LYS H H 7.83 0.02 1 486 142 141 LYS C C 175.8 0.10 1 487 142 141 LYS CA C 55.93 0.30 1 488 142 141 LYS N N 120.31 0.40 1 489 143 142 LEU H H 8.07 0.02 1 490 143 142 LEU C C 176.96 0.10 1 491 143 142 LEU CA C 54.94 0.30 1 492 143 142 LEU N N 124.26 0.40 1 493 144 143 LEU H H 8.16 0.02 1 494 144 143 LEU C C 177.84 0.10 1 495 144 143 LEU CA C 54.93 0.30 1 496 144 143 LEU N N 124.12 0.40 1 497 145 144 THR H H 8.73 0.02 1 498 145 144 THR C C 173.55 0.10 1 499 145 144 THR CA C 60.68 0.30 1 500 145 144 THR N N 114.94 0.40 1 501 146 145 PRO C C 177.45 0.10 1 502 146 145 PRO CA C 66.18 0.30 1 503 147 146 GLU H H 8.7 0.02 1 504 147 146 GLU C C 178.35 0.10 1 505 147 146 GLU CA C 60.68 0.30 1 506 147 146 GLU N N 114.93 0.40 1 507 148 147 GLU H H 7.49 0.02 1 508 148 147 GLU C C 180.09 0.10 1 509 148 147 GLU CA C 59.18 0.30 1 510 148 147 GLU N N 118.77 0.40 1 511 149 148 VAL H H 8.23 0.02 1 512 149 148 VAL C C 177.69 0.10 1 513 149 148 VAL CA C 67.68 0.30 1 514 149 148 VAL N N 120.62 0.40 1 515 150 149 VAL H H 8.17 0.02 1 516 150 149 VAL C C 177.69 0.10 1 517 150 149 VAL CA C 67.68 0.30 1 518 150 149 VAL N N 118.79 0.40 1 519 151 150 ASP H H 8.3 0.02 1 520 151 150 ASP C C 179.17 0.10 1 521 151 150 ASP CA C 57.93 0.30 1 522 151 150 ASP N N 118.99 0.40 1 523 152 151 ARG H H 8.04 0.02 1 524 152 151 ARG C C 178.19 0.10 1 525 152 151 ARG CA C 59.43 0.30 1 526 152 151 ARG N N 119.81 0.40 1 527 153 152 ILE H H 8.66 0.02 1 528 153 152 ILE C C 178.1 0.10 1 529 153 152 ILE CA C 66.19 0.30 1 530 153 152 ILE N N 118.32 0.40 1 531 154 153 PHE H H 8.68 0.02 1 532 154 153 PHE C C 178.51 0.10 1 533 154 153 PHE CA C 64.43 0.30 1 534 154 153 PHE N N 118.32 0.40 1 535 155 154 LEU H H 8.06 0.02 1 536 155 154 LEU C C 179.08 0.10 1 537 155 154 LEU CA C 58.43 0.30 1 538 155 154 LEU N N 119.2 0.40 1 539 156 155 LEU H H 7.66 0.02 1 540 156 155 LEU C C 179.03 0.10 1 541 156 155 LEU CA C 56.68 0.30 1 542 156 155 LEU N N 115.55 0.40 1 543 157 156 VAL H H 8.35 0.02 1 544 157 156 VAL C C 176.43 0.10 1 545 157 156 VAL CA C 62.93 0.30 1 546 157 156 VAL N N 114.33 0.40 1 547 158 157 ASP H H 8.14 0.02 1 548 158 157 ASP C C 177.13 0.10 1 549 158 157 ASP CA C 53.43 0.30 1 550 158 157 ASP N N 119.47 0.40 1 551 159 158 GLU H H 7.9 0.02 1 552 159 158 GLU C C 177.25 0.10 1 553 159 158 GLU CA C 59.18 0.30 1 554 159 158 GLU N N 128.95 0.40 1 555 160 159 ASN H H 7.91 0.02 1 556 160 159 ASN C C 176.64 0.10 1 557 160 159 ASN CA C 51.69 0.30 1 558 160 159 ASN N N 111.89 0.40 1 559 161 160 GLY H H 7.62 0.02 1 560 161 160 GLY C C 174.66 0.10 1 561 161 160 GLY CA C 47.69 0.30 1 562 161 160 GLY N N 108.62 0.40 1 563 162 161 ASP H H 8 0.02 1 564 162 161 ASP C C 177.78 0.10 1 565 162 161 ASP CA C 53.43 0.30 1 566 162 161 ASP N N 117.63 0.40 1 567 163 162 GLY H H 10.35 0.02 1 568 163 162 GLY C C 173.16 0.10 1 569 163 162 GLY CA C 46.34 0.30 1 570 163 162 GLY N N 112.41 0.40 1 571 164 163 GLN H H 8.07 0.02 1 572 164 163 GLN C C 174.96 0.10 1 573 164 163 GLN CA C 53.68 0.30 1 574 164 163 GLN N N 115.94 0.40 1 575 165 164 LEU H H 9.79 0.02 1 576 165 164 LEU C C 176.76 0.10 1 577 165 164 LEU CA C 52.95 0.30 1 578 165 164 LEU N N 124.33 0.40 1 579 166 165 SER H H 9.15 0.02 1 580 166 165 SER C C 174.58 0.10 1 581 166 165 SER CA C 56.93 0.30 1 582 166 165 SER N N 121.34 0.40 1 583 167 166 LEU H H 8.43 0.02 1 584 167 166 LEU C C 178.2 0.10 1 585 167 166 LEU CA C 58.94 0.30 1 586 167 166 LEU N N 122.85 0.40 1 587 168 167 ASN H H 8.15 0.02 1 588 168 167 ASN CA C 56.68 0.30 1 589 168 167 ASN N N 114.12 0.40 1 590 169 168 GLU H H 7.57 0.02 1 591 169 168 GLU C C 179.28 0.10 1 592 169 168 GLU CA C 59.18 0.30 1 593 169 168 GLU N N 118.16 0.40 1 594 170 169 PHE H H 8.5 0.02 1 595 170 169 PHE C C 175.81 0.10 1 596 170 169 PHE CA C 62.18 0.30 1 597 170 169 PHE N N 120.21 0.40 1 598 171 170 VAL H H 8.49 0.02 1 599 171 170 VAL C C 177.77 0.10 1 600 171 170 VAL CA C 66.68 0.30 1 601 171 170 VAL N N 115.95 0.40 1 602 172 171 GLU H H 8.02 0.02 1 603 172 171 GLU C C 179.73 0.10 1 604 172 171 GLU CA C 58.93 0.30 1 605 172 171 GLU N N 116.15 0.40 1 606 173 172 GLY H H 8.46 0.02 1 607 173 172 GLY C C 174.89 0.10 1 608 173 172 GLY CA C 47.18 0.30 1 609 173 172 GLY N N 107 0.40 1 610 174 173 ALA H H 7.63 0.02 1 611 174 173 ALA C C 177.7 0.10 1 612 174 173 ALA CA C 54.43 0.30 1 613 174 173 ALA N N 121.62 0.40 1 614 175 174 ARG H H 7.47 0.02 1 615 175 174 ARG C C 177.98 0.10 1 616 175 174 ARG CA C 58.67 0.30 1 617 175 174 ARG N N 112.68 0.40 1 618 176 175 ARG H H 7.57 0.02 1 619 176 175 ARG C C 175.94 0.10 1 620 176 175 ARG CA C 57.42 0.30 1 621 176 175 ARG N N 115.74 0.40 1 622 177 176 ASP H H 7.57 0.02 1 623 177 176 ASP C C 174.9 0.10 1 624 177 176 ASP CA C 54.18 0.30 1 625 177 176 ASP N N 120.32 0.40 1 626 178 177 LYS H H 8.5 0.02 1 627 178 177 LYS C C 178.54 0.10 1 628 178 177 LYS CA C 59.18 0.30 1 629 178 177 LYS N N 125.08 0.40 1 630 179 178 TRP H H 8.59 0.02 1 631 179 178 TRP C C 177.7 0.10 1 632 179 178 TRP CA C 62.31 0.30 1 633 179 178 TRP N N 122.64 0.40 1 634 180 179 VAL H H 8.44 0.02 1 635 180 179 VAL C C 177.68 0.10 1 636 180 179 VAL CA C 67.43 0.30 1 637 180 179 VAL N N 120.01 0.40 1 638 181 180 MET H H 7.95 0.02 1 639 181 180 MET C C 177.75 0.10 1 640 181 180 MET CA C 59.17 0.30 1 641 181 180 MET N N 116.15 0.40 1 642 182 181 LYS H H 7.74 0.02 1 643 182 181 LYS CA C 59.45 0.30 1 644 182 181 LYS N N 118.79 0.40 1 645 191 190 SER C C 175.38 0.10 1 646 191 190 SER CA C 60.69 0.30 1 647 192 191 SER H H 7.91 0.02 1 648 192 191 SER C C 175.31 0.10 1 649 192 191 SER CA C 59.71 0.30 1 650 192 191 SER N N 116.15 0.40 1 651 193 192 TRP H H 7.36 0.02 1 652 193 192 TRP C C 176.78 0.10 1 653 193 192 TRP CA C 56.96 0.30 1 654 193 192 TRP N N 120.86 0.40 1 655 194 193 ILE H H 7.6 0.02 1 656 194 193 ILE C C 176.22 0.10 1 657 194 193 ILE CA C 62.06 0.30 1 658 194 193 ILE N N 117.77 0.40 1 659 195 194 SER H H 7.97 0.02 1 660 195 194 SER C C 175.06 0.10 1 661 195 194 SER CA C 58.93 0.30 1 662 195 194 SER N N 117.15 0.40 1 663 196 195 GLN H H 8.12 0.02 1 664 196 195 GLN C C 176.01 0.10 1 665 196 195 GLN CA C 58.86 0.30 1 666 196 195 GLN N N 121.33 0.40 1 667 197 196 GLN C C 175.13 0.10 1 668 197 196 GLN CA C 56.44 0.30 1 669 198 197 ARG H H 7.77 0.02 1 670 198 197 ARG N N 127.32 0.40 1 671 199 198 ARG CA C 56.43 0.30 1 672 200 199 LYS H H 8.15 0.02 1 673 200 199 LYS C C 176.47 0.10 1 674 200 199 LYS CA C 56.67 0.30 1 675 200 199 LYS N N 121.83 0.40 1 676 201 200 SER H H 8.06 0.02 1 677 201 200 SER C C 173.93 0.10 1 678 201 200 SER CA C 58.41 0.30 1 679 201 200 SER N N 115.96 0.40 1 680 202 201 ALA H H 8.04 0.02 1 681 202 201 ALA C C 177.05 0.10 1 682 202 201 ALA CA C 52.9 0.30 1 683 202 201 ALA N N 124.88 0.40 1 684 203 202 MET H H 7.98 0.02 1 685 203 202 MET C C 174.6 0.10 1 686 203 202 MET N N 118.59 0.40 1 687 204 203 PHE H H 7.43 0.02 1 688 204 203 PHE C C 179.88 0.10 1 689 204 203 PHE CA C 60.19 0.30 1 690 204 203 PHE N N 124.27 0.40 1 stop_ save_