data_17922 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N assignment of HIV-1 accessory protein Nef ; _BMRB_accession_number 17922 _BMRB_flat_file_name bmr17922.str _Entry_type original _Submission_date 2011-09-06 _Accession_date 2011-09-06 _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 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 153 "13C chemical shifts" 509 "15N chemical shifts" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-09-20 original author . stop_ _Original_release_date 2012-09-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21365684 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Gronenborn Angela M. . stop_ _Journal_abbreviation Proteins _Journal_name_full Proteins _Journal_volume 79 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1609 _Page_last 1622 _Year 2011 _Details . loop_ _Keyword AIDS Hck HIV Nef SH2 SH3 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Nef _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Nef $Nef 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_Nef _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Nef _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 217 _Mol_residue_sequence ; MEGKWSKRSVSGWPAVRERM RRAEPAAEGVGAVSRDLEKH GAITSSNTAATNAACAWLEA QEEEEVGFPVRPQVPLRPMT YKAAVDLSHFLKEKGGLEGL IYSQKRQDILDLWVYHTQGY FPDWQNYTPGPGIRYPLTFG WCFKLVPVEPEKVEEANEGE NNCLLHPMSQHGMDDPEKEV LVWKFDSKLAFHHMARELHP EYYKDCAAALEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLY 4 LYS 5 TRP 6 SER 7 LYS 8 ARG 9 SER 10 VAL 11 SER 12 GLY 13 TRP 14 PRO 15 ALA 16 VAL 17 ARG 18 GLU 19 ARG 20 MET 21 ARG 22 ARG 23 ALA 24 GLU 25 PRO 26 ALA 27 ALA 28 GLU 29 GLY 30 VAL 31 GLY 32 ALA 33 VAL 34 SER 35 ARG 36 ASP 37 LEU 38 GLU 39 LYS 40 HIS 41 GLY 42 ALA 43 ILE 44 THR 45 SER 46 SER 47 ASN 48 THR 49 ALA 50 ALA 51 THR 52 ASN 53 ALA 54 ALA 55 CYS 56 ALA 57 TRP 58 LEU 59 GLU 60 ALA 61 GLN 62 GLU 63 GLU 64 GLU 65 GLU 66 VAL 67 GLY 68 PHE 69 PRO 70 VAL 71 ARG 72 PRO 73 GLN 74 VAL 75 PRO 76 LEU 77 ARG 78 PRO 79 MET 80 THR 81 TYR 82 LYS 83 ALA 84 ALA 85 VAL 86 ASP 87 LEU 88 SER 89 HIS 90 PHE 91 LEU 92 LYS 93 GLU 94 LYS 95 GLY 96 GLY 97 LEU 98 GLU 99 GLY 100 LEU 101 ILE 102 TYR 103 SER 104 GLN 105 LYS 106 ARG 107 GLN 108 ASP 109 ILE 110 LEU 111 ASP 112 LEU 113 TRP 114 VAL 115 TYR 116 HIS 117 THR 118 GLN 119 GLY 120 TYR 121 PHE 122 PRO 123 ASP 124 TRP 125 GLN 126 ASN 127 TYR 128 THR 129 PRO 130 GLY 131 PRO 132 GLY 133 ILE 134 ARG 135 TYR 136 PRO 137 LEU 138 THR 139 PHE 140 GLY 141 TRP 142 CYS 143 PHE 144 LYS 145 LEU 146 VAL 147 PRO 148 VAL 149 GLU 150 PRO 151 GLU 152 LYS 153 VAL 154 GLU 155 GLU 156 ALA 157 ASN 158 GLU 159 GLY 160 GLU 161 ASN 162 ASN 163 CYS 164 LEU 165 LEU 166 HIS 167 PRO 168 MET 169 SER 170 GLN 171 HIS 172 GLY 173 MET 174 ASP 175 ASP 176 PRO 177 GLU 178 LYS 179 GLU 180 VAL 181 LEU 182 VAL 183 TRP 184 LYS 185 PHE 186 ASP 187 SER 188 LYS 189 LEU 190 ALA 191 PHE 192 HIS 193 HIS 194 MET 195 ALA 196 ARG 197 GLU 198 LEU 199 HIS 200 PRO 201 GLU 202 TYR 203 TYR 204 LYS 205 ASP 206 CYS 207 ALA 208 ALA 209 ALA 210 LEU 211 GLU 212 HIS 213 HIS 214 HIS 215 HIS 216 HIS 217 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-05 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 GB AAA03700 "HIV-1 consensus Nef protein [Human immunodeficiency virus 1]" 94.93 206 99.51 99.51 2.10e-150 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Nef HIV-1 11676 Viruses . Lentivirus HIV-1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $Nef 'recombinant technology' . Escherichia coli BL21 Rosetta2(DE3) pET21 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 $Nef 0.1 mM '[U-13C; U-15N; U-2H]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' DTT 10 mM 'natural abundance' HEPES 10 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.02 w/v 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . http://www.nmr.ch stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details ; CARA is the application for the analysis of NMR spectra and computer aided resonance assignment developed at and used by the group of Prof. Dr. Kurt W thrich, Institute of Molecular Biology and Biophysics, ETH Z rich. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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 'ionic strength' 0.1 . M pH 8.0 . pH pressure 1 . atm temperature 300 . K 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 C 13 'methyl protons' ppm 0.00 external indirect cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 1.000000000 DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 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 '2D 1H-15N HSQC' '3D HNCACB' '3D HNCA' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CO)CA' '3D HN(CA)CO' '3D 1H-15N NOESY' 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 Nef _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 14 14 PRO C C 178.4 0.3 1 2 14 14 PRO CA C 66.1 0.3 1 3 14 14 PRO CB C 29.5 0.3 1 4 15 15 ALA H H 7.31 0.02 1 5 15 15 ALA C C 180.3 0.3 1 6 15 15 ALA CA C 53.9 0.3 1 7 15 15 ALA CB C 17.5 0.3 1 8 15 15 ALA N N 117.8 0.3 1 9 16 16 VAL H H 7.36 0.02 1 10 16 16 VAL C C 177.3 0.3 1 11 16 16 VAL CA C 65.6 0.3 1 12 16 16 VAL CB C 30.2 0.3 1 13 16 16 VAL N N 122.4 0.3 1 14 17 17 ARG H H 8.11 0.02 1 15 17 17 ARG C C 178.7 0.3 1 16 17 17 ARG CA C 58.0 0.3 1 17 17 17 ARG CB C 26.7 0.3 1 18 17 17 ARG N N 120.4 0.3 1 19 18 18 GLU H H 7.04 0.02 1 20 18 18 GLU C C 178.1 0.3 1 21 18 18 GLU CA C 57.8 0.3 1 22 18 18 GLU CB C 27.7 0.3 1 23 18 18 GLU N N 118.9 0.3 1 24 19 19 ARG H H 7.57 0.02 1 25 19 19 ARG C C 180.0 0.3 1 26 19 19 ARG CA C 59.1 0.3 1 27 19 19 ARG CB C 28.7 0.3 1 28 19 19 ARG N N 119.9 0.3 1 29 20 20 MET H H 8.60 0.02 1 30 20 20 MET CA C 59.4 0.3 1 31 20 20 MET CB C 33.0 0.3 1 32 20 20 MET N N 116.8 0.3 1 33 21 21 ARG C C 178.1 0.3 1 34 21 21 ARG CA C 58.9 0.3 1 35 21 21 ARG CB C 28.7 0.3 1 36 22 22 ARG H H 7.73 0.02 1 37 22 22 ARG C C 176.2 0.3 1 38 22 22 ARG CA C 56.5 0.3 1 39 22 22 ARG CB C 29.3 0.3 1 40 22 22 ARG N N 115.3 0.3 1 41 23 23 ALA H H 7.35 0.02 1 42 23 23 ALA C C 176.3 0.3 1 43 23 23 ALA CA C 51.4 0.3 1 44 23 23 ALA CB C 16.2 0.3 1 45 23 23 ALA N N 123.6 0.3 1 46 24 24 GLU H H 7.84 0.02 1 47 24 24 GLU C C 175.1 0.3 1 48 24 24 GLU CA C 53.5 0.3 1 49 24 24 GLU CB C 29.2 0.3 1 50 24 24 GLU N N 122.0 0.3 1 51 25 25 PRO C C 176.6 0.3 1 52 25 25 PRO CA C 63.0 0.3 1 53 26 26 ALA H H 8.35 0.02 1 54 26 26 ALA C C 177.5 0.3 1 55 26 26 ALA CA C 51.9 0.3 1 56 26 26 ALA CB C 18.5 0.3 1 57 26 26 ALA N N 122.8 0.3 1 58 27 27 ALA H H 8.17 0.02 1 59 27 27 ALA C C 177.7 0.3 1 60 27 27 ALA CA C 52.0 0.3 1 61 27 27 ALA CB C 18.4 0.3 1 62 27 27 ALA N N 122.8 0.3 1 63 28 28 GLU H H 8.30 0.02 1 64 28 28 GLU C C 177.0 0.3 1 65 28 28 GLU CA C 56.2 0.3 1 66 28 28 GLU CB C 29.5 0.3 1 67 28 28 GLU N N 119.3 0.3 1 68 29 29 GLY H H 8.36 0.02 1 69 29 29 GLY C C 174.3 0.3 1 70 29 29 GLY CA C 44.7 0.3 1 71 29 29 GLY N N 109.4 0.3 1 72 30 30 VAL H H 7.99 0.02 1 73 30 30 VAL C C 176.9 0.3 1 74 30 30 VAL CA C 62.1 0.3 1 75 30 30 VAL CB C 31.5 0.3 1 76 30 30 VAL N N 118.9 0.3 1 77 31 31 GLY H H 8.49 0.02 1 78 31 31 GLY C C 173.8 0.3 1 79 31 31 GLY CA C 44.7 0.3 1 80 31 31 GLY N N 111.8 0.3 1 81 32 32 ALA H H 8.07 0.02 1 82 32 32 ALA C C 177.8 0.3 1 83 32 32 ALA CA C 52.0 0.3 1 84 32 32 ALA CB C 18.1 0.3 1 85 32 32 ALA N N 123.5 0.3 1 86 33 33 VAL H H 8.08 0.02 1 87 33 33 VAL C C 176.3 0.3 1 88 33 33 VAL CA C 61.7 0.3 1 89 33 33 VAL CB C 31.6 0.3 1 90 33 33 VAL N N 118.6 0.3 1 91 35 35 ARG C C 175.3 0.3 1 92 35 35 ARG CA C 55.7 0.3 1 93 35 35 ARG CB C 29.5 0.3 1 94 36 36 ASP H H 8.08 0.02 1 95 36 36 ASP C C 179.2 0.3 1 96 36 36 ASP CA C 54.5 0.3 1 97 36 36 ASP CB C 40.2 0.3 1 98 36 36 ASP N N 124.6 0.3 1 99 37 37 LEU H H 8.11 0.02 1 100 37 37 LEU C C 177.9 0.3 1 101 37 37 LEU CA C 55.3 0.3 1 102 37 37 LEU CB C 40.7 0.3 1 103 37 37 LEU N N 121.6 0.3 1 104 38 38 GLU H H 8.23 0.02 1 105 38 38 GLU C C 176.9 0.3 1 106 38 38 GLU CA C 56.5 0.3 1 107 38 38 GLU CB C 29.0 0.3 1 108 38 38 GLU N N 120.1 0.3 1 109 39 39 LYS H H 8.06 0.02 1 110 39 39 LYS C C 176.6 0.3 1 111 39 39 LYS CA C 56.2 0.3 1 112 39 39 LYS CB C 31.6 0.3 1 113 39 39 LYS N N 120.6 0.3 1 114 42 42 ALA C C 177.7 0.3 1 115 42 42 ALA CA C 51.9 0.3 1 116 42 42 ALA CB C 18.4 0.3 1 117 43 43 ILE H H 8.15 0.02 1 118 43 43 ILE C C 176.7 0.3 1 119 43 43 ILE CA C 60.7 0.3 1 120 43 43 ILE CB C 37.2 0.3 1 121 43 43 ILE N N 119.6 0.3 1 122 51 51 THR C C 173.4 0.3 1 123 51 51 THR CA C 60.9 0.3 1 124 51 51 THR CB C 69.2 0.3 1 125 52 52 ASN H H 8.00 0.02 1 126 52 52 ASN C C 179.2 0.3 1 127 52 52 ASN CA C 54.5 0.3 1 128 52 52 ASN CB C 40.1 0.3 1 129 52 52 ASN N N 125.5 0.3 1 130 53 53 ALA C C 177.1 0.3 1 131 53 53 ALA CA C 52.6 0.3 1 132 54 54 ALA H H 7.92 0.02 1 133 54 54 ALA C C 177.7 0.3 1 134 54 54 ALA CA C 51.8 0.3 1 135 54 54 ALA CB C 18.4 0.3 1 136 54 54 ALA N N 122.2 0.3 1 137 55 55 CYS H H 8.60 0.02 1 138 55 55 CYS C C 175.5 0.3 1 139 55 55 CYS CA C 56.6 0.3 1 140 55 55 CYS CB C 29.4 0.3 1 141 55 55 CYS N N 120.0 0.3 1 142 56 56 ALA H H 8.06 0.02 1 143 56 56 ALA C C 177.7 0.3 1 144 56 56 ALA CA C 52.8 0.3 1 145 56 56 ALA CB C 18.1 0.3 1 146 56 56 ALA N N 122.8 0.3 1 147 57 57 TRP H H 7.88 0.02 1 148 57 57 TRP C C 176.3 0.3 1 149 57 57 TRP CA C 57.1 0.3 1 150 57 57 TRP CB C 28.0 0.3 1 151 57 57 TRP N N 118.4 0.3 1 152 58 58 LEU H H 7.70 0.02 1 153 58 58 LEU C C 177.4 0.3 1 154 58 58 LEU CA C 55.0 0.3 1 155 58 58 LEU CB C 41.2 0.3 1 156 58 58 LEU N N 122.4 0.3 1 157 59 59 GLU H H 8.05 0.02 1 158 59 59 GLU C C 176.4 0.3 1 159 59 59 GLU CA C 56.3 0.3 1 160 59 59 GLU CB C 29.0 0.3 1 161 59 59 GLU N N 120.2 0.3 1 162 60 60 ALA H H 8.06 0.02 1 163 60 60 ALA C C 177.7 0.3 1 164 60 60 ALA CA C 52.0 0.3 1 165 60 60 ALA CB C 18.0 0.3 1 166 60 60 ALA N N 123.4 0.3 1 167 61 61 GLN H H 8.17 0.02 1 168 61 61 GLN C C 176.1 0.3 1 169 61 61 GLN CA C 55.3 0.3 1 170 61 61 GLN CB C 28.4 0.3 1 171 61 61 GLN N N 118.9 0.3 1 172 62 62 GLU H H 8.34 0.02 1 173 62 62 GLU C C 176.1 0.3 1 174 62 62 GLU CA C 56.1 0.3 1 175 62 62 GLU CB C 29.2 0.3 1 176 62 62 GLU N N 121.4 0.3 1 177 63 63 GLU H H 8.34 0.02 1 178 63 63 GLU C C 176.6 0.3 1 179 63 63 GLU CA C 56.4 0.3 1 180 63 63 GLU CB C 29.5 0.3 1 181 63 63 GLU N N 121.3 0.3 1 182 64 64 GLU H H 8.31 0.02 1 183 64 64 GLU C C 176.6 0.3 1 184 64 64 GLU CA C 56.5 0.3 1 185 64 64 GLU CB C 29.3 0.3 1 186 64 64 GLU N N 121.3 0.3 1 187 65 65 GLU H H 8.36 0.02 1 188 65 65 GLU C C 176.6 0.3 1 189 65 65 GLU CA C 56.3 0.3 1 190 65 65 GLU CB C 29.4 0.3 1 191 65 65 GLU N N 121.1 0.3 1 192 66 66 VAL H H 8.09 0.02 1 193 66 66 VAL C C 176.4 0.3 1 194 66 66 VAL CA C 62.1 0.3 1 195 66 66 VAL CB C 31.6 0.3 1 196 66 66 VAL N N 120.3 0.3 1 197 67 67 GLY H H 8.28 0.02 1 198 67 67 GLY C C 173.2 0.3 1 199 67 67 GLY CA C 44.4 0.3 1 200 67 67 GLY N N 110.4 0.3 1 201 68 68 PHE H H 7.91 0.02 1 202 68 68 PHE C C 174.1 0.3 1 203 68 68 PHE CA C 55.2 0.3 1 204 68 68 PHE CB C 38.1 0.3 1 205 68 68 PHE N N 119.9 0.3 1 206 69 69 PRO C C 176.5 0.3 1 207 69 69 PRO CA C 62.2 0.3 1 208 69 69 PRO CB C 31.1 0.3 1 209 70 70 VAL H H 8.18 0.02 1 210 70 70 VAL C C 175.8 0.3 1 211 70 70 VAL CA C 55.3 0.3 1 212 70 70 VAL CB C 30.9 0.3 1 213 70 70 VAL N N 118.7 0.3 1 214 72 72 PRO C C 177.2 0.3 1 215 72 72 PRO CA C 63.1 0.3 1 216 72 72 PRO CB C 31.0 0.3 1 217 73 73 GLN H H 8.76 0.02 1 218 73 73 GLN C C 176.6 0.3 1 219 73 73 GLN CA C 55.2 0.3 1 220 73 73 GLN CB C 31.8 0.3 1 221 73 73 GLN N N 119.7 0.3 1 222 74 74 VAL H H 7.37 0.02 1 223 74 74 VAL C C 173.2 0.3 1 224 74 74 VAL CA C 58.0 0.3 1 225 74 74 VAL CB C 31.4 0.3 1 226 74 74 VAL N N 116.6 0.3 1 227 75 75 PRO C C 175.5 0.3 1 228 75 75 PRO CA C 62.4 0.3 1 229 75 75 PRO CB C 30.9 0.3 1 230 76 76 LEU H H 7.90 0.02 1 231 76 76 LEU C C 177.7 0.3 1 232 76 76 LEU CA C 54.0 0.3 1 233 76 76 LEU CB C 41.2 0.3 1 234 76 76 LEU N N 121.4 0.3 1 235 78 78 PRO C C 177.2 0.3 1 236 78 78 PRO CA C 61.3 0.3 1 237 78 78 PRO CB C 31.0 0.3 1 238 79 79 MET H H 9.34 0.02 1 239 79 79 MET C C 175.6 0.3 1 240 79 79 MET CA C 55.0 0.3 1 241 79 79 MET CB C 29.5 0.3 1 242 79 79 MET N N 121.2 0.3 1 243 80 80 THR H H 6.29 0.02 1 244 80 80 THR HG2 H 1.22 0.02 1 245 80 80 THR C C 173.3 0.3 1 246 80 80 THR CA C 58.5 0.3 1 247 80 80 THR CB C 71.9 0.3 1 248 80 80 THR N N 115.2 0.3 1 249 81 81 TYR H H 8.57 0.02 1 250 81 81 TYR C C 176.2 0.3 1 251 81 81 TYR CA C 60.8 0.3 1 252 81 81 TYR CB C 36.9 0.3 1 253 81 81 TYR N N 120.8 0.3 1 254 82 82 LYS H H 8.37 0.02 1 255 82 82 LYS C C 178.1 0.3 1 256 82 82 LYS CA C 58.2 0.3 1 257 82 82 LYS CB C 31.3 0.3 1 258 82 82 LYS N N 117.1 0.3 1 259 83 83 ALA H H 7.51 0.02 1 260 83 83 ALA C C 180.1 0.3 1 261 83 83 ALA CA C 53.9 0.3 1 262 83 83 ALA CB C 17.9 0.3 1 263 83 83 ALA N N 119.3 0.3 1 264 84 84 ALA H H 7.95 0.02 1 265 84 84 ALA C C 181.1 0.3 1 266 84 84 ALA CA C 54.9 0.3 1 267 84 84 ALA CB C 15.9 0.3 1 268 84 84 ALA N N 122.4 0.3 1 269 85 85 VAL H H 8.35 0.02 1 270 85 85 VAL C C 178.9 0.3 1 271 85 85 VAL CA C 66.2 0.3 1 272 85 85 VAL CB C 30.6 0.3 1 273 85 85 VAL N N 125.9 0.3 1 274 86 86 ASP H H 8.29 0.02 1 275 86 86 ASP C C 179.8 0.3 1 276 86 86 ASP CA C 57.2 0.3 1 277 86 86 ASP CB C 39.0 0.3 1 278 86 86 ASP N N 121.6 0.3 1 279 87 87 LEU H H 8.52 0.02 1 280 87 87 LEU C C 178.7 0.3 1 281 87 87 LEU CA C 57.4 0.3 1 282 87 87 LEU CB C 40.8 0.3 1 283 87 87 LEU N N 121.6 0.3 1 284 88 88 SER H H 8.59 0.02 1 285 88 88 SER C C 175.5 0.3 1 286 88 88 SER CA C 62.5 0.3 1 287 88 88 SER N N 113.7 0.3 1 288 89 89 HIS H H 8.49 0.02 1 289 89 89 HIS C C 177.5 0.3 1 290 89 89 HIS CA C 60.2 0.3 1 291 89 89 HIS CB C 28.8 0.3 1 292 89 89 HIS N N 119.8 0.3 1 293 90 90 PHE H H 8.28 0.02 1 294 90 90 PHE C C 176.4 0.3 1 295 90 90 PHE CA C 60.7 0.3 1 296 90 90 PHE CB C 37.7 0.3 1 297 90 90 PHE N N 122.1 0.3 1 298 91 91 LEU H H 8.33 0.02 1 299 91 91 LEU CA C 56.6 0.3 1 300 91 91 LEU CB C 38.4 0.3 1 301 91 91 LEU N N 117.7 0.3 1 302 93 93 GLU H H 7.98 0.02 1 303 93 93 GLU C C 178.6 0.3 1 304 93 93 GLU CA C 58.0 0.3 1 305 93 93 GLU CB C 28.5 0.3 1 306 93 93 GLU N N 119.0 0.3 1 307 94 94 LYS H H 8.21 0.02 1 308 94 94 LYS CA C 55.9 0.3 1 309 94 94 LYS CB C 31.0 0.3 1 310 94 94 LYS N N 115.5 0.3 1 311 97 97 LEU C C 175.8 0.3 1 312 97 97 LEU CA C 54.5 0.3 1 313 97 97 LEU CB C 42.7 0.3 1 314 98 98 GLU H H 7.93 0.02 1 315 98 98 GLU C C 178.2 0.3 1 316 98 98 GLU CA C 57.4 0.3 1 317 98 98 GLU CB C 29.0 0.3 1 318 98 98 GLU N N 115.9 0.3 1 319 99 99 GLY H H 9.31 0.02 1 320 99 99 GLY C C 173.2 0.3 1 321 99 99 GLY CA C 45.0 0.3 1 322 99 99 GLY N N 115.2 0.3 1 323 100 100 LEU H H 8.30 0.02 1 324 100 100 LEU C C 176.6 0.3 1 325 100 100 LEU CA C 54.4 0.3 1 326 100 100 LEU CB C 41.8 0.3 1 327 100 100 LEU N N 123.5 0.3 1 328 101 101 ILE H H 7.98 0.02 1 329 101 101 ILE C C 176.2 0.3 1 330 101 101 ILE CA C 61.4 0.3 1 331 101 101 ILE CB C 36.5 0.3 1 332 101 101 ILE N N 124.1 0.3 1 333 102 102 TYR H H 9.11 0.02 1 334 102 102 TYR C C 176.2 0.3 1 335 102 102 TYR CA C 59.0 0.3 1 336 102 102 TYR CB C 38.4 0.3 1 337 102 102 TYR N N 128.4 0.3 1 338 103 103 SER H H 5.79 0.02 1 339 103 103 SER CA C 56.2 0.3 1 340 103 103 SER CB C 65.9 0.3 1 341 103 103 SER N N 117.9 0.3 1 342 104 104 GLN C C 177.2 0.3 1 343 104 104 GLN CA C 57.9 0.3 1 344 104 104 GLN CB C 27.2 0.3 1 345 105 105 LYS H H 8.26 0.02 1 346 105 105 LYS C C 179.5 0.3 1 347 105 105 LYS CA C 58.5 0.3 1 348 105 105 LYS CB C 30.8 0.3 1 349 105 105 LYS N N 117.9 0.3 1 350 106 106 ARG H H 7.90 0.02 1 351 106 106 ARG C C 177.7 0.3 1 352 106 106 ARG CA C 60.4 0.3 1 353 106 106 ARG CB C 29.5 0.3 1 354 106 106 ARG N N 116.5 0.3 1 355 107 107 GLN H H 8.44 0.02 1 356 107 107 GLN C C 177.3 0.3 1 357 107 107 GLN CA C 59.7 0.3 1 358 107 107 GLN CB C 26.7 0.3 1 359 107 107 GLN N N 119.7 0.3 1 360 108 108 ASP H H 8.85 0.02 1 361 108 108 ASP C C 178.5 0.3 1 362 108 108 ASP CA C 57.1 0.3 1 363 108 108 ASP CB C 39.4 0.3 1 364 108 108 ASP N N 118.9 0.3 1 365 109 109 ILE H H 7.68 0.02 1 366 109 109 ILE CA C 65.2 0.3 1 367 109 109 ILE CB C 37.3 0.3 1 368 109 109 ILE N N 119.7 0.3 1 369 110 110 LEU H H 7.43 0.02 1 370 110 110 LEU C C 178.3 0.3 1 371 110 110 LEU CA C 58.5 0.3 1 372 110 110 LEU CB C 40.6 0.3 1 373 110 110 LEU N N 121.7 0.3 1 374 111 111 ASP H H 9.17 0.02 1 375 111 111 ASP C C 180.9 0.3 1 376 111 111 ASP CA C 57.5 0.3 1 377 111 111 ASP CB C 39.6 0.3 1 378 111 111 ASP N N 119.6 0.3 1 379 112 112 LEU H H 8.79 0.02 1 380 112 112 LEU C C 178.4 0.3 1 381 112 112 LEU CA C 57.3 0.3 1 382 112 112 LEU CB C 40.1 0.3 1 383 112 112 LEU N N 122.0 0.3 1 384 113 113 TRP H H 8.25 0.02 1 385 113 113 TRP C C 179.9 0.3 1 386 113 113 TRP CA C 60.9 0.3 1 387 113 113 TRP CB C 26.8 0.3 1 388 113 113 TRP N N 121.8 0.3 1 389 114 114 VAL H H 8.75 0.02 1 390 114 114 VAL C C 178.1 0.3 1 391 114 114 VAL CA C 66.4 0.3 1 392 114 114 VAL CB C 30.6 0.3 1 393 114 114 VAL N N 122.0 0.3 1 394 115 115 TYR H H 8.29 0.02 1 395 115 115 TYR C C 177.7 0.3 1 396 115 115 TYR CA C 58.6 0.3 1 397 115 115 TYR CB C 37.7 0.3 1 398 115 115 TYR N N 122.0 0.3 1 399 116 116 HIS H H 8.82 0.02 1 400 116 116 HIS C C 177.0 0.3 1 401 116 116 HIS CA C 58.4 0.3 1 402 116 116 HIS CB C 30.2 0.3 1 403 116 116 HIS N N 116.0 0.3 1 404 117 117 THR H H 8.02 0.02 1 405 117 117 THR C C 175.9 0.3 1 406 117 117 THR CA C 62.8 0.3 1 407 117 117 THR CB C 69.7 0.3 1 408 117 117 THR N N 105.5 0.3 1 409 118 118 GLN H H 7.74 0.02 1 410 118 118 GLN C C 173.0 0.3 1 411 118 118 GLN CA C 55.2 0.3 1 412 118 118 GLN CB C 30.6 0.3 1 413 118 118 GLN N N 117.5 0.3 1 414 119 119 GLY H H 7.50 0.02 1 415 119 119 GLY C C 172.6 0.3 1 416 119 119 GLY CA C 45.2 0.3 1 417 119 119 GLY N N 108.1 0.3 1 418 120 120 TYR H H 6.03 0.02 1 419 120 120 TYR C C 176.3 0.3 1 420 120 120 TYR CA C 56.1 0.3 1 421 120 120 TYR CB C 37.2 0.3 1 422 120 120 TYR N N 115.3 0.3 1 423 121 121 PHE H H 8.27 0.02 1 424 121 121 PHE CA C 56.3 0.3 1 425 121 121 PHE CB C 37.9 0.3 1 426 121 121 PHE N N 125.7 0.3 1 427 122 122 PRO C C 174.8 0.3 1 428 122 122 PRO CA C 62.9 0.3 1 429 122 122 PRO CB C 27.3 0.3 1 430 123 123 ASP H H 8.97 0.02 1 431 123 123 ASP C C 176.3 0.3 1 432 123 123 ASP CA C 52.2 0.3 1 433 123 123 ASP CB C 40.9 0.3 1 434 123 123 ASP N N 123.7 0.3 1 435 124 124 TRP H H 7.25 0.02 1 436 124 124 TRP C C 177.5 0.3 1 437 124 124 TRP CA C 54.5 0.3 1 438 124 124 TRP CB C 30.2 0.3 1 439 124 124 TRP N N 114.8 0.3 1 440 125 125 GLN H H 8.62 0.02 1 441 125 125 GLN C C 171.3 0.3 1 442 125 125 GLN CA C 54.3 0.3 1 443 125 125 GLN CB C 23.4 0.3 1 444 125 125 GLN N N 133.1 0.3 1 445 126 126 ASN H H 6.61 0.02 1 446 126 126 ASN C C 174.9 0.3 1 447 126 126 ASN CA C 50.9 0.3 1 448 126 126 ASN CB C 40.3 0.3 1 449 126 126 ASN N N 116.0 0.3 1 450 127 127 TYR H H 9.16 0.02 1 451 127 127 TYR C C 175.2 0.3 1 452 127 127 TYR CA C 56.5 0.3 1 453 127 127 TYR CB C 42.0 0.3 1 454 127 127 TYR N N 121.3 0.3 1 455 128 128 THR H H 9.27 0.02 1 456 128 128 THR HG2 H 1.38 0.02 1 457 128 128 THR CA C 61.1 0.3 1 458 128 128 THR CB C 66.3 0.3 1 459 128 128 THR N N 112.9 0.3 1 460 129 129 PRO C C 177.3 0.3 1 461 130 130 GLY H H 8.52 0.02 1 462 130 130 GLY C C 174.1 0.3 1 463 130 130 GLY CA C 44.8 0.3 1 464 130 130 GLY N N 109.6 0.3 1 465 131 131 PRO C C 176.0 0.3 1 466 131 131 PRO CA C 61.7 0.3 1 467 131 131 PRO CB C 33.6 0.3 1 468 132 132 GLY H H 10.24 0.02 1 469 132 132 GLY CA C 43.4 0.3 1 470 132 132 GLY N N 111.5 0.3 1 471 133 133 ILE C C 175.6 0.3 1 472 133 133 ILE CA C 62.2 0.3 1 473 133 133 ILE CB C 37.3 0.3 1 474 134 134 ARG H H 9.01 0.02 1 475 134 134 ARG C C 175.6 0.3 1 476 134 134 ARG CA C 51.8 0.3 1 477 134 134 ARG CB C 27.4 0.3 1 478 134 134 ARG N N 124.2 0.3 1 479 135 135 TYR H H 9.03 0.02 1 480 135 135 TYR C C 174.7 0.3 1 481 135 135 TYR CA C 56.8 0.3 1 482 135 135 TYR CB C 37.7 0.3 1 483 135 135 TYR N N 122.1 0.3 1 484 136 136 PRO C C 177.4 0.3 1 485 136 136 PRO CA C 62.4 0.3 1 486 136 136 PRO CB C 32.7 0.3 1 487 137 137 LEU H H 8.53 0.02 1 488 137 137 LEU C C 180.7 0.3 1 489 137 137 LEU CA C 56.2 0.3 1 490 137 137 LEU CB C 40.0 0.3 1 491 137 137 LEU N N 121.0 0.3 1 492 138 138 THR H H 9.11 0.02 1 493 138 138 THR HG2 H 1.08 0.02 1 494 138 138 THR C C 174.1 0.3 1 495 138 138 THR CA C 62.4 0.3 1 496 138 138 THR CB C 68.0 0.3 1 497 138 138 THR N N 119.8 0.3 1 498 139 139 PHE H H 9.11 0.02 1 499 139 139 PHE C C 174.9 0.3 1 500 139 139 PHE CA C 55.6 0.3 1 501 139 139 PHE CB C 36.0 0.3 1 502 139 139 PHE N N 132.2 0.3 1 503 140 140 GLY H H 8.34 0.02 1 504 140 140 GLY C C 171.7 0.3 1 505 140 140 GLY CA C 45.0 0.3 1 506 140 140 GLY N N 117.0 0.3 1 507 141 141 TRP H H 7.41 0.02 1 508 141 141 TRP HE1 H 10.63 0.02 1 509 141 141 TRP C C 177.7 0.3 1 510 141 141 TRP CA C 55.3 0.3 1 511 141 141 TRP CB C 29.2 0.3 1 512 141 141 TRP N N 118.6 0.3 1 513 141 141 TRP NE1 N 129.0 0.3 1 514 142 142 CYS H H 8.19 0.02 1 515 142 142 CYS C C 171.0 0.3 1 516 142 142 CYS CA C 59.2 0.3 1 517 142 142 CYS CB C 25.6 0.3 1 518 142 142 CYS N N 125.6 0.3 1 519 143 143 PHE H H 5.78 0.02 1 520 143 143 PHE C C 172.1 0.3 1 521 143 143 PHE CA C 56.1 0.3 1 522 143 143 PHE CB C 41.5 0.3 1 523 143 143 PHE N N 114.4 0.3 1 524 144 144 LYS H H 8.97 0.02 1 525 144 144 LYS C C 173.0 0.3 1 526 144 144 LYS CA C 51.7 0.3 1 527 144 144 LYS CB C 34.6 0.3 1 528 144 144 LYS N N 115.1 0.3 1 529 145 145 LEU H H 8.32 0.02 1 530 145 145 LEU C C 176.0 0.3 1 531 145 145 LEU CA C 51.7 0.3 1 532 145 145 LEU CB C 41.1 0.3 1 533 145 145 LEU N N 117.7 0.3 1 534 146 146 VAL H H 8.92 0.02 1 535 146 146 VAL C C 173.9 0.3 1 536 146 146 VAL CA C 57.5 0.3 1 537 146 146 VAL CB C 33.3 0.3 1 538 146 146 VAL N N 120.4 0.3 1 539 147 147 PRO C C 177.2 0.3 1 540 147 147 PRO CA C 61.8 0.3 1 541 147 147 PRO CB C 31.0 0.3 1 542 148 148 VAL H H 8.48 0.02 1 543 148 148 VAL C C 175.7 0.3 1 544 148 148 VAL CA C 61.2 0.3 1 545 148 148 VAL CB C 32.0 0.3 1 546 148 148 VAL N N 122.2 0.3 1 547 149 149 GLU H H 8.44 0.02 1 548 149 149 GLU C C 174.6 0.3 1 549 149 149 GLU CA C 53.6 0.3 1 550 149 149 GLU CB C 28.9 0.3 1 551 149 149 GLU N N 125.8 0.3 1 552 150 150 PRO C C 176.9 0.3 1 553 150 150 PRO CA C 62.6 0.3 1 554 150 150 PRO CB C 31.0 0.3 1 555 151 151 GLU H H 8.55 0.02 1 556 151 151 GLU C C 176.5 0.3 1 557 151 151 GLU CA C 56.2 0.3 1 558 151 151 GLU CB C 29.0 0.3 1 559 151 151 GLU N N 120.3 0.3 1 560 152 152 LYS H H 8.30 0.02 1 561 152 152 LYS C C 176.4 0.3 1 562 152 152 LYS CA C 55.4 0.3 1 563 152 152 LYS CB C 31.7 0.3 1 564 152 152 LYS N N 122.3 0.3 1 565 153 153 VAL H H 8.16 0.02 1 566 153 153 VAL C C 176.2 0.3 1 567 153 153 VAL CA C 61.7 0.3 1 568 153 153 VAL CB C 31.7 0.3 1 569 153 153 VAL N N 122.1 0.3 1 570 154 154 GLU H H 8.51 0.02 1 571 154 154 GLU C C 176.4 0.3 1 572 154 154 GLU CA C 56.1 0.3 1 573 154 154 GLU CB C 29.2 0.3 1 574 154 154 GLU N N 124.2 0.3 1 575 155 155 GLU H H 8.38 0.02 1 576 155 155 GLU C C 176.1 0.3 1 577 155 155 GLU CA C 56.0 0.3 1 578 155 155 GLU CB C 29.2 0.3 1 579 155 155 GLU N N 121.8 0.3 1 580 156 156 ALA H H 8.32 0.02 1 581 156 156 ALA C C 177.4 0.3 1 582 156 156 ALA CA C 52.0 0.3 1 583 156 156 ALA CB C 18.2 0.3 1 584 156 156 ALA N N 124.5 0.3 1 585 157 157 ASN H H 8.40 0.02 1 586 157 157 ASN C C 175.2 0.3 1 587 157 157 ASN CA C 52.7 0.3 1 588 157 157 ASN CB C 38.7 0.3 1 589 157 157 ASN N N 118.0 0.3 1 590 158 158 GLU H H 8.45 0.02 1 591 158 158 GLU C C 176.9 0.3 1 592 158 158 GLU CA C 56.4 0.3 1 593 158 158 GLU CB C 29.2 0.3 1 594 158 158 GLU N N 121.3 0.3 1 595 159 159 GLY H H 8.42 0.02 1 596 159 159 GLY C C 174.2 0.3 1 597 159 159 GLY CA C 44.7 0.3 1 598 159 159 GLY N N 109.6 0.3 1 599 160 160 GLU H H 8.22 0.02 1 600 160 160 GLU C C 176.4 0.3 1 601 160 160 GLU CA C 56.2 0.3 1 602 160 160 GLU CB C 29.0 0.3 1 603 160 160 GLU N N 120.2 0.3 1 604 163 163 CYS C C 174.7 0.3 1 605 163 163 CYS CA C 58.5 0.3 1 606 163 163 CYS CB C 26.7 0.3 1 607 164 164 LEU H H 8.19 0.02 1 608 164 164 LEU C C 177.1 0.3 1 609 164 164 LEU CA C 54.9 0.3 1 610 164 164 LEU CB C 40.7 0.3 1 611 164 164 LEU N N 123.3 0.3 1 612 165 165 LEU H H 8.03 0.02 1 613 165 165 LEU C C 176.6 0.3 1 614 165 165 LEU CA C 54.6 0.3 1 615 165 165 LEU CB C 41.1 0.3 1 616 165 165 LEU N N 121.5 0.3 1 617 166 166 HIS H H 8.11 0.02 1 618 166 166 HIS C C 173.7 0.3 1 619 166 166 HIS CA C 53.8 0.3 1 620 166 166 HIS CB C 30.0 0.3 1 621 166 166 HIS N N 120.7 0.3 1 622 171 171 HIS C C 176.0 0.3 1 623 171 171 HIS CA C 55.9 0.3 1 624 172 172 GLY H H 8.36 0.02 1 625 172 172 GLY C C 174.1 0.3 1 626 172 172 GLY CA C 44.9 0.3 1 627 172 172 GLY N N 110.0 0.3 1 628 173 173 MET H H 8.25 0.02 1 629 173 173 MET C C 175.9 0.3 1 630 173 173 MET CA C 54.9 0.3 1 631 173 173 MET CB C 32.0 0.3 1 632 173 173 MET N N 119.4 0.3 1 633 174 174 ASP H H 8.36 0.02 1 634 174 174 ASP C C 175.4 0.3 1 635 174 174 ASP CA C 53.9 0.3 1 636 174 174 ASP CB C 40.4 0.3 1 637 174 174 ASP N N 120.5 0.3 1 638 175 175 ASP H H 8.06 0.02 1 639 175 175 ASP C C 175.2 0.3 1 640 175 175 ASP CA C 51.4 0.3 1 641 175 175 ASP CB C 40.5 0.3 1 642 175 175 ASP N N 120.6 0.3 1 643 176 176 PRO C C 177.7 0.3 1 644 176 176 PRO CA C 63.5 0.3 1 645 176 176 PRO CB C 31.0 0.3 1 646 177 177 GLU H H 8.42 0.02 1 647 177 177 GLU C C 176.9 0.3 1 648 177 177 GLU CA C 56.5 0.3 1 649 177 177 GLU CB C 28.5 0.3 1 650 177 177 GLU N N 117.9 0.3 1 651 178 178 LYS H H 7.78 0.02 1 652 178 178 LYS C C 176.1 0.3 1 653 178 178 LYS CA C 55.2 0.3 1 654 178 178 LYS CB C 31.7 0.3 1 655 178 178 LYS N N 119.3 0.3 1 656 179 179 GLU H H 7.79 0.02 1 657 179 179 GLU C C 175.1 0.3 1 658 179 179 GLU CA C 56.2 0.3 1 659 179 179 GLU CB C 30.0 0.3 1 660 179 179 GLU N N 121.4 0.3 1 661 180 180 VAL H H 8.62 0.02 1 662 180 180 VAL C C 174.5 0.3 1 663 180 180 VAL CA C 62.2 0.3 1 664 180 180 VAL CB C 31.1 0.3 1 665 180 180 VAL N N 127.3 0.3 1 666 181 181 LEU H H 8.75 0.02 1 667 181 181 LEU C C 176.1 0.3 1 668 181 181 LEU CA C 52.2 0.3 1 669 181 181 LEU CB C 45.0 0.3 1 670 181 181 LEU N N 126.8 0.3 1 671 182 182 VAL H H 8.65 0.02 1 672 182 182 VAL CA C 58.2 0.3 1 673 182 182 VAL CB C 34.7 0.3 1 674 182 182 VAL N N 113.9 0.3 1 675 183 183 TRP H H 8.03 0.02 1 676 183 183 TRP HE1 H 9.72 0.02 1 677 183 183 TRP C C 178.2 0.3 1 678 183 183 TRP CA C 61.5 0.3 1 679 183 183 TRP CB C 29.9 0.3 1 680 183 183 TRP N N 122.0 0.3 1 681 183 183 TRP NE1 N 125.8 0.3 1 682 184 184 LYS H H 9.51 0.02 1 683 184 184 LYS C C 174.4 0.3 1 684 184 184 LYS CA C 54.6 0.3 1 685 184 184 LYS CB C 35.6 0.3 1 686 184 184 LYS N N 123.0 0.3 1 687 185 185 PHE H H 9.78 0.02 1 688 185 185 PHE C C 175.5 0.3 1 689 185 185 PHE CA C 56.8 0.3 1 690 185 185 PHE CB C 38.5 0.3 1 691 185 185 PHE N N 128.5 0.3 1 692 186 186 ASP H H 7.74 0.02 1 693 186 186 ASP C C 175.5 0.3 1 694 186 186 ASP CA C 52.5 0.3 1 695 186 186 ASP CB C 42.1 0.3 1 696 186 186 ASP N N 125.9 0.3 1 697 187 187 SER H H 8.74 0.02 1 698 187 187 SER C C 176.6 0.3 1 699 187 187 SER CA C 60.4 0.3 1 700 187 187 SER CB C 62.3 0.3 1 701 187 187 SER N N 121.6 0.3 1 702 188 188 LYS H H 8.37 0.02 1 703 188 188 LYS C C 179.6 0.3 1 704 188 188 LYS CA C 58.3 0.3 1 705 188 188 LYS CB C 30.6 0.3 1 706 188 188 LYS N N 120.4 0.3 1 707 189 189 LEU H H 7.58 0.02 1 708 189 189 LEU C C 176.5 0.3 1 709 189 189 LEU CA C 55.4 0.3 1 710 189 189 LEU CB C 39.1 0.3 1 711 189 189 LEU N N 117.2 0.3 1 712 190 190 ALA H H 7.20 0.02 1 713 190 190 ALA C C 177.2 0.3 1 714 190 190 ALA CA C 52.2 0.3 1 715 190 190 ALA CB C 17.1 0.3 1 716 190 190 ALA N N 117.4 0.3 1 717 191 191 PHE H H 7.70 0.02 1 718 191 191 PHE CA C 57.3 0.3 1 719 191 191 PHE CB C 40.1 0.3 1 720 191 191 PHE N N 114.5 0.3 1 721 193 193 HIS C C 175.7 0.3 1 722 193 193 HIS CA C 51.1 0.3 1 723 193 193 HIS CB C 27.6 0.3 1 724 194 194 MET H H 7.25 0.02 1 725 194 194 MET C C 177.7 0.3 1 726 194 194 MET CA C 57.6 0.3 1 727 194 194 MET CB C 30.5 0.3 1 728 194 194 MET N N 126.3 0.3 1 729 195 195 ALA H H 9.97 0.02 1 730 195 195 ALA C C 177.5 0.3 1 731 195 195 ALA CA C 55.1 0.3 1 732 195 195 ALA CB C 19.5 0.3 1 733 195 195 ALA N N 119.2 0.3 1 734 196 196 ARG H H 5.90 0.02 1 735 196 196 ARG C C 176.7 0.3 1 736 196 196 ARG CA C 56.9 0.3 1 737 196 196 ARG CB C 28.8 0.3 1 738 196 196 ARG N N 113.7 0.3 1 739 197 197 GLU H H 6.99 0.02 1 740 197 197 GLU C C 178.3 0.3 1 741 197 197 GLU CA C 57.5 0.3 1 742 197 197 GLU CB C 28.4 0.3 1 743 197 197 GLU N N 116.7 0.3 1 744 198 198 LEU H H 7.71 0.02 1 745 198 198 LEU C C 177.2 0.3 1 746 198 198 LEU CA C 55.8 0.3 1 747 198 198 LEU CB C 42.9 0.3 1 748 198 198 LEU N N 116.4 0.3 1 749 199 199 HIS H H 7.92 0.02 1 750 199 199 HIS C C 172.4 0.3 1 751 199 199 HIS CA C 53.3 0.3 1 752 199 199 HIS CB C 29.4 0.3 1 753 199 199 HIS N N 116.0 0.3 1 754 201 201 GLU C C 177.7 0.3 1 755 201 201 GLU CA C 57.7 0.3 1 756 201 201 GLU CB C 26.5 0.3 1 757 202 202 TYR H H 7.76 0.02 1 758 202 202 TYR C C 176.0 0.3 1 759 202 202 TYR CA C 58.0 0.3 1 760 202 202 TYR CB C 36.7 0.3 1 761 202 202 TYR N N 119.8 0.3 1 762 203 203 TYR H H 7.91 0.02 1 763 203 203 TYR C C 175.5 0.3 1 764 203 203 TYR CA C 58.1 0.3 1 765 203 203 TYR CB C 37.9 0.3 1 766 203 203 TYR N N 117.6 0.3 1 767 204 204 LYS H H 7.75 0.02 1 768 204 204 LYS C C 176.7 0.3 1 769 204 204 LYS CA C 56.7 0.3 1 770 204 204 LYS CB C 32.1 0.3 1 771 204 204 LYS N N 120.5 0.3 1 772 206 206 CYS C C 175.8 0.3 1 773 206 206 CYS CA C 62.1 0.3 1 774 206 206 CYS CB C 32.8 0.3 1 775 207 207 ALA H H 8.63 0.02 1 776 207 207 ALA C C 177.2 0.3 1 777 207 207 ALA CA C 52.6 0.3 1 778 207 207 ALA CB C 17.4 0.3 1 779 207 207 ALA N N 128.2 0.3 1 780 208 208 ALA C C 177.8 0.3 1 781 208 208 ALA CA C 52.2 0.3 1 782 208 208 ALA CB C 18.2 0.3 1 783 209 209 ALA H H 8.04 0.02 1 784 209 209 ALA C C 177.8 0.3 1 785 209 209 ALA CA C 52.2 0.3 1 786 209 209 ALA CB C 18.0 0.3 1 787 209 209 ALA N N 122.0 0.3 1 788 210 210 LEU H H 7.98 0.02 1 789 210 210 LEU C C 177.5 0.3 1 790 210 210 LEU CA C 54.8 0.3 1 791 210 210 LEU CB C 41.0 0.3 1 792 210 210 LEU N N 120.1 0.3 1 793 211 211 GLU H H 8.17 0.02 1 794 211 211 GLU C C 176.3 0.3 1 795 211 211 GLU CA C 56.1 0.3 1 796 211 211 GLU CB C 29.4 0.3 1 797 211 211 GLU N N 120.3 0.3 1 798 213 213 HIS CA C 57.9 0.3 1 799 213 213 HIS CB C 26.4 0.3 1 800 214 214 HIS C C 177.4 0.3 1 801 214 214 HIS CA C 57.9 0.3 1 802 214 214 HIS CB C 27.5 0.3 1 803 215 215 HIS CA C 58.4 0.3 1 804 215 215 HIS CB C 31.1 0.3 1 805 216 216 HIS C C 174.2 0.3 1 806 216 216 HIS CA C 55.7 0.3 1 807 216 216 HIS CB C 30.1 0.3 1 808 217 217 HIS H H 7.81 0.02 1 809 217 217 HIS C C 179.8 0.3 1 810 217 217 HIS CA C 57.2 0.3 1 811 217 217 HIS CB C 30.6 0.3 1 812 217 217 HIS N N 125.6 0.3 1 stop_ save_