data_25029 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Specific and Non-Specific Interactions in Ultra-Weak Protein-Protein Associations Revealed by Solvent Paramagnetic Relaxation Enhancements ; _BMRB_accession_number 25029 _BMRB_flat_file_name bmr25029.str _Entry_type original _Submission_date 2014-06-19 _Accession_date 2014-06-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johansson Helle . . 2 Jensen Malene R. . 3 Gesmar Henrik . . 4 Meier Sebastian . . 5 Vinther Joachim M. . 6 Keeler Camille . . 7 Hodsdon Michael E. . 8 Led Jens J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 148 "13C chemical shifts" 455 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-26 update BMRB 'update entry citation' 2014-06-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4689 'NMR Studies of the Backbone Flexibility and Structure of Human Growth Hormone' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24969589 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johansson Helle . . 2 Jensen 'Malene Ringkjobing' R. . 3 Gesmar Henrik . . 4 Meier Sebastian . . 5 Vinther Joachim M. . 6 Keeler Camille . . 7 Hodsdon Michael E. . 8 Led Jens J. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 136 _Journal_issue 29 _Journal_ISSN 1520-5126 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10277 _Page_last 10286 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hGH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hGH $hGH 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_hGH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hGH _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 191 _Mol_residue_sequence ; FPTIPLSRLFDNAMLRAHRL HQLAFDTYQEFEEAYIPKEQ KYSFLQNPQTSLCFSESIPT PSNREETQQKSNLELLRISL LLIQSWLEPVQFLRSVFANS LVYGASDSNVYDLLKDLEEG IQTLMGRLEDGSPRTGQIFK QTYSKFDTNSHNDDALLKNY GLLYCFRKDMDKVETFLRIV QCRSVEGSCGF ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 PRO 3 THR 4 ILE 5 PRO 6 LEU 7 SER 8 ARG 9 LEU 10 PHE 11 ASP 12 ASN 13 ALA 14 MET 15 LEU 16 ARG 17 ALA 18 HIS 19 ARG 20 LEU 21 HIS 22 GLN 23 LEU 24 ALA 25 PHE 26 ASP 27 THR 28 TYR 29 GLN 30 GLU 31 PHE 32 GLU 33 GLU 34 ALA 35 TYR 36 ILE 37 PRO 38 LYS 39 GLU 40 GLN 41 LYS 42 TYR 43 SER 44 PHE 45 LEU 46 GLN 47 ASN 48 PRO 49 GLN 50 THR 51 SER 52 LEU 53 CYS 54 PHE 55 SER 56 GLU 57 SER 58 ILE 59 PRO 60 THR 61 PRO 62 SER 63 ASN 64 ARG 65 GLU 66 GLU 67 THR 68 GLN 69 GLN 70 LYS 71 SER 72 ASN 73 LEU 74 GLU 75 LEU 76 LEU 77 ARG 78 ILE 79 SER 80 LEU 81 LEU 82 LEU 83 ILE 84 GLN 85 SER 86 TRP 87 LEU 88 GLU 89 PRO 90 VAL 91 GLN 92 PHE 93 LEU 94 ARG 95 SER 96 VAL 97 PHE 98 ALA 99 ASN 100 SER 101 LEU 102 VAL 103 TYR 104 GLY 105 ALA 106 SER 107 ASP 108 SER 109 ASN 110 VAL 111 TYR 112 ASP 113 LEU 114 LEU 115 LYS 116 ASP 117 LEU 118 GLU 119 GLU 120 GLY 121 ILE 122 GLN 123 THR 124 LEU 125 MET 126 GLY 127 ARG 128 LEU 129 GLU 130 ASP 131 GLY 132 SER 133 PRO 134 ARG 135 THR 136 GLY 137 GLN 138 ILE 139 PHE 140 LYS 141 GLN 142 THR 143 TYR 144 SER 145 LYS 146 PHE 147 ASP 148 THR 149 ASN 150 SER 151 HIS 152 ASN 153 ASP 154 ASP 155 ALA 156 LEU 157 LEU 158 LYS 159 ASN 160 TYR 161 GLY 162 LEU 163 LEU 164 TYR 165 CYS 166 PHE 167 ARG 168 LYS 169 ASP 170 MET 171 ASP 172 LYS 173 VAL 174 GLU 175 THR 176 PHE 177 LEU 178 ARG 179 ILE 180 VAL 181 GLN 182 CYS 183 ARG 184 SER 185 VAL 186 GLU 187 GLY 188 SER 189 CYS 190 GLY 191 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 4689 "Human Growth Hormone" 100.00 191 100.00 100.00 1.35e-137 PDB 1A22 "Human Growth Hormone Bound To Single Receptor" 100.00 191 99.48 99.48 2.55e-136 PDB 1BP3 "The Xray Structure Of A Growth Hormone-Prolactin Receptor Complex" 100.00 191 99.48 99.48 2.55e-136 PDB 1HWG "1:2 Complex Of Human Growth Hormone With Its Soluble Binding Protein" 100.00 191 100.00 100.00 1.35e-137 PDB 1HWH "1:1 Complex Of Human Growth Hormone Mutant G120r With Its Soluble Binding Protein" 100.00 191 99.48 99.48 2.55e-136 PDB 3HHR "Human Growth Hormone And Extracellular Domain Of Its Receptor: Crystal Structure Of The Complex" 99.48 190 100.00 100.00 7.82e-137 DBJ BAJ21175 "growth hormone 1 [synthetic construct]" 100.00 217 100.00 100.00 2.67e-137 EMBL CAA23778 "unnamed protein product [Homo sapiens]" 100.00 217 99.48 99.48 4.16e-136 EMBL CAA23779 "growth hormone [Homo sapiens]" 100.00 217 99.48 99.48 3.53e-136 GB AAA52549 "growth hormone GH-1 [Homo sapiens]" 100.00 217 100.00 100.00 2.67e-137 GB AAA72260 "human growth hormone [synthetic construct]" 100.00 192 100.00 100.00 1.20e-137 GB AAA98618 "growth hormone [Homo sapiens]" 100.00 217 100.00 100.00 2.67e-137 GB AAC42099 "growth hormone [synthetic construct]" 100.00 192 100.00 100.00 1.20e-137 GB AAF23135 "recombinant ubiquitin-somatotropin fusion protein [synthetic construct]" 100.00 270 100.00 100.00 1.99e-137 PRF 1403262B "somatoliberin 20kD variant" 100.00 217 99.48 99.48 3.53e-136 REF NP_000506 "somatotropin isoform 1 precursor [Homo sapiens]" 100.00 217 100.00 100.00 2.67e-137 REF NP_001184093 "somatotropin precursor [Pan troglodytes]" 100.00 217 100.00 100.00 4.88e-137 REF NP_001277233 "growth hormone 1 precursor [Papio anubis]" 100.00 217 97.38 98.95 1.57e-133 REF XP_002827754 "PREDICTED: somatotropin isoform X7 [Pongo abelii]" 100.00 217 100.00 100.00 2.03e-137 REF XP_003262698 "PREDICTED: somatotropin isoform X1 [Nomascus leucogenys]" 65.97 252 98.41 99.21 4.66e-82 SP P01241 "RecName: Full=Somatotropin; AltName: Full=Growth hormone; Short=GH; Short=GH-N; AltName: Full=Growth hormone 1; AltName: Full=P" 100.00 217 100.00 100.00 2.67e-137 SP P58756 "RecName: Full=Somatotropin; AltName: Full=Growth hormone; Short=GH; Short=GH-N; AltName: Full=Growth hormone 1; AltName: Full=P" 100.00 217 100.00 100.00 4.88e-137 TPE CDW51387 "TPA: growth hormone B5 [Homo sapiens]" 100.00 217 100.00 100.00 2.67e-137 TPE CDW51389 "TPA: growth hormone B2 [Pan troglodytes]" 100.00 217 98.43 98.43 5.22e-134 TPE CDW51391 "TPA: growth hormone B2 [Gorilla gorilla]" 100.00 217 100.00 100.00 2.35e-137 TPE CDW51396 "TPA: growth hormone B4 [Pongo abelii]" 100.00 217 100.00 100.00 2.03e-137 TPE CDW51399 "TPA: growth hormone B2 [Nomascus leucogenys]" 100.00 217 98.95 99.48 5.35e-136 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hGH 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 _Variant _Vector_name $hGH 'recombinant technology' . 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 _Isotopic_labeling $hGH 0.175 mM '[U-100% 13C; U-100% 15N]' NaCl 25 mM 'natural abundance' NaH2PO4 15.4 mM 'natural abundance' Na2HPO4 9.5 mM 'natural abundance' NaN3 1.54 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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 298 . K pH 7 . pH pressure 1 . atm 'ionic strength' 0.0706 . M 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 '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' 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 hGH _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 2 PRO C C 176.70 0.10 1 2 2 2 PRO CA C 63.40 0.10 1 3 2 2 PRO CB C 31.77 0.10 1 4 3 3 THR H H 8.24 0.02 1 5 3 3 THR C C 174.60 0.10 1 6 3 3 THR CA C 62.19 0.10 1 7 3 3 THR CB C 69.95 0.10 1 8 3 3 THR N N 115.40 0.15 1 9 4 4 ILE H H 8.33 0.02 1 10 4 4 ILE CA C 58.63 0.10 1 11 4 4 ILE CB C 38.60 0.10 1 12 4 4 ILE N N 126.40 0.15 1 13 5 5 PRO C C 177.20 0.10 1 14 5 5 PRO CA C 62.69 0.10 1 15 5 5 PRO CB C 31.69 0.10 1 16 6 6 LEU H H 8.87 0.02 1 17 6 6 LEU C C 178.70 0.10 1 18 6 6 LEU CA C 58.10 0.10 1 19 6 6 LEU CB C 41.08 0.10 1 20 6 6 LEU N N 124.90 0.15 1 21 7 7 SER H H 8.90 0.02 1 22 7 7 SER C C 176.60 0.10 1 23 7 7 SER CA C 60.31 0.10 1 24 7 7 SER CB C 61.90 0.10 1 25 7 7 SER N N 111.50 0.15 1 26 8 8 ARG H H 7.05 0.02 1 27 8 8 ARG C C 178.30 0.10 1 28 8 8 ARG CA C 58.16 0.10 1 29 8 8 ARG CB C 29.67 0.10 1 30 8 8 ARG N N 122.70 0.15 1 31 9 9 LEU H H 7.59 0.02 1 32 9 9 LEU C C 181.40 0.10 1 33 9 9 LEU CA C 57.91 0.10 1 34 9 9 LEU CB C 41.10 0.10 1 35 9 9 LEU N N 119.40 0.15 1 36 10 10 PHE H H 8.49 0.02 1 37 10 10 PHE C C 177.70 0.10 1 38 10 10 PHE CA C 63.48 0.10 1 39 10 10 PHE CB C 38.53 0.10 1 40 10 10 PHE N N 118.20 0.15 1 41 11 11 ASP H H 8.37 0.02 1 42 11 11 ASP C C 179.00 0.10 1 43 11 11 ASP CA C 57.99 0.10 1 44 11 11 ASP CB C 43.72 0.10 1 45 11 11 ASP N N 120.60 0.15 1 46 12 12 ASN H H 8.21 0.02 1 47 12 12 ASN C C 177.60 0.10 1 48 12 12 ASN CA C 55.84 0.10 1 49 12 12 ASN CB C 38.06 0.10 1 50 12 12 ASN N N 117.20 0.15 1 51 13 13 ALA H H 7.70 0.02 1 52 13 13 ALA C C 179.00 0.10 1 53 13 13 ALA CA C 55.08 0.10 1 54 13 13 ALA CB C 16.65 0.10 1 55 13 13 ALA N N 122.10 0.15 1 56 14 14 MET H H 8.97 0.02 1 57 14 14 MET C C 179.50 0.10 1 58 14 14 MET CA C 56.79 0.10 1 59 14 14 MET CB C 29.41 0.10 1 60 14 14 MET N N 116.80 0.15 1 61 15 15 LEU H H 8.11 0.02 1 62 15 15 LEU C C 180.60 0.10 1 63 15 15 LEU CA C 58.53 0.10 1 64 15 15 LEU CB C 41.10 0.10 1 65 15 15 LEU N N 120.90 0.15 1 66 16 16 ARG H H 7.34 0.02 1 67 16 16 ARG C C 178.30 0.10 1 68 16 16 ARG CA C 59.26 0.10 1 69 16 16 ARG CB C 31.45 0.10 1 70 16 16 ARG N N 118.20 0.15 1 71 17 17 ALA H H 8.90 0.02 1 72 17 17 ALA C C 179.20 0.10 1 73 17 17 ALA CA C 55.24 0.10 1 74 17 17 ALA CB C 17.21 0.10 1 75 17 17 ALA N N 121.90 0.15 1 76 18 18 HIS H H 8.99 0.02 1 77 18 18 HIS C C 177.20 0.10 1 78 18 18 HIS CA C 59.35 0.10 1 79 18 18 HIS N N 116.50 0.15 1 80 19 19 ARG H H 7.87 0.02 1 81 19 19 ARG C C 178.70 0.10 1 82 19 19 ARG CA C 59.06 0.10 1 83 19 19 ARG CB C 28.82 0.10 1 84 19 19 ARG N N 118.90 0.15 1 85 20 20 LEU H H 8.05 0.02 1 86 20 20 LEU C C 178.00 0.10 1 87 20 20 LEU CA C 58.27 0.10 1 88 20 20 LEU CB C 41.62 0.10 1 89 20 20 LEU N N 119.60 0.15 1 90 21 21 HIS H H 8.15 0.02 1 91 21 21 HIS C C 176.20 0.10 1 92 21 21 HIS CA C 58.51 0.10 1 93 21 21 HIS CB C 27.65 0.10 1 94 21 21 HIS N N 117.10 0.15 1 95 22 22 GLN H H 8.35 0.02 1 96 22 22 GLN C C 177.40 0.10 1 97 22 22 GLN CA C 58.96 0.10 1 98 22 22 GLN CB C 27.62 0.10 1 99 22 22 GLN N N 119.40 0.15 1 100 23 23 LEU H H 8.34 0.02 1 101 23 23 LEU C C 180.50 0.10 1 102 23 23 LEU CA C 54.97 0.10 1 103 23 23 LEU CB C 47.36 0.10 1 104 23 23 LEU N N 119.10 0.15 1 105 24 24 ALA H H 8.45 0.02 1 106 24 24 ALA C C 179.20 0.10 1 107 24 24 ALA CA C 55.69 0.10 1 108 24 24 ALA CB C 18.84 0.10 1 109 24 24 ALA N N 123.90 0.15 1 110 25 25 PHE H H 8.91 0.02 1 111 25 25 PHE C C 177.80 0.10 1 112 25 25 PHE CA C 61.91 0.10 1 113 25 25 PHE CB C 38.76 0.10 1 114 25 25 PHE N N 119.00 0.15 1 115 26 26 ASP H H 9.31 0.02 1 116 26 26 ASP C C 180.10 0.10 1 117 26 26 ASP CA C 57.74 0.10 1 118 26 26 ASP CB C 39.92 0.10 1 119 26 26 ASP N N 120.40 0.15 1 120 27 27 THR H H 8.64 0.02 1 121 27 27 THR C C 176.90 0.10 1 122 27 27 THR CA C 67.45 0.10 1 123 27 27 THR N N 116.50 0.15 1 124 28 28 TYR H H 8.20 0.02 1 125 28 28 TYR C C 175.90 0.10 1 126 28 28 TYR CA C 62.80 0.10 1 127 28 28 TYR CB C 37.41 0.10 1 128 28 28 TYR N N 123.30 0.15 1 129 29 29 GLN H H 8.15 0.02 1 130 29 29 GLN C C 178.00 0.10 1 131 29 29 GLN CA C 58.93 0.10 1 132 29 29 GLN CB C 28.22 0.10 1 133 29 29 GLN N N 117.50 0.15 1 134 30 30 GLU H H 7.86 0.02 1 135 30 30 GLU C C 178.20 0.10 1 136 30 30 GLU CA C 58.98 0.10 1 137 30 30 GLU N N 119.10 0.15 1 138 31 31 PHE H H 8.50 0.02 1 139 31 31 PHE C C 177.00 0.10 1 140 31 31 PHE CA C 61.10 0.10 1 141 31 31 PHE CB C 35.22 0.10 1 142 31 31 PHE N N 121.60 0.15 1 143 32 32 GLU H H 8.77 0.02 1 144 32 32 GLU C C 178.10 0.10 1 145 32 32 GLU CA C 59.51 0.10 1 146 32 32 GLU CB C 30.33 0.10 1 147 32 32 GLU N N 118.80 0.15 1 148 33 33 GLU H H 7.86 0.02 1 149 33 33 GLU C C 178.70 0.10 1 150 33 33 GLU CA C 58.44 0.10 1 151 33 33 GLU CB C 29.42 0.10 1 152 33 33 GLU N N 115.30 0.15 1 153 34 34 ALA H H 7.58 0.02 1 154 34 34 ALA C C 180.20 0.10 1 155 34 34 ALA CA C 54.28 0.10 1 156 34 34 ALA CB C 21.24 0.10 1 157 34 34 ALA N N 118.60 0.15 1 158 35 35 TYR H H 7.59 0.02 1 159 35 35 TYR C C 175.10 0.10 1 160 35 35 TYR CA C 58.13 0.10 1 161 35 35 TYR CB C 39.96 0.10 1 162 35 35 TYR N N 110.90 0.15 1 163 36 36 ILE H H 7.31 0.02 1 164 36 36 ILE C C 173.80 0.10 1 165 36 36 ILE CA C 54.99 0.10 1 166 36 36 ILE CB C 35.25 0.10 1 167 36 36 ILE N N 119.60 0.15 1 168 37 37 PRO C C 177.80 0.10 1 169 37 37 PRO CA C 62.73 0.10 1 170 37 37 PRO CB C 29.38 0.10 1 171 38 38 LYS H H 8.64 0.02 1 172 38 38 LYS C C 178.10 0.10 1 173 38 38 LYS CA C 60.41 0.10 1 174 38 38 LYS CB C 31.76 0.10 1 175 38 38 LYS N N 122.00 0.15 1 176 39 39 GLU H H 9.13 0.02 1 177 39 39 GLU C C 177.10 0.10 1 178 39 39 GLU CA C 59.15 0.10 1 179 39 39 GLU CB C 27.64 0.10 1 180 39 39 GLU N N 115.30 0.15 1 181 40 40 GLN H H 7.85 0.02 1 182 40 40 GLN C C 175.70 0.10 1 183 40 40 GLN CA C 55.35 0.10 1 184 40 40 GLN N N 117.10 0.15 1 185 41 41 LYS C C 175.70 0.10 1 186 41 41 LYS CA C 58.48 0.10 1 187 41 41 LYS CB C 32.46 0.10 1 188 42 42 TYR H H 8.16 0.02 1 189 42 42 TYR C C 173.90 0.10 1 190 42 42 TYR CA C 55.56 0.10 1 191 42 42 TYR CB C 38.74 0.10 1 192 42 42 TYR N N 120.60 0.15 1 193 48 48 PRO C C 177.30 0.10 1 194 48 48 PRO CA C 63.99 0.10 1 195 49 49 GLN H H 8.34 0.02 1 196 49 49 GLN C C 176.60 0.10 1 197 49 49 GLN CA C 58.01 0.10 1 198 49 49 GLN CB C 31.65 0.10 1 199 49 49 GLN N N 118.30 0.15 1 200 50 50 THR H H 7.86 0.02 1 201 50 50 THR C C 174.60 0.10 1 202 50 50 THR CA C 62.42 0.10 1 203 50 50 THR CB C 69.10 0.10 1 204 50 50 THR N N 112.70 0.15 1 205 51 51 SER H H 8.17 0.02 1 206 51 51 SER C C 173.90 0.10 1 207 51 51 SER CA C 58.48 0.10 1 208 51 51 SER CB C 64.15 0.10 1 209 51 51 SER N N 116.70 0.15 1 210 52 52 LEU H H 7.98 0.02 1 211 52 52 LEU C C 177.40 0.10 1 212 52 52 LEU CA C 55.82 0.10 1 213 52 52 LEU CB C 42.66 0.10 1 214 52 52 LEU N N 123.40 0.15 1 215 53 53 CYS H H 8.52 0.02 1 216 53 53 CYS C C 176.90 0.10 1 217 53 53 CYS CA C 53.58 0.10 1 218 53 53 CYS N N 118.80 0.15 1 219 55 55 SER C C 176.20 0.10 1 220 55 55 SER CA C 59.24 0.10 1 221 56 56 GLU H H 7.81 0.02 1 222 56 56 GLU C C 176.40 0.10 1 223 56 56 GLU CA C 58.48 0.10 1 224 56 56 GLU CB C 28.71 0.10 1 225 56 56 GLU N N 122.40 0.15 1 226 57 57 SER H H 7.41 0.02 1 227 57 57 SER C C 174.40 0.10 1 228 57 57 SER CA C 59.59 0.10 1 229 57 57 SER CB C 63.61 0.10 1 230 57 57 SER N N 111.30 0.15 1 231 58 58 ILE H H 7.79 0.02 1 232 58 58 ILE C C 173.50 0.10 1 233 58 58 ILE CA C 58.94 0.10 1 234 58 58 ILE CB C 37.59 0.10 1 235 58 58 ILE N N 125.50 0.15 1 236 59 59 PRO C C 174.40 0.10 1 237 59 59 PRO CA C 63.02 0.10 1 238 59 59 PRO CB C 29.96 0.10 1 239 60 60 THR H H 8.17 0.02 1 240 60 60 THR C C 176.30 0.10 1 241 60 60 THR CA C 58.48 0.10 1 242 60 60 THR CB C 70.03 0.10 1 243 60 60 THR N N 115.50 0.15 1 244 61 61 PRO C C 177.30 0.10 1 245 61 61 PRO CA C 62.75 0.10 1 246 61 61 PRO CB C 31.76 0.10 1 247 62 62 SER H H 9.03 0.02 1 248 62 62 SER C C 173.70 0.10 1 249 62 62 SER CA C 59.62 0.10 1 250 62 62 SER CB C 63.98 0.10 1 251 62 62 SER N N 116.90 0.15 1 252 63 63 ASN H H 7.46 0.02 1 253 63 63 ASN C C 176.10 0.10 1 254 63 63 ASN CA C 51.94 0.10 1 255 63 63 ASN CB C 39.80 0.10 1 256 63 63 ASN N N 115.30 0.15 1 257 65 65 GLU H H 8.64 0.02 1 258 65 65 GLU C C 179.40 0.10 1 259 65 65 GLU CA C 60.33 0.10 1 260 65 65 GLU CB C 28.02 0.10 1 261 65 65 GLU N N 121.80 0.15 1 262 66 66 GLU H H 8.57 0.02 1 263 66 66 GLU C C 179.70 0.10 1 264 66 66 GLU CA C 58.76 0.10 1 265 66 66 GLU CB C 29.99 0.10 1 266 66 66 GLU N N 118.10 0.15 1 267 67 67 THR H H 8.04 0.02 1 268 67 67 THR C C 177.80 0.10 1 269 67 67 THR CA C 67.26 0.10 1 270 67 67 THR CB C 67.80 0.10 1 271 67 67 THR N N 115.30 0.15 1 272 68 68 GLN H H 7.87 0.02 1 273 68 68 GLN C C 176.70 0.10 1 274 68 68 GLN CA C 57.75 0.10 1 275 68 68 GLN CB C 28.41 0.10 1 276 68 68 GLN N N 117.80 0.15 1 277 69 69 GLN H H 7.18 0.02 1 278 69 69 GLN C C 176.60 0.10 1 279 69 69 GLN CA C 56.03 0.10 1 280 69 69 GLN CB C 28.23 0.10 1 281 69 69 GLN N N 114.10 0.15 1 282 70 70 LYS H H 7.50 0.02 1 283 70 70 LYS C C 176.60 0.10 1 284 70 70 LYS CA C 53.73 0.10 1 285 70 70 LYS CB C 33.02 0.10 1 286 70 70 LYS N N 118.10 0.15 1 287 71 71 SER H H 9.45 0.02 1 288 71 71 SER C C 174.50 0.10 1 289 71 71 SER CA C 57.24 0.10 1 290 71 71 SER CB C 65.13 0.10 1 291 71 71 SER N N 120.10 0.15 1 292 72 72 ASN H H 9.17 0.02 1 293 72 72 ASN C C 177.50 0.10 1 294 72 72 ASN CA C 56.11 0.10 1 295 72 72 ASN N N 119.30 0.15 1 296 73 73 LEU H H 8.60 0.02 1 297 73 73 LEU C C 179.10 0.10 1 298 73 73 LEU CA C 58.10 0.10 1 299 73 73 LEU CB C 40.95 0.10 1 300 73 73 LEU N N 118.50 0.15 1 301 74 74 GLU H H 7.95 0.02 1 302 74 74 GLU C C 178.60 0.10 1 303 74 74 GLU CA C 59.70 0.10 1 304 74 74 GLU CB C 28.95 0.10 1 305 74 74 GLU N N 118.90 0.15 1 306 75 75 LEU H H 8.08 0.02 1 307 75 75 LEU C C 180.90 0.10 1 308 75 75 LEU CA C 57.77 0.10 1 309 75 75 LEU CB C 40.58 0.10 1 310 75 75 LEU N N 116.90 0.15 1 311 76 76 LEU H H 8.43 0.02 1 312 76 76 LEU C C 177.40 0.10 1 313 76 76 LEU CA C 58.12 0.10 1 314 76 76 LEU CB C 41.71 0.10 1 315 76 76 LEU N N 120.10 0.15 1 316 77 77 ARG H H 8.51 0.02 1 317 77 77 ARG C C 178.20 0.10 1 318 77 77 ARG CA C 59.43 0.10 1 319 77 77 ARG N N 120.60 0.15 1 320 78 78 ILE H H 8.35 0.02 1 321 78 78 ILE C C 177.40 0.10 1 322 78 78 ILE CA C 62.87 0.10 1 323 78 78 ILE N N 118.30 0.15 1 324 79 79 SER H H 7.70 0.02 1 325 79 79 SER C C 174.70 0.10 1 326 79 79 SER CA C 64.26 0.10 1 327 79 79 SER N N 114.90 0.15 1 328 80 80 LEU H H 8.71 0.02 1 329 80 80 LEU C C 178.00 0.10 1 330 80 80 LEU CA C 58.04 0.10 1 331 80 80 LEU N N 121.60 0.15 1 332 81 81 LEU H H 8.31 0.02 1 333 81 81 LEU C C 181.20 0.10 1 334 81 81 LEU CA C 58.02 0.10 1 335 81 81 LEU CB C 42.27 0.10 1 336 81 81 LEU N N 117.80 0.15 1 337 82 82 LEU H H 8.46 0.02 1 338 82 82 LEU C C 178.60 0.10 1 339 82 82 LEU CA C 58.67 0.10 1 340 82 82 LEU CB C 41.19 0.10 1 341 82 82 LEU N N 122.30 0.15 1 342 83 83 ILE H H 7.90 0.02 1 343 83 83 ILE C C 178.80 0.10 1 344 83 83 ILE CA C 63.21 0.10 1 345 83 83 ILE CB C 35.26 0.10 1 346 83 83 ILE N N 117.90 0.15 1 347 84 84 GLN H H 9.07 0.02 1 348 84 84 GLN C C 179.60 0.10 1 349 84 84 GLN CA C 59.08 0.10 1 350 84 84 GLN CB C 27.08 0.10 1 351 84 84 GLN N N 116.10 0.15 1 352 85 85 SER H H 8.19 0.02 1 353 85 85 SER C C 176.20 0.10 1 354 85 85 SER CA C 61.25 0.10 1 355 85 85 SER CB C 67.30 0.10 1 356 85 85 SER N N 114.30 0.15 1 357 86 86 TRP H H 7.65 0.02 1 358 86 86 TRP C C 176.40 0.10 1 359 86 86 TRP CA C 57.25 0.10 1 360 86 86 TRP CB C 31.48 0.10 1 361 86 86 TRP N N 118.50 0.15 1 362 87 87 LEU H H 7.24 0.02 1 363 87 87 LEU C C 177.40 0.10 1 364 87 87 LEU CA C 59.51 0.10 1 365 87 87 LEU CB C 40.02 0.10 1 366 87 87 LEU N N 120.20 0.15 1 367 88 88 GLU H H 8.52 0.02 1 368 88 88 GLU C C 176.90 0.10 1 369 88 88 GLU CA C 59.52 0.10 1 370 88 88 GLU CB C 26.94 0.10 1 371 88 88 GLU N N 113.30 0.15 1 372 89 89 PRO C C 178.00 0.10 1 373 90 90 VAL H H 8.31 0.02 1 374 90 90 VAL C C 178.30 0.10 1 375 90 90 VAL CA C 65.72 0.10 1 376 90 90 VAL N N 113.90 0.15 1 377 91 91 GLN H H 7.71 0.02 1 378 91 91 GLN C C 179.20 0.10 1 379 91 91 GLN CA C 57.76 0.10 1 380 91 91 GLN CB C 27.05 0.10 1 381 91 91 GLN N N 119.90 0.15 1 382 92 92 PHE H H 7.77 0.02 1 383 92 92 PHE C C 177.10 0.10 1 384 92 92 PHE CA C 59.43 0.10 1 385 92 92 PHE CB C 37.49 0.10 1 386 92 92 PHE N N 119.30 0.15 1 387 93 93 LEU H H 7.57 0.02 1 388 93 93 LEU C C 176.50 0.10 1 389 93 93 LEU CA C 54.16 0.10 1 390 93 93 LEU CB C 42.26 0.10 1 391 93 93 LEU N N 117.00 0.15 1 392 94 94 ARG H H 7.35 0.02 1 393 94 94 ARG C C 178.60 0.10 1 394 94 94 ARG CA C 60.97 0.10 1 395 94 94 ARG CB C 29.82 0.10 1 396 94 94 ARG N N 121.10 0.15 1 397 95 95 SER C C 176.00 0.10 1 398 95 95 SER CA C 61.48 0.10 1 399 96 96 VAL H H 7.24 0.02 1 400 96 96 VAL C C 179.10 0.10 1 401 96 96 VAL CA C 65.24 0.10 1 402 96 96 VAL CB C 30.26 0.10 1 403 96 96 VAL N N 122.70 0.15 1 404 97 97 PHE H H 7.67 0.02 1 405 97 97 PHE C C 177.80 0.10 1 406 97 97 PHE CA C 59.79 0.10 1 407 97 97 PHE CB C 42.29 0.10 1 408 97 97 PHE N N 117.60 0.15 1 409 98 98 ALA H H 8.17 0.02 1 410 98 98 ALA C C 178.60 0.10 1 411 98 98 ALA CA C 54.55 0.10 1 412 98 98 ALA CB C 18.82 0.10 1 413 98 98 ALA N N 118.60 0.15 1 414 99 99 ASN H H 7.37 0.02 1 415 99 99 ASN C C 174.50 0.10 1 416 99 99 ASN CA C 53.03 0.10 1 417 99 99 ASN CB C 39.58 0.10 1 418 99 99 ASN N N 113.40 0.15 1 419 100 100 SER H H 7.39 0.02 1 420 100 100 SER C C 176.10 0.10 1 421 100 100 SER CA C 57.86 0.10 1 422 100 100 SER CB C 64.25 0.10 1 423 100 100 SER N N 115.60 0.15 1 424 103 103 TYR C C 177.60 0.10 1 425 103 103 TYR CA C 60.52 0.10 1 426 104 104 GLY H H 8.36 0.02 1 427 104 104 GLY C C 174.90 0.10 1 428 104 104 GLY CA C 45.51 0.10 1 429 104 104 GLY N N 112.40 0.15 1 430 105 105 ALA H H 7.87 0.02 1 431 105 105 ALA C C 178.20 0.10 1 432 105 105 ALA CA C 53.77 0.10 1 433 105 105 ALA CB C 18.25 0.10 1 434 105 105 ALA N N 123.10 0.15 1 435 106 106 SER H H 8.08 0.02 1 436 106 106 SER CA C 59.43 0.10 1 437 106 106 SER N N 112.80 0.15 1 438 107 107 ASP C C 176.10 0.10 1 439 107 107 ASP CA C 54.72 0.10 1 440 108 108 SER H H 7.69 0.02 1 441 108 108 SER C C 174.30 0.10 1 442 108 108 SER CA C 58.60 0.10 1 443 108 108 SER CB C 63.93 0.10 1 444 108 108 SER N N 114.20 0.15 1 445 109 109 ASN H H 8.52 0.02 1 446 109 109 ASN C C 176.60 0.10 1 447 109 109 ASN CA C 52.73 0.10 1 448 109 109 ASN N N 121.40 0.15 1 449 116 116 ASP C C 177.70 0.10 1 450 116 116 ASP CA C 55.55 0.10 1 451 116 116 ASP CB C 36.67 0.10 1 452 117 117 LEU H H 8.22 0.02 1 453 117 117 LEU C C 177.40 0.10 1 454 117 117 LEU CA C 57.28 0.10 1 455 117 117 LEU CB C 40.00 0.10 1 456 117 117 LEU N N 123.00 0.15 1 457 118 118 GLU H H 8.92 0.02 1 458 118 118 GLU C C 177.80 0.10 1 459 118 118 GLU CA C 60.23 0.10 1 460 118 118 GLU CB C 28.24 0.10 1 461 118 118 GLU N N 122.50 0.15 1 462 119 119 GLU H H 7.78 0.02 1 463 119 119 GLU C C 179.70 0.10 1 464 119 119 GLU CA C 59.16 0.10 1 465 119 119 GLU CB C 28.24 0.10 1 466 119 119 GLU N N 117.70 0.15 1 467 120 120 GLY H H 8.36 0.02 1 468 120 120 GLY C C 176.70 0.10 1 469 120 120 GLY CA C 47.14 0.10 1 470 120 120 GLY N N 109.00 0.15 1 471 121 121 ILE H H 9.03 0.02 1 472 121 121 ILE C C 178.00 0.10 1 473 121 121 ILE CA C 66.19 0.10 1 474 121 121 ILE CB C 36.95 0.10 1 475 121 121 ILE N N 122.60 0.15 1 476 122 122 GLN H H 8.37 0.02 1 477 122 122 GLN C C 179.80 0.10 1 478 122 122 GLN CA C 60.29 0.10 1 479 122 122 GLN CB C 27.92 0.10 1 480 122 122 GLN N N 120.10 0.15 1 481 123 123 THR H H 8.56 0.02 1 482 123 123 THR C C 177.30 0.10 1 483 123 123 THR CA C 65.56 0.10 1 484 123 123 THR CB C 67.42 0.10 1 485 123 123 THR N N 118.00 0.15 1 486 124 124 LEU H H 7.94 0.02 1 487 124 124 LEU C C 178.20 0.10 1 488 124 124 LEU CA C 58.36 0.10 1 489 124 124 LEU CB C 41.68 0.10 1 490 124 124 LEU N N 123.30 0.15 1 491 125 125 MET H H 8.55 0.02 1 492 125 125 MET C C 178.30 0.10 1 493 125 125 MET CA C 60.03 0.10 1 494 125 125 MET CB C 31.77 0.10 1 495 125 125 MET N N 116.70 0.15 1 496 126 126 GLY H H 7.72 0.02 1 497 126 126 GLY C C 176.30 0.10 1 498 126 126 GLY CA C 46.98 0.10 1 499 126 126 GLY N N 103.81 0.15 1 500 127 127 ARG H H 7.58 0.02 1 501 127 127 ARG C C 177.30 0.10 1 502 127 127 ARG CA C 55.69 0.10 1 503 127 127 ARG CB C 28.74 0.10 1 504 127 127 ARG N N 118.80 0.15 1 505 128 128 LEU H H 7.73 0.02 1 506 128 128 LEU C C 176.40 0.10 1 507 128 128 LEU CA C 55.05 0.10 1 508 128 128 LEU CB C 40.59 0.10 1 509 128 128 LEU N N 119.00 0.15 1 510 129 129 GLU H H 7.32 0.02 1 511 129 129 GLU C C 176.10 0.10 1 512 129 129 GLU CA C 58.00 0.10 1 513 129 129 GLU CB C 29.54 0.10 1 514 129 129 GLU N N 120.60 0.15 1 515 130 130 ASP H H 7.88 0.02 1 516 130 130 ASP C C 177.50 0.10 1 517 130 130 ASP CA C 53.46 0.10 1 518 130 130 ASP CB C 41.28 0.10 1 519 130 130 ASP N N 124.10 0.15 1 520 131 131 GLY H H 9.12 0.02 1 521 131 131 GLY C C 174.50 0.10 1 522 131 131 GLY CA C 45.38 0.10 1 523 131 131 GLY N N 110.60 0.15 1 524 132 132 SER H H 8.12 0.02 1 525 132 132 SER C C 172.60 0.10 1 526 132 132 SER CA C 57.39 0.10 1 527 132 132 SER CB C 62.59 0.10 1 528 132 132 SER N N 117.70 0.15 1 529 135 135 THR C C 175.40 0.10 1 530 135 135 THR CA C 61.72 0.10 1 531 135 135 THR CB C 69.74 0.10 1 532 136 136 GLY H H 8.50 0.02 1 533 136 136 GLY C C 174.30 0.10 1 534 136 136 GLY CA C 44.99 0.10 1 535 136 136 GLY N N 110.20 0.15 1 536 139 139 PHE C C 175.90 0.10 1 537 139 139 PHE CA C 56.30 0.10 1 538 140 140 LYS H H 7.88 0.02 1 539 140 140 LYS C C 175.80 0.10 1 540 140 140 LYS CA C 60.15 0.10 1 541 140 140 LYS CB C 37.57 0.10 1 542 140 140 LYS N N 120.30 0.15 1 543 141 141 GLN H H 7.67 0.02 1 544 141 141 GLN C C 174.50 0.10 1 545 141 141 GLN CA C 55.65 0.10 1 546 141 141 GLN CB C 29.62 0.10 1 547 141 141 GLN N N 121.30 0.15 1 548 142 142 THR H H 8.00 0.02 1 549 142 142 THR C C 174.10 0.10 1 550 142 142 THR CA C 60.25 0.10 1 551 142 142 THR CB C 69.95 0.10 1 552 142 142 THR N N 114.60 0.15 1 553 143 143 TYR H H 7.94 0.02 1 554 143 143 TYR C C 174.80 0.10 1 555 143 143 TYR CA C 58.01 0.10 1 556 143 143 TYR CB C 37.62 0.10 1 557 143 143 TYR N N 119.30 0.15 1 558 144 144 SER H H 8.28 0.02 1 559 144 144 SER C C 173.50 0.10 1 560 144 144 SER CA C 58.57 0.10 1 561 144 144 SER CB C 64.28 0.10 1 562 144 144 SER N N 117.00 0.15 1 563 145 145 LYS H H 8.30 0.02 1 564 145 145 LYS C C 175.50 0.10 1 565 145 145 LYS CA C 55.61 0.10 1 566 145 145 LYS CB C 33.84 0.10 1 567 145 145 LYS N N 122.80 0.15 1 568 146 146 PHE H H 8.25 0.02 1 569 146 146 PHE C C 174.30 0.10 1 570 146 146 PHE CA C 56.83 0.10 1 571 146 146 PHE CB C 39.56 0.10 1 572 146 146 PHE N N 123.40 0.15 1 573 147 147 ASP H H 8.09 0.02 1 574 147 147 ASP C C 175.90 0.10 1 575 147 147 ASP CA C 51.63 0.10 1 576 147 147 ASP CB C 42.94 0.10 1 577 147 147 ASP N N 125.70 0.15 1 578 148 148 THR H H 7.94 0.02 1 579 148 148 THR C C 174.80 0.10 1 580 148 148 THR CA C 62.71 0.10 1 581 148 148 THR CB C 69.20 0.10 1 582 148 148 THR N N 116.20 0.15 1 583 149 149 ASN H H 8.29 0.02 1 584 149 149 ASN C C 175.30 0.10 1 585 149 149 ASN CA C 53.82 0.10 1 586 149 149 ASN CB C 38.68 0.10 1 587 149 149 ASN N N 120.00 0.15 1 588 150 150 SER H H 7.82 0.02 1 589 150 150 SER C C 174.20 0.10 1 590 150 150 SER CA C 58.86 0.10 1 591 150 150 SER CB C 64.11 0.10 1 592 150 150 SER N N 115.30 0.15 1 593 152 152 ASN C C 175.00 0.10 1 594 152 152 ASN CA C 53.94 0.10 1 595 152 152 ASN CB C 41.14 0.10 1 596 153 153 ASP H H 8.42 0.02 1 597 153 153 ASP C C 175.80 0.10 1 598 153 153 ASP CA C 54.75 0.10 1 599 153 153 ASP CB C 39.98 0.10 1 600 153 153 ASP N N 119.90 0.15 1 601 154 154 ASP H H 8.07 0.02 1 602 154 154 ASP C C 175.90 0.10 1 603 154 154 ASP CA C 54.14 0.10 1 604 154 154 ASP CB C 41.41 0.10 1 605 154 154 ASP N N 120.20 0.15 1 606 155 155 ALA H H 8.44 0.02 1 607 155 155 ALA C C 179.00 0.10 1 608 155 155 ALA CA C 55.03 0.10 1 609 155 155 ALA CB C 17.80 0.10 1 610 155 155 ALA N N 126.90 0.15 1 611 156 156 LEU H H 8.00 0.02 1 612 156 156 LEU C C 178.40 0.10 1 613 156 156 LEU CA C 59.45 0.10 1 614 156 156 LEU CB C 41.54 0.10 1 615 156 156 LEU N N 119.00 0.15 1 616 157 157 LEU H H 7.85 0.02 1 617 157 157 LEU C C 180.80 0.10 1 618 157 157 LEU CA C 57.17 0.10 1 619 157 157 LEU CB C 40.08 0.10 1 620 157 157 LEU N N 117.60 0.15 1 621 158 158 LYS H H 8.37 0.02 1 622 158 158 LYS C C 179.40 0.10 1 623 158 158 LYS CA C 59.48 0.10 1 624 158 158 LYS CB C 31.05 0.10 1 625 158 158 LYS N N 122.10 0.15 1 626 159 159 ASN H H 8.25 0.02 1 627 159 159 ASN C C 176.60 0.10 1 628 159 159 ASN CA C 55.71 0.10 1 629 159 159 ASN CB C 37.05 0.10 1 630 159 159 ASN N N 119.30 0.15 1 631 160 160 TYR H H 8.47 0.02 1 632 160 160 TYR C C 177.30 0.10 1 633 160 160 TYR CA C 58.46 0.10 1 634 160 160 TYR N N 120.90 0.15 1 635 161 161 GLY H H 8.29 0.02 1 636 161 161 GLY C C 176.70 0.10 1 637 161 161 GLY CA C 47.17 0.10 1 638 161 161 GLY N N 103.58 0.15 1 639 162 162 LEU H H 8.16 0.02 1 640 162 162 LEU C C 179.10 0.10 1 641 162 162 LEU CA C 57.77 0.10 1 642 162 162 LEU CB C 42.69 0.10 1 643 162 162 LEU N N 122.60 0.15 1 644 163 163 LEU H H 8.51 0.02 1 645 163 163 LEU CA C 58.08 0.10 1 646 163 163 LEU CB C 42.59 0.10 1 647 163 163 LEU N N 119.60 0.15 1 648 167 167 ARG C C 177.20 0.10 1 649 167 167 ARG CA C 60.13 0.10 1 650 168 168 LYS H H 7.56 0.02 1 651 168 168 LYS C C 179.50 0.10 1 652 168 168 LYS CA C 59.06 0.10 1 653 168 168 LYS CB C 31.15 0.10 1 654 168 168 LYS N N 119.00 0.15 1 655 169 169 ASP H H 8.76 0.02 1 656 169 169 ASP C C 178.30 0.10 1 657 169 169 ASP CA C 57.23 0.10 1 658 169 169 ASP CB C 38.71 0.10 1 659 169 169 ASP N N 120.80 0.15 1 660 170 170 MET H H 8.28 0.02 1 661 170 170 MET C C 178.90 0.10 1 662 170 170 MET CA C 56.25 0.10 1 663 170 170 MET N N 118.60 0.15 1 664 171 171 ASP H H 7.57 0.02 1 665 171 171 ASP C C 178.60 0.10 1 666 171 171 ASP CA C 56.85 0.10 1 667 171 171 ASP CB C 41.30 0.10 1 668 171 171 ASP N N 120.10 0.15 1 669 172 172 LYS H H 7.24 0.02 1 670 172 172 LYS C C 176.50 0.10 1 671 172 172 LYS CA C 59.55 0.10 1 672 172 172 LYS CB C 30.60 0.10 1 673 172 172 LYS N N 119.70 0.15 1 674 173 173 VAL H H 7.75 0.02 1 675 173 173 VAL C C 178.00 0.10 1 676 173 173 VAL CA C 67.40 0.10 1 677 173 173 VAL CB C 30.56 0.10 1 678 173 173 VAL N N 116.90 0.15 1 679 175 175 THR H H 7.94 0.02 1 680 175 175 THR C C 176.60 0.10 1 681 175 175 THR CA C 67.23 0.10 1 682 175 175 THR CB C 68.02 0.10 1 683 175 175 THR N N 114.30 0.15 1 684 176 176 PHE H H 8.70 0.02 1 685 176 176 PHE C C 178.30 0.10 1 686 176 176 PHE CA C 57.92 0.10 1 687 176 176 PHE CB C 36.42 0.10 1 688 176 176 PHE N N 120.80 0.15 1 689 177 177 LEU H H 8.53 0.02 1 690 177 177 LEU C C 178.40 0.10 1 691 177 177 LEU CA C 58.31 0.10 1 692 177 177 LEU CB C 41.04 0.10 1 693 177 177 LEU N N 118.70 0.15 1 694 178 178 ARG H H 8.07 0.02 1 695 178 178 ARG C C 178.60 0.10 1 696 178 178 ARG CA C 58.55 0.10 1 697 178 178 ARG CB C 28.83 0.10 1 698 178 178 ARG N N 119.10 0.15 1 699 179 179 ILE H H 7.81 0.02 1 700 179 179 ILE C C 178.20 0.10 1 701 179 179 ILE CA C 64.98 0.10 1 702 179 179 ILE CB C 36.96 0.10 1 703 179 179 ILE N N 119.30 0.15 1 704 180 180 VAL H H 7.77 0.02 1 705 180 180 VAL C C 178.50 0.10 1 706 180 180 VAL CA C 66.57 0.10 1 707 180 180 VAL CB C 30.45 0.10 1 708 180 180 VAL N N 118.60 0.15 1 709 181 181 GLN H H 8.75 0.02 1 710 181 181 GLN C C 177.40 0.10 1 711 181 181 GLN CA C 59.62 0.10 1 712 181 181 GLN CB C 27.50 0.10 1 713 181 181 GLN N N 123.70 0.15 1 714 182 182 CYS H H 8.43 0.02 1 715 182 182 CYS C C 177.00 0.10 1 716 182 182 CYS CA C 57.93 0.10 1 717 182 182 CYS N N 116.10 0.15 1 718 183 183 ARG H H 7.90 0.02 1 719 183 183 ARG C C 178.20 0.10 1 720 183 183 ARG CA C 58.57 0.10 1 721 183 183 ARG N N 116.30 0.15 1 722 184 184 SER H H 7.81 0.02 1 723 184 184 SER C C 174.10 0.10 1 724 184 184 SER CA C 60.70 0.10 1 725 184 184 SER N N 113.20 0.15 1 726 185 185 VAL H H 7.94 0.02 1 727 185 185 VAL C C 175.70 0.10 1 728 185 185 VAL CA C 61.41 0.10 1 729 185 185 VAL CB C 31.15 0.10 1 730 185 185 VAL N N 120.00 0.15 1 731 186 186 GLU H H 8.39 0.02 1 732 186 186 GLU C C 177.40 0.10 1 733 186 186 GLU CA C 54.53 0.10 1 734 186 186 GLU CB C 28.78 0.10 1 735 186 186 GLU N N 124.70 0.15 1 736 187 187 GLY H H 8.58 0.02 1 737 187 187 GLY C C 174.50 0.10 1 738 187 187 GLY N N 111.20 0.15 1 739 188 188 SER H H 8.00 0.02 1 740 188 188 SER CA C 59.46 0.10 1 741 188 188 SER N N 114.90 0.15 1 742 189 189 CYS C C 174.60 0.10 1 743 190 190 GLY H H 8.25 0.02 1 744 190 190 GLY C C 172.60 0.10 1 745 190 190 GLY CA C 47.46 0.10 1 746 190 190 GLY N N 109.60 0.15 1 747 191 191 PHE H H 7.43 0.02 1 748 191 191 PHE C C 177.40 0.10 1 749 191 191 PHE CA C 55.77 0.10 1 750 191 191 PHE CB C 40.35 0.10 1 751 191 191 PHE N N 124.00 0.15 1 stop_ save_