data_15148 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HMGB1 AB boxes + basic tail backbone assignment ; _BMRB_accession_number 15148 _BMRB_flat_file_name bmr15148.str _Entry_type original _Submission_date 2007-02-26 _Accession_date 2007-02-26 _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 Mollica Luca . . 2 Musco Francesco . . 3 Spitaleri Andrea . . 4 Dallacosta Corrado . . 5 Zamai Moreno . . 6 Agresti Alessandra . . 7 Trisciuoglio Lisa . . 8 Bianchi Marco E. . 9 Musco Giovanna . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 174 "13C chemical shifts" 336 "15N chemical shifts" 174 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-06-05 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 15149 'HMGB1 Full Length' stop_ _Original_release_date 2007-06-05 save_ ############################# # Citation for this entry # ############################# save_Citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17462578 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mollica Luca . . 2 'De Marchis' Francesco . . 3 Spitaleri Andrea . . 4 Dallacosta Corrado . . 5 Pennacchini D. . . 6 Zamai Moreno . . 7 Agresti Alessandra . . 8 Trisciuoglio Lisa . . 9 Musco Giovanna . . 10 Bianchi Marco E. . stop_ _Journal_abbreviation 'Chem. Biol.' _Journal_volume 14 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 431 _Page_last 441 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HMGB1 AB boxes + basic tail' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HMGB1 ABbtail' $HMGB1_ABbtail stop_ _System_molecular_weight 21416.7 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HMGB1_ABbtail _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HMGB1_ABbtail _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 187 _Mol_residue_sequence ; GKGDPKKPRGKMSSYAFFVQ TCREEHKKKHPDASVNFSEF SKKCSERWKTMSAKEKGKFE DMAKADKARYEREMKTYIPP KGETKKKFKDPNAPKRPPSA FFLFCSEYRPKIKGEHPGLS IGDVAKKLGEMWNNTAADDK QPYEKKAAKLKEKYEKDIAA YRAKGKPDAAKKGVVKAEKS KKKKEEE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 LYS 3 GLY 4 ASP 5 PRO 6 LYS 7 LYS 8 PRO 9 ARG 10 GLY 11 LYS 12 MET 13 SER 14 SER 15 TYR 16 ALA 17 PHE 18 PHE 19 VAL 20 GLN 21 THR 22 CYS 23 ARG 24 GLU 25 GLU 26 HIS 27 LYS 28 LYS 29 LYS 30 HIS 31 PRO 32 ASP 33 ALA 34 SER 35 VAL 36 ASN 37 PHE 38 SER 39 GLU 40 PHE 41 SER 42 LYS 43 LYS 44 CYS 45 SER 46 GLU 47 ARG 48 TRP 49 LYS 50 THR 51 MET 52 SER 53 ALA 54 LYS 55 GLU 56 LYS 57 GLY 58 LYS 59 PHE 60 GLU 61 ASP 62 MET 63 ALA 64 LYS 65 ALA 66 ASP 67 LYS 68 ALA 69 ARG 70 TYR 71 GLU 72 ARG 73 GLU 74 MET 75 LYS 76 THR 77 TYR 78 ILE 79 PRO 80 PRO 81 LYS 82 GLY 83 GLU 84 THR 85 LYS 86 LYS 87 LYS 88 PHE 89 LYS 90 ASP 91 PRO 92 ASN 93 ALA 94 PRO 95 LYS 96 ARG 97 PRO 98 PRO 99 SER 100 ALA 101 PHE 102 PHE 103 LEU 104 PHE 105 CYS 106 SER 107 GLU 108 TYR 109 ARG 110 PRO 111 LYS 112 ILE 113 LYS 114 GLY 115 GLU 116 HIS 117 PRO 118 GLY 119 LEU 120 SER 121 ILE 122 GLY 123 ASP 124 VAL 125 ALA 126 LYS 127 LYS 128 LEU 129 GLY 130 GLU 131 MET 132 TRP 133 ASN 134 ASN 135 THR 136 ALA 137 ALA 138 ASP 139 ASP 140 LYS 141 GLN 142 PRO 143 TYR 144 GLU 145 LYS 146 LYS 147 ALA 148 ALA 149 LYS 150 LEU 151 LYS 152 GLU 153 LYS 154 TYR 155 GLU 156 LYS 157 ASP 158 ILE 159 ALA 160 ALA 161 TYR 162 ARG 163 ALA 164 LYS 165 GLY 166 LYS 167 PRO 168 ASP 169 ALA 170 ALA 171 LYS 172 LYS 173 GLY 174 VAL 175 VAL 176 LYS 177 ALA 178 GLU 179 LYS 180 SER 181 LYS 182 LYS 183 LYS 184 LYS 185 GLU 186 GLU 187 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 BMRB 11147 "HMG box domain" 88.24 173 100.00 100.00 3.14e-114 BMRB 15149 HMGB1_Full_Length 100.00 214 100.00 100.00 1.46e-128 BMRB 15502 HMGB1 100.00 214 100.00 100.00 1.46e-128 PDB 2YRQ "Solution Structure Of The Tandem Hmg Box Domain From Human High Mobility Group Protein B1" 88.24 173 100.00 100.00 3.14e-114 DBJ BAA09924 "HMG-1 [Homo sapiens]" 100.00 215 98.93 98.93 2.44e-126 DBJ BAC29902 "unnamed protein product [Mus musculus]" 100.00 215 100.00 100.00 1.86e-128 DBJ BAC34367 "unnamed protein product [Mus musculus]" 94.65 178 100.00 100.00 2.77e-122 DBJ BAC34773 "unnamed protein product [Mus musculus]" 100.00 215 99.47 99.47 3.41e-127 DBJ BAC38678 "unnamed protein product [Mus musculus]" 96.26 181 100.00 100.00 4.52e-124 EMBL CAA31110 "unnamed protein product [Homo sapiens]" 100.00 215 100.00 100.00 1.86e-128 EMBL CAA31284 "unnamed protein product [Bos taurus]" 100.00 215 100.00 100.00 1.88e-128 EMBL CAA56631 "high mobility group protein [Mus musculus]" 100.00 215 100.00 100.00 1.88e-128 EMBL CAA68441 "high mobility group protein [Cricetulus griseus]" 81.82 180 100.00 100.00 1.44e-101 EMBL CAA68526 "unnamed protein product [Rattus norvegicus]" 100.00 215 100.00 100.00 1.86e-128 GB AAA20508 "HMG-1 [Mus musculus]" 100.00 215 100.00 100.00 1.86e-128 GB AAA31050 "non-histone protein HMG1 [Sus scrofa]" 100.00 215 99.47 99.47 1.54e-127 GB AAA40729 "Amphoterin [Rattus norvegicus]" 100.00 215 100.00 100.00 1.86e-128 GB AAA57042 "high mobility group 1 protein [Mus musculus]" 100.00 215 99.47 99.47 2.33e-127 GB AAA64970 "HMG-1 [Homo sapiens]" 100.00 216 98.93 98.93 2.64e-126 PIR S29857 "nonhistone chromosomal protein HMG-1 - human" 100.00 216 98.93 98.93 2.64e-126 REF NP_001002937 "high mobility group protein B1 [Canis lupus familiaris]" 100.00 215 100.00 100.00 1.86e-128 REF NP_001004034 "high mobility group protein B1 [Sus scrofa]" 100.00 215 99.47 99.47 1.54e-127 REF NP_001075304 "high mobility group protein B1 [Equus caballus]" 100.00 215 100.00 100.00 1.86e-128 REF NP_001102843 "high mobility group box 1 like [Rattus norvegicus]" 100.00 214 99.47 99.47 2.56e-127 REF NP_001162380 "high mobility group protein B1 [Papio anubis]" 100.00 215 100.00 100.00 1.86e-128 SP A9RA84 "RecName: Full=High mobility group protein B1; AltName: Full=High mobility group protein 1; Short=HMG-1" 100.00 215 100.00 100.00 1.86e-128 SP B0CM99 "RecName: Full=High mobility group protein B1; AltName: Full=High mobility group protein 1; Short=HMG-1" 100.00 215 100.00 100.00 1.86e-128 SP B1MTB0 "RecName: Full=High mobility group protein B1; AltName: Full=High mobility group protein 1; Short=HMG-1" 100.00 215 100.00 100.00 1.86e-128 SP P07156 "RecName: Full=High mobility group protein B1; AltName: Full=High mobility group protein 1; Short=HMG-1" 81.82 180 100.00 100.00 1.44e-101 SP P09429 "RecName: Full=High mobility group protein B1; AltName: Full=High mobility group protein 1; Short=HMG-1" 100.00 215 100.00 100.00 1.86e-128 TPG DAA21468 "TPA: high-mobility group box 1-like [Bos taurus]" 100.00 215 98.40 98.40 1.49e-126 TPG DAA23902 "TPA: high mobility group protein B1 [Bos taurus]" 100.00 215 100.00 100.00 1.88e-128 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HMGB1_ABbtail 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $HMGB1_ABbtail 'recombinant technology' . Escherichia coli . pET-24d 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 $HMGB1_ABbtail . mM 0.1 0.3 '[U-100% 13C; U-100% 15N]' NaCl 150 mM . . . 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _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 'ionic strength' 150 . mM pH 7 . pH pressure 1 . atm temperature 298 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 'HMGB1 ABbtail' _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 1 1 GLY H H 7.363 0.090 1 2 1 1 GLY N N 110.541 0.100 1 3 1 1 GLY CA C 41.124 0.200 1 4 2 2 LYS H H 8.739 0.090 1 5 2 2 LYS N N 120.996 0.100 1 6 2 2 LYS CA C 54.666 0.200 1 7 2 2 LYS CB C 30.074 0.200 1 8 3 3 GLY H H 8.663 0.090 1 9 3 3 GLY N N 110.554 0.100 1 10 3 3 GLY CA C 42.463 0.200 1 11 4 4 ASP H H 8.121 0.090 1 12 4 4 ASP N N 121.098 0.100 1 13 4 4 ASP CA C 49.960 0.200 1 14 4 4 ASP CB C 37.957 0.200 1 15 5 5 PRO CA C 60.744 0.200 1 16 6 6 LYS H H 8.407 0.090 1 17 6 6 LYS N N 120.395 0.100 1 18 6 6 LYS CA C 53.169 0.200 1 19 6 6 LYS CB C 30.025 0.200 1 20 7 7 LYS H H 8.010 0.090 1 21 7 7 LYS N N 123.587 0.100 1 22 7 7 LYS CA C 52.005 0.200 1 23 7 7 LYS CB C 30.145 0.200 1 24 8 8 PRO CA C 60.117 0.200 1 25 8 8 PRO CB C 29.151 0.200 1 26 9 9 ARG H H 8.960 0.090 1 27 9 9 ARG N N 124.122 0.100 1 28 9 9 ARG CA C 54.162 0.200 1 29 9 9 ARG CB C 27.588 0.200 1 30 10 10 GLY H H 8.622 0.090 1 31 10 10 GLY N N 110.733 0.100 1 32 10 10 GLY CA C 42.794 0.200 1 33 11 11 LYS H H 7.681 0.090 1 34 11 11 LYS N N 119.747 0.100 1 35 11 11 LYS CA C 54.054 0.200 1 36 11 11 LYS CB C 29.364 0.200 1 37 12 12 MET H H 9.031 0.090 1 38 12 12 MET N N 124.497 0.100 1 39 12 12 MET CA C 52.432 0.200 1 40 12 12 MET CB C 32.418 0.200 1 41 13 13 SER H H 8.203 0.090 1 42 13 13 SER N N 118.984 0.100 1 43 13 13 SER CA C 54.666 0.200 1 44 13 13 SER CB C 62.815 0.200 1 45 14 14 SER H H 9.322 0.090 1 46 14 14 SER N N 116.067 0.100 1 47 14 14 SER CA C 58.868 0.200 1 48 14 14 SER CB C 59.477 0.200 1 49 15 15 TYR H H 7.973 0.090 1 50 15 15 TYR N N 121.607 0.100 1 51 15 15 TYR CA C 58.034 0.200 1 52 15 15 TYR CB C 35.330 0.200 1 53 16 16 ALA H H 7.899 0.090 1 54 16 16 ALA N N 121.500 0.100 1 55 16 16 ALA CA C 52.699 0.200 1 56 16 16 ALA CB C 15.372 0.200 1 57 17 17 PHE H H 8.325 0.090 1 58 17 17 PHE N N 117.887 0.100 1 59 17 17 PHE CA C 61.169 0.200 1 60 17 17 PHE CB C 37.176 0.200 1 61 18 18 PHE H H 8.104 0.090 1 62 18 18 PHE N N 124.925 0.100 1 63 18 18 PHE CA C 58.468 0.200 1 64 18 18 PHE CB C 35.685 0.200 1 65 19 19 VAL H H 8.475 0.090 1 66 19 19 VAL N N 122.102 0.100 1 67 19 19 VAL CA C 64.740 0.200 1 68 19 19 VAL CB C 27.730 0.200 1 69 20 20 GLN H H 7.841 0.090 1 70 20 20 GLN N N 117.994 0.100 1 71 20 20 GLN CA C 56.963 0.200 1 72 20 20 GLN CB C 26.381 0.200 1 73 21 21 THR H H 8.192 0.090 1 74 21 21 THR N N 116.107 0.100 1 75 21 21 THR CA C 64.728 0.200 1 76 21 21 THR CB C 66.438 0.200 1 77 22 22 CYS H H 8.372 0.090 1 78 22 22 CYS N N 120.603 0.100 1 79 22 22 CYS CA C 61.177 0.200 1 80 23 23 ARG H H 8.898 0.090 1 81 23 23 ARG N N 122.530 0.100 1 82 23 23 ARG CA C 57.350 0.200 1 83 23 23 ARG CB C 27.304 0.200 1 84 24 24 GLU H H 8.194 0.090 1 85 24 24 GLU N N 120.175 0.100 1 86 24 24 GLU CA C 56.863 0.200 1 87 24 24 GLU CB C 26.665 0.200 1 88 25 25 GLU H H 8.323 0.090 1 89 25 25 GLU N N 119.599 0.100 1 90 25 25 GLU CA C 56.767 0.200 1 91 25 25 GLU CB C 26.949 0.200 1 92 26 26 HIS H H 8.207 0.090 1 93 26 26 HIS N N 118.676 0.100 1 94 26 26 HIS CA C 58.057 0.200 1 95 27 27 LYS H H 7.945 0.090 1 96 27 27 LYS N N 118.101 0.100 1 97 27 27 LYS CA C 55.900 0.200 1 98 27 27 LYS CB C 29.577 0.200 1 99 28 28 LYS H H 7.559 0.090 1 100 28 28 LYS N N 116.468 0.100 1 101 28 28 LYS CA C 56.067 0.200 1 102 28 28 LYS CB C 29.790 0.200 1 103 29 29 LYS H H 7.505 0.090 1 104 29 29 LYS N N 115.612 0.100 1 105 29 29 LYS CA C 54.745 0.200 1 106 29 29 LYS CB C 31.139 0.200 1 107 30 30 HIS H H 7.990 0.090 1 108 30 30 HIS N N 115.050 0.100 1 109 30 30 HIS CA C 49.823 0.200 1 110 30 30 HIS CB C 25.883 0.200 1 111 31 31 PRO CA C 62.318 0.200 1 112 31 31 PRO CB C 29.080 0.200 1 113 32 32 ASP H H 8.537 0.090 1 114 32 32 ASP N N 115.866 0.100 1 115 32 32 ASP CA C 51.332 0.200 1 116 32 32 ASP CB C 38.312 0.200 1 117 33 33 ALA H H 7.528 0.090 1 118 33 33 ALA N N 122.516 0.100 1 119 33 33 ALA CA C 49.564 0.200 1 120 33 33 ALA CB C 17.574 0.200 1 121 34 34 SER H H 8.596 0.090 1 122 34 34 SER N N 117.405 0.100 1 123 34 34 SER CA C 55.433 0.200 1 124 34 34 SER CB C 60.969 0.200 1 125 35 35 VAL H H 8.300 0.090 1 126 35 35 VAL N N 122.102 0.100 1 127 35 35 VAL CA C 59.034 0.200 1 128 35 35 VAL CB C 30.358 0.200 1 129 36 36 ASN H H 8.692 0.090 1 130 36 36 ASN N N 124.952 0.100 1 131 36 36 ASN CA C 49.998 0.200 1 132 36 36 ASN CB C 35.685 0.200 1 133 37 37 PHE H H 8.945 0.090 1 134 37 37 PHE N N 125.915 0.100 1 135 37 37 PHE CA C 59.601 0.200 1 136 37 37 PHE CB C 36.278 0.200 1 137 38 38 SER H H 8.665 0.090 1 138 38 38 SER N N 116.281 0.100 1 139 38 38 SER CA C 59.301 0.200 1 140 38 38 SER CB C 60.097 0.200 1 141 39 39 GLU H H 7.857 0.090 1 142 39 39 GLU N N 121.901 0.100 1 143 39 39 GLU CA C 56.203 0.200 1 144 39 39 GLU CB C 27.218 0.200 1 145 40 40 PHE H H 8.584 0.090 1 146 40 40 PHE N N 121.459 0.100 1 147 40 40 PHE CA C 59.072 0.200 1 148 40 40 PHE CB C 36.936 0.200 1 149 41 41 SER H H 8.474 0.090 1 150 41 41 SER N N 114.541 0.100 1 151 41 41 SER CA C 59.405 0.200 1 152 41 41 SER CB C 60.243 0.200 1 153 42 42 LYS H H 7.503 0.090 1 154 42 42 LYS N N 121.794 0.100 1 155 42 42 LYS CA C 56.962 0.200 1 156 42 42 LYS CB C 29.630 0.200 1 157 43 43 LYS H H 7.854 0.090 1 158 43 43 LYS N N 119.332 0.100 1 159 43 43 LYS CA C 56.700 0.200 1 160 43 43 LYS CB C 29.191 0.200 1 161 44 44 CYS H H 8.066 0.090 1 162 44 44 CYS N N 117.218 0.100 1 163 44 44 CYS CA C 61.969 0.200 1 164 44 44 CYS CB C 24.150 0.200 1 165 45 45 SER H H 8.320 0.090 1 166 45 45 SER N N 116.870 0.100 1 167 45 45 SER CA C 59.584 0.200 1 168 46 46 GLU H H 8.054 0.090 1 169 46 46 GLU N N 120.817 0.100 1 170 46 46 GLU CA C 56.664 0.200 1 171 46 46 GLU CB C 26.874 0.200 1 172 47 47 ARG H H 8.045 0.090 1 173 47 47 ARG N N 119.318 0.100 1 174 47 47 ARG CA C 56.431 0.200 1 175 47 47 ARG CB C 27.932 0.200 1 176 48 48 TRP H H 8.665 0.090 1 177 48 48 TRP N N 120.389 0.100 1 178 48 48 TRP CA C 57.095 0.200 1 179 48 48 TRP CB C 28.144 0.200 1 180 49 49 LYS H H 7.588 0.090 1 181 49 49 LYS N N 114.354 0.100 1 182 49 49 LYS CA C 56.392 0.200 1 183 49 49 LYS CB C 30.191 0.200 1 184 50 50 THR H H 7.398 0.090 1 185 50 50 THR N N 106.138 0.100 1 186 50 50 THR CA C 58.834 0.200 1 187 50 50 THR CB C 67.101 0.200 1 188 51 51 MET H H 7.129 0.090 1 189 51 51 MET N N 123.480 0.100 1 190 51 51 MET CA C 53.966 0.200 1 191 51 51 MET CB C 32.449 0.200 1 192 52 52 SER H H 9.026 0.090 1 193 52 52 SER N N 119.653 0.100 1 194 52 52 SER CA C 54.666 0.200 1 195 52 52 SER CB C 62.726 0.200 1 196 53 53 ALA H H 8.871 0.090 1 197 53 53 ALA N N 122.958 0.100 1 198 53 53 ALA CA C 53.097 0.200 1 199 53 53 ALA CB C 15.158 0.200 1 200 54 54 LYS H H 8.257 0.090 1 201 54 54 LYS N N 117.753 0.100 1 202 54 54 LYS CA C 56.667 0.200 1 203 54 54 LYS CB C 29.626 0.200 1 204 55 55 GLU H H 7.680 0.090 1 205 55 55 GLU N N 119.961 0.100 1 206 55 55 GLU CA C 56.709 0.200 1 207 55 55 GLU CB C 27.579 0.200 1 208 56 56 LYS H H 8.130 0.090 1 209 56 56 LYS N N 116.749 0.100 1 210 56 56 LYS CA C 57.080 0.200 1 211 56 56 LYS CB C 35.343 0.200 1 212 57 57 GLY H H 7.859 0.090 1 213 57 57 GLY N N 106.807 0.100 1 214 57 57 GLY CA C 45.449 0.200 1 215 58 58 LYS H H 7.921 0.090 1 216 58 58 LYS N N 119.011 0.100 1 217 58 58 LYS CA C 56.473 0.200 1 218 58 58 LYS CB C 28.920 0.200 1 219 59 59 PHE H H 7.311 0.090 1 220 59 59 PHE N N 119.549 0.100 1 221 59 59 PHE CA C 58.295 0.200 1 222 59 59 PHE CB C 35.978 0.200 1 223 60 60 GLU H H 8.429 0.090 1 224 60 60 GLU N N 121.775 0.100 1 225 60 60 GLU CA C 56.776 0.200 1 226 60 60 GLU CB C 26.027 0.200 1 227 61 61 ASP H H 8.641 0.090 1 228 61 61 ASP N N 120.817 0.100 1 229 61 61 ASP CA C 55.171 0.200 1 230 61 61 ASP CB C 36.825 0.200 1 231 62 62 MET H H 7.382 0.090 1 232 62 62 MET N N 120.400 0.100 1 233 62 62 MET CA C 56.797 0.200 1 234 62 62 MET CB C 36.717 0.200 1 235 63 63 ALA H H 8.011 0.090 1 236 63 63 ALA N N 122.945 0.100 1 237 63 63 ALA CA C 53.030 0.200 1 238 63 63 ALA CB C 15.934 0.200 1 239 64 64 LYS H H 8.601 0.090 1 240 64 64 LYS N N 122.062 0.100 1 241 64 64 LYS CA C 57.654 0.200 1 242 64 64 LYS CB C 29.767 0.200 1 243 65 65 ALA H H 7.943 0.090 1 244 65 65 ALA N N 122.516 0.100 1 245 65 65 ALA CA C 52.253 0.200 1 246 65 65 ALA CB C 15.229 0.200 1 247 66 66 ASP H H 8.348 0.090 1 248 66 66 ASP N N 119.961 0.100 1 249 66 66 ASP CA C 54.987 0.200 1 250 66 66 ASP CB C 40.071 0.200 1 251 67 67 LYS H H 8.229 0.090 1 252 67 67 LYS N N 120.402 0.100 1 253 67 67 LYS CA C 57.350 0.200 1 254 67 67 LYS CB C 30.049 0.200 1 255 68 68 ALA H H 7.481 0.090 1 256 68 68 ALA N N 120.456 0.100 1 257 68 68 ALA CA C 52.456 0.200 1 258 68 68 ALA CB C 15.158 0.200 1 259 69 69 ARG H H 7.992 0.090 1 260 69 69 ARG N N 120.590 0.100 1 261 69 69 ARG CA C 56.515 0.200 1 262 69 69 ARG CB C 26.874 0.200 1 263 70 70 TYR H H 8.585 0.090 1 264 70 70 TYR N N 121.360 0.100 1 265 70 70 TYR CA C 59.268 0.200 1 266 70 70 TYR CB C 37.036 0.200 1 267 71 71 GLU H H 8.449 0.090 1 268 71 71 GLU N N 116.656 0.100 1 269 71 71 GLU CA C 56.878 0.200 1 270 71 71 GLU CB C 26.634 0.200 1 271 72 72 ARG H H 8.079 0.090 1 272 72 72 ARG N N 119.626 0.100 1 273 72 72 ARG CA C 57.046 0.200 1 274 72 72 ARG CB C 26.874 0.200 1 275 73 73 GLU H H 8.488 0.090 1 276 73 73 GLU N N 119.492 0.100 1 277 73 73 GLU CA C 56.934 0.200 1 278 73 73 GLU CB C 27.085 0.200 1 279 74 74 MET H H 8.454 0.090 1 280 74 74 MET N N 117.191 0.100 1 281 74 74 MET CA C 53.299 0.200 1 282 74 74 MET CB C 28.003 0.200 1 283 75 75 LYS H H 7.517 0.090 1 284 75 75 LYS N N 118.502 0.100 1 285 75 75 LYS CA C 56.167 0.200 1 286 75 75 LYS CB C 29.979 0.200 1 287 76 76 THR H H 7.355 0.090 1 288 76 76 THR N N 106.995 0.100 1 289 76 76 THR CA C 59.001 0.200 1 290 76 76 THR CB C 66.678 0.200 1 291 77 77 TYR H H 7.530 0.090 1 292 77 77 TYR N N 123.426 0.100 1 293 77 77 TYR CA C 55.833 0.200 1 294 77 77 TYR CB C 36.331 0.200 1 295 78 78 ILE H H 7.799 0.090 1 296 78 78 ILE N N 128.672 0.100 1 297 78 78 ILE CA C 54.933 0.200 1 298 78 78 ILE CB C 36.331 0.200 1 299 80 80 PRO CA C 59.973 0.200 1 300 81 81 LYS H H 8.457 0.090 1 301 81 81 LYS N N 121.633 0.100 1 302 81 81 LYS CA C 54.191 0.200 1 303 81 81 LYS CB C 30.544 0.200 1 304 82 82 GLY H H 8.455 0.090 1 305 82 82 GLY N N 109.688 0.100 1 306 82 82 GLY CA C 42.731 0.200 1 307 83 83 GLU H H 8.347 0.090 1 308 83 83 GLU N N 120.389 0.100 1 309 83 83 GLU CA C 53.923 0.200 1 310 83 83 GLU CB C 27.932 0.200 1 311 84 84 THR H H 8.371 0.090 1 312 84 84 THR N N 116.040 0.100 1 313 84 84 THR CA C 59.652 0.200 1 314 84 84 THR CB C 67.101 0.200 1 315 85 85 LYS H H 8.422 0.090 1 316 85 85 LYS N N 124.122 0.100 1 317 85 85 LYS CA C 53.856 0.200 1 318 85 85 LYS CB C 30.473 0.200 1 319 86 86 LYS H H 8.337 0.090 1 320 86 86 LYS N N 122.784 0.100 1 321 86 86 LYS CA C 53.799 0.200 1 322 86 86 LYS CB C 30.402 0.200 1 323 87 87 LYS H H 8.299 0.090 1 324 87 87 LYS N N 122.530 0.100 1 325 87 87 LYS CA C 53.788 0.200 1 326 87 87 LYS CB C 30.658 0.200 1 327 88 88 PHE H H 8.324 0.090 1 328 88 88 PHE N N 121.888 0.100 1 329 88 88 PHE CA C 55.028 0.200 1 330 88 88 PHE CB C 37.258 0.200 1 331 89 89 LYS H H 8.214 0.090 1 332 89 89 LYS N N 124.457 0.100 1 333 89 89 LYS CA C 53.185 0.200 1 334 89 89 LYS CB C 30.394 0.200 1 335 90 90 ASP H H 8.039 0.090 1 336 90 90 ASP N N 119.104 0.100 1 337 90 90 ASP CA C 56.830 0.200 1 338 92 92 ASN H H 8.372 0.090 1 339 92 92 ASN N N 115.893 0.100 1 340 92 92 ASN CA C 50.224 0.200 1 341 92 92 ASN CB C 36.478 0.200 1 342 93 93 ALA H H 7.319 0.090 1 343 93 93 ALA N N 123.346 0.100 1 344 93 93 ALA CA C 48.030 0.200 1 345 95 95 LYS H H 8.525 0.090 1 346 95 95 LYS N N 123.266 0.100 1 347 95 95 LYS CA C 52.962 0.200 1 348 95 95 LYS CB C 30.725 0.200 1 349 96 96 ARG H H 8.394 0.090 1 350 96 96 ARG N N 123.386 0.100 1 351 96 96 ARG CA C 55.932 0.200 1 352 99 99 SER H H 7.841 0.090 1 353 99 99 SER N N 114.247 0.100 1 354 99 99 SER CA C 53.876 0.200 1 355 99 99 SER CB C 63.311 0.200 1 356 100 100 ALA H H 9.037 0.090 1 357 100 100 ALA N N 122.276 0.100 1 358 100 100 ALA CA C 53.599 0.200 1 359 100 100 ALA CB C 15.967 0.200 1 360 101 101 PHE H H 8.416 0.090 1 361 101 101 PHE N N 115.639 0.100 1 362 101 101 PHE CA C 56.433 0.200 1 363 101 101 PHE CB C 36.205 0.200 1 364 102 102 PHE H H 8.177 0.090 1 365 102 102 PHE N N 122.436 0.100 1 366 102 102 PHE CA C 59.477 0.200 1 367 102 102 PHE CB C 36.059 0.200 1 368 103 103 LEU H H 8.252 0.090 1 369 103 103 LEU N N 120.509 0.100 1 370 103 103 LEU CA C 55.629 0.200 1 371 103 103 LEU CB C 39.493 0.200 1 372 104 104 PHE H H 8.144 0.090 1 373 104 104 PHE N N 123.548 0.100 1 374 104 104 PHE CA C 59.034 0.200 1 375 104 104 PHE CB C 36.644 0.200 1 376 105 105 CYS H H 8.491 0.090 1 377 105 105 CYS N N 117.887 0.100 1 378 105 105 CYS CA C 61.485 0.200 1 379 105 105 CYS CB C 23.931 0.200 1 380 106 106 SER H H 8.113 0.090 1 381 106 106 SER N N 114.595 0.100 1 382 106 106 SER CA C 58.925 0.200 1 383 106 106 SER CB C 59.731 0.200 1 384 107 107 GLU H H 7.114 0.090 1 385 107 107 GLU N N 118.663 0.100 1 386 107 107 GLU CA C 55.501 0.200 1 387 107 107 GLU CB C 27.145 0.200 1 388 108 108 TYR H H 7.900 0.090 1 389 108 108 TYR N N 114.060 0.100 1 390 108 108 TYR CA C 59.319 0.200 1 391 108 108 TYR CB C 36.863 0.200 1 392 109 109 ARG H H 9.229 0.090 1 393 109 109 ARG N N 123.212 0.100 1 394 109 109 ARG CA C 59.924 0.200 1 395 111 111 LYS H H 6.765 0.090 1 396 111 111 LYS N N 117.271 0.100 1 397 111 111 LYS CA C 56.476 0.200 1 398 111 111 LYS CB C 29.849 0.200 1 399 112 112 ILE H H 8.161 0.090 1 400 112 112 ILE N N 119.104 0.100 1 401 112 112 ILE CA C 61.483 0.200 1 402 112 112 ILE CB C 35.182 0.200 1 403 113 113 LYS H H 8.191 0.090 1 404 113 113 LYS N N 118.315 0.100 1 405 113 113 LYS CA C 56.335 0.200 1 406 113 113 LYS CB C 29.203 0.200 1 407 114 114 GLY H H 7.677 0.090 1 408 114 114 GLY N N 103.810 0.100 1 409 114 114 GLY CA C 43.770 0.200 1 410 115 115 GLU H H 7.481 0.090 1 411 115 115 GLU N N 118.074 0.100 1 412 115 115 GLU CA C 54.900 0.200 1 413 115 115 GLU CB C 28.168 0.200 1 414 116 116 HIS H H 7.847 0.090 1 415 116 116 HIS N N 114.836 0.100 1 416 116 116 HIS CA C 50.103 0.200 1 417 116 116 HIS CB C 26.451 0.200 1 418 117 117 PRO CB C 29.259 0.200 1 419 118 118 GLY H H 8.767 0.090 1 420 118 118 GLY N N 107.637 0.100 1 421 118 118 GLY CA C 42.762 0.200 1 422 119 119 LEU H H 7.402 0.090 1 423 119 119 LEU N N 120.643 0.100 1 424 119 119 LEU CA C 52.532 0.200 1 425 119 119 LEU CB C 40.565 0.200 1 426 120 120 SER H H 9.299 0.090 1 427 120 120 SER N N 120.563 0.100 1 428 120 120 SER CA C 54.735 0.200 1 429 120 120 SER CB C 62.443 0.200 1 430 121 121 ILE H H 8.719 0.090 1 431 121 121 ILE N N 120.161 0.100 1 432 121 121 ILE CA C 62.402 0.200 1 433 121 121 ILE CB C 35.548 0.200 1 434 122 122 GLY H H 8.691 0.090 1 435 122 122 GLY N N 108.948 0.100 1 436 122 122 GLY CA C 44.162 0.200 1 437 123 123 ASP H H 7.975 0.090 1 438 123 123 ASP N N 123.838 0.100 1 439 123 123 ASP CA C 54.700 0.200 1 440 123 123 ASP CB C 38.105 0.200 1 441 124 124 VAL H H 8.586 0.090 1 442 124 124 VAL N N 123.132 0.100 1 443 124 124 VAL CA C 64.870 0.200 1 444 124 124 VAL CB C 28.992 0.200 1 445 125 125 ALA H H 7.910 0.090 1 446 125 125 ALA N N 120.750 0.100 1 447 125 125 ALA CA C 53.185 0.200 1 448 125 125 ALA CB C 15.229 0.200 1 449 126 126 LYS H H 8.043 0.090 1 450 126 126 LYS N N 119.278 0.100 1 451 126 126 LYS CA C 57.034 0.200 1 452 126 126 LYS CB C 29.928 0.200 1 453 127 127 LYS H H 8.034 0.090 1 454 127 127 LYS N N 120.775 0.100 1 455 127 127 LYS CA C 56.224 0.200 1 456 127 127 LYS CB C 29.126 0.200 1 457 128 128 LEU H H 8.639 0.090 1 458 128 128 LEU N N 119.653 0.100 1 459 128 128 LEU CA C 56.000 0.200 1 460 128 128 LEU CB C 39.201 0.200 1 461 129 129 GLY H H 8.195 0.090 1 462 129 129 GLY N N 105.335 0.100 1 463 129 129 GLY CA C 45.196 0.200 1 464 130 130 GLU H H 8.043 0.090 1 465 130 130 GLU N N 122.733 0.100 1 466 130 130 GLU CA C 56.788 0.200 1 467 130 130 GLU CB C 27.072 0.200 1 468 131 131 MET H H 8.798 0.090 1 469 131 131 MET N N 118.368 0.100 1 470 131 131 MET CA C 56.767 0.200 1 471 131 131 MET CB C 31.383 0.200 1 472 132 132 TRP H H 8.685 0.090 1 473 132 132 TRP N N 122.088 0.100 1 474 132 132 TRP CA C 57.034 0.200 1 475 132 132 TRP CB C 27.949 0.200 1 476 133 133 ASN H H 8.137 0.090 1 477 133 133 ASN N N 116.709 0.100 1 478 133 133 ASN CA C 52.968 0.200 1 479 133 133 ASN CB C 35.401 0.200 1 480 134 134 ASN H H 7.570 0.090 1 481 134 134 ASN N N 115.318 0.100 1 482 134 134 ASN CA C 50.542 0.200 1 483 134 134 ASN CB C 36.644 0.200 1 484 135 135 THR H H 7.273 0.090 1 485 135 135 THR N N 119.359 0.100 1 486 135 135 THR CA C 61.302 0.200 1 487 135 135 THR CB C 66.254 0.200 1 488 136 136 ALA H H 9.216 0.090 1 489 136 136 ALA N N 130.889 0.100 1 490 136 136 ALA CA C 49.598 0.200 1 491 136 136 ALA CB C 16.488 0.200 1 492 137 137 ALA H H 8.831 0.090 1 493 137 137 ALA N N 124.443 0.100 1 494 137 137 ALA CA C 53.860 0.200 1 495 137 137 ALA CB C 15.652 0.200 1 496 138 138 ASP H H 8.966 0.090 1 497 138 138 ASP N N 115.157 0.100 1 498 138 138 ASP CA C 54.700 0.200 1 499 138 138 ASP CB C 37.319 0.200 1 500 139 139 ASP H H 7.321 0.090 1 501 139 139 ASP N N 117.405 0.100 1 502 139 139 ASP CA C 53.166 0.200 1 503 139 139 ASP CB C 38.942 0.200 1 504 140 140 LYS H H 7.789 0.090 1 505 140 140 LYS N N 118.556 0.100 1 506 140 140 LYS CA C 56.634 0.200 1 507 140 140 LYS CB C 31.237 0.200 1 508 141 141 GLN H H 7.413 0.090 1 509 141 141 GLN N N 117.699 0.100 1 510 141 141 GLN CA C 58.267 0.200 1 511 141 141 GLN CB C 24.442 0.200 1 512 143 143 TYR H H 7.195 0.090 1 513 143 143 TYR N N 115.103 0.100 1 514 143 143 TYR CA C 58.996 0.200 1 515 143 143 TYR CB C 35.837 0.200 1 516 144 144 GLU H H 8.139 0.090 1 517 144 144 GLU N N 119.104 0.100 1 518 144 144 GLU CA C 56.962 0.200 1 519 144 144 GLU CB C 26.852 0.200 1 520 145 145 LYS H H 9.176 0.090 1 521 145 145 LYS N N 120.603 0.100 1 522 145 145 LYS CA C 56.896 0.200 1 523 145 145 LYS CB C 29.908 0.200 1 524 146 146 LYS H H 7.687 0.090 1 525 146 146 LYS N N 120.028 0.100 1 526 146 146 LYS CA C 56.406 0.200 1 527 146 146 LYS CB C 29.767 0.200 1 528 147 147 ALA H H 8.348 0.090 1 529 147 147 ALA N N 120.389 0.100 1 530 147 147 ALA CA C 53.677 0.200 1 531 148 148 ALA H H 8.361 0.090 1 532 148 148 ALA N N 121.580 0.100 1 533 148 148 ALA CA C 52.932 0.200 1 534 148 148 ALA CB C 15.229 0.200 1 535 149 149 LYS H H 7.969 0.090 1 536 149 149 LYS N N 120.295 0.100 1 537 149 149 LYS CA C 56.467 0.200 1 538 149 149 LYS CB C 29.191 0.200 1 539 150 150 LEU H H 8.273 0.090 1 540 150 150 LEU N N 119.599 0.100 1 541 150 150 LEU CA C 55.257 0.200 1 542 150 150 LEU CB C 38.689 0.200 1 543 151 151 LYS H H 8.420 0.090 1 544 151 151 LYS N N 123.150 0.100 1 545 151 151 LYS CA C 57.586 0.200 1 546 151 151 LYS CB C 29.483 0.200 1 547 152 152 GLU H H 8.051 0.090 1 548 152 152 GLU N N 119.533 0.100 1 549 152 152 GLU CA C 56.332 0.200 1 550 152 152 GLU CB C 26.986 0.200 1 551 153 153 LYS H H 7.750 0.090 1 552 153 153 LYS N N 119.252 0.100 1 553 153 153 LYS CA C 56.767 0.200 1 554 153 153 LYS CB C 29.861 0.200 1 555 154 154 TYR H H 8.101 0.090 1 556 154 154 TYR N N 119.961 0.100 1 557 154 154 TYR CA C 58.721 0.200 1 558 154 154 TYR CB C 35.767 0.200 1 559 155 155 GLU H H 8.497 0.090 1 560 155 155 GLU N N 117.068 0.100 1 561 155 155 GLU CA C 56.863 0.200 1 562 155 155 GLU CB C 26.196 0.200 1 563 156 156 LYS H H 7.668 0.090 1 564 156 156 LYS N N 120.026 0.100 1 565 156 156 LYS CA C 56.741 0.200 1 566 156 156 LYS CB C 29.861 0.200 1 567 157 157 ASP H H 8.862 0.090 1 568 157 157 ASP N N 122.971 0.100 1 569 157 157 ASP CA C 54.617 0.200 1 570 158 158 ILE H H 9.156 0.090 1 571 158 158 ILE N N 121.981 0.100 1 572 158 158 ILE CA C 59.585 0.200 1 573 158 158 ILE CB C 34.306 0.200 1 574 159 159 ALA H H 7.342 0.090 1 575 159 159 ALA N N 124.336 0.100 1 576 159 159 ALA CA C 52.499 0.200 1 577 159 159 ALA CB C 15.299 0.200 1 578 160 160 ALA H H 7.759 0.090 1 579 160 160 ALA N N 119.867 0.100 1 580 160 160 ALA CA C 51.965 0.200 1 581 160 160 ALA CB C 15.511 0.200 1 582 161 161 TYR H H 8.148 0.090 1 583 161 161 TYR N N 119.743 0.100 1 584 161 161 TYR CA C 58.319 0.200 1 585 161 161 TYR CB C 36.280 0.200 1 586 162 162 ARG H H 8.280 0.090 1 587 162 162 ARG N N 118.636 0.100 1 588 162 162 ARG CA C 55.322 0.200 1 589 162 162 ARG CB C 27.862 0.200 1 590 163 163 ALA H H 7.613 0.090 1 591 163 163 ALA N N 121.018 0.100 1 592 163 163 ALA CA C 50.773 0.200 1 593 163 163 ALA CB C 16.005 0.200 1 594 164 164 LYS H H 7.655 0.090 1 595 164 164 LYS N N 118.181 0.100 1 596 164 164 LYS CA C 54.599 0.200 1 597 164 164 LYS CB C 29.995 0.200 1 598 165 165 GLY H H 8.096 0.090 1 599 165 165 GLY N N 108.306 0.100 1 600 165 165 GLY CA C 42.597 0.200 1 601 166 166 LYS H H 8.029 0.090 1 602 166 166 LYS N N 121.339 0.100 1 603 166 166 LYS CA C 51.781 0.200 1 604 166 166 LYS CB C 29.849 0.200 1 605 167 167 PRO CA C 60.754 0.200 1 606 167 167 PRO CB C 29.393 0.200 1 607 168 168 ASP H H 8.465 0.090 1 608 168 168 ASP N N 120.188 0.100 1 609 168 168 ASP CA C 51.845 0.200 1 610 168 168 ASP CB C 38.441 0.200 1 611 169 169 ALA H H 8.254 0.090 1 612 169 169 ALA N N 124.524 0.100 1 613 169 169 ALA CA C 50.431 0.200 1 614 169 169 ALA CB C 16.350 0.200 1 615 170 170 ALA H H 8.235 0.090 1 616 170 170 ALA N N 121.954 0.100 1 617 170 170 ALA CA C 50.193 0.200 1 618 170 170 ALA CB C 16.429 0.200 1 619 171 171 LYS H H 8.125 0.090 1 620 171 171 LYS N N 119.947 0.100 1 621 171 171 LYS CA C 53.766 0.200 1 622 171 171 LYS CB C 30.214 0.200 1 623 172 172 LYS H H 8.421 0.090 1 624 172 172 LYS N N 123.774 0.100 1 625 172 172 LYS CA C 53.966 0.200 1 626 172 172 LYS CB C 30.433 0.200 1 627 173 173 GLY H H 8.432 0.090 1 628 173 173 GLY N N 109.831 0.100 1 629 173 173 GLY CA C 42.698 0.200 1 630 174 174 VAL H H 8.008 0.090 1 631 174 174 VAL N N 119.626 0.100 1 632 174 174 VAL CA C 59.868 0.200 1 633 174 174 VAL CB C 30.049 0.200 1 634 175 175 VAL H H 8.326 0.090 1 635 175 175 VAL N N 125.059 0.100 1 636 175 175 VAL CA C 59.768 0.200 1 637 175 175 VAL CB C 30.191 0.200 1 638 176 176 LYS H H 8.477 0.090 1 639 176 176 LYS N N 126.210 0.100 1 640 176 176 LYS CA C 53.632 0.200 1 641 176 176 LYS CB C 30.402 0.200 1 642 177 177 ALA H H 8.399 0.090 1 643 177 177 ALA N N 125.888 0.100 1 644 177 177 ALA CA C 49.864 0.200 1 645 177 177 ALA CB C 16.640 0.200 1 646 178 178 GLU H H 8.458 0.090 1 647 178 178 GLU N N 120.817 0.100 1 648 178 178 GLU CA C 53.895 0.200 1 649 178 178 GLU CB C 27.887 0.200 1 650 179 179 LYS H H 8.456 0.090 1 651 179 179 LYS N N 122.530 0.100 1 652 179 179 LYS CA C 53.909 0.200 1 653 179 179 LYS CB C 30.262 0.200 1 654 180 180 SER H H 8.341 0.090 1 655 180 180 SER N N 116.468 0.100 1 656 180 180 SER CA C 55.834 0.200 1 657 180 180 SER CB C 61.215 0.200 1 658 181 181 LYS H H 8.387 0.090 1 659 181 181 LYS N N 123.389 0.100 1 660 181 181 LYS CA C 53.590 0.200 1 661 181 181 LYS CB C 30.096 0.200 1 662 182 182 LYS H H 8.341 0.090 1 663 182 182 LYS N N 116.468 0.100 1 664 182 182 LYS CA C 53.730 0.200 1 665 182 182 LYS CB C 30.166 0.200 1 666 183 183 LYS H H 8.390 0.090 1 667 183 183 LYS N N 123.583 0.100 1 668 183 183 LYS CB C 31.983 0.200 1 669 184 184 LYS H H 8.299 0.090 1 670 184 184 LYS N N 122.460 0.100 1 671 184 184 LYS CA C 51.977 0.200 1 672 184 184 LYS CB C 30.166 0.200 1 673 185 185 GLU H H 8.292 0.090 1 674 185 185 GLU N N 122.316 0.100 1 675 185 185 GLU CA C 53.730 0.200 1 676 185 185 GLU CB C 30.376 0.200 1 677 186 186 GLU H H 8.289 0.090 1 678 186 186 GLU N N 121.888 0.100 1 679 186 186 GLU CA C 53.923 0.200 1 680 186 186 GLU CB C 30.287 0.200 1 681 187 187 GLU H H 8.070 0.090 1 682 187 187 GLU N N 127.655 0.100 1 683 187 187 GLU CA C 55.403 0.200 1 684 187 187 GLU CB C 28.298 0.200 1 stop_ save_