data_5340 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure for BID, and Intracellular Amplifier of Apoptotic Signaling ; _BMRB_accession_number 5340 _BMRB_flat_file_name bmr5340.str _Entry_type original _Submission_date 2002-04-08 _Accession_date 2002-04-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chou James J . 2 Li Honglin . . 3 Salvesen Guy S . 4 Yuan Junying . . 5 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 178 "13C chemical shifts" 524 "15N chemical shifts" 178 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-07 original author . stop_ _Original_release_date 2002-06-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure for BID, and Intracellular Amplifier of Apoptotic Signaling' _Citation_status submitted _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chou James J . 2 Li Honglin . . 3 Salvesen Guy S . 4 Yuan Junying . . 5 Wagner Gerhard . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 1999 Mar 5;96(5):615-24. ; _Citation_title 'Solution structure of BID, an intracellular amplifier of apoptotic signaling.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10089877 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chou 'J. J.' J. . 2 Li H. . . 3 Salvesen 'G. S.' S. . 4 Yuan J. . . 5 Wagner G. . . stop_ _Journal_abbreviation Cell _Journal_name_full Cell _Journal_volume 96 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 615 _Page_last 624 _Year 1999 _Details ; We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 1998 Aug 21;94(4):491-501. ; _Citation_title 'Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9727492 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li H. . . 2 Zhu H. . . 3 Xu 'C. J.' J. . 4 Yuan J. . . stop_ _Journal_abbreviation Cell _Journal_name_full Cell _Journal_volume 94 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 491 _Page_last 501 _Year 1998 _Details ; We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8. ; save_ ################################## # Molecular system description # ################################## save_system_bid _Saveframe_category molecular_system _Mol_system_name 'proapoptotic bid' _Abbreviation_common bid _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'bid monomer' $bid stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'an intracellular amplifier of apoptotic signaling' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bid _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common bid _Abbreviation_common bid _Molecular_mass 22139 _Mol_thiol_state 'all free' _Details ; The protein was overexpressed as a GST-fusion protein. So there are additional two N-terminal residues GS. ; ############################## # Polymer residue sequence # ############################## _Residue_count 197 _Mol_residue_sequence ; GSMDCEVNNGSSLRDECITN LLVFGFLQSCSDNSFRRELD ALGHELPVLAPQWEGYDELQ TDGNRSSHSRLGRIEADSES QEDIIRNIARHLAQVGDSMD RSIPPGLVNGLALQLRNTSR SEEDRNRDLATALEQLLQAY PRDMEKEKTMLVLALLLAKK VASHTPSLLRDVFHTTVNFI NQNLRTYVRSLARNGMD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 MET 4 ASP 5 CYS 6 GLU 7 VAL 8 ASN 9 ASN 10 GLY 11 SER 12 SER 13 LEU 14 ARG 15 ASP 16 GLU 17 CYS 18 ILE 19 THR 20 ASN 21 LEU 22 LEU 23 VAL 24 PHE 25 GLY 26 PHE 27 LEU 28 GLN 29 SER 30 CYS 31 SER 32 ASP 33 ASN 34 SER 35 PHE 36 ARG 37 ARG 38 GLU 39 LEU 40 ASP 41 ALA 42 LEU 43 GLY 44 HIS 45 GLU 46 LEU 47 PRO 48 VAL 49 LEU 50 ALA 51 PRO 52 GLN 53 TRP 54 GLU 55 GLY 56 TYR 57 ASP 58 GLU 59 LEU 60 GLN 61 THR 62 ASP 63 GLY 64 ASN 65 ARG 66 SER 67 SER 68 HIS 69 SER 70 ARG 71 LEU 72 GLY 73 ARG 74 ILE 75 GLU 76 ALA 77 ASP 78 SER 79 GLU 80 SER 81 GLN 82 GLU 83 ASP 84 ILE 85 ILE 86 ARG 87 ASN 88 ILE 89 ALA 90 ARG 91 HIS 92 LEU 93 ALA 94 GLN 95 VAL 96 GLY 97 ASP 98 SER 99 MET 100 ASP 101 ARG 102 SER 103 ILE 104 PRO 105 PRO 106 GLY 107 LEU 108 VAL 109 ASN 110 GLY 111 LEU 112 ALA 113 LEU 114 GLN 115 LEU 116 ARG 117 ASN 118 THR 119 SER 120 ARG 121 SER 122 GLU 123 GLU 124 ASP 125 ARG 126 ASN 127 ARG 128 ASP 129 LEU 130 ALA 131 THR 132 ALA 133 LEU 134 GLU 135 GLN 136 LEU 137 LEU 138 GLN 139 ALA 140 TYR 141 PRO 142 ARG 143 ASP 144 MET 145 GLU 146 LYS 147 GLU 148 LYS 149 THR 150 MET 151 LEU 152 VAL 153 LEU 154 ALA 155 LEU 156 LEU 157 LEU 158 ALA 159 LYS 160 LYS 161 VAL 162 ALA 163 SER 164 HIS 165 THR 166 PRO 167 SER 168 LEU 169 LEU 170 ARG 171 ASP 172 VAL 173 PHE 174 HIS 175 THR 176 THR 177 VAL 178 ASN 179 PHE 180 ILE 181 ASN 182 GLN 183 ASN 184 LEU 185 ARG 186 THR 187 TYR 188 VAL 189 ARG 190 SER 191 LEU 192 ALA 193 ARG 194 ASN 195 GLY 196 MET 197 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 19054 entity 68.53 135 100.00 100.00 4.28e-90 PDB 2BID "Human Pro-Apoptotic Protein Bid" 100.00 197 100.00 100.00 8.23e-141 PDB 2M5I "Nmr Structures Of Human Apoptotic Protein Tbid In Lppg Micelle" 68.53 135 100.00 100.00 4.28e-90 DBJ BAF79673 "desmocollin type 4 [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 DBJ BAG10922 "BH3-interacting domain death agonist [synthetic construct]" 99.49 241 99.49 100.00 1.13e-138 DBJ BAG36471 "unnamed protein product [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 DBJ BAG52933 "unnamed protein product [Homo sapiens]" 99.49 241 98.98 100.00 6.61e-138 EMBL CAG28531 "BID [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 EMBL CAG30275 "BID [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 EMBL CAH92211 "hypothetical protein [Pongo abelii]" 50.25 99 97.98 98.99 5.30e-61 EMBL CAK54378 "BID [synthetic construct]" 98.98 195 100.00 100.00 3.30e-139 EMBL CAK54677 "BID [synthetic construct]" 98.98 195 100.00 100.00 3.30e-139 GB AAC34365 "BH3 interacting domain death agonist [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 GB AAH09197 "BID protein [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 GB AAH22072 "BID protein, partial [Homo sapiens]" 99.49 252 99.49 100.00 5.05e-138 GB AAH33634 "BH3 interacting domain death agonist [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 GB AAH36364 "BH3 interacting domain death agonist [Homo sapiens]" 99.49 241 98.98 99.49 1.33e-137 REF NP_001126293 "BH3-interacting domain death agonist [Pongo abelii]" 50.25 99 97.98 98.99 5.30e-61 REF NP_001187 "BH3-interacting domain death agonist isoform 2 [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 REF NP_001231496 "BH3-interacting domain death agonist isoform 2 [Homo sapiens]" 98.98 195 100.00 100.00 3.30e-139 REF NP_001231498 "BH3-interacting domain death agonist isoform 3 [Homo sapiens]" 50.25 99 100.00 100.00 1.41e-62 REF NP_001231499 "BH3-interacting domain death agonist isoform 3 [Homo sapiens]" 50.25 99 100.00 100.00 1.41e-62 SP P55957 "RecName: Full=BH3-interacting domain death agonist; AltName: Full=p22 BID; Short=BID; Contains: RecName: Full=BH3-interacting d" 98.98 195 100.00 100.00 3.30e-139 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _ATCC_number _Fraction $bid Human 9606 Eukaryota Metazoa Homo sapien 52055 cytoplasm 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 _Details $bid 'recombinant technology' . . . . . 'GST-fusion, pGEX-2T vector' 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 $bid 1.0 mM 0.7 1.2 '[U-95% 13C; U-95% 15N; U-85% 2H]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_13C_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HCCH-TOCSY' _Sample_label $sample_1 save_ save_13C-edited_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label $sample_1 save_ save_15N-edited_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label $sample_1 save_ save_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-13C_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Experimental_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.3 n/a temperature 298 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Experimental_Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'bid monomer' _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 . 3 MET H H 8.58 . . 2 . 3 MET C C 175.85 . . 3 . 3 MET CA C 56.41 . . 4 . 3 MET CB C 32.73 . . 5 . 3 MET N N 121.13 . . 6 . 4 ASP H H 8.19 . . 7 . 4 ASP C C 175.88 . . 8 . 4 ASP CA C 55.45 . . 9 . 4 ASP CB C 41.66 . . 10 . 4 ASP N N 120.69 . . 11 . 9 ASN H H 8.32 . . 12 . 9 ASN C C 175.65 . . 13 . 9 ASN CA C 54.30 . . 14 . 9 ASN CB C 39.43 . . 15 . 9 ASN N N 118.74 . . 16 . 10 GLY H H 8.37 . . 17 . 10 GLY C C 174.22 . . 18 . 10 GLY CA C 46.45 . . 19 . 10 GLY N N 108.62 . . 20 . 11 SER H H 8.21 . . 21 . 11 SER C C 174.68 . . 22 . 11 SER CA C 59.54 . . 23 . 11 SER CB C 64.71 . . 24 . 11 SER N N 115.51 . . 25 . 12 SER H H 8.47 . . 26 . 12 SER C C 175.10 . . 27 . 12 SER CA C 59.69 . . 28 . 12 SER CB C 64.71 . . 29 . 12 SER N N 118.32 . . 30 . 13 LEU H H 8.23 . . 31 . 13 LEU C C 178.33 . . 32 . 13 LEU CA C 57.34 . . 33 . 13 LEU CB C 42.06 . . 34 . 13 LEU N N 123.39 . . 35 . 14 ARG H H 8.17 . . 36 . 14 ARG C C 178.34 . . 37 . 14 ARG CA C 59.21 . . 38 . 14 ARG CB C 42.14 . . 39 . 14 ARG N N 120.81 . . 40 . 15 ASP H H 8.17 . . 41 . 15 ASP C C 178.38 . . 42 . 15 ASP CA C 58.25 . . 43 . 15 ASP CB C 40.95 . . 44 . 15 ASP N N 119.49 . . 45 . 16 GLU H H 8.45 . . 46 . 16 GLU C C 178.57 . . 47 . 16 GLU CA C 60.20 . . 48 . 16 GLU CB C 29.62 . . 49 . 16 GLU N N 119.16 . . 50 . 17 CYS H H 8.03 . . 51 . 17 CYS C C 176.49 . . 52 . 17 CYS CA C 63.35 . . 53 . 17 CYS CB C 27.71 . . 54 . 17 CYS N N 119.24 . . 55 . 18 ILE H H 8.11 . . 56 . 18 ILE C C 177.14 . . 57 . 18 ILE CA C 65.88 . . 58 . 18 ILE CB C 37.44 . . 59 . 18 ILE N N 118.70 . . 60 . 19 THR H H 8.04 . . 61 . 19 THR N N 115.87 . . 62 . 21 LEU H H 8.01 . . 63 . 21 LEU C C 179.71 . . 64 . 21 LEU CA C 58.70 . . 65 . 21 LEU CB C 41.98 . . 66 . 21 LEU N N 117.67 . . 67 . 22 LEU H H 8.63 . . 68 . 22 LEU C C 177.51 . . 69 . 22 LEU CA C 59.23 . . 70 . 22 LEU CB C 42.54 . . 71 . 22 LEU N N 123.03 . . 72 . 23 VAL H H 8.27 . . 73 . 23 VAL C C 177.79 . . 74 . 23 VAL CA C 66.89 . . 75 . 23 VAL CB C 30.98 . . 76 . 23 VAL N N 117.23 . . 77 . 24 PHE H H 8.77 . . 78 . 24 PHE C C 176.88 . . 79 . 24 PHE CA C 63.71 . . 80 . 24 PHE CB C 41.11 . . 81 . 24 PHE N N 119.01 . . 82 . 25 GLY H H 8.94 . . 83 . 25 GLY C C 176.54 . . 84 . 25 GLY CA C 47.57 . . 85 . 25 GLY N N 105.02 . . 86 . 26 PHE H H 8.61 . . 87 . 26 PHE C C 176.93 . . 88 . 26 PHE CA C 62.49 . . 89 . 26 PHE CB C 40.23 . . 90 . 26 PHE N N 124.42 . . 91 . 27 LEU H H 8.17 . . 92 . 27 LEU C C 178.63 . . 93 . 27 LEU CA C 58.36 . . 94 . 27 LEU CB C 41.98 . . 95 . 27 LEU N N 119.31 . . 96 . 28 GLN H H 8.50 . . 97 . 28 GLN C C 177.74 . . 98 . 28 GLN CA C 59.01 . . 99 . 28 GLN CB C 29.54 . . 100 . 28 GLN N N 116.90 . . 101 . 29 SER H H 7.54 . . 102 . 29 SER C C 173.83 . . 103 . 29 SER CA C 61.05 . . 104 . 29 SER CB C 64.87 . . 105 . 29 SER N N 112.99 . . 106 . 30 CYS H H 7.19 . . 107 . 30 CYS C C 173.74 . . 108 . 30 CYS CA C 59.46 . . 109 . 30 CYS CB C 28.27 . . 110 . 30 CYS N N 117.74 . . 111 . 31 SER H H 8.13 . . 112 . 31 SER C C 173.46 . . 113 . 31 SER CA C 59.73 . . 114 . 31 SER CB C 64.15 . . 115 . 31 SER N N 116.43 . . 116 . 32 ASP H H 7.34 . . 117 . 32 ASP C C 175.49 . . 118 . 32 ASP CA C 54.27 . . 119 . 32 ASP CB C 42.70 . . 120 . 32 ASP N N 120.46 . . 121 . 33 ASN H H 8.51 . . 122 . 33 ASN C C 176.75 . . 123 . 33 ASN CA C 54.83 . . 124 . 33 ASN CB C 39.19 . . 125 . 33 ASN N N 120.81 . . 126 . 34 SER H H 8.69 . . 127 . 34 SER C C 174.66 . . 128 . 34 SER CA C 62.15 . . 129 . 34 SER CB C 64.31 . . 130 . 34 SER N N 117.13 . . 131 . 35 PHE H H 7.18 . . 132 . 35 PHE C C 174.92 . . 133 . 35 PHE CA C 56.33 . . 134 . 35 PHE CB C 38.32 . . 135 . 35 PHE N N 115.13 . . 136 . 36 ARG H H 7.15 . . 137 . 36 ARG C C 177.51 . . 138 . 36 ARG CA C 60.13 . . 139 . 36 ARG CB C 30.22 . . 140 . 36 ARG N N 122.30 . . 141 . 37 ARG H H 8.67 . . 142 . 37 ARG C C 179.44 . . 143 . 37 ARG CA C 60.20 . . 144 . 37 ARG CB C 29.73 . . 145 . 37 ARG N N 118.79 . . 146 . 38 GLU H H 8.97 . . 147 . 38 GLU C C 179.13 . . 148 . 38 GLU CA C 61.16 . . 149 . 38 GLU CB C 28.61 . . 150 . 38 GLU N N 121.74 . . 151 . 39 LEU H H 8.60 . . 152 . 39 LEU C C 177.91 . . 153 . 39 LEU CA C 58.55 . . 154 . 39 LEU CB C 42.65 . . 155 . 39 LEU N N 123.14 . . 156 . 40 ASP H H 8.50 . . 157 . 40 ASP C C 179.15 . . 158 . 40 ASP CA C 57.90 . . 159 . 40 ASP CB C 40.73 . . 160 . 40 ASP N N 119.42 . . 161 . 41 ALA H H 7.59 . . 162 . 41 ALA C C 180.29 . . 163 . 41 ALA CA C 55.83 . . 164 . 41 ALA CB C 18.26 . . 165 . 41 ALA N N 120.88 . . 166 . 42 LEU H H 7.90 . . 167 . 42 LEU C C 178.75 . . 168 . 42 LEU CA C 58.32 . . 169 . 42 LEU CB C 42.17 . . 170 . 42 LEU N N 120.99 . . 171 . 43 GLY H H 8.33 . . 172 . 43 GLY C C 175.08 . . 173 . 43 GLY CA C 48.30 . . 174 . 43 GLY N N 104.07 . . 175 . 44 HIS H H 7.28 . . 176 . 44 HIS C C 175.24 . . 177 . 44 HIS CA C 57.98 . . 178 . 44 HIS CB C 29.65 . . 179 . 44 HIS N N 115.11 . . 180 . 45 GLU H H 7.87 . . 181 . 45 GLU C C 176.27 . . 182 . 45 GLU CA C 56.87 . . 183 . 45 GLU CB C 31.02 . . 184 . 45 GLU N N 117.28 . . 185 . 46 LEU H H 7.05 . . 186 . 46 LEU C C 174.90 . . 187 . 46 LEU CA C 53.95 . . 188 . 46 LEU CB C 41.45 . . 189 . 46 LEU N N 120.32 . . 190 . 48 VAL H H 7.76 . . 191 . 48 VAL C C 175.38 . . 192 . 48 VAL CA C 62.39 . . 193 . 48 VAL CB C 32.94 . . 194 . 48 VAL N N 115.64 . . 195 . 49 LEU H H 8.04 . . 196 . 49 LEU C C 176.00 . . 197 . 49 LEU CA C 55.48 . . 198 . 49 LEU CB C 42.09 . . 199 . 49 LEU N N 122.95 . . 200 . 50 ALA H H 7.89 . . 201 . 50 ALA C C 175.24 . . 202 . 50 ALA CA C 51.84 . . 203 . 50 ALA CB C 18.26 . . 204 . 50 ALA N N 125.90 . . 205 . 53 TRP H H 8.00 . . 206 . 53 TRP C C 175.96 . . 207 . 53 TRP CA C 57.86 . . 208 . 53 TRP CB C 30.46 . . 209 . 53 TRP N N 121.17 . . 210 . 54 GLU H H 8.30 . . 211 . 54 GLU C C 176.27 . . 212 . 54 GLU CA C 57.59 . . 213 . 54 GLU CB C 30.54 . . 214 . 54 GLU N N 122.55 . . 215 . 55 GLY H H 7.69 . . 216 . 55 GLY C C 173.53 . . 217 . 55 GLY CA C 45.86 . . 218 . 55 GLY N N 108.58 . . 219 . 56 TYR H H 7.88 . . 220 . 56 TYR C C 175.28 . . 221 . 56 TYR CA C 58.98 . . 222 . 56 TYR CB C 39.44 . . 223 . 56 TYR N N 119.42 . . 224 . 57 ASP H H 8.25 . . 225 . 57 ASP C C 175.93 . . 226 . 57 ASP CA C 55.14 . . 227 . 57 ASP CB C 42.01 . . 228 . 57 ASP N N 121.58 . . 229 . 58 GLU H H 8.29 . . 230 . 58 GLU C C 176.32 . . 231 . 58 GLU CA C 57.71 . . 232 . 58 GLU CB C 30.38 . . 233 . 58 GLU N N 120.94 . . 234 . 59 LEU H H 8.17 . . 235 . 59 LEU C C 176.32 . . 236 . 59 LEU CA C 56.16 . . 237 . 59 LEU CB C 42.17 . . 238 . 59 LEU N N 121.15 . . 239 . 60 GLN H H 8.15 . . 240 . 60 GLN C C 176.10 . . 241 . 60 GLN CA C 56.44 . . 242 . 60 GLN CB C 29.57 . . 243 . 60 GLN N N 119.93 . . 244 . 61 THR H H 8.15 . . 245 . 61 THR C C 174.29 . . 246 . 61 THR CA C 62.77 . . 247 . 61 THR CB C 70.58 . . 248 . 61 THR N N 114.15 . . 249 . 62 ASP H H 8.31 . . 250 . 62 ASP C C 174.29 . . 251 . 62 ASP CA C 55.25 . . 252 . 62 ASP CB C 41.66 . . 253 . 62 ASP N N 121.46 . . 254 . 63 GLY H H 8.32 . . 255 . 63 GLY C C 174.03 . . 256 . 63 GLY CA C 46.37 . . 257 . 63 GLY N N 108.61 . . 258 . 64 ASN H H 8.26 . . 259 . 64 ASN C C 175.18 . . 260 . 64 ASN CA C 54.22 . . 261 . 64 ASN CB C 39.43 . . 262 . 64 ASN N N 118.31 . . 263 . 65 ARG H H 8.22 . . 264 . 65 ARG C C 176.32 . . 265 . 65 ARG CA C 57.22 . . 266 . 65 ARG CB C 30.82 . . 267 . 65 ARG N N 120.66 . . 268 . 66 SER H H 8.35 . . 269 . 66 SER C C 174.61 . . 270 . 66 SER CA C 59.47 . . 271 . 66 SER CB C 64.71 . . 272 . 66 SER N N 116.01 . . 273 . 71 LEU H H 8.19 . . 274 . 71 LEU C C 177.51 . . 275 . 71 LEU CA C 56.14 . . 276 . 71 LEU CB C 42.22 . . 277 . 71 LEU N N 121.78 . . 278 . 72 GLY H H 8.32 . . 279 . 72 GLY C C 173.53 . . 280 . 72 GLY CA C 46.57 . . 281 . 72 GLY N N 108.97 . . 282 . 73 ARG H H 8.01 . . 283 . 73 ARG C C 175.94 . . 284 . 73 ARG CA C 56.66 . . 285 . 73 ARG CB C 31.06 . . 286 . 73 ARG N N 120.05 . . 287 . 74 ILE H H 8.27 . . 288 . 74 ILE C C 176.13 . . 289 . 74 ILE CA C 61.93 . . 290 . 74 ILE CB C 38.79 . . 291 . 74 ILE N N 121.99 . . 292 . 75 GLU H H 8.50 . . 293 . 75 GLU C C 175.99 . . 294 . 75 GLU CA C 57.34 . . 295 . 75 GLU CB C 30.26 . . 296 . 75 GLU N N 124.08 . . 297 . 76 ALA H H 8.26 . . 298 . 76 ALA C C 177.25 . . 299 . 76 ALA CA C 53.55 . . 300 . 76 ALA CB C 19.74 . . 301 . 76 ALA N N 123.92 . . 302 . 77 ASP H H 8.27 . . 303 . 77 ASP C C 176.11 . . 304 . 77 ASP CA C 55.37 . . 305 . 77 ASP CB C 41.42 . . 306 . 77 ASP N N 118.65 . . 307 . 78 SER H H 8.09 . . 308 . 78 SER C C 174.27 . . 309 . 78 SER CA C 59.69 . . 310 . 78 SER CB C 64.95 . . 311 . 78 SER N N 115.09 . . 312 . 79 GLU H H 8.37 . . 313 . 79 GLU C C 176.38 . . 314 . 79 GLU CA C 57.60 . . 315 . 79 GLU CB C 30.74 . . 316 . 79 GLU N N 122.09 . . 317 . 80 SER H H 8.71 . . 318 . 80 SER C C 175.21 . . 319 . 80 SER CA C 58.85 . . 320 . 80 SER CB C 65.43 . . 321 . 80 SER N N 117.56 . . 322 . 81 GLN H H 8.76 . . 323 . 81 GLN C C 177.90 . . 324 . 81 GLN CA C 59.35 . . 325 . 81 GLN CB C 29.46 . . 326 . 81 GLN N N 121.76 . . 327 . 82 GLU H H 8.98 . . 328 . 82 GLU C C 178.22 . . 329 . 82 GLU CA C 60.98 . . 330 . 82 GLU CB C 29.30 . . 331 . 82 GLU N N 118.65 . . 332 . 83 ASP H H 7.91 . . 333 . 83 ASP C C 178.15 . . 334 . 83 ASP CA C 60.97 . . 335 . 83 ASP CB C 41.19 . . 336 . 83 ASP N N 120.60 . . 337 . 84 ILE H H 7.97 . . 338 . 84 ILE C C 178.73 . . 339 . 84 ILE CA C 65.55 . . 340 . 84 ILE CB C 38.40 . . 341 . 84 ILE N N 121.16 . . 342 . 85 ILE H H 8.05 . . 343 . 85 ILE C C 177.19 . . 344 . 85 ILE CA C 64.28 . . 345 . 85 ILE CB C 36.80 . . 346 . 85 ILE N N 118.80 . . 347 . 86 ARG H H 8.14 . . 348 . 86 ARG C C 178.73 . . 349 . 86 ARG CA C 60.60 . . 350 . 86 ARG CB C 29.94 . . 351 . 86 ARG N N 119.95 . . 352 . 87 ASN H H 8.12 . . 353 . 87 ASN C C 178.56 . . 354 . 87 ASN CA C 57.11 . . 355 . 87 ASN CB C 38.63 . . 356 . 87 ASN N N 117.93 . . 357 . 88 ILE H H 8.40 . . 358 . 88 ILE C C 177.72 . . 359 . 88 ILE CA C 65.45 . . 360 . 88 ILE CB C 38.40 . . 361 . 88 ILE N N 122.73 . . 362 . 89 ALA H H 8.81 . . 363 . 89 ALA C C 178.84 . . 364 . 89 ALA CA C 56.81 . . 365 . 89 ALA CB C 18.14 . . 366 . 89 ALA N N 122.46 . . 367 . 90 ARG H H 7.97 . . 368 . 90 ARG C C 179.11 . . 369 . 90 ARG CA C 60.11 . . 370 . 90 ARG CB C 30.50 . . 371 . 90 ARG N N 115.98 . . 372 . 91 HIS H H 7.90 . . 373 . 91 HIS C C 177.79 . . 374 . 91 HIS CA C 60.07 . . 375 . 91 HIS CB C 29.46 . . 376 . 91 HIS N N 119.88 . . 377 . 92 LEU H H 8.97 . . 378 . 92 LEU C C 178.88 . . 379 . 92 LEU CA C 58.40 . . 380 . 92 LEU CB C 41.19 . . 381 . 92 LEU N N 118.18 . . 382 . 93 ALA H H 8.34 . . 383 . 93 ALA C C 179.32 . . 384 . 93 ALA CA C 55.86 . . 385 . 93 ALA CB C 17.82 . . 386 . 93 ALA N N 121.96 . . 387 . 94 GLN H H 7.57 . . 388 . 94 GLN C C 179.32 . . 389 . 94 GLN CA C 59.58 . . 390 . 94 GLN CB C 28.35 . . 391 . 94 GLN N N 119.08 . . 392 . 95 VAL H H 8.06 . . 393 . 95 VAL C C 179.57 . . 394 . 95 VAL CA C 66.21 . . 395 . 95 VAL CB C 31.86 . . 396 . 95 VAL N N 120.77 . . 397 . 96 GLY H H 9.03 . . 398 . 96 GLY C C 174.93 . . 399 . 96 GLY CA C 48.24 . . 400 . 96 GLY N N 108.56 . . 401 . 97 ASP H H 7.93 . . 402 . 97 ASP C C 178.43 . . 403 . 97 ASP CA C 58.44 . . 404 . 97 ASP CB C 41.27 . . 405 . 97 ASP N N 121.18 . . 406 . 98 SER H H 7.72 . . 407 . 98 SER C C 175.09 . . 408 . 98 SER CA C 61.47 . . 409 . 98 SER CB C 64.39 . . 410 . 98 SER N N 113.13 . . 411 . 99 MET H H 7.61 . . 412 . 99 MET C C 176.89 . . 413 . 99 MET CA C 57.26 . . 414 . 99 MET CB C 35.05 . . 415 . 99 MET N N 119.82 . . 416 . 100 ASP H H 7.64 . . 417 . 100 ASP C C 177.25 . . 418 . 100 ASP CA C 59.34 . . 419 . 100 ASP CB C 43.74 . . 420 . 100 ASP N N 122.07 . . 421 . 101 ARG H H 8.30 . . 422 . 101 ARG C C 176.80 . . 423 . 101 ARG CA C 58.06 . . 424 . 101 ARG CB C 29.70 . . 425 . 101 ARG N N 114.09 . . 426 . 102 SER H H 7.92 . . 427 . 102 SER C C 173.42 . . 428 . 102 SER CA C 60.03 . . 429 . 102 SER CB C 64.71 . . 430 . 102 SER N N 114.10 . . 431 . 103 ILE H H 7.26 . . 432 . 103 ILE C C 173.44 . . 433 . 103 ILE CA C 58.88 . . 434 . 103 ILE CB C 37.76 . . 435 . 103 ILE N N 122.11 . . 436 . 107 LEU H H 7.09 . . 437 . 107 LEU C C 178.91 . . 438 . 107 LEU CA C 58.25 . . 439 . 107 LEU CB C 42.62 . . 440 . 107 LEU N N 123.20 . . 441 . 108 VAL H H 6.96 . . 442 . 108 VAL C C 176.38 . . 443 . 108 VAL CA C 66.84 . . 444 . 108 VAL CB C 31.94 . . 445 . 108 VAL N N 119.43 . . 446 . 109 ASN H H 8.29 . . 447 . 109 ASN C C 176.98 . . 448 . 109 ASN CA C 57.17 . . 449 . 109 ASN CB C 39.43 . . 450 . 109 ASN N N 116.01 . . 451 . 110 GLY H H 7.87 . . 452 . 110 GLY C C 175.85 . . 453 . 110 GLY CA C 47.73 . . 454 . 110 GLY N N 104.21 . . 455 . 111 LEU H H 7.71 . . 456 . 111 LEU C C 178.26 . . 457 . 111 LEU CA C 57.94 . . 458 . 111 LEU CB C 42.14 . . 459 . 111 LEU N N 122.74 . . 460 . 112 ALA H H 8.32 . . 461 . 112 ALA C C 179.12 . . 462 . 112 ALA CA C 56.09 . . 463 . 112 ALA CB C 18.30 . . 464 . 112 ALA N N 120.70 . . 465 . 113 LEU H H 7.67 . . 466 . 113 LEU C C 180.20 . . 467 . 113 LEU CA C 58.67 . . 468 . 113 LEU CB C 41.66 . . 469 . 113 LEU N N 115.51 . . 470 . 114 GLN H H 7.67 . . 471 . 114 GLN C C 179.26 . . 472 . 114 GLN CA C 59.01 . . 473 . 114 GLN CB C 28.99 . . 474 . 114 GLN N N 118.42 . . 475 . 115 LEU H H 8.24 . . 476 . 115 LEU C C 177.35 . . 477 . 115 LEU CA C 57.64 . . 478 . 115 LEU CB C 42.62 . . 479 . 115 LEU N N 118.01 . . 480 . 116 ARG H H 7.55 . . 481 . 116 ARG C C 175.97 . . 482 . 116 ARG CA C 57.49 . . 483 . 116 ARG CB C 31.06 . . 484 . 116 ARG N N 115.38 . . 485 . 117 ASN H H 7.30 . . 486 . 117 ASN C C 176.27 . . 487 . 117 ASN CA C 53.85 . . 488 . 117 ASN CB C 38.56 . . 489 . 117 ASN N N 116.61 . . 490 . 118 THR H H 8.31 . . 491 . 118 THR C C 177.39 . . 492 . 118 THR CA C 64.05 . . 493 . 118 THR CB C 69.73 . . 494 . 118 THR N N 117.27 . . 495 . 119 SER H H 8.29 . . 496 . 119 SER C C 173.90 . . 497 . 119 SER CA C 59.65 . . 498 . 119 SER CB C 64.31 . . 499 . 119 SER N N 116.43 . . 500 . 120 ARG H H 7.42 . . 501 . 120 ARG C C 175.65 . . 502 . 120 ARG CA C 56.31 . . 503 . 120 ARG CB C 31.14 . . 504 . 120 ARG N N 122.59 . . 505 . 121 SER H H 9.25 . . 506 . 121 SER C C 174.47 . . 507 . 121 SER CA C 58.21 . . 508 . 121 SER CB C 66.62 . . 509 . 121 SER N N 120.68 . . 510 . 122 GLU H H 8.94 . . 511 . 122 GLU C C 178.43 . . 512 . 122 GLU CA C 60.60 . . 513 . 122 GLU CB C 29.62 . . 514 . 122 GLU N N 121.36 . . 515 . 123 GLU H H 8.50 . . 516 . 123 GLU C C 178.98 . . 517 . 123 GLU CA C 60.26 . . 518 . 123 GLU CB C 29.54 . . 519 . 123 GLU N N 118.30 . . 520 . 124 ASP H H 7.85 . . 521 . 124 ASP C C 177.55 . . 522 . 124 ASP CA C 58.29 . . 523 . 124 ASP CB C 40.47 . . 524 . 124 ASP N N 121.19 . . 525 . 125 ARG H H 8.16 . . 526 . 125 ARG C C 178.61 . . 527 . 125 ARG CA C 60.26 . . 528 . 125 ARG CB C 41.58 . . 529 . 125 ARG N N 119.10 . . 530 . 126 ASN H H 8.23 . . 531 . 126 ASN C C 177.58 . . 532 . 126 ASN CA C 57.22 . . 533 . 126 ASN CB C 38.95 . . 534 . 126 ASN N N 117.18 . . 535 . 127 ARG H H 7.87 . . 536 . 127 ARG C C 178.91 . . 537 . 127 ARG CA C 59.84 . . 538 . 127 ARG CB C 29.94 . . 539 . 127 ARG N N 120.78 . . 540 . 128 ASP H H 8.61 . . 541 . 128 ASP C C 179.21 . . 542 . 128 ASP CA C 58.48 . . 543 . 128 ASP CB C 40.15 . . 544 . 128 ASP N N 122.56 . . 545 . 129 LEU H H 7.84 . . 546 . 129 LEU C C 177.36 . . 547 . 129 LEU CA C 58.89 . . 548 . 129 LEU CB C 41.90 . . 549 . 129 LEU N N 121.67 . . 550 . 130 ALA H H 8.29 . . 551 . 130 ALA C C 180.26 . . 552 . 130 ALA CA C 56.39 . . 553 . 130 ALA CB C 18.78 . . 554 . 130 ALA N N 120.35 . . 555 . 131 THR H H 8.61 . . 556 . 131 THR C C 176.17 . . 557 . 131 THR CA C 66.74 . . 558 . 131 THR CB C 69.73 . . 559 . 131 THR N N 114.61 . . 560 . 132 ALA H H 7.48 . . 561 . 132 ALA C C 179.03 . . 562 . 132 ALA CA C 55.97 . . 563 . 132 ALA CB C 18.54 . . 564 . 132 ALA N N 124.74 . . 565 . 133 LEU H H 8.19 . . 566 . 133 LEU C C 178.54 . . 567 . 133 LEU CA C 58.74 . . 568 . 133 LEU CB C 41.58 . . 569 . 133 LEU N N 117.20 . . 570 . 134 GLU H H 8.24 . . 571 . 134 GLU C C 179.10 . . 572 . 134 GLU CA C 60.26 . . 573 . 134 GLU CB C 29.62 . . 574 . 134 GLU N N 118.72 . . 575 . 135 GLN H H 7.62 . . 576 . 135 GLN C C 179.22 . . 577 . 135 GLN CA C 59.35 . . 578 . 135 GLN CB C 28.51 . . 579 . 135 GLN N N 117.09 . . 580 . 136 LEU H H 7.95 . . 581 . 136 LEU C C 179.05 . . 582 . 136 LEU CA C 57.98 . . 583 . 136 LEU CB C 42.70 . . 584 . 136 LEU N N 119.91 . . 585 . 137 LEU H H 8.45 . . 586 . 137 LEU C C 178.82 . . 587 . 137 LEU CA C 58.02 . . 588 . 137 LEU CB C 41.90 . . 589 . 137 LEU N N 118.31 . . 590 . 138 GLN H H 7.49 . . 591 . 138 GLN C C 176.29 . . 592 . 138 GLN CA C 58.29 . . 593 . 138 GLN CB C 28.67 . . 594 . 138 GLN N N 115.57 . . 595 . 139 ALA H H 7.46 . . 596 . 139 ALA C C 176.54 . . 597 . 139 ALA CA C 53.28 . . 598 . 139 ALA CB C 19.34 . . 599 . 139 ALA N N 119.09 . . 600 . 140 TYR H H 7.49 . . 601 . 140 TYR C C 173.30 . . 602 . 140 TYR CA C 57.49 . . 603 . 140 TYR CB C 39.43 . . 604 . 140 TYR N N 118.81 . . 605 . 141 PRO C C 177.14 . . 606 . 141 PRO CA C 63.82 . . 607 . 141 PRO CB C 32.41 . . 608 . 142 ARG H H 8.48 . . 609 . 142 ARG C C 176.04 . . 610 . 142 ARG CA C 57.10 . . 611 . 142 ARG CB C 30.18 . . 612 . 142 ARG N N 120.79 . . 613 . 143 ASP H H 8.14 . . 614 . 143 ASP C C 175.78 . . 615 . 143 ASP CA C 55.10 . . 616 . 143 ASP CB C 41.19 . . 617 . 143 ASP N N 118.88 . . 618 . 144 MET H H 7.75 . . 619 . 144 MET C C 175.30 . . 620 . 144 MET CA C 56.18 . . 621 . 144 MET CB C 34.25 . . 622 . 144 MET N N 118.38 . . 623 . 145 GLU H H 8.74 . . 624 . 145 GLU C C 177.10 . . 625 . 145 GLU CA C 57.12 . . 626 . 145 GLU CB C 29.38 . . 627 . 145 GLU N N 121.75 . . 628 . 146 LYS H H 8.49 . . 629 . 146 LYS C C 177.55 . . 630 . 146 LYS CA C 60.94 . . 631 . 146 LYS CB C 32.89 . . 632 . 146 LYS N N 125.22 . . 633 . 147 GLU H H 8.72 . . 634 . 147 GLU C C 176.70 . . 635 . 147 GLU CA C 61.70 . . 636 . 147 GLU CB C 28.19 . . 637 . 147 GLU N N 118.05 . . 638 . 148 LYS H H 7.29 . . 639 . 148 LYS C C 177.71 . . 640 . 148 LYS CA C 60.64 . . 641 . 148 LYS CB C 32.97 . . 642 . 148 LYS N N 117.93 . . 643 . 149 THR H H 7.77 . . 644 . 149 THR C C 175.14 . . 645 . 149 THR CA C 67.46 . . 646 . 149 THR CB C 68.94 . . 647 . 149 THR N N 113.84 . . 648 . 150 MET H H 8.36 . . 649 . 150 MET C C 176.38 . . 650 . 150 MET CA C 60.52 . . 651 . 150 MET CB C 34.41 . . 652 . 150 MET N N 118.92 . . 653 . 151 LEU H H 8.11 . . 654 . 151 LEU C C 177.05 . . 655 . 151 LEU CA C 58.85 . . 656 . 151 LEU CB C 41.82 . . 657 . 151 LEU N N 117.52 . . 658 . 152 VAL H H 8.27 . . 659 . 152 VAL CB C 31.70 . . 660 . 152 VAL N N 115.98 . . 661 . 153 LEU H H 8.34 . . 662 . 153 LEU C C 177.87 . . 663 . 153 LEU CA C 58.78 . . 664 . 153 LEU CB C 42.22 . . 665 . 153 LEU N N 117.72 . . 666 . 154 ALA H H 8.12 . . 667 . 154 ALA C C 178.93 . . 668 . 154 ALA CA C 56.28 . . 669 . 154 ALA CB C 17.26 . . 670 . 154 ALA N N 120.60 . . 671 . 155 LEU H H 7.56 . . 672 . 155 LEU C C 177.72 . . 673 . 155 LEU CA C 58.17 . . 674 . 155 LEU CB C 37.92 . . 675 . 155 LEU N N 117.11 . . 676 . 156 LEU H H 8.69 . . 677 . 156 LEU C C 179.19 . . 678 . 156 LEU CA C 58.17 . . 679 . 156 LEU CB C 43.58 . . 680 . 156 LEU N N 118.82 . . 681 . 157 LEU H H 8.60 . . 682 . 157 LEU C C 178.01 . . 683 . 157 LEU CA C 58.78 . . 684 . 157 LEU CB C 41.19 . . 685 . 157 LEU N N 119.38 . . 686 . 158 ALA H H 7.51 . . 687 . 158 ALA C C 178.27 . . 688 . 158 ALA CA C 55.93 . . 689 . 158 ALA CB C 17.02 . . 690 . 158 ALA N N 120.88 . . 691 . 159 LYS H H 7.77 . . 692 . 159 LYS C C 178.18 . . 693 . 159 LYS CA C 60.22 . . 694 . 159 LYS CB C 32.81 . . 695 . 159 LYS N N 116.30 . . 696 . 160 LYS H H 8.91 . . 697 . 160 LYS C C 179.88 . . 698 . 160 LYS CA C 59.61 . . 699 . 160 LYS CB C 32.33 . . 700 . 160 LYS N N 117.20 . . 701 . 161 VAL H H 8.76 . . 702 . 161 VAL C C 176.06 . . 703 . 161 VAL CA C 67.20 . . 704 . 161 VAL CB C 31.46 . . 705 . 161 VAL N N 121.21 . . 706 . 162 ALA H H 7.88 . . 707 . 162 ALA C C 176.80 . . 708 . 162 ALA CA C 55.02 . . 709 . 162 ALA CB C 17.58 . . 710 . 162 ALA N N 120.46 . . 711 . 163 SER H H 7.89 . . 712 . 163 SER C C 175.62 . . 713 . 163 SER CA C 61.78 . . 714 . 163 SER CB C 64.55 . . 715 . 163 SER N N 107.57 . . 716 . 164 HIS H H 7.59 . . 717 . 164 HIS C C 177.14 . . 718 . 164 HIS CA C 60.52 . . 719 . 164 HIS CB C 31.46 . . 720 . 164 HIS N N 121.43 . . 721 . 165 THR H H 8.41 . . 722 . 165 THR C C 171.42 . . 723 . 165 THR CB C 72.68 . . 724 . 165 THR N N 113.21 . . 725 . 166 PRO C C 178.17 . . 726 . 166 PRO CA C 66.29 . . 727 . 166 PRO CB C 32.49 . . 728 . 167 SER H H 8.15 . . 729 . 167 SER C C 176.26 . . 730 . 167 SER CA C 61.17 . . 731 . 167 SER CB C 63.12 . . 732 . 167 SER N N 109.11 . . 733 . 168 LEU H H 8.48 . . 734 . 168 LEU C C 176.83 . . 735 . 168 LEU CA C 55.45 . . 736 . 168 LEU CB C 42.78 . . 737 . 168 LEU N N 121.54 . . 738 . 169 LEU H H 7.98 . . 739 . 169 LEU C C 177.28 . . 740 . 169 LEU CA C 59.84 . . 741 . 169 LEU CB C 40.31 . . 742 . 169 LEU N N 120.62 . . 743 . 170 ARG H H 8.82 . . 744 . 170 ARG C C 177.42 . . 745 . 170 ARG CA C 61.57 . . 746 . 170 ARG CB C 29.46 . . 747 . 170 ARG N N 117.43 . . 748 . 171 ASP H H 8.06 . . 749 . 171 ASP C C 179.65 . . 750 . 171 ASP CA C 58.25 . . 751 . 171 ASP CB C 41.42 . . 752 . 171 ASP N N 117.95 . . 753 . 172 VAL H H 9.06 . . 754 . 172 VAL C C 177.79 . . 755 . 172 VAL CA C 65.79 . . 756 . 172 VAL CB C 31.86 . . 757 . 172 VAL N N 120.71 . . 758 . 173 PHE H H 9.33 . . 759 . 173 PHE C C 175.90 . . 760 . 173 PHE CA C 63.45 . . 761 . 173 PHE CB C 40.15 . . 762 . 173 PHE N N 127.31 . . 763 . 174 HIS H H 8.29 . . 764 . 174 HIS C C 177.76 . . 765 . 174 HIS CA C 60.41 . . 766 . 174 HIS CB C 29.86 . . 767 . 174 HIS N N 116.35 . . 768 . 175 THR H H 8.25 . . 769 . 175 THR C C 175.94 . . 770 . 175 THR CA C 67.16 . . 771 . 175 THR CB C 69.65 . . 772 . 175 THR N N 114.84 . . 773 . 176 THR H H 8.22 . . 774 . 176 THR C C 176.33 . . 775 . 176 THR CB C 68.22 . . 776 . 176 THR N N 120.68 . . 777 . 177 VAL H H 8.19 . . 778 . 177 VAL C C 177.34 . . 779 . 177 VAL CA C 67.08 . . 780 . 177 VAL CB C 31.94 . . 781 . 177 VAL N N 121.70 . . 782 . 178 ASN H H 7.98 . . 783 . 178 ASN C C 176.98 . . 784 . 178 ASN CA C 57.15 . . 785 . 178 ASN CB C 38.40 . . 786 . 178 ASN N N 116.71 . . 787 . 179 PHE H H 8.34 . . 788 . 179 PHE C C 178.54 . . 789 . 179 PHE CA C 63.10 . . 790 . 179 PHE CB C 40.23 . . 791 . 179 PHE N N 120.37 . . 792 . 180 ILE H H 8.54 . . 793 . 180 ILE C C 177.51 . . 794 . 180 ILE CA C 66.21 . . 795 . 180 ILE CB C 37.92 . . 796 . 180 ILE N N 121.25 . . 797 . 181 ASN H H 8.68 . . 798 . 181 ASN C C 176.70 . . 799 . 181 ASN CA C 56.47 . . 800 . 181 ASN CB C 38.63 . . 801 . 181 ASN N N 117.94 . . 802 . 182 GLN H H 7.87 . . 803 . 182 GLN C C 177.19 . . 804 . 182 GLN CA C 58.29 . . 805 . 182 GLN CB C 29.78 . . 806 . 182 GLN N N 114.40 . . 807 . 183 ASN H H 7.54 . . 808 . 183 ASN C C 175.07 . . 809 . 183 ASN CA C 55.86 . . 810 . 183 ASN CB C 42.38 . . 811 . 183 ASN N N 112.97 . . 812 . 184 LEU H H 8.67 . . 813 . 184 LEU C C 175.99 . . 814 . 184 LEU CA C 54.53 . . 815 . 184 LEU CB C 45.17 . . 816 . 184 LEU N N 120.26 . . 817 . 185 ARG H H 7.37 . . 818 . 185 ARG C C 178.24 . . 819 . 185 ARG CA C 61.09 . . 820 . 185 ARG CB C 30.74 . . 821 . 185 ARG N N 121.62 . . 822 . 186 THR H H 8.38 . . 823 . 186 THR C C 176.33 . . 824 . 186 THR CA C 66.51 . . 825 . 186 THR CB C 68.78 . . 826 . 186 THR N N 112.29 . . 827 . 187 TYR H H 7.98 . . 828 . 187 TYR C C 177.87 . . 829 . 187 TYR CA C 61.81 . . 830 . 187 TYR CB C 38.95 . . 831 . 187 TYR N N 124.26 . . 832 . 188 VAL H H 8.53 . . 833 . 188 VAL C C 177.26 . . 834 . 188 VAL CA C 67.39 . . 835 . 188 VAL CB C 31.38 . . 836 . 188 VAL N N 118.64 . . 837 . 189 ARG H H 7.96 . . 838 . 189 ARG C C 178.75 . . 839 . 189 ARG CA C 60.22 . . 840 . 189 ARG CB C 30.26 . . 841 . 189 ARG N N 118.13 . . 842 . 190 SER H H 7.63 . . 843 . 190 SER C C 176.24 . . 844 . 190 SER CA C 61.85 . . 845 . 190 SER CB C 63.75 . . 846 . 190 SER N N 114.36 . . 847 . 191 LEU H H 7.85 . . 848 . 191 LEU C C 178.26 . . 849 . 191 LEU CA C 57.91 . . 850 . 191 LEU CB C 42.06 . . 851 . 191 LEU N N 122.95 . . 852 . 192 ALA H H 7.75 . . 853 . 192 ALA C C 177.00 . . 854 . 192 ALA CA C 54.46 . . 855 . 192 ALA CB C 18.70 . . 856 . 192 ALA N N 117.56 . . 857 . 193 ARG H H 7.44 . . 858 . 193 ARG C C 176.80 . . 859 . 193 ARG CA C 57.64 . . 860 . 193 ARG CB C 31.14 . . 861 . 193 ARG N N 114.47 . . 862 . 194 ASN H H 8.23 . . 863 . 194 ASN C C 175.88 . . 864 . 194 ASN CA C 54.72 . . 865 . 194 ASN CB C 40.39 . . 866 . 194 ASN N N 115.99 . . 867 . 195 GLY H H 8.31 . . 868 . 195 GLY C C 172.64 . . 869 . 195 GLY CA C 45.89 . . 870 . 195 GLY N N 108.63 . . 871 . 196 MET H H 8.14 . . 872 . 196 MET C C 174.52 . . 873 . 196 MET CA C 56.01 . . 874 . 196 MET CB C 34.01 . . 875 . 196 MET N N 117.95 . . 876 . 197 ASP H H 7.94 . . 877 . 197 ASP C C 180.52 . . 878 . 197 ASP CA C 56.66 . . 879 . 197 ASP CB C 42.62 . . 880 . 197 ASP N N 126.78 . . stop_ save_