data_10052 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; characterization of PCP-0SH in the D1 state was examined by using H/D exchange experiments. ; _BMRB_accession_number 10052 _BMRB_flat_file_name bmr10052.str _Entry_type original _Submission_date 2006-11-20 _Accession_date 2006-11-20 _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 Iimura Satoshi . . 2 Umezaki Taro . . 3 Takeuchi Makoto . . 4 Mizuguchi Mineyuki . . 5 Ogasahara Kyoko . . 6 Yagi Hiromasa . . 7 Akutsu Hideo . . 8 Noda Yasuo . . 9 Segawa Shin-ichi . . 10 Yutani Katsuhide . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 296 "13C chemical shifts" 513 "15N chemical shifts" 296 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2007-06-13 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under non-denaturing conditions: Role of the C-terminal a-helix of the protein in folding and stability ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17309236 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Iimura Satoshi . . 2 Umezaki Taro . . 3 Takeuchi Makoto . . 4 Mizuguchi Mineyuki . . 5 Yagi Hiromasa . . 6 Ogasahara Kyoko . . 7 Akutsu Hideo . . 8 Noda Yasuo . . 9 Segawa Shin-ichi . . 10 Yutani Katsuhide . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3664 _Page_last 3672 _Year 2007 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full . _Citation_title ; Unusually slow denaturation and refolding processes of pyrrolidone carboxyl peptidase from a hyperthermophile are highly cooperative: Real-time NMR studies ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15362877 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Iimura Satoshi . . 2 Yagi Hiromasa . . 3 Ogasahara Kyoko . . 4 Akutsu Hideo . . 5 Noda Yasuo . . 6 Segawa Shin-ichi . . 7 Yutani Katsuhide . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume 43 _Journal_issue 37 _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 11906 _Page_last 11915 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PCP homo tetramer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PCP homo tetramer subunit 1' $PCP-0SH 'PCP homo tetramer subunit 2' $PCP-0SH 'PCP homo tetramer subunit 3' $PCP-0SH 'PCP homo tetramer subunit 4' $PCP-0SH stop_ _System_molecular_weight 91200 _System_physical_state native _System_oligomer_state 'protein-protein complex' _System_paramagnetic no _System_thiol_state 'free and other bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'PCP homo tetramer subunit 1' 1 'PCP homo tetramer subunit 2' 1 'PCP homo tetramer subunit 3' 1 'PCP homo tetramer subunit 4' stop_ loop_ _Biological_function 'removal of N-terminal pyroglutamic acid from polypeptide' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PCP-0SH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pyrrolidone carboxyl peptidase cys-free mutant' _Molecular_mass 22800 _Mol_thiol_state 'not present' _Details 'PCP exists in monomeric form in this condition that NMR peak assignment has done.' ############################## # Polymer residue sequence # ############################## _Residue_count 208 _Mol_residue_sequence ; MKVLVTGFEPFGGEKINPTE RIAKDLDGIKIGDAQVFGRV LPVVFGKAKEVLEKTLEEIK PDIAIHVGLAPGRSAISIER IAVNAIDARIPDNEGKKIED EPIVPGAPTAYFSTLPIKKI MKKLHERGIPAYISNSAGLY LSNYVMYLSLHHSATKGYPK MSGFIHVPYIPEQIIDKIGK GQVPPSMSYEMELEAVKVAI EVALEELL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 VAL 4 LEU 5 VAL 6 THR 7 GLY 8 PHE 9 GLU 10 PRO 11 PHE 12 GLY 13 GLY 14 GLU 15 LYS 16 ILE 17 ASN 18 PRO 19 THR 20 GLU 21 ARG 22 ILE 23 ALA 24 LYS 25 ASP 26 LEU 27 ASP 28 GLY 29 ILE 30 LYS 31 ILE 32 GLY 33 ASP 34 ALA 35 GLN 36 VAL 37 PHE 38 GLY 39 ARG 40 VAL 41 LEU 42 PRO 43 VAL 44 VAL 45 PHE 46 GLY 47 LYS 48 ALA 49 LYS 50 GLU 51 VAL 52 LEU 53 GLU 54 LYS 55 THR 56 LEU 57 GLU 58 GLU 59 ILE 60 LYS 61 PRO 62 ASP 63 ILE 64 ALA 65 ILE 66 HIS 67 VAL 68 GLY 69 LEU 70 ALA 71 PRO 72 GLY 73 ARG 74 SER 75 ALA 76 ILE 77 SER 78 ILE 79 GLU 80 ARG 81 ILE 82 ALA 83 VAL 84 ASN 85 ALA 86 ILE 87 ASP 88 ALA 89 ARG 90 ILE 91 PRO 92 ASP 93 ASN 94 GLU 95 GLY 96 LYS 97 LYS 98 ILE 99 GLU 100 ASP 101 GLU 102 PRO 103 ILE 104 VAL 105 PRO 106 GLY 107 ALA 108 PRO 109 THR 110 ALA 111 TYR 112 PHE 113 SER 114 THR 115 LEU 116 PRO 117 ILE 118 LYS 119 LYS 120 ILE 121 MET 122 LYS 123 LYS 124 LEU 125 HIS 126 GLU 127 ARG 128 GLY 129 ILE 130 PRO 131 ALA 132 TYR 133 ILE 134 SER 135 ASN 136 SER 137 ALA 138 GLY 139 LEU 140 TYR 141 LEU 142 SER 143 ASN 144 TYR 145 VAL 146 MET 147 TYR 148 LEU 149 SER 150 LEU 151 HIS 152 HIS 153 SER 154 ALA 155 THR 156 LYS 157 GLY 158 TYR 159 PRO 160 LYS 161 MET 162 SER 163 GLY 164 PHE 165 ILE 166 HIS 167 VAL 168 PRO 169 TYR 170 ILE 171 PRO 172 GLU 173 GLN 174 ILE 175 ILE 176 ASP 177 LYS 178 ILE 179 GLY 180 LYS 181 GLY 182 GLN 183 VAL 184 PRO 185 PRO 186 SER 187 MET 188 SER 189 TYR 190 GLU 191 MET 192 GLU 193 LEU 194 GLU 195 ALA 196 VAL 197 LYS 198 VAL 199 ALA 200 ILE 201 GLU 202 VAL 203 ALA 204 LEU 205 GLU 206 GLU 207 LEU 208 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 PDB 1IOF "X-Ray Crystalline Structures Of Pyrrolidone Carboxyl Peptidase From A Hyperthermophile, Pyrococcus Furiosus, And Its Cys-Free M" 100.00 208 99.04 99.04 3.57e-143 PDB 1IOI "X-Ray Crystalline Structures Of Pyrrolidone Carboxyl Peptidase From A Hyperthermophile, Pyrococcus Furiosus, And Its Cys-Free M" 100.00 208 100.00 100.00 4.18e-144 PDB 1X10 "Structure Of Mutant Pyrrolidone Carboxyl Peptidase (E192a) From A Hyperthermophile, Pyrococcus Furiosus" 100.00 208 99.52 99.52 1.91e-143 PDB 1X12 "Structure Of Mutant Pyrrolidone Carboxyl Peptidase (E192d) From A Hyperthermophile, Pyrococcus Furiosus" 100.00 208 99.52 100.00 9.50e-144 PDB 1Z8T "Structure Of Mutant Pyrrolidone Carboxyl Peptidase (E192q) From A Hyperthermophile, Pyrococcus Furiosus" 100.00 208 99.52 100.00 9.19e-144 PDB 1Z8W "Structure Of Mutant Pyrrolidone Carboxyl Peptidase (E192i) From A Hyperthermophile, Pyrococcus Furiosus" 100.00 208 99.52 99.52 6.16e-143 PDB 1Z8X "Structure Of Mutant Pyrrolidone Carboxyl Peptidase (E192v) From A Hyperthermophile, Pyrococcus Furiosus" 100.00 208 99.52 99.52 4.49e-143 PDB 2DF5 "Crystal Structure Of Pf-Pcp(1-204)-C" 99.04 213 98.06 98.54 8.19e-141 PDB 2EO8 "Crystal Structure Of A Mutant Pyrrolidone Carboxyl Peptidase (A199p) From P. Furiosus" 100.00 208 99.52 99.52 4.59e-143 DBJ BAA32989 "pyrrolidone carboxyl peptidase [Pyrococcus furiosus]" 100.00 208 99.04 99.04 3.57e-143 GB AAL81423 "pyroglutamyl-peptidase i [Pyrococcus furiosus DSM 3638]" 100.00 208 99.04 99.04 3.57e-143 GB AFN04083 "pyrrolidone-carboxylate peptidase [Pyrococcus furiosus COM1]" 100.00 208 99.04 99.04 3.57e-143 REF WP_011012443 "pyrrolidone-carboxylate peptidase [Pyrococcus furiosus]" 100.00 208 99.04 99.04 3.57e-143 SP O73944 "RecName: Full=Pyrrolidone-carboxylate peptidase; AltName: Full=5-oxoprolyl-peptidase; AltName: Full=Pyroglutamyl-peptidase I; S" 100.00 208 99.04 99.04 3.57e-143 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $PCP-0SH 'P. furiosus' 2261 Archaea . Pyrococcus furiosus no stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $PCP-0SH 'recombinant technology' 'E. coli' Escherichia coli JM109 plasmid pPCP3022 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 $PCP-0SH 0.4 mM '[U-13C; U-15N]' Glycine 20 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'the protein of component is PCP-OSH_Ala199Pro' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PCP-0SH 0.4 mM [U-15N] Glycine 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name XWIN-NMR _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address 'University of California' . . stop_ loop_ _Task 'peak assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HSQC-NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-NOESY-HSQC _Sample_label $sample_2 save_ save_1H-15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(CO)CACB _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HSQC-NOESY-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.01 pH temperature 303 0.1 K stop_ save_ save_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.0 0.01 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_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 0.0 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 external 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_PCP-0SH_pH2.5_30C _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' HNCACB HN(CO)CACB HNCO HN(CA)CO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'PCP homo tetramer subunit 1' _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 MET C C 169.606 0.3 1 2 1 1 MET CA C 54.53 0.3 1 3 1 1 MET CB C 32.605 0.3 1 4 2 2 LYS H H 9.77 0.01 1 5 2 2 LYS C C 172.594 0.3 1 6 2 2 LYS CA C 55.334 0.3 1 7 2 2 LYS CB C 36.681 0.3 1 8 2 2 LYS N N 123.618 0.2 1 9 3 3 VAL H H 9.222 0.01 1 10 3 3 VAL C C 170.678 0.3 1 11 3 3 VAL CA C 59.507 0.3 1 12 3 3 VAL CB C 34.162 0.3 1 13 3 3 VAL N N 123.245 0.2 1 14 4 4 LEU H H 9.034 0.01 1 15 4 4 LEU C C 170.654 0.3 1 16 4 4 LEU CA C 52.253 0.3 1 17 4 4 LEU CB C 45.566 0.3 1 18 4 4 LEU N N 127.954 0.2 1 19 5 5 VAL H H 9.338 0.01 1 20 5 5 VAL C C 173.196 0.3 1 21 5 5 VAL CA C 58.924 0.3 1 22 5 5 VAL CB C 33.707 0.3 1 23 5 5 VAL N N 127.178 0.2 1 24 6 6 THR H H 8.155 0.01 1 25 6 6 THR C C 170.726 0.3 1 26 6 6 THR CA C 57.623 0.3 1 27 6 6 THR CB C 71.628 0.3 1 28 6 6 THR N N 112.29 0.2 1 29 7 7 GLY H H 7.5 0.01 1 30 7 7 GLY C C 169.154 0.3 1 31 7 7 GLY CA C 42.544 0.3 1 32 7 7 GLY N N 107.126 0.2 1 33 10 10 PRO C C 173.428 0.3 1 34 10 10 PRO CA C 62.642 0.3 1 35 10 10 PRO CB C 31.261 0.3 1 36 11 11 PHE H H 7.901 0.01 1 37 11 11 PHE C C 173.62 0.3 1 38 11 11 PHE CA C 56.824 0.3 1 39 11 11 PHE CB C 40.156 0.3 1 40 11 11 PHE N N 119.17 0.2 1 41 12 12 GLY H H 8.55 0.01 1 42 12 12 GLY C C 172.541 0.3 1 43 12 12 GLY CA C 46.165 0.3 1 44 12 12 GLY N N 109.694 0.2 1 45 13 13 GLY H H 8.563 0.01 1 46 13 13 GLY C C 171.835 0.3 1 47 13 13 GLY CA C 44.781 0.3 1 48 13 13 GLY N N 110.62 0.2 1 49 14 14 GLU H H 7.651 0.01 1 50 14 14 GLU C C 176.579 0.3 1 51 14 14 GLU CA C 54.895 0.3 1 52 14 14 GLU CB C 28.456 0.3 1 53 14 14 GLU N N 119.149 0.2 1 54 15 15 LYS H H 8.506 0.01 1 55 15 15 LYS C C 173.884 0.3 1 56 15 15 LYS CA C 56.937 0.3 1 57 15 15 LYS CB C 32.474 0.3 1 58 15 15 LYS N N 121.115 0.2 1 59 16 16 ILE H H 7.883 0.01 1 60 16 16 ILE C C 171.836 0.3 1 61 16 16 ILE CA C 59.409 0.3 1 62 16 16 ILE CB C 40.263 0.3 1 63 16 16 ILE N N 116.532 0.2 1 64 17 17 ASN H H 8.624 0.01 1 65 17 17 ASN CA C 50.177 0.3 1 66 17 17 ASN CB C 40.214 0.3 1 67 17 17 ASN N N 120.498 0.2 1 68 18 18 PRO C C 174.997 0.3 1 69 18 18 PRO CA C 64.726 0.3 1 70 18 18 PRO CB C 32.291 0.3 1 71 19 19 THR H H 8.562 0.01 1 72 19 19 THR C C 173.311 0.3 1 73 19 19 THR CA C 65.1 0.3 1 74 19 19 THR CB C 67.125 0.3 1 75 19 19 THR N N 107.724 0.2 1 76 20 20 GLU H H 7.281 0.01 1 77 20 20 GLU C C 174.037 0.3 1 78 20 20 GLU CA C 58.323 0.3 1 79 20 20 GLU CB C 26.631 0.3 1 80 20 20 GLU N N 124.609 0.2 1 81 21 21 ARG H H 6.834 0.01 1 82 21 21 ARG C C 175.002 0.3 1 83 21 21 ARG CA C 58.818 0.3 1 84 21 21 ARG CB C 29.201 0.3 1 85 21 21 ARG N N 118.75 0.2 1 86 22 22 ILE H H 8.17 0.01 1 87 22 22 ILE C C 172.647 0.3 1 88 22 22 ILE CA C 65.052 0.3 1 89 22 22 ILE CB C 38.088 0.3 1 90 22 22 ILE N N 119.811 0.2 1 91 23 23 ALA H H 7.155 0.01 1 92 23 23 ALA C C 176.081 0.3 1 93 23 23 ALA CA C 55.06 0.3 1 94 23 23 ALA CB C 16.957 0.3 1 95 23 23 ALA N N 118.638 0.2 1 96 24 24 LYS H H 7.549 0.01 1 97 24 24 LYS C C 176.698 0.3 1 98 24 24 LYS CA C 58.487 0.3 1 99 24 24 LYS CB C 31.182 0.3 1 100 24 24 LYS N N 114.192 0.2 1 101 25 25 ASP H H 8.739 0.01 1 102 25 25 ASP C C 175.514 0.3 1 103 25 25 ASP CA C 55.896 0.3 1 104 25 25 ASP CB C 39.349 0.3 1 105 25 25 ASP N N 119.2 0.2 1 106 26 26 LEU H H 7.553 0.01 1 107 26 26 LEU C C 173.003 0.3 1 108 26 26 LEU CA C 53.843 0.3 1 109 26 26 LEU CB C 40.99 0.3 1 110 26 26 LEU N N 116.782 0.2 1 111 27 27 ASP H H 6.999 0.01 1 112 27 27 ASP C C 173.932 0.3 1 113 27 27 ASP CA C 56.498 0.3 1 114 27 27 ASP CB C 40.421 0.3 1 115 27 27 ASP N N 116.669 0.2 1 116 28 28 GLY H H 8.512 0.01 1 117 28 28 GLY C C 172.252 0.3 1 118 28 28 GLY CA C 45.098 0.3 1 119 28 28 GLY N N 115.006 0.2 1 120 29 29 ILE H H 7.254 0.01 1 121 29 29 ILE C C 171.233 0.3 1 122 29 29 ILE CA C 60.245 0.3 1 123 29 29 ILE CB C 38.072 0.3 1 124 29 29 ILE N N 117.083 0.2 1 125 30 30 LYS H H 7.996 0.01 1 126 30 30 LYS C C 174.186 0.3 1 127 30 30 LYS CA C 54.257 0.3 1 128 30 30 LYS CB C 33.423 0.3 1 129 30 30 LYS N N 119.906 0.2 1 130 31 31 ILE H H 8.044 0.01 1 131 31 31 ILE C C 173.073 0.3 1 132 31 31 ILE CA C 59.955 0.3 1 133 31 31 ILE CB C 39.006 0.3 1 134 31 31 ILE N N 123.946 0.2 1 135 32 32 GLY H H 8.741 0.01 1 136 32 32 GLY C C 172.095 0.3 1 137 32 32 GLY CA C 46.578 0.3 1 138 32 32 GLY N N 116.503 0.2 1 139 33 33 ASP H H 8.563 0.01 1 140 33 33 ASP C C 172.041 0.3 1 141 33 33 ASP CA C 52.448 0.3 1 142 33 33 ASP CB C 37.611 0.3 1 143 33 33 ASP N N 122.621 0.2 1 144 34 34 ALA H H 8.382 0.01 1 145 34 34 ALA C C 173.141 0.3 1 146 34 34 ALA CA C 50.677 0.3 1 147 34 34 ALA CB C 20.891 0.3 1 148 34 34 ALA N N 123.731 0.2 1 149 35 35 GLN H H 7.873 0.01 1 150 35 35 GLN C C 171.649 0.3 1 151 35 35 GLN CA C 54.799 0.3 1 152 35 35 GLN CB C 30.44 0.3 1 153 35 35 GLN N N 120.381 0.2 1 154 36 36 VAL H H 8.373 0.01 1 155 36 36 VAL C C 172.004 0.3 1 156 36 36 VAL CA C 61.121 0.3 1 157 36 36 VAL CB C 30.691 0.3 1 158 36 36 VAL N N 124.589 0.2 1 159 37 37 PHE H H 9.385 0.01 1 160 37 37 PHE C C 171.32 0.3 1 161 37 37 PHE CA C 55.694 0.3 1 162 37 37 PHE CB C 41.018 0.3 1 163 37 37 PHE N N 127.276 0.2 1 164 38 38 GLY H H 9.592 0.01 1 165 38 38 GLY C C 172.023 0.3 1 166 38 38 GLY CA C 43.441 0.3 1 167 38 38 GLY N N 111.376 0.2 1 168 39 39 ARG H H 8.643 0.01 1 169 39 39 ARG C C 170.999 0.3 1 170 39 39 ARG CA C 51.927 0.3 1 171 39 39 ARG CB C 33.374 0.3 1 172 39 39 ARG N N 124.298 0.2 1 173 40 40 VAL H H 8.558 0.01 1 174 40 40 VAL C C 172.346 0.3 1 175 40 40 VAL CA C 60.775 0.3 1 176 40 40 VAL CB C 32.131 0.3 1 177 40 40 VAL N N 120.566 0.2 1 178 41 41 LEU H H 9.044 0.01 1 179 41 41 LEU C C 171.202 0.3 1 180 41 41 LEU CA C 51.34 0.3 1 181 41 41 LEU CB C 41.576 0.3 1 182 41 41 LEU N N 126.663 0.2 1 183 42 42 PRO C C 171.769 0.3 1 184 42 42 PRO CA C 61.567 0.3 1 185 42 42 PRO CB C 32.334 0.3 1 186 43 43 VAL H H 7.647 0.01 1 187 43 43 VAL C C 172.863 0.3 1 188 43 43 VAL CA C 60.103 0.3 1 189 43 43 VAL CB C 29.704 0.3 1 190 43 43 VAL N N 104.993 0.2 1 191 44 44 VAL H H 6.613 0.01 1 192 44 44 VAL C C 174.926 0.3 1 193 44 44 VAL CA C 60.244 0.3 1 194 44 44 VAL CB C 32.645 0.3 1 195 44 44 VAL N N 118.456 0.2 1 196 45 45 PHE H H 8.428 0.01 1 197 45 45 PHE C C 174.865 0.3 1 198 45 45 PHE CA C 61.803 0.3 1 199 45 45 PHE CB C 37.284 0.3 1 200 45 45 PHE N N 126.09 0.2 1 201 46 46 GLY H H 8.814 0.01 1 202 46 46 GLY C C 174.412 0.3 1 203 46 46 GLY CA C 47.09 0.3 1 204 46 46 GLY N N 106.048 0.2 1 205 47 47 LYS H H 6.993 0.01 1 206 47 47 LYS C C 175.329 0.3 1 207 47 47 LYS CA C 57.362 0.3 1 208 47 47 LYS CB C 31.562 0.3 1 209 47 47 LYS N N 119.542 0.2 1 210 48 48 ALA H H 8.672 0.01 1 211 48 48 ALA C C 176.603 0.3 1 212 48 48 ALA CA C 55.977 0.3 1 213 48 48 ALA CB C 16.151 0.3 1 214 48 48 ALA N N 122.111 0.2 1 215 49 49 LYS H H 8.284 0.01 1 216 49 49 LYS C C 174.824 0.3 1 217 49 49 LYS CA C 59.879 0.3 1 218 49 49 LYS CB C 31.042 0.3 1 219 49 49 LYS N N 116.05 0.2 1 220 50 50 GLU H H 7.447 0.01 1 221 50 50 GLU C C 176.422 0.3 1 222 50 50 GLU CA C 58.655 0.3 1 223 50 50 GLU CB C 27.578 0.3 1 224 50 50 GLU N N 117.082 0.2 1 225 51 51 VAL H H 8.595 0.01 1 226 51 51 VAL C C 177.096 0.3 1 227 51 51 VAL CA C 65.892 0.3 1 228 51 51 VAL CB C 31.294 0.3 1 229 51 51 VAL N N 118.488 0.2 1 230 52 52 LEU H H 8.904 0.01 1 231 52 52 LEU C C 175.188 0.3 1 232 52 52 LEU CA C 58.565 0.3 1 233 52 52 LEU CB C 40.874 0.3 1 234 52 52 LEU N N 123.6 0.2 1 235 53 53 GLU H H 8.464 0.01 1 236 53 53 GLU C C 175.843 0.3 1 237 53 53 GLU CA C 58.822 0.3 1 238 53 53 GLU CB C 26.706 0.3 1 239 53 53 GLU N N 116.142 0.2 1 240 54 54 LYS H H 7.857 0.01 1 241 54 54 LYS C C 176.217 0.3 1 242 54 54 LYS CA C 58.872 0.3 1 243 54 54 LYS CB C 31.467 0.3 1 244 54 54 LYS N N 118.335 0.2 1 245 55 55 THR H H 8.242 0.01 1 246 55 55 THR C C 173.938 0.3 1 247 55 55 THR CA C 66.656 0.3 1 248 55 55 THR CB C 67.726 0.3 1 249 55 55 THR N N 115.188 0.2 1 250 56 56 LEU H H 8.381 0.01 1 251 56 56 LEU C C 176.283 0.3 1 252 56 56 LEU CA C 57.896 0.3 1 253 56 56 LEU CB C 40.55 0.3 1 254 56 56 LEU N N 119.303 0.2 1 255 57 57 GLU H H 7.767 0.01 1 256 57 57 GLU C C 174.317 0.3 1 257 57 57 GLU CA C 57.836 0.3 1 258 57 57 GLU CB C 27.688 0.3 1 259 57 57 GLU N N 116.801 0.2 1 260 58 58 GLU H H 8.044 0.01 1 261 58 58 GLU C C 175.168 0.3 1 262 58 58 GLU CA C 57.53 0.3 1 263 58 58 GLU CB C 28.171 0.3 1 264 58 58 GLU N N 117.025 0.2 1 265 59 59 ILE H H 7.724 0.01 1 266 59 59 ILE C C 171.969 0.3 1 267 59 59 ILE CA C 61.876 0.3 1 268 59 59 ILE CB C 38.514 0.3 1 269 59 59 ILE N N 116.533 0.2 1 270 60 60 LYS H H 7.687 0.01 1 271 60 60 LYS C C 170.968 0.3 1 272 60 60 LYS CA C 55.84 0.3 1 273 60 60 LYS CB C 29.029 0.3 1 274 60 60 LYS N N 112.949 0.2 1 275 61 61 PRO C C 172.048 0.3 1 276 61 61 PRO CA C 62.144 0.3 1 277 61 61 PRO CB C 30.784 0.3 1 278 62 62 ASP H H 8.468 0.01 1 279 62 62 ASP C C 173.962 0.3 1 280 62 62 ASP CA C 56.353 0.3 1 281 62 62 ASP CB C 42.923 0.3 1 282 62 62 ASP N N 116.972 0.2 1 283 63 63 ILE H H 7.454 0.01 1 284 63 63 ILE C C 170.733 0.3 1 285 63 63 ILE CA C 58.757 0.3 1 286 63 63 ILE CB C 42.183 0.3 1 287 63 63 ILE N N 115.824 0.2 1 288 64 64 ALA H H 8.692 0.01 1 289 64 64 ALA C C 170.919 0.3 1 290 64 64 ALA CA C 49.588 0.3 1 291 64 64 ALA CB C 21.069 0.3 1 292 64 64 ALA N N 129.545 0.2 1 293 65 65 ILE H H 8.681 0.01 1 294 65 65 ILE C C 169.831 0.3 1 295 65 65 ILE CA C 59.215 0.3 1 296 65 65 ILE CB C 38.971 0.3 1 297 65 65 ILE N N 120.851 0.2 1 298 66 66 HIS H H 7.903 0.01 1 299 66 66 HIS C C 169.603 0.3 1 300 66 66 HIS CA C 53.622 0.3 1 301 66 66 HIS CB C 30.102 0.3 1 302 66 66 HIS N N 126.619 0.2 1 303 71 71 PRO C C 173.709 0.3 1 304 71 71 PRO CA C 55.669 0.3 1 305 71 71 PRO CB C 27.689 0.3 1 306 72 72 GLY H H 8.213 0.01 1 307 72 72 GLY C C 171.393 0.3 1 308 72 72 GLY CA C 45.206 0.3 1 309 72 72 GLY N N 108.948 0.2 1 310 73 73 ARG H H 7.644 0.01 1 311 73 73 ARG C C 173.98 0.3 1 312 73 73 ARG CA C 55.595 0.3 1 313 73 73 ARG CB C 30.229 0.3 1 314 73 73 ARG N N 118.623 0.2 1 315 74 74 SER H H 8.677 0.01 1 316 74 74 SER C C 169.93 0.3 1 317 74 74 SER CA C 57.645 0.3 1 318 74 74 SER CB C 63.617 0.3 1 319 74 74 SER N N 114.21 0.2 1 320 75 75 ALA H H 7.477 0.01 1 321 75 75 ALA C C 173.203 0.3 1 322 75 75 ALA CA C 50.006 0.3 1 323 75 75 ALA CB C 21.442 0.3 1 324 75 75 ALA N N 122.915 0.2 1 325 76 76 ILE H H 7.944 0.01 1 326 76 76 ILE C C 171.962 0.3 1 327 76 76 ILE CA C 59.753 0.3 1 328 76 76 ILE CB C 36.282 0.3 1 329 76 76 ILE N N 120.226 0.2 1 330 77 77 SER H H 8.482 0.01 1 331 77 77 SER C C 170.814 0.3 1 332 77 77 SER CA C 54.854 0.3 1 333 77 77 SER CB C 64.796 0.3 1 334 77 77 SER N N 118.147 0.2 1 335 78 78 ILE C C 171.585 0.3 1 336 78 78 ILE CA C 59.864 0.3 1 337 78 78 ILE CB C 38.681 0.3 1 338 79 79 GLU H H 8.117 0.01 1 339 79 79 GLU C C 174.283 0.3 1 340 79 79 GLU CA C 55.748 0.3 1 341 79 79 GLU CB C 30.272 0.3 1 342 79 79 GLU N N 125.477 0.2 1 343 80 80 ARG H H 8.925 0.01 1 344 80 80 ARG CA C 59.012 0.3 1 345 80 80 ARG CB C 32.065 0.3 1 346 80 80 ARG N N 124.981 0.2 1 347 81 81 ILE C C 169.96 0.3 1 348 81 81 ILE CA C 59.789 0.3 1 349 81 81 ILE CB C 42.691 0.3 1 350 82 82 ALA H H 8.775 0.01 1 351 82 82 ALA C C 173.569 0.3 1 352 82 82 ALA CA C 50.253 0.3 1 353 82 82 ALA CB C 21.314 0.3 1 354 82 82 ALA N N 127.029 0.2 1 355 83 83 VAL H H 9.273 0.01 1 356 83 83 VAL C C 173.927 0.3 1 357 83 83 VAL CA C 59.17 0.3 1 358 83 83 VAL CB C 34.058 0.3 1 359 83 83 VAL N N 117.001 0.2 1 360 92 92 ASP C C 172.49 0.3 1 361 92 92 ASP CA C 52.736 0.3 1 362 92 92 ASP CB C 38.032 0.3 1 363 93 93 ASN H H 8.308 0.01 1 364 93 93 ASN C C 172.539 0.3 1 365 93 93 ASN CA C 53.232 0.3 1 366 93 93 ASN CB C 38.125 0.3 1 367 93 93 ASN N N 118.278 0.2 1 368 94 94 GLU H H 8.229 0.01 1 369 94 94 GLU C C 173.641 0.3 1 370 94 94 GLU CA C 55.685 0.3 1 371 94 94 GLU CB C 27.562 0.3 1 372 94 94 GLU N N 119.125 0.2 1 373 95 95 GLY H H 8.203 0.01 1 374 95 95 GLY C C 171.353 0.3 1 375 95 95 GLY CA C 45.066 0.3 1 376 95 95 GLY N N 108.757 0.2 1 377 96 96 LYS H H 7.985 0.01 1 378 96 96 LYS C C 173.607 0.3 1 379 96 96 LYS CA C 55.643 0.3 1 380 96 96 LYS CB C 32.252 0.3 1 381 96 96 LYS N N 120.123 0.2 1 382 97 97 LYS H H 8.18 0.01 1 383 97 97 LYS C C 173.352 0.3 1 384 97 97 LYS CA C 55.849 0.3 1 385 97 97 LYS CB C 32.14 0.3 1 386 97 97 LYS N N 121.513 0.2 1 387 98 98 ILE H H 8.033 0.01 1 388 98 98 ILE C C 173.03 0.3 1 389 98 98 ILE CA C 60.276 0.3 1 390 98 98 ILE CB C 38.063 0.3 1 391 98 98 ILE N N 122.258 0.2 1 392 99 99 GLU H H 8.363 0.01 1 393 99 99 GLU C C 172.092 0.3 1 394 99 99 GLU CA C 54.7 0.3 1 395 99 99 GLU CB C 28.778 0.3 1 396 99 99 GLU N N 124.338 0.2 1 397 100 100 ASP H H 8.289 0.01 1 398 100 100 ASP C C 171.7 0.3 1 399 100 100 ASP CA C 52.166 0.3 1 400 100 100 ASP CB C 38.328 0.3 1 401 100 100 ASP N N 120.601 0.2 1 402 103 103 ILE C C 174.704 0.3 1 403 103 103 ILE CA C 64.517 0.3 1 404 103 103 ILE CB C 36.61 0.3 1 405 104 104 VAL H H 8.536 0.01 1 406 104 104 VAL C C 170.971 0.3 1 407 104 104 VAL CA C 58.226 0.3 1 408 104 104 VAL CB C 32.749 0.3 1 409 104 104 VAL N N 117.102 0.2 1 410 105 105 PRO C C 174.95 0.3 1 411 105 105 PRO CA C 63.432 0.3 1 412 105 105 PRO CB C 30.532 0.3 1 413 106 106 GLY H H 8.937 0.01 1 414 106 106 GLY C C 170.657 0.3 1 415 106 106 GLY CA C 45.134 0.3 1 416 106 106 GLY N N 113.475 0.2 1 417 107 107 ALA H H 7.168 0.01 1 418 107 107 ALA C C 171.325 0.3 1 419 107 107 ALA CA C 50.308 0.3 1 420 107 107 ALA CB C 17.323 0.3 1 421 107 107 ALA N N 123.673 0.2 1 422 108 108 PRO C C 174.696 0.3 1 423 108 108 PRO CA C 63.2 0.3 1 424 108 108 PRO CB C 31.426 0.3 1 425 109 109 THR H H 8.582 0.01 1 426 109 109 THR C C 170.312 0.3 1 427 109 109 THR CA C 65.276 0.3 1 428 109 109 THR CB C 68.296 0.3 1 429 109 109 THR N N 117.162 0.2 1 430 110 110 ALA H H 7.347 0.01 1 431 110 110 ALA C C 173.116 0.3 1 432 110 110 ALA CA C 50.677 0.3 1 433 110 110 ALA CB C 21.762 0.3 1 434 110 110 ALA N N 118.636 0.2 1 435 111 111 TYR H H 8.676 0.01 1 436 111 111 TYR C C 172.096 0.3 1 437 111 111 TYR CA C 57.081 0.3 1 438 111 111 TYR CB C 44.36 0.3 1 439 111 111 TYR N N 115.184 0.2 1 440 112 112 PHE H H 8.665 0.01 1 441 112 112 PHE C C 173.955 0.3 1 442 112 112 PHE CA C 56.316 0.3 1 443 112 112 PHE CB C 39.247 0.3 1 444 112 112 PHE N N 118.913 0.2 1 445 113 113 SER H H 8.404 0.01 1 446 113 113 SER C C 172.93 0.3 1 447 113 113 SER CA C 59.025 0.3 1 448 113 113 SER CB C 63.856 0.3 1 449 113 113 SER N N 111.794 0.2 1 450 114 114 THR H H 8.142 0.01 1 451 114 114 THR C C 173.846 0.3 1 452 114 114 THR CA C 60.145 0.3 1 453 114 114 THR CB C 68.328 0.3 1 454 114 114 THR N N 114.794 0.2 1 455 115 115 LEU H H 7.41 0.01 1 456 115 115 LEU C C 173.381 0.3 1 457 115 115 LEU CA C 53.161 0.3 1 458 115 115 LEU CB C 40.522 0.3 1 459 115 115 LEU N N 118.697 0.2 1 460 116 116 PRO C C 173.455 0.3 1 461 116 116 PRO CA C 61.112 0.3 1 462 116 116 PRO CB C 26.73 0.3 1 463 117 117 ILE H H 7.875 0.01 1 464 117 117 ILE C C 173.946 0.3 1 465 117 117 ILE CA C 67.139 0.3 1 466 117 117 ILE CB C 37.027 0.3 1 467 117 117 ILE N N 120.533 0.2 1 468 118 118 LYS H H 8.352 0.01 1 469 118 118 LYS C C 176.707 0.3 1 470 118 118 LYS CA C 59.993 0.3 1 471 118 118 LYS CB C 30.797 0.3 1 472 118 118 LYS N N 120.734 0.2 1 473 119 119 LYS H H 7.677 0.01 1 474 119 119 LYS C C 177.069 0.3 1 475 119 119 LYS CA C 59.19 0.3 1 476 119 119 LYS CB C 31.951 0.3 1 477 119 119 LYS N N 120.123 0.2 1 478 120 120 ILE H H 8.305 0.01 1 479 120 120 ILE C C 173.879 0.3 1 480 120 120 ILE CA C 65.773 0.3 1 481 120 120 ILE CB C 36.831 0.3 1 482 120 120 ILE N N 119.471 0.2 1 483 121 121 MET H H 8.118 0.01 1 484 121 121 MET C C 174.912 0.3 1 485 121 121 MET CA C 58.389 0.3 1 486 121 121 MET CB C 30.906 0.3 1 487 121 121 MET N N 117.842 0.2 1 488 122 122 LYS H H 7.676 0.01 1 489 122 122 LYS C C 176.146 0.3 1 490 122 122 LYS CA C 59.114 0.3 1 491 122 122 LYS CB C 31.662 0.3 1 492 122 122 LYS N N 117.992 0.2 1 493 123 123 LYS H H 7.635 0.01 1 494 123 123 LYS C C 173.243 0.3 1 495 123 123 LYS CA C 57.403 0.3 1 496 123 123 LYS CB C 30.273 0.3 1 497 123 123 LYS N N 119.147 0.2 1 498 124 124 LEU H H 8.476 0.01 1 499 124 124 LEU C C 176.519 0.3 1 500 124 124 LEU CA C 57.988 0.3 1 501 124 124 LEU CB C 38.615 0.3 1 502 124 124 LEU N N 118.469 0.2 1 503 125 125 HIS H H 8.208 0.01 1 504 125 125 HIS C C 176.804 0.3 1 505 125 125 HIS CA C 57.487 0.3 1 506 125 125 HIS CB C 27.262 0.3 1 507 125 125 HIS N N 116.966 0.2 1 508 126 126 GLU H H 8.271 0.01 1 509 126 126 GLU C C 175.034 0.3 1 510 126 126 GLU CA C 58.326 0.3 1 511 126 126 GLU CB C 27.483 0.3 1 512 126 126 GLU N N 120.802 0.2 1 513 127 127 ARG H H 7.502 0.01 1 514 127 127 ARG C C 173.123 0.3 1 515 127 127 ARG CA C 54.176 0.3 1 516 127 127 ARG CB C 29.255 0.3 1 517 127 127 ARG N N 116.243 0.2 1 518 128 128 GLY H H 7.86 0.01 1 519 128 128 GLY C C 171.304 0.3 1 520 128 128 GLY CA C 45.4 0.3 1 521 128 128 GLY N N 108.33 0.2 1 522 129 129 ILE H H 7.968 0.01 1 523 129 129 ILE C C 170.858 0.3 1 524 129 129 ILE CA C 58.084 0.3 1 525 129 129 ILE CB C 38.533 0.3 1 526 129 129 ILE N N 122.669 0.2 1 527 130 130 PRO C C 173.886 0.3 1 528 130 130 PRO CA C 62.693 0.3 1 529 130 130 PRO CB C 31.239 0.3 1 530 131 131 ALA H H 8.153 0.01 1 531 131 131 ALA C C 173.095 0.3 1 532 131 131 ALA CA C 50.768 0.3 1 533 131 131 ALA CB C 22.795 0.3 1 534 131 131 ALA N N 122.624 0.2 1 535 132 132 TYR H H 8.658 0.01 1 536 132 132 TYR C C 169.946 0.3 1 537 132 132 TYR CA C 55.916 0.3 1 538 132 132 TYR CB C 40.269 0.3 1 539 132 132 TYR N N 118.281 0.2 1 540 133 133 ILE H H 8.67 0.01 1 541 133 133 ILE C C 173.187 0.3 1 542 133 133 ILE CA C 60.076 0.3 1 543 133 133 ILE CB C 38.127 0.3 1 544 133 133 ILE N N 120.546 0.2 1 545 134 134 SER H H 8.472 0.01 1 546 134 134 SER C C 170.81 0.3 1 547 134 134 SER CA C 55.714 0.3 1 548 134 134 SER CB C 63.685 0.3 1 549 134 134 SER N N 122.064 0.2 1 550 135 135 ASN H H 8.82 0.01 1 551 135 135 ASN C C 172.175 0.3 1 552 135 135 ASN CA C 53.285 0.3 1 553 135 135 ASN CB C 39.304 0.3 1 554 135 135 ASN N N 124.305 0.2 1 555 136 136 SER C C 171.14 0.3 1 556 136 136 SER CA C 57.754 0.3 1 557 136 136 SER CB C 63.829 0.3 1 558 137 137 ALA H H 8.8 0.01 1 559 137 137 ALA C C 175.098 0.3 1 560 137 137 ALA CA C 51.705 0.3 1 561 137 137 ALA CB C 18.719 0.3 1 562 137 137 ALA N N 128.255 0.2 1 563 138 138 GLY H H 8.155 0.01 1 564 138 138 GLY C C 169.833 0.3 1 565 138 138 GLY CA C 44.297 0.3 1 566 138 138 GLY N N 108.007 0.2 1 567 139 139 LEU H H 7.619 0.01 1 568 139 139 LEU C C 176.148 0.3 1 569 139 139 LEU CA C 53.159 0.3 1 570 139 139 LEU CB C 41.075 0.3 1 571 139 139 LEU N N 118.175 0.2 1 572 143 143 ASN C C 172.205 0.3 1 573 143 143 ASN CA C 57.396 0.3 1 574 143 143 ASN CB C 39.913 0.3 1 575 144 144 TYR H H 7.826 0.01 1 576 144 144 TYR C C 174.207 0.3 1 577 144 144 TYR CA C 60.837 0.3 1 578 144 144 TYR CB C 39.105 0.3 1 579 144 144 TYR N N 119.892 0.2 1 580 145 145 VAL H H 8.054 0.01 1 581 145 145 VAL C C 173.715 0.3 1 582 145 145 VAL CA C 66.028 0.3 1 583 145 145 VAL CB C 31.313 0.3 1 584 145 145 VAL N N 115.95 0.2 1 585 146 146 MET H H 8.17 0.01 1 586 146 146 MET C C 175.677 0.3 1 587 146 146 MET CA C 58.959 0.3 1 588 146 146 MET CB C 31.28 0.3 1 589 146 146 MET N N 118.321 0.2 1 590 147 147 TYR H H 9.161 0.01 1 591 147 147 TYR C C 174.85 0.3 1 592 147 147 TYR CA C 63.052 0.3 1 593 147 147 TYR CB C 38.325 0.3 1 594 147 147 TYR N N 118.607 0.2 1 595 148 148 LEU H H 8.149 0.01 1 596 148 148 LEU C C 177.732 0.3 1 597 148 148 LEU CA C 57.681 0.3 1 598 148 148 LEU CB C 41.449 0.3 1 599 148 148 LEU N N 117.945 0.2 1 600 149 149 SER H H 8.12 0.01 1 601 149 149 SER C C 174.367 0.3 1 602 149 149 SER CA C 61.331 0.3 1 603 149 149 SER CB C 62.619 0.3 1 604 149 149 SER N N 115.976 0.2 1 605 150 150 LEU H H 7.573 0.01 1 606 150 150 LEU C C 176.938 0.3 1 607 150 150 LEU CA C 57.314 0.3 1 608 150 150 LEU CB C 40.482 0.3 1 609 150 150 LEU N N 118.865 0.2 1 610 151 151 HIS H H 8.929 0.01 1 611 151 151 HIS C C 174.452 0.3 1 612 151 151 HIS CA C 58.258 0.3 1 613 151 151 HIS CB C 27.695 0.3 1 614 151 151 HIS N N 119.539 0.2 1 615 152 152 HIS C C 174.053 0.3 1 616 152 152 HIS CA C 59.25 0.3 1 617 152 152 HIS CB C 27.325 0.3 1 618 153 153 SER H H 7.7 0.01 1 619 153 153 SER C C 174.082 0.3 1 620 153 153 SER CA C 60.691 0.3 1 621 153 153 SER CB C 62.48 0.3 1 622 153 153 SER N N 113.184 0.2 1 623 154 154 ALA H H 7.317 0.01 1 624 154 154 ALA C C 176.323 0.3 1 625 154 154 ALA CA C 54.002 0.3 1 626 154 154 ALA CB C 18.333 0.3 1 627 154 154 ALA N N 119.999 0.2 1 628 155 155 THR H H 7.287 0.01 1 629 155 155 THR C C 173.64 0.3 1 630 155 155 THR CA C 62.206 0.3 1 631 155 155 THR CB C 69.619 0.3 1 632 155 155 THR N N 104.94 0.2 1 633 156 156 LYS H H 7.932 0.01 1 634 156 156 LYS C C 174.826 0.3 1 635 156 156 LYS CA C 54.237 0.3 1 636 156 156 LYS CB C 32.514 0.3 1 637 156 156 LYS N N 117.977 0.2 1 638 157 157 GLY H H 7.459 0.01 1 639 157 157 GLY C C 169.796 0.3 1 640 157 157 GLY CA C 45.179 0.3 1 641 157 157 GLY N N 106.817 0.2 1 642 158 158 TYR H H 6.71 0.01 1 643 158 158 TYR C C 169.979 0.3 1 644 158 158 TYR CA C 54.053 0.3 1 645 158 158 TYR CB C 37.911 0.3 1 646 158 158 TYR N N 113.22 0.2 1 647 159 159 PRO C C 169.615 0.3 1 648 159 159 PRO CA C 61.151 0.3 1 649 159 159 PRO CB C 33.6 0.3 1 650 160 160 LYS H H 8.611 0.01 1 651 160 160 LYS C C 174.015 0.3 1 652 160 160 LYS CA C 58.272 0.3 1 653 160 160 LYS CB C 31.885 0.3 1 654 160 160 LYS N N 124.9 0.2 1 655 161 161 MET H H 7.343 0.01 1 656 161 161 MET C C 172.143 0.3 1 657 161 161 MET CA C 53.428 0.3 1 658 161 161 MET CB C 37.444 0.3 1 659 161 161 MET N N 113.088 0.2 1 660 162 162 SER H H 8.41 0.01 1 661 162 162 SER C C 171.186 0.3 1 662 162 162 SER CA C 54.954 0.3 1 663 162 162 SER CB C 63.053 0.3 1 664 162 162 SER N N 116.066 0.2 1 665 163 163 GLY H H 7.789 0.01 1 666 163 163 GLY C C 166.57 0.3 1 667 163 163 GLY CA C 45.677 0.3 1 668 163 163 GLY N N 111.803 0.2 1 669 164 164 PHE H H 8.853 0.01 1 670 164 164 PHE C C 171.614 0.3 1 671 164 164 PHE CA C 55.141 0.3 1 672 164 164 PHE CB C 45.078 0.3 1 673 164 164 PHE N N 121.413 0.2 1 674 165 165 ILE H H 8.653 0.01 1 675 165 165 ILE C C 170.897 0.3 1 676 165 165 ILE CA C 59.07 0.3 1 677 165 165 ILE CB C 41.153 0.3 1 678 165 165 ILE N N 127.288 0.2 1 679 166 166 HIS H H 9.632 0.01 1 680 166 166 HIS C C 172.863 0.3 1 681 166 166 HIS CA C 54.215 0.3 1 682 166 166 HIS CB C 30.213 0.3 1 683 166 166 HIS N N 122.775 0.2 1 684 167 167 VAL H H 9.096 0.01 1 685 167 167 VAL C C 170.151 0.3 1 686 167 167 VAL CA C 56.391 0.3 1 687 167 167 VAL CB C 31.249 0.3 1 688 167 167 VAL N N 114.797 0.2 1 689 176 176 ASP C C 172.386 0.3 1 690 176 176 ASP CA C 52.908 0.3 1 691 176 176 ASP CB C 37.688 0.3 1 692 177 177 LYS H H 8.011 0.01 1 693 177 177 LYS C C 173.588 0.3 1 694 177 177 LYS CA C 55.68 0.3 1 695 177 177 LYS CB C 32.156 0.3 1 696 177 177 LYS N N 120.851 0.2 1 697 178 178 ILE H H 7.835 0.01 1 698 178 178 ILE C C 174.088 0.3 1 699 178 178 ILE CA C 61.178 0.3 1 700 178 178 ILE CB C 37.733 0.3 1 701 178 178 ILE N N 120.75 0.2 1 702 179 179 GLY H H 8.385 0.01 1 703 179 179 GLY C C 171.418 0.3 1 704 179 179 GLY CA C 44.801 0.3 1 705 179 179 GLY N N 112.852 0.2 1 706 180 180 LYS H H 8.171 0.01 1 707 180 180 LYS C C 174.187 0.3 1 708 180 180 LYS CA C 55.768 0.3 1 709 180 180 LYS CB C 31.797 0.3 1 710 180 180 LYS N N 120.814 0.2 1 711 181 181 GLY H H 8.304 0.01 1 712 181 181 GLY C C 170.881 0.3 1 713 181 181 GLY CA C 44.614 0.3 1 714 181 181 GLY N N 109.594 0.2 1 715 182 182 GLN H H 8.111 0.01 1 716 182 182 GLN C C 173.131 0.3 1 717 182 182 GLN CA C 55.023 0.3 1 718 182 182 GLN CB C 28.777 0.3 1 719 182 182 GLN N N 119.708 0.2 1 720 183 183 VAL H H 8.297 0.01 1 721 183 183 VAL C C 171.442 0.3 1 722 183 183 VAL CA C 59.465 0.3 1 723 183 183 VAL CB C 31.805 0.3 1 724 183 183 VAL N N 123.883 0.2 1 725 188 188 SER C C 172.662 0.3 1 726 188 188 SER CA C 57.515 0.3 1 727 188 188 SER CB C 63.978 0.3 1 728 189 189 TYR H H 9.267 0.01 1 729 189 189 TYR C C 174.175 0.3 1 730 189 189 TYR CA C 62.177 0.3 1 731 189 189 TYR CB C 37.473 0.3 1 732 189 189 TYR N N 124.43 0.2 1 733 190 190 GLU H H 8.492 0.01 1 734 190 190 GLU C C 175.898 0.3 1 735 190 190 GLU CA C 58.753 0.3 1 736 190 190 GLU CB C 26.606 0.3 1 737 190 190 GLU N N 114.865 0.2 1 738 191 191 MET H H 7.469 0.01 1 739 191 191 MET C C 174.51 0.3 1 740 191 191 MET CA C 58.731 0.3 1 741 191 191 MET CB C 32.687 0.3 1 742 191 191 MET N N 119.063 0.2 1 743 192 192 GLU H H 7.49 0.01 1 744 192 192 GLU C C 174.637 0.3 1 745 192 192 GLU CA C 59.642 0.3 1 746 192 192 GLU CB C 26.861 0.3 1 747 192 192 GLU N N 118.943 0.2 1 748 193 193 LEU H H 7.951 0.01 1 749 193 193 LEU C C 175.933 0.3 1 750 193 193 LEU CA C 57.546 0.3 1 751 193 193 LEU CB C 40.46 0.3 1 752 193 193 LEU N N 118.163 0.2 1 753 194 194 GLU H H 7.875 0.01 1 754 194 194 GLU C C 174.937 0.3 1 755 194 194 GLU CA C 57.795 0.3 1 756 194 194 GLU CB C 26.806 0.3 1 757 194 194 GLU N N 117.142 0.2 1 758 195 195 ALA H H 8.323 0.01 1 759 195 195 ALA C C 176.282 0.3 1 760 195 195 ALA CA C 54.212 0.3 1 761 195 195 ALA CB C 18.109 0.3 1 762 195 195 ALA N N 119.988 0.2 1 763 196 196 VAL H H 7.449 0.01 1 764 196 196 VAL C C 174.676 0.3 1 765 196 196 VAL CA C 66.485 0.3 1 766 196 196 VAL CB C 30.208 0.3 1 767 196 196 VAL N N 116.07 0.2 1 768 197 197 LYS H H 8.001 0.01 1 769 197 197 LYS C C 175.987 0.3 1 770 197 197 LYS CA C 61.068 0.3 1 771 197 197 LYS CB C 31.096 0.3 1 772 197 197 LYS N N 119.18 0.2 1 773 198 198 VAL H H 8.614 0.01 1 774 198 198 VAL C C 174.578 0.3 1 775 198 198 VAL CA C 65.681 0.3 1 776 198 198 VAL CB C 30.092 0.3 1 777 198 198 VAL N N 119.435 0.2 1 778 199 199 ALA H H 7.824 0.01 1 779 199 199 ALA C C 175.751 0.3 1 780 199 199 ALA CA C 55.155 0.3 1 781 199 199 ALA CB C 16.872 0.3 1 782 199 199 ALA N N 120.41 0.2 1 783 200 200 ILE H H 7.873 0.01 1 784 200 200 ILE C C 174.118 0.3 1 785 200 200 ILE CA C 65.774 0.3 1 786 200 200 ILE CB C 37.441 0.3 1 787 200 200 ILE N N 115.2 0.2 1 788 201 201 GLU H H 8.252 0.01 1 789 201 201 GLU C C 176.264 0.3 1 790 201 201 GLU CA C 58.89 0.3 1 791 201 201 GLU CB C 27.092 0.3 1 792 201 201 GLU N N 117.484 0.2 1 793 202 202 VAL H H 8.53 0.01 1 794 202 202 VAL C C 175.439 0.3 1 795 202 202 VAL CA C 65.195 0.3 1 796 202 202 VAL CB C 30.734 0.3 1 797 202 202 VAL N N 118.757 0.2 1 798 203 203 ALA H H 7.884 0.01 1 799 203 203 ALA C C 175.691 0.3 1 800 203 203 ALA CA C 55.704 0.3 1 801 203 203 ALA CB C 17.611 0.3 1 802 203 203 ALA N N 121.902 0.2 1 803 204 204 LEU H H 8.378 0.01 1 804 204 204 LEU C C 176.77 0.3 1 805 204 204 LEU CA C 57.467 0.3 1 806 204 204 LEU CB C 41.17 0.3 1 807 204 204 LEU N N 115.775 0.2 1 808 205 205 GLU H H 7.666 0.01 1 809 205 205 GLU C C 175.167 0.3 1 810 205 205 GLU CA C 57.551 0.3 1 811 205 205 GLU CB C 27.104 0.3 1 812 205 205 GLU N N 116.462 0.2 1 813 206 206 GLU H H 7.535 0.01 1 814 206 206 GLU C C 173.794 0.3 1 815 206 206 GLU CA C 55.827 0.3 1 816 206 206 GLU CB C 28.017 0.3 1 817 206 206 GLU N N 115.6 0.2 1 818 207 207 LEU H H 7.574 0.01 1 819 207 207 LEU C C 174.347 0.3 1 820 207 207 LEU CA C 55.185 0.3 1 821 207 207 LEU CB C 41.606 0.3 1 822 207 207 LEU N N 119.733 0.2 1 823 208 208 LEU H H 7.627 0.01 1 824 208 208 LEU C C 176.342 0.3 1 825 208 208 LEU CA C 54.175 0.3 1 826 208 208 LEU CB C 41.213 0.3 1 827 208 208 LEU N N 121.551 0.2 1 stop_ save_ save_A199P_pH3.0_25C _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC-NOESY-HSQC stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $condition_2 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'PCP homo tetramer subunit 1' _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 LYS H H 9.86 0.01 1 2 2 2 LYS N N 123.599 0.2 1 3 3 3 VAL H H 9.192 0.01 1 4 3 3 VAL N N 123.217 0.2 1 5 4 4 LEU H H 8.969 0.01 1 6 4 4 LEU N N 127.988 0.2 1 7 5 5 VAL H H 9.35 0.01 1 8 5 5 VAL N N 127.624 0.2 1 9 6 6 THR H H 8.236 0.01 1 10 6 6 THR N N 112.423 0.2 1 11 7 7 GLY H H 7.5 0.01 1 12 7 7 GLY N N 107.39 0.2 1 13 11 11 PHE H H 7.527 0.01 1 14 11 11 PHE N N 119.126 0.2 1 15 12 12 GLY H H 8.638 0.01 1 16 12 12 GLY N N 109.65 0.2 1 17 13 13 GLY H H 8.61 0.01 1 18 13 13 GLY N N 110.539 0.2 1 19 14 14 GLU H H 7.544 0.01 1 20 14 14 GLU N N 119.317 0.2 1 21 15 15 LYS H H 8.497 0.01 1 22 15 15 LYS N N 121.009 0.2 1 23 16 16 ILE H H 7.984 0.01 1 24 16 16 ILE N N 116.232 0.2 1 25 17 17 ASN H H 8.307 0.01 1 26 17 17 ASN N N 121.463 0.2 1 27 19 19 THR H H 8.459 0.01 1 28 19 19 THR N N 107.39 0.2 1 29 20 20 GLU H H 7.318 0.01 1 30 20 20 GLU N N 124.849 0.2 1 31 21 21 ARG H H 6.742 0.01 1 32 21 21 ARG N N 118.557 0.2 1 33 22 22 ILE H H 8.139 0.01 1 34 22 22 ILE N N 119.472 0.2 1 35 23 23 ALA H H 7.21 0.01 1 36 23 23 ALA N N 118.651 0.2 1 37 24 24 LYS H H 7.449 0.01 1 38 24 24 LYS N N 114.032 0.2 1 39 25 25 ASP H H 8.697 0.01 1 40 25 25 ASP N N 119.715 0.2 1 41 26 26 LEU H H 7.602 0.01 1 42 26 26 LEU N N 117.256 0.2 1 43 27 27 ASP H H 6.998 0.01 1 44 27 27 ASP N N 116.947 0.2 1 45 28 28 GLY H H 8.464 0.01 1 46 28 28 GLY N N 114.836 0.2 1 47 29 29 ILE H H 7.265 0.01 1 48 29 29 ILE N N 117.028 0.2 1 49 30 30 LYS H H 8.012 0.01 1 50 30 30 LYS N N 119.907 0.2 1 51 31 31 ILE H H 7.988 0.01 1 52 31 31 ILE N N 123.968 0.2 1 53 32 32 GLY H H 8.747 0.01 1 54 32 32 GLY N N 116.601 0.2 1 55 33 33 ASP H H 8.545 0.01 1 56 33 33 ASP N N 123.147 0.2 1 57 34 34 ALA H H 8.369 0.01 1 58 34 34 ALA N N 123.813 0.2 1 59 35 35 GLN H H 7.851 0.01 1 60 35 35 GLN N N 120.484 0.2 1 61 36 36 VAL H H 8.336 0.01 1 62 36 36 VAL N N 124.735 0.2 1 63 37 37 PHE H H 9.385 0.01 1 64 37 37 PHE N N 127.55 0.2 1 65 38 38 GLY H H 9.876 0.01 1 66 38 38 GLY N N 112.124 0.2 1 67 39 39 ARG H H 8.663 0.01 1 68 39 39 ARG N N 124.055 0.2 1 69 40 40 VAL H H 8.568 0.01 1 70 40 40 VAL N N 120.929 0.2 1 71 41 41 LEU H H 9.051 0.01 1 72 41 41 LEU N N 127.403 0.2 1 73 43 43 VAL H H 7.675 0.01 1 74 43 43 VAL N N 104.526 0.2 1 75 44 44 VAL H H 6.6 0.01 1 76 44 44 VAL N N 118.437 0.2 1 77 45 45 PHE H H 8.412 0.01 1 78 45 45 PHE N N 126.159 0.2 1 79 46 46 GLY H H 8.836 0.01 1 80 46 46 GLY N N 106.009 0.2 1 81 47 47 LYS H H 6.976 0.01 1 82 47 47 LYS N N 119.554 0.2 1 83 48 48 ALA H H 8.664 0.01 1 84 48 48 ALA N N 122.175 0.2 1 85 49 49 LYS H H 8.254 0.01 1 86 49 49 LYS N N 116.116 0.2 1 87 50 50 GLU H H 7.442 0.01 1 88 50 50 GLU N N 117.226 0.2 1 89 51 51 VAL H H 8.626 0.01 1 90 51 51 VAL N N 118.233 0.2 1 91 52 52 LEU H H 8.898 0.01 1 92 52 52 LEU N N 123.658 0.2 1 93 53 53 GLU H H 8.471 0.01 1 94 53 53 GLU N N 116.428 0.2 1 95 54 54 LYS H H 7.868 0.01 1 96 54 54 LYS N N 117.977 0.2 1 97 55 55 THR H H 8.221 0.01 1 98 55 55 THR N N 115.446 0.2 1 99 56 56 LEU H H 8.402 0.01 1 100 56 56 LEU N N 119.731 0.2 1 101 57 57 GLU H H 7.764 0.01 1 102 57 57 GLU N N 116.534 0.2 1 103 58 58 GLU H H 8.027 0.01 1 104 58 58 GLU N N 117.948 0.2 1 105 59 59 ILE H H 7.722 0.01 1 106 59 59 ILE N N 116.448 0.2 1 107 60 60 LYS H H 7.655 0.01 1 108 60 60 LYS N N 112.81 0.2 1 109 62 62 ASP H H 8.461 0.01 1 110 62 62 ASP N N 117.217 0.2 1 111 63 63 ILE H H 7.467 0.01 1 112 63 63 ILE N N 115.765 0.2 1 113 64 64 ALA H H 8.639 0.01 1 114 64 64 ALA N N 129.543 0.2 1 115 65 65 ILE H H 8.683 0.01 1 116 65 65 ILE N N 120.903 0.2 1 117 66 66 HIS H H 7.933 0.01 1 118 66 66 HIS N N 126.54 0.2 1 119 72 72 GLY H H 8.271 0.01 1 120 72 72 GLY N N 108.923 0.2 1 121 73 73 ARG H H 7.576 0.01 1 122 73 73 ARG N N 118.536 0.2 1 123 74 74 SER H H 8.745 0.01 1 124 74 74 SER N N 113.386 0.2 1 125 75 75 ALA H H 7.407 0.01 1 126 75 75 ALA N N 122.845 0.2 1 127 79 79 GLU H H 8.18 0.01 1 128 79 79 GLU N N 124.75 0.2 1 129 80 80 ARG H H 9.048 0.01 1 130 80 80 ARG N N 124.254 0.2 1 131 83 83 VAL H H 9.257 0.01 1 132 83 83 VAL N N 117.184 0.2 1 133 93 93 ASN H H 8.288 0.01 1 134 93 93 ASN N N 117.932 0.2 1 135 94 94 GLU H H 8.248 0.01 1 136 94 94 GLU N N 119.017 0.2 1 137 95 95 GLY H H 8.247 0.01 1 138 95 95 GLY N N 108.743 0.2 1 139 96 96 LYS H H 7.993 0.01 1 140 96 96 LYS N N 120.048 0.2 1 141 97 97 LYS H H 8.186 0.01 1 142 97 97 LYS N N 121.605 0.2 1 143 98 98 ILE H H 8.062 0.01 1 144 98 98 ILE N N 122.439 0.2 1 145 99 99 GLU H H 8.328 0.01 1 146 99 99 GLU N N 124.455 0.2 1 147 100 100 ASP H H 8.244 0.01 1 148 100 100 ASP N N 120.651 0.2 1 149 104 104 VAL H H 8.474 0.01 1 150 104 104 VAL N N 117.104 0.2 1 151 106 106 GLY H H 8.945 0.01 1 152 106 106 GLY N N 113.524 0.2 1 153 107 107 ALA H H 7.153 0.01 1 154 107 107 ALA N N 123.835 0.2 1 155 109 109 THR H H 8.587 0.01 1 156 109 109 THR N N 117.207 0.2 1 157 110 110 ALA H H 7.334 0.01 1 158 110 110 ALA N N 118.7 0.2 1 159 111 111 TYR H H 8.688 0.01 1 160 111 111 TYR N N 115.457 0.2 1 161 112 112 PHE H H 8.658 0.01 1 162 112 112 PHE N N 118.967 0.2 1 163 113 113 SER H H 8.398 0.01 1 164 113 113 SER N N 112.052 0.2 1 165 114 114 THR H H 8.085 0.01 1 166 114 114 THR N N 114.753 0.2 1 167 115 115 LEU H H 7.375 0.01 1 168 115 115 LEU N N 118.598 0.2 1 169 118 118 LYS H H 8.289 0.01 1 170 118 118 LYS N N 120.839 0.2 1 171 121 121 MET H H 8.355 0.01 1 172 121 121 MET N N 117.853 0.2 1 173 124 124 LEU H H 8.572 0.01 1 174 124 124 LEU N N 118.778 0.2 1 175 125 125 HIS H H 8.048 0.01 1 176 125 125 HIS N N 116.428 0.2 1 177 126 126 GLU H H 8.256 0.01 1 178 126 126 GLU N N 121.39 0.2 1 179 127 127 ARG H H 7.5 0.01 1 180 127 127 ARG N N 115.844 0.2 1 181 128 128 GLY H H 7.806 0.01 1 182 128 128 GLY N N 108.194 0.2 1 183 129 129 ILE H H 7.83 0.01 1 184 129 129 ILE N N 122.308 0.2 1 185 132 132 TYR H H 8.578 0.01 1 186 132 132 TYR N N 117.69 0.2 1 187 133 133 ILE H H 8.624 0.01 1 188 133 133 ILE N N 120.244 0.2 1 189 134 134 SER H H 8.538 0.01 1 190 134 134 SER N N 122.787 0.2 1 191 135 135 ASN H H 8.774 0.01 1 192 135 135 ASN N N 123.897 0.2 1 193 137 137 ALA H H 8.86 0.01 1 194 137 137 ALA N N 128.774 0.2 1 195 144 144 TYR H H 7.832 0.01 1 196 144 144 TYR N N 119.538 0.2 1 197 145 145 VAL H H 7.936 0.01 1 198 145 145 VAL N N 116.167 0.2 1 199 146 146 MET H H 8.183 0.01 1 200 146 146 MET N N 118.615 0.2 1 201 147 147 TYR H H 9.133 0.01 1 202 147 147 TYR N N 118.332 0.2 1 203 148 148 LEU H H 8.127 0.01 1 204 148 148 LEU N N 117.852 0.2 1 205 150 150 LEU H H 7.463 0.01 1 206 150 150 LEU N N 118.748 0.2 1 207 151 151 HIS H H 8.924 0.01 1 208 151 151 HIS N N 120.127 0.2 1 209 153 153 SER H H 7.681 0.01 1 210 153 153 SER N N 112.859 0.2 1 211 154 154 ALA H H 7.351 0.01 1 212 154 154 ALA N N 120.209 0.2 1 213 155 155 THR H H 7.294 0.01 1 214 155 155 THR N N 104.928 0.2 1 215 156 156 LYS H H 7.942 0.01 1 216 156 156 LYS N N 118.031 0.2 1 217 157 157 GLY H H 7.454 0.01 1 218 157 157 GLY N N 106.588 0.2 1 219 158 158 TYR H H 6.668 0.01 1 220 158 158 TYR N N 113.382 0.2 1 221 160 160 LYS H H 8.631 0.01 1 222 160 160 LYS N N 124.969 0.2 1 223 161 161 MET H H 7.326 0.01 1 224 161 161 MET N N 113.078 0.2 1 225 163 163 GLY H H 7.868 0.01 1 226 163 163 GLY N N 112.457 0.2 1 227 164 164 PHE H H 8.886 0.01 1 228 164 164 PHE N N 121.186 0.2 1 229 165 165 ILE H H 8.589 0.01 1 230 165 165 ILE N N 127.836 0.2 1 231 166 166 HIS H H 9.425 0.01 1 232 166 166 HIS N N 122.345 0.2 1 233 167 167 VAL H H 9.112 0.01 1 234 167 167 VAL N N 115.217 0.2 1 235 178 178 ILE H H 7.661 0.01 1 236 178 178 ILE N N 120.238 0.2 1 237 179 179 GLY H H 8.475 0.01 1 238 179 179 GLY N N 113.14 0.2 1 239 180 180 LYS H H 8.106 0.01 1 240 180 180 LYS N N 120.439 0.2 1 241 181 181 GLY H H 8.224 0.01 1 242 181 181 GLY N N 109.252 0.2 1 243 182 182 GLN H H 8.139 0.01 1 244 182 182 GLN N N 119.896 0.2 1 245 183 183 VAL H H 8.349 0.01 1 246 183 183 VAL N N 124.368 0.2 1 247 189 189 TYR H H 9.35 0.01 1 248 189 189 TYR N N 124.651 0.2 1 249 190 190 GLU H H 8.548 0.01 1 250 190 190 GLU N N 114.725 0.2 1 251 191 191 MET H H 7.432 0.01 1 252 191 191 MET N N 119.108 0.2 1 253 192 192 GLU H H 7.664 0.01 1 254 192 192 GLU N N 118.907 0.2 1 255 193 193 LEU H H 7.94 0.01 1 256 193 193 LEU N N 117.101 0.2 1 257 196 196 VAL H H 8.101 0.01 1 258 196 196 VAL N N 116.616 0.2 1 259 197 197 LYS H H 7.783 0.01 1 260 197 197 LYS N N 118.82 0.2 1 261 198 198 VAL H H 7.09 0.01 1 262 198 198 VAL N N 112.787 0.2 1 263 201 201 GLU H H 8.269 0.01 1 264 201 201 GLU N N 118.733 0.2 1 265 202 202 VAL H H 8.438 0.01 1 266 202 202 VAL N N 117.843 0.2 1 267 203 203 ALA H H 8.154 0.01 1 268 203 203 ALA N N 121.909 0.2 1 269 204 204 LEU H H 8.1 0.01 1 270 204 204 LEU N N 115.809 0.2 1 271 205 205 GLU H H 7.488 0.01 1 272 205 205 GLU N N 116.276 0.2 1 273 206 206 GLU H H 7.561 0.01 1 274 206 206 GLU N N 116.142 0.2 1 275 207 207 LEU H H 7.568 0.01 1 276 207 207 LEU N N 118.98 0.2 1 277 208 208 LEU H H 7.516 0.01 1 278 208 208 LEU N N 122.82 0.2 1 stop_ save_