data_4996 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR-Based Structure of the Conserved Protein MTH865 from the Archea Methanobacterium thermoautotrophicum ; _BMRB_accession_number 4996 _BMRB_flat_file_name bmr4996.str _Entry_type original _Submission_date 2001-04-20 _Accession_date 2001-04-23 _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 Lee Gregory M. . 2 Edwards Aled M. . 3 Arrowsmith Cheryl H. . 4 McIntosh Lawrence P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 442 "13C chemical shifts" 324 "15N chemical shifts" 81 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-10-08 original author . stop_ _Original_release_date 2001-10-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: NMR-Based Structure of the Conserved Protein MTH865 from the Archaeon Methanobacterium thermoautotrophicum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Gregory M. . 2 Edwards Aled M. . 3 Arrowsmith Cheryl H. . 4 McIntosh Lawrence P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 63 _Page_last 66 _Year 2001 _Details . loop_ _Keyword 'helical bundle' 'heternuclear NMR' 'structural proteomics' 'Methanobacterium thermoautotrophicum' stop_ save_ ################################## # Molecular system description # ################################## save_system_MTH865 _Saveframe_category molecular_system _Mol_system_name MTH865 _Abbreviation_common MTH865 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MTH865 $MTH865 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'conserved archeal protein' 'unknown function' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MTH865 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Methanobacterium thermoautotrophicum open reading frame 865' _Abbreviation_common MTH865 _Molecular_mass 8675 _Mol_thiol_state 'all free' _Details ; Includes GSH at N-terminal from proteolytic cleavage of His6-affinity tag. ; ############################## # Polymer residue sequence # ############################## _Residue_count 84 _Mol_residue_sequence ; GSHMKMGVKEDIRGQIIGAL AGADFPINSPEELMAALPNG PDTTCKSGDVELKASDAGQV LTADDFPFKSAEEVADTIVN KAGL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 SER 3 -1 HIS 4 1 MET 5 2 LYS 6 3 MET 7 4 GLY 8 5 VAL 9 6 LYS 10 7 GLU 11 8 ASP 12 9 ILE 13 10 ARG 14 11 GLY 15 12 GLN 16 13 ILE 17 14 ILE 18 15 GLY 19 16 ALA 20 17 LEU 21 18 ALA 22 19 GLY 23 20 ALA 24 21 ASP 25 22 PHE 26 23 PRO 27 24 ILE 28 25 ASN 29 26 SER 30 27 PRO 31 28 GLU 32 29 GLU 33 30 LEU 34 31 MET 35 32 ALA 36 33 ALA 37 34 LEU 38 35 PRO 39 36 ASN 40 37 GLY 41 38 PRO 42 39 ASP 43 40 THR 44 41 THR 45 42 CYS 46 43 LYS 47 44 SER 48 45 GLY 49 46 ASP 50 47 VAL 51 48 GLU 52 49 LEU 53 50 LYS 54 51 ALA 55 52 SER 56 53 ASP 57 54 ALA 58 55 GLY 59 56 GLN 60 57 VAL 61 58 LEU 62 59 THR 63 60 ALA 64 61 ASP 65 62 ASP 66 63 PHE 67 64 PRO 68 65 PHE 69 66 LYS 70 67 SER 71 68 ALA 72 69 GLU 73 70 GLU 74 71 VAL 75 72 ALA 76 73 ASP 77 74 THR 78 75 ILE 79 76 VAL 80 77 ASN 81 78 LYS 82 79 ALA 83 80 GLY 84 81 LEU 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 PDB 1IIO "Nmr-Based Structure Of The Conserved Protein Mth865 From The Archea Methanobacterium Thermoautotrophicum" 100.00 84 100.00 100.00 2.32e-52 DBJ BAM70032 "conserved hypothetical protein [Methanothermobacter thermautotrophicus CaT2]" 94.05 79 100.00 100.00 6.20e-48 EMBL CAA48863 "unnamed protein product [Methanothermobacter thermautotrophicus]" 94.05 79 100.00 100.00 6.20e-48 EMBL CAA48865 "unnamed protein product [Methanothermobacter thermautotrophicus]" 94.05 79 100.00 100.00 6.20e-48 GB AAB85363 "conserved protein [Methanothermobacter thermautotrophicus str. Delta H]" 96.43 81 100.00 100.00 1.47e-49 REF NP_276002 "hypothetical protein MTH865 [Methanothermobacter thermautotrophicus str. Delta H]" 96.43 81 100.00 100.00 1.47e-49 REF WP_010876498 "hypothetical protein [Methanothermobacter thermautotrophicus]" 96.43 81 100.00 100.00 1.47e-49 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MTH865 'Methanothermobacter thermautotrophicus' 145262 Archaea Euryarchaeota Methanothermobacter thermautotrophicus 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 $MTH865 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N-labeled_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MTH865 0.5 mM '[U-100% 15N]' stop_ save_ save_13C_15N-labeled_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MTH865 0.5 mM '[U-100% 13C; U-100% 15N]' stop_ save_ save_10%_13C-labeled_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MTH865 0.5 mM '[U-10% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2000 loop_ _Task 'raw data processing' 'peak picking' 'peak assignments' stop_ _Details ; Molecular Simulations, Inc., San Diego, CA ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_500MHz_Unity_housed_at_Univ._of_British_Columbia_1 _Saveframe_category NMR_applied_experiment _Experiment_name '500MHz Unity housed at Univ. of British Columbia' _Sample_label . save_ save_600MHz_INOVA_housed_at_Univ._of_Toronto_2 _Saveframe_category NMR_applied_experiment _Experiment_name '600MHz INOVA housed at Univ. of Toronto' _Sample_label . save_ save_800MHz_INOVA_housed_at_Univ._of_Alberta_3 _Saveframe_category NMR_applied_experiment _Experiment_name '800MHz INOVA housed at Univ. of Alberta' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.51 0.05 n/a temperature 303 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shifts _Saveframe_category assigned_chemical_shifts _Details 'Residues Gly-3 to Met1 unobserved in the spectra.' loop_ _Sample_label $15N-labeled_sample $13C_15N-labeled_sample $10%_13C-labeled_sample stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MTH865 _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 . 5 LYS H H 8.411 0.020 1 2 . 5 LYS HA H 4.302 0.020 1 3 . 5 LYS HB2 H 1.846 0.020 2 4 . 5 LYS HB3 H 1.779 0.020 2 5 . 5 LYS HG2 H 1.446 0.020 2 6 . 5 LYS HG3 H 1.498 0.020 2 7 . 5 LYS HD2 H 1.712 0.020 1 8 . 5 LYS HD3 H 1.712 0.020 1 9 . 5 LYS HE2 H 3.074 0.020 1 10 . 5 LYS HE3 H 3.074 0.020 1 11 . 5 LYS C C 176.445 0.300 1 12 . 5 LYS CA C 56.225 0.300 1 13 . 5 LYS CB C 33.012 0.300 1 14 . 5 LYS CG C 24.058 0.300 1 15 . 5 LYS CD C 29.065 0.300 1 16 . 5 LYS CE C 42.304 0.300 1 17 . 5 LYS N N 122.806 0.200 1 18 . 6 MET H H 8.391 0.020 1 19 . 6 MET HA H 4.413 0.020 1 20 . 6 MET HB2 H 2.025 0.020 1 21 . 6 MET HB3 H 2.025 0.020 1 22 . 6 MET HG2 H 2.567 0.020 1 23 . 6 MET HG3 H 2.567 0.020 1 24 . 6 MET HE H 2.069 0.020 1 25 . 6 MET C C 176.610 0.300 1 26 . 6 MET CA C 56.031 0.300 1 27 . 6 MET CB C 33.645 0.300 1 28 . 6 MET CG C 31.965 0.300 1 29 . 6 MET CE C 17.131 0.300 1 30 . 6 MET N N 122.119 0.200 1 31 . 7 GLY H H 8.545 0.020 1 32 . 7 GLY HA2 H 4.012 0.020 2 33 . 7 GLY HA3 H 4.101 0.020 2 34 . 7 GLY C C 175.346 0.300 1 35 . 7 GLY CA C 45.254 0.300 1 36 . 7 GLY N N 110.963 0.200 1 37 . 8 VAL H H 7.964 0.020 1 38 . 8 VAL HA H 3.864 0.020 1 39 . 8 VAL HB H 2.069 0.020 1 40 . 8 VAL HG1 H 0.975 0.020 1 41 . 8 VAL HG2 H 1.064 0.020 1 42 . 8 VAL C C 177.882 0.300 1 43 . 8 VAL CA C 65.460 0.300 1 44 . 8 VAL CB C 32.300 0.300 1 45 . 8 VAL CG1 C 21.746 0.300 1 46 . 8 VAL CG2 C 22.118 0.300 1 47 . 8 VAL N N 120.588 0.200 1 48 . 9 LYS H H 8.358 0.020 1 49 . 9 LYS HA H 3.605 0.020 1 50 . 9 LYS HB2 H 1.824 0.020 2 51 . 9 LYS HB3 H 1.758 0.020 2 52 . 9 LYS HG2 H 1.198 0.020 2 53 . 9 LYS HG3 H 1.148 0.020 2 54 . 9 LYS HD2 H 1.644 0.020 1 55 . 9 LYS HD3 H 1.644 0.020 1 56 . 9 LYS HE2 H 2.737 0.020 2 57 . 9 LYS HE3 H 2.895 0.020 2 58 . 9 LYS C C 177.533 0.300 1 59 . 9 LYS CA C 60.818 0.300 1 60 . 9 LYS CB C 32.401 0.300 1 61 . 9 LYS CG C 25.152 0.300 1 62 . 9 LYS CD C 29.537 0.300 1 63 . 9 LYS CE C 42.297 0.300 1 64 . 9 LYS N N 119.275 0.200 1 65 . 10 GLU H H 8.192 0.020 1 66 . 10 GLU HA H 3.915 0.020 1 67 . 10 GLU HB2 H 2.001 0.020 1 68 . 10 GLU HB3 H 2.001 0.020 1 69 . 10 GLU HG2 H 2.287 0.020 2 70 . 10 GLU HG3 H 2.443 0.020 2 71 . 10 GLU C C 179.161 0.300 1 72 . 10 GLU CA C 59.310 0.300 1 73 . 10 GLU CB C 29.211 0.300 1 74 . 10 GLU CG C 36.816 0.300 1 75 . 10 GLU N N 116.650 0.200 1 76 . 11 ASP H H 8.213 0.020 1 77 . 11 ASP HA H 4.503 0.020 1 78 . 11 ASP HB2 H 2.905 0.020 2 79 . 11 ASP HB3 H 2.805 0.020 2 80 . 11 ASP C C 179.048 0.300 1 81 . 11 ASP CA C 56.317 0.300 1 82 . 11 ASP CB C 41.281 0.300 1 83 . 11 ASP N N 121.463 0.200 1 84 . 12 ILE H H 8.587 0.020 1 85 . 12 ILE HA H 3.386 0.020 1 86 . 12 ILE HB H 1.891 0.020 1 87 . 12 ILE HG12 H 1.094 0.020 2 88 . 12 ILE HG13 H 1.504 0.020 2 89 . 12 ILE HG2 H 0.658 0.020 1 90 . 12 ILE HD1 H 0.529 0.020 1 91 . 12 ILE C C 177.422 0.300 1 92 . 12 ILE CA C 64.840 0.300 1 93 . 12 ILE CB C 35.879 0.300 1 94 . 12 ILE CG1 C 29.517 0.300 1 95 . 12 ILE CG2 C 17.548 0.300 1 96 . 12 ILE CD1 C 11.702 0.300 1 97 . 12 ILE N N 119.306 0.200 1 98 . 13 ARG H H 8.557 0.020 1 99 . 13 ARG HA H 3.654 0.020 1 100 . 13 ARG HB2 H 1.891 0.020 1 101 . 13 ARG HB3 H 1.980 0.020 1 102 . 13 ARG HG2 H 1.399 0.020 1 103 . 13 ARG HG3 H 1.399 0.020 1 104 . 13 ARG HD2 H 3.211 0.020 2 105 . 13 ARG HD3 H 3.065 0.020 2 106 . 13 ARG HE H 6.516 0.020 1 107 . 13 ARG C C 178.118 0.300 1 108 . 13 ARG CA C 60.449 0.300 1 109 . 13 ARG CB C 30.691 0.300 1 110 . 13 ARG CG C 28.301 0.300 1 111 . 13 ARG CD C 43.346 0.300 1 112 . 13 ARG N N 119.650 0.200 1 113 . 13 ARG NE N 113.835 0.200 1 114 . 14 GLY H H 7.994 0.020 1 115 . 14 GLY HA2 H 4.146 0.020 2 116 . 14 GLY HA3 H 3.788 0.020 2 117 . 14 GLY C C 177.366 0.300 1 118 . 14 GLY CA C 47.162 0.300 1 119 . 14 GLY N N 103.900 0.200 1 120 . 15 GLN H H 8.158 0.020 1 121 . 15 GLN HA H 4.180 0.020 1 122 . 15 GLN HB2 H 2.148 0.020 1 123 . 15 GLN HB3 H 2.337 0.020 1 124 . 15 GLN HG2 H 2.672 0.020 2 125 . 15 GLN HG3 H 2.394 0.020 2 126 . 15 GLN HE21 H 7.238 0.020 1 127 . 15 GLN HE22 H 7.070 0.020 1 128 . 15 GLN C C 179.427 0.300 1 129 . 15 GLN CA C 58.864 0.300 1 130 . 15 GLN CB C 29.795 0.300 1 131 . 15 GLN CG C 35.168 0.300 1 132 . 15 GLN N N 122.931 0.200 1 133 . 15 GLN NE2 N 112.494 0.200 1 134 . 16 ILE H H 8.292 0.020 1 135 . 16 ILE HA H 3.418 0.020 1 136 . 16 ILE HB H 1.882 0.020 1 137 . 16 ILE HG12 H 2.025 0.020 1 138 . 16 ILE HG13 H 2.025 0.020 1 139 . 16 ILE HG2 H 0.640 0.020 1 140 . 16 ILE HD1 H 0.685 0.020 1 141 . 16 ILE C C 176.821 0.300 1 142 . 16 ILE CA C 65.809 0.300 1 143 . 16 ILE CB C 37.740 0.300 1 144 . 16 ILE CG1 C 29.667 0.300 1 145 . 16 ILE CG2 C 17.608 0.300 1 146 . 16 ILE CD1 C 14.605 0.300 1 147 . 16 ILE N N 122.440 0.200 1 148 . 17 ILE H H 7.860 0.020 1 149 . 17 ILE HA H 3.364 0.020 1 150 . 17 ILE HB H 1.801 0.020 1 151 . 17 ILE HG12 H 1.742 0.020 2 152 . 17 ILE HG13 H 0.512 0.020 2 153 . 17 ILE HG2 H 0.822 0.020 1 154 . 17 ILE HD1 H 0.819 0.020 1 155 . 17 ILE C C 179.497 0.300 1 156 . 17 ILE CA C 66.327 0.300 1 157 . 17 ILE CB C 38.377 0.300 1 158 . 17 ILE CG1 C 30.239 0.300 1 159 . 17 ILE CG2 C 17.417 0.300 1 160 . 17 ILE CD1 C 14.616 0.300 1 161 . 17 ILE N N 118.088 0.200 1 162 . 18 GLY H H 8.234 0.020 1 163 . 18 GLY HA2 H 3.878 0.020 1 164 . 18 GLY HA3 H 3.878 0.020 1 165 . 18 GLY C C 176.565 0.300 1 166 . 18 GLY CA C 47.072 0.300 1 167 . 18 GLY N N 105.306 0.200 1 168 . 19 ALA H H 7.933 0.020 1 169 . 19 ALA HA H 4.257 0.020 1 170 . 19 ALA HB H 1.446 0.020 1 171 . 19 ALA C C 178.025 0.300 1 172 . 19 ALA CA C 53.755 0.300 1 173 . 19 ALA CB C 18.355 0.300 1 174 . 19 ALA N N 123.744 0.200 1 175 . 20 LEU H H 7.288 0.020 1 176 . 20 LEU HA H 4.493 0.020 1 177 . 20 LEU HB2 H 1.820 0.020 1 178 . 20 LEU HB3 H 1.945 0.020 1 179 . 20 LEU HG H 1.690 0.020 1 180 . 20 LEU HD1 H 0.819 0.020 1 181 . 20 LEU HD2 H 0.707 0.020 1 182 . 20 LEU C C 177.031 0.300 1 183 . 20 LEU CA C 53.635 0.300 1 184 . 20 LEU CB C 43.345 0.300 1 185 . 20 LEU CG C 27.535 0.300 1 186 . 20 LEU CD1 C 27.266 0.300 1 187 . 20 LEU CD2 C 23.594 0.300 1 188 . 20 LEU N N 115.369 0.200 1 189 . 21 ALA H H 7.404 0.020 1 190 . 21 ALA HA H 4.257 0.020 1 191 . 21 ALA HB H 1.529 0.020 1 192 . 21 ALA C C 179.003 0.300 1 193 . 21 ALA CA C 54.857 0.300 1 194 . 21 ALA CB C 18.823 0.300 1 195 . 21 ALA N N 123.775 0.200 1 196 . 22 GLY H H 8.711 0.020 1 197 . 22 GLY HA2 H 4.190 0.020 2 198 . 22 GLY HA3 H 3.855 0.020 2 199 . 22 GLY C C 174.258 0.300 1 200 . 22 GLY CA C 44.889 0.300 1 201 . 22 GLY N N 107.963 0.200 1 202 . 23 ALA H H 7.653 0.020 1 203 . 23 ALA HA H 4.235 0.020 1 204 . 23 ALA HB H 1.197 0.020 1 205 . 23 ALA C C 176.173 0.300 1 206 . 23 ALA CA C 51.880 0.300 1 207 . 23 ALA CB C 20.222 0.300 1 208 . 23 ALA N N 123.337 0.200 1 209 . 24 ASP H H 8.317 0.020 1 210 . 24 ASP HA H 4.738 0.020 1 211 . 24 ASP HB2 H 2.446 0.020 1 212 . 24 ASP HB3 H 2.585 0.020 1 213 . 24 ASP C C 173.867 0.300 1 214 . 24 ASP CA C 53.679 0.300 1 215 . 24 ASP CB C 41.519 0.300 1 216 . 24 ASP N N 120.463 0.200 1 217 . 25 PHE H H 8.192 0.020 1 218 . 25 PHE HA H 4.168 0.020 1 219 . 25 PHE HB2 H 2.739 0.020 1 220 . 25 PHE HB3 H 2.899 0.020 1 221 . 25 PHE HD1 H 7.240 0.020 1 222 . 25 PHE HD2 H 7.240 0.020 1 223 . 25 PHE HE1 H 7.105 0.020 1 224 . 25 PHE HE2 H 7.105 0.020 1 225 . 25 PHE HZ H 6.906 0.020 1 226 . 25 PHE CA C 56.830 0.300 1 227 . 25 PHE CB C 40.666 0.300 1 228 . 25 PHE CD1 C 131.894 0.300 1 229 . 25 PHE CD2 C 131.894 0.300 1 230 . 25 PHE CE1 C 130.758 0.300 1 231 . 25 PHE CE2 C 130.758 0.300 1 232 . 25 PHE CZ C 127.833 0.300 1 233 . 25 PHE N N 120.119 0.200 1 234 . 26 PRO HA H 5.128 0.020 1 235 . 26 PRO HB2 H 2.417 0.020 2 236 . 26 PRO HB3 H 2.063 0.020 2 237 . 26 PRO HG2 H 2.002 0.020 1 238 . 26 PRO HG3 H 2.002 0.020 1 239 . 26 PRO HD2 H 3.709 0.020 2 240 . 26 PRO HD3 H 3.637 0.020 2 241 . 26 PRO C C 174.973 0.300 1 242 . 26 PRO CA C 62.145 0.300 1 243 . 26 PRO CB C 35.826 0.300 1 244 . 26 PRO CG C 25.377 0.300 1 245 . 26 PRO CD C 50.835 0.300 1 246 . 27 ILE H H 8.649 0.020 1 247 . 27 ILE HA H 4.436 0.020 1 248 . 27 ILE HB H 1.868 0.020 1 249 . 27 ILE HG12 H 0.865 0.020 2 250 . 27 ILE HG13 H 1.260 0.020 2 251 . 27 ILE HG2 H 1.177 0.020 1 252 . 27 ILE HD1 H 0.429 0.020 1 253 . 27 ILE C C 177.070 0.300 1 254 . 27 ILE CA C 61.182 0.300 1 255 . 27 ILE CB C 40.030 0.300 1 256 . 27 ILE CG1 C 27.496 0.300 1 257 . 27 ILE CG2 C 18.236 0.300 1 258 . 27 ILE CD1 C 13.930 0.300 1 259 . 27 ILE N N 119.931 0.200 1 260 . 28 ASN H H 9.313 0.020 1 261 . 28 ASN HA H 4.888 0.020 1 262 . 28 ASN HB2 H 2.918 0.020 1 263 . 28 ASN HB3 H 2.784 0.020 1 264 . 28 ASN HD21 H 8.006 0.020 1 265 . 28 ASN HD22 H 6.532 0.020 1 266 . 28 ASN C C 174.223 0.300 1 267 . 28 ASN CA C 55.160 0.300 1 268 . 28 ASN CB C 40.966 0.300 1 269 . 28 ASN N N 124.962 0.200 1 270 . 28 ASN ND2 N 113.806 0.200 1 271 . 29 SER H H 7.404 0.020 1 272 . 29 SER HA H 3.932 0.020 1 273 . 29 SER HB2 H 4.041 0.020 1 274 . 29 SER HB3 H 3.654 0.020 1 275 . 29 SER CA C 55.719 0.300 1 276 . 29 SER CB C 64.000 0.300 1 277 . 29 SER N N 112.775 0.200 1 278 . 30 PRO HA H 4.123 0.020 1 279 . 30 PRO HB2 H 1.965 0.020 2 280 . 30 PRO HB3 H 2.380 0.020 2 281 . 30 PRO HG2 H 2.090 0.020 2 282 . 30 PRO HG3 H 1.824 0.020 2 283 . 30 PRO HD2 H 3.587 0.020 1 284 . 30 PRO HD3 H 3.587 0.020 1 285 . 30 PRO C C 177.821 0.300 1 286 . 30 PRO CA C 65.216 0.300 1 287 . 30 PRO CB C 31.696 0.300 1 288 . 30 PRO CG C 27.500 0.300 1 289 . 30 PRO CD C 50.352 0.300 1 290 . 31 GLU H H 8.659 0.020 1 291 . 31 GLU HA H 3.922 0.020 1 292 . 31 GLU HB2 H 2.017 0.020 1 293 . 31 GLU HB3 H 1.877 0.020 1 294 . 31 GLU HG2 H 2.408 0.020 2 295 . 31 GLU HG3 H 2.214 0.020 2 296 . 31 GLU C C 180.003 0.300 1 297 . 31 GLU CA C 60.643 0.300 1 298 . 31 GLU CB C 28.675 0.300 1 299 . 31 GLU CG C 37.132 0.300 1 300 . 31 GLU N N 117.556 0.200 1 301 . 32 GLU H H 7.653 0.020 1 302 . 32 GLU HA H 4.023 0.020 1 303 . 32 GLU HB2 H 2.100 0.020 1 304 . 32 GLU HB3 H 2.203 0.020 1 305 . 32 GLU HG2 H 2.339 0.020 1 306 . 32 GLU HG3 H 2.339 0.020 1 307 . 32 GLU C C 179.002 0.300 1 308 . 32 GLU CA C 58.754 0.300 1 309 . 32 GLU CB C 31.001 0.300 1 310 . 32 GLU CG C 37.308 0.300 1 311 . 32 GLU N N 119.869 0.200 1 312 . 33 LEU H H 7.891 0.020 1 313 . 33 LEU HA H 4.079 0.020 1 314 . 33 LEU HB2 H 2.449 0.020 2 315 . 33 LEU HB3 H 1.556 0.020 2 316 . 33 LEU HG H 1.569 0.020 1 317 . 33 LEU HD1 H 0.874 0.020 1 318 . 33 LEU HD2 H 0.863 0.020 1 319 . 33 LEU C C 177.063 0.300 1 320 . 33 LEU CA C 58.210 0.300 1 321 . 33 LEU CB C 41.659 0.300 1 322 . 33 LEU CG C 27.572 0.300 1 323 . 33 LEU CD1 C 24.090 0.300 1 324 . 33 LEU CD2 C 26.091 0.300 1 325 . 33 LEU N N 121.431 0.200 1 326 . 34 MET H H 8.151 0.020 1 327 . 34 MET HA H 4.146 0.020 1 328 . 34 MET HB2 H 2.235 0.020 1 329 . 34 MET HB3 H 1.675 0.020 1 330 . 34 MET HG2 H 2.920 0.020 2 331 . 34 MET HG3 H 2.784 0.020 2 332 . 34 MET HE H 2.028 0.020 1 333 . 34 MET C C 178.696 0.300 1 334 . 34 MET CA C 56.933 0.300 1 335 . 34 MET CB C 32.588 0.300 1 336 . 34 MET CG C 33.248 0.300 1 337 . 34 MET CE C 18.533 0.300 1 338 . 34 MET N N 113.744 0.200 1 339 . 35 ALA H H 7.528 0.020 1 340 . 35 ALA HA H 4.168 0.020 1 341 . 35 ALA HB H 1.437 0.020 1 342 . 35 ALA C C 178.106 0.300 1 343 . 35 ALA CA C 53.520 0.300 1 344 . 35 ALA CB C 18.823 0.300 1 345 . 35 ALA N N 117.650 0.200 1 346 . 36 ALA H H 7.362 0.020 1 347 . 36 ALA HA H 4.212 0.020 1 348 . 36 ALA HB H 1.405 0.020 1 349 . 36 ALA C C 177.410 0.300 1 350 . 36 ALA CA C 52.348 0.300 1 351 . 36 ALA CB C 19.937 0.300 1 352 . 36 ALA N N 118.931 0.200 1 353 . 37 LEU H H 7.072 0.020 1 354 . 37 LEU HA H 4.584 0.020 1 355 . 37 LEU HB2 H 1.724 0.020 1 356 . 37 LEU HB3 H 1.599 0.020 1 357 . 37 LEU HG H 2.069 0.020 1 358 . 37 LEU HD1 H 0.738 0.020 1 359 . 37 LEU HD2 H 0.693 0.020 1 360 . 37 LEU CA C 52.466 0.300 1 361 . 37 LEU CB C 41.897 0.300 1 362 . 37 LEU CG C 25.982 0.300 1 363 . 37 LEU CD1 C 27.964 0.300 1 364 . 37 LEU CD2 C 23.595 0.300 1 365 . 37 LEU N N 117.890 0.200 1 366 . 38 PRO HA H 4.358 0.020 1 367 . 38 PRO HB2 H 2.476 0.020 2 368 . 38 PRO HB3 H 1.947 0.020 2 369 . 38 PRO HG2 H 2.270 0.020 2 370 . 38 PRO HG3 H 2.203 0.020 2 371 . 38 PRO HD2 H 3.605 0.020 2 372 . 38 PRO HD3 H 4.324 0.020 2 373 . 38 PRO C C 177.328 0.300 1 374 . 38 PRO CA C 65.437 0.300 1 375 . 38 PRO CB C 32.195 0.300 1 376 . 38 PRO CG C 27.721 0.300 1 377 . 38 PRO CD C 50.633 0.300 1 378 . 39 ASN H H 7.528 0.020 1 379 . 39 ASN HA H 5.240 0.020 1 380 . 39 ASN HB2 H 2.248 0.020 1 381 . 39 ASN HB3 H 2.971 0.020 1 382 . 39 ASN HD21 H 7.494 0.020 1 383 . 39 ASN HD22 H 6.914 0.020 1 384 . 39 ASN C C 175.898 0.300 1 385 . 39 ASN CA C 51.199 0.300 1 386 . 39 ASN CB C 39.756 0.300 1 387 . 39 ASN N N 112.978 0.200 1 388 . 39 ASN ND2 N 111.681 0.200 1 389 . 40 GLY H H 7.653 0.020 1 390 . 40 GLY HA2 H 4.391 0.020 1 391 . 40 GLY HA3 H 4.190 0.020 1 392 . 40 GLY CA C 45.367 0.300 1 393 . 40 GLY N N 108.869 0.200 1 394 . 41 PRO HA H 4.352 0.020 1 395 . 41 PRO HB2 H 2.471 0.020 2 396 . 41 PRO HB3 H 1.951 0.020 2 397 . 41 PRO HG2 H 2.069 0.020 2 398 . 41 PRO HG3 H 1.962 0.020 2 399 . 41 PRO HD2 H 4.034 0.020 2 400 . 41 PRO HD3 H 3.632 0.020 2 401 . 41 PRO C C 175.173 0.300 1 402 . 41 PRO CA C 64.437 0.300 1 403 . 41 PRO CB C 32.208 0.300 1 404 . 41 PRO CG C 27.111 0.300 1 405 . 41 PRO CD C 51.226 0.300 1 406 . 42 ASP H H 7.321 0.020 1 407 . 42 ASP HA H 4.669 0.020 1 408 . 42 ASP HB2 H 2.627 0.020 1 409 . 42 ASP HB3 H 2.895 0.020 1 410 . 42 ASP C C 176.231 0.300 1 411 . 42 ASP CA C 54.561 0.300 1 412 . 42 ASP CB C 41.326 0.300 1 413 . 42 ASP N N 114.088 0.200 1 414 . 43 THR H H 7.715 0.020 1 415 . 43 THR HA H 4.092 0.020 1 416 . 43 THR HB H 4.012 0.020 1 417 . 43 THR HG2 H 1.260 0.020 1 418 . 43 THR CA C 65.044 0.300 1 419 . 43 THR CB C 69.115 0.300 1 420 . 43 THR CG2 C 20.641 0.300 1 421 . 43 THR N N 119.369 0.200 1 422 . 44 THR H H 9.085 0.020 1 423 . 44 THR HA H 5.079 0.020 1 424 . 44 THR HB H 3.958 0.020 1 425 . 44 THR HG2 H 1.064 0.020 1 426 . 44 THR CA C 61.301 0.300 1 427 . 44 THR CB C 71.296 0.300 1 428 . 44 THR CG2 C 21.435 0.300 1 429 . 44 THR N N 123.650 0.200 1 430 . 45 CYS H H 8.732 0.020 1 431 . 45 CYS HA H 4.694 0.020 1 432 . 45 CYS HB2 H 2.583 0.020 1 433 . 45 CYS HB3 H 2.717 0.020 1 434 . 45 CYS C C 181.200 0.300 1 435 . 45 CYS CA C 57.558 0.300 1 436 . 45 CYS CB C 30.433 0.300 1 437 . 45 CYS N N 124.556 0.200 1 438 . 46 LYS H H 8.617 0.020 1 439 . 46 LYS HA H 5.266 0.020 1 440 . 46 LYS HB2 H 1.757 0.020 2 441 . 46 LYS HB3 H 1.608 0.020 2 442 . 46 LYS HG2 H 1.232 0.020 1 443 . 46 LYS HG3 H 1.232 0.020 1 444 . 46 LYS HD2 H 1.623 0.020 2 445 . 46 LYS HD3 H 1.658 0.020 2 446 . 46 LYS HE2 H 2.962 0.020 2 447 . 46 LYS HE3 H 2.902 0.020 2 448 . 46 LYS C C 175.554 0.300 1 449 . 46 LYS CA C 55.153 0.300 1 450 . 46 LYS CB C 36.598 0.300 1 451 . 46 LYS CG C 25.017 0.300 1 452 . 46 LYS CD C 29.604 0.300 1 453 . 46 LYS CE C 42.298 0.300 1 454 . 46 LYS N N 123.244 0.200 1 455 . 47 SER H H 8.836 0.020 1 456 . 47 SER HA H 4.436 0.020 1 457 . 47 SER HB2 H 3.647 0.020 1 458 . 47 SER HB3 H 3.431 0.020 1 459 . 47 SER C C 174.599 0.300 1 460 . 47 SER CA C 57.595 0.300 1 461 . 47 SER CB C 63.405 0.300 1 462 . 47 SER N N 120.994 0.200 1 463 . 48 GLY H H 9.043 0.020 1 464 . 48 GLY HA2 H 3.945 0.020 2 465 . 48 GLY HA3 H 3.654 0.020 2 466 . 48 GLY C C 174.784 0.300 1 467 . 48 GLY CA C 47.333 0.300 1 468 . 48 GLY N N 117.806 0.200 1 469 . 49 ASP H H 8.753 0.020 1 470 . 49 ASP HA H 4.686 0.020 1 471 . 49 ASP HB2 H 2.650 0.020 1 472 . 49 ASP HB3 H 2.806 0.020 1 473 . 49 ASP C C 175.710 0.300 1 474 . 49 ASP CA C 54.277 0.300 1 475 . 49 ASP CB C 41.064 0.300 1 476 . 49 ASP N N 125.994 0.200 1 477 . 50 VAL H H 8.268 0.020 1 478 . 50 VAL HA H 4.041 0.020 1 479 . 50 VAL HB H 2.248 0.020 1 480 . 50 VAL HG1 H 0.774 0.020 1 481 . 50 VAL HG2 H 1.031 0.020 1 482 . 50 VAL C C 174.074 0.300 1 483 . 50 VAL CA C 62.956 0.300 1 484 . 50 VAL CB C 32.638 0.300 1 485 . 50 VAL CG1 C 20.938 0.300 1 486 . 50 VAL CG2 C 21.847 0.300 1 487 . 50 VAL N N 122.620 0.200 1 488 . 51 GLU H H 8.400 0.020 1 489 . 51 GLU HA H 4.927 0.020 1 490 . 51 GLU HB2 H 1.860 0.020 2 491 . 51 GLU HB3 H 1.779 0.020 2 492 . 51 GLU HG2 H 2.069 0.020 2 493 . 51 GLU HG3 H 1.905 0.020 2 494 . 51 GLU C C 174.372 0.300 1 495 . 51 GLU CA C 54.655 0.300 1 496 . 51 GLU CB C 33.276 0.300 1 497 . 51 GLU CG C 37.028 0.300 1 498 . 51 GLU N N 126.619 0.200 1 499 . 52 LEU H H 8.836 0.020 1 500 . 52 LEU HA H 4.715 0.020 1 501 . 52 LEU HB2 H 1.556 0.020 2 502 . 52 LEU HB3 H 1.198 0.020 2 503 . 52 LEU HG H 1.377 0.020 1 504 . 52 LEU HD1 H 0.797 0.020 1 505 . 52 LEU HD2 H 0.636 0.020 1 506 . 52 LEU CA C 54.039 0.300 1 507 . 52 LEU CB C 45.277 0.300 1 508 . 52 LEU CG C 27.595 0.300 1 509 . 52 LEU CD1 C 24.453 0.300 1 510 . 52 LEU CD2 C 25.552 0.300 1 511 . 52 LEU N N 125.806 0.200 1 512 . 53 LYS H H 8.397 0.020 1 513 . 53 LYS HA H 4.707 0.020 1 514 . 53 LYS HB2 H 1.910 0.020 1 515 . 53 LYS HB3 H 1.910 0.020 1 516 . 53 LYS HG2 H 1.384 0.020 1 517 . 53 LYS HG3 H 1.384 0.020 1 518 . 53 LYS HD2 H 1.803 0.020 1 519 . 53 LYS HD3 H 1.803 0.020 1 520 . 53 LYS HE2 H 3.195 0.020 2 521 . 53 LYS HE3 H 3.038 0.020 2 522 . 53 LYS C C 178.289 0.300 1 523 . 53 LYS CA C 55.045 0.300 1 524 . 53 LYS CB C 34.151 0.300 1 525 . 53 LYS CG C 24.833 0.300 1 526 . 53 LYS CD C 26.541 0.300 1 527 . 53 LYS N N 127.518 0.200 1 528 . 54 ALA H H 9.095 0.020 1 529 . 54 ALA HA H 3.864 0.020 1 530 . 54 ALA HB H 1.426 0.020 1 531 . 54 ALA C C 178.752 0.300 1 532 . 54 ALA CA C 55.858 0.300 1 533 . 54 ALA CB C 19.419 0.300 1 534 . 54 ALA N N 127.775 0.200 1 535 . 55 SER H H 8.421 0.020 1 536 . 55 SER HA H 4.123 0.020 1 537 . 55 SER HB2 H 3.989 0.020 1 538 . 55 SER HB3 H 3.900 0.020 1 539 . 55 SER CA C 60.551 0.300 1 540 . 55 SER CB C 61.384 0.300 1 541 . 55 SER N N 111.181 0.200 1 542 . 56 ASP H H 7.134 0.020 1 543 . 56 ASP HA H 4.614 0.020 1 544 . 56 ASP HB2 H 2.969 0.020 1 545 . 56 ASP HB3 H 2.775 0.020 1 546 . 56 ASP C C 174.540 0.300 1 547 . 56 ASP CA C 56.817 0.300 1 548 . 56 ASP CB C 40.618 0.300 1 549 . 56 ASP N N 122.431 0.200 1 550 . 57 ALA H H 8.069 0.020 1 551 . 57 ALA HA H 4.056 0.020 1 552 . 57 ALA HB H 1.361 0.020 1 553 . 57 ALA C C 179.061 0.300 1 554 . 57 ALA CA C 54.457 0.300 1 555 . 57 ALA CB C 18.296 0.300 1 556 . 57 ALA N N 123.025 0.200 1 557 . 58 GLY H H 8.545 0.020 1 558 . 58 GLY HA2 H 3.878 0.020 2 559 . 58 GLY HA3 H 3.744 0.020 2 560 . 58 GLY C C 175.193 0.300 1 561 . 58 GLY CA C 46.442 0.300 1 562 . 58 GLY N N 101.318 0.200 1 563 . 59 GLN H H 7.332 0.020 1 564 . 59 GLN HA H 4.332 0.020 1 565 . 59 GLN HB2 H 2.236 0.020 2 566 . 59 GLN HB3 H 2.321 0.020 2 567 . 59 GLN HG2 H 2.560 0.020 2 568 . 59 GLN HG3 H 2.653 0.020 2 569 . 59 GLN HE21 H 7.455 0.020 1 570 . 59 GLN HE22 H 6.861 0.020 1 571 . 59 GLN C C 177.246 0.300 1 572 . 59 GLN CA C 57.248 0.300 1 573 . 59 GLN CB C 29.349 0.300 1 574 . 59 GLN CG C 34.285 0.300 1 575 . 59 GLN N N 115.775 0.200 1 576 . 59 GLN NE2 N 111.963 0.200 1 577 . 60 VAL H H 7.321 0.020 1 578 . 60 VAL HA H 4.498 0.020 1 579 . 60 VAL HB H 2.359 0.020 1 580 . 60 VAL HG1 H 0.975 0.020 1 581 . 60 VAL HG2 H 0.998 0.020 1 582 . 60 VAL C C 175.696 0.300 1 583 . 60 VAL CA C 61.206 0.300 1 584 . 60 VAL CB C 31.954 0.300 1 585 . 60 VAL CG1 C 21.539 0.300 1 586 . 60 VAL CG2 C 19.540 0.300 1 587 . 60 VAL N N 109.963 0.200 1 588 . 61 LEU H H 7.175 0.020 1 589 . 61 LEU HA H 4.715 0.020 1 590 . 61 LEU HB2 H 2.091 0.020 1 591 . 61 LEU HB3 H 1.600 0.020 1 592 . 61 LEU HG H 2.037 0.020 1 593 . 61 LEU HD1 H 0.886 0.020 1 594 . 61 LEU HD2 H 0.817 0.020 1 595 . 61 LEU C C 176.835 0.300 1 596 . 61 LEU CA C 54.099 0.300 1 597 . 61 LEU CB C 42.971 0.300 1 598 . 61 LEU CG C 26.253 0.300 1 599 . 61 LEU CD1 C 26.192 0.300 1 600 . 61 LEU CD2 C 23.378 0.300 1 601 . 61 LEU N N 120.494 0.200 1 602 . 62 THR H H 9.459 0.020 1 603 . 62 THR HA H 4.838 0.020 1 604 . 62 THR HB H 4.547 0.020 1 605 . 62 THR HG2 H 1.197 0.020 1 606 . 62 THR C C 175.990 0.300 1 607 . 62 THR CA C 59.507 0.300 1 608 . 62 THR CB C 71.837 0.300 1 609 . 62 THR CG2 C 22.121 0.300 1 610 . 62 THR N N 114.431 0.200 1 611 . 63 ALA H H 8.753 0.020 1 612 . 63 ALA HA H 4.212 0.020 1 613 . 63 ALA HB H 1.509 0.020 1 614 . 63 ALA C C 179.676 0.300 1 615 . 63 ALA CA C 55.478 0.300 1 616 . 63 ALA CB C 18.763 0.300 1 617 . 63 ALA N N 122.088 0.200 1 618 . 64 ASP H H 7.985 0.020 1 619 . 64 ASP HA H 4.525 0.020 1 620 . 64 ASP HB2 H 2.484 0.020 1 621 . 64 ASP HB3 H 2.717 0.020 1 622 . 64 ASP C C 176.365 0.300 1 623 . 64 ASP CA C 55.079 0.300 1 624 . 64 ASP CB C 40.632 0.300 1 625 . 64 ASP N N 112.650 0.200 1 626 . 65 ASP H H 7.943 0.020 1 627 . 65 ASP HA H 4.235 0.020 1 628 . 65 ASP HB2 H 2.560 0.020 1 629 . 65 ASP HB3 H 2.318 0.020 1 630 . 65 ASP C C 173.512 0.300 1 631 . 65 ASP CA C 55.984 0.300 1 632 . 65 ASP CB C 42.033 0.300 1 633 . 65 ASP N N 118.275 0.200 1 634 . 66 PHE H H 6.947 0.020 1 635 . 66 PHE HA H 3.587 0.020 1 636 . 66 PHE HB2 H 2.784 0.020 1 637 . 66 PHE HB3 H 2.784 0.020 1 638 . 66 PHE HD1 H 7.370 0.020 1 639 . 66 PHE HD2 H 7.370 0.020 1 640 . 66 PHE HE1 H 7.121 0.020 1 641 . 66 PHE HE2 H 7.121 0.020 1 642 . 66 PHE HZ H 7.010 0.020 1 643 . 66 PHE CA C 55.470 0.300 1 644 . 66 PHE CB C 40.060 0.300 1 645 . 66 PHE CD1 C 133.063 0.300 1 646 . 66 PHE CD2 C 133.063 0.300 1 647 . 66 PHE CE1 C 130.758 0.300 1 648 . 66 PHE CE2 C 130.758 0.300 1 649 . 66 PHE CZ C 127.803 0.300 1 650 . 66 PHE N N 114.088 0.200 1 651 . 67 PRO HA H 4.994 0.020 1 652 . 67 PRO HB2 H 1.820 0.020 2 653 . 67 PRO HB3 H 2.774 0.020 2 654 . 67 PRO HG2 H 2.025 0.020 2 655 . 67 PRO HG3 H 1.847 0.020 2 656 . 67 PRO HD2 H 3.584 0.020 1 657 . 67 PRO HD3 H 3.584 0.020 1 658 . 67 PRO C C 175.947 0.300 1 659 . 67 PRO CA C 61.685 0.300 1 660 . 67 PRO CB C 36.092 0.300 1 661 . 67 PRO CG C 24.777 0.300 1 662 . 67 PRO CD C 50.388 0.300 1 663 . 68 PHE H H 8.808 0.020 1 664 . 68 PHE HA H 5.173 0.020 1 665 . 68 PHE HB2 H 2.851 0.020 1 666 . 68 PHE HB3 H 3.169 0.020 1 667 . 68 PHE HD1 H 6.984 0.020 1 668 . 68 PHE HD2 H 6.984 0.020 1 669 . 68 PHE HE1 H 6.669 0.020 1 670 . 68 PHE HE2 H 6.669 0.020 1 671 . 68 PHE HZ H 6.719 0.020 1 672 . 68 PHE C C 177.237 0.300 1 673 . 68 PHE CA C 56.851 0.300 1 674 . 68 PHE CB C 43.467 0.300 1 675 . 68 PHE CD1 C 131.359 0.300 1 676 . 68 PHE CD2 C 131.359 0.300 1 677 . 68 PHE CE1 C 131.059 0.300 1 678 . 68 PHE CE2 C 131.059 0.300 1 679 . 68 PHE CZ C 128.304 0.300 1 680 . 68 PHE N N 116.619 0.200 1 681 . 69 LYS H H 9.687 0.020 1 682 . 69 LYS HA H 4.413 0.020 1 683 . 69 LYS HB2 H 1.958 0.020 1 684 . 69 LYS HB3 H 1.958 0.020 1 685 . 69 LYS HG2 H 1.489 0.020 2 686 . 69 LYS HG3 H 1.557 0.020 2 687 . 69 LYS HD2 H 1.779 0.020 1 688 . 69 LYS HD3 H 1.779 0.020 1 689 . 69 LYS HE2 H 3.007 0.020 2 690 . 69 LYS HE3 H 3.053 0.020 2 691 . 69 LYS C C 175.425 0.300 1 692 . 69 LYS CA C 57.334 0.300 1 693 . 69 LYS CB C 33.026 0.300 1 694 . 69 LYS CG C 25.169 0.300 1 695 . 69 LYS CD C 28.872 0.300 1 696 . 69 LYS CE C 41.477 0.300 1 697 . 69 LYS N N 121.119 0.200 1 698 . 70 SER H H 7.300 0.020 1 699 . 70 SER HA H 3.303 0.020 1 700 . 70 SER HB2 H 3.900 0.020 1 701 . 70 SER HB3 H 3.699 0.020 1 702 . 70 SER C C 173.377 0.300 1 703 . 70 SER CA C 56.033 0.300 1 704 . 70 SER CB C 66.164 0.300 1 705 . 70 SER N N 110.775 0.200 1 706 . 71 ALA H H 8.566 0.020 1 707 . 71 ALA HA H 3.766 0.020 1 708 . 71 ALA HB H 1.415 0.020 1 709 . 71 ALA C C 178.546 0.300 1 710 . 71 ALA CA C 54.766 0.300 1 711 . 71 ALA CB C 19.995 0.300 1 712 . 71 ALA N N 124.119 0.200 1 713 . 72 GLU H H 8.836 0.020 1 714 . 72 GLU HA H 3.598 0.020 1 715 . 72 GLU HB2 H 1.958 0.020 1 716 . 72 GLU HB3 H 1.833 0.020 1 717 . 72 GLU HG2 H 2.403 0.020 2 718 . 72 GLU HG3 H 2.152 0.020 2 719 . 72 GLU C C 177.345 0.300 1 720 . 72 GLU CA C 60.673 0.300 1 721 . 72 GLU CB C 28.744 0.300 1 722 . 72 GLU CG C 37.361 0.300 1 723 . 72 GLU N N 117.338 0.200 1 724 . 73 GLU H H 7.362 0.020 1 725 . 73 GLU HA H 4.168 0.020 1 726 . 73 GLU HB2 H 2.203 0.020 2 727 . 73 GLU HB3 H 2.449 0.020 2 728 . 73 GLU HG2 H 2.493 0.020 2 729 . 73 GLU HG3 H 2.382 0.020 2 730 . 73 GLU C C 179.845 0.300 1 731 . 73 GLU CA C 59.220 0.300 1 732 . 73 GLU CB C 31.027 0.300 1 733 . 73 GLU CG C 36.206 0.300 1 734 . 73 GLU N N 117.838 0.200 1 735 . 74 VAL H H 7.238 0.020 1 736 . 74 VAL HA H 2.484 0.020 1 737 . 74 VAL HB H 1.851 0.020 1 738 . 74 VAL HG1 H 0.388 0.020 1 739 . 74 VAL HG2 H 0.575 0.020 1 740 . 74 VAL C C 176.401 0.300 1 741 . 74 VAL CA C 65.192 0.300 1 742 . 74 VAL CB C 31.070 0.300 1 743 . 74 VAL CG1 C 22.076 0.300 1 744 . 74 VAL CG2 C 21.627 0.300 1 745 . 74 VAL N N 118.619 0.200 1 746 . 75 ALA H H 7.998 0.020 1 747 . 75 ALA HA H 3.709 0.020 1 748 . 75 ALA HB H 1.446 0.020 1 749 . 75 ALA C C 178.553 0.300 1 750 . 75 ALA CA C 55.678 0.300 1 751 . 75 ALA CB C 20.783 0.300 1 752 . 75 ALA N N 120.056 0.200 1 753 . 76 ASP H H 8.659 0.020 1 754 . 76 ASP HA H 4.324 0.020 1 755 . 76 ASP HB2 H 2.717 0.020 1 756 . 76 ASP HB3 H 2.538 0.020 1 757 . 76 ASP C C 178.391 0.300 1 758 . 76 ASP CA C 57.474 0.300 1 759 . 76 ASP CB C 40.949 0.300 1 760 . 76 ASP N N 115.900 0.200 1 761 . 77 THR H H 7.765 0.020 1 762 . 77 THR HA H 4.041 0.020 1 763 . 77 THR HB H 4.257 0.020 1 764 . 77 THR HG2 H 1.243 0.020 1 765 . 77 THR C C 176.045 0.300 1 766 . 77 THR CA C 67.228 0.300 1 767 . 77 THR CB C 68.108 0.300 1 768 . 77 THR CG2 C 21.875 0.300 1 769 . 77 THR N N 115.556 0.200 1 770 . 78 ILE H H 8.296 0.020 1 771 . 78 ILE HA H 3.439 0.020 1 772 . 78 ILE HB H 1.737 0.020 1 773 . 78 ILE HG12 H 1.862 0.020 2 774 . 78 ILE HG13 H 0.803 0.020 2 775 . 78 ILE HG2 H 0.636 0.020 1 776 . 78 ILE HD1 H 0.596 0.020 1 777 . 78 ILE C C 177.639 0.300 1 778 . 78 ILE CA C 66.686 0.300 1 779 . 78 ILE CB C 37.586 0.300 1 780 . 78 ILE CG1 C 30.027 0.300 1 781 . 78 ILE CG2 C 17.579 0.300 1 782 . 78 ILE CD1 C 13.543 0.300 1 783 . 78 ILE N N 119.306 0.200 1 784 . 79 VAL H H 8.400 0.020 1 785 . 79 VAL HA H 3.766 0.020 1 786 . 79 VAL HB H 2.173 0.020 1 787 . 79 VAL HG1 H 0.953 0.020 1 788 . 79 VAL HG2 H 1.064 0.020 1 789 . 79 VAL C C 177.712 0.300 1 790 . 79 VAL CA C 66.322 0.300 1 791 . 79 VAL CB C 31.194 0.300 1 792 . 79 VAL CG1 C 21.804 0.300 1 793 . 79 VAL CG2 C 20.000 0.300 1 794 . 79 VAL N N 111.400 0.200 1 795 . 80 ASN H H 7.757 0.020 1 796 . 80 ASN HA H 4.619 0.020 1 797 . 80 ASN HB2 H 3.029 0.020 1 798 . 80 ASN HB3 H 2.828 0.020 1 799 . 80 ASN HD21 H 7.606 0.020 1 800 . 80 ASN HD22 H 6.905 0.020 1 801 . 80 ASN C C 178.731 0.300 1 802 . 80 ASN CA C 55.741 0.300 1 803 . 80 ASN CB C 38.596 0.300 1 804 . 80 ASN N N 117.931 0.200 1 805 . 80 ASN ND2 N 112.900 0.200 1 806 . 81 LYS H H 8.483 0.020 1 807 . 81 LYS HA H 4.207 0.020 1 808 . 81 LYS HB2 H 1.868 0.020 2 809 . 81 LYS HB3 H 1.801 0.020 2 810 . 81 LYS HG2 H 1.422 0.020 1 811 . 81 LYS HG3 H 1.422 0.020 1 812 . 81 LYS HD2 H 1.645 0.020 2 813 . 81 LYS HD3 H 1.687 0.020 2 814 . 81 LYS HE2 H 2.739 0.020 2 815 . 81 LYS HE3 H 2.895 0.020 2 816 . 81 LYS C C 177.873 0.300 1 817 . 81 LYS CA C 59.319 0.300 1 818 . 81 LYS CB C 32.011 0.300 1 819 . 81 LYS CG C 26.999 0.300 1 820 . 81 LYS CD C 29.840 0.300 1 821 . 81 LYS CE C 42.281 0.300 1 822 . 81 LYS N N 119.869 0.200 1 823 . 82 ALA H H 8.369 0.020 1 824 . 82 ALA HA H 4.330 0.020 1 825 . 82 ALA HB H 1.393 0.020 1 826 . 82 ALA C C 177.567 0.300 1 827 . 82 ALA CA C 52.500 0.300 1 828 . 82 ALA CB C 18.822 0.300 1 829 . 82 ALA N N 119.056 0.200 1 830 . 83 GLY H H 7.684 0.020 1 831 . 83 GLY HA2 H 3.922 0.020 1 832 . 83 GLY HA3 H 3.922 0.020 1 833 . 83 GLY C C 174.536 0.300 1 834 . 83 GLY CA C 46.808 0.300 1 835 . 83 GLY N N 105.869 0.200 1 836 . 84 LEU H H 7.217 0.020 1 837 . 84 LEU HA H 4.056 0.020 1 838 . 84 LEU HB2 H 1.623 0.020 1 839 . 84 LEU HB3 H 1.444 0.020 1 840 . 84 LEU HG H 1.544 0.020 1 841 . 84 LEU HD1 H 0.819 0.020 1 842 . 84 LEU HD2 H 0.797 0.020 1 843 . 84 LEU CA C 56.320 0.300 1 844 . 84 LEU CB C 42.948 0.300 1 845 . 84 LEU CD1 C 26.797 0.300 1 846 . 84 LEU CD2 C 22.996 0.300 1 847 . 84 LEU N N 123.587 0.200 1 stop_ save_