data_6079 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignment of the reduced form of thioredoxin h1 from Poplar, a plant CPPC active site variant ; _BMRB_accession_number 6079 _BMRB_flat_file_name bmr6079.str _Entry_type original _Submission_date 2004-01-14 _Accession_date 2004-01-15 _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 Coudevylle Nicolas . . 2 Thureau Aurelien . . 3 Hemmerlin Christine . . 4 Gelhaye Eric . . 5 Jacquot Jean-Pierre . . 6 Cung Manh-Thong . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 543 "13C chemical shifts" 451 "15N chemical shifts" 104 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-04 update author 'chemical shift table update' 2004-11-29 original author 'Original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignment of the reduced form of thioredoxin h1 from Poplar, a CPPC active site variant ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15557810 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Coudevylle Nicolas . . 2 Thureau Aurelien . . 3 Hemmerlin Christine . . 4 Gelhaye Eric . . 5 Jacquot Jean-Pierre . . 6 Cung Manh-Thong . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 229 _Page_last 230 _Year 2004 _Details . loop_ _Keyword oxidoreductase thioredoxin 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_popTrxh1 _Saveframe_category molecular_system _Mol_system_name 'thioredoxin h1 from poplar' _Abbreviation_common popTrxh1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label popTrxh1 $popTrxh1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_popTrxh1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'thioredoxin h1 from poplar' _Abbreviation_common popTrxh1 _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; AEEGQVIACHTVDTWKEHFE KGKGSQKLIVVDFTASWCPP CKMIAPIFAELAKKFPNVTF LKVDVDELKAVAEEWNVEAM PTFIFLKDGKLVDKTVGADK DGLPTLVAKHATA ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLU 3 GLU 4 GLY 5 GLN 6 VAL 7 ILE 8 ALA 9 CYS 10 HIS 11 THR 12 VAL 13 ASP 14 THR 15 TRP 16 LYS 17 GLU 18 HIS 19 PHE 20 GLU 21 LYS 22 GLY 23 LYS 24 GLY 25 SER 26 GLN 27 LYS 28 LEU 29 ILE 30 VAL 31 VAL 32 ASP 33 PHE 34 THR 35 ALA 36 SER 37 TRP 38 CYS 39 PRO 40 PRO 41 CYS 42 LYS 43 MET 44 ILE 45 ALA 46 PRO 47 ILE 48 PHE 49 ALA 50 GLU 51 LEU 52 ALA 53 LYS 54 LYS 55 PHE 56 PRO 57 ASN 58 VAL 59 THR 60 PHE 61 LEU 62 LYS 63 VAL 64 ASP 65 VAL 66 ASP 67 GLU 68 LEU 69 LYS 70 ALA 71 VAL 72 ALA 73 GLU 74 GLU 75 TRP 76 ASN 77 VAL 78 GLU 79 ALA 80 MET 81 PRO 82 THR 83 PHE 84 ILE 85 PHE 86 LEU 87 LYS 88 ASP 89 GLY 90 LYS 91 LEU 92 VAL 93 ASP 94 LYS 95 THR 96 VAL 97 GLY 98 ALA 99 ASP 100 LYS 101 ASP 102 GLY 103 LEU 104 PRO 105 THR 106 LEU 107 VAL 108 ALA 109 LYS 110 HIS 111 ALA 112 THR 113 ALA 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 1TI3 "Solution Structure Of The Thioredoxin H1 From Poplar, A Cppc Active Site Variant" 100.00 113 100.00 100.00 2.94e-74 GB AAL99941 "thioredoxin H [Populus tremula x Populus tremuloides]" 100.00 114 100.00 100.00 2.49e-74 GB ABK94440 "unknown [Populus trichocarpa]" 100.00 114 100.00 100.00 2.49e-74 GB EEE94683 "thioredoxin h family protein [Populus trichocarpa]" 100.00 114 100.00 100.00 2.49e-74 REF XP_002307687 "thioredoxin h family protein [Populus trichocarpa]" 100.00 114 100.00 100.00 2.49e-74 REF XP_011048838 "PREDICTED: thioredoxin H-type [Populus euphratica]" 100.00 114 97.35 98.23 7.51e-73 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $popTrxh1 Poplar 3694 Eukaryota . Populus trichocarpa 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 $popTrxh1 'recombinant technology' . . . . . 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 $popTrxh1 1.85 mM '[U-98% 13C; U-98% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.9 0.1 n/a temperature 298 1 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name popTrxh1 _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 GLU C C 176.414 0.100 1 2 . 2 GLU CA C 57.159 0.100 1 3 . 2 GLU CB C 30.441 0.100 1 4 . 2 GLU HB2 H 2.921 0.010 1 5 . 2 GLU HB3 H 2.659 0.010 1 6 . 3 GLU H H 8.479 0.010 1 7 . 3 GLU N N 121.401 0.100 1 8 . 3 GLU C C 178.091 0.100 1 9 . 3 GLU CA C 57.410 0.100 1 10 . 3 GLU HA H 4.358 0.010 1 11 . 3 GLU CB C 31.134 0.100 1 12 . 3 GLU HB2 H 1.920 0.010 1 13 . 3 GLU HG2 H 2.325 0.010 1 14 . 4 GLY H H 8.640 0.010 1 15 . 4 GLY N N 110.453 0.100 1 16 . 4 GLY C C 173.681 0.100 1 17 . 4 GLY CA C 46.299 0.100 1 18 . 4 GLY HA2 H 3.957 0.010 1 19 . 4 GLY HA3 H 3.957 0.010 1 20 . 5 GLN H H 7.665 0.010 1 21 . 5 GLN N N 116.198 0.100 1 22 . 5 GLN C C 175.589 0.100 1 23 . 5 GLN CA C 54.702 0.100 1 24 . 5 GLN HA H 4.438 0.010 1 25 . 5 GLN CB C 32.165 0.100 1 26 . 5 GLN HB2 H 1.762 0.010 1 27 . 5 GLN HB3 H 1.735 0.010 1 28 . 5 GLN CG C 34.310 0.100 1 29 . 5 GLN HG2 H 2.153 0.010 1 30 . 6 VAL H H 8.347 0.010 1 31 . 6 VAL N N 122.670 0.100 1 32 . 6 VAL C C 176.505 0.100 1 33 . 6 VAL CA C 63.415 0.100 1 34 . 6 VAL HA H 3.864 0.010 1 35 . 6 VAL CB C 32.727 0.100 1 36 . 6 VAL HB H 1.908 0.010 1 37 . 6 VAL CG1 C 22.904 0.100 1 38 . 6 VAL HG1 H 0.796 0.010 1 39 . 6 VAL CG2 C 23.216 0.100 1 40 . 6 VAL HG2 H 0.682 0.010 1 41 . 7 ILE H H 8.859 0.010 1 42 . 7 ILE N N 131.459 0.100 1 43 . 7 ILE C C 175.481 0.100 1 44 . 7 ILE CA C 61.240 0.100 1 45 . 7 ILE HA H 4.030 0.010 1 46 . 7 ILE CB C 38.745 0.100 1 47 . 7 ILE HB H 1.701 0.010 1 48 . 7 ILE CG1 C 27.747 0.100 1 49 . 7 ILE HG12 H 1.378 0.010 1 50 . 7 ILE HG13 H 0.974 0.010 1 51 . 7 ILE CG2 C 19.966 0.100 1 52 . 7 ILE HG2 H 0.398 0.010 1 53 . 7 ILE CD1 C 13.841 0.100 1 54 . 7 ILE HD1 H 0.617 0.010 1 55 . 8 ALA H H 8.694 0.010 1 56 . 8 ALA N N 131.197 0.100 1 57 . 8 ALA C C 177.039 0.100 1 58 . 8 ALA CA C 51.751 0.100 1 59 . 8 ALA HA H 4.510 0.010 1 60 . 8 ALA CB C 19.542 0.100 1 61 . 8 ALA HB H 1.101 0.010 1 62 . 9 CYS H H 7.938 0.010 1 63 . 9 CYS N N 121.479 0.100 1 64 . 9 CYS C C 174.778 0.100 1 65 . 9 CYS CA C 58.190 0.100 1 66 . 9 CYS HA H 4.552 0.010 1 67 . 9 CYS CB C 28.370 0.100 1 68 . 9 CYS HB2 H 2.921 0.010 1 69 . 9 CYS HB3 H 2.659 0.010 1 70 . 10 HIS H H 9.110 0.010 1 71 . 10 HIS N N 120.867 0.100 1 72 . 10 HIS C C 173.831 0.100 1 73 . 10 HIS CA C 57.456 0.100 1 74 . 10 HIS HA H 4.677 0.010 1 75 . 10 HIS CB C 30.178 0.100 1 76 . 10 HIS HB2 H 3.390 0.010 1 77 . 10 HIS HB3 H 3.210 0.010 1 78 . 11 THR H H 7.305 0.010 1 79 . 11 THR N N 104.491 0.100 1 80 . 11 THR C C 175.478 0.100 1 81 . 11 THR CA C 59.134 0.100 1 82 . 11 THR HA H 4.851 0.010 1 83 . 11 THR CB C 73.249 0.100 1 84 . 11 THR HB H 4.655 0.010 1 85 . 11 THR CG2 C 22.122 0.100 1 86 . 11 THR HG2 H 1.244 0.010 1 87 . 12 VAL H H 9.240 0.010 1 88 . 12 VAL N N 122.669 0.100 1 89 . 12 VAL C C 177.822 0.100 1 90 . 12 VAL CA C 66.711 0.100 1 91 . 12 VAL HA H 3.828 0.010 1 92 . 12 VAL CB C 32.064 0.100 1 93 . 12 VAL HB H 2.141 0.010 1 94 . 12 VAL CG1 C 23.529 0.100 1 95 . 12 VAL HG1 H 1.073 0.010 1 96 . 12 VAL CG2 C 21.653 0.100 1 97 . 12 VAL HG2 H 1.049 0.010 1 98 . 13 ASP H H 8.230 0.010 1 99 . 13 ASP N N 119.154 0.100 1 100 . 13 ASP C C 179.463 0.100 1 101 . 13 ASP CA C 58.348 0.100 1 102 . 13 ASP HA H 4.418 0.010 1 103 . 13 ASP CB C 40.789 0.100 1 104 . 13 ASP HB2 H 2.737 0.010 1 105 . 13 ASP HB3 H 2.469 0.010 1 106 . 14 THR H H 7.967 0.010 1 107 . 14 THR N N 116.516 0.100 1 108 . 14 THR C C 177.714 0.100 1 109 . 14 THR CA C 66.905 0.100 1 110 . 14 THR HA H 4.234 0.010 1 111 . 14 THR CB C 69.592 0.100 1 112 . 14 THR HB H 4.241 0.010 1 113 . 14 THR CG2 C 23.841 0.100 1 114 . 14 THR HG2 H 1.519 0.010 1 115 . 15 TRP H H 7.791 0.010 1 116 . 15 TRP N N 123.196 0.100 1 117 . 15 TRP C C 176.973 0.100 1 118 . 15 TRP CA C 61.306 0.100 1 119 . 15 TRP HA H 4.558 0.010 1 120 . 15 TRP CB C 30.012 0.100 1 121 . 15 TRP HB2 H 3.528 0.010 1 122 . 15 TRP HB3 H 3.126 0.010 1 123 . 16 LYS H H 8.888 0.010 1 124 . 16 LYS N N 117.746 0.100 1 125 . 16 LYS C C 179.308 0.100 1 126 . 16 LYS CA C 60.867 0.100 1 127 . 16 LYS HA H 3.621 0.010 1 128 . 16 LYS CB C 33.138 0.100 1 129 . 16 LYS HB2 H 1.950 0.010 1 130 . 16 LYS HB3 H 1.869 0.010 1 131 . 16 LYS CG C 26.341 0.100 1 132 . 16 LYS HG2 H 1.778 0.010 1 133 . 16 LYS HG3 H 1.512 0.010 1 134 . 16 LYS CD C 30.404 0.100 1 135 . 16 LYS HD2 H 1.702 0.010 1 136 . 16 LYS CE C 42.748 0.100 1 137 . 16 LYS HE2 H 2.923 0.010 1 138 . 17 GLU H H 7.877 0.010 1 139 . 17 GLU N N 118.048 0.100 1 140 . 17 GLU C C 176.419 0.100 1 141 . 17 GLU CA C 59.738 0.100 1 142 . 17 GLU HA H 3.858 0.010 1 143 . 17 GLU CB C 33.055 0.100 1 144 . 17 GLU HB2 H 2.045 0.010 1 145 . 17 GLU HB3 H 2.019 0.010 1 146 . 17 GLU CG C 36.185 0.100 1 147 . 17 GLU HG2 H 2.039 0.010 1 148 . 17 GLU HG3 H 1.725 0.010 1 149 . 18 HIS H H 7.367 0.010 1 150 . 18 HIS N N 115.023 0.100 1 151 . 18 HIS C C 177.629 0.100 1 152 . 18 HIS CA C 60.441 0.100 1 153 . 18 HIS HA H 4.016 0.010 1 154 . 18 HIS CB C 30.011 0.100 1 155 . 18 HIS HB2 H 2.714 0.010 1 156 . 18 HIS HB3 H 2.694 0.010 1 157 . 19 PHE H H 8.716 0.010 1 158 . 19 PHE N N 121.355 0.100 1 159 . 19 PHE C C 179.306 0.100 1 160 . 19 PHE CA C 61.831 0.100 1 161 . 19 PHE HA H 3.509 0.010 1 162 . 19 PHE CB C 39.617 0.100 1 163 . 19 PHE HB2 H 2.425 0.010 1 164 . 19 PHE HB3 H 1.658 0.010 1 165 . 20 GLU H H 8.523 0.010 1 166 . 20 GLU N N 118.362 0.100 1 167 . 20 GLU C C 179.813 0.100 1 168 . 20 GLU CA C 59.523 0.100 1 169 . 20 GLU HA H 3.795 0.010 1 170 . 20 GLU CB C 29.629 0.100 1 171 . 20 GLU HB2 H 2.018 0.010 1 172 . 20 GLU CG C 36.185 0.100 1 173 . 20 GLU HG2 H 2.062 0.010 1 174 . 20 GLU HG3 H 1.725 0.010 1 175 . 21 LYS H H 7.277 0.010 1 176 . 21 LYS N N 118.059 0.100 1 177 . 21 LYS C C 178.557 0.100 1 178 . 21 LYS CA C 58.671 0.100 1 179 . 21 LYS HA H 4.017 0.010 1 180 . 21 LYS CB C 32.708 0.100 1 181 . 21 LYS HB2 H 1.761 0.010 1 182 . 21 LYS HB3 H 1.761 0.010 1 183 . 21 LYS CG C 26.029 0.100 1 184 . 21 LYS HG2 H 1.462 0.010 1 185 . 21 LYS HG3 H 1.331 0.010 1 186 . 21 LYS CD C 29.779 0.100 1 187 . 21 LYS HD2 H 1.537 0.010 1 188 . 21 LYS HD3 H 1.459 0.010 1 189 . 21 LYS CE C 42.748 0.100 1 190 . 21 LYS HE2 H 2.761 0.010 1 191 . 22 GLY H H 7.454 0.010 1 192 . 22 GLY N N 105.180 0.100 1 193 . 22 GLY C C 175.475 0.100 1 194 . 22 GLY CA C 46.385 0.100 1 195 . 22 GLY HA2 H 3.897 0.010 1 196 . 22 GLY HA3 H 3.388 0.010 1 197 . 23 LYS H H 7.118 0.010 1 198 . 23 LYS N N 120.738 0.100 1 199 . 23 LYS C C 177.823 0.100 1 200 . 23 LYS CA C 58.882 0.100 1 201 . 23 LYS HA H 3.738 0.010 1 202 . 23 LYS CB C 32.412 0.100 1 203 . 23 LYS HB2 H 1.683 0.010 1 204 . 23 LYS HB3 H 1.592 0.010 1 205 . 23 LYS CG C 26.029 0.100 1 206 . 23 LYS HG2 H 1.232 0.010 1 207 . 23 LYS HG3 H 1.072 0.010 1 208 . 23 LYS CE C 42.748 0.100 1 209 . 23 LYS HE2 H 2.769 0.010 1 210 . 24 GLY H H 8.684 0.010 1 211 . 24 GLY N N 111.592 0.100 1 212 . 24 GLY C C 174.662 0.100 1 213 . 24 GLY CA C 46.072 0.100 1 214 . 24 GLY HA2 H 4.017 0.010 1 215 . 24 GLY HA3 H 3.756 0.010 1 216 . 25 SER H H 7.776 0.010 1 217 . 25 SER N N 114.670 0.100 1 218 . 25 SER C C 176.499 0.100 1 219 . 25 SER CA C 57.419 0.100 1 220 . 25 SER HA H 4.592 0.010 1 221 . 25 SER CB C 65.509 0.100 1 222 . 25 SER HB2 H 3.815 0.010 1 223 . 25 SER HB3 H 3.695 0.010 1 224 . 26 GLN H H 8.464 0.010 1 225 . 26 GLN N N 119.416 0.100 1 226 . 26 GLN C C 175.644 0.100 1 227 . 26 GLN CA C 55.807 0.100 1 228 . 26 GLN HA H 4.539 0.010 1 229 . 26 GLN CB C 28.515 0.100 1 230 . 26 GLN HB2 H 2.378 0.010 1 231 . 26 GLN HB3 H 1.879 0.010 1 232 . 27 LYS H H 7.752 0.010 1 233 . 27 LYS N N 120.434 0.100 1 234 . 27 LYS C C 176.181 0.100 1 235 . 27 LYS CA C 57.093 0.100 1 236 . 27 LYS HA H 4.208 0.010 1 237 . 27 LYS CB C 33.809 0.100 1 238 . 27 LYS HB2 H 1.712 0.010 1 239 . 27 LYS HB3 H 1.552 0.010 1 240 . 27 LYS CG C 25.404 0.100 1 241 . 27 LYS HG2 H 1.329 0.010 1 242 . 27 LYS CD C 29.779 0.100 1 243 . 27 LYS HD2 H 1.614 0.010 1 244 . 27 LYS CE C 42.904 0.100 1 245 . 27 LYS HE2 H 2.929 0.010 1 246 . 28 LEU H H 8.775 0.010 1 247 . 28 LEU N N 126.525 0.100 1 248 . 28 LEU C C 175.327 0.100 1 249 . 28 LEU CA C 55.522 0.100 1 250 . 28 LEU HA H 4.535 0.010 1 251 . 28 LEU CB C 43.593 0.100 1 252 . 28 LEU HB2 H 1.872 0.010 1 253 . 28 LEU HB3 H 1.294 0.010 1 254 . 28 LEU CG C 27.270 0.100 1 255 . 28 LEU HG H 1.200 0.010 1 256 . 28 LEU CD1 C 23.990 0.100 1 257 . 28 LEU HD1 H 0.910 0.010 1 258 . 28 LEU CD2 C 26.810 0.100 1 259 . 28 LEU HD2 H 0.660 0.010 1 260 . 29 ILE H H 8.808 0.010 1 261 . 29 ILE N N 126.495 0.100 1 262 . 29 ILE C C 175.210 0.100 1 263 . 29 ILE CA C 60.178 0.100 1 264 . 29 ILE HA H 4.677 0.010 1 265 . 29 ILE CB C 41.107 0.100 1 266 . 29 ILE HB H 1.492 0.010 1 267 . 29 ILE CG1 C 28.060 0.100 1 268 . 29 ILE HG12 H 0.691 0.010 1 269 . 29 ILE CG2 C 17.903 0.100 1 270 . 29 ILE HG2 H 0.427 0.010 1 271 . 29 ILE CD1 C 14.622 0.100 1 272 . 29 ILE HD1 H 0.501 0.010 1 273 . 30 VAL H H 8.738 0.010 1 274 . 30 VAL N N 126.523 0.100 1 275 . 30 VAL C C 175.028 0.100 1 276 . 30 VAL CA C 60.530 0.100 1 277 . 30 VAL HA H 4.486 0.010 1 278 . 30 VAL CB C 33.681 0.100 1 279 . 30 VAL HB H 1.891 0.010 1 280 . 30 VAL CG1 C 21.810 0.100 1 281 . 30 VAL HG1 H 0.210 0.010 1 282 . 30 VAL CG2 C 21.810 0.100 1 283 . 30 VAL HG2 H 0.081 0.010 1 284 . 31 VAL H H 8.831 0.010 1 285 . 31 VAL N N 126.363 0.100 1 286 . 31 VAL C C 174.886 0.100 1 287 . 31 VAL CA C 60.603 0.100 1 288 . 31 VAL HA H 4.655 0.010 1 289 . 31 VAL CB C 34.469 0.100 1 290 . 31 VAL HB H 1.649 0.010 1 291 . 31 VAL CG1 C 21.960 0.100 1 292 . 31 VAL HG1 H 0.650 0.010 1 293 . 31 VAL CG2 C 21.960 0.100 1 294 . 31 VAL HG2 H -0.070 0.010 1 295 . 32 ASP H H 8.406 0.010 1 296 . 32 ASP N N 123.118 0.100 1 297 . 32 ASP C C 175.021 0.100 1 298 . 32 ASP CA C 51.287 0.100 1 299 . 32 ASP HA H 4.077 0.010 1 300 . 32 ASP CB C 39.570 0.100 1 301 . 32 ASP HB2 H 2.128 0.010 1 302 . 32 ASP HB3 H 1.235 0.010 1 303 . 33 PHE H H 8.684 0.010 1 304 . 33 PHE N N 125.848 0.100 1 305 . 33 PHE C C 173.784 0.100 1 306 . 33 PHE CA C 58.811 0.100 1 307 . 33 PHE HA H 4.921 0.010 1 308 . 33 PHE CB C 39.683 0.100 1 309 . 33 PHE HB2 H 2.860 0.010 1 310 . 33 PHE HB3 H 2.399 0.010 1 311 . 34 THR H H 8.339 0.010 1 312 . 34 THR N N 116.343 0.100 1 313 . 34 THR C C 171.024 0.100 1 314 . 34 THR CA C 59.110 0.100 1 315 . 34 THR HA H 4.385 0.010 1 316 . 34 THR CB C 71.410 0.100 1 317 . 34 THR HB H 3.360 0.010 1 318 . 34 THR CG2 C 19.153 0.100 1 319 . 34 THR HG2 H 0.675 0.010 1 320 . 35 ALA H H 6.993 0.010 1 321 . 35 ALA N N 121.130 0.100 1 322 . 35 ALA C C 178.776 0.100 1 323 . 35 ALA CA C 51.721 0.100 1 324 . 35 ALA HA H 4.559 0.010 1 325 . 35 ALA CB C 22.994 0.100 1 326 . 35 ALA HB H 0.300 0.010 1 327 . 36 SER H H 9.409 0.010 1 328 . 36 SER N N 118.628 0.100 1 329 . 36 SER CA C 61.536 0.100 1 330 . 36 SER HA H 3.977 0.010 1 331 . 36 SER CB C 63.464 0.100 1 332 . 36 SER HB2 H 3.818 0.010 1 333 . 36 SER HB3 H 3.818 0.010 1 334 . 37 TRP H H 6.825 0.010 1 335 . 37 TRP N N 117.255 0.100 1 336 . 37 TRP C C 175.634 0.100 1 337 . 37 TRP CA C 54.444 0.100 1 338 . 37 TRP HA H 3.852 0.010 1 339 . 37 TRP CB C 29.150 0.100 1 340 . 37 TRP HB2 H 2.171 0.010 1 341 . 37 TRP HB3 H 3.123 0.010 1 342 . 39 PRO CA C 67.593 0.100 1 343 . 39 PRO HA H 4.452 0.010 1 344 . 40 PRO C C 178.600 0.100 1 345 . 40 PRO CA C 66.684 0.100 1 346 . 40 PRO HA H 4.465 0.010 1 347 . 40 PRO CB C 31.874 0.100 1 348 . 40 PRO HB2 H 3.801 0.010 1 349 . 40 PRO HB3 H 3.128 0.010 1 350 . 40 PRO CG C 28.998 0.100 1 351 . 40 PRO HG2 H 2.157 0.010 1 352 . 40 PRO CD C 51.498 0.100 1 353 . 40 PRO HD2 H 3.768 0.010 1 354 . 41 CYS H H 8.098 0.010 1 355 . 41 CYS N N 113.267 0.100 1 356 . 41 CYS C C 177.100 0.100 1 357 . 41 CYS CA C 64.014 0.100 1 358 . 41 CYS HA H 4.129 0.010 1 359 . 41 CYS CB C 33.747 0.100 1 360 . 41 CYS HB2 H 3.995 0.010 1 361 . 41 CYS HB3 H 3.190 0.010 1 362 . 42 LYS H H 7.615 0.010 1 363 . 42 LYS N N 120.820 0.100 1 364 . 42 LYS C C 179.617 0.100 1 365 . 42 LYS CA C 59.434 0.100 1 366 . 42 LYS HA H 4.041 0.010 1 367 . 42 LYS CB C 32.661 0.100 1 368 . 42 LYS HB2 H 1.918 0.010 1 369 . 42 LYS HB3 H 1.887 0.010 1 370 . 42 LYS CG C 25.716 0.100 1 371 . 42 LYS HG2 H 1.542 0.010 1 372 . 42 LYS HG3 H 1.415 0.010 1 373 . 42 LYS CD C 29.935 0.100 1 374 . 42 LYS HD2 H 1.621 0.010 1 375 . 42 LYS CE C 42.904 0.100 1 376 . 42 LYS HE2 H 3.041 0.010 1 377 . 43 MET H H 7.528 0.010 1 378 . 43 MET N N 118.008 0.100 1 379 . 43 MET C C 178.284 0.100 1 380 . 43 MET CA C 58.742 0.100 1 381 . 43 MET HA H 4.161 0.010 1 382 . 43 MET CB C 33.064 0.100 1 383 . 43 MET HB2 H 2.690 0.010 1 384 . 43 MET HB3 H 2.510 0.010 1 385 . 44 ILE H H 7.484 0.010 1 386 . 44 ILE N N 114.582 0.100 1 387 . 44 ILE C C 176.576 0.100 1 388 . 44 ILE CA C 58.943 0.100 1 389 . 44 ILE HA H 4.590 0.010 1 390 . 44 ILE CB C 41.270 0.100 1 391 . 44 ILE HB H 1.726 0.010 1 392 . 44 ILE CG1 C 31.029 0.100 1 393 . 44 ILE HG12 H 1.599 0.010 1 394 . 44 ILE HG13 H 1.416 0.010 1 395 . 44 ILE CG2 C 20.091 0.100 1 396 . 44 ILE HG2 H 1.127 0.010 1 397 . 44 ILE CD1 C 14.622 0.100 1 398 . 44 ILE HD1 H 0.735 0.010 1 399 . 45 ALA H H 7.748 0.010 1 400 . 45 ALA N N 127.417 0.100 1 401 . 45 ALA C C 177.410 0.100 1 402 . 45 ALA CA C 57.561 0.100 1 403 . 45 ALA HA H 4.147 0.010 1 404 . 45 ALA CB C 16.538 0.100 1 405 . 45 ALA HB H 1.577 0.010 1 406 . 46 PRO C C 180.013 0.100 1 407 . 46 PRO CA C 66.377 0.100 1 408 . 46 PRO HA H 4.456 0.010 1 409 . 46 PRO CB C 31.810 0.100 1 410 . 46 PRO HB2 H 2.310 0.010 1 411 . 46 PRO HB3 H 1.840 0.010 1 412 . 46 PRO CG C 29.146 0.100 1 413 . 46 PRO HG2 H 2.214 0.010 1 414 . 46 PRO HG3 H 2.134 0.010 1 415 . 46 PRO CD C 51.685 0.100 1 416 . 46 PRO HD2 H 3.748 0.010 1 417 . 47 ILE H H 7.001 0.010 1 418 . 47 ILE N N 119.503 0.100 1 419 . 47 ILE C C 178.208 0.100 1 420 . 47 ILE CA C 64.003 0.100 1 421 . 47 ILE HA H 3.850 0.010 1 422 . 47 ILE CB C 37.848 0.100 1 423 . 47 ILE HB H 2.167 0.010 1 424 . 47 ILE CG1 C 30.091 0.100 1 425 . 47 ILE HG12 H 1.541 0.010 1 426 . 47 ILE HG13 H 1.414 0.010 1 427 . 47 ILE CG2 C 17.903 0.100 1 428 . 47 ILE HG2 H 0.915 0.010 1 429 . 47 ILE CD1 C 13.372 0.100 1 430 . 47 ILE HD1 H 0.917 0.010 1 431 . 48 PHE H H 7.996 0.010 1 432 . 48 PHE N N 122.492 0.100 1 433 . 48 PHE C C 176.333 0.100 1 434 . 48 PHE CA C 62.887 0.100 1 435 . 48 PHE HA H 4.043 0.010 1 436 . 48 PHE CB C 40.113 0.100 1 437 . 48 PHE HB2 H 3.310 0.010 1 438 . 48 PHE HB3 H 2.830 0.010 1 439 . 49 ALA H H 7.736 0.010 1 440 . 49 ALA N N 116.255 0.100 1 441 . 49 ALA C C 180.982 0.100 1 442 . 49 ALA CA C 55.199 0.100 1 443 . 49 ALA HA H 3.754 0.010 1 444 . 49 ALA CB C 18.570 0.100 1 445 . 49 ALA HB H 1.419 0.010 1 446 . 50 GLU H H 7.784 0.010 1 447 . 50 GLU N N 120.257 0.100 1 448 . 50 GLU C C 180.103 0.100 1 449 . 50 GLU CA C 59.630 0.100 1 450 . 50 GLU HA H 3.885 0.010 1 451 . 50 GLU CB C 29.783 0.100 1 452 . 50 GLU HB2 H 2.260 0.010 1 453 . 50 GLU HB3 H 2.190 0.010 1 454 . 51 LEU H H 7.996 0.010 1 455 . 51 LEU N N 121.085 0.100 1 456 . 51 LEU C C 177.669 0.100 1 457 . 51 LEU CA C 58.327 0.100 1 458 . 51 LEU HA H 3.921 0.010 1 459 . 51 LEU CB C 42.064 0.100 1 460 . 51 LEU HB2 H 1.120 0.010 1 461 . 51 LEU HB3 H 1.660 0.010 1 462 . 51 LEU CG C 27.122 0.100 1 463 . 51 LEU HG H 1.919 0.010 1 464 . 51 LEU CD1 C 24.154 0.100 1 465 . 51 LEU HD1 H 0.947 0.010 1 466 . 51 LEU CD2 C 24.122 0.100 1 467 . 51 LEU HD2 H 0.701 0.010 1 468 . 52 ALA H H 6.650 0.010 1 469 . 52 ALA N N 119.817 0.100 1 470 . 52 ALA C C 179.911 0.100 1 471 . 52 ALA CA C 54.394 0.100 1 472 . 52 ALA HA H 3.165 0.010 1 473 . 52 ALA CB C 18.253 0.100 1 474 . 52 ALA HB H 0.458 0.010 1 475 . 53 LYS H H 6.694 0.010 1 476 . 53 LYS N N 114.545 0.100 1 477 . 53 LYS C C 178.835 0.100 1 478 . 53 LYS CA C 58.576 0.100 1 479 . 53 LYS HA H 3.946 0.010 1 480 . 53 LYS CB C 33.323 0.100 1 481 . 53 LYS HB2 H 1.762 0.010 1 482 . 53 LYS HB3 H 1.584 0.010 1 483 . 53 LYS CG C 25.716 0.100 1 484 . 53 LYS HG2 H 1.442 0.010 1 485 . 53 LYS HG3 H 1.299 0.010 1 486 . 53 LYS CD C 29.935 0.100 1 487 . 53 LYS HD2 H 1.583 0.010 1 488 . 53 LYS CE C 42.748 0.100 1 489 . 53 LYS HE2 H 2.862 0.010 1 490 . 54 LYS H H 7.474 0.010 1 491 . 54 LYS N N 118.668 0.100 1 492 . 54 LYS C C 176.412 0.100 1 493 . 54 LYS CA C 58.305 0.100 1 494 . 54 LYS HA H 3.845 0.010 1 495 . 54 LYS CB C 34.076 0.100 1 496 . 54 LYS HB2 H 1.677 0.010 1 497 . 54 LYS HB3 H 1.550 0.010 1 498 . 54 LYS CG C 26.029 0.100 1 499 . 54 LYS HG2 H 1.244 0.010 1 500 . 54 LYS HG3 H 0.994 0.010 1 501 . 54 LYS CD C 30.091 0.100 1 502 . 54 LYS HD2 H 1.433 0.010 1 503 . 54 LYS CE C 42.748 0.100 1 504 . 54 LYS HE2 H 2.774 0.010 1 505 . 55 PHE H H 7.718 0.010 1 506 . 55 PHE N N 116.516 0.100 1 507 . 55 PHE C C 174.077 0.100 1 508 . 55 PHE CA C 56.410 0.100 1 509 . 55 PHE HA H 4.980 0.010 1 510 . 55 PHE CB C 39.230 0.100 1 511 . 55 PHE HB2 H 3.048 0.010 1 512 . 55 PHE HB3 H 2.974 0.010 1 513 . 56 PRO C C 177.232 0.100 1 514 . 56 PRO CA C 64.920 0.100 1 515 . 56 PRO HA H 4.674 0.010 1 516 . 56 PRO CB C 32.130 0.100 1 517 . 56 PRO HB2 H 3.618 0.010 1 518 . 56 PRO HB3 H 3.260 0.010 1 519 . 56 PRO CG C 27.747 0.100 1 520 . 56 PRO HG2 H 1.915 0.010 1 521 . 56 PRO HG3 H 1.856 0.010 1 522 . 56 PRO CD C 51.186 0.100 1 523 . 56 PRO HD2 H 3.591 0.010 1 524 . 56 PRO HD3 H 3.247 0.010 1 525 . 57 ASN H H 8.955 0.010 1 526 . 57 ASN N N 114.762 0.100 1 527 . 57 ASN C C 174.150 0.100 1 528 . 57 ASN CA C 54.065 0.100 1 529 . 57 ASN HA H 4.708 0.010 1 530 . 57 ASN CB C 38.012 0.100 1 531 . 57 ASN HB2 H 2.918 0.010 1 532 . 57 ASN HB3 H 2.821 0.010 1 533 . 58 VAL H H 8.068 0.010 1 534 . 58 VAL N N 125.172 0.100 1 535 . 58 VAL C C 176.411 0.100 1 536 . 58 VAL CA C 61.667 0.100 1 537 . 58 VAL HA H 4.179 0.010 1 538 . 58 VAL CB C 34.455 0.100 1 539 . 58 VAL HB H 2.308 0.010 1 540 . 58 VAL CG1 C 23.997 0.100 1 541 . 58 VAL HG1 H 0.805 0.010 1 542 . 58 VAL CG2 C 22.904 0.100 1 543 . 58 VAL HG2 H -0.041 0.010 1 544 . 59 THR H H 8.076 0.010 1 545 . 59 THR N N 123.484 0.100 1 546 . 59 THR C C 176.414 0.100 1 547 . 59 THR CA C 63.103 0.100 1 548 . 59 THR HA H 4.387 0.010 1 549 . 59 THR CB C 70.346 0.100 1 550 . 59 THR HB H 3.846 0.010 1 551 . 59 THR CG2 C 22.591 0.100 1 552 . 59 THR HG2 H 0.966 0.010 1 553 . 60 PHE H H 9.240 0.010 1 554 . 60 PHE N N 128.386 0.100 1 555 . 60 PHE C C 176.578 0.100 1 556 . 60 PHE CA C 57.233 0.100 1 557 . 60 PHE HA H 5.017 0.010 1 558 . 60 PHE CB C 40.073 0.100 1 559 . 60 PHE HB2 H 2.689 0.010 1 560 . 60 PHE HB3 H 2.157 0.010 1 561 . 61 LEU H H 9.108 0.010 1 562 . 61 LEU N N 121.353 0.100 1 563 . 61 LEU C C 176.354 0.100 1 564 . 61 LEU CA C 53.022 0.100 1 565 . 61 LEU HA H 5.426 0.010 1 566 . 61 LEU CB C 46.030 0.100 1 567 . 61 LEU HB2 H 1.617 0.010 1 568 . 61 LEU HB3 H 1.224 0.010 1 569 . 61 LEU CG C 27.590 0.100 1 570 . 61 LEU HG H 1.310 0.010 1 571 . 61 LEU CD1 C 26.810 0.100 1 572 . 61 LEU HD1 H 0.510 0.010 1 573 . 61 LEU CD2 C 24.620 0.100 1 574 . 62 LYS HD2 H 1.527 0.010 1 575 . 62 LYS H H 8.524 0.010 1 576 . 62 LYS N N 121.704 0.100 1 577 . 62 LYS C C 175.225 0.100 1 578 . 62 LYS CA C 55.456 0.100 1 579 . 62 LYS HA H 4.853 0.010 1 580 . 62 LYS CB C 36.619 0.100 1 581 . 62 LYS HB2 H 1.547 0.010 1 582 . 62 LYS HB3 H 1.452 0.010 1 583 . 62 LYS CG C 25.560 0.100 1 584 . 62 LYS HG2 H 1.098 0.010 1 585 . 62 LYS HG3 H 0.920 0.010 1 586 . 62 LYS CD C 30.716 0.100 1 587 . 62 LYS HD3 H 1.462 0.010 1 588 . 62 LYS CE C 42.436 0.100 1 589 . 62 LYS HE2 H 2.723 0.010 1 590 . 63 VAL H H 8.639 0.010 1 591 . 63 VAL N N 128.995 0.100 1 592 . 63 VAL C C 173.225 0.100 1 593 . 63 VAL CA C 62.090 0.100 1 594 . 63 VAL HA H 3.761 0.010 1 595 . 63 VAL CB C 35.410 0.100 1 596 . 63 VAL HB H 1.075 0.010 1 597 . 63 VAL CG1 C 22.747 0.100 1 598 . 63 VAL HG1 H 0.610 0.010 1 599 . 63 VAL CG2 C 22.122 0.100 1 600 . 63 VAL HG2 H 0.293 0.010 1 601 . 64 ASP H H 9.161 0.010 1 602 . 64 ASP N N 129.241 0.100 1 603 . 64 ASP C C 178.455 0.100 1 604 . 64 ASP CA C 53.085 0.100 1 605 . 64 ASP HA H 4.834 0.010 1 606 . 64 ASP CB C 42.780 0.100 1 607 . 64 ASP HB2 H 2.836 0.010 1 608 . 64 ASP HB3 H 2.192 0.010 1 609 . 65 VAL H H 8.801 0.010 1 610 . 65 VAL N N 121.704 0.100 1 611 . 65 VAL C C 176.284 0.100 1 612 . 65 VAL CA C 65.313 0.100 1 613 . 65 VAL HA H 3.557 0.010 1 614 . 65 VAL CB C 31.540 0.100 1 615 . 65 VAL HB H 2.134 0.010 1 616 . 65 VAL CG1 C 23.060 0.100 1 617 . 65 VAL HG1 H 0.993 0.010 1 618 . 65 VAL CG2 C 19.153 0.100 1 619 . 65 VAL HG2 H 0.902 0.010 1 620 . 66 ASP H H 8.428 0.010 1 621 . 66 ASP N N 118.248 0.100 1 622 . 66 ASP C C 178.452 0.100 1 623 . 66 ASP CA C 56.652 0.100 1 624 . 66 ASP HA H 4.725 0.010 1 625 . 66 ASP CB C 41.416 0.100 1 626 . 66 ASP HB2 H 2.797 0.010 1 627 . 66 ASP HB3 H 2.693 0.010 1 628 . 67 GLU H H 8.011 0.010 1 629 . 67 GLU N N 121.261 0.100 1 630 . 67 GLU C C 176.424 0.100 1 631 . 67 GLU CA C 58.865 0.100 1 632 . 67 GLU HA H 4.243 0.010 1 633 . 67 GLU CB C 31.655 0.100 1 634 . 67 GLU HB2 H 2.362 0.010 1 635 . 67 GLU HB3 H 2.362 0.010 1 636 . 67 GLU CG C 37.435 0.100 1 637 . 67 GLU HG2 H 2.360 0.010 1 638 . 68 LEU H H 7.922 0.010 1 639 . 68 LEU N N 121.705 0.100 1 640 . 68 LEU C C 176.656 0.100 1 641 . 68 LEU CA C 52.689 0.100 1 642 . 68 LEU HA H 4.739 0.010 1 643 . 68 LEU CB C 41.589 0.100 1 644 . 68 LEU HB2 H 1.488 0.010 1 645 . 68 LEU HB3 H 1.425 0.010 1 646 . 68 LEU CG C 28.060 0.100 1 647 . 68 LEU HG H 1.393 0.010 1 648 . 68 LEU CD1 C 26.341 0.100 1 649 . 68 LEU HD1 H 0.655 0.010 1 650 . 68 LEU CD2 C 25.091 0.100 1 651 . 68 LEU HD2 H 0.651 0.010 1 652 . 69 LYS H H 7.367 0.010 1 653 . 69 LYS N N 124.196 0.100 1 654 . 69 LYS C C 179.150 0.100 1 655 . 69 LYS CA C 60.661 0.100 1 656 . 69 LYS HA H 4.047 0.010 1 657 . 69 LYS CB C 33.170 0.100 1 658 . 69 LYS HB2 H 1.909 0.010 1 659 . 69 LYS HB3 H 1.708 0.010 1 660 . 69 LYS CG C 25.247 0.100 1 661 . 69 LYS HG2 H 1.415 0.010 1 662 . 69 LYS CD C 29.935 0.100 1 663 . 69 LYS HD2 H 1.675 0.010 1 664 . 69 LYS CE C 42.904 0.100 1 665 . 69 LYS HE2 H 3.036 0.010 1 666 . 70 ALA H H 8.640 0.010 1 667 . 70 ALA N N 117.750 0.100 1 668 . 70 ALA C C 181.491 0.100 1 669 . 70 ALA CA C 55.445 0.100 1 670 . 70 ALA HA H 4.078 0.010 1 671 . 70 ALA CB C 19.016 0.100 1 672 . 70 ALA HB H 1.323 0.010 1 673 . 71 VAL H H 6.869 0.010 1 674 . 71 VAL N N 118.274 0.100 1 675 . 71 VAL C C 177.738 0.100 1 676 . 71 VAL CA C 65.948 0.100 1 677 . 71 VAL HA H 3.622 0.010 1 678 . 71 VAL CB C 32.106 0.100 1 679 . 71 VAL HB H 1.684 0.010 1 680 . 71 VAL CG1 C 23.216 0.100 1 681 . 71 VAL HG1 H 0.486 0.010 1 682 . 71 VAL CG2 C 20.872 0.100 1 683 . 71 VAL HG2 H 0.151 0.010 1 684 . 72 ALA H H 7.250 0.010 1 685 . 72 ALA N N 121.354 0.100 1 686 . 72 ALA C C 179.935 0.100 1 687 . 72 ALA CA C 55.644 0.100 1 688 . 72 ALA HA H 3.450 0.010 1 689 . 72 ALA CB C 18.514 0.100 1 690 . 72 ALA HB H 1.197 0.010 1 691 . 73 GLU H H 8.201 0.010 1 692 . 73 GLU N N 116.076 0.100 1 693 . 73 GLU C C 181.039 0.100 1 694 . 73 GLU CA C 59.579 0.100 1 695 . 73 GLU HA H 3.982 0.010 1 696 . 73 GLU CB C 29.963 0.100 1 697 . 73 GLU HB2 H 2.066 0.010 1 698 . 73 GLU HB3 H 1.959 0.010 1 699 . 73 GLU CG C 37.123 0.100 1 700 . 73 GLU HG2 H 2.360 0.010 1 701 . 73 GLU HG3 H 2.111 0.010 1 702 . 74 GLU H H 7.586 0.010 1 703 . 74 GLU N N 122.095 0.100 1 704 . 74 GLU C C 177.894 0.100 1 705 . 74 GLU CA C 59.472 0.100 1 706 . 74 GLU HA H 3.711 0.010 1 707 . 74 GLU CB C 29.456 0.100 1 708 . 74 GLU HB2 H 1.938 0.010 1 709 . 74 GLU HB3 H 1.938 0.010 1 710 . 74 GLU CG C 36.029 0.100 1 711 . 74 GLU HG2 H 1.928 0.010 1 712 . 74 GLU HG3 H 1.488 0.010 1 713 . 75 TRP H H 6.989 0.010 1 714 . 75 TRP N N 116.423 0.100 1 715 . 75 TRP C C 174.507 0.100 1 716 . 75 TRP CA C 57.442 0.100 1 717 . 75 TRP HA H 4.225 0.010 1 718 . 75 TRP CB C 28.908 0.100 1 719 . 75 TRP HB2 H 3.402 0.010 1 720 . 75 TRP HB3 H 2.248 0.010 1 721 . 76 ASN H H 7.762 0.010 1 722 . 76 ASN N N 116.690 0.100 1 723 . 76 ASN C C 175.042 0.100 1 724 . 76 ASN CA C 54.554 0.100 1 725 . 76 ASN HA H 4.177 0.010 1 726 . 76 ASN CB C 37.763 0.100 1 727 . 76 ASN HB2 H 3.383 0.010 1 728 . 76 ASN HB3 H 2.215 0.010 1 729 . 77 VAL H H 7.586 0.010 1 730 . 77 VAL N N 118.892 0.100 1 731 . 77 VAL C C 176.809 0.100 1 732 . 77 VAL CA C 65.134 0.100 1 733 . 77 VAL HA H 3.537 0.010 1 734 . 77 VAL CB C 31.257 0.100 1 735 . 77 VAL HB H 1.452 0.010 1 736 . 77 VAL CG1 C 21.966 0.100 1 737 . 77 VAL HG1 H 0.580 0.010 1 738 . 77 VAL CG2 C 22.435 0.100 1 739 . 77 VAL HG2 H -0.082 0.010 1 740 . 78 GLU H H 8.727 0.010 1 741 . 78 GLU N N 128.651 0.100 1 742 . 78 GLU C C 175.319 0.100 1 743 . 78 GLU CA C 56.833 0.100 1 744 . 78 GLU HA H 4.356 0.010 1 745 . 78 GLU CB C 32.778 0.100 1 746 . 78 GLU HB2 H 1.850 0.010 1 747 . 78 GLU HB3 H 1.630 0.010 1 748 . 78 GLU CG C 36.654 0.100 1 749 . 78 GLU HG2 H 2.115 0.010 1 750 . 78 GLU HG3 H 2.000 0.010 1 751 . 79 ALA H H 7.659 0.010 1 752 . 79 ALA N N 122.935 0.100 1 753 . 79 ALA C C 176.200 0.100 1 754 . 79 ALA CA C 52.006 0.100 1 755 . 79 ALA HA H 4.411 0.010 1 756 . 79 ALA CB C 21.620 0.100 1 757 . 79 ALA HB H 1.237 0.010 1 758 . 80 MET H H 8.327 0.010 1 759 . 80 MET N N 118.191 0.100 1 760 . 80 MET C C 174.857 0.100 1 761 . 80 MET CA C 52.570 0.100 1 762 . 80 MET HA H 4.910 0.010 1 763 . 80 MET CB C 34.163 0.100 1 764 . 80 MET HB2 H 1.865 0.010 1 765 . 80 MET HB3 H 1.660 0.010 1 766 . 80 MET CE C 18.216 0.100 1 767 . 80 MET HE H 1.679 0.010 1 768 . 81 PRO C C 176.701 0.100 1 769 . 81 PRO CA C 63.910 0.100 1 770 . 81 PRO HA H 4.958 0.010 1 771 . 81 PRO CB C 34.860 0.100 1 772 . 81 PRO HB2 H 2.120 0.010 1 773 . 81 PRO HB3 H 1.430 0.010 1 774 . 81 PRO CG C 25.560 0.100 1 775 . 81 PRO HG2 H 1.840 0.010 1 776 . 81 PRO HG3 H 1.630 0.010 1 777 . 81 PRO CD C 50.240 0.100 1 778 . 81 PRO HD2 H 3.620 0.010 1 779 . 81 PRO HD3 H 3.240 0.010 1 780 . 82 THR H H 7.849 0.010 1 781 . 82 THR N N 115.112 0.100 1 782 . 82 THR C C 172.120 0.100 1 783 . 82 THR CA C 63.934 0.100 1 784 . 82 THR HA H 4.830 0.010 1 785 . 82 THR CB C 73.453 0.100 1 786 . 82 THR HB H 3.864 0.010 1 787 . 82 THR CG2 C 21.966 0.100 1 788 . 82 THR HG2 H 1.200 0.010 1 789 . 83 PHE H H 9.314 0.010 1 790 . 83 PHE N N 124.615 0.100 1 791 . 83 PHE C C 176.415 0.100 1 792 . 83 PHE CA C 56.163 0.100 1 793 . 83 PHE HA H 5.875 0.010 1 794 . 83 PHE CB C 41.490 0.100 1 795 . 83 PHE HB2 H 2.990 0.010 1 796 . 83 PHE HB3 H 2.390 0.010 1 797 . 84 ILE H H 8.523 0.010 1 798 . 84 ILE N N 117.048 0.100 1 799 . 84 ILE C C 173.610 0.100 1 800 . 84 ILE CA C 60.317 0.100 1 801 . 84 ILE HA H 4.993 0.010 1 802 . 84 ILE CB C 41.036 0.100 1 803 . 84 ILE HB H 1.716 0.010 1 804 . 84 ILE CG1 C 27.904 0.100 1 805 . 84 ILE HG12 H 1.313 0.010 1 806 . 84 ILE HG13 H 1.093 0.010 1 807 . 84 ILE CG2 C 18.060 0.100 1 808 . 84 ILE HG2 H 0.827 0.010 1 809 . 84 ILE CD1 C 13.528 0.100 1 810 . 84 ILE HD1 H 0.387 0.010 1 811 . 85 PHE H H 8.143 0.010 1 812 . 85 PHE N N 123.497 0.100 1 813 . 85 PHE C C 176.728 0.100 1 814 . 85 PHE CA C 56.887 0.100 1 815 . 85 PHE HA H 4.938 0.010 1 816 . 85 PHE CB C 40.334 0.100 1 817 . 85 PHE HB2 H 2.723 0.010 1 818 . 85 PHE HB3 H 2.119 0.010 1 819 . 86 LEU H H 9.588 0.010 1 820 . 86 LEU N N 126.152 0.100 1 821 . 86 LEU C C 176.283 0.100 1 822 . 86 LEU CA C 53.985 0.100 1 823 . 86 LEU HA H 5.316 0.010 1 824 . 86 LEU CB C 46.848 0.100 1 825 . 86 LEU HB2 H 1.568 0.010 1 826 . 86 LEU HB3 H 1.148 0.010 1 827 . 86 LEU CG C 26.966 0.100 1 828 . 86 LEU HG H 1.173 0.010 1 829 . 86 LEU CD1 C 24.779 0.100 1 830 . 86 LEU HD1 H 0.479 0.010 1 831 . 86 LEU CD2 C 26.654 0.100 1 832 . 86 LEU HD2 H 0.497 0.010 1 833 . 87 LYS H H 8.612 0.010 1 834 . 87 LYS N N 119.417 0.100 1 835 . 87 LYS C C 177.696 0.100 1 836 . 87 LYS CA C 57.023 0.100 1 837 . 87 LYS HA H 4.534 0.010 1 838 . 87 LYS CB C 37.400 0.100 1 839 . 87 LYS HB2 H 1.542 0.010 1 840 . 87 LYS HB3 H 1.446 0.010 1 841 . 87 LYS CG C 26.654 0.100 1 842 . 87 LYS HG2 H 1.231 0.010 1 843 . 87 LYS CD C 31.029 0.100 1 844 . 87 LYS HD2 H 1.742 0.010 1 845 . 87 LYS CE C 42.904 0.100 1 846 . 87 LYS HE2 H 2.971 0.010 1 847 . 88 ASP H H 9.224 0.010 1 848 . 88 ASP N N 128.736 0.100 1 849 . 88 ASP C C 176.652 0.100 1 850 . 88 ASP CA C 55.888 0.100 1 851 . 88 ASP HA H 4.535 0.010 1 852 . 88 ASP CB C 40.590 0.100 1 853 . 88 ASP HB2 H 2.964 0.010 1 854 . 88 ASP HB3 H 2.319 0.010 1 855 . 89 GLY H H 9.299 0.010 1 856 . 89 GLY N N 104.213 0.100 1 857 . 89 GLY C C 173.759 0.100 1 858 . 89 GLY CA C 46.066 0.100 1 859 . 89 GLY HA2 H 3.848 0.010 1 860 . 89 GLY HA3 H 3.245 0.010 1 861 . 90 LYS H H 7.748 0.010 1 862 . 90 LYS N N 119.422 0.100 1 863 . 90 LYS C C 175.408 0.100 1 864 . 90 LYS CA C 54.920 0.100 1 865 . 90 LYS HA H 4.712 0.010 1 866 . 90 LYS CB C 35.904 0.100 1 867 . 90 LYS HB2 H 1.809 0.010 1 868 . 90 LYS HB3 H 1.695 0.010 1 869 . 90 LYS CG C 25.404 0.100 1 870 . 90 LYS HG2 H 1.391 0.010 1 871 . 90 LYS CD C 29.935 0.100 1 872 . 90 LYS HD2 H 1.684 0.010 1 873 . 90 LYS CE C 43.061 0.100 1 874 . 90 LYS HE2 H 3.023 0.010 1 875 . 91 LEU H H 8.727 0.010 1 876 . 91 LEU N N 123.285 0.100 1 877 . 91 LEU C C 178.527 0.100 1 878 . 91 LEU CA C 56.868 0.100 1 879 . 91 LEU HA H 4.581 0.010 1 880 . 91 LEU CB C 43.320 0.100 1 881 . 91 LEU HB2 H 1.734 0.010 1 882 . 91 LEU HB3 H 1.620 0.010 1 883 . 91 LEU CG C 28.097 0.100 1 884 . 91 LEU HG H 1.672 0.010 1 885 . 91 LEU CD1 C 27.591 0.100 1 886 . 91 LEU HD1 H 1.210 0.010 1 887 . 91 LEU CD2 C 26.810 0.100 1 888 . 91 LEU HD2 H 0.987 0.010 1 889 . 92 VAL H H 9.298 0.010 1 890 . 92 VAL N N 122.290 0.100 1 891 . 92 VAL C C 175.917 0.100 1 892 . 92 VAL CA C 61.829 0.100 1 893 . 92 VAL HA H 4.499 0.010 1 894 . 92 VAL CB C 33.789 0.100 1 895 . 92 VAL HB H 2.023 0.010 1 896 . 92 VAL CG1 C 22.747 0.100 1 897 . 92 VAL HG1 H 0.790 0.010 1 898 . 92 VAL CG2 C 19.310 0.100 1 899 . 92 VAL HG2 H 0.783 0.010 1 900 . 93 ASP H H 7.849 0.010 1 901 . 93 ASP N N 119.059 0.100 1 902 . 93 ASP C C 174.493 0.100 1 903 . 93 ASP CA C 54.270 0.100 1 904 . 93 ASP HA H 4.633 0.010 1 905 . 93 ASP CB C 44.620 0.100 1 906 . 93 ASP HB2 H 2.886 0.010 1 907 . 93 ASP HB3 H 2.848 0.010 1 908 . 94 LYS H H 8.918 0.010 1 909 . 94 LYS N N 119.065 0.100 1 910 . 94 LYS C C 175.455 0.100 1 911 . 94 LYS CA C 56.608 0.100 1 912 . 94 LYS HA H 5.525 0.010 1 913 . 94 LYS CB C 36.905 0.100 1 914 . 94 LYS HB2 H 1.870 0.010 1 915 . 94 LYS HB3 H 2.027 0.010 1 916 . 94 LYS CG C 25.091 0.100 1 917 . 94 LYS HG2 H 1.503 0.010 1 918 . 94 LYS HG3 H 1.304 0.010 1 919 . 94 LYS CD C 30.560 0.100 1 920 . 94 LYS HD2 H 1.684 0.010 1 921 . 94 LYS CE C 42.748 0.100 1 922 . 94 LYS HE2 H 2.850 0.010 1 923 . 95 THR H H 9.298 0.010 1 924 . 95 THR N N 119.244 0.100 1 925 . 95 THR C C 172.201 0.100 1 926 . 95 THR CA C 61.674 0.100 1 927 . 95 THR HA H 4.825 0.010 1 928 . 95 THR CB C 71.062 0.100 1 929 . 95 THR HB H 4.064 0.010 1 930 . 95 THR CG2 C 21.653 0.100 1 931 . 95 THR HG2 H 1.285 0.010 1 932 . 96 VAL H H 8.304 0.010 1 933 . 96 VAL N N 123.807 0.100 1 934 . 96 VAL C C 176.802 0.100 1 935 . 96 VAL CA C 60.452 0.100 1 936 . 96 VAL HA H 4.901 0.010 1 937 . 96 VAL CB C 35.037 0.100 1 938 . 96 VAL HB H 1.980 0.010 1 939 . 96 VAL CG1 C 20.710 0.100 1 940 . 96 VAL HG1 H 0.900 0.010 1 941 . 96 VAL CG2 C 22.120 0.100 1 942 . 96 VAL HG2 H 0.870 0.010 1 943 . 97 GLY H H 8.567 0.010 1 944 . 97 GLY N N 112.300 0.100 1 945 . 97 GLY C C 173.523 0.100 1 946 . 97 GLY CA C 44.407 0.100 1 947 . 97 GLY HA2 H 4.416 0.010 1 948 . 97 GLY HA3 H 3.690 0.010 1 949 . 98 ALA H H 8.581 0.010 1 950 . 98 ALA N N 121.879 0.100 1 951 . 98 ALA C C 176.574 0.100 1 952 . 98 ALA CA C 51.294 0.100 1 953 . 98 ALA HA H 4.327 0.010 1 954 . 98 ALA CB C 19.205 0.100 1 955 . 98 ALA HB H 1.286 0.010 1 956 . 99 ASP H H 7.938 0.010 1 957 . 99 ASP N N 123.368 0.100 1 958 . 99 ASP C C 176.341 0.100 1 959 . 99 ASP CA C 51.220 0.100 1 960 . 99 ASP HA H 4.693 0.010 1 961 . 99 ASP CB C 40.697 0.100 1 962 . 99 ASP HB2 H 2.640 0.010 1 963 . 99 ASP HB3 H 2.469 0.010 1 964 . 100 LYS H H 8.231 0.010 1 965 . 100 LYS N N 123.811 0.100 1 966 . 100 LYS C C 176.874 0.100 1 967 . 100 LYS CA C 60.129 0.100 1 968 . 100 LYS HA H 3.711 0.010 1 969 . 100 LYS CB C 33.064 0.100 1 970 . 100 LYS HB2 H 1.672 0.010 1 971 . 101 ASP H H 8.113 0.010 1 972 . 101 ASP N N 116.163 0.100 1 973 . 101 ASP C C 178.768 0.100 1 974 . 101 ASP CA C 56.260 0.100 1 975 . 101 ASP HA H 4.635 0.010 1 976 . 101 ASP CB C 42.140 0.100 1 977 . 101 ASP HB2 H 2.620 0.010 1 978 . 101 ASP HB3 H 2.540 0.010 1 979 . 102 GLY H H 8.157 0.010 1 980 . 102 GLY N N 109.660 0.100 1 981 . 102 GLY C C 176.336 0.100 1 982 . 102 GLY CA C 47.240 0.100 1 983 . 102 GLY HA2 H 3.933 0.010 1 984 . 102 GLY HA3 H 3.850 0.010 1 985 . 103 LEU H H 7.820 0.010 1 986 . 103 LEU N N 120.997 0.100 1 987 . 103 LEU C C 175.360 0.100 1 988 . 103 LEU CA C 60.607 0.100 1 989 . 103 LEU HA H 4.180 0.010 1 990 . 103 LEU CB C 39.910 0.100 1 991 . 103 LEU HB2 H 1.480 0.010 1 992 . 103 LEU HB3 H 1.440 0.010 1 993 . 103 LEU CG C 27.591 0.100 1 994 . 103 LEU HG H 1.194 0.010 1 995 . 103 LEU CD1 C 23.372 0.100 1 996 . 103 LEU HD1 H 0.295 0.010 1 997 . 103 LEU CD2 C 25.560 0.100 1 998 . 103 LEU HD2 H 0.245 0.010 1 999 . 104 PRO C C 179.765 0.100 1 1000 . 104 PRO CA C 67.150 0.100 1 1001 . 104 PRO HA H 4.070 0.010 1 1002 . 104 PRO CB C 31.550 0.100 1 1003 . 104 PRO HB2 H 1.911 0.010 1 1004 . 104 PRO HB3 H 2.340 0.010 1 1005 . 104 PRO CG C 29.154 0.100 1 1006 . 104 PRO HG2 H 2.258 0.010 1 1007 . 104 PRO HG3 H 1.795 0.010 1 1008 . 104 PRO CD C 51.186 0.100 1 1009 . 104 PRO HD2 H 3.478 0.010 1 1010 . 104 PRO HD3 H 3.417 0.010 1 1011 . 105 THR H H 6.858 0.010 1 1012 . 105 THR N N 113.066 0.100 1 1013 . 105 THR C C 176.965 0.100 1 1014 . 105 THR CA C 66.220 0.100 1 1015 . 105 THR HA H 3.870 0.010 1 1016 . 105 THR CB C 69.061 0.100 1 1017 . 105 THR HB H 4.156 0.010 1 1018 . 105 THR CG2 C 22.591 0.100 1 1019 . 105 THR HG2 H 1.145 0.010 1 1020 . 106 LEU H H 7.930 0.010 1 1021 . 106 LEU N N 123.980 0.100 1 1022 . 106 LEU C C 179.181 0.100 1 1023 . 106 LEU CA C 58.230 0.100 1 1024 . 106 LEU HA H 3.773 0.010 1 1025 . 106 LEU CB C 43.410 0.100 1 1026 . 106 LEU HB2 H 1.664 0.010 1 1027 . 106 LEU HB3 H 0.844 0.010 1 1028 . 106 LEU CG C 27.747 0.100 1 1029 . 106 LEU HG H 1.395 0.010 1 1030 . 106 LEU CD1 C 25.404 0.100 1 1031 . 106 LEU HD1 H 0.562 0.010 1 1032 . 106 LEU CD2 C 24.154 0.100 1 1033 . 106 LEU HD2 H 0.491 0.010 1 1034 . 107 VAL H H 7.950 0.010 1 1035 . 107 VAL N N 117.308 0.100 1 1036 . 107 VAL C C 176.950 0.100 1 1037 . 107 VAL CA C 68.108 0.100 1 1038 . 107 VAL HA H 3.344 0.010 1 1039 . 107 VAL CB C 31.720 0.100 1 1040 . 107 VAL HB H 1.738 0.010 1 1041 . 107 VAL CG1 C 24.466 0.100 1 1042 . 107 VAL HG1 H 1.047 0.010 1 1043 . 107 VAL CG2 C 21.966 0.100 1 1044 . 107 VAL HG2 H 0.061 0.010 1 1045 . 108 ALA H H 7.440 0.010 1 1046 . 108 ALA N N 118.007 0.100 1 1047 . 108 ALA C C 180.326 0.100 1 1048 . 108 ALA CA C 55.601 0.100 1 1049 . 108 ALA HA H 3.860 0.010 1 1050 . 108 ALA CB C 18.661 0.100 1 1051 . 108 ALA HB H 1.486 0.010 1 1052 . 109 LYS H H 7.674 0.010 1 1053 . 109 LYS N N 116.867 0.100 1 1054 . 109 LYS C C 178.474 0.100 1 1055 . 109 LYS CA C 59.420 0.100 1 1056 . 109 LYS HA H 3.825 0.010 1 1057 . 109 LYS CB C 33.120 0.100 1 1058 . 109 LYS HB2 H 1.636 0.010 1 1059 . 109 LYS HB3 H 1.426 0.010 1 1060 . 109 LYS CG C 24.659 0.100 1 1061 . 109 LYS HG2 H 0.964 0.010 1 1062 . 109 LYS HG3 H 0.543 0.010 1 1063 . 109 LYS CD C 30.470 0.100 1 1064 . 109 LYS HD2 H 1.313 0.010 1 1065 . 109 LYS HD3 H 1.148 0.010 1 1066 . 109 LYS CE C 42.520 0.100 1 1067 . 109 LYS HE2 H 2.606 0.010 1 1068 . 110 HIS H H 7.202 0.010 1 1069 . 110 HIS N N 113.560 0.100 1 1070 . 110 HIS C C 176.456 0.100 1 1071 . 110 HIS CA C 57.590 0.100 1 1072 . 110 HIS HA H 4.677 0.010 1 1073 . 110 HIS CB C 33.750 0.100 1 1074 . 110 HIS HB2 H 3.033 0.010 1 1075 . 110 HIS HB3 H 2.707 0.010 1 1076 . 111 ALA H H 8.109 0.010 1 1077 . 111 ALA N N 123.370 0.100 1 1078 . 111 ALA C C 178.094 0.100 1 1079 . 111 ALA CA C 54.430 0.100 1 1080 . 111 ALA HA H 4.092 0.010 1 1081 . 111 ALA CB C 19.867 0.100 1 1082 . 111 ALA HB H 1.241 0.010 1 1083 . 112 THR H H 7.462 0.010 1 1084 . 112 THR N N 110.980 0.100 1 1085 . 112 THR C C 173.994 0.100 1 1086 . 112 THR CA C 61.830 0.100 1 1087 . 112 THR HA H 4.370 0.010 1 1088 . 112 THR CB C 70.890 0.100 1 1089 . 112 THR HB H 4.268 0.010 1 1090 . 112 THR CG2 C 22.435 0.100 1 1091 . 112 THR HG2 H 1.206 0.010 1 1092 . 113 ALA H H 7.931 0.010 1 1093 . 113 ALA N N 131.750 0.100 1 1094 . 113 ALA C C 183.000 0.100 1 1095 . 113 ALA CA C 56.610 0.100 1 1096 . 113 ALA HA H 4.124 0.010 1 1097 . 113 ALA CB C 20.795 0.100 1 1098 . 113 ALA HB H 1.270 0.010 1 stop_ save_