data_5921 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignment of TM1442, a putative anti-sigma-factor antagonist from Thrmotoga maritima ; _BMRB_accession_number 5921 _BMRB_flat_file_name bmr5921.str _Entry_type original _Submission_date 2003-08-26 _Accession_date 2003-08-28 _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 Etezady-Esfarjani Touraj . . 2 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 603 "13C chemical shifts" 487 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-08 update BMRB 'Addition of Relationship Loop' 2004-03-18 update BMRB 'Updated Citation' 2004-02-11 original author 'Original Release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6232 'the same protein but phosphorylated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the ditor: NMR assignment of TM1442, a putative anti-sigma factor antagonist from Thermotoga maritima ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15017147 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Etezady-Esfarjani Touraj . . 2 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 99 _Page_last 100 _Year 2004 _Details . loop_ _Keyword 'NMR assignment' sigma-factor 'structural proteomics' 'thermotoga maritima' stop_ save_ ################################## # Molecular system description # ################################## save_system_TM1442 _Saveframe_category molecular_system _Mol_system_name TM1442 _Abbreviation_common TM1442 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Tm1442 monomer' $TM1442 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'putative anti-sigma-factor antagonist' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TM1442 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'anti-sigma-factor antagonist' _Abbreviation_common TM1442 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; MNNLKLDIVEQDDKAIVRVQ GDIDAYNSSELKEQLRNFIS TTSKKKIVLDLSSVSYMDSA GLGTLVVILKDAKINGKEFI LSSLKESISRILKLTHLDKI FKITDTVEEA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 ASN 4 LEU 5 LYS 6 LEU 7 ASP 8 ILE 9 VAL 10 GLU 11 GLN 12 ASP 13 ASP 14 LYS 15 ALA 16 ILE 17 VAL 18 ARG 19 VAL 20 GLN 21 GLY 22 ASP 23 ILE 24 ASP 25 ALA 26 TYR 27 ASN 28 SER 29 SER 30 GLU 31 LEU 32 LYS 33 GLU 34 GLN 35 LEU 36 ARG 37 ASN 38 PHE 39 ILE 40 SER 41 THR 42 THR 43 SER 44 LYS 45 LYS 46 LYS 47 ILE 48 VAL 49 LEU 50 ASP 51 LEU 52 SER 53 SER 54 VAL 55 SER 56 TYR 57 MET 58 ASP 59 SER 60 ALA 61 GLY 62 LEU 63 GLY 64 THR 65 LEU 66 VAL 67 VAL 68 ILE 69 LEU 70 LYS 71 ASP 72 ALA 73 LYS 74 ILE 75 ASN 76 GLY 77 LYS 78 GLU 79 PHE 80 ILE 81 LEU 82 SER 83 SER 84 LEU 85 LYS 86 GLU 87 SER 88 ILE 89 SER 90 ARG 91 ILE 92 LEU 93 LYS 94 LEU 95 THR 96 HIS 97 LEU 98 ASP 99 LYS 100 ILE 101 PHE 102 LYS 103 ILE 104 THR 105 ASP 106 THR 107 VAL 108 GLU 109 GLU 110 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 6232 TM1442 100.00 110 99.09 99.09 7.76e-68 PDB 1SBO "Solution Structure Of Putative Anti Sigma Factor Antagonist From Thermotoga Maritima (Tm1442)" 100.00 110 100.00 100.00 1.43e-68 PDB 1T6R "Solution Structure Of Tm1442, A Putative Anti Sigma Factor Antagonist In Phosphorylated State" 100.00 110 99.09 99.09 7.76e-68 PDB 1VC1 "Crystal Structure Of The Tm1442 Protein From Thermotoga Maritima, A Homolog Of The Bacillus Subtilis General Stress Response An" 100.00 110 100.00 100.00 1.43e-68 GB AAD36511 "anti-sigma factor antagonist, putative [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 GB ACB09678 "anti-sigma-factor antagonist [Thermotoga sp. RQ2]" 100.00 110 100.00 100.00 1.43e-68 GB ADA67453 "anti-sigma-factor antagonist [Thermotoga naphthophila RKU-10]" 100.00 110 100.00 100.00 1.43e-68 GB AGL50372 "anti-sigma F factor antagonist (spoIIAA-2); anti sigma b factor antagonist RsbV [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 GB AHD18665 "anti-sigma factor antagonist [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 REF NP_229241 "anti-sigma factor antagonist [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 REF WP_004081714 "MULTISPECIES: anti-sigma factor antagonist [Thermotoga]" 100.00 110 100.00 100.00 1.43e-68 REF YP_001739361 "anti-sigma-factor antagonist [Thermotoga sp. RQ2]" 100.00 110 100.00 100.00 1.43e-68 REF YP_003346867 "anti-sigma-factor antagonist [Thermotoga naphthophila RKU-10]" 100.00 110 100.00 100.00 1.43e-68 REF YP_007977797 "anti-sigma F factor antagonist (spoIIAA-2); anti sigma b factor antagonist RsbV [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 SP Q9X1F5 "RecName: Full=Putative anti-sigma factor antagonist TM_1442 [Thermotoga maritima MSB8]" 100.00 110 100.00 100.00 1.43e-68 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TM1442 'Thermotoga maritima' 2336 Eubacteria . Thermotoga maritima 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 $TM1442 '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 $TM1442 4 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1442 2 mM '[U-98% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1442 2 mM '[U-99% 13C; U-98% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _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 4.8 0.1 n/a temperature 313 0.1 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 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Tm1442 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HE H 2.100 0.02 1 2 . 1 MET CE C 16.800 0.05 1 3 . 2 ASN ND2 N 112.310 0.03 1 4 . 2 ASN HD21 H 6.921 0.02 1 5 . 2 ASN HD22 H 7.649 0.02 1 6 . 3 ASN N N 120.034 0.03 1 7 . 3 ASN H H 8.620 0.02 1 8 . 3 ASN CA C 53.285 0.05 1 9 . 3 ASN HA H 4.785 0.02 1 10 . 3 ASN CB C 38.904 0.05 1 11 . 3 ASN HB2 H 2.941 0.02 1 12 . 3 ASN HB3 H 3.010 0.02 1 13 . 3 ASN ND2 N 112.493 0.03 1 14 . 3 ASN HD21 H 7.007 0.02 1 15 . 3 ASN HD22 H 7.732 0.02 1 16 . 3 ASN C C 174.034 0.05 1 17 . 4 LEU N N 121.647 0.03 1 18 . 4 LEU H H 8.031 0.02 1 19 . 4 LEU CA C 54.905 0.05 1 20 . 4 LEU HA H 4.774 0.02 1 21 . 4 LEU CB C 43.506 0.05 1 22 . 4 LEU HB2 H 1.660 0.02 1 23 . 4 LEU HB3 H 1.572 0.02 1 24 . 4 LEU CG C 26.989 0.05 1 25 . 4 LEU HG H 1.462 0.02 1 26 . 4 LEU HD1 H 0.834 0.02 1 27 . 4 LEU HD2 H 0.825 0.02 1 28 . 4 LEU CD1 C 24.403 0.05 1 29 . 4 LEU CD2 C 25.709 0.05 1 30 . 4 LEU C C 175.792 0.05 1 31 . 5 LYS N N 126.500 0.03 1 32 . 5 LYS H H 8.552 0.02 1 33 . 5 LYS CA C 55.356 0.05 1 34 . 5 LYS HA H 4.613 0.02 1 35 . 5 LYS CB C 35.076 0.05 1 36 . 5 LYS HB2 H 1.832 0.02 1 37 . 5 LYS HB3 H 1.729 0.02 1 38 . 5 LYS CG C 24.605 0.05 1 39 . 5 LYS HG2 H 1.413 0.02 1 40 . 5 LYS HD2 H 1.798 0.02 1 41 . 5 LYS CD C 28.822 0.05 1 42 . 5 LYS CE C 42.035 0.05 1 43 . 5 LYS HE2 H 3.024 0.02 1 44 . 5 LYS C C 174.208 0.05 1 45 . 6 LEU N N 123.766 0.03 1 46 . 6 LEU H H 8.524 0.02 1 47 . 6 LEU CA C 53.417 0.05 1 48 . 6 LEU HA H 5.114 0.02 1 49 . 6 LEU CB C 43.981 0.05 1 50 . 6 LEU HB2 H 1.672 0.02 1 51 . 6 LEU HB3 H 1.145 0.02 1 52 . 6 LEU CG C 27.049 0.05 1 53 . 6 LEU HG H 1.557 0.02 1 54 . 6 LEU HD1 H 0.744 0.02 1 55 . 6 LEU HD2 H 0.681 0.02 1 56 . 6 LEU CD1 C 25.038 0.05 1 57 . 6 LEU CD2 C 25.631 0.05 1 58 . 6 LEU C C 175.601 0.05 1 59 . 7 ASP N N 122.814 0.03 1 60 . 7 ASP H H 8.334 0.02 1 61 . 7 ASP CA C 53.314 0.05 1 62 . 7 ASP HA H 4.984 0.02 1 63 . 7 ASP CB C 43.612 0.05 1 64 . 7 ASP HB2 H 2.695 0.02 1 65 . 7 ASP HB3 H 2.551 0.02 1 66 . 7 ASP C C 174.358 0.05 1 67 . 8 ILE N N 124.551 0.03 1 68 . 8 ILE H H 8.472 0.02 1 69 . 8 ILE CA C 60.711 0.05 1 70 . 8 ILE HA H 4.934 0.02 1 71 . 8 ILE CB C 39.770 0.05 1 72 . 8 ILE HB H 1.553 0.02 1 73 . 8 ILE HG2 H 0.455 0.02 1 74 . 8 ILE CG2 C 17.201 0.05 1 75 . 8 ILE CG1 C 27.952 0.05 1 76 . 8 ILE HG12 H 1.325 0.02 1 77 . 8 ILE HG13 H 0.606 0.02 1 78 . 8 ILE HD1 H 0.318 0.02 1 79 . 8 ILE CD1 C 12.304 0.05 1 80 . 8 ILE C C 175.543 0.05 1 81 . 9 VAL N N 127.816 0.03 1 82 . 9 VAL H H 9.163 0.02 1 83 . 9 VAL CA C 60.506 0.05 1 84 . 9 VAL HA H 4.480 0.02 1 85 . 9 VAL CB C 35.124 0.05 1 86 . 9 VAL HB H 2.070 0.02 1 87 . 9 VAL HG1 H 0.946 0.02 1 88 . 9 VAL HG2 H 0.946 0.02 1 89 . 9 VAL CG1 C 20.553 0.05 1 90 . 9 VAL CG2 C 20.375 0.05 1 91 . 9 VAL C C 174.530 0.05 1 92 . 10 GLU N N 124.353 0.03 1 93 . 10 GLU H H 8.787 0.02 1 94 . 10 GLU CA C 55.748 0.05 1 95 . 10 GLU HA H 4.979 0.02 1 96 . 10 GLU CB C 31.431 0.05 1 97 . 10 GLU HB2 H 2.136 0.02 1 98 . 10 GLU HB3 H 1.947 0.02 1 99 . 10 GLU CG C 36.939 0.05 1 100 . 10 GLU HG2 H 2.495 0.02 1 101 . 10 GLU HG3 H 2.161 0.02 1 102 . 10 GLU C C 175.868 0.05 1 103 . 11 GLN N N 122.966 0.03 1 104 . 11 GLN H H 8.728 0.02 1 105 . 11 GLN CA C 54.456 0.05 1 106 . 11 GLN HA H 4.673 0.02 1 107 . 11 GLN CB C 31.055 0.05 1 108 . 11 GLN HB2 H 2.212 0.02 1 109 . 11 GLN HB3 H 1.992 0.02 1 110 . 11 GLN CG C 33.671 0.05 1 111 . 11 GLN HG2 H 2.293 0.02 1 112 . 11 GLN NE2 N 110.573 0.03 1 113 . 11 GLN HE21 H 6.818 0.02 1 114 . 11 GLN HE22 H 7.494 0.02 1 115 . 11 GLN C C 174.722 0.05 1 116 . 12 ASP N N 121.888 0.03 1 117 . 12 ASP H H 8.820 0.02 1 118 . 12 ASP CA C 57.381 0.05 1 119 . 12 ASP HA H 4.278 0.02 1 120 . 12 ASP CB C 39.715 0.05 1 121 . 12 ASP HB2 H 2.859 0.02 1 122 . 12 ASP C C 176.108 0.05 1 123 . 13 ASP N N 117.939 0.03 1 124 . 13 ASP H H 8.815 0.02 1 125 . 13 ASP CA C 53.600 0.05 1 126 . 13 ASP HA H 4.850 0.02 1 127 . 13 ASP CB C 40.737 0.05 1 128 . 13 ASP HB2 H 2.943 0.02 1 129 . 13 ASP HB3 H 2.765 0.02 1 130 . 13 ASP C C 175.614 0.05 1 131 . 14 LYS N N 116.448 0.03 1 132 . 14 LYS H H 7.951 0.02 1 133 . 14 LYS CA C 54.712 0.05 1 134 . 14 LYS HA H 5.197 0.02 1 135 . 14 LYS CB C 35.249 0.05 1 136 . 14 LYS HB2 H 1.735 0.02 1 137 . 14 LYS HB3 H 1.687 0.02 1 138 . 14 LYS CG C 23.086 0.05 1 139 . 14 LYS HG2 H 1.455 0.02 1 140 . 14 LYS HG3 H 1.267 0.02 1 141 . 14 LYS CD C 28.450 0.05 1 142 . 14 LYS HD2 H 1.547 0.02 1 143 . 14 LYS CE C 41.573 0.05 1 144 . 14 LYS HE2 H 2.922 0.02 1 145 . 14 LYS C C 175.841 0.05 1 146 . 15 ALA N N 123.050 0.03 1 147 . 15 ALA H H 8.780 0.02 1 148 . 15 ALA CA C 50.292 0.05 1 149 . 15 ALA HA H 5.166 0.02 1 150 . 15 ALA HB H 1.575 0.02 1 151 . 15 ALA CB C 21.270 0.05 1 152 . 15 ALA C C 175.002 0.05 1 153 . 16 ILE N N 123.451 0.03 1 154 . 16 ILE H H 9.341 0.02 1 155 . 16 ILE CA C 60.159 0.05 1 156 . 16 ILE HA H 4.761 0.02 1 157 . 16 ILE CB C 39.421 0.05 1 158 . 16 ILE HB H 1.886 0.02 1 159 . 16 ILE HG2 H 0.855 0.02 1 160 . 16 ILE CG2 C 18.471 0.05 1 161 . 16 ILE CG1 C 27.817 0.05 1 162 . 16 ILE HG12 H 1.425 0.02 1 163 . 16 ILE HD1 H 0.779 0.02 1 164 . 16 ILE CD1 C 14.313 0.05 1 165 . 16 ILE C C 174.459 0.05 1 166 . 17 VAL N N 127.934 0.03 1 167 . 17 VAL H H 9.492 0.02 1 168 . 17 VAL CA C 60.353 0.05 1 169 . 17 VAL HA H 4.465 0.02 1 170 . 17 VAL CB C 32.131 0.05 1 171 . 17 VAL HB H 2.147 0.02 1 172 . 17 VAL HG1 H 0.672 0.02 1 173 . 17 VAL HG2 H 0.615 0.02 1 174 . 17 VAL CG1 C 21.597 0.05 1 175 . 17 VAL CG2 C 19.536 0.05 1 176 . 17 VAL C C 174.923 0.05 1 177 . 18 ARG N N 127.724 0.03 1 178 . 18 ARG H H 9.328 0.02 1 179 . 18 ARG CA C 55.798 0.05 1 180 . 18 ARG HA H 4.897 0.02 1 181 . 18 ARG CB C 30.499 0.05 1 182 . 18 ARG HB2 H 1.937 0.02 1 183 . 18 ARG CG C 27.991 0.05 1 184 . 18 ARG HG2 H 1.627 0.02 1 185 . 18 ARG HG3 H 1.613 0.02 1 186 . 18 ARG CD C 43.455 0.05 1 187 . 18 ARG HD2 H 3.205 0.02 1 188 . 18 ARG NE N 85.213 0.03 1 189 . 18 ARG HE H 7.426 0.02 1 190 . 18 ARG C C 175.654 0.05 1 191 . 19 VAL N N 123.451 0.03 1 192 . 19 VAL H H 7.263 0.02 1 193 . 19 VAL CA C 61.415 0.05 1 194 . 19 VAL HA H 4.409 0.02 1 195 . 19 VAL CB C 32.984 0.05 1 196 . 19 VAL HB H 1.889 0.02 1 197 . 19 VAL HG1 H 0.790 0.02 1 198 . 19 VAL HG2 H 0.789 0.02 1 199 . 19 VAL CG1 C 21.675 0.05 1 200 . 19 VAL CG2 C 21.791 0.05 1 201 . 19 VAL C C 174.746 0.05 1 202 . 20 GLN N N 126.643 0.03 1 203 . 20 GLN H H 8.752 0.02 1 204 . 20 GLN CA C 55.014 0.05 1 205 . 20 GLN HA H 4.620 0.02 1 206 . 20 GLN CB C 30.324 0.05 1 207 . 20 GLN HB2 H 2.150 0.02 1 208 . 20 GLN HB3 H 2.036 0.02 1 209 . 20 GLN CG C 33.514 0.05 1 210 . 20 GLN HG2 H 2.267 0.02 1 211 . 20 GLN HG3 H 2.035 0.02 1 212 . 20 GLN NE2 N 111.132 0.03 1 213 . 20 GLN HE21 H 7.460 0.02 1 214 . 20 GLN HE22 H 6.933 0.02 1 215 . 20 GLN C C 174.311 0.05 1 216 . 21 GLY N N 111.744 0.03 1 217 . 21 GLY H H 7.753 0.02 1 218 . 21 GLY CA C 43.947 0.05 1 219 . 21 GLY HA2 H 4.518 0.02 1 220 . 21 GLY HA3 H 3.753 0.02 1 221 . 21 GLY C C 171.410 0.05 1 222 . 22 ASP N N 117.259 0.03 1 223 . 22 ASP H H 7.920 0.02 1 224 . 22 ASP CA C 53.946 0.05 1 225 . 22 ASP HA H 5.117 0.02 1 226 . 22 ASP CB C 42.019 0.05 1 227 . 22 ASP HB2 H 2.627 0.02 1 228 . 22 ASP HB3 H 2.701 0.02 1 229 . 22 ASP C C 175.853 0.05 1 230 . 23 ILE N N 120.335 0.03 1 231 . 23 ILE H H 7.811 0.02 1 232 . 23 ILE CA C 60.413 0.05 1 233 . 23 ILE HA H 4.484 0.02 1 234 . 23 ILE CB C 37.319 0.05 1 235 . 23 ILE HB H 1.834 0.02 1 236 . 23 ILE HG2 H 0.826 0.02 1 237 . 23 ILE CG2 C 18.002 0.05 1 238 . 23 ILE CG1 C 26.664 0.05 1 239 . 23 ILE HG12 H 1.724 0.02 1 240 . 23 ILE HD1 H 0.833 0.02 1 241 . 23 ILE CD1 C 13.338 0.05 1 242 . 23 ILE C C 173.877 0.05 1 243 . 24 ASP N N 124.736 0.03 1 244 . 24 ASP H H 8.476 0.02 1 245 . 24 ASP CA C 51.500 0.05 1 246 . 24 ASP HA H 5.462 0.02 1 247 . 24 ASP CB C 43.526 0.05 1 248 . 24 ASP HB2 H 3.303 0.02 1 249 . 24 ASP HB3 H 2.575 0.02 1 250 . 24 ASP C C 178.358 0.05 1 251 . 25 ALA N N 122.760 0.03 1 252 . 25 ALA H H 9.651 0.02 1 253 . 25 ALA CA C 54.946 0.05 1 254 . 25 ALA HA H 3.890 0.02 1 255 . 25 ALA HB H 1.277 0.02 1 256 . 25 ALA CB C 18.335 0.05 1 257 . 25 ALA C C 179.444 0.05 1 258 . 26 TYR N N 116.131 0.03 1 259 . 26 TYR H H 7.983 0.02 1 260 . 26 TYR CA C 59.952 0.05 1 261 . 26 TYR HA H 4.433 0.02 1 262 . 26 TYR CB C 37.822 0.05 1 263 . 26 TYR HB2 H 3.241 0.02 1 264 . 26 TYR HB3 H 3.188 0.02 1 265 . 26 TYR HD1 H 7.272 0.02 1 266 . 26 TYR HE1 H 6.939 0.02 1 267 . 26 TYR CD1 C 132.744 0.05 1 268 . 26 TYR CE1 C 118.087 0.05 1 269 . 26 TYR C C 177.509 0.05 1 270 . 27 ASN N N 115.727 0.03 1 271 . 27 ASN H H 8.276 0.02 1 272 . 27 ASN CA C 53.179 0.05 1 273 . 27 ASN HA H 5.093 0.02 1 274 . 27 ASN CB C 39.725 0.05 1 275 . 27 ASN HB2 H 3.207 0.02 1 276 . 27 ASN HB3 H 2.949 0.02 1 277 . 27 ASN ND2 N 111.450 0.03 1 278 . 27 ASN HD21 H 7.469 0.02 1 279 . 27 ASN HD22 H 7.917 0.02 1 280 . 27 ASN C C 177.786 0.05 1 281 . 28 SER N N 116.905 0.03 1 282 . 28 SER H H 8.257 0.02 1 283 . 28 SER CA C 63.876 0.05 1 284 . 28 SER HA H 4.253 0.02 1 285 . 28 SER CB C 62.595 0.05 1 286 . 28 SER HB2 H 3.960 0.02 1 287 . 28 SER C C 176.246 0.05 1 288 . 29 SER N N 117.884 0.03 1 289 . 29 SER H H 8.482 0.02 1 290 . 29 SER CA C 62.022 0.05 1 291 . 29 SER HA H 4.012 0.02 1 292 . 29 SER CB C 63.297 0.05 1 293 . 29 SER HB2 H 4.250 0.02 1 294 . 29 SER C C 176.582 0.05 1 295 . 30 GLU N N 122.902 0.03 1 296 . 30 GLU H H 7.984 0.02 1 297 . 30 GLU CA C 58.957 0.05 1 298 . 30 GLU HA H 4.257 0.02 1 299 . 30 GLU CB C 28.963 0.05 1 300 . 30 GLU HB2 H 2.209 0.02 1 301 . 30 GLU HB3 H 2.116 0.02 1 302 . 30 GLU CG C 35.412 0.05 1 303 . 30 GLU HG2 H 2.431 0.02 1 304 . 30 GLU C C 178.477 0.05 1 305 . 31 LEU N N 119.680 0.03 1 306 . 31 LEU H H 7.886 0.02 1 307 . 31 LEU CA C 58.254 0.05 1 308 . 31 LEU HA H 3.955 0.02 1 309 . 31 LEU CB C 41.548 0.05 1 310 . 31 LEU HB2 H 2.047 0.02 1 311 . 31 LEU HB3 H 1.563 0.02 1 312 . 31 LEU CG C 26.742 0.05 1 313 . 31 LEU HG H 1.562 0.02 1 314 . 31 LEU HD1 H 0.933 0.02 1 315 . 31 LEU HD2 H 0.886 0.02 1 316 . 31 LEU CD1 C 24.265 0.05 1 317 . 31 LEU CD2 C 26.215 0.05 1 318 . 31 LEU C C 177.707 0.05 1 319 . 32 LYS N N 117.438 0.03 1 320 . 32 LYS H H 8.322 0.02 1 321 . 32 LYS CA C 60.113 0.05 1 322 . 32 LYS HA H 3.705 0.02 1 323 . 32 LYS CB C 32.034 0.05 1 324 . 32 LYS HB2 H 2.093 0.02 1 325 . 32 LYS HB3 H 2.042 0.02 1 326 . 32 LYS CG C 24.497 0.05 1 327 . 32 LYS HG2 H 1.474 0.02 1 328 . 32 LYS HG3 H 1.414 0.02 1 329 . 32 LYS CD C 29.041 0.05 1 330 . 32 LYS HD2 H 1.811 0.02 1 331 . 32 LYS HD3 H 1.763 0.02 1 332 . 32 LYS CE C 42.098 0.05 1 333 . 32 LYS HE2 H 3.005 0.02 1 334 . 32 LYS HE3 H 2.999 0.02 1 335 . 32 LYS C C 177.766 0.05 1 336 . 33 GLU N N 117.527 0.03 1 337 . 33 GLU H H 8.008 0.02 1 338 . 33 GLU CA C 59.109 0.05 1 339 . 33 GLU HA H 4.114 0.02 1 340 . 33 GLU CB C 29.197 0.05 1 341 . 33 GLU HB2 H 2.214 0.02 1 342 . 33 GLU HB3 H 2.172 0.02 1 343 . 33 GLU CG C 35.385 0.05 1 344 . 33 GLU HG2 H 2.430 0.02 1 345 . 33 GLU C C 179.207 0.05 1 346 . 34 GLN N N 116.775 0.03 1 347 . 34 GLN H H 8.390 0.02 1 348 . 34 GLN CA C 59.125 0.05 1 349 . 34 GLN HA H 4.175 0.02 1 350 . 34 GLN CB C 28.687 0.05 1 351 . 34 GLN HB2 H 2.052 0.02 1 352 . 34 GLN CG C 34.432 0.05 1 353 . 34 GLN HG2 H 2.643 0.02 1 354 . 34 GLN HG3 H 2.486 0.02 1 355 . 34 GLN NE2 N 110.892 0.03 1 356 . 34 GLN HE21 H 6.890 0.02 1 357 . 34 GLN HE22 H 7.527 0.02 1 358 . 34 GLN C C 180.293 0.05 1 359 . 35 LEU N N 118.789 0.03 1 360 . 35 LEU H H 8.594 0.02 1 361 . 35 LEU CA C 57.166 0.05 1 362 . 35 LEU HA H 4.339 0.02 1 363 . 35 LEU CB C 40.574 0.05 1 364 . 35 LEU HB2 H 2.132 0.02 1 365 . 35 LEU HB3 H 1.436 0.02 1 366 . 35 LEU CG C 27.694 0.05 1 367 . 35 LEU HG H 1.943 0.02 1 368 . 35 LEU HD1 H 0.998 0.02 1 369 . 35 LEU HD2 H 0.945 0.02 1 370 . 35 LEU CD1 C 25.512 0.05 1 371 . 35 LEU CD2 C 23.000 0.05 1 372 . 35 LEU C C 178.694 0.05 1 373 . 36 ARG N N 120.698 0.03 1 374 . 36 ARG H H 8.709 0.02 1 375 . 36 ARG CA C 60.484 0.05 1 376 . 36 ARG HA H 3.954 0.02 1 377 . 36 ARG CB C 29.609 0.05 1 378 . 36 ARG HB2 H 1.912 0.02 1 379 . 36 ARG HB3 H 1.984 0.02 1 380 . 36 ARG CG C 27.595 0.05 1 381 . 36 ARG HG2 H 1.804 0.02 1 382 . 36 ARG HG3 H 1.557 0.02 1 383 . 36 ARG CD C 43.473 0.05 1 384 . 36 ARG HD2 H 3.129 0.02 1 385 . 36 ARG NE N 85.216 0.03 1 386 . 36 ARG HE H 7.750 0.02 1 387 . 36 ARG NH2 N 71.809 0.03 1 388 . 36 ARG HH21 H 6.885 0.02 1 389 . 36 ARG C C 179.424 0.05 1 390 . 37 ASN N N 117.558 0.03 1 391 . 37 ASN H H 7.975 0.02 1 392 . 37 ASN CA C 56.147 0.05 1 393 . 37 ASN HA H 4.473 0.02 1 394 . 37 ASN CB C 38.121 0.05 1 395 . 37 ASN HB2 H 2.973 0.02 1 396 . 37 ASN HB3 H 2.911 0.02 1 397 . 37 ASN ND2 N 113.198 0.03 1 398 . 37 ASN HD21 H 7.647 0.02 1 399 . 37 ASN HD22 H 6.986 0.02 1 400 . 37 ASN C C 177.509 0.05 1 401 . 38 PHE N N 121.195 0.03 1 402 . 38 PHE H H 8.130 0.02 1 403 . 38 PHE CA C 61.515 0.05 1 404 . 38 PHE HA H 4.342 0.02 1 405 . 38 PHE CB C 39.337 0.05 1 406 . 38 PHE HB2 H 3.433 0.02 1 407 . 38 PHE HB3 H 3.048 0.02 1 408 . 38 PHE HD1 H 7.168 0.02 1 409 . 38 PHE HE1 H 7.225 0.02 1 410 . 38 PHE CD1 C 130.545 0.05 1 411 . 38 PHE CE1 C 130.901 0.05 1 412 . 38 PHE C C 177.470 0.05 1 413 . 39 ILE N N 119.388 0.03 1 414 . 39 ILE H H 8.930 0.02 1 415 . 39 ILE CA C 65.664 0.05 1 416 . 39 ILE HA H 3.297 0.02 1 417 . 39 ILE CB C 37.648 0.05 1 418 . 39 ILE HB H 1.995 0.02 1 419 . 39 ILE HG2 H 0.820 0.02 1 420 . 39 ILE CG2 C 17.613 0.05 1 421 . 39 ILE CG1 C 31.334 0.05 1 422 . 39 ILE HG12 H 0.976 0.02 1 423 . 39 ILE HD1 H 0.819 0.02 1 424 . 39 ILE CD1 C 14.089 0.05 1 425 . 39 ILE C C 175.989 0.05 1 426 . 40 SER N N 110.330 0.03 1 427 . 40 SER H H 7.473 0.02 1 428 . 40 SER CA C 60.349 0.05 1 429 . 40 SER HA H 4.272 0.02 1 430 . 40 SER CB C 63.788 0.05 1 431 . 40 SER HB2 H 4.092 0.02 1 432 . 40 SER HB3 H 4.024 0.02 1 433 . 40 SER C C 174.686 0.05 1 434 . 41 THR N N 110.749 0.03 1 435 . 41 THR H H 7.476 0.02 1 436 . 41 THR CA C 62.578 0.05 1 437 . 41 THR HA H 4.455 0.02 1 438 . 41 THR CB C 70.709 0.05 1 439 . 41 THR HB H 4.205 0.02 1 440 . 41 THR HG2 H 1.257 0.02 1 441 . 41 THR CG2 C 21.276 0.05 1 442 . 41 THR C C 175.239 0.05 1 443 . 42 THR N N 117.634 0.03 1 444 . 42 THR H H 7.635 0.02 1 445 . 42 THR CA C 61.849 0.05 1 446 . 42 THR HA H 4.287 0.02 1 447 . 42 THR CB C 67.668 0.05 1 448 . 42 THR HB H 3.217 0.02 1 449 . 42 THR HG2 H 0.848 0.02 1 450 . 42 THR CG2 C 19.156 0.05 1 451 . 42 THR C C 173.838 0.05 1 452 . 43 SER N N 122.258 0.03 1 453 . 43 SER H H 8.773 0.02 1 454 . 43 SER CA C 58.447 0.05 1 455 . 43 SER HA H 4.552 0.02 1 456 . 43 SER CB C 63.677 0.05 1 457 . 43 SER HB2 H 4.055 0.02 1 458 . 43 SER HB3 H 3.984 0.02 1 459 . 43 SER C C 175.752 0.05 1 460 . 44 LYS N N 122.221 0.03 1 461 . 44 LYS H H 8.304 0.02 1 462 . 44 LYS CA C 54.438 0.05 1 463 . 44 LYS HA H 4.307 0.02 1 464 . 44 LYS CB C 31.565 0.05 1 465 . 44 LYS HB2 H 1.881 0.02 1 466 . 44 LYS HB3 H 1.737 0.02 1 467 . 44 LYS CG C 24.034 0.05 1 468 . 44 LYS HG2 H 1.357 0.02 1 469 . 44 LYS HD2 H 1.517 0.02 1 470 . 44 LYS HE2 H 2.891 0.02 1 471 . 44 LYS CE C 42.728 0.05 1 472 . 44 LYS C C 176.779 0.05 1 473 . 45 LYS N N 120.094 0.03 1 474 . 45 LYS H H 8.482 0.02 1 475 . 45 LYS CA C 57.165 0.05 1 476 . 45 LYS HA H 4.350 0.02 1 477 . 45 LYS CB C 33.509 0.05 1 478 . 45 LYS HB2 H 2.117 0.02 1 479 . 45 LYS HB3 H 1.977 0.02 1 480 . 45 LYS CG C 25.110 0.05 1 481 . 45 LYS HG2 H 1.668 0.02 1 482 . 45 LYS HG3 H 1.630 0.02 1 483 . 45 LYS CD C 29.005 0.05 1 484 . 45 LYS HD2 H 1.824 0.02 1 485 . 45 LYS CE C 42.089 0.05 1 486 . 45 LYS HE2 H 3.114 0.02 1 487 . 45 LYS C C 175.279 0.05 1 488 . 46 LYS N N 117.363 0.03 1 489 . 46 LYS H H 7.397 0.02 1 490 . 46 LYS CA C 55.143 0.05 1 491 . 46 LYS HA H 4.976 0.02 1 492 . 46 LYS CB C 35.037 0.05 1 493 . 46 LYS HB2 H 1.845 0.02 1 494 . 46 LYS HB3 H 1.615 0.02 1 495 . 46 LYS CG C 25.287 0.05 1 496 . 46 LYS HG2 H 1.316 0.02 1 497 . 46 LYS C C 173.778 0.05 1 498 . 47 ILE N N 125.902 0.03 1 499 . 47 ILE H H 9.022 0.02 1 500 . 47 ILE CA C 59.648 0.05 1 501 . 47 ILE HA H 4.852 0.02 1 502 . 47 ILE CB C 39.442 0.05 1 503 . 47 ILE HB H 2.179 0.02 1 504 . 47 ILE HG2 H 0.975 0.02 1 505 . 47 ILE CG2 C 17.558 0.05 1 506 . 47 ILE CG1 C 27.939 0.05 1 507 . 47 ILE HG12 H 1.554 0.02 1 508 . 47 ILE HG13 H 1.427 0.02 1 509 . 47 ILE HD1 H 0.910 0.02 1 510 . 47 ILE CD1 C 14.158 0.05 1 511 . 47 ILE C C 173.226 0.05 1 512 . 48 VAL N N 126.983 0.03 1 513 . 48 VAL H H 9.136 0.02 1 514 . 48 VAL CA C 60.136 0.05 1 515 . 48 VAL HA H 4.645 0.02 1 516 . 48 VAL CB C 33.665 0.05 1 517 . 48 VAL HB H 2.031 0.02 1 518 . 48 VAL HG1 H 0.742 0.02 1 519 . 48 VAL HG2 H 0.742 0.02 1 520 . 48 VAL CG1 C 21.486 0.05 1 521 . 48 VAL CG2 C 21.465 0.05 1 522 . 48 VAL C C 174.055 0.05 1 523 . 49 LEU N N 129.064 0.03 1 524 . 49 LEU H H 9.205 0.02 1 525 . 49 LEU CA C 53.214 0.05 1 526 . 49 LEU HA H 4.970 0.02 1 527 . 49 LEU CB C 42.336 0.05 1 528 . 49 LEU HB2 H 1.769 0.02 1 529 . 49 LEU HB3 H 1.264 0.02 1 530 . 49 LEU CG C 27.608 0.05 1 531 . 49 LEU HG H 1.447 0.02 1 532 . 49 LEU HD1 H 0.860 0.02 1 533 . 49 LEU HD2 H 0.854 0.02 1 534 . 49 LEU CD1 C 25.973 0.05 1 535 . 49 LEU CD2 C 24.373 0.05 1 536 . 49 LEU C C 174.114 0.05 1 537 . 50 ASP N N 125.657 0.03 1 538 . 50 ASP H H 8.861 0.02 1 539 . 50 ASP CA C 52.945 0.05 1 540 . 50 ASP HA H 4.560 0.02 1 541 . 50 ASP CB C 41.183 0.05 1 542 . 50 ASP HB2 H 2.893 0.02 1 543 . 50 ASP HB3 H 2.218 0.02 1 544 . 50 ASP C C 177.430 0.05 1 545 . 51 LEU N N 126.701 0.03 1 546 . 51 LEU H H 8.472 0.02 1 547 . 51 LEU CA C 54.067 0.05 1 548 . 51 LEU HA H 4.673 0.02 1 549 . 51 LEU CB C 40.368 0.05 1 550 . 51 LEU HB2 H 1.951 0.02 1 551 . 51 LEU HB3 H 1.639 0.02 1 552 . 51 LEU CG C 26.455 0.05 1 553 . 51 LEU HG H 1.698 0.02 1 554 . 51 LEU HD1 H 0.804 0.02 1 555 . 51 LEU HD2 H 0.798 0.02 1 556 . 51 LEU CD1 C 26.033 0.05 1 557 . 51 LEU CD2 C 23.693 0.05 1 558 . 51 LEU C C 178.102 0.05 1 559 . 52 SER N N 119.990 0.03 1 560 . 52 SER H H 8.938 0.02 1 561 . 52 SER CA C 62.983 0.05 1 562 . 52 SER HA H 4.433 0.02 1 563 . 52 SER CB C 63.232 0.05 1 564 . 52 SER HB2 H 4.204 0.02 1 565 . 52 SER HB3 H 3.971 0.02 1 566 . 52 SER C C 176.345 0.05 1 567 . 53 SER N N 114.639 0.03 1 568 . 53 SER H H 9.050 0.02 1 569 . 53 SER CA C 57.664 0.05 1 570 . 53 SER HA H 4.836 0.02 1 571 . 53 SER CB C 63.148 0.05 1 572 . 53 SER HB2 H 4.259 0.02 1 573 . 53 SER HB3 H 3.961 0.02 1 574 . 53 SER C C 174.410 0.05 1 575 . 54 VAL N N 123.995 0.03 1 576 . 54 VAL H H 7.799 0.02 1 577 . 54 VAL CA C 62.309 0.05 1 578 . 54 VAL HA H 4.364 0.02 1 579 . 54 VAL CB C 32.115 0.05 1 580 . 54 VAL HB H 2.258 0.02 1 581 . 54 VAL HG1 H 1.068 0.02 1 582 . 54 VAL HG2 H 1.068 0.02 1 583 . 54 VAL CG1 C 21.285 0.05 1 584 . 54 VAL CG2 C 21.298 0.05 1 585 . 54 VAL C C 175.298 0.05 1 586 . 55 SER N N 121.245 0.03 1 587 . 55 SER H H 8.787 0.02 1 588 . 55 SER CA C 58.961 0.05 1 589 . 55 SER HA H 4.633 0.02 1 590 . 55 SER CB C 64.335 0.05 1 591 . 55 SER HB2 H 4.079 0.02 1 592 . 55 SER HB3 H 3.882 0.02 1 593 . 55 SER C C 173.838 0.05 1 594 . 56 TYR N N 122.470 0.03 1 595 . 56 TYR H H 7.836 0.02 1 596 . 56 TYR CA C 57.884 0.05 1 597 . 56 TYR HA H 4.648 0.02 1 598 . 56 TYR CB C 41.364 0.05 1 599 . 56 TYR HB2 H 2.999 0.02 1 600 . 56 TYR HB3 H 2.702 0.02 1 601 . 56 TYR HD1 H 7.078 0.02 1 602 . 56 TYR HE1 H 6.909 0.02 1 603 . 56 TYR CD1 C 132.551 0.05 1 604 . 56 TYR CE1 C 118.087 0.05 1 605 . 56 TYR C C 172.022 0.05 1 606 . 57 MET N N 124.481 0.03 1 607 . 57 MET H H 6.944 0.02 1 608 . 57 MET CA C 54.017 0.05 1 609 . 57 MET HA H 4.983 0.02 1 610 . 57 MET CB C 37.820 0.05 1 611 . 57 MET HB2 H 1.823 0.02 1 612 . 57 MET HB3 H 1.719 0.02 1 613 . 57 MET CG C 31.261 0.05 1 614 . 57 MET HG2 H 2.596 0.02 1 615 . 57 MET HG3 H 2.436 0.02 1 616 . 57 MET HE H 1.828 0.02 1 617 . 57 MET CE C 16.638 0.05 1 618 . 57 MET C C 173.344 0.05 1 619 . 58 ASP N N 121.928 0.03 1 620 . 58 ASP H H 7.509 0.02 1 621 . 58 ASP CA C 51.450 0.05 1 622 . 58 ASP HA H 4.781 0.02 1 623 . 58 ASP CB C 42.618 0.05 1 624 . 58 ASP HB2 H 3.430 0.02 1 625 . 58 ASP HB3 H 2.826 0.02 1 626 . 58 ASP C C 176.700 0.05 1 627 . 59 SER N N 113.049 0.03 1 628 . 59 SER H H 8.486 0.02 1 629 . 59 SER CA C 62.019 0.05 1 630 . 59 SER HA H 4.011 0.02 1 631 . 59 SER CB C 62.034 0.05 1 632 . 59 SER HB2 H 4.252 0.02 1 633 . 59 SER C C 176.601 0.05 1 634 . 60 ALA N N 126.648 0.03 1 635 . 60 ALA H H 7.937 0.02 1 636 . 60 ALA CA C 54.707 0.05 1 637 . 60 ALA HA H 4.236 0.02 1 638 . 60 ALA HB H 1.500 0.02 1 639 . 60 ALA CB C 17.533 0.05 1 640 . 60 ALA C C 181.438 0.05 1 641 . 61 GLY N N 110.784 0.03 1 642 . 61 GLY H H 8.905 0.02 1 643 . 61 GLY CA C 47.479 0.05 1 644 . 61 GLY HA2 H 3.608 0.02 1 645 . 61 GLY HA3 H 3.704 0.02 1 646 . 61 GLY C C 175.002 0.05 1 647 . 62 LEU N N 121.920 0.03 1 648 . 62 LEU H H 8.315 0.02 1 649 . 62 LEU CA C 58.058 0.05 1 650 . 62 LEU HA H 4.074 0.02 1 651 . 62 LEU CB C 41.813 0.05 1 652 . 62 LEU HB2 H 1.739 0.02 1 653 . 62 LEU HB3 H 1.624 0.02 1 654 . 62 LEU CG C 26.557 0.05 1 655 . 62 LEU HG H 1.654 0.02 1 656 . 62 LEU HD1 H 0.951 0.02 1 657 . 62 LEU HD2 H 0.854 0.02 1 658 . 62 LEU CD1 C 23.555 0.05 1 659 . 62 LEU CD2 C 24.851 0.05 1 660 . 62 LEU C C 179.049 0.05 1 661 . 63 GLY N N 104.163 0.03 1 662 . 63 GLY H H 8.236 0.02 1 663 . 63 GLY CA C 46.981 0.05 1 664 . 63 GLY HA2 H 4.104 0.02 1 665 . 63 GLY HA3 H 3.777 0.02 1 666 . 63 GLY C C 176.759 0.05 1 667 . 64 THR N N 119.156 0.03 1 668 . 64 THR H H 7.976 0.02 1 669 . 64 THR CA C 67.516 0.05 1 670 . 64 THR HA H 3.961 0.02 1 671 . 64 THR CB C 67.882 0.05 1 672 . 64 THR HB H 4.575 0.02 1 673 . 64 THR HG2 H 1.245 0.02 1 674 . 64 THR CG2 C 21.607 0.05 1 675 . 64 THR C C 175.496 0.05 1 676 . 65 LEU N N 120.645 0.03 1 677 . 65 LEU H H 7.922 0.02 1 678 . 65 LEU CA C 58.463 0.05 1 679 . 65 LEU HA H 4.065 0.02 1 680 . 65 LEU CB C 41.378 0.05 1 681 . 65 LEU HB2 H 2.293 0.02 1 682 . 65 LEU HB3 H 1.606 0.02 1 683 . 65 LEU CG C 26.281 0.05 1 684 . 65 LEU HG H 2.030 0.02 1 685 . 65 LEU HD1 H 0.737 0.02 1 686 . 65 LEU HD2 H 0.745 0.02 1 687 . 65 LEU CD1 C 25.033 0.05 1 688 . 65 LEU CD2 C 22.427 0.05 1 689 . 65 LEU C C 178.477 0.05 1 690 . 66 VAL N N 117.791 0.03 1 691 . 66 VAL H H 7.831 0.02 1 692 . 66 VAL CA C 66.769 0.05 1 693 . 66 VAL HA H 3.743 0.02 1 694 . 66 VAL CB C 31.542 0.05 1 695 . 66 VAL HB H 2.425 0.02 1 696 . 66 VAL HG1 H 1.259 0.02 1 697 . 66 VAL HG2 H 1.002 0.02 1 698 . 66 VAL CG1 C 23.081 0.05 1 699 . 66 VAL CG2 C 21.705 0.05 1 700 . 66 VAL C C 177.786 0.05 1 701 . 67 VAL N N 119.369 0.03 1 702 . 67 VAL H H 7.668 0.02 1 703 . 67 VAL CA C 66.524 0.05 1 704 . 67 VAL HA H 3.732 0.02 1 705 . 67 VAL CB C 31.375 0.05 1 706 . 67 VAL HB H 2.348 0.02 1 707 . 67 VAL HG1 H 1.158 0.02 1 708 . 67 VAL HG2 H 1.016 0.02 1 709 . 67 VAL CG1 C 22.664 0.05 1 710 . 67 VAL CG2 C 21.430 0.05 1 711 . 67 VAL C C 178.141 0.05 1 712 . 68 ILE N N 120.858 0.03 1 713 . 68 ILE H H 8.184 0.02 1 714 . 68 ILE CA C 63.110 0.05 1 715 . 68 ILE HA H 3.753 0.02 1 716 . 68 ILE CB C 35.943 0.05 1 717 . 68 ILE HB H 1.842 0.02 1 718 . 68 ILE HG2 H 0.407 0.02 1 719 . 68 ILE CG2 C 18.225 0.05 1 720 . 68 ILE CG1 C 27.582 0.05 1 721 . 68 ILE HG12 H 1.563 0.02 1 722 . 68 ILE HG13 H 1.479 0.02 1 723 . 68 ILE HD1 H 0.815 0.02 1 724 . 68 ILE CD1 C 12.161 0.05 1 725 . 68 ILE C C 176.976 0.05 1 726 . 69 LEU N N 121.973 0.03 1 727 . 69 LEU H H 8.001 0.02 1 728 . 69 LEU CA C 58.459 0.05 1 729 . 69 LEU HA H 3.724 0.02 1 730 . 69 LEU CB C 41.282 0.05 1 731 . 69 LEU HB2 H 2.247 0.02 1 732 . 69 LEU HB3 H 1.781 0.02 1 733 . 69 LEU CG C 26.713 0.05 1 734 . 69 LEU HG H 1.574 0.02 1 735 . 69 LEU HD1 H 1.263 0.02 1 736 . 69 LEU HD2 H 0.648 0.02 1 737 . 69 LEU CD1 C 24.147 0.05 1 738 . 69 LEU CD2 C 25.138 0.05 1 739 . 69 LEU C C 178.220 0.05 1 740 . 70 LYS N N 118.204 0.03 1 741 . 70 LYS H H 7.573 0.02 1 742 . 70 LYS CA C 59.685 0.05 1 743 . 70 LYS HA H 3.952 0.02 1 744 . 70 LYS CB C 30.670 0.05 1 745 . 70 LYS HB2 H 2.130 0.02 1 746 . 70 LYS HB3 H 1.962 0.02 1 747 . 70 LYS CG C 24.848 0.05 1 748 . 70 LYS HG2 H 1.625 0.02 1 749 . 70 LYS HG3 H 1.515 0.02 1 750 . 70 LYS CD C 29.001 0.05 1 751 . 70 LYS HD2 H 1.707 0.02 1 752 . 70 LYS HE2 H 3.011 0.02 1 753 . 70 LYS C C 178.437 0.05 1 754 . 71 ASP N N 119.684 0.03 1 755 . 71 ASP H H 8.150 0.02 1 756 . 71 ASP CA C 57.017 0.05 1 757 . 71 ASP HA H 4.462 0.02 1 758 . 71 ASP CB C 39.835 0.05 1 759 . 71 ASP HB2 H 2.817 0.02 1 760 . 71 ASP HB3 H 2.643 0.02 1 761 . 71 ASP C C 178.990 0.05 1 762 . 72 ALA N N 123.421 0.03 1 763 . 72 ALA H H 8.969 0.02 1 764 . 72 ALA CA C 55.870 0.05 1 765 . 72 ALA HA H 3.898 0.02 1 766 . 72 ALA HB H 1.474 0.02 1 767 . 72 ALA CB C 17.313 0.05 1 768 . 72 ALA C C 177.213 0.05 1 769 . 73 LYS N N 118.640 0.03 1 770 . 73 LYS H H 8.364 0.02 1 771 . 73 LYS CA C 59.541 0.05 1 772 . 73 LYS HA H 4.273 0.02 1 773 . 73 LYS CB C 31.953 0.05 1 774 . 73 LYS HB2 H 2.137 0.02 1 775 . 73 LYS HB3 H 2.042 0.02 1 776 . 73 LYS CG C 24.964 0.05 1 777 . 73 LYS HG2 H 1.658 0.02 1 778 . 73 LYS CD C 29.018 0.05 1 779 . 73 LYS HD2 H 1.815 0.02 1 780 . 73 LYS CE C 42.081 0.05 1 781 . 73 LYS HE2 H 3.111 0.02 1 782 . 73 LYS C C 174.963 0.05 1 783 . 74 ILE N N 120.095 0.03 1 784 . 74 ILE H H 8.390 0.02 1 785 . 74 ILE CA C 64.160 0.05 1 786 . 74 ILE HA H 4.045 0.02 1 787 . 74 ILE CB C 37.652 0.05 1 788 . 74 ILE HB H 2.096 0.02 1 789 . 74 ILE HG2 H 1.031 0.02 1 790 . 74 ILE CG2 C 17.170 0.05 1 791 . 74 ILE CG1 C 28.757 0.05 1 792 . 74 ILE HG12 H 1.708 0.02 1 793 . 74 ILE HG13 H 1.451 0.02 1 794 . 74 ILE HD1 H 0.945 0.02 1 795 . 74 ILE CD1 C 13.392 0.05 1 796 . 74 ILE C C 176.996 0.05 1 797 . 75 ASN N N 116.863 0.03 1 798 . 75 ASN H H 7.421 0.02 1 799 . 75 ASN CA C 53.917 0.05 1 800 . 75 ASN HA H 4.843 0.02 1 801 . 75 ASN CB C 40.193 0.05 1 802 . 75 ASN HB2 H 2.938 0.02 1 803 . 75 ASN HB3 H 2.551 0.02 1 804 . 75 ASN ND2 N 115.539 0.03 1 805 . 75 ASN HD21 H 7.178 0.02 1 806 . 75 ASN HD22 H 7.776 0.02 1 807 . 75 ASN C C 174.459 0.05 1 808 . 76 GLY N N 108.089 0.03 1 809 . 76 GLY H H 7.996 0.02 1 810 . 76 GLY CA C 46.809 0.05 1 811 . 76 GLY HA2 H 4.099 0.02 1 812 . 76 GLY HA3 H 3.994 0.02 1 813 . 76 GLY C C 174.647 0.05 1 814 . 77 LYS N N 117.725 0.03 1 815 . 77 LYS H H 8.383 0.02 1 816 . 77 LYS CA C 53.299 0.05 1 817 . 77 LYS HA H 4.978 0.02 1 818 . 77 LYS CB C 34.333 0.05 1 819 . 77 LYS HB2 H 1.789 0.02 1 820 . 77 LYS HB3 H 1.628 0.02 1 821 . 77 LYS CG C 25.444 0.05 1 822 . 77 LYS HG2 H 1.446 0.02 1 823 . 77 LYS HG3 H 1.323 0.02 1 824 . 77 LYS CD C 27.597 0.05 1 825 . 77 LYS HD2 H 1.451 0.02 1 826 . 77 LYS CE C 43.343 0.05 1 827 . 77 LYS HE2 H 3.125 0.02 1 828 . 77 LYS C C 176.068 0.05 1 829 . 78 GLU N N 121.528 0.03 1 830 . 78 GLU H H 8.625 0.02 1 831 . 78 GLU CA C 55.406 0.05 1 832 . 78 GLU HA H 4.611 0.02 1 833 . 78 GLU CB C 31.562 0.05 1 834 . 78 GLU HB2 H 2.130 0.02 1 835 . 78 GLU HB3 H 1.933 0.02 1 836 . 78 GLU CG C 35.895 0.05 1 837 . 78 GLU HG2 H 2.378 0.02 1 838 . 78 GLU HG3 H 2.281 0.02 1 839 . 78 GLU C C 174.292 0.05 1 840 . 79 PHE N N 126.907 0.03 1 841 . 79 PHE H H 8.552 0.02 1 842 . 79 PHE CA C 56.490 0.05 1 843 . 79 PHE HA H 5.705 0.02 1 844 . 79 PHE CB C 42.038 0.05 1 845 . 79 PHE HB2 H 3.268 0.02 1 846 . 79 PHE HB3 H 2.699 0.02 1 847 . 79 PHE HD1 H 7.080 0.02 1 848 . 79 PHE HE1 H 7.276 0.02 1 849 . 79 PHE CD1 C 132.681 0.05 1 850 . 79 PHE CE1 C 130.901 0.05 1 851 . 79 PHE CZ C 130.259 0.05 1 852 . 79 PHE HZ H 7.535 0.02 1 853 . 79 PHE C C 173.857 0.05 1 854 . 80 ILE N N 130.116 0.03 1 855 . 80 ILE H H 8.742 0.02 1 856 . 80 ILE CA C 60.185 0.05 1 857 . 80 ILE HA H 4.541 0.02 1 858 . 80 ILE CB C 43.085 0.05 1 859 . 80 ILE HB H 1.520 0.02 1 860 . 80 ILE HG2 H 0.855 0.02 1 861 . 80 ILE CG2 C 18.863 0.05 1 862 . 80 ILE CG1 C 28.685 0.05 1 863 . 80 ILE HG12 H 1.509 0.02 1 864 . 80 ILE HG13 H 1.084 0.02 1 865 . 80 ILE HD1 H 0.869 0.02 1 866 . 80 ILE CD1 C 14.853 0.05 1 867 . 80 ILE C C 173.739 0.05 1 868 . 81 LEU N N 123.589 0.03 1 869 . 81 LEU H H 8.547 0.02 1 870 . 81 LEU CA C 53.009 0.05 1 871 . 81 LEU HA H 4.784 0.02 1 872 . 81 LEU CB C 43.700 0.05 1 873 . 81 LEU HB2 H 1.850 0.02 1 874 . 81 LEU HB3 H 1.210 0.02 1 875 . 81 LEU CG C 26.908 0.05 1 876 . 81 LEU HG H 1.531 0.02 1 877 . 81 LEU HD1 H 0.542 0.02 1 878 . 81 LEU HD2 H 0.081 0.02 1 879 . 81 LEU CD1 C 23.765 0.05 1 880 . 81 LEU CD2 C 24.497 0.05 1 881 . 81 LEU C C 175.338 0.05 1 882 . 82 SER N N 114.166 0.03 1 883 . 82 SER H H 8.500 0.02 1 884 . 82 SER CA C 56.497 0.05 1 885 . 82 SER HA H 5.467 0.02 1 886 . 82 SER CB C 67.280 0.05 1 887 . 82 SER HB2 H 3.129 0.02 1 888 . 82 SER HB3 H 3.022 0.02 1 889 . 82 SER C C 173.601 0.05 1 890 . 83 SER N N 115.283 0.03 1 891 . 83 SER H H 7.473 0.02 1 892 . 83 SER CA C 57.680 0.05 1 893 . 83 SER HA H 4.092 0.02 1 894 . 83 SER CB C 61.015 0.05 1 895 . 83 SER HB2 H 3.971 0.02 1 896 . 83 SER C C 173.541 0.05 1 897 . 84 LEU N N 118.666 0.03 1 898 . 84 LEU H H 8.234 0.02 1 899 . 84 LEU CA C 55.811 0.05 1 900 . 84 LEU HA H 3.930 0.02 1 901 . 84 LEU CB C 41.807 0.05 1 902 . 84 LEU HB2 H 1.551 0.02 1 903 . 84 LEU CG C 28.915 0.05 1 904 . 84 LEU HG H 1.637 0.02 1 905 . 84 LEU HD1 H 0.808 0.02 1 906 . 84 LEU HD2 H 0.716 0.02 1 907 . 84 LEU CD1 C 25.939 0.05 1 908 . 84 LEU CD2 C 26.041 0.05 1 909 . 84 LEU C C 179.128 0.05 1 910 . 85 LYS N N 123.305 0.03 1 911 . 85 LYS H H 9.440 0.02 1 912 . 85 LYS CA C 56.077 0.05 1 913 . 85 LYS HA H 4.446 0.02 1 914 . 85 LYS CB C 33.440 0.05 1 915 . 85 LYS HB2 H 2.177 0.02 1 916 . 85 LYS HB3 H 1.873 0.02 1 917 . 85 LYS CG C 25.745 0.05 1 918 . 85 LYS HG2 H 1.813 0.02 1 919 . 85 LYS HG3 H 1.646 0.02 1 920 . 85 LYS CD C 29.008 0.05 1 921 . 85 LYS HD2 H 1.815 0.02 1 922 . 85 LYS CE C 39.522 0.05 1 923 . 85 LYS HE2 H 3.112 0.02 1 924 . 85 LYS C C 178.496 0.05 1 925 . 86 GLU N N 123.767 0.03 1 926 . 86 GLU H H 8.974 0.02 1 927 . 86 GLU CA C 59.668 0.05 1 928 . 86 GLU HA H 4.124 0.02 1 929 . 86 GLU CB C 29.002 0.05 1 930 . 86 GLU HB2 H 2.207 0.02 1 931 . 86 GLU HB3 H 2.110 0.02 1 932 . 86 GLU CG C 35.399 0.05 1 933 . 86 GLU HG2 H 2.423 0.02 1 934 . 86 GLU C C 178.102 0.05 1 935 . 87 SER N N 111.346 0.03 1 936 . 87 SER H H 8.368 0.02 1 937 . 87 SER CA C 60.803 0.05 1 938 . 87 SER HA H 4.144 0.02 1 939 . 87 SER CB C 61.976 0.05 1 940 . 87 SER HB2 H 4.133 0.02 1 941 . 87 SER C C 176.285 0.05 1 942 . 88 ILE N N 121.612 0.03 1 943 . 88 ILE H H 7.157 0.02 1 944 . 88 ILE CA C 61.307 0.05 1 945 . 88 ILE HA H 4.102 0.02 1 946 . 88 ILE CB C 35.972 0.05 1 947 . 88 ILE HB H 2.158 0.02 1 948 . 88 ILE HG2 H 0.825 0.02 1 949 . 88 ILE CG2 C 17.406 0.05 1 950 . 88 ILE CG1 C 27.830 0.05 1 951 . 88 ILE HG12 H 1.483 0.02 1 952 . 88 ILE HD1 H 0.646 0.02 1 953 . 88 ILE CD1 C 10.423 0.05 1 954 . 88 ILE C C 177.766 0.05 1 955 . 89 SER N N 116.561 0.03 1 956 . 89 SER H H 8.487 0.02 1 957 . 89 SER CA C 62.153 0.05 1 958 . 89 SER HA H 3.912 0.02 1 959 . 89 SER CB C 62.947 0.05 1 960 . 89 SER HB2 H 3.871 0.02 1 961 . 89 SER C C 179.197 0.05 1 962 . 90 ARG N N 118.707 0.03 1 963 . 90 ARG H H 8.384 0.02 1 964 . 90 ARG CA C 59.683 0.05 1 965 . 90 ARG HA H 4.063 0.02 1 966 . 90 ARG CB C 29.858 0.05 1 967 . 90 ARG HB2 H 2.139 0.02 1 968 . 90 ARG HB3 H 1.998 0.02 1 969 . 90 ARG CG C 27.369 0.05 1 970 . 90 ARG HG2 H 1.818 0.02 1 971 . 90 ARG HG3 H 1.659 0.02 1 972 . 90 ARG CD C 43.336 0.05 1 973 . 90 ARG HD2 H 3.284 0.02 1 974 . 90 ARG NE N 85.216 0.03 1 975 . 90 ARG HE H 7.549 0.02 1 976 . 90 ARG NH1 N 72.321 0.03 1 977 . 90 ARG HH21 H 6.956 0.02 1 978 . 90 ARG C C 178.457 0.05 1 979 . 91 ILE N N 118.216 0.03 1 980 . 91 ILE H H 7.278 0.02 1 981 . 91 ILE CA C 64.482 0.05 1 982 . 91 ILE HA H 3.926 0.02 1 983 . 91 ILE CB C 37.999 0.05 1 984 . 91 ILE HB H 2.047 0.02 1 985 . 91 ILE HG2 H 0.970 0.02 1 986 . 91 ILE CG2 C 17.590 0.05 1 987 . 91 ILE CG1 C 28.787 0.05 1 988 . 91 ILE HG12 H 1.318 0.02 1 989 . 91 ILE HD1 H 0.951 0.02 1 990 . 91 ILE CD1 C 13.463 0.05 1 991 . 91 ILE C C 178.931 0.05 1 992 . 92 LEU N N 121.539 0.03 1 993 . 92 LEU H H 7.870 0.02 1 994 . 92 LEU CA C 58.414 0.05 1 995 . 92 LEU HA H 3.917 0.02 1 996 . 92 LEU CB C 40.681 0.05 1 997 . 92 LEU HB2 H 1.970 0.02 1 998 . 92 LEU HB3 H 1.269 0.02 1 999 . 92 LEU CG C 27.563 0.05 1 1000 . 92 LEU HG H 1.730 0.02 1 1001 . 92 LEU HD1 H 0.636 0.02 1 1002 . 92 LEU HD2 H 0.636 0.02 1 1003 . 92 LEU CD1 C 26.314 0.05 1 1004 . 92 LEU CD2 C 24.007 0.05 1 1005 . 92 LEU C C 178.082 0.05 1 1006 . 93 LYS N N 118.163 0.03 1 1007 . 93 LYS H H 8.008 0.02 1 1008 . 93 LYS CA C 59.091 0.05 1 1009 . 93 LYS HA H 4.204 0.02 1 1010 . 93 LYS CB C 32.356 0.05 1 1011 . 93 LYS HB2 H 1.912 0.02 1 1012 . 93 LYS CG C 25.230 0.05 1 1013 . 93 LYS HG2 H 1.607 0.02 1 1014 . 93 LYS HG3 H 1.436 0.02 1 1015 . 93 LYS CD C 28.944 0.05 1 1016 . 93 LYS HD2 H 1.706 0.02 1 1017 . 93 LYS CE C 44.357 0.05 1 1018 . 93 LYS HE2 H 2.996 0.02 1 1019 . 93 LYS C C 180.628 0.05 1 1020 . 94 LEU N N 120.868 0.03 1 1021 . 94 LEU H H 8.426 0.02 1 1022 . 94 LEU CA C 57.881 0.05 1 1023 . 94 LEU HA H 4.075 0.02 1 1024 . 94 LEU CB C 42.539 0.05 1 1025 . 94 LEU HB2 H 1.912 0.02 1 1026 . 94 LEU HB3 H 1.626 0.02 1 1027 . 94 LEU CG C 26.957 0.05 1 1028 . 94 LEU HG H 1.854 0.02 1 1029 . 94 LEU HD1 H 0.943 0.02 1 1030 . 94 LEU HD2 H 0.944 0.02 1 1031 . 94 LEU CD1 C 24.825 0.05 1 1032 . 94 LEU CD2 C 23.483 0.05 1 1033 . 94 LEU C C 178.575 0.05 1 1034 . 95 THR N N 104.636 0.03 1 1035 . 95 THR H H 7.466 0.02 1 1036 . 95 THR CA C 61.769 0.05 1 1037 . 95 THR HA H 4.163 0.02 1 1038 . 95 THR CB C 70.547 0.05 1 1039 . 95 THR HB H 4.369 0.02 1 1040 . 95 THR HG2 H 1.301 0.02 1 1041 . 95 THR CG2 C 21.705 0.05 1 1042 . 95 THR C C 178.258 0.05 1 1043 . 96 HIS N N 112.176 0.03 1 1044 . 96 HIS H H 7.482 0.02 1 1045 . 96 HIS CA C 56.934 0.05 1 1046 . 96 HIS HA H 4.669 0.02 1 1047 . 96 HIS CB C 25.565 0.05 1 1048 . 96 HIS HB2 H 3.771 0.02 1 1049 . 96 HIS HB3 H 3.561 0.02 1 1050 . 96 HIS CD2 C 119.867 0.05 1 1051 . 96 HIS CE1 C 135.885 0.05 1 1052 . 96 HIS HD2 H 7.378 0.02 1 1053 . 96 HIS HE1 H 8.671 0.02 1 1054 . 96 HIS C C 180.589 0.05 1 1055 . 97 LEU N N 120.355 0.03 1 1056 . 97 LEU H H 8.369 0.02 1 1057 . 97 LEU CA C 56.141 0.05 1 1058 . 97 LEU HA H 4.444 0.02 1 1059 . 97 LEU CB C 42.284 0.05 1 1060 . 97 LEU HB2 H 1.823 0.02 1 1061 . 97 LEU HB3 H 1.864 0.02 1 1062 . 97 LEU CG C 26.988 0.05 1 1063 . 97 LEU HG H 1.845 0.02 1 1064 . 97 LEU HD1 H 1.026 0.02 1 1065 . 97 LEU HD2 H 0.940 0.02 1 1066 . 97 LEU CD1 C 25.976 0.05 1 1067 . 97 LEU CD2 C 23.582 0.05 1 1068 . 97 LEU C C 177.904 0.05 1 1069 . 98 ASP N N 119.450 0.03 1 1070 . 98 ASP H H 8.785 0.02 1 1071 . 98 ASP CA C 56.018 0.05 1 1072 . 98 ASP HA H 4.254 0.02 1 1073 . 98 ASP CB C 38.394 0.05 1 1074 . 98 ASP HB2 H 2.822 0.02 1 1075 . 98 ASP HB3 H 2.325 0.02 1 1076 . 98 ASP C C 176.108 0.05 1 1077 . 99 LYS N N 115.188 0.03 1 1078 . 99 LYS H H 7.404 0.02 1 1079 . 99 LYS CA C 56.350 0.05 1 1080 . 99 LYS HA H 4.406 0.02 1 1081 . 99 LYS CB C 32.340 0.05 1 1082 . 99 LYS HB2 H 2.010 0.02 1 1083 . 99 LYS HB3 H 1.901 0.02 1 1084 . 99 LYS CG C 24.682 0.05 1 1085 . 99 LYS HG2 H 1.612 0.02 1 1086 . 99 LYS HG3 H 1.536 0.02 1 1087 . 99 LYS CD C 28.448 0.05 1 1088 . 99 LYS HD2 H 1.718 0.02 1 1089 . 99 LYS CE C 42.042 0.05 1 1090 . 99 LYS HE2 H 3.053 0.02 1 1091 . 99 LYS C C 177.373 0.05 1 1092 . 100 ILE N N 115.131 0.03 1 1093 . 100 ILE H H 7.466 0.02 1 1094 . 100 ILE CA C 61.095 0.05 1 1095 . 100 ILE HA H 4.313 0.02 1 1096 . 100 ILE CB C 38.427 0.05 1 1097 . 100 ILE HB H 1.914 0.02 1 1098 . 100 ILE HG2 H 0.659 0.02 1 1099 . 100 ILE CG2 C 17.097 0.05 1 1100 . 100 ILE CG1 C 26.885 0.05 1 1101 . 100 ILE HG12 H 1.298 0.02 1 1102 . 100 ILE HG13 H 1.121 0.02 1 1103 . 100 ILE HD1 H 0.733 0.02 1 1104 . 100 ILE CD1 C 12.918 0.05 1 1105 . 100 ILE C C 175.595 0.05 1 1106 . 101 PHE N N 117.702 0.03 1 1107 . 101 PHE H H 7.394 0.02 1 1108 . 101 PHE CA C 57.529 0.05 1 1109 . 101 PHE HA H 4.844 0.02 1 1110 . 101 PHE CB C 41.356 0.05 1 1111 . 101 PHE HB2 H 3.032 0.02 1 1112 . 101 PHE HB3 H 2.630 0.02 1 1113 . 101 PHE HD1 H 7.539 0.02 1 1114 . 101 PHE HE1 H 7.249 0.02 1 1115 . 101 PHE CD1 C 132.325 0.05 1 1116 . 101 PHE CE1 C 130.190 0.05 1 1117 . 101 PHE CZ C 130.312 0.05 1 1118 . 101 PHE HZ H 7.074 0.02 1 1119 . 101 PHE C C 175.200 0.05 1 1120 . 102 LYS N N 123.382 0.03 1 1121 . 102 LYS H H 9.140 0.02 1 1122 . 102 LYS CA C 56.193 0.05 1 1123 . 102 LYS HA H 4.552 0.02 1 1124 . 102 LYS CB C 32.559 0.05 1 1125 . 102 LYS HB2 H 2.060 0.02 1 1126 . 102 LYS HB3 H 1.963 0.02 1 1127 . 102 LYS CG C 25.411 0.05 1 1128 . 102 LYS HG2 H 1.533 0.02 1 1129 . 102 LYS HG3 H 1.417 0.02 1 1130 . 102 LYS CD C 29.039 0.05 1 1131 . 102 LYS HD2 H 1.759 0.02 1 1132 . 102 LYS CE C 42.112 0.05 1 1133 . 102 LYS HE2 H 2.997 0.02 1 1134 . 102 LYS C C 174.864 0.05 1 1135 . 103 ILE N N 127.329 0.03 1 1136 . 103 ILE H H 8.321 0.02 1 1137 . 103 ILE CA C 59.456 0.05 1 1138 . 103 ILE HA H 5.426 0.02 1 1139 . 103 ILE CB C 41.218 0.05 1 1140 . 103 ILE HB H 1.634 0.02 1 1141 . 103 ILE HG2 H 0.844 0.02 1 1142 . 103 ILE CG2 C 18.063 0.05 1 1143 . 103 ILE CG1 C 27.905 0.05 1 1144 . 103 ILE HG12 H 1.623 0.02 1 1145 . 103 ILE HG13 H 0.851 0.02 1 1146 . 103 ILE HD1 H 0.899 0.02 1 1147 . 103 ILE CD1 C 14.194 0.05 1 1148 . 103 ILE C C 176.937 0.05 1 1149 . 104 THR N N 117.159 0.03 1 1150 . 104 THR H H 9.085 0.02 1 1151 . 104 THR CA C 59.291 0.05 1 1152 . 104 THR HA H 4.927 0.02 1 1153 . 104 THR CB C 70.886 0.05 1 1154 . 104 THR HB H 4.460 0.02 1 1155 . 104 THR HG2 H 1.026 0.02 1 1156 . 104 THR CG2 C 21.607 0.05 1 1157 . 104 THR C C 175.437 0.05 1 1158 . 105 ASP N N 122.561 0.03 1 1159 . 105 ASP H H 8.934 0.02 1 1160 . 105 ASP CA C 57.052 0.05 1 1161 . 105 ASP HA H 4.648 0.02 1 1162 . 105 ASP CB C 40.817 0.05 1 1163 . 105 ASP HB2 H 3.007 0.02 1 1164 . 105 ASP HB3 H 2.835 0.02 1 1165 . 105 ASP C C 176.680 0.05 1 1166 . 106 THR N N 106.211 0.03 1 1167 . 106 THR H H 7.553 0.02 1 1168 . 106 THR CA C 58.740 0.05 1 1169 . 106 THR HA H 4.821 0.02 1 1170 . 106 THR CB C 72.036 0.05 1 1171 . 106 THR HB H 4.553 0.02 1 1172 . 106 THR HG2 H 1.201 0.02 1 1173 . 106 THR CG2 C 21.364 0.05 1 1174 . 106 THR C C 175.970 0.05 1 1175 . 107 VAL N N 121.266 0.03 1 1176 . 107 VAL H H 8.734 0.02 1 1177 . 107 VAL CA C 64.515 0.05 1 1178 . 107 VAL HA H 3.733 0.02 1 1179 . 107 VAL CB C 31.546 0.05 1 1180 . 107 VAL HB H 2.029 0.02 1 1181 . 107 VAL HG1 H 0.958 0.02 1 1182 . 107 VAL HG2 H 0.947 0.02 1 1183 . 107 VAL CG1 C 20.979 0.05 1 1184 . 107 VAL CG2 C 21.619 0.05 1 1185 . 107 VAL C C 178.102 0.05 1 1186 . 108 GLU N N 119.573 0.03 1 1187 . 108 GLU H H 8.572 0.02 1 1188 . 108 GLU CA C 59.061 0.05 1 1189 . 108 GLU HA H 4.054 0.02 1 1190 . 108 GLU CB C 28.659 0.05 1 1191 . 108 GLU HB2 H 2.051 0.02 1 1192 . 108 GLU CG C 36.363 0.05 1 1193 . 108 GLU HG2 H 2.487 0.02 1 1194 . 108 GLU HG3 H 2.323 0.02 1 1195 . 108 GLU C C 177.272 0.05 1 1196 . 109 GLU N N 115.984 0.03 1 1197 . 109 GLU H H 7.210 0.02 1 1198 . 109 GLU CA C 56.022 0.05 1 1199 . 109 GLU HA H 4.243 0.02 1 1200 . 109 GLU CB C 30.567 0.05 1 1201 . 109 GLU HB2 H 2.283 0.02 1 1202 . 109 GLU HB3 H 2.148 0.02 1 1203 . 109 GLU CG C 35.579 0.05 1 1204 . 109 GLU HG2 H 2.459 0.02 1 1205 . 109 GLU C C 175.555 0.05 1 1206 . 110 ALA N N 126.971 0.03 1 1207 . 110 ALA H H 7.205 0.02 1 1208 . 110 ALA CA C 54.307 0.05 1 1209 . 110 ALA HA H 3.955 0.02 1 1210 . 110 ALA HB H 1.342 0.02 1 1211 . 110 ALA CB C 20.368 0.05 1 stop_ save_