data_7325 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Ile(d1), Leu and Val Sidechain Resonance Assignments of the NUDIX Domain of Yeast Dcp2 ; _BMRB_accession_number 7325 _BMRB_flat_file_name bmr7325.str _Entry_type original _Submission_date 2006-11-04 _Accession_date 2006-11-06 _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 Deshmukh Mandar V. . 2 Oku Yuko . . 3 Gross John D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 459 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2007-08-22 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'mRNA decapping is promoted by an RNA-binding channel in Dcp2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18280238 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deshmukh Mandar V. . 2 Jones Brittnee N. . 3 Quang-Dang Duc-Uy . . 4 Flinders Jeremy . . 5 Floor Stephen N. . 6 Kim Candice . . 7 Jemielity Jacek . . 8 Kalek Marcin . . 9 Darzynkiewicz Edward . . 10 Gross John D. . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 324 _Page_last 336 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name yDcp2(100-245) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gb1-yDcp2 $Nudix_Domain_of_yDcp2 stop_ _System_molecular_weight 24767.9 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state unknown _Database_query_date . _Details 'Residues 100-245 of yeast Dcp2 as C-terminal fusion to the B1 domain of protein G' save_ ######################## # Monomeric polymers # ######################## save_Nudix_Domain_of_yDcp2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common yDcp2(100-245) _Molecular_mass 17353.9 _Mol_thiol_state unknown _Details 'Assigned as a fusion to the B1 domain of Streptococcal protein G' ############################## # Polymer residue sequence # ############################## _Residue_count 146 _Mol_residue_sequence ; KKSIPVRGAAIFNENLSKIL LVQGTESDSWSFPRGKISKD ENDIDCCIREVKEEIGFDLT DYIDDNQFIERNIQGKNYKI FLISGVSEVFNFKPQVRNEI DKIEWFDFKKISKTMYKSNI KYYLINSMMRPLSMWLRHQR QIKNED ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 59 LYS 2 60 LYS 3 61 SER 4 62 ILE 5 63 PRO 6 64 VAL 7 65 ARG 8 66 GLY 9 67 ALA 10 68 ALA 11 69 ILE 12 70 PHE 13 71 ASN 14 72 GLU 15 73 ASN 16 74 LEU 17 75 SER 18 76 LYS 19 77 ILE 20 78 LEU 21 79 LEU 22 80 VAL 23 81 GLN 24 82 GLY 25 83 THR 26 84 GLU 27 85 SER 28 86 ASP 29 87 SER 30 88 TRP 31 89 SER 32 90 PHE 33 91 PRO 34 92 ARG 35 93 GLY 36 94 LYS 37 95 ILE 38 96 SER 39 97 LYS 40 98 ASP 41 99 GLU 42 100 ASN 43 101 ASP 44 102 ILE 45 103 ASP 46 104 CYS 47 105 CYS 48 106 ILE 49 107 ARG 50 108 GLU 51 109 VAL 52 110 LYS 53 111 GLU 54 112 GLU 55 113 ILE 56 114 GLY 57 115 PHE 58 116 ASP 59 117 LEU 60 118 THR 61 119 ASP 62 120 TYR 63 121 ILE 64 122 ASP 65 123 ASP 66 124 ASN 67 125 GLN 68 126 PHE 69 127 ILE 70 128 GLU 71 129 ARG 72 130 ASN 73 131 ILE 74 132 GLN 75 133 GLY 76 134 LYS 77 135 ASN 78 136 TYR 79 137 LYS 80 138 ILE 81 139 PHE 82 140 LEU 83 141 ILE 84 142 SER 85 143 GLY 86 144 VAL 87 145 SER 88 146 GLU 89 147 VAL 90 148 PHE 91 149 ASN 92 150 PHE 93 151 LYS 94 152 PRO 95 153 GLN 96 154 VAL 97 155 ARG 98 156 ASN 99 157 GLU 100 158 ILE 101 159 ASP 102 160 LYS 103 161 ILE 104 162 GLU 105 163 TRP 106 164 PHE 107 165 ASP 108 166 PHE 109 167 LYS 110 168 LYS 111 169 ILE 112 170 SER 113 171 LYS 114 172 THR 115 173 MET 116 174 TYR 117 175 LYS 118 176 SER 119 177 ASN 120 178 ILE 121 179 LYS 122 180 TYR 123 181 TYR 124 182 LEU 125 183 ILE 126 184 ASN 127 185 SER 128 186 MET 129 187 MET 130 188 ARG 131 189 PRO 132 190 LEU 133 191 SER 134 192 MET 135 193 TRP 136 194 LEU 137 195 ARG 138 196 HIS 139 197 GLN 140 198 ARG 141 199 GLN 142 200 ILE 143 201 LYS 144 202 ASN 145 203 GLU 146 204 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2JVB "Solution Structure Of Catalytic Domain Of Ydcp2" 100.00 146 100.00 100.00 1.26e-100 PDB 4K6E "Crystal Structure Of Saccharomyces Cerevisiae Dcp2 Nudix Domain In Complex With Mg" 98.63 144 100.00 100.00 2.32e-99 PDB 4KG3 "Crystal Structure Of Saccharomyces Cerevisiae Dcp2 Nudix Domain In Complex With Mg (e153q Mutation)" 100.00 146 99.32 100.00 3.66e-100 PDB 4KG4 "Crystal Structure Of Saccharomyces Cerevisiae Dcp2 Nudix Domain (e198q Mutation)" 100.00 146 99.32 100.00 3.66e-100 DBJ GAA25980 "K7_Dcp2p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 970 100.00 100.00 1.74e-96 EMBL CAA93389 "N1917 [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.49e-96 EMBL CAA95998 "PSU1 [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.49e-96 GB AAA68866 "suppresses the respiratory deficiency of a yeast pet mutant [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.20e-96 GB AAC99860 "Nmd1p [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.49e-96 GB ABN58539 "DCP2 [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.49e-96 GB ABN58548 "DCP2 [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.34e-96 GB ABN58557 "DCP2 [Saccharomyces cerevisiae]" 100.00 970 100.00 100.00 2.49e-96 REF NP_014281 "Dcp2p [Saccharomyces cerevisiae S288c]" 100.00 970 100.00 100.00 2.49e-96 SP A6ZRW5 "RecName: Full=mRNA-decapping enzyme subunit 2; AltName: Full=Protein PSU1 [Saccharomyces cerevisiae YJM789]" 100.00 970 100.00 100.00 1.95e-96 SP P53550 "RecName: Full=mRNA-decapping enzyme subunit 2; AltName: Full=Protein PSU1 [Saccharomyces cerevisiae S288c]" 100.00 970 100.00 100.00 2.49e-96 TPG DAA10430 "TPA: decapping enzyme complex catalytic subunit DCP1 [Saccharomyces cerevisiae S288c]" 100.00 970 100.00 100.00 2.49e-96 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Nudix_Domain_of_yDcp2 'Baker's Yeast' 4932 Eukaryota Fungi Saccharomyces Cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $Nudix_Domain_of_yDcp2 'recombinant technology' 'E. Coli' Eschericia Coli BL21 DE3 GB1-pET30a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 20mM Na Phosphate 100mM Sodium Sulfate 50mM Arginine 50mM Glutamate 100mM NaCl Sample one was made with 1H/13C glucose, 99% D2O and 15N4Cl in standard M9. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_Domain_of_yDcp2 0.5 mM '[U-2H; U-13C; U-15N]' 'Na Phosphate' 20 mM . 'Sodium Sulfate' 100 mM . Arginine 50 mM . Glutamate 50 mM . NaCl 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; 20mM Na Phosphate 100mM Sodium Sulfate 50mM Arginine 50mM Glutamate 100mM NaCl Sample two was made with 2H/13C glucose, 99%D2O and 15N4Cl in standard M9 but with addition of uniform gamma protonated 13C/2H precursors 30 minutes prior to induction as described by Goto et al, JBNMR. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_Domain_of_yDcp2 0.5 mM '[U-2H; NA-Ile,Leu,Val metthyl; U-13C; U-15N]' 'Na Phosphate' 20 mM . 'Sodium Sulfate' 100 mM . Arginine 50 mM . Glutamate 50 mM . NaCl 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample_1 save_ save_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label $sample_1 save_ save_(H)C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_NMR_Buffer _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.04 pH temperature 298 0.4 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_Backbone_ILVMET _Saveframe_category assigned_chemical_shifts _Details 'Backbone and Ile(d1), Leu and Val Chemical shift assignments' loop_ _Experiment_label HNCA HN(CO)CA HN(CA)CB HN(COCA)CB HNCO HN(CA)CO H(CCO)NH (H)C(CO)NH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $NMR_Buffer _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name gb1-yDcp2 _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 61 3 SER C C 174.003 0.000 . 2 61 3 SER CA C 57.238 0.000 . 3 61 3 SER CB C 63.886 0.000 . 4 62 4 ILE H H 8.201 0.000 . 5 62 4 ILE HD1 H 0.798 0.000 . 6 62 4 ILE C C 174.479 0.000 . 7 62 4 ILE CA C 58.254 0.000 . 8 62 4 ILE CB C 38.863 0.000 . 9 62 4 ILE CD1 C 12.253 0.000 . 10 62 4 ILE N N 127.564 0.000 . 11 63 5 PRO C C 175.896 0.000 . 12 63 5 PRO CA C 53.661 0.000 . 13 63 5 PRO CB C 38.786 0.000 . 14 64 6 VAL H H 8.226 0.000 . 15 64 6 VAL HG1 H 0.709 0.000 . 16 64 6 VAL HG2 H 0.839 0.000 . 17 64 6 VAL C C 177.452 0.008 . 18 64 6 VAL CA C 60.459 0.000 . 19 64 6 VAL CB C 34.176 0.066 . 20 64 6 VAL CG1 C 21.090 0.000 . 21 64 6 VAL CG2 C 21.230 0.000 . 22 64 6 VAL N N 121.321 0.000 . 23 65 7 ARG H H 9.512 0.000 . 24 65 7 ARG C C 175.059 0.010 . 25 65 7 ARG CA C 53.988 0.000 . 26 65 7 ARG CB C 32.608 0.000 . 27 65 7 ARG N N 131.838 0.000 . 28 66 8 GLY H H 8.376 0.000 . 29 66 8 GLY C C 171.521 0.004 . 30 66 8 GLY CA C 45.597 0.016 . 31 66 8 GLY N N 107.089 0.000 . 32 67 9 ALA H H 7.855 0.000 . 33 67 9 ALA C C 173.473 0.008 . 34 67 9 ALA CA C 50.520 0.006 . 35 67 9 ALA CB C 23.322 0.017 . 36 67 9 ALA N N 121.629 0.000 . 37 68 10 ALA H H 8.834 0.000 . 38 68 10 ALA C C 173.276 0.000 . 39 68 10 ALA CA C 49.301 0.000 . 40 68 10 ALA CB C 18.860 0.000 . 41 68 10 ALA N N 128.779 0.000 . 42 69 11 ILE H H 9.583 0.000 . 43 69 11 ILE HD1 H 0.523 0.000 . 44 69 11 ILE C C 173.374 0.000 . 45 69 11 ILE CA C 60.990 0.015 . 46 69 11 ILE CB C 38.632 0.024 . 47 69 11 ILE CD1 C 14.701 0.000 . 48 69 11 ILE N N 124.902 0.000 . 49 70 12 PHE H H 8.816 0.000 . 50 70 12 PHE C C 176.277 0.016 . 51 70 12 PHE CA C 55.922 0.000 . 52 70 12 PHE CB C 42.667 0.196 . 53 70 12 PHE N N 124.833 0.000 . 54 71 13 ASN H H 8.281 0.000 . 55 71 13 ASN C C 177.941 0.013 . 56 71 13 ASN CA C 51.422 0.000 . 57 71 13 ASN CB C 37.009 0.000 . 58 71 13 ASN N N 118.863 0.000 . 59 72 14 GLU H H 8.407 0.000 . 60 72 14 GLU C C 177.214 0.016 . 61 72 14 GLU CA C 59.599 0.088 . 62 72 14 GLU CB C 29.381 0.000 . 63 72 14 GLU N N 118.635 0.000 . 64 73 15 ASN H H 7.433 0.000 . 65 73 15 ASN C C 174.572 0.024 . 66 73 15 ASN CA C 51.479 0.000 . 67 73 15 ASN CB C 37.904 0.000 . 68 73 15 ASN N N 113.125 0.000 . 69 74 16 LEU H H 7.667 0.000 . 70 74 16 LEU HD1 H 0.583 0.000 . 71 74 16 LEU HD2 H 0.652 0.000 . 72 74 16 LEU C C 174.083 0.031 . 73 74 16 LEU CA C 56.311 0.033 . 74 74 16 LEU CB C 37.157 0.019 . 75 74 16 LEU CD1 C 25.918 0.000 . 76 74 16 LEU CD2 C 23.502 0.000 . 77 74 16 LEU N N 114.869 0.000 . 78 75 17 SER H H 8.862 0.000 . 79 75 17 SER C C 175.809 0.025 . 80 75 17 SER CA C 58.106 0.003 . 81 75 17 SER CB C 66.150 0.300 . 82 75 17 SER N N 110.761 0.000 . 83 76 18 LYS H H 8.207 0.000 . 84 76 18 LYS C C 172.717 0.000 . 85 76 18 LYS CA C 54.462 0.022 . 86 76 18 LYS CB C 38.914 0.051 . 87 76 18 LYS N N 123.280 0.000 . 88 77 19 ILE H H 9.354 0.000 . 89 77 19 ILE HD1 H 0.606 0.000 . 90 77 19 ILE C C 172.737 0.049 . 91 77 19 ILE CA C 56.472 0.015 . 92 77 19 ILE CB C 42.354 0.062 . 93 77 19 ILE CD1 C 14.559 0.000 . 94 77 19 ILE N N 119.977 0.000 . 95 78 20 LEU H H 8.120 0.000 . 96 78 20 LEU HD1 H -1.006 0.000 . 97 78 20 LEU HD2 H -0.591 0.000 . 98 78 20 LEU C C 174.901 0.017 . 99 78 20 LEU CA C 53.786 0.023 . 100 78 20 LEU CB C 41.529 0.041 . 101 78 20 LEU CD1 C 22.244 0.000 . 102 78 20 LEU CD2 C 25.326 0.000 . 103 78 20 LEU N N 133.142 0.000 . 104 79 21 LEU H H 8.816 0.000 . 105 79 21 LEU HD1 H -0.071 0.000 . 106 79 21 LEU HD2 H 0.452 0.000 . 107 79 21 LEU C C 175.306 0.007 . 108 79 21 LEU CA C 52.447 0.000 . 109 79 21 LEU CB C 45.062 0.097 . 110 79 21 LEU CD1 C 24.701 0.000 . 111 79 21 LEU CD2 C 22.829 0.000 . 112 79 21 LEU N N 125.910 0.000 . 113 80 22 VAL H H 9.069 0.000 . 114 80 22 VAL HG1 H 0.747 0.000 . 115 80 22 VAL HG2 H 0.606 0.000 . 116 80 22 VAL C C 175.406 0.023 . 117 80 22 VAL CA C 57.817 0.007 . 118 80 22 VAL CB C 34.979 0.080 . 119 80 22 VAL CG1 C 23.040 0.000 . 120 80 22 VAL CG2 C 18.155 0.000 . 121 80 22 VAL N N 110.223 0.000 . 122 81 23 GLN H H 8.688 0.000 . 123 81 23 GLN C C 176.041 0.000 . 124 81 23 GLN CA C 53.730 0.003 . 125 81 23 GLN CB C 31.209 0.036 . 126 81 23 GLN N N 126.501 0.000 . 127 82 24 GLY H H 8.832 0.000 . 128 82 24 GLY C C 173.354 0.009 . 129 82 24 GLY CA C 44.302 0.097 . 130 82 24 GLY N N 115.742 0.000 . 131 83 25 THR H H 7.963 0.000 . 132 83 25 THR C C 176.014 0.020 . 133 83 25 THR CA C 63.158 0.055 . 134 83 25 THR CB C 68.802 0.104 . 135 83 25 THR N N 113.171 0.000 . 136 84 26 GLU H H 8.634 0.000 . 137 84 26 GLU C C 175.682 0.003 . 138 84 26 GLU CA C 56.302 0.052 . 139 84 26 GLU CB C 28.918 0.196 . 140 84 26 GLU N N 120.795 0.000 . 141 85 27 SER H H 7.433 0.000 . 142 85 27 SER C C 174.731 0.000 . 143 85 27 SER CA C 56.581 0.000 . 144 85 27 SER CB C 65.122 0.000 . 145 85 27 SER N N 113.433 0.000 . 146 86 28 ASP C C 175.859 0.000 . 147 86 28 ASP CA C 53.128 0.000 . 148 86 28 ASP CB C 40.454 0.000 . 149 87 29 SER H H 7.681 0.000 . 150 87 29 SER C C 173.604 0.043 . 151 87 29 SER CA C 56.910 0.006 . 152 87 29 SER CB C 65.365 0.298 . 153 87 29 SER N N 114.679 0.000 . 154 88 30 TRP H H 8.620 0.000 . 155 88 30 TRP HE1 H 10.023 0.000 . 156 88 30 TRP C C 176.421 0.021 . 157 88 30 TRP CA C 55.796 0.000 . 158 88 30 TRP CB C 31.358 0.137 . 159 88 30 TRP N N 125.224 0.000 . 160 88 30 TRP NE1 N 129.091 0.000 . 161 89 31 SER H H 8.946 0.000 . 162 89 31 SER C C 174.020 0.005 . 163 89 31 SER CA C 56.153 0.000 . 164 89 31 SER CB C 64.937 0.124 . 165 89 31 SER N N 113.816 0.000 . 166 90 32 PHE H H 7.963 0.000 . 167 90 32 PHE C C 174.780 0.000 . 168 90 32 PHE CA C 54.459 0.000 . 169 90 32 PHE CB C 38.940 0.000 . 170 90 32 PHE N N 118.604 0.000 . 171 91 33 PRO C C 176.109 0.000 . 172 91 33 PRO CA C 62.817 0.000 . 173 91 33 PRO CB C 31.336 0.000 . 174 92 34 ARG H H 8.261 0.000 . 175 92 34 ARG C C 173.462 0.003 . 176 92 34 ARG CA C 54.250 0.016 . 177 92 34 ARG CB C 30.309 0.097 . 178 92 34 ARG N N 120.176 0.000 . 179 93 35 GLY H H 8.820 0.000 . 180 93 35 GLY C C 171.305 0.013 . 181 93 35 GLY CA C 44.946 0.000 . 182 93 35 GLY N N 105.849 0.000 . 183 94 36 LYS H H 8.284 0.000 . 184 94 36 LYS C C 176.654 0.012 . 185 94 36 LYS CA C 55.594 0.001 . 186 94 36 LYS CB C 33.804 0.038 . 187 94 36 LYS N N 119.977 0.000 . 188 95 37 ILE H H 7.633 0.000 . 189 95 37 ILE HD1 H 0.797 0.000 . 190 95 37 ILE C C 175.834 0.000 . 191 95 37 ILE CA C 61.114 0.014 . 192 95 37 ILE CB C 39.520 0.038 . 193 95 37 ILE CD1 C 13.637 0.000 . 194 95 37 ILE N N 122.524 0.000 . 195 96 38 SER H H 9.041 0.000 . 196 96 38 SER C C 174.576 0.005 . 197 96 38 SER CA C 56.759 0.022 . 198 96 38 SER CB C 64.940 0.204 . 199 96 38 SER N N 123.944 0.000 . 200 97 39 LYS H H 8.535 0.000 . 201 97 39 LYS C C 176.243 0.031 . 202 97 39 LYS CA C 57.445 0.054 . 203 97 39 LYS CB C 31.734 0.178 . 204 97 39 LYS N N 123.111 0.000 . 205 98 40 ASP H H 8.466 0.000 . 206 98 40 ASP C C 175.055 0.027 . 207 98 40 ASP CA C 54.411 0.066 . 208 98 40 ASP CB C 40.562 0.000 . 209 98 40 ASP N N 120.024 0.000 . 210 99 41 GLU H H 7.851 0.000 . 211 99 41 GLU C C 175.315 0.002 . 212 99 41 GLU CA C 55.038 0.018 . 213 99 41 GLU CB C 31.670 0.010 . 214 99 41 GLU N N 121.321 0.000 . 215 100 42 ASN H H 8.609 0.000 . 216 100 42 ASN C C 175.784 0.000 . 217 100 42 ASN CA C 51.453 0.010 . 218 100 42 ASN CB C 39.018 0.078 . 219 100 42 ASN N N 120.070 0.000 . 220 101 43 ASP H H 8.374 0.000 . 221 101 43 ASP C C 177.735 0.000 . 222 101 43 ASP CA C 58.313 0.038 . 223 101 43 ASP CB C 41.952 0.231 . 224 101 43 ASP N N 119.195 0.000 . 225 102 44 ILE H H 7.946 0.000 . 226 102 44 ILE HD1 H 0.534 0.000 . 227 102 44 ILE C C 177.014 0.000 . 228 102 44 ILE CA C 63.534 0.069 . 229 102 44 ILE CB C 37.280 0.116 . 230 102 44 ILE CD1 C 13.254 0.000 . 231 102 44 ILE N N 119.063 0.000 . 232 103 45 ASP H H 8.021 0.000 . 233 103 45 ASP C C 179.334 0.000 . 234 103 45 ASP CA C 56.987 0.014 . 235 103 45 ASP CB C 40.035 0.014 . 236 103 45 ASP N N 121.239 0.000 . 237 104 46 CYS H H 7.935 0.000 . 238 104 46 CYS C C 174.863 0.000 . 239 104 46 CYS CA C 61.691 0.000 . 240 104 46 CYS N N 119.963 0.000 . 241 105 47 CYS H H 7.656 0.000 . 242 105 47 CYS C C 175.985 0.024 . 243 105 47 CYS CA C 62.530 0.000 . 244 105 47 CYS CB C 26.979 0.067 . 245 105 47 CYS N N 117.801 0.000 . 246 106 48 ILE H H 8.556 0.000 . 247 106 48 ILE HD1 H 0.789 0.000 . 248 106 48 ILE C C 179.360 0.049 . 249 106 48 ILE CA C 64.596 0.018 . 250 106 48 ILE CB C 30.942 0.034 . 251 106 48 ILE CD1 C 14.878 0.000 . 252 106 48 ILE N N 116.937 0.000 . 253 107 49 ARG H H 8.134 0.000 . 254 107 49 ARG C C 178.997 0.000 . 255 107 49 ARG CA C 59.448 0.100 . 256 107 49 ARG CB C 29.209 0.077 . 257 107 49 ARG N N 121.121 0.000 . 258 108 50 GLU H H 8.842 0.000 . 259 108 50 GLU C C 179.236 0.006 . 260 108 50 GLU CA C 58.611 0.014 . 261 108 50 GLU CB C 28.340 0.097 . 262 108 50 GLU N N 118.664 0.000 . 263 109 51 VAL H H 8.567 0.000 . 264 109 51 VAL HG1 H 0.912 0.000 . 265 109 51 VAL HG2 H 0.917 0.000 . 266 109 51 VAL C C 173.853 0.000 . 267 109 51 VAL CA C 67.337 0.000 . 268 109 51 VAL CB C 40.023 0.000 . 269 109 51 VAL CG1 C 22.422 0.000 . 270 109 51 VAL CG2 C 24.444 0.000 . 271 109 51 VAL N N 118.664 0.000 . 272 110 52 LYS H H 7.859 0.000 . 273 110 52 LYS C C 178.923 0.583 . 274 110 52 LYS CA C 60.228 0.044 . 275 110 52 LYS CB C 31.954 0.042 . 276 110 52 LYS N N 122.915 0.000 . 277 111 53 GLU H H 7.961 0.000 . 278 111 53 GLU C C 178.772 0.063 . 279 111 53 GLU CA C 59.117 0.025 . 280 111 53 GLU CB C 29.672 0.000 . 281 111 53 GLU N N 118.066 0.000 . 282 112 54 GLU H H 8.218 0.000 . 283 112 54 GLU C C 176.701 0.010 . 284 112 54 GLU CA C 59.581 0.035 . 285 112 54 GLU CB C 30.441 0.003 . 286 112 54 GLU N N 117.012 0.000 . 287 113 55 ILE H H 8.245 0.000 . 288 113 55 ILE HD1 H 0.324 0.000 . 289 113 55 ILE C C 177.224 0.058 . 290 113 55 ILE CA C 59.253 0.013 . 291 113 55 ILE CB C 39.812 0.208 . 292 113 55 ILE CD1 C 14.228 0.000 . 293 113 55 ILE N N 104.252 0.000 . 294 114 56 GLY H H 8.195 0.000 . 295 114 56 GLY C C 173.677 0.032 . 296 114 56 GLY CA C 46.632 0.056 . 297 114 56 GLY N N 111.479 0.000 . 298 115 57 PHE H H 6.870 0.000 . 299 115 57 PHE C C 172.960 0.027 . 300 115 57 PHE CA C 56.060 0.033 . 301 115 57 PHE CB C 44.213 0.014 . 302 115 57 PHE N N 119.893 0.000 . 303 116 58 ASP H H 7.778 0.000 . 304 116 58 ASP C C 176.104 0.013 . 305 116 58 ASP CA C 52.153 0.078 . 306 116 58 ASP CB C 41.578 0.077 . 307 116 58 ASP N N 127.497 0.000 . 308 117 59 LEU H H 9.419 0.000 . 309 117 59 LEU HD1 H 0.696 0.000 . 310 117 59 LEU HD2 H 0.693 0.000 . 311 117 59 LEU C C 177.448 0.008 . 312 117 59 LEU CA C 54.590 0.001 . 313 117 59 LEU CB C 43.197 0.078 . 314 117 59 LEU CD1 C 27.172 0.000 . 315 117 59 LEU CD2 C 23.108 0.000 . 316 117 59 LEU N N 126.368 0.000 . 317 118 60 THR H H 8.888 0.000 . 318 118 60 THR C C 175.620 0.000 . 319 118 60 THR CA C 69.215 0.068 . 320 118 60 THR CB C 67.763 0.125 . 321 118 60 THR N N 122.253 0.000 . 322 119 61 ASP H H 9.349 0.000 . 323 119 61 ASP C C 175.439 0.005 . 324 119 61 ASP CA C 55.384 0.018 . 325 119 61 ASP CB C 40.304 0.000 . 326 119 61 ASP N N 118.375 0.000 . 327 120 62 TYR H H 8.320 0.000 . 328 120 62 TYR C C 175.973 0.011 . 329 120 62 TYR CA C 58.680 0.000 . 330 120 62 TYR CB C 41.616 0.039 . 331 120 62 TYR N N 117.581 0.000 . 332 121 63 ILE H H 7.486 0.000 . 333 121 63 ILE HD1 H 0.236 0.000 . 334 121 63 ILE C C 172.930 0.013 . 335 121 63 ILE CA C 61.921 0.002 . 336 121 63 ILE CB C 40.093 0.098 . 337 121 63 ILE CD1 C 14.901 0.000 . 338 121 63 ILE N N 120.875 0.000 . 339 122 64 ASP H H 9.414 0.000 . 340 122 64 ASP C C 177.121 0.045 . 341 122 64 ASP CA C 52.655 0.066 . 342 122 64 ASP CB C 43.810 0.073 . 343 122 64 ASP N N 128.361 0.000 . 344 123 65 ASP H H 8.993 0.000 . 345 123 65 ASP C C 176.087 0.008 . 346 123 65 ASP CA C 55.827 0.052 . 347 123 65 ASP CB C 40.794 0.155 . 348 123 65 ASP N N 125.638 0.000 . 349 124 66 ASN H H 8.898 0.000 . 350 124 66 ASN C C 175.900 0.008 . 351 124 66 ASN CA C 52.904 0.045 . 352 124 66 ASN CB C 41.588 0.053 . 353 124 66 ASN N N 114.311 0.000 . 354 125 67 GLN H H 8.182 0.000 . 355 125 67 GLN C C 173.382 0.017 . 356 125 67 GLN CA C 54.020 0.000 . 357 125 67 GLN CB C 29.034 0.022 . 358 125 67 GLN N N 120.708 0.000 . 359 126 68 PHE H H 7.406 0.000 . 360 126 68 PHE C C 172.904 0.005 . 361 126 68 PHE CA C 55.217 0.053 . 362 126 68 PHE CB C 40.130 0.046 . 363 126 68 PHE N N 119.903 0.000 . 364 127 69 ILE H H 8.814 0.000 . 365 127 69 ILE HD1 H 0.630 0.000 . 366 127 69 ILE C C 174.056 0.025 . 367 127 69 ILE CA C 60.092 0.030 . 368 127 69 ILE CB C 40.948 0.077 . 369 127 69 ILE CD1 C 14.721 0.000 . 370 127 69 ILE N N 120.324 0.000 . 371 128 70 GLU H H 9.021 0.000 . 372 128 70 GLU C C 176.479 0.016 . 373 128 70 GLU CA C 53.389 0.022 . 374 128 70 GLU CB C 32.774 0.142 . 375 128 70 GLU N N 129.746 0.000 . 376 129 71 ARG H H 9.032 0.000 . 377 129 71 ARG C C 173.796 0.014 . 378 129 71 ARG CA C 53.264 0.111 . 379 129 71 ARG CB C 35.593 0.025 . 380 129 71 ARG N N 125.682 0.000 . 381 130 72 ASN H H 8.858 0.000 . 382 130 72 ASN C C 175.257 0.006 . 383 130 72 ASN CA C 52.117 0.000 . 384 130 72 ASN CB C 39.713 0.000 . 385 130 72 ASN N N 123.329 0.000 . 386 131 73 ILE H H 9.128 0.000 . 387 131 73 ILE HD1 H 0.518 0.000 . 388 131 73 ILE C C 175.884 0.045 . 389 131 73 ILE CA C 60.280 0.021 . 390 131 73 ILE CB C 40.447 0.038 . 391 131 73 ILE CD1 C 13.117 0.000 . 392 131 73 ILE N N 126.103 0.000 . 393 132 74 GLN H H 7.845 0.000 . 394 132 74 GLN C C 175.861 0.034 . 395 132 74 GLN CA C 56.068 0.000 . 396 132 74 GLN CB C 26.939 0.262 . 397 132 74 GLN N N 124.065 0.000 . 398 133 75 GLY H H 8.508 0.000 . 399 133 75 GLY C C 173.886 0.016 . 400 133 75 GLY CA C 45.235 0.012 . 401 133 75 GLY N N 105.182 0.000 . 402 134 76 LYS H H 7.866 0.000 . 403 134 76 LYS C C 173.658 0.010 . 404 134 76 LYS CA C 54.568 0.000 . 405 134 76 LYS CB C 34.476 0.000 . 406 134 76 LYS N N 122.580 0.000 . 407 135 77 ASN H H 8.441 0.000 . 408 135 77 ASN C C 173.079 0.020 . 409 135 77 ASN CA C 53.335 0.076 . 410 135 77 ASN CB C 42.108 0.000 . 411 135 77 ASN N N 123.512 0.000 . 412 136 78 TYR H H 8.899 0.000 . 413 136 78 TYR C C 174.762 0.017 . 414 136 78 TYR CA C 56.713 0.004 . 415 136 78 TYR CB C 40.942 0.006 . 416 136 78 TYR N N 124.176 0.000 . 417 137 79 LYS H H 8.068 0.000 . 418 137 79 LYS C C 173.365 0.000 . 419 137 79 LYS CA C 55.461 0.047 . 420 137 79 LYS CB C 34.878 0.000 . 421 137 79 LYS N N 122.516 0.000 . 422 138 80 ILE H H 8.884 0.000 . 423 138 80 ILE HD1 H 0.252 0.000 . 424 138 80 ILE C C 175.545 0.008 . 425 138 80 ILE CA C 55.095 0.039 . 426 138 80 ILE CB C 36.490 0.000 . 427 138 80 ILE CD1 C 7.689 0.000 . 428 138 80 ILE N N 127.232 0.000 . 429 139 81 PHE H H 9.144 0.000 . 430 139 81 PHE C C 174.748 0.000 . 431 139 81 PHE CA C 59.178 0.056 . 432 139 81 PHE CB C 38.863 0.000 . 433 139 81 PHE N N 127.497 0.000 . 434 140 82 LEU H H 7.828 0.000 . 435 140 82 LEU HD1 H -0.383 0.000 . 436 140 82 LEU HD2 H 0.084 0.000 . 437 140 82 LEU C C 175.877 0.016 . 438 140 82 LEU CA C 54.192 0.047 . 439 140 82 LEU CB C 40.283 0.030 . 440 140 82 LEU CD1 C 23.201 0.000 . 441 140 82 LEU CD2 C 22.988 0.000 . 442 140 82 LEU N N 124.376 0.000 . 443 141 83 ILE H H 9.075 0.000 . 444 141 83 ILE HD1 H 0.730 0.000 . 445 141 83 ILE C C 174.551 0.062 . 446 141 83 ILE CA C 58.300 0.025 . 447 141 83 ILE CB C 39.736 0.179 . 448 141 83 ILE CD1 C 12.716 0.000 . 449 141 83 ILE N N 128.228 0.000 . 450 142 84 SER H H 9.134 0.000 . 451 142 84 SER C C 173.878 0.008 . 452 142 84 SER CA C 56.974 0.022 . 453 142 84 SER CB C 67.295 0.074 . 454 142 84 SER N N 120.657 0.000 . 455 143 85 GLY H H 6.916 0.000 . 456 143 85 GLY C C 174.117 0.003 . 457 143 85 GLY CA C 45.782 0.000 . 458 143 85 GLY N N 104.149 0.000 . 459 144 86 VAL H H 7.880 0.000 . 460 144 86 VAL HG1 H 0.338 0.000 . 461 144 86 VAL HG2 H 0.191 0.000 . 462 144 86 VAL C C 174.615 0.019 . 463 144 86 VAL CA C 62.835 0.018 . 464 144 86 VAL CB C 31.653 0.000 . 465 144 86 VAL CG1 C 20.318 0.000 . 466 144 86 VAL CG2 C 23.228 0.000 . 467 144 86 VAL N N 123.821 0.000 . 468 145 87 SER H H 7.878 0.000 . 469 145 87 SER C C 176.087 0.008 . 470 145 87 SER CA C 57.708 0.029 . 471 145 87 SER CB C 64.243 0.076 . 472 145 87 SER N N 119.304 0.000 . 473 146 88 GLU H H 8.671 0.000 . 474 146 88 GLU C C 177.962 0.001 . 475 146 88 GLU CA C 57.135 0.040 . 476 146 88 GLU CB C 30.165 0.048 . 477 146 88 GLU N N 125.872 0.000 . 478 147 89 VAL H H 7.834 0.000 . 479 147 89 VAL HG1 H 0.820 0.000 . 480 147 89 VAL HG2 H 0.745 0.000 . 481 147 89 VAL C C 175.997 0.000 . 482 147 89 VAL CA C 60.852 0.010 . 483 147 89 VAL CB C 30.695 0.019 . 484 147 89 VAL CG1 C 21.054 0.000 . 485 147 89 VAL CG2 C 19.104 0.000 . 486 147 89 VAL N N 114.157 0.000 . 487 148 90 PHE H H 7.150 0.000 . 488 148 90 PHE C C 174.129 0.049 . 489 148 90 PHE CA C 58.558 0.069 . 490 148 90 PHE CB C 39.269 0.135 . 491 148 90 PHE N N 124.523 0.000 . 492 149 91 ASN H H 7.472 0.000 . 493 149 91 ASN C C 173.205 0.027 . 494 149 91 ASN CA C 51.328 0.044 . 495 149 91 ASN CB C 37.445 0.127 . 496 149 91 ASN N N 124.997 0.000 . 497 150 92 PHE H H 7.802 0.000 . 498 150 92 PHE C C 175.671 0.008 . 499 150 92 PHE CA C 59.254 0.022 . 500 150 92 PHE CB C 39.625 0.088 . 501 150 92 PHE N N 124.973 0.000 . 502 151 93 LYS H H 7.925 0.000 . 503 151 93 LYS C C 172.709 0.000 . 504 151 93 LYS CA C 53.583 0.000 . 505 151 93 LYS CB C 34.384 0.000 . 506 151 93 LYS N N 123.778 0.000 . 507 152 94 PRO C C 177.893 0.000 . 508 152 94 PRO CA C 62.333 0.000 . 509 152 94 PRO CB C 31.912 0.000 . 510 153 95 GLN H H 8.553 0.000 . 511 153 95 GLN C C 176.496 0.001 . 512 153 95 GLN CA C 55.791 0.016 . 513 153 95 GLN CB C 29.466 0.052 . 514 153 95 GLN N N 120.657 0.000 . 515 154 96 VAL H H 7.750 0.000 . 516 154 96 VAL HG1 H 0.901 0.000 . 517 154 96 VAL HG2 H 0.869 0.000 . 518 154 96 VAL C C 175.870 0.024 . 519 154 96 VAL CA C 60.469 0.023 . 520 154 96 VAL CB C 33.150 0.000 . 521 154 96 VAL CG1 C 21.256 0.000 . 522 154 96 VAL CG2 C 19.689 0.000 . 523 154 96 VAL N N 116.871 0.000 . 524 155 97 ARG H H 8.416 0.000 . 525 155 97 ARG C C 176.154 0.000 . 526 155 97 ARG CA C 56.049 0.028 . 527 155 97 ARG CB C 30.212 0.076 . 528 155 97 ARG N N 123.180 0.000 . 529 156 98 ASN H H 8.501 0.000 . 530 156 98 ASN C C 174.637 0.007 . 531 156 98 ASN CA C 53.703 0.028 . 532 156 98 ASN CB C 38.556 0.000 . 533 156 98 ASN N N 119.129 0.000 . 534 157 99 GLU H H 8.473 0.000 . 535 157 99 GLU C C 176.323 0.000 . 536 157 99 GLU CA C 56.933 0.014 . 537 157 99 GLU CB C 30.528 0.000 . 538 157 99 GLU N N 118.664 0.000 . 539 158 100 ILE H H 8.199 0.000 . 540 158 100 ILE HD1 H 0.635 0.000 . 541 158 100 ILE C C 174.885 0.000 . 542 158 100 ILE CA C 58.819 0.079 . 543 158 100 ILE CB C 37.768 0.035 . 544 158 100 ILE CD1 C 9.537 0.000 . 545 158 100 ILE N N 121.770 0.000 . 546 159 101 ASP H H 8.792 0.000 . 547 159 101 ASP C C 176.164 0.000 . 548 159 101 ASP CA C 54.621 0.003 . 549 159 101 ASP CB C 43.928 0.115 . 550 159 101 ASP N N 126.577 0.000 . 551 160 102 LYS H H 7.713 0.000 . 552 160 102 LYS C C 174.433 0.019 . 553 160 102 LYS CA C 55.010 0.072 . 554 160 102 LYS CB C 37.732 0.028 . 555 160 102 LYS N N 116.539 0.000 . 556 161 103 ILE H H 8.305 0.000 . 557 161 103 ILE HD1 H 0.858 0.000 . 558 161 103 ILE C C 175.381 0.015 . 559 161 103 ILE CA C 60.827 0.013 . 560 161 103 ILE CB C 42.298 0.038 . 561 161 103 ILE CD1 C 14.795 0.000 . 562 161 103 ILE N N 122.715 0.000 . 563 162 104 GLU H H 9.096 0.000 . 564 162 104 GLU C C 174.084 0.030 . 565 162 104 GLU CA C 54.825 0.055 . 566 162 104 GLU CB C 35.001 0.058 . 567 162 104 GLU N N 126.793 0.000 . 568 163 105 TRP H H 8.604 0.000 . 569 163 105 TRP HE1 H 10.030 0.000 . 570 163 105 TRP C C 177.262 0.044 . 571 163 105 TRP CA C 55.944 0.009 . 572 163 105 TRP CB C 31.491 0.000 . 573 163 105 TRP N N 122.626 0.000 . 574 163 105 TRP NE1 N 128.892 0.000 . 575 164 106 PHE H H 9.971 0.000 . 576 164 106 PHE C C 175.831 0.014 . 577 164 106 PHE CA C 56.270 0.034 . 578 164 106 PHE CB C 42.129 0.023 . 579 164 106 PHE N N 124.308 0.000 . 580 165 107 ASP H H 8.864 0.000 . 581 165 107 ASP C C 176.696 0.020 . 582 165 107 ASP CA C 54.554 0.001 . 583 165 107 ASP CB C 41.586 0.020 . 584 165 107 ASP N N 123.567 0.000 . 585 166 108 PHE H H 8.871 0.000 . 586 166 108 PHE C C 177.094 0.028 . 587 166 108 PHE CA C 62.100 0.037 . 588 166 108 PHE CB C 40.145 0.031 . 589 166 108 PHE N N 131.315 0.000 . 590 167 109 LYS H H 8.778 0.000 . 591 167 109 LYS C C 179.354 0.003 . 592 167 109 LYS CA C 58.883 0.055 . 593 167 109 LYS CB C 31.083 0.000 . 594 167 109 LYS N N 120.524 0.000 . 595 168 110 LYS H H 8.132 0.000 . 596 168 110 LYS C C 180.093 0.052 . 597 168 110 LYS CA C 58.591 0.077 . 598 168 110 LYS CB C 32.067 0.078 . 599 168 110 LYS N N 120.192 0.000 . 600 169 111 ILE H H 7.759 0.000 . 601 169 111 ILE HD1 H 0.308 0.000 . 602 169 111 ILE C C 177.681 0.029 . 603 169 111 ILE CA C 64.734 0.085 . 604 169 111 ILE CB C 36.716 0.010 . 605 169 111 ILE CD1 C 13.743 0.000 . 606 169 111 ILE N N 120.258 0.000 . 607 170 112 SER H H 7.535 0.000 . 608 170 112 SER C C 176.079 0.033 . 609 170 112 SER CA C 60.827 0.022 . 610 170 112 SER CB C 63.118 0.000 . 611 170 112 SER N N 114.480 0.000 . 612 171 113 LYS H H 7.533 0.000 . 613 171 113 LYS C C 178.283 0.000 . 614 171 113 LYS CA C 57.184 0.000 . 615 171 113 LYS CB C 32.773 0.000 . 616 171 113 LYS N N 119.395 0.000 . 617 172 114 THR H H 8.365 0.000 . 618 172 114 THR C C 175.950 0.000 . 619 172 114 THR CA C 53.549 0.000 . 620 172 114 THR CB C 64.38 3.482 . 621 172 114 THR N N 118.582 0.000 . 622 173 115 MET H H 7.855 0.000 . 623 173 115 MET C C 176.421 0.013 . 624 173 115 MET CA C 57.772 0.047 . 625 173 115 MET CB C 32.187 0.120 . 626 173 115 MET N N 123.180 0.000 . 627 174 116 TYR H H 8.135 0.000 . 628 174 116 TYR C C 176.077 0.017 . 629 174 116 TYR CA C 57.943 0.097 . 630 174 116 TYR CB C 38.008 0.115 . 631 174 116 TYR N N 118.105 0.000 . 632 175 117 LYS H H 7.968 0.000 . 633 175 117 LYS C C 176.103 0.007 . 634 175 117 LYS CA C 55.666 0.035 . 635 175 117 LYS CB C 32.074 0.244 . 636 175 117 LYS N N 120.922 0.000 . 637 176 118 SER H H 8.020 0.000 . 638 176 118 SER C C 176.045 0.000 . 639 176 118 SER CA C 57.635 0.000 . 640 176 118 SER CB C 64.838 0.000 . 641 176 118 SER N N 115.476 0.000 . 642 177 119 ASN C C 174.585 0.000 . 643 177 119 ASN CA C 56.870 0.000 . 644 177 119 ASN CB C 40.623 0.000 . 645 178 120 ILE H H 8.190 0.000 . 646 178 120 ILE HD1 H 0.694 0.000 . 647 178 120 ILE C C 174.883 0.000 . 648 178 120 ILE CA C 60.488 0.007 . 649 178 120 ILE CB C 38.496 0.077 . 650 178 120 ILE CD1 C 12.253 0.000 . 651 178 120 ILE N N 121.254 0.000 . 652 179 121 LYS H H 8.468 0.000 . 653 179 121 LYS C C 174.760 0.075 . 654 179 121 LYS CA C 54.966 0.008 . 655 179 121 LYS CB C 33.257 0.028 . 656 179 121 LYS N N 126.985 0.000 . 657 180 122 TYR H H 8.305 0.000 . 658 180 122 TYR C C 176.749 0.000 . 659 180 122 TYR CA C 56.082 0.000 . 660 180 122 TYR N N 121.121 0.000 . 661 182 124 LEU HD1 H 0.252 0.000 . 662 182 124 LEU HD2 H -0.214 0.000 . 663 182 124 LEU C C 175.194 0.000 . 664 182 124 LEU CA C 61.963 0.000 . 665 182 124 LEU CD1 C 24.351 0.000 . 666 182 124 LEU CD2 C 21.885 0.000 . 667 183 125 ILE H H 7.837 0.000 . 668 183 125 ILE HD1 H 0.483 0.000 . 669 183 125 ILE C C 175.010 0.000 . 670 183 125 ILE CA C 57.793 0.000 . 671 183 125 ILE CB C 37.809 0.000 . 672 183 125 ILE CD1 C 14.294 0.000 . 673 183 125 ILE N N 122.118 0.000 . 674 184 126 ASN C C 176.857 0.000 . 675 184 126 ASN CA C 55.700 0.000 . 676 185 127 SER H H 7.568 0.000 . 677 185 127 SER C C 176.857 0.000 . 678 185 127 SER CA C 59.748 0.021 . 679 185 127 SER N N 116.192 0.000 . 680 186 128 MET H H 7.651 0.000 . 681 186 128 MET C C 175.966 0.033 . 682 186 128 MET CA C 54.76 0.000 . 683 186 128 MET CB C 31.012 0.144 . 684 186 128 MET N N 118.531 0.000 . 685 187 129 MET H H 7.483 0.000 . 686 187 129 MET C C 176.616 2.031 . 687 187 129 MET CA C 57.541 0.037 . 688 187 129 MET N N 121.562 0.000 . 689 188 130 ARG H H 9.199 0.000 . 690 188 130 ARG C C 176.200 0.000 . 691 188 130 ARG CA C 60.769 0.000 . 692 188 130 ARG N N 120.747 0.000 . 693 189 131 PRO C C 179.110 0.000 . 694 189 131 PRO CA C 65.106 0.000 . 695 189 131 PRO CB C 29.414 0.000 . 696 190 132 LEU H H 8.040 0.000 . 697 190 132 LEU HD1 H 0.985 0.000 . 698 190 132 LEU HD2 H 0.854 0.000 . 699 190 132 LEU C C 177.867 0.001 . 700 190 132 LEU CA C 58.255 0.017 . 701 190 132 LEU CB C 42.582 0.000 . 702 190 132 LEU CD1 C 25.817 0.000 . 703 190 132 LEU CD2 C 25.087 0.000 . 704 190 132 LEU N N 120.917 0.000 . 705 191 133 SER H H 8.693 0.000 . 706 191 133 SER C C 174.880 0.008 . 707 191 133 SER CA C 61.952 0.000 . 708 191 133 SER CB C 64.311 0.079 . 709 191 133 SER N N 115.476 0.000 . 710 192 134 MET H H 8.238 0.000 . 711 192 134 MET C C 178.449 0.017 . 712 192 134 MET CA C 57.972 0.016 . 713 192 134 MET CB C 27.78 0.035 . 714 192 134 MET N N 121.770 0.000 . 715 193 135 TRP H H 8.077 0.000 . 716 193 135 TRP HE1 H 10.098 0.000 . 717 193 135 TRP C C 178.588 0.000 . 718 193 135 TRP CA C 61.756 0.011 . 719 193 135 TRP CB C 28.295 0.013 . 720 193 135 TRP N N 123.247 0.000 . 721 193 135 TRP NE1 N 130.951 0.000 . 722 194 136 LEU H H 8.420 0.000 . 723 194 136 LEU HD1 H 0.033 0.000 . 724 194 136 LEU HD2 H 0.052 0.000 . 725 194 136 LEU C C 178.981 0.000 . 726 194 136 LEU CA C 57.351 0.005 . 727 194 136 LEU CB C 41.936 0.017 . 728 194 136 LEU CD1 C 24.462 0.000 . 729 194 136 LEU CD2 C 24.037 0.000 . 730 194 136 LEU N N 120.590 0.000 . 731 195 137 ARG H H 7.793 0.000 . 732 195 137 ARG C C 178.834 0.000 . 733 195 137 ARG CA C 58.856 0.009 . 734 195 137 ARG CB C 29.840 0.000 . 735 195 137 ARG N N 118.199 0.000 . 736 196 138 HIS H H 7.565 0.000 . 737 196 138 HIS C C 177.089 0.066 . 738 196 138 HIS CA C 58.174 0.028 . 739 196 138 HIS CB C 29.169 0.058 . 740 196 138 HIS N N 119.262 0.000 . 741 197 139 GLN H H 8.049 0.000 . 742 197 139 GLN C C 175.976 0.000 . 743 197 139 GLN CA C 56.592 0.038 . 744 197 139 GLN CB C 27.742 0.126 . 745 197 139 GLN N N 118.313 0.000 . 746 198 140 ARG H H 7.990 0.000 . 747 198 140 ARG C C 177.866 0.000 . 748 198 140 ARG CA C 57.960 0.029 . 749 198 140 ARG CB C 29.742 0.009 . 750 198 140 ARG N N 118.704 0.000 . 751 199 141 GLN H H 7.621 0.000 . 752 199 141 GLN C C 177.473 0.000 . 753 199 141 GLN CA C 57.153 0.049 . 754 199 141 GLN CB C 28.441 0.000 . 755 199 141 GLN N N 119.528 0.000 . 756 200 142 ILE H H 7.677 0.000 . 757 200 142 ILE HD1 H 0.555 0.000 . 758 200 142 ILE C C 177.719 0.000 . 759 200 142 ILE CA C 62.422 0.072 . 760 200 142 ILE CB C 37.423 0.169 . 761 200 142 ILE CD1 C 12.658 0.000 . 762 200 142 ILE N N 119.395 0.000 . 763 201 143 LYS H H 7.816 0.000 . 764 201 143 LYS C C 177.168 0.022 . 765 201 143 LYS CA C 56.519 0.000 . 766 201 143 LYS CB C 32.030 0.003 . 767 201 143 LYS N N 122.583 0.000 . 768 202 144 ASN H H 8.058 0.000 . 769 202 144 ASN C C 178.237 0.000 . 770 202 144 ASN CA C 55.783 0.000 . 771 202 144 ASN CB C 38.920 0.000 . 772 202 144 ASN N N 119.068 0.000 . 773 204 146 ASP C C 176.716 0.000 . 774 204 146 ASP CA C 54.378 0.000 . 775 204 146 ASP CB C 40.948 0.000 . stop_ save_