data_4028 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal: Chemical Shifts for the Protein-RNA Complex ; _BMRB_accession_number 4028 _BMRB_flat_file_name bmr4028.str _Entry_type update _Submission_date 1997-03-15 _Accession_date 1997-03-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Andrew L . 2 Volkman Brian F . 3 Robertson Stephanie A . 4 Rudner David Z . 5 Barbash Daniel A . 6 Cline Thomas W . 7 Kanaar Roland . . 8 Rio Donald C . 9 Wemmer David E . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 261 "13C chemical shifts" 308 "15N chemical shifts" 149 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-22 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ loop_ _Related_BMRB_accession_number _Relationship 4029 'chemical shifts for the free Sex-Lethal protein' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Lee, A.L., Volkman, B.F., Rudner, D.Z., Barbash, D.A., Cline, T.W, Kanaar, R., Rio D.C., and Wemmer, D.E., "Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal," Biochemistry 36, 14306-14317 (1997). ; _Citation_title ; Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal ; _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98062897 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Andrew L . 2 Volkman Brian F . 3 Robertson Stephanie A . 4 Rudner David Z . 5 Barbash Daniel A . 6 Cline Thomas W . 7 Kanaar Roland . . 8 Rio Donald C . 9 Wemmer David E . stop_ _Journal_abbreviation Biochemistry _Journal_volume 36 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14306 _Page_last 14317 _Year 1997 _Details . loop_ _Keyword 'ALTERNATIVE SPLICING' RNA-BINDING 'SEXUAL DIFFERENTIATION' stop_ save_ ################################## # Molecular system description # ################################## save_system_Sxl-RBD1+2 _Saveframe_category molecular_system _Mol_system_name 'Sex-lethal protein' _Abbreviation_common Sxl-RBD1+2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Sex-lethal protein' $Sxl-RBD1+2 RNA $RNA stop_ _System_molecular_weight 20744 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sxl-RBD1+2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sex-lethal protein' _Abbreviation_common Sxl-RBD1+2 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 184 _Mol_residue_sequence ; MGSDDLMNDPRASNTNLIVN YLPQDMTDRELYALFRAIGP INTCRIMRDYKTGYSFGYAF VDFTSEMDSQRAIKVLNGIT VRNKRLKVSYARPGGESIKD TNLYVTNLPRTITDDQLDTI FGKYGSIVQKNILRDKLTGR PRGVAFVRYNKREEAQEAIS ALNNVIPEGGSQPLSVRLAE EHGK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 ASP 5 ASP 6 LEU 7 MET 8 ASN 9 ASP 10 PRO 11 ARG 12 ALA 13 SER 14 ASN 15 THR 16 ASN 17 LEU 18 ILE 19 VAL 20 ASN 21 TYR 22 LEU 23 PRO 24 GLN 25 ASP 26 MET 27 THR 28 ASP 29 ARG 30 GLU 31 LEU 32 TYR 33 ALA 34 LEU 35 PHE 36 ARG 37 ALA 38 ILE 39 GLY 40 PRO 41 ILE 42 ASN 43 THR 44 CYS 45 ARG 46 ILE 47 MET 48 ARG 49 ASP 50 TYR 51 LYS 52 THR 53 GLY 54 TYR 55 SER 56 PHE 57 GLY 58 TYR 59 ALA 60 PHE 61 VAL 62 ASP 63 PHE 64 THR 65 SER 66 GLU 67 MET 68 ASP 69 SER 70 GLN 71 ARG 72 ALA 73 ILE 74 LYS 75 VAL 76 LEU 77 ASN 78 GLY 79 ILE 80 THR 81 VAL 82 ARG 83 ASN 84 LYS 85 ARG 86 LEU 87 LYS 88 VAL 89 SER 90 TYR 91 ALA 92 ARG 93 PRO 94 GLY 95 GLY 96 GLU 97 SER 98 ILE 99 LYS 100 ASP 101 THR 102 ASN 103 LEU 104 TYR 105 VAL 106 THR 107 ASN 108 LEU 109 PRO 110 ARG 111 THR 112 ILE 113 THR 114 ASP 115 ASP 116 GLN 117 LEU 118 ASP 119 THR 120 ILE 121 PHE 122 GLY 123 LYS 124 TYR 125 GLY 126 SER 127 ILE 128 VAL 129 GLN 130 LYS 131 ASN 132 ILE 133 LEU 134 ARG 135 ASP 136 LYS 137 LEU 138 THR 139 GLY 140 ARG 141 PRO 142 ARG 143 GLY 144 VAL 145 ALA 146 PHE 147 VAL 148 ARG 149 TYR 150 ASN 151 LYS 152 ARG 153 GLU 154 GLU 155 ALA 156 GLN 157 GLU 158 ALA 159 ILE 160 SER 161 ALA 162 LEU 163 ASN 164 ASN 165 VAL 166 ILE 167 PRO 168 GLU 169 GLY 170 GLY 171 SER 172 GLN 173 PRO 174 LEU 175 SER 176 VAL 177 ARG 178 LEU 179 ALA 180 GLU 181 GLU 182 HIS 183 GLY 184 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4029 "Sex-lethal protein" 100.00 184 100.00 100.00 4.37e-131 PDB 1B7F "Sxl-Lethal ProteinRNA COMPLEX" 91.30 168 99.40 100.00 5.78e-117 PDB 3SXL "Sex-Lethal Rna Recognition Domains 1 And 2 From Drosophila Melanogaster" 98.91 184 98.35 98.35 2.89e-126 GB AAA28884 "sex-linked protein [Drosophila melanogaster]" 99.46 354 100.00 100.00 6.22e-128 GB AAA28921 "putative [Drosophila melanogaster]" 99.46 366 100.00 100.00 2.58e-127 GB AAA28922 "Sx1 [Drosophila melanogaster]" 99.46 354 100.00 100.00 6.22e-128 GB AAF46240 "Sex lethal, isoform H [Drosophila melanogaster]" 99.46 366 100.00 100.00 2.42e-127 GB AAF46241 "Sex lethal, isoform W [Drosophila melanogaster]" 99.46 344 100.00 100.00 1.10e-127 PIR B39725 "sex-lethal sex determination protein MS11 - fruit fly (Drosophila melanogaster)" 99.46 366 100.00 100.00 2.58e-127 REF NP_001027062 "Sex lethal, isoform O [Drosophila melanogaster]" 99.46 364 100.00 100.00 1.56e-127 REF NP_001027063 "Sex lethal, isoform N [Drosophila melanogaster]" 99.46 344 100.00 100.00 2.73e-128 REF NP_001027065 "Sex lethal, isoform L [Drosophila melanogaster]" 99.46 354 100.00 100.00 6.22e-128 REF NP_001162686 "Sex lethal, isoform P [Drosophila melanogaster]" 99.46 352 100.00 100.00 1.04e-127 REF NP_001162688 "Sex lethal, isoform R [Drosophila melanogaster]" 99.46 342 100.00 100.00 6.73e-128 SP P19339 "RecName: Full=Protein sex-lethal" 99.46 354 100.00 100.00 6.22e-128 stop_ save_ save_RNA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class RNA _Name_common 'polypyrimidine tract 10-mer RNA' _Abbreviation_common 'Tra-PPT RNA' _Molecular_mass . _Mol_thiol_state . _Details ; 10-mer RNA from transformer (Tra) pre-mRNA polypyrimidine tract (PPT) ; _Residue_count 10 _Mol_residue_sequence GUUUUUUUUC loop_ _Residue_seq_code _Residue_label 1 G 2 U 3 U 4 U 5 U 6 U 7 U 8 U 9 U 10 C stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sxl-RBD1+2 fruitfly 7215 Eukaryota Metazoa Drosophila melanogaster $RNA fruitfly 7215 Eukaryota Metazoa Drosophila melanogaster stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $Sxl-RBD1+2 'recombinant technology' 'E. coli' . . BL21(DE3)pLysS plasmid pET-3b 'natural source' $RNA 'chemical synthesis' . . . . . . '. ( RNA synthesized on ABI 391 RNA synthesizer)' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sxl-RBD1+2 . mM 0.5 1.0 '[U-95% 13C; U-95% 15N]' $RNA . mM 0.5 1.0 . H2O 90 % . . . D2O 10 % . . . NaCl 30 mM . . . NaN3 0.02 % . . . 'sodium phosphate buffer' 30 mM . . . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_one loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $RNA 95 percent HPLC $Sxl-RBD1+2 95 percent 'SDS gel electrophoresis' stop_ save_ ############################ # Computer software used # ############################ save_software_uxnmr _Saveframe_category software _Name xwinnmr _Version 1.1 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'NMR data acquisition' stop_ _Details . save_ save_software_felix _Saveframe_category software _Name FELIX _Version 2.30 loop_ _Vendor _Address _Electronic_address biosym . . stop_ loop_ _Task 'fourier transformation' 'peak picking' 'strip plotting' visualization stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_condition_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.30 0.02 na temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.2514495192 DSS H 1 'methyl protons' ppm 0 external direct . . . 1.0 'liquid ammonia' N 15 nitrogen ppm 0 external indirect . . . 0.1013290513 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details 'backbone 1H, 15N and 13C resonance assignments of Sxl-RNA complex' loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name 'Sex-lethal protein' _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 . 4 ASP H H 8.61 0.015 1 2 . 4 ASP HA H 4.64 0.015 1 3 . 4 ASP C C 174.61 0.15 1 4 . 4 ASP CA C 54.5 0.15 1 5 . 4 ASP N N 121.58 0.2 1 6 . 5 ASP H H 8.12 0.015 1 7 . 5 ASP HA H 4.54 0.015 1 8 . 5 ASP C C 175.97 0.15 1 9 . 5 ASP CA C 54.7 0.15 1 10 . 5 ASP N N 120.06 0.2 1 11 . 6 LEU H H 8.2 0.015 1 12 . 6 LEU HA H 4.29 0.015 1 13 . 6 LEU C C 176.35 0.15 1 14 . 6 LEU CA C 55.5 0.15 1 15 . 6 LEU N N 121.85 0.2 1 16 . 7 MET H H 8.29 0.015 1 17 . 7 MET HA H 4.43 0.015 1 18 . 7 MET C C 175.89 0.15 1 19 . 7 MET CA C 55.6 0.15 1 20 . 7 MET N N 119.78 0.2 1 21 . 8 ASN H H 8.28 0.015 1 22 . 8 ASN HA H 4.68 0.015 1 23 . 8 ASN C C 174.29 0.15 1 24 . 8 ASN CA C 53.1 0.15 1 25 . 8 ASN N N 119.26 0.2 1 26 . 9 ASP H H 8.28 0.015 1 27 . 9 ASP CA C 52.1 0.15 1 28 . 9 ASP N N 122.38 0.2 1 29 . 10 PRO HA H 4.43 0.015 1 30 . 10 PRO C C 177.05 0.15 1 31 . 10 PRO CA C 63.5 0.15 1 32 . 11 ARG H H 8.44 0.015 1 33 . 11 ARG HA H 4.27 0.015 1 34 . 11 ARG C C 176.05 0.15 1 35 . 11 ARG CA C 56.00 0.15 1 36 . 11 ARG N N 120.06 0.2 1 37 . 12 ALA H H 8.14 0.015 1 38 . 12 ALA HA H 4.31 0.015 1 39 . 12 ALA C C 177.16 0.15 1 40 . 12 ALA CA C 52.4 0.15 1 41 . 12 ALA N N 124.42 0.2 1 42 . 13 SER H H 8.28 0.015 1 43 . 13 SER HA H 4.29 0.015 1 44 . 13 SER C C 173.99 0.15 1 45 . 13 SER CA C 57.8 0.15 1 46 . 13 SER N N 114.74 0.2 1 47 . 14 ASN H H 8.51 0.015 1 48 . 14 ASN C C 175.07 0.15 1 49 . 14 ASN CA C 53.1 0.15 1 50 . 14 ASN N N 121.44 0.2 1 51 . 15 THR H H 8.32 0.015 1 52 . 15 THR HA H 4.56 0.015 1 53 . 15 THR C C 174.66 0.15 1 54 . 15 THR CA C 62.7 0.15 1 55 . 15 THR N N 111.01 0.2 1 56 . 23 PRO C C 177.94 0.15 1 57 . 24 GLN H H 9.04 0.015 1 58 . 24 GLN HA H 3.95 0.015 1 59 . 24 GLN C C 174.51 0.15 1 60 . 24 GLN CA C 58.00 0.15 1 61 . 24 GLN N N 127.34 0.2 1 62 . 25 ASP H H 7.88 0.015 1 63 . 25 ASP HA H 4.49 0.015 1 64 . 25 ASP C C 176.73 0.15 1 65 . 25 ASP CA C 52.3 0.15 1 66 . 25 ASP N N 111.87 0.2 1 67 . 26 MET H H 7.38 0.015 1 68 . 26 MET HA H 4.22 0.015 1 69 . 26 MET C C 175.66 0.15 1 70 . 26 MET CA C 56.5 0.15 1 71 . 26 MET N N 120.11 0.2 1 72 . 27 THR H H 7.95 0.015 1 73 . 27 THR HA H 4.43 0.015 1 74 . 27 THR C C 174.71 0.15 1 75 . 27 THR CA C 60.00 0.15 1 76 . 27 THR N N 118.39 0.2 1 77 . 28 ASP H H 9.01 0.015 1 78 . 28 ASP HA H 4.06 0.015 1 79 . 28 ASP C C 178.45 0.15 1 80 . 28 ASP CA C 58.3 0.15 1 81 . 28 ASP N N 122.00 0.2 1 82 . 29 ARG H H 8.3 0.015 1 83 . 29 ARG C C 178.42 0.15 1 84 . 29 ARG CA C 58.8 0.15 1 85 . 29 ARG N N 117.96 0.2 1 86 . 30 GLU H H 7.88 0.015 1 87 . 30 GLU HA H 4.03 0.015 1 88 . 30 GLU C C 179.04 0.15 1 89 . 30 GLU CA C 59.1 0.15 1 90 . 30 GLU N N 123.03 0.2 1 91 . 31 LEU H H 7.95 0.015 1 92 . 31 LEU HA H 4.05 0.015 1 93 . 31 LEU C C 177.68 0.15 1 94 . 31 LEU CA C 58.2 0.15 1 95 . 31 LEU N N 121.25 0.2 1 96 . 32 TYR H H 8.49 0.015 1 97 . 32 TYR HA H 3.93 0.015 1 98 . 32 TYR C C 176.67 0.15 1 99 . 32 TYR CA C 62.1 0.15 1 100 . 32 TYR N N 118.67 0.2 1 101 . 33 ALA H H 8.09 0.015 1 102 . 33 ALA HA H 3.97 0.015 1 103 . 33 ALA C C 180.55 0.15 1 104 . 33 ALA CA C 55.2 0.15 1 105 . 33 ALA N N 118.88 0.2 1 106 . 34 LEU H H 7.58 0.015 1 107 . 34 LEU HA H 4.01 0.015 1 108 . 34 LEU C C 177.63 0.15 1 109 . 34 LEU CA C 57.7 0.15 1 110 . 34 LEU N N 118.31 0.2 1 111 . 35 PHE H H 7.75 0.015 1 112 . 35 PHE HA H 4.11 0.015 1 113 . 35 PHE C C 178.02 0.15 1 114 . 35 PHE CA C 61.3 0.15 1 115 . 35 PHE N N 114.9 0.2 1 116 . 36 ARG H H 9.6 0.015 1 117 . 36 ARG HA H 4.38 0.015 1 118 . 36 ARG C C 176.76 0.15 1 119 . 36 ARG CA C 55.00 0.15 1 120 . 36 ARG N N 123.09 0.2 1 121 . 37 ALA H H 6.75 0.015 1 122 . 37 ALA HA H 4.04 0.015 1 123 . 37 ALA C C 178.92 0.15 1 124 . 37 ALA CA C 53.8 0.15 1 125 . 37 ALA N N 118.17 0.2 1 126 . 38 ILE H H 7.89 0.015 1 127 . 38 ILE HA H 3.86 0.015 1 128 . 38 ILE C C 175.99 0.15 1 129 . 38 ILE CA C 61.00 0.15 1 130 . 38 ILE N N 116.57 0.2 1 131 . 39 GLY H H 7.29 0.015 1 132 . 39 GLY CA C 45.6 0.15 1 133 . 39 GLY N N 105.91 0.2 1 134 . 40 PRO C C 175.79 0.15 1 135 . 40 PRO CA C 63.8 0.15 1 136 . 41 ILE H H 8.28 0.015 1 137 . 41 ILE C C 175.51 0.15 1 138 . 41 ILE CA C 60.4 0.15 1 139 . 41 ILE N N 123.79 0.2 1 140 . 42 ASN H H 9.19 0.015 1 141 . 42 ASN HA H 4.8 0.015 1 142 . 42 ASN C C 174.74 0.15 1 143 . 42 ASN CA C 54.8 0.15 1 144 . 42 ASN N N 125.01 0.2 1 145 . 43 THR H H 7.39 0.015 1 146 . 43 THR HA H 4.58 0.015 1 147 . 43 THR C C 172.19 0.15 1 148 . 43 THR CA C 60.00 0.15 1 149 . 43 THR N N 108.27 0.2 1 150 . 44 CYS H H 8.72 0.015 1 151 . 44 CYS HA H 5.00 0.015 1 152 . 44 CYS C C 172.00 0.15 1 153 . 44 CYS CA C 58.3 0.15 1 154 . 44 CYS N N 123.23 0.2 1 155 . 45 ARG H H 8.55 0.015 1 156 . 45 ARG HA H 4.7 0.015 1 157 . 45 ARG C C 173.77 0.15 1 158 . 45 ARG CA C 55.9 0.15 1 159 . 45 ARG N N 126.75 0.2 1 160 . 46 ILE H H 8.48 0.015 1 161 . 46 ILE CA C 61.9 0.15 1 162 . 46 ILE N N 125.5 0.2 1 163 . 49 ASP HA H 4.5 0.015 1 164 . 49 ASP C C 177.74 0.15 1 165 . 49 ASP CA C 53.6 0.15 1 166 . 50 TYR H H 8.95 0.015 1 167 . 50 TYR HA H 4.24 0.015 1 168 . 50 TYR C C 177.18 0.15 1 169 . 50 TYR CA C 60.1 0.15 1 170 . 50 TYR N N 128.35 0.2 1 171 . 51 LYS H H 8.49 0.015 1 172 . 51 LYS HA H 4.14 0.015 1 173 . 51 LYS C C 178.57 0.15 1 174 . 51 LYS CA C 58.7 0.15 1 175 . 51 LYS N N 118.2 0.2 1 176 . 52 THR H H 7.68 0.015 1 177 . 52 THR HA H 4.38 0.015 1 178 . 52 THR C C 176.28 0.15 1 179 . 52 THR CA C 61.6 0.15 1 180 . 52 THR N N 105.73 0.2 1 181 . 53 GLY C C 173.56 0.15 1 182 . 53 GLY CA C 45.5 0.15 1 183 . 54 TYR H H 7.78 0.015 1 184 . 54 TYR CA C 58.00 0.15 1 185 . 54 TYR N N 122.32 0.2 1 186 . 56 PHE C C 176.06 0.15 1 187 . 56 PHE CA C 55.6 0.15 1 188 . 57 GLY H H 8.93 0.015 1 189 . 57 GLY C C 173.28 0.15 1 190 . 57 GLY CA C 45.6 0.15 1 191 . 57 GLY N N 103.92 0.2 1 192 . 58 TYR H H 7.13 0.015 1 193 . 58 TYR HA H 5.26 0.015 1 194 . 58 TYR C C 170.96 0.15 1 195 . 58 TYR CA C 54.9 0.15 1 196 . 58 TYR N N 114.08 0.2 1 197 . 59 ALA H H 8.68 0.015 1 198 . 59 ALA HA H 4.75 0.015 1 199 . 59 ALA C C 174.07 0.15 1 200 . 59 ALA CA C 49.6 0.15 1 201 . 59 ALA N N 120.63 0.2 1 202 . 60 PHE H H 7.99 0.015 1 203 . 60 PHE HA H 5.58 0.015 1 204 . 60 PHE C C 176.23 0.15 1 205 . 60 PHE CA C 56.9 0.15 1 206 . 60 PHE N N 113.88 0.2 1 207 . 61 VAL H H 9.01 0.015 1 208 . 61 VAL HA H 4.22 0.015 1 209 . 61 VAL CA C 63.5 0.15 1 210 . 61 VAL N N 125.00 0.2 1 211 . 63 PHE C C 174.02 0.15 1 212 . 63 PHE CA C 60.1 0.15 1 213 . 64 THR H H 8.03 0.015 1 214 . 64 THR HA H 4.14 0.015 1 215 . 64 THR C C 174.8 0.15 1 216 . 64 THR CA C 65.3 0.15 1 217 . 64 THR N N 111.05 0.2 1 218 . 65 SER H H 8.74 0.015 1 219 . 65 SER HA H 4.91 0.015 1 220 . 65 SER C C 175.55 0.15 1 221 . 65 SER CA C 55.8 0.15 1 222 . 65 SER N N 114.17 0.2 1 223 . 66 GLU H H 9.6 0.015 1 224 . 66 GLU HA H 4.33 0.015 1 225 . 66 GLU C C 177.96 0.15 1 226 . 66 GLU CA C 58.4 0.15 1 227 . 66 GLU N N 128.75 0.2 1 228 . 67 MET H H 8.29 0.015 1 229 . 67 MET C C 178.82 0.15 1 230 . 67 MET CA C 58.3 0.15 1 231 . 67 MET N N 119.48 0.2 1 232 . 68 ASP H H 7.18 0.015 1 233 . 68 ASP HA H 4.29 0.015 1 234 . 68 ASP C C 176.83 0.15 1 235 . 68 ASP CA C 56.6 0.15 1 236 . 68 ASP N N 120.28 0.2 1 237 . 69 SER H H 7.71 0.015 1 238 . 69 SER HA H 3.77 0.015 1 239 . 69 SER C C 175.66 0.15 1 240 . 69 SER CA C 62.00 0.15 1 241 . 69 SER N N 116.43 0.2 1 242 . 70 GLN H H 7.58 0.015 1 243 . 70 GLN HA H 3.99 0.015 1 244 . 70 GLN C C 178.9 0.15 1 245 . 70 GLN CA C 59.1 0.15 1 246 . 70 GLN N N 119.22 0.2 1 247 . 71 ARG H H 7.47 0.015 1 248 . 71 ARG HA H 3.98 0.015 1 249 . 71 ARG C C 177.13 0.15 1 250 . 71 ARG CA C 59.2 0.15 1 251 . 71 ARG N N 120.52 0.2 1 252 . 72 ALA H H 8.41 0.015 1 253 . 72 ALA C C 179.4 0.15 1 254 . 72 ALA CA C 55.5 0.15 1 255 . 72 ALA N N 120.94 0.2 1 256 . 73 ILE H H 7.45 0.015 1 257 . 73 ILE C C 177.69 0.15 1 258 . 73 ILE CA C 66.3 0.15 1 259 . 73 ILE N N 116.73 0.2 1 260 . 74 LYS H H 7.29 0.015 1 261 . 74 LYS HA H 4.00 0.015 1 262 . 74 LYS C C 178.88 0.15 1 263 . 74 LYS CA C 59.2 0.15 1 264 . 74 LYS N N 117.73 0.2 1 265 . 75 VAL H H 8.53 0.015 1 266 . 75 VAL HA H 3.92 0.015 1 267 . 75 VAL C C 177.37 0.15 1 268 . 75 VAL CA C 64.7 0.15 1 269 . 75 VAL N N 115.36 0.2 1 270 . 76 LEU H H 8.37 0.015 1 271 . 76 LEU HA H 4.43 0.015 1 272 . 76 LEU C C 177.26 0.15 1 273 . 76 LEU CA C 55.2 0.15 1 274 . 76 LEU N N 117.02 0.2 1 275 . 77 ASN H H 7.63 0.015 1 276 . 77 ASN C C 176.73 0.15 1 277 . 77 ASN CA C 56.8 0.15 1 278 . 77 ASN N N 115.39 0.2 1 279 . 78 GLY H H 8.61 0.015 1 280 . 78 GLY C C 174.01 0.15 1 281 . 78 GLY CA C 45.5 0.15 1 282 . 78 GLY N N 116.88 0.2 1 283 . 79 ILE H H 7.62 0.015 1 284 . 79 ILE C C 176.23 0.15 1 285 . 79 ILE CA C 62.1 0.15 1 286 . 79 ILE N N 119.31 0.2 1 287 . 80 THR H H 8.2 0.015 1 288 . 80 THR HA H 5.17 0.015 1 289 . 80 THR C C 175.3 0.15 1 290 . 80 THR CA C 62.2 0.15 1 291 . 80 THR N N 120.07 0.2 1 292 . 81 VAL H H 8.83 0.015 1 293 . 81 VAL HA H 4.00 0.015 1 294 . 81 VAL C C 173.73 0.15 1 295 . 81 VAL CA C 62.1 0.15 1 296 . 81 VAL N N 128.04 0.2 1 297 . 82 ARG H H 9.18 0.015 1 298 . 82 ARG CA C 59.2 0.15 1 299 . 82 ARG N N 123.46 0.2 1 300 . 84 LYS HA H 4.69 0.015 1 301 . 84 LYS C C 175.3 0.15 1 302 . 85 ARG H H 8.35 0.015 1 303 . 85 ARG HA H 5.02 0.015 1 304 . 85 ARG C C 176.42 0.15 1 305 . 85 ARG CA C 54.1 0.15 1 306 . 85 ARG N N 120.15 0.2 1 307 . 86 LEU H H 8.93 0.015 1 308 . 86 LEU C C 178.56 0.15 1 309 . 86 LEU CA C 56.4 0.15 1 310 . 86 LEU N N 124.45 0.2 1 311 . 87 LYS H H 8.68 0.015 1 312 . 87 LYS C C 174.2 0.15 1 313 . 87 LYS CA C 54.8 0.15 1 314 . 87 LYS N N 124.62 0.2 1 315 . 88 VAL H H 8.74 0.015 1 316 . 88 VAL C C 173.4 0.15 1 317 . 88 VAL CA C 61.4 0.15 1 318 . 88 VAL N N 127.5 0.2 1 319 . 89 SER H H 8.55 0.015 1 320 . 89 SER HA H 4.63 0.015 1 321 . 89 SER C C 172.48 0.15 1 322 . 89 SER CA C 56.6 0.15 1 323 . 89 SER N N 118.96 0.2 1 324 . 90 TYR H H 8.43 0.015 1 325 . 90 TYR C C 177.2 0.15 1 326 . 90 TYR CA C 60.7 0.15 1 327 . 90 TYR N N 119.06 0.2 1 328 . 91 ALA H H 9.28 0.015 1 329 . 91 ALA C C 177.67 0.15 1 330 . 91 ALA CA C 52.8 0.15 1 331 . 91 ALA N N 126.3 0.2 1 332 . 93 PRO HA H 4.34 0.015 1 333 . 93 PRO C C 176.63 0.15 1 334 . 93 PRO CA C 64.00 0.15 1 335 . 94 GLY H H 8.13 0.015 1 336 . 94 GLY C C 174.76 0.15 1 337 . 94 GLY CA C 45.00 0.15 1 338 . 94 GLY N N 109.48 0.2 1 339 . 95 GLY H H 7.54 0.015 1 340 . 95 GLY C C 175.33 0.15 1 341 . 95 GLY CA C 44.7 0.15 1 342 . 95 GLY N N 107.61 0.2 1 343 . 96 GLU H H 8.84 0.015 1 344 . 96 GLU HA H 3.87 0.015 1 345 . 96 GLU C C 178.48 0.15 1 346 . 96 GLU CA C 59.2 0.15 1 347 . 96 GLU N N 120.71 0.2 1 348 . 97 SER H H 8.48 0.015 1 349 . 97 SER HA H 4.29 0.015 1 350 . 97 SER CA C 61.3 0.15 1 351 . 97 SER N N 111.76 0.2 1 352 . 99 LYS C C 174.37 0.15 1 353 . 99 LYS CA C 56.4 0.15 1 354 . 100 ASP H H 8.65 0.015 1 355 . 100 ASP HA H 4.42 0.015 1 356 . 100 ASP C C 174.75 0.15 1 357 . 100 ASP CA C 55.3 0.15 1 358 . 100 ASP N N 114.48 0.2 1 359 . 101 THR H H 7.64 0.015 1 360 . 101 THR HA H 4.2 0.015 1 361 . 101 THR C C 174.38 0.15 1 362 . 101 THR CA C 60.1 0.15 1 363 . 101 THR N N 100.97 0.2 1 364 . 102 ASN H H 8.15 0.015 1 365 . 102 ASN HA H 5.23 0.015 1 366 . 102 ASN C C 174.28 0.15 1 367 . 102 ASN CA C 52.2 0.15 1 368 . 102 ASN N N 120.81 0.2 1 369 . 103 LEU H H 9.75 0.015 1 370 . 103 LEU N N 129.26 0.2 1 371 . 104 TYR H H 9.06 0.015 1 372 . 104 TYR HA H 4.42 0.015 1 373 . 104 TYR C C 174.08 0.15 1 374 . 104 TYR CA C 56.9 0.15 1 375 . 104 TYR N N 122.38 0.2 1 376 . 105 VAL H H 8.53 0.015 1 377 . 105 VAL HA H 4.93 0.015 1 378 . 105 VAL C C 174.39 0.15 1 379 . 105 VAL CA C 60.1 0.15 1 380 . 105 VAL N N 129.9 0.2 1 381 . 106 THR H H 8.87 0.015 1 382 . 106 THR C C 173.35 0.15 1 383 . 106 THR CA C 59.6 0.15 1 384 . 106 THR N N 114.35 0.2 1 385 . 107 ASN H H 8.31 0.015 1 386 . 107 ASN C C 175.89 0.15 1 387 . 107 ASN CA C 53.8 0.15 1 388 . 107 ASN N N 113.2 0.2 1 389 . 108 LEU H H 8.31 0.015 1 390 . 108 LEU HA H 4.1 0.015 1 391 . 108 LEU C C 177.72 0.15 1 392 . 108 LEU CA C 53.8 0.15 1 393 . 108 LEU N N 117.69 0.2 1 394 . 109 PRO HA H 4.48 0.015 1 395 . 109 PRO C C 177.76 0.15 1 396 . 109 PRO CA C 62.5 0.15 1 397 . 110 ARG H H 8.97 0.015 1 398 . 110 ARG HA H 3.92 0.015 1 399 . 110 ARG C C 175.54 0.15 1 400 . 110 ARG CA C 57.8 0.15 1 401 . 110 ARG N N 120.32 0.2 1 402 . 111 THR H H 7.06 0.015 1 403 . 111 THR HA H 4.23 0.015 1 404 . 111 THR C C 174.37 0.15 1 405 . 111 THR CA C 60.3 0.15 1 406 . 111 THR N N 103.74 0.2 1 407 . 112 ILE H H 7.24 0.015 1 408 . 112 ILE HA H 4.33 0.015 1 409 . 112 ILE C C 172.2 0.15 1 410 . 112 ILE CA C 59.4 0.15 1 411 . 112 ILE N N 122.54 0.2 1 412 . 113 THR H H 6.97 0.015 1 413 . 113 THR HA H 4.71 0.015 1 414 . 113 THR C C 175.15 0.15 1 415 . 113 THR CA C 58.7 0.15 1 416 . 113 THR N N 113.79 0.2 1 417 . 114 ASP H H 8.95 0.015 1 418 . 114 ASP C C 177.79 0.15 1 419 . 114 ASP CA C 58.6 0.15 1 420 . 114 ASP N N 122.5 0.2 1 421 . 115 ASP H H 8.4 0.015 1 422 . 115 ASP HA H 4.43 0.015 1 423 . 115 ASP C C 178.88 0.15 1 424 . 115 ASP CA C 57.00 0.15 1 425 . 115 ASP N N 116.8 0.2 1 426 . 116 GLN H H 7.75 0.015 1 427 . 116 GLN HA H 4.13 0.015 1 428 . 116 GLN C C 178.84 0.15 1 429 . 116 GLN CA C 58.6 0.15 1 430 . 116 GLN N N 120.39 0.2 1 431 . 117 LEU H H 8.46 0.015 1 432 . 117 LEU HA H 4.13 0.015 1 433 . 117 LEU C C 179.09 0.15 1 434 . 117 LEU CA C 58.8 0.15 1 435 . 117 LEU N N 120.67 0.2 1 436 . 118 ASP H H 8.28 0.015 1 437 . 118 ASP HA H 4.32 0.015 1 438 . 118 ASP C C 179.65 0.15 1 439 . 118 ASP CA C 57.9 0.15 1 440 . 118 ASP N N 119.48 0.2 1 441 . 119 THR H H 8.09 0.015 1 442 . 119 THR C C 176.16 0.15 1 443 . 119 THR CA C 66.8 0.15 1 444 . 119 THR N N 117.81 0.2 1 445 . 120 ILE H H 8.18 0.015 1 446 . 120 ILE C C 177.34 0.15 1 447 . 120 ILE CA C 65.1 0.15 1 448 . 120 ILE N N 120.18 0.2 1 449 . 121 PHE H H 8.71 0.015 1 450 . 121 PHE C C 180.64 0.15 1 451 . 121 PHE CA C 61.2 0.15 1 452 . 121 PHE N N 112.35 0.2 1 453 . 122 GLY H H 9.13 0.015 1 454 . 122 GLY C C 173.82 0.15 1 455 . 122 GLY CA C 46.5 0.15 1 456 . 122 GLY N N 115.11 0.2 1 457 . 123 LYS H H 6.52 0.015 1 458 . 123 LYS HA H 3.92 0.015 1 459 . 123 LYS C C 176.85 0.15 1 460 . 123 LYS CA C 57.4 0.15 1 461 . 123 LYS N N 116.16 0.2 1 462 . 124 TYR H H 6.88 0.015 1 463 . 124 TYR HA H 4.37 0.015 1 464 . 124 TYR C C 173.79 0.15 1 465 . 124 TYR CA C 58.6 0.15 1 466 . 124 TYR N N 113.4 0.2 1 467 . 125 GLY H H 7.33 0.015 1 468 . 125 GLY C C 171.2 0.15 1 469 . 125 GLY CA C 45.4 0.15 1 470 . 125 GLY N N 103.71 0.2 1 471 . 126 SER H H 8.23 0.015 1 472 . 126 SER HA H 4.59 0.015 1 473 . 126 SER C C 172.95 0.15 1 474 . 126 SER CA C 57.8 0.15 1 475 . 126 SER N N 114.02 0.2 1 476 . 127 ILE H H 8.77 0.015 1 477 . 127 ILE C C 176.9 0.15 1 478 . 127 ILE N N 126.84 0.2 1 479 . 128 VAL H H 9.08 0.015 1 480 . 128 VAL HA H 3.83 0.015 1 481 . 128 VAL C C 174.81 0.15 1 482 . 128 VAL CA C 63.7 0.15 1 483 . 128 VAL N N 130.46 0.2 1 484 . 129 GLN H H 7.55 0.015 1 485 . 129 GLN HA H 4.44 0.015 1 486 . 129 GLN C C 171.51 0.15 1 487 . 129 GLN CA C 55.00 0.15 1 488 . 129 GLN N N 119.08 0.2 1 489 . 130 LYS H H 8.39 0.015 1 490 . 130 LYS HA H 4.97 0.015 1 491 . 130 LYS C C 174.78 0.15 1 492 . 130 LYS CA C 54.7 0.15 1 493 . 130 LYS N N 120.22 0.2 1 494 . 131 ASN H H 8.84 0.015 1 495 . 131 ASN HA H 4.6 0.015 1 496 . 131 ASN C C 171.93 0.15 1 497 . 131 ASN CA C 53.7 0.15 1 498 . 131 ASN N N 116.91 0.2 1 499 . 132 ILE H H 8.78 0.015 1 500 . 132 ILE C C 174.81 0.15 1 501 . 132 ILE CA C 61.8 0.15 1 502 . 132 ILE N N 127.02 0.2 1 503 . 133 LEU H H 7.86 0.015 1 504 . 133 LEU HA H 4.5 0.015 1 505 . 133 LEU C C 177.93 0.15 1 506 . 133 LEU CA C 56.5 0.15 1 507 . 133 LEU N N 127.26 0.2 1 508 . 134 ARG H H 9.23 0.015 1 509 . 134 ARG HA H 4.74 0.015 1 510 . 134 ARG C C 175.64 0.15 1 511 . 134 ARG CA C 54.8 0.15 1 512 . 134 ARG N N 123.86 0.2 1 513 . 135 ASP H H 8.59 0.015 1 514 . 135 ASP C C 177.79 0.15 1 515 . 135 ASP CA C 54.4 0.15 1 516 . 135 ASP N N 123.22 0.2 1 517 . 136 LYS H H 9.06 0.015 1 518 . 136 LYS HA H 4.01 0.015 1 519 . 136 LYS C C 177.46 0.15 1 520 . 136 LYS CA C 58.8 0.15 1 521 . 136 LYS N N 128.04 0.2 1 522 . 137 LEU H H 8.53 0.015 1 523 . 137 LEU HA H 4.4 0.015 1 524 . 137 LEU C C 179.12 0.15 1 525 . 137 LEU CA C 56.9 0.15 1 526 . 137 LEU N N 118.16 0.2 1 527 . 138 THR H H 8.2 0.015 1 528 . 138 THR HA H 4.42 0.015 1 529 . 138 THR C C 176.63 0.15 1 530 . 138 THR CA C 61.8 0.15 1 531 . 138 THR N N 106.86 0.2 1 532 . 139 GLY H H 8.33 0.015 1 533 . 139 GLY HA2 H 4.23 0.015 1 534 . 139 GLY HA3 H 4.23 0.015 1 535 . 139 GLY C C 173.55 0.15 1 536 . 139 GLY CA C 45.6 0.15 1 537 . 139 GLY N N 111.01 0.2 1 538 . 140 ARG H H 7.86 0.015 1 539 . 140 ARG HA H 4.63 0.015 1 540 . 140 ARG C C 175.89 0.15 1 541 . 140 ARG CA C 54.6 0.15 1 542 . 140 ARG N N 121.12 0.2 1 543 . 141 PRO C C 176.8 0.15 1 544 . 141 PRO CA C 61.1 0.15 1 545 . 142 ARG H H 7.33 0.015 1 546 . 142 ARG HA H 4.34 0.015 1 547 . 142 ARG C C 176.52 0.15 1 548 . 142 ARG CA C 56.4 0.15 1 549 . 142 ARG N N 126.32 0.2 1 550 . 143 GLY H H 8.8 0.015 1 551 . 143 GLY C C 171.35 0.15 1 552 . 143 GLY CA C 45.6 0.15 1 553 . 143 GLY N N 107.5 0.2 1 554 . 144 VAL H H 6.85 0.015 1 555 . 144 VAL HA H 5.14 0.015 1 556 . 144 VAL C C 175.16 0.15 1 557 . 144 VAL CA C 58.9 0.15 1 558 . 144 VAL N N 115.91 0.2 1 559 . 145 ALA H H 9.16 0.015 1 560 . 145 ALA HA H 5.16 0.015 1 561 . 145 ALA C C 173.92 0.15 1 562 . 145 ALA CA C 51.3 0.15 1 563 . 145 ALA N N 127.41 0.2 1 564 . 146 PHE H H 8.18 0.015 1 565 . 146 PHE HA H 5.49 0.015 1 566 . 146 PHE C C 176.19 0.15 1 567 . 146 PHE CA C 57.00 0.15 1 568 . 146 PHE N N 116.24 0.2 1 569 . 147 VAL H H 8.46 0.015 1 570 . 147 VAL HA H 4.1 0.015 1 571 . 147 VAL CA C 62.3 0.15 1 572 . 147 VAL N N 120.05 0.2 1 573 . 151 LYS C C 178.25 0.15 1 574 . 152 ARG H H 8.9 0.015 1 575 . 152 ARG C C 178.88 0.15 1 576 . 152 ARG CA C 60.00 0.15 1 577 . 152 ARG N N 125.64 0.2 1 578 . 153 GLU H H 9.65 0.015 1 579 . 153 GLU HA H 4.1 0.015 1 580 . 153 GLU CA C 59.9 0.15 1 581 . 153 GLU N N 118.2 0.2 1 582 . 154 GLU H H 7.17 0.015 1 583 . 154 GLU C C 176.28 0.15 1 584 . 154 GLU CA C 58.2 0.15 1 585 . 154 GLU N N 120.36 0.2 1 586 . 155 ALA H H 6.73 0.015 1 587 . 155 ALA HA H 3.79 0.015 1 588 . 155 ALA C C 178.92 0.15 1 589 . 155 ALA CA C 54.7 0.15 1 590 . 155 ALA N N 118.26 0.2 1 591 . 156 GLN H H 7.86 0.015 1 592 . 156 GLN HA H 3.88 0.015 1 593 . 156 GLN C C 178.72 0.15 1 594 . 156 GLN CA C 58.6 0.15 1 595 . 156 GLN N N 114.27 0.2 1 596 . 157 GLU H H 7.74 0.015 1 597 . 157 GLU HA H 3.96 0.015 1 598 . 157 GLU C C 178.45 0.15 1 599 . 157 GLU CA C 59.1 0.15 1 600 . 157 GLU N N 120.97 0.2 1 601 . 158 ALA H H 7.94 0.015 1 602 . 158 ALA HA H 3.01 0.015 1 603 . 158 ALA C C 179.28 0.15 1 604 . 158 ALA CA C 55.4 0.15 1 605 . 158 ALA N N 122.32 0.2 1 606 . 159 ILE H H 8.05 0.015 1 607 . 159 ILE C C 178.36 0.15 1 608 . 159 ILE CA C 66.5 0.15 1 609 . 159 ILE N N 116.84 0.2 1 610 . 160 SER H H 7.77 0.015 1 611 . 160 SER C C 176.11 0.15 1 612 . 160 SER CA C 61.4 0.15 1 613 . 160 SER N N 112.57 0.2 1 614 . 161 ALA H H 7.99 0.015 1 615 . 161 ALA HA H 4.15 0.015 1 616 . 161 ALA C C 179.15 0.15 1 617 . 161 ALA CA C 53.8 0.15 1 618 . 161 ALA N N 120.63 0.2 1 619 . 162 LEU H H 7.9 0.015 1 620 . 162 LEU HA H 4.4 0.015 1 621 . 162 LEU C C 177.58 0.15 1 622 . 162 LEU CA C 54.8 0.15 1 623 . 162 LEU N N 113.55 0.2 1 624 . 163 ASN H H 8.01 0.015 1 625 . 163 ASN C C 175.9 0.15 1 626 . 163 ASN CA C 56.3 0.15 1 627 . 163 ASN N N 116.02 0.2 1 628 . 164 ASN H H 8.98 0.015 1 629 . 164 ASN HA H 4.36 0.015 1 630 . 164 ASN C C 173.92 0.15 1 631 . 164 ASN CA C 55.2 0.15 1 632 . 164 ASN N N 119.42 0.2 1 633 . 165 VAL H H 7.66 0.015 1 634 . 165 VAL HA H 4.21 0.015 1 635 . 165 VAL C C 175.56 0.15 1 636 . 165 VAL CA C 61.6 0.15 1 637 . 165 VAL N N 120.03 0.2 1 638 . 166 ILE H H 8.71 0.015 1 639 . 166 ILE CA C 59.1 0.15 1 640 . 166 ILE N N 128.98 0.2 1 641 . 167 PRO HA H 4.53 0.015 1 642 . 167 PRO C C 175.76 0.15 1 643 . 167 PRO CA C 62.1 0.15 1 644 . 168 GLU H H 8.66 0.015 1 645 . 168 GLU C C 177.73 0.15 1 646 . 168 GLU CA C 58.3 0.15 1 647 . 168 GLU N N 121.9 0.2 1 648 . 169 GLY H H 8.87 0.015 1 649 . 169 GLY C C 174.67 0.15 1 650 . 169 GLY CA C 45.3 0.15 1 651 . 169 GLY N N 114.27 0.2 1 652 . 170 GLY H H 8.52 0.015 1 653 . 170 GLY HA2 H 4.54 0.015 1 654 . 170 GLY HA3 H 4.54 0.015 1 655 . 170 GLY C C 172.43 0.15 1 656 . 170 GLY CA C 43.9 0.15 1 657 . 170 GLY N N 108.12 0.2 1 658 . 171 SER H H 9.05 0.015 1 659 . 171 SER HA H 4.08 0.015 1 660 . 171 SER C C 173.4 0.15 1 661 . 171 SER CA C 58.3 0.15 1 662 . 171 SER N N 110.74 0.2 1 663 . 172 GLN H H 7.85 0.015 1 664 . 172 GLN HA H 4.3 0.015 1 665 . 172 GLN N N 120.69 0.2 1 666 . 173 PRO HA H 4.08 0.015 1 667 . 173 PRO C C 176.6 0.15 1 668 . 173 PRO CA C 62.1 0.15 1 669 . 174 LEU H H 8.42 0.015 1 670 . 174 LEU C C 177.62 0.15 1 671 . 174 LEU CA C 55.3 0.15 1 672 . 174 LEU N N 122.59 0.2 1 673 . 175 SER H H 7.82 0.015 1 674 . 175 SER HA H 5.17 0.015 1 675 . 175 SER C C 173.59 0.15 1 676 . 175 SER CA C 56.9 0.15 1 677 . 175 SER N N 115.89 0.2 1 678 . 176 VAL H H 8.83 0.015 1 679 . 176 VAL HA H 4.49 0.015 1 680 . 176 VAL C C 172.89 0.15 1 681 . 176 VAL CA C 61.8 0.15 1 682 . 176 VAL N N 127.16 0.2 1 683 . 177 ARG H H 8.14 0.015 1 684 . 177 ARG HA H 4.78 0.015 1 685 . 177 ARG C C 174.46 0.15 1 686 . 177 ARG CA C 53.4 0.15 1 687 . 177 ARG N N 122.28 0.2 1 688 . 178 LEU H H 8.77 0.015 1 689 . 178 LEU C C 178.47 0.15 1 690 . 178 LEU CA C 55.9 0.15 1 691 . 178 LEU N N 120.92 0.2 1 692 . 179 ALA H H 9.16 0.015 1 693 . 179 ALA C C 177.7 0.15 1 694 . 179 ALA CA C 53.8 0.15 1 695 . 179 ALA N N 126.11 0.2 1 696 . 180 GLU H H 8.54 0.015 1 697 . 180 GLU HA H 4.36 0.015 1 698 . 180 GLU C C 175.82 0.15 1 699 . 180 GLU CA C 56.2 0.15 1 700 . 180 GLU N N 117.29 0.2 1 701 . 181 GLU H H 8.31 0.015 1 702 . 181 GLU HA H 4.25 0.015 1 703 . 181 GLU C C 176.16 0.15 1 704 . 181 GLU CA C 56.6 0.15 1 705 . 181 GLU N N 122.29 0.2 1 706 . 182 HIS H H 8.64 0.015 1 707 . 182 HIS HA H 4.68 0.015 1 708 . 182 HIS C C 174.93 0.15 1 709 . 182 HIS CA C 55.4 0.15 1 710 . 182 HIS N N 120.41 0.2 1 711 . 183 GLY H H 8.57 0.015 1 712 . 183 GLY HA2 H 3.89 0.015 1 713 . 183 GLY HA3 H 3.89 0.015 1 714 . 183 GLY CA C 45.2 0.15 1 715 . 183 GLY N N 110.99 0.2 1 716 . 184 LYS H H 7.89 0.015 1 717 . 184 LYS CA C 57.5 0.15 1 718 . 184 LYS N N 126.02 0.2 1 stop_ save_