data_5799 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Protein Signal Assignments using Specific Labeling and Cell-free Synthesis ; _BMRB_accession_number 5799 _BMRB_flat_file_name bmr5799.str _Entry_type original _Submission_date 2003-05-16 _Accession_date 2003-05-19 _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 Shi Jianxia . . 2 Pelton Jefferey G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 529 "13C chemical shifts" 599 "15N chemical shifts" 206 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-23 original author . stop_ _Original_release_date 2004-03-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protein Signal Assignments using Specific Labeling and Cell-free Synthesis' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14752257 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shi Jianxia . . 2 Pelton Jefferey G. . 3 Cho H. S. . 4 Wemmer D. E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 235 _Page_last 247 _Year 2004 _Details . loop_ _Keyword 'Cell-free protein synthesis' 'NMR assignment' PSP 'Selective stable isotope labeling' stop_ save_ ################################## # Molecular system description # ################################## save_system_PSP _Saveframe_category molecular_system _Mol_system_name 'PSP monomer' _Abbreviation_common PSP _Enzyme_commission_number 3.1.3.3 loop_ _Mol_system_component_name _Mol_label 'PSP monomer' $PSP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function hydrolase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PSP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Phosphoserine phosphatase' _Abbreviation_common PSP _Molecular_mass 23594 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 211 _Mol_residue_sequence ; MEKKKKLILFDFDSTLVNNE TIDEIAREAGVEEEVKKITK EAMEGKLNFEQSLRKRVSLL KDLPIEKVEKAIKRITPTEG AEETIKELKNRGYVVAVVSG GFDIAVNKIKEKLGLDYAFA NRLIVKDGKLTGDVEGEVLK ENAKGEILEKIAKIEGINLE DTVAVGDGANDISMFKKAGL KIAFCAKPILKEKADICIEK RDLREILKYIK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LYS 4 LYS 5 LYS 6 LYS 7 LEU 8 ILE 9 LEU 10 PHE 11 ASP 12 PHE 13 ASP 14 SER 15 THR 16 LEU 17 VAL 18 ASN 19 ASN 20 GLU 21 THR 22 ILE 23 ASP 24 GLU 25 ILE 26 ALA 27 ARG 28 GLU 29 ALA 30 GLY 31 VAL 32 GLU 33 GLU 34 GLU 35 VAL 36 LYS 37 LYS 38 ILE 39 THR 40 LYS 41 GLU 42 ALA 43 MET 44 GLU 45 GLY 46 LYS 47 LEU 48 ASN 49 PHE 50 GLU 51 GLN 52 SER 53 LEU 54 ARG 55 LYS 56 ARG 57 VAL 58 SER 59 LEU 60 LEU 61 LYS 62 ASP 63 LEU 64 PRO 65 ILE 66 GLU 67 LYS 68 VAL 69 GLU 70 LYS 71 ALA 72 ILE 73 LYS 74 ARG 75 ILE 76 THR 77 PRO 78 THR 79 GLU 80 GLY 81 ALA 82 GLU 83 GLU 84 THR 85 ILE 86 LYS 87 GLU 88 LEU 89 LYS 90 ASN 91 ARG 92 GLY 93 TYR 94 VAL 95 VAL 96 ALA 97 VAL 98 VAL 99 SER 100 GLY 101 GLY 102 PHE 103 ASP 104 ILE 105 ALA 106 VAL 107 ASN 108 LYS 109 ILE 110 LYS 111 GLU 112 LYS 113 LEU 114 GLY 115 LEU 116 ASP 117 TYR 118 ALA 119 PHE 120 ALA 121 ASN 122 ARG 123 LEU 124 ILE 125 VAL 126 LYS 127 ASP 128 GLY 129 LYS 130 LEU 131 THR 132 GLY 133 ASP 134 VAL 135 GLU 136 GLY 137 GLU 138 VAL 139 LEU 140 LYS 141 GLU 142 ASN 143 ALA 144 LYS 145 GLY 146 GLU 147 ILE 148 LEU 149 GLU 150 LYS 151 ILE 152 ALA 153 LYS 154 ILE 155 GLU 156 GLY 157 ILE 158 ASN 159 LEU 160 GLU 161 ASP 162 THR 163 VAL 164 ALA 165 VAL 166 GLY 167 ASP 168 GLY 169 ALA 170 ASN 171 ASP 172 ILE 173 SER 174 MET 175 PHE 176 LYS 177 LYS 178 ALA 179 GLY 180 LEU 181 LYS 182 ILE 183 ALA 184 PHE 185 CYS 186 ALA 187 LYS 188 PRO 189 ILE 190 LEU 191 LYS 192 GLU 193 LYS 194 ALA 195 ASP 196 ILE 197 CYS 198 ILE 199 GLU 200 LYS 201 ARG 202 ASP 203 LEU 204 ARG 205 GLU 206 ILE 207 LEU 208 LYS 209 TYR 210 ILE 211 LYS 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 1F5S "Crystal Structure Of Phosphoserine Phosphatase From Methanococcus Jannaschii" 100.00 211 100.00 100.00 1.28e-140 PDB 1J97 "Phospho-Aspartyl Intermediate Analogue Of Phosphoserine Phosphatase" 100.00 211 99.53 99.53 1.52e-139 PDB 1L7M "High Resolution Liganded Structure Of Phosphoserine Phosphatase (Pi Complex)" 99.53 211 99.05 99.05 3.44e-137 PDB 1L7N "Transition State Analogue Of Phosphoserine Phosphatase (Aluminum Fluoride Complex)" 99.53 211 99.05 99.05 3.44e-137 PDB 1L7O "Crystal Structure Of Phosphoserine Phosphatase In Apo Form" 99.53 211 98.57 99.05 1.59e-136 PDB 1L7P "Substrate Bound Phosphoserine Phosphatase Complex Structure" 99.53 211 98.57 99.05 1.59e-136 GB AAB99612 "phosphoserine phosphatase (serB) [Methanocaldococcus jannaschii DSM 2661]" 100.00 211 100.00 100.00 1.28e-140 GB AIJ05608 "phosphoserine phosphatase SerB [Methanocaldococcus sp. JH146]" 100.00 211 98.10 99.53 1.29e-137 REF NP_248603 "phosphoserine phosphatase SerB [Methanocaldococcus jannaschii DSM 2661]" 100.00 211 100.00 100.00 1.28e-140 REF WP_010871118 "phosphoserine phosphatase [Methanocaldococcus jannaschii]" 100.00 211 100.00 100.00 1.28e-140 SP Q58989 "RecName: Full=Phosphoserine phosphatase; Short=PSP; Short=PSPase; AltName: Full=O-phosphoserine phosphohydrolase [Methanocaldoc" 100.00 211 100.00 100.00 1.28e-140 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PSP . 2190 Eubacteria . Methanococcous jannichi 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 $PSP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PSP 1.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_hsqc_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N hsqc' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNcaCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNcaCO _Sample_label . save_ save_HNcoCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNcoCA _Sample_label . save_ save_CBCAcoNH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCAcoNH _Sample_label . save_ save_HAHN_8 _Saveframe_category NMR_applied_experiment _Experiment_name HAHN _Sample_label . save_ save_HBHAcoNH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHAcoNH _Sample_label . save_ save_HNcaNH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNcaNH _Sample_label . save_ save_15N_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N hsqc' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNcaCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNcoCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCAcoNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HAHN _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHAcoNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNcaNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY' _BMRB_pulse_sequence_accession_number . _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 6.2 0.2 na temperature 313 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 . . . 1.000000000 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_ _Experiment_label '15N hsqc' HNCA HNCACB HNCO HNcaCO HNcoCA CBCAcoNH HAHN HBHAcoNH HNcaNH '15N NOESY' stop_ loop_ _Sample_label $Sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PSP 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 . 2 GLU CA C 56.7 0.20 1 2 . 2 GLU HA H 4.47 0.02 1 3 . 2 GLU CB C 30.9 0.20 1 4 . 2 GLU HB3 H 2.09 0.02 2 5 . 2 GLU C C 175.9 0.20 1 6 . 3 LYS N N 123.6 0.20 1 7 . 3 LYS H H 8.42 0.02 1 8 . 3 LYS CA C 55.8 0.20 1 9 . 3 LYS HA H 4.41 0.02 1 10 . 3 LYS CB C 33.5 0.20 1 11 . 3 LYS HB2 H 1.88 0.02 2 12 . 3 LYS HB3 H 2.11 0.02 2 13 . 3 LYS C C 176.1 0.20 1 14 . 4 LYS N N 124.2 0.20 1 15 . 4 LYS H H 8.31 0.02 1 16 . 4 LYS CA C 55.8 0.20 1 17 . 4 LYS HA H 4.41 0.02 1 18 . 4 LYS CB C 33.7 0.20 1 19 . 4 LYS HB2 H 1.81 0.02 2 20 . 4 LYS HB3 H 2.09 0.02 2 21 . 4 LYS C C 176.0 0.20 1 22 . 5 LYS N N 124.0 0.20 1 23 . 5 LYS H H 8.41 0.02 1 24 . 5 LYS CA C 56.4 0.20 1 25 . 5 LYS HA H 4.44 0.02 1 26 . 5 LYS CB C 34.0 0.20 1 27 . 5 LYS HB3 H 1.82 0.02 2 28 . 5 LYS C C 174.9 0.20 1 29 . 6 LYS N N 120.0 0.20 1 30 . 6 LYS H H 7.06 0.02 1 31 . 6 LYS CA C 54.5 0.20 1 32 . 6 LYS HA H 4.79 0.02 1 33 . 6 LYS CB C 36.0 0.20 1 34 . 6 LYS C C 174.3 0.20 1 35 . 7 LEU N N 121.2 0.20 1 36 . 7 LEU H H 7.83 0.02 1 37 . 7 LEU CA C 53.4 0.20 1 38 . 7 LEU HA H 5.52 0.02 1 39 . 7 LEU CB C 47.3 0.20 1 40 . 7 LEU HB3 H 1.65 0.02 2 41 . 7 LEU C C 174.1 0.20 1 42 . 8 ILE N N 125.8 0.20 1 43 . 8 ILE H H 9.22 0.02 1 44 . 8 ILE CA C 58.1 0.20 1 45 . 8 ILE HA H 5.35 0.02 1 46 . 8 ILE CB C 41.1 0.20 1 47 . 8 ILE HB H 1.60 0.02 1 48 . 8 ILE C C 171.0 0.20 1 49 . 9 LEU N N 129.8 0.20 1 50 . 9 LEU H H 9.31 0.02 1 51 . 9 LEU CA C 52.4 0.20 1 52 . 9 LEU HA H 5.01 0.02 1 53 . 9 LEU CB C 45.3 0.20 1 54 . 9 LEU HB3 H 2.10 0.02 2 55 . 9 LEU C C 174.1 0.20 1 56 . 10 PHE N N 122.3 0.20 1 57 . 10 PHE H H 9.09 0.02 1 58 . 10 PHE CA C 57.3 0.20 1 59 . 10 PHE HA H 5.07 0.02 1 60 . 10 PHE CB C 38.7 0.20 1 61 . 10 PHE C C 177.6 0.20 1 62 . 11 ASP N N 119.4 0.20 1 63 . 11 ASP H H 8.40 0.02 1 64 . 11 ASP CA C 53.7 0.20 1 65 . 11 ASP CB C 45.0 0.20 1 66 . 11 ASP C C 175.4 0.20 1 67 . 12 PHE N N 124.6 0.20 1 68 . 12 PHE H H 7.75 0.02 1 69 . 12 PHE CA C 59.6 0.20 1 70 . 12 PHE C C 175.6 0.20 1 71 . 13 ASP N N 122.0 0.20 1 72 . 13 ASP H H 8.98 0.02 1 73 . 13 ASP CA C 58.1 0.20 1 74 . 13 ASP C C 175.8 0.20 1 75 . 14 SER N N 118.9 0.20 1 76 . 14 SER H H 7.62 0.02 1 77 . 14 SER CA C 63.8 0.20 1 78 . 14 SER CB C 61.4 0.20 1 79 . 14 SER C C 173.9 0.20 1 80 . 15 THR N N 120.8 0.20 1 81 . 15 THR H H 7.89 0.02 1 82 . 15 THR CA C 65.2 0.20 1 83 . 15 THR HA H 4.73 0.02 1 84 . 15 THR CB C 68.1 0.20 1 85 . 15 THR C C 173.3 0.20 1 86 . 16 LEU N N 124.2 0.20 1 87 . 16 LEU H H 7.68 0.02 1 88 . 16 LEU CA C 56.8 0.20 1 89 . 16 LEU HA H 3.84 0.02 1 90 . 16 LEU CB C 44.3 0.20 1 91 . 16 LEU HB3 H 1.68 0.02 2 92 . 16 LEU C C 176.1 0.20 1 93 . 17 VAL N N 134.9 0.20 1 94 . 17 VAL H H 7.21 0.02 1 95 . 17 VAL CA C 57.6 0.20 1 96 . 17 VAL HA H 4.77 0.02 1 97 . 17 VAL CB C 33.7 0.20 1 98 . 17 VAL HB H 2.03 0.02 1 99 . 17 VAL C C 175.7 0.20 1 100 . 18 ASN N N 116.4 0.20 1 101 . 18 ASN H H 8.09 0.02 1 102 . 18 ASN CA C 54.0 0.20 1 103 . 18 ASN HA H 4.59 0.02 1 104 . 18 ASN CB C 40.0 0.20 1 105 . 18 ASN HB2 H 2.48 0.02 2 106 . 18 ASN HB3 H 2.77 0.02 2 107 . 18 ASN C C 175.7 0.20 1 108 . 19 ASN N N 113.0 0.20 1 109 . 19 ASN H H 7.50 0.02 1 110 . 19 ASN CA C 52.4 0.20 1 111 . 19 ASN HA H 4.85 0.02 1 112 . 19 ASN CB C 42.5 0.20 1 113 . 19 ASN C C 172.9 0.20 1 114 . 20 GLU N N 116.3 0.20 1 115 . 20 GLU H H 8.38 0.02 1 116 . 20 GLU CA C 55.0 0.20 1 117 . 20 GLU HA H 3.38 0.02 1 118 . 20 GLU CB C 39.8 0.20 1 119 . 20 GLU C C 176.8 0.20 1 120 . 21 THR N N 123.5 0.20 1 121 . 21 THR H H 9.31 0.02 1 122 . 21 THR CA C 68.3 0.20 1 123 . 21 THR C C 176.4 0.20 1 124 . 22 ILE N N 118.7 0.20 1 125 . 22 ILE H H 8.86 0.02 1 126 . 22 ILE CA C 64.9 0.20 1 127 . 22 ILE HA H 3.54 0.02 1 128 . 22 ILE CB C 36.5 0.20 1 129 . 22 ILE C C 176.2 0.20 1 130 . 23 ASP N N 123.9 0.20 1 131 . 23 ASP H H 6.73 0.02 1 132 . 23 ASP CA C 57.4 0.20 1 133 . 23 ASP HA H 4.25 0.02 1 134 . 23 ASP CB C 40.1 0.20 1 135 . 23 ASP C C 179.3 0.20 1 136 . 24 GLU N N 118.2 0.20 1 137 . 24 GLU H H 7.92 0.02 1 138 . 24 GLU CA C 58.3 0.20 1 139 . 24 GLU HA H 4.29 0.02 1 140 . 24 GLU CB C 29.5 0.20 1 141 . 24 GLU C C 180.1 0.20 1 142 . 25 ILE N N 118.7 0.20 1 143 . 25 ILE H H 7.99 0.02 1 144 . 25 ILE CA C 65.3 0.20 1 145 . 25 ILE HA H 3.51 0.02 1 146 . 25 ILE CB C 38.4 0.20 1 147 . 25 ILE C C 178.0 0.20 1 148 . 26 ALA N N 120.8 0.20 1 149 . 26 ALA H H 8.52 0.02 1 150 . 26 ALA CA C 54.6 0.20 1 151 . 26 ALA HA H 3.86 0.02 1 152 . 26 ALA CB C 19.4 0.20 1 153 . 26 ALA C C 179.7 0.20 1 154 . 27 ARG N N 117.9 0.20 1 155 . 27 ARG H H 7.65 0.02 1 156 . 27 ARG CA C 59.3 0.20 1 157 . 27 ARG HA H 4.24 0.02 1 158 . 27 ARG CB C 30.4 0.20 1 159 . 27 ARG C C 179.7 0.20 1 160 . 28 GLU N N 117.9 0.20 1 161 . 28 GLU H H 7.58 0.02 1 162 . 28 GLU CA C 57.1 0.20 1 163 . 28 GLU HA H 4.52 0.02 1 164 . 28 GLU CB C 30.1 0.20 1 165 . 28 GLU C C 177.6 0.20 1 166 . 29 ALA N N 118.0 0.20 1 167 . 29 ALA H H 7.50 0.02 1 168 . 29 ALA CA C 51.3 0.20 1 169 . 29 ALA HA H 4.52 0.02 1 170 . 29 ALA CB C 21.7 0.20 1 171 . 29 ALA HB H 1.65 0.02 1 172 . 29 ALA C C 177.0 0.20 1 173 . 30 GLY N N 106.6 0.20 1 174 . 30 GLY H H 7.73 0.02 1 175 . 30 GLY CA C 46.2 0.20 1 176 . 30 GLY HA2 H 4.28 0.02 2 177 . 30 GLY C C 175.8 0.20 1 178 . 31 VAL N N 111.1 0.20 1 179 . 31 VAL H H 7.53 0.02 1 180 . 31 VAL CA C 59.1 0.20 1 181 . 31 VAL HA H 5.08 0.02 1 182 . 31 VAL CB C 31.5 0.20 1 183 . 31 VAL HB H 2.13 0.02 1 184 . 31 VAL C C 175.6 0.20 1 185 . 32 GLU N N 122.7 0.20 1 186 . 32 GLU H H 8.53 0.02 1 187 . 32 GLU CA C 60.2 0.20 1 188 . 32 GLU HA H 3.75 0.02 1 189 . 32 GLU CB C 30.0 0.20 1 190 . 32 GLU HB3 H 2.05 0.02 2 191 . 32 GLU C C 177.6 0.20 1 192 . 33 GLU N N 118.6 0.20 1 193 . 33 GLU H H 8.74 0.02 1 194 . 33 GLU CA C 59.8 0.20 1 195 . 33 GLU HA H 3.99 0.02 1 196 . 33 GLU CB C 29.1 0.20 1 197 . 33 GLU C C 179.3 0.20 1 198 . 34 GLU N N 119.2 0.20 1 199 . 34 GLU H H 8.38 0.02 1 200 . 34 GLU CA C 59.1 0.20 1 201 . 34 GLU HA H 4.12 0.02 1 202 . 34 GLU CB C 30.0 0.20 1 203 . 34 GLU C C 179.5 0.20 1 204 . 35 VAL N N 118.1 0.20 1 205 . 35 VAL H H 7.96 0.02 1 206 . 35 VAL CA C 67.3 0.20 1 207 . 35 VAL HA H 3.53 0.02 1 208 . 35 VAL CB C 31.8 0.20 1 209 . 35 VAL C C 177.2 0.20 1 210 . 36 LYS N N 118.5 0.20 1 211 . 36 LYS H H 8.85 0.02 1 212 . 36 LYS CA C 59.2 0.20 1 213 . 36 LYS HA H 4.30 0.02 1 214 . 36 LYS CB C 32.9 0.20 1 215 . 36 LYS HB3 H 1.96 0.02 2 216 . 36 LYS C C 180.4 0.20 1 217 . 37 LYS N N 119.3 0.20 1 218 . 37 LYS H H 7.26 0.02 1 219 . 37 LYS CA C 59.4 0.20 1 220 . 37 LYS HA H 4.10 0.02 1 221 . 37 LYS CB C 32.9 0.20 1 222 . 37 LYS HB3 H 2.04 0.02 2 223 . 37 LYS C C 178.5 0.20 1 224 . 38 ILE N N 120.0 0.20 1 225 . 38 ILE H H 7.38 0.02 1 226 . 38 ILE CA C 64.6 0.20 1 227 . 38 ILE HA H 3.84 0.02 1 228 . 38 ILE CB C 38.4 0.20 1 229 . 38 ILE HB H 2.13 0.02 1 230 . 38 ILE C C 178.3 0.20 1 231 . 39 THR N N 119.4 0.20 1 232 . 39 THR H H 9.22 0.02 1 233 . 39 THR CA C 66.2 0.20 1 234 . 39 THR HA H 3.75 0.02 1 235 . 39 THR CB C 68.3 0.20 1 236 . 39 THR C C 176.3 0.20 1 237 . 40 LYS N N 121.2 0.20 1 238 . 40 LYS H H 7.90 0.02 1 239 . 40 LYS CA C 60.0 0.20 1 240 . 40 LYS HA H 4.09 0.02 1 241 . 40 LYS CB C 33.0 0.20 1 242 . 40 LYS C C 178.7 0.20 1 243 . 41 GLU N N 118.1 0.20 1 244 . 41 GLU H H 8.01 0.02 1 245 . 41 GLU CA C 59.7 0.20 1 246 . 41 GLU HA H 4.12 0.02 1 247 . 41 GLU CB C 29.6 0.20 1 248 . 41 GLU C C 180.1 0.20 1 249 . 42 ALA N N 121.8 0.20 1 250 . 42 ALA H H 8.95 0.02 1 251 . 42 ALA CA C 55.3 0.20 1 252 . 42 ALA HA H 4.33 0.02 1 253 . 42 ALA CB C 18.5 0.20 1 254 . 42 ALA C C 182.4 0.20 1 255 . 43 MET N N 119.7 0.20 1 256 . 43 MET H H 8.93 0.02 1 257 . 43 MET CA C 57.3 0.20 1 258 . 43 MET HA H 4.78 0.02 1 259 . 43 MET CB C 34.7 0.20 1 260 . 43 MET C C 178.9 0.20 1 261 . 44 GLU N N 116.5 0.20 1 262 . 44 GLU H H 8.24 0.02 1 263 . 44 GLU CA C 56.8 0.20 1 264 . 44 GLU HA H 4.38 0.02 1 265 . 44 GLU CB C 31.0 0.20 1 266 . 44 GLU HB3 H 2.30 0.02 2 267 . 44 GLU C C 177.9 0.20 1 268 . 45 GLY N N 106.9 0.20 1 269 . 45 GLY H H 7.86 0.02 1 270 . 45 GLY CA C 45.3 0.20 1 271 . 45 GLY HA2 H 4.28 0.02 2 272 . 45 GLY C C 174.6 0.20 1 273 . 46 LYS N N 118.5 0.20 1 274 . 46 LYS H H 8.25 0.02 1 275 . 46 LYS CA C 56.9 0.20 1 276 . 46 LYS HA H 4.32 0.02 1 277 . 46 LYS CB C 33.7 0.20 1 278 . 46 LYS HB3 H 1.80 0.02 2 279 . 46 LYS C C 175.6 0.20 1 280 . 47 LEU N N 115.2 0.20 1 281 . 47 LEU H H 6.81 0.02 1 282 . 47 LEU CA C 52.6 0.20 1 283 . 47 LEU HA H 4.76 0.02 1 284 . 47 LEU C C 176.0 0.20 1 285 . 48 ASN N N 122.5 0.20 1 286 . 48 ASN H H 8.65 0.02 1 287 . 48 ASN CA C 53.8 0.20 1 288 . 48 ASN CB C 40.4 0.20 1 289 . 48 ASN C C 175.7 0.20 1 290 . 49 PHE N N 128.7 0.20 1 291 . 49 PHE H H 9.64 0.02 1 292 . 49 PHE CA C 63.2 0.20 1 293 . 49 PHE HA H 3.97 0.02 1 294 . 49 PHE CB C 39.1 0.20 1 295 . 49 PHE C C 178.0 0.20 1 296 . 50 GLU N N 124.5 0.20 1 297 . 50 GLU H H 9.21 0.02 1 298 . 50 GLU CA C 60.2 0.20 1 299 . 50 GLU HA H 3.62 0.02 1 300 . 50 GLU CB C 28.7 0.20 1 301 . 50 GLU C C 178.9 0.20 1 302 . 51 GLN N N 118.1 0.20 1 303 . 51 GLN H H 8.84 0.02 1 304 . 51 GLN CA C 58.7 0.20 1 305 . 51 GLN HA H 4.03 0.02 1 306 . 51 GLN CB C 28.6 0.20 1 307 . 51 GLN C C 179.7 0.20 1 308 . 52 SER N N 115.9 0.20 1 309 . 52 SER H H 8.38 0.02 1 310 . 52 SER CA C 61.2 0.20 1 311 . 52 SER HA H 4.20 0.02 1 312 . 52 SER CB C 62.8 0.20 1 313 . 52 SER C C 177.5 0.20 1 314 . 53 LEU N N 132.5 0.20 1 315 . 53 LEU H H 8.44 0.02 1 316 . 53 LEU CA C 57.5 0.20 1 317 . 53 LEU HA H 4.06 0.02 1 318 . 53 LEU CB C 42.0 0.20 1 319 . 53 LEU C C 178.3 0.20 1 320 . 54 ARG N N 118.2 0.20 1 321 . 54 ARG H H 8.50 0.02 1 322 . 54 ARG CA C 60.0 0.20 1 323 . 54 ARG CB C 29.3 0.20 1 324 . 54 ARG C C 180.5 0.20 1 325 . 55 LYS N N 119.0 0.20 1 326 . 55 LYS H H 8.33 0.02 1 327 . 55 LYS CA C 58.7 0.20 1 328 . 55 LYS HA H 4.23 0.02 1 329 . 55 LYS CB C 32.6 0.20 1 330 . 55 LYS HB3 H 1.93 0.02 2 331 . 55 LYS C C 179.5 0.20 1 332 . 56 ARG N N 116.9 0.20 1 333 . 56 ARG H H 7.52 0.02 1 334 . 56 ARG CA C 60.5 0.20 1 335 . 56 ARG HA H 3.91 0.02 1 336 . 56 ARG CB C 32.0 0.20 1 337 . 56 ARG C C 177.2 0.20 1 338 . 57 VAL N N 115.3 0.20 1 339 . 57 VAL H H 8.48 0.02 1 340 . 57 VAL CA C 66.0 0.20 1 341 . 57 VAL HA H 3.52 0.02 1 342 . 57 VAL CB C 31.1 0.20 1 343 . 57 VAL HB H 2.04 0.02 1 344 . 57 VAL C C 178.8 0.20 1 345 . 58 SER N N 116.6 0.20 1 346 . 58 SER H H 7.98 0.02 1 347 . 58 SER CA C 62.2 0.20 1 348 . 58 SER HA H 4.44 0.02 1 349 . 58 SER C C 177.3 0.20 1 350 . 59 LEU N N 120.4 0.20 1 351 . 59 LEU H H 7.09 0.02 1 352 . 59 LEU CA C 56.2 0.20 1 353 . 59 LEU HA H 4.31 0.02 1 354 . 59 LEU CB C 42.1 0.20 1 355 . 59 LEU HB3 H 1.57 0.02 2 356 . 59 LEU C C 177.0 0.20 1 357 . 60 LEU N N 116.8 0.20 1 358 . 60 LEU H H 7.71 0.02 1 359 . 60 LEU CA C 52.8 0.20 1 360 . 60 LEU HA H 4.28 0.02 1 361 . 60 LEU CB C 41.6 0.20 1 362 . 60 LEU HB2 H 1.66 0.02 2 363 . 60 LEU HB3 H 1.93 0.02 2 364 . 60 LEU C C 174.9 0.20 1 365 . 61 LYS N N 117.7 0.20 1 366 . 61 LYS H H 6.77 0.02 1 367 . 61 LYS CA C 58.6 0.20 1 368 . 61 LYS HA H 3.33 0.02 1 369 . 61 LYS CB C 33.0 0.20 1 370 . 61 LYS HB3 H 1.80 0.02 2 371 . 61 LYS C C 176.3 0.20 1 372 . 62 ASP N N 118.9 0.20 1 373 . 62 ASP H H 8.71 0.02 1 374 . 62 ASP CA C 57.0 0.20 1 375 . 62 ASP HA H 4.31 0.02 1 376 . 62 ASP CB C 39.3 0.20 1 377 . 62 ASP HB2 H 2.99 0.02 2 378 . 62 ASP HB3 H 3.32 0.02 2 379 . 62 ASP C C 175.0 0.20 1 380 . 63 LEU N N 124.4 0.20 1 381 . 63 LEU H H 7.97 0.02 1 382 . 63 LEU CA C 53.6 0.20 1 383 . 63 LEU HA H 4.65 0.02 1 384 . 64 PRO CA C 63.1 0.20 1 385 . 64 PRO HA H 4.94 0.02 1 386 . 64 PRO CB C 33.6 0.20 1 387 . 64 PRO C C 179.6 0.20 1 388 . 65 ILE N N 124.6 0.20 1 389 . 65 ILE H H 8.62 0.02 1 390 . 65 ILE CA C 61.7 0.20 1 391 . 65 ILE HA H 4.03 0.02 1 392 . 65 ILE CB C 39.0 0.20 1 393 . 65 ILE HB H 1.66 0.02 1 394 . 65 ILE C C 177.1 0.20 1 395 . 66 GLU N N 122.1 0.20 1 396 . 66 GLU H H 9.40 0.02 1 397 . 66 GLU CA C 59.7 0.20 1 398 . 66 GLU HA H 4.27 0.02 1 399 . 66 GLU CB C 28.9 0.20 1 400 . 66 GLU C C 180.1 0.20 1 401 . 67 LYS N N 117.8 0.20 1 402 . 67 LYS H H 7.64 0.02 1 403 . 67 LYS CA C 58.7 0.20 1 404 . 67 LYS HA H 4.25 0.02 1 405 . 67 LYS CB C 32.7 0.20 1 406 . 67 LYS HB2 H 1.94 0.02 2 407 . 67 LYS HB3 H 2.20 0.02 2 408 . 67 LYS C C 178.6 0.20 1 409 . 68 VAL N N 120.5 0.20 1 410 . 68 VAL H H 7.28 0.02 1 411 . 68 VAL CA C 66.3 0.20 1 412 . 68 VAL HA H 3.54 0.02 1 413 . 68 VAL CB C 31.4 0.20 1 414 . 68 VAL C C 178.1 0.20 1 415 . 69 GLU N N 117.4 0.20 1 416 . 69 GLU H H 8.16 0.02 1 417 . 69 GLU CA C 59.5 0.20 1 418 . 69 GLU HA H 3.93 0.02 1 419 . 69 GLU CB C 29.6 0.20 1 420 . 69 GLU HB3 H 2.12 0.02 2 421 . 69 GLU C C 179.1 0.20 1 422 . 70 LYS N N 119.0 0.20 1 423 . 70 LYS H H 7.49 0.02 1 424 . 70 LYS CA C 59.4 0.20 1 425 . 70 LYS HA H 3.99 0.02 1 426 . 70 LYS CB C 33.4 0.20 1 427 . 70 LYS HB3 H 2.05 0.02 2 428 . 70 LYS C C 178.9 0.20 1 429 . 71 ALA N N 121.1 0.20 1 430 . 71 ALA H H 7.55 0.02 1 431 . 71 ALA CA C 54.6 0.20 1 432 . 71 ALA HA H 4.11 0.02 1 433 . 71 ALA CB C 19.5 0.20 1 434 . 71 ALA HB H 1.58 0.02 1 435 . 71 ALA C C 179.9 0.20 1 436 . 72 ILE N N 113.4 0.20 1 437 . 72 ILE H H 8.04 0.02 1 438 . 72 ILE CA C 63.2 0.20 1 439 . 72 ILE HA H 3.92 0.02 1 440 . 72 ILE CB C 37.7 0.20 1 441 . 72 ILE HB H 2.21 0.02 1 442 . 72 ILE C C 178.8 0.20 1 443 . 73 LYS N N 120.9 0.20 1 444 . 73 LYS H H 7.62 0.02 1 445 . 73 LYS CA C 58.5 0.20 1 446 . 73 LYS HA H 4.17 0.02 1 447 . 73 LYS CB C 32.8 0.20 1 448 . 73 LYS HB3 H 2.05 0.02 2 449 . 73 LYS C C 177.6 0.20 1 450 . 74 ARG N N 115.1 0.20 1 451 . 74 ARG H H 7.47 0.02 1 452 . 74 ARG CA C 57.2 0.20 1 453 . 74 ARG HA H 4.30 0.02 1 454 . 74 ARG CB C 31.4 0.20 1 455 . 74 ARG C C 176.9 0.20 1 456 . 75 ILE N N 120.3 0.20 1 457 . 75 ILE H H 7.41 0.02 1 458 . 75 ILE CA C 61.7 0.20 1 459 . 75 ILE HA H 3.84 0.02 1 460 . 75 ILE CB C 36.8 0.20 1 461 . 75 ILE HB H 2.17 0.02 1 462 . 75 ILE C C 176.4 0.20 1 463 . 76 THR N N 121.9 0.20 1 464 . 76 THR H H 8.65 0.02 1 465 . 76 THR CA C 57.7 0.20 1 466 . 76 THR HA H 5.01 0.02 1 467 . 77 PRO CA C 62.7 0.20 1 468 . 77 PRO HA H 4.70 0.02 1 469 . 77 PRO CB C 32.5 0.20 1 470 . 77 PRO HB3 H 2.08 0.02 2 471 . 77 PRO C C 175.3 0.20 1 472 . 78 THR N N 125.3 0.20 1 473 . 78 THR H H 8.76 0.02 1 474 . 78 THR CA C 62.4 0.20 1 475 . 78 THR HA H 3.91 0.02 1 476 . 78 THR CB C 69.6 0.20 1 477 . 78 THR HB H 3.67 0.02 1 478 . 78 THR C C 173.2 0.20 1 479 . 79 GLU N N 128.9 0.20 1 480 . 79 GLU H H 8.94 0.02 1 481 . 79 GLU CA C 58.1 0.20 1 482 . 79 GLU HA H 4.22 0.02 1 483 . 79 GLU CB C 29.8 0.20 1 484 . 79 GLU HB3 H 2.35 0.02 2 485 . 79 GLU C C 176.3 0.20 1 486 . 80 GLY N N 112.9 0.20 1 487 . 80 GLY H H 8.97 0.02 1 488 . 80 GLY CA C 45.3 0.20 1 489 . 80 GLY HA3 H 3.95 0.02 2 490 . 80 GLY HA2 H 4.45 0.02 2 491 . 80 GLY C C 177.0 0.20 1 492 . 81 ALA N N 125.6 0.20 1 493 . 81 ALA H H 8.50 0.02 1 494 . 81 ALA CA C 56.7 0.20 1 495 . 81 ALA HA H 3.71 0.02 1 496 . 81 ALA CB C 19.3 0.20 1 497 . 81 ALA HB H 1.46 0.02 1 498 . 81 ALA C C 178.3 0.20 1 499 . 82 GLU N N 117.7 0.20 1 500 . 82 GLU H H 9.22 0.02 1 501 . 82 GLU CA C 60.6 0.20 1 502 . 82 GLU HA H 3.83 0.02 1 503 . 82 GLU CB C 29.3 0.20 1 504 . 82 GLU C C 179.4 0.20 1 505 . 83 GLU N N 119.1 0.20 1 506 . 83 GLU H H 8.96 0.02 1 507 . 83 GLU CA C 59.5 0.20 1 508 . 83 GLU HA H 3.97 0.02 1 509 . 83 GLU CB C 29.8 0.20 1 510 . 83 GLU HB3 H 1.79 0.02 2 511 . 83 GLU C C 179.5 0.20 1 512 . 84 THR N N 117.1 0.20 1 513 . 84 THR H H 8.08 0.02 1 514 . 84 THR CA C 67.9 0.20 1 515 . 84 THR HA H 4.59 0.02 1 516 . 84 THR CB C 76.6 0.20 1 517 . 84 THR HB H 4.46 0.02 1 518 . 84 THR C C 176.0 0.20 1 519 . 85 ILE N N 121.2 0.20 1 520 . 85 ILE H H 8.40 0.02 1 521 . 85 ILE CA C 64.4 0.20 1 522 . 85 ILE HA H 3.65 0.02 1 523 . 85 ILE CB C 36.5 0.20 1 524 . 85 ILE C C 177.6 0.20 1 525 . 86 LYS N N 118.7 0.20 1 526 . 86 LYS H H 7.74 0.02 1 527 . 86 LYS CA C 59.8 0.20 1 528 . 86 LYS HA H 4.03 0.02 1 529 . 86 LYS CB C 32.6 0.20 1 530 . 86 LYS HB3 H 2.01 0.02 2 531 . 86 LYS C C 179.5 0.20 1 532 . 87 GLU N N 119.2 0.20 1 533 . 87 GLU H H 7.79 0.02 1 534 . 87 GLU CA C 58.1 0.20 1 535 . 87 GLU HA H 4.45 0.02 1 536 . 87 GLU CB C 29.0 0.20 1 537 . 87 GLU HB2 H 2.34 0.02 2 538 . 87 GLU HB3 H 2.75 0.02 2 539 . 87 GLU C C 179.3 0.20 1 540 . 88 LEU N N 120.1 0.20 1 541 . 88 LEU H H 8.61 0.02 1 542 . 88 LEU CA C 58.0 0.20 1 543 . 88 LEU HA H 3.88 0.02 1 544 . 88 LEU CB C 41.6 0.20 1 545 . 88 LEU C C 180.2 0.20 1 546 . 89 LYS N N 119.8 0.20 1 547 . 89 LYS H H 8.47 0.02 1 548 . 89 LYS CA C 59.8 0.20 1 549 . 89 LYS HA H 4.48 0.02 1 550 . 89 LYS CB C 31.6 0.20 1 551 . 89 LYS C C 181.7 0.20 1 552 . 90 ASN N N 120.9 0.20 1 553 . 90 ASN H H 8.10 0.02 1 554 . 90 ASN CA C 55.6 0.20 1 555 . 90 ASN HA H 4.65 0.02 1 556 . 90 ASN CB C 38.6 0.20 1 557 . 90 ASN HB3 H 3.13 0.02 2 558 . 90 ASN C C 177.3 0.20 1 559 . 91 ARG N N 117.9 0.20 1 560 . 91 ARG H H 7.86 0.02 1 561 . 91 ARG CA C 56.4 0.20 1 562 . 91 ARG HA H 4.46 0.02 1 563 . 91 ARG CB C 31.0 0.20 1 564 . 91 ARG HB2 H 1.87 0.02 2 565 . 91 ARG HB3 H 2.34 0.02 2 566 . 91 ARG C C 175.9 0.20 1 567 . 92 GLY N N 106.6 0.20 1 568 . 92 GLY H H 7.95 0.02 1 569 . 92 GLY CA C 45.5 0.20 1 570 . 92 GLY HA2 H 3.91 0.02 2 571 . 92 GLY C C 174.7 0.20 1 572 . 93 TYR N N 118.7 0.20 1 573 . 93 TYR H H 8.04 0.02 1 574 . 93 TYR CA C 58.0 0.20 1 575 . 93 TYR HA H 4.56 0.02 1 576 . 93 TYR CB C 38.0 0.20 1 577 . 93 TYR HB3 H 2.71 0.02 2 578 . 93 TYR C C 177.0 0.20 1 579 . 94 VAL N N 123.8 0.20 1 580 . 94 VAL H H 8.88 0.02 1 581 . 94 VAL CA C 62.6 0.20 1 582 . 94 VAL HA H 4.26 0.02 1 583 . 94 VAL CB C 32.9 0.20 1 584 . 94 VAL C C 175.9 0.20 1 585 . 95 VAL N N 126.8 0.20 1 586 . 95 VAL H H 9.87 0.02 1 587 . 95 VAL CA C 60.8 0.20 1 588 . 95 VAL HA H 5.20 0.02 1 589 . 95 VAL CB C 33.9 0.20 1 590 . 95 VAL C C 174.7 0.20 1 591 . 96 ALA N N 129.3 0.20 1 592 . 96 ALA H H 9.21 0.02 1 593 . 96 ALA CA C 49.3 0.20 1 594 . 96 ALA HA H 5.82 0.02 1 595 . 96 ALA CB C 26.7 0.20 1 596 . 96 ALA HB H 1.57 0.02 1 597 . 96 ALA C C 174.7 0.20 1 598 . 97 VAL N N 118.9 0.20 1 599 . 97 VAL H H 8.30 0.02 1 600 . 97 VAL CA C 57.9 0.20 1 601 . 97 VAL HA H 2.53 0.02 1 602 . 97 VAL CB C 35.6 0.20 1 603 . 97 VAL HB H 1.23 0.02 1 604 . 97 VAL C C 172.0 0.20 1 605 . 98 VAL N N 125.1 0.20 1 606 . 98 VAL H H 8.83 0.02 1 607 . 98 VAL CA C 58.8 0.20 1 608 . 98 VAL HA H 5.40 0.02 1 609 . 98 VAL CB C 35.0 0.20 1 610 . 98 VAL C C 172.5 0.20 1 611 . 99 SER N N 118.3 0.20 1 612 . 99 SER H H 8.49 0.02 1 613 . 99 SER CA C 55.7 0.20 1 614 . 99 SER C C 173.0 0.20 1 615 . 100 GLY N N 118.0 0.20 1 616 . 100 GLY H H 9.12 0.02 1 617 . 100 GLY CA C 45.3 0.20 1 618 . 100 GLY C C 174.1 0.20 1 619 . 101 GLY N N 108.0 0.20 1 620 . 101 GLY H H 8.55 0.02 1 621 . 101 GLY CA C 43.1 0.20 1 622 . 101 GLY C C 174.3 0.20 1 623 . 102 PHE N N 117.1 0.20 1 624 . 102 PHE H H 7.14 0.02 1 625 . 102 PHE CA C 55.6 0.20 1 626 . 102 PHE HA H 5.45 0.02 1 627 . 102 PHE CB C 43.1 0.20 1 628 . 102 PHE HB2 H 2.52 0.02 2 629 . 102 PHE HB3 H 3.84 0.02 2 630 . 102 PHE C C 176.9 0.20 1 631 . 103 ASP N N 128.4 0.20 1 632 . 103 ASP H H 9.58 0.02 1 633 . 103 ASP CA C 57.1 0.20 1 634 . 103 ASP HA H 3.88 0.02 1 635 . 103 ASP CB C 39.2 0.20 1 636 . 103 ASP C C 177.2 0.20 1 637 . 104 ILE N N 118.1 0.20 1 638 . 104 ILE H H 8.14 0.02 1 639 . 104 ILE CA C 63.8 0.20 1 640 . 104 ILE HA H 4.11 0.02 1 641 . 104 ILE CB C 38.3 0.20 1 642 . 104 ILE HB H 1.97 0.02 1 643 . 104 ILE C C 176.2 0.20 1 644 . 105 ALA N N 121.0 0.20 1 645 . 105 ALA H H 7.26 0.02 1 646 . 105 ALA CA C 53.3 0.20 1 647 . 105 ALA HA H 4.57 0.02 1 648 . 105 ALA CB C 20.9 0.20 1 649 . 105 ALA HB H 1.64 0.02 1 650 . 105 ALA C C 178.4 0.20 1 651 . 106 VAL N N 117.0 0.20 1 652 . 106 VAL H H 7.55 0.02 1 653 . 106 VAL CA C 64.7 0.20 1 654 . 106 VAL HA H 2.96 0.02 1 655 . 106 VAL CB C 31.8 0.20 1 656 . 106 VAL C C 178.4 0.20 1 657 . 107 ASN N N 118.2 0.20 1 658 . 107 ASN H H 9.03 0.02 1 659 . 107 ASN CA C 55.5 0.20 1 660 . 107 ASN HA H 4.38 0.02 1 661 . 107 ASN CB C 37.5 0.20 1 662 . 107 ASN HB3 H 2.84 0.02 2 663 . 107 ASN C C 178.2 0.20 1 664 . 108 LYS N N 118.2 0.20 1 665 . 108 LYS H H 6.94 0.02 1 666 . 108 LYS CA C 58.4 0.20 1 667 . 108 LYS HA H 4.24 0.02 1 668 . 108 LYS CB C 32.5 0.20 1 669 . 108 LYS HB3 H 2.03 0.02 2 670 . 108 LYS C C 179.5 0.20 1 671 . 109 ILE N N 119.5 0.20 1 672 . 109 ILE H H 7.11 0.02 1 673 . 109 ILE CA C 60.9 0.20 1 674 . 109 ILE HA H 4.06 0.02 1 675 . 109 ILE CB C 36.7 0.20 1 676 . 109 ILE C C 177.4 0.20 1 677 . 110 LYS N N 122.7 0.20 1 678 . 110 LYS H H 8.70 0.02 1 679 . 110 LYS CA C 59.9 0.20 1 680 . 110 LYS HA H 3.79 0.02 1 681 . 110 LYS CB C 32.3 0.20 1 682 . 110 LYS C C 178.4 0.20 1 683 . 111 GLU N N 116.9 0.20 1 684 . 111 GLU H H 7.66 0.02 1 685 . 111 GLU CA C 58.4 0.20 1 686 . 111 GLU HA H 4.20 0.02 1 687 . 111 GLU CB C 30.0 0.20 1 688 . 111 GLU HB3 H 2.16 0.02 2 689 . 111 GLU C C 178.8 0.20 1 690 . 112 LYS N N 119.3 0.20 1 691 . 112 LYS H H 7.71 0.02 1 692 . 112 LYS CA C 58.5 0.20 1 693 . 112 LYS HA H 4.18 0.02 1 694 . 112 LYS CB C 33.5 0.20 1 695 . 112 LYS HB3 H 2.10 0.02 2 696 . 112 LYS C C 178.3 0.20 1 697 . 113 LEU N N 113.2 0.20 1 698 . 113 LEU H H 8.13 0.02 1 699 . 113 LEU CA C 54.1 0.20 1 700 . 113 LEU HA H 4.47 0.02 1 701 . 113 LEU CB C 42.6 0.20 1 702 . 113 LEU HB3 H 1.64 0.02 2 703 . 113 LEU C C 176.8 0.20 1 704 . 114 GLY N N 108.5 0.20 1 705 . 114 GLY H H 7.61 0.02 1 706 . 114 GLY CA C 46.8 0.20 1 707 . 114 GLY HA2 H 3.96 0.02 2 708 . 114 GLY C C 175.6 0.20 1 709 . 115 LEU N N 116.3 0.20 1 710 . 115 LEU H H 7.65 0.02 1 711 . 115 LEU CA C 54.7 0.20 1 712 . 115 LEU HA H 4.16 0.02 1 713 . 115 LEU CB C 42.0 0.20 1 714 . 115 LEU C C 176.2 0.20 1 715 . 116 ASP N N 119.4 0.20 1 716 . 116 ASP H H 8.45 0.02 1 717 . 116 ASP CA C 57.6 0.20 1 718 . 116 ASP HA H 4.44 0.02 1 719 . 116 ASP CB C 43.9 0.20 1 720 . 116 ASP HB2 H 2.58 0.02 2 721 . 116 ASP HB3 H 2.84 0.02 2 722 . 116 ASP C C 176.2 0.20 1 723 . 117 TYR N N 111.3 0.20 1 724 . 117 TYR H H 7.33 0.02 1 725 . 117 TYR CA C 56.9 0.20 1 726 . 117 TYR HA H 4.72 0.02 1 727 . 117 TYR CB C 45.4 0.20 1 728 . 117 TYR C C 174.9 0.20 1 729 . 118 ALA N N 122.6 0.20 1 730 . 118 ALA H H 8.60 0.02 1 731 . 118 ALA CA C 51.3 0.20 1 732 . 118 ALA HA H 5.36 0.02 1 733 . 118 ALA CB C 22.8 0.20 1 734 . 118 ALA HB H 1.11 0.02 1 735 . 118 ALA C C 174.9 0.20 1 736 . 119 PHE N N 121.4 0.20 1 737 . 119 PHE H H 8.18 0.02 1 738 . 119 PHE CA C 56.9 0.20 1 739 . 119 PHE HA H 4.93 0.02 1 740 . 119 PHE CB C 43.8 0.20 1 741 . 119 PHE HB3 H 3.02 0.02 2 742 . 119 PHE C C 173.7 0.20 1 743 . 120 ALA N N 123.3 0.20 1 744 . 120 ALA H H 8.43 0.02 1 745 . 120 ALA CA C 50.6 0.20 1 746 . 120 ALA HA H 5.76 0.02 1 747 . 120 ALA CB C 21.7 0.20 1 748 . 120 ALA HB H 1.22 0.02 1 749 . 120 ALA C C 176.9 0.20 1 750 . 121 ASN N N 117.0 0.20 1 751 . 121 ASN H H 7.95 0.02 1 752 . 121 ASN CA C 53.4 0.20 1 753 . 121 ASN HA H 5.30 0.02 1 754 . 121 ASN CB C 39.8 0.20 1 755 . 121 ASN HB3 H 2.88 0.02 2 756 . 121 ASN C C 173.7 0.20 1 757 . 122 ARG N N 117.1 0.20 1 758 . 122 ARG H H 9.30 0.02 1 759 . 122 ARG CA C 55.3 0.20 1 760 . 122 ARG HA H 5.06 0.02 1 761 . 122 ARG CB C 33.6 0.20 1 762 . 122 ARG C C 175.4 0.20 1 763 . 123 LEU N N 124.5 0.20 1 764 . 123 LEU H H 8.84 0.02 1 765 . 123 LEU CA C 53.8 0.20 1 766 . 123 LEU HA H 4.26 0.02 1 767 . 123 LEU CB C 42.9 0.20 1 768 . 123 LEU HB3 H 1.34 0.02 2 769 . 123 LEU C C 176.8 0.20 1 770 . 124 ILE N N 123.0 0.20 1 771 . 124 ILE H H 7.08 0.02 1 772 . 124 ILE CA C 60.5 0.20 1 773 . 124 ILE HA H 4.21 0.02 1 774 . 124 ILE CB C 35.1 0.20 1 775 . 124 ILE C C 176.0 0.20 1 776 . 125 VAL N N 130.2 0.20 1 777 . 125 VAL H H 8.51 0.02 1 778 . 125 VAL CA C 60.6 0.20 1 779 . 125 VAL HA H 4.69 0.02 1 780 . 125 VAL CB C 35.2 0.20 1 781 . 125 VAL HB H 1.93 0.02 1 782 . 125 VAL C C 175.2 0.20 1 783 . 126 LYS N N 127.1 0.20 1 784 . 126 LYS H H 8.98 0.02 1 785 . 126 LYS CA C 55.7 0.20 1 786 . 126 LYS HA H 4.60 0.02 1 787 . 126 LYS CB C 36.3 0.20 1 788 . 126 LYS HB3 H 1.70 0.02 2 789 . 126 LYS C C 176.1 0.20 1 790 . 127 ASP N N 127.6 0.20 1 791 . 127 ASP H H 9.46 0.02 1 792 . 127 ASP CA C 55.6 0.20 1 793 . 127 ASP HA H 4.37 0.02 1 794 . 127 ASP CB C 39.9 0.20 1 795 . 127 ASP HB2 H 2.73 0.02 2 796 . 127 ASP HB3 H 3.02 0.02 2 797 . 127 ASP C C 176.1 0.20 1 798 . 128 GLY N N 101.7 0.20 1 799 . 128 GLY H H 8.51 0.02 1 800 . 128 GLY CA C 45.5 0.20 1 801 . 128 GLY C C 174.5 0.20 1 802 . 129 LYS N N 120.4 0.20 1 803 . 129 LYS H H 7.89 0.02 1 804 . 129 LYS CA C 54.0 0.20 1 805 . 129 LYS HA H 5.17 0.02 1 806 . 129 LYS CB C 37.0 0.20 1 807 . 129 LYS HB2 H 0.64 0.02 2 808 . 129 LYS HB3 H 1.47 0.02 2 809 . 129 LYS C C 175.3 0.20 1 810 . 130 LEU N N 120.9 0.20 1 811 . 130 LEU H H 8.71 0.02 1 812 . 130 LEU CA C 55.5 0.20 1 813 . 130 LEU HA H 4.60 0.02 1 814 . 130 LEU CB C 40.4 0.20 1 815 . 130 LEU HB3 H 2.04 0.02 2 816 . 130 LEU C C 180.1 0.20 1 817 . 131 THR N N 113.6 0.20 1 818 . 131 THR H H 8.25 0.02 1 819 . 131 THR CA C 62.5 0.20 1 820 . 131 THR HA H 4.54 0.02 1 821 . 131 THR CB C 69.6 0.20 1 822 . 131 THR HB H 5.11 0.02 1 823 . 131 THR C C 176.8 0.20 1 824 . 132 GLY N N 109.0 0.20 1 825 . 132 GLY H H 8.91 0.02 1 826 . 132 GLY CA C 44.6 0.20 1 827 . 132 GLY HA3 H 3.54 0.02 2 828 . 132 GLY HA2 H 4.41 0.02 2 829 . 132 GLY C C 172.0 0.20 1 830 . 133 ASP N N 119.6 0.20 1 831 . 133 ASP H H 7.57 0.02 1 832 . 133 ASP CA C 53.0 0.20 1 833 . 133 ASP HA H 5.12 0.02 1 834 . 133 ASP CB C 44.3 0.20 1 835 . 133 ASP C C 175.1 0.20 1 836 . 134 VAL N N 120.0 0.20 1 837 . 134 VAL H H 8.57 0.02 1 838 . 134 VAL CA C 58.8 0.20 1 839 . 134 VAL HA H 5.17 0.02 1 840 . 134 VAL CB C 35.9 0.20 1 841 . 134 VAL C C 171.9 0.20 1 842 . 135 GLU N N 123.1 0.20 1 843 . 135 GLU H H 8.54 0.02 1 844 . 135 GLU CA C 54.1 0.20 1 845 . 135 GLU HA H 4.95 0.02 1 846 . 135 GLU CB C 34.4 0.20 1 847 . 135 GLU HB2 H 1.98 0.02 2 848 . 135 GLU HB3 H 2.20 0.02 2 849 . 135 GLU C C 174.1 0.20 1 850 . 136 GLY N N 107.3 0.20 1 851 . 136 GLY H H 8.40 0.02 1 852 . 136 GLY CA C 45.1 0.20 1 853 . 136 GLY HA3 H 4.08 0.02 2 854 . 136 GLY HA2 H 5.48 0.02 2 855 . 136 GLY C C 173.5 0.20 1 856 . 137 GLU N N 115.5 0.20 1 857 . 137 GLU H H 8.64 0.02 1 858 . 137 GLU CA C 55.9 0.20 1 859 . 137 GLU HA H 4.62 0.02 1 860 . 137 GLU CB C 31.2 0.20 1 861 . 137 GLU C C 176.4 0.20 1 862 . 138 VAL N N 122.9 0.20 1 863 . 138 VAL H H 8.91 0.02 1 864 . 138 VAL CA C 59.3 0.20 1 865 . 138 VAL HA H 4.33 0.02 1 866 . 138 VAL CB C 30.8 0.20 1 867 . 138 VAL C C 176.2 0.20 1 868 . 139 LEU N N 121.2 0.20 1 869 . 139 LEU H H 7.79 0.02 1 870 . 139 LEU CA C 55.9 0.20 1 871 . 139 LEU C C 176.6 0.20 1 872 . 140 LYS N N 115.7 0.20 1 873 . 140 LYS H H 7.99 0.02 1 874 . 140 LYS CA C 55.8 0.20 1 875 . 140 LYS HA H 4.56 0.02 1 876 . 140 LYS CB C 33.8 0.20 1 877 . 140 LYS C C 178.8 0.20 1 878 . 141 GLU N N 122.1 0.20 1 879 . 141 GLU H H 9.01 0.02 1 880 . 141 GLU CA C 59.4 0.20 1 881 . 141 GLU HA H 4.17 0.02 1 882 . 141 GLU CB C 30.2 0.20 1 883 . 141 GLU C C 177.7 0.20 1 884 . 142 ASN N N 114.6 0.20 1 885 . 142 ASN H H 8.30 0.02 1 886 . 142 ASN CA C 52.2 0.20 1 887 . 142 ASN HA H 4.98 0.02 1 888 . 142 ASN CB C 38.5 0.20 1 889 . 142 ASN HB3 H 3.02 0.02 2 890 . 142 ASN C C 177.4 0.20 1 891 . 143 ALA N N 121.4 0.20 1 892 . 143 ALA H H 7.66 0.02 1 893 . 143 ALA CA C 56.0 0.20 1 894 . 143 ALA HA H 4.04 0.02 1 895 . 143 ALA CB C 21.2 0.20 1 896 . 143 ALA HB H 1.67 0.02 1 897 . 143 ALA C C 180.1 0.20 1 898 . 144 LYS N N 114.3 0.20 1 899 . 144 LYS H H 8.30 0.02 1 900 . 144 LYS CA C 61.9 0.20 1 901 . 144 LYS HA H 3.77 0.02 1 902 . 144 LYS CB C 32.0 0.20 1 903 . 144 LYS C C 178.6 0.20 1 904 . 145 GLY N N 105.6 0.20 1 905 . 145 GLY H H 7.77 0.02 1 906 . 145 GLY CA C 47.5 0.20 1 907 . 145 GLY HA2 H 3.61 0.02 2 908 . 145 GLY C C 175.1 0.20 1 909 . 146 GLU N N 121.6 0.20 1 910 . 146 GLU H H 7.52 0.02 1 911 . 146 GLU CA C 58.8 0.20 1 912 . 146 GLU HA H 4.12 0.02 1 913 . 146 GLU CB C 29.1 0.20 1 914 . 146 GLU C C 180.1 0.20 1 915 . 147 ILE N N 121.6 0.20 1 916 . 147 ILE H H 7.95 0.02 1 917 . 147 ILE CA C 63.3 0.20 1 918 . 147 ILE HA H 3.39 0.02 1 919 . 147 ILE CB C 38.5 0.20 1 920 . 147 ILE C C 177.0 0.20 1 921 . 148 LEU N N 121.2 0.20 1 922 . 148 LEU H H 7.65 0.02 1 923 . 148 LEU CA C 59.9 0.20 1 924 . 148 LEU HA H 3.67 0.02 1 925 . 148 LEU CB C 41.9 0.20 1 926 . 148 LEU HB2 H 2.04 0.02 2 927 . 148 LEU HB3 H 2.24 0.02 2 928 . 148 LEU C C 177.8 0.20 1 929 . 149 GLU N N 116.0 0.20 1 930 . 149 GLU H H 7.59 0.02 1 931 . 149 GLU CA C 59.6 0.20 1 932 . 149 GLU HA H 3.80 0.02 1 933 . 149 GLU CB C 30.5 0.20 1 934 . 149 GLU C C 178.2 0.20 1 935 . 150 LYS N N 120.7 0.20 1 936 . 150 LYS H H 8.00 0.02 1 937 . 150 LYS CA C 59.5 0.20 1 938 . 150 LYS HA H 4.01 0.02 1 939 . 150 LYS CB C 32.9 0.20 1 940 . 150 LYS HB3 H 1.91 0.02 2 941 . 150 LYS C C 179.2 0.20 1 942 . 151 ILE N N 118.0 0.20 1 943 . 151 ILE H H 8.24 0.02 1 944 . 151 ILE CA C 64.5 0.20 1 945 . 151 ILE HA H 3.40 0.02 1 946 . 151 ILE CB C 38.0 0.20 1 947 . 151 ILE C C 177.8 0.20 1 948 . 152 ALA N N 121.2 0.20 1 949 . 152 ALA H H 8.07 0.02 1 950 . 152 ALA CA C 56.1 0.20 1 951 . 152 ALA HA H 3.73 0.02 1 952 . 152 ALA CB C 17.0 0.20 1 953 . 152 ALA HB H 1.47 0.02 1 954 . 152 ALA C C 179.7 0.20 1 955 . 153 LYS N N 117.2 0.20 1 956 . 153 LYS H H 8.06 0.02 1 957 . 153 LYS CA C 59.0 0.20 1 958 . 153 LYS HA H 4.16 0.02 1 959 . 153 LYS CB C 32.4 0.20 1 960 . 153 LYS C C 180.6 0.20 1 961 . 154 ILE N N 121.2 0.20 1 962 . 154 ILE H H 7.99 0.02 1 963 . 154 ILE CA C 65.2 0.20 1 964 . 154 ILE HA H 3.81 0.02 1 965 . 154 ILE CB C 39.1 0.20 1 966 . 154 ILE C C 178.9 0.20 1 967 . 155 GLU N N 115.5 0.20 1 968 . 155 GLU H H 7.93 0.02 1 969 . 155 GLU CA C 56.1 0.20 1 970 . 155 GLU HA H 4.25 0.02 1 971 . 155 GLU CB C 31.4 0.20 1 972 . 155 GLU HB2 H 1.72 0.02 2 973 . 155 GLU HB3 H 2.42 0.02 2 974 . 155 GLU C C 176.8 0.20 1 975 . 156 GLY N N 111.0 0.20 1 976 . 156 GLY H H 7.89 0.02 1 977 . 156 GLY CA C 46.7 0.20 1 978 . 156 GLY HA2 H 4.00 0.02 2 979 . 156 GLY C C 174.7 0.20 1 980 . 157 ILE N N 122.6 0.20 1 981 . 157 ILE H H 8.58 0.02 1 982 . 157 ILE CA C 60.0 0.20 1 983 . 157 ILE HA H 4.07 0.02 1 984 . 157 ILE CB C 42.0 0.20 1 985 . 157 ILE HB H 1.40 0.02 1 986 . 157 ILE C C 175.3 0.20 1 987 . 158 ASN N N 126.5 0.20 1 988 . 158 ASN H H 8.87 0.02 1 989 . 158 ASN CA C 52.9 0.20 1 990 . 158 ASN HA H 4.63 0.02 1 991 . 158 ASN CB C 39.0 0.20 1 992 . 158 ASN HB2 H 2.83 0.02 2 993 . 158 ASN HB3 H 3.10 0.02 2 994 . 158 ASN C C 177.8 0.20 1 995 . 159 LEU N N 124.2 0.20 1 996 . 159 LEU H H 8.81 0.02 1 997 . 159 LEU CA C 58.0 0.20 1 998 . 159 LEU HA H 4.00 0.02 1 999 . 159 LEU CB C 40.3 0.20 1 1000 . 159 LEU HB3 H 1.79 0.02 2 1001 . 159 LEU C C 179.9 0.20 1 1002 . 160 GLU N N 118.2 0.20 1 1003 . 160 GLU H H 9.31 0.02 1 1004 . 160 GLU CA C 58.9 0.20 1 1005 . 160 GLU HA H 4.17 0.02 1 1006 . 160 GLU CB C 28.6 0.20 1 1007 . 160 GLU C C 177.3 0.20 1 1008 . 161 ASP N N 121.2 0.20 1 1009 . 161 ASP H H 8.03 0.02 1 1010 . 161 ASP CA C 54.4 0.20 1 1011 . 161 ASP HA H 5.03 0.02 1 1012 . 161 ASP CB C 41.5 0.20 1 1013 . 161 ASP HB2 H 2.92 0.02 2 1014 . 161 ASP HB3 H 3.21 0.02 2 1015 . 161 ASP C C 174.3 0.20 1 1016 . 162 THR N N 106.7 0.20 1 1017 . 162 THR H H 7.25 0.02 1 1018 . 162 THR CA C 59.7 0.20 1 1019 . 162 THR HA H 5.71 0.02 1 1020 . 162 THR CB C 73.3 0.20 1 1021 . 162 THR HB H 4.04 0.02 1 1022 . 162 THR C C 175.1 0.20 1 1023 . 163 VAL N N 124.2 0.20 1 1024 . 163 VAL H H 8.85 0.02 1 1025 . 163 VAL CA C 60.0 0.20 1 1026 . 163 VAL HA H 5.08 0.02 1 1027 . 163 VAL CB C 35.6 0.20 1 1028 . 163 VAL HB H 1.90 0.02 1 1029 . 163 VAL C C 173.5 0.20 1 1030 . 164 ALA N N 128.1 0.20 1 1031 . 164 ALA H H 8.51 0.02 1 1032 . 164 ALA CA C 49.7 0.20 1 1033 . 164 ALA HA H 5.54 0.02 1 1034 . 164 ALA CB C 23.6 0.20 1 1035 . 164 ALA HB H 1.35 0.02 1 1036 . 164 ALA C C 175.5 0.20 1 1037 . 165 VAL N N 121.2 0.20 1 1038 . 165 VAL H H 8.33 0.02 1 1039 . 165 VAL CA C 59.9 0.20 1 1040 . 165 VAL HA H 5.56 0.02 1 1041 . 165 VAL CB C 34.5 0.20 1 1042 . 165 VAL HB H 1.93 0.02 1 1043 . 165 VAL C C 175.4 0.20 1 1044 . 166 GLY N N 110.4 0.20 1 1045 . 166 GLY H H 8.28 0.02 1 1046 . 166 GLY CA C 45.8 0.20 1 1047 . 166 GLY C C 170.7 0.20 1 1048 . 167 ASP N N 115.4 0.20 1 1049 . 167 ASP H H 7.66 0.02 1 1050 . 167 ASP CA C 54.4 0.20 1 1051 . 167 ASP HA H 5.12 0.02 1 1052 . 167 ASP CB C 46.0 0.20 1 1053 . 167 ASP C C 174.5 0.20 1 1054 . 168 GLY N N 109.4 0.20 1 1055 . 168 GLY H H 9.01 0.02 1 1056 . 168 GLY CA C 44.0 0.20 1 1057 . 168 GLY C C 175.4 0.20 1 1058 . 169 ALA N N 119.3 0.20 1 1059 . 169 ALA H H 8.97 0.02 1 1060 . 169 ALA CA C 54.9 0.20 1 1061 . 169 ALA CB C 19.6 0.20 1 1062 . 169 ALA C C 179.5 0.20 1 1063 . 170 ASN N N 112.0 0.20 1 1064 . 170 ASN H H 8.04 0.02 1 1065 . 170 ASN CA C 53.6 0.20 1 1066 . 170 ASN HA H 4.04 0.02 1 1067 . 170 ASN CB C 36.3 0.20 1 1068 . 170 ASN C C 175.1 0.20 1 1069 . 171 ASP N N 118.4 0.20 1 1070 . 171 ASP H H 7.80 0.02 1 1071 . 171 ASP CA C 55.6 0.20 1 1072 . 171 ASP HA H 4.73 0.02 1 1073 . 171 ASP CB C 41.7 0.20 1 1074 . 171 ASP C C 177.6 0.20 1 1075 . 172 ILE N N 123.0 0.20 1 1076 . 172 ILE H H 7.54 0.02 1 1077 . 172 ILE CA C 65.4 0.20 1 1078 . 172 ILE CB C 37.9 0.20 1 1079 . 172 ILE C C 178.6 0.20 1 1080 . 173 SER N N 113.2 0.20 1 1081 . 173 SER H H 8.52 0.02 1 1082 . 173 SER CA C 61.5 0.20 1 1083 . 173 SER HA H 4.10 0.02 1 1084 . 173 SER CB C 62.8 0.20 1 1085 . 173 SER C C 177.2 0.20 1 1086 . 174 MET N N 117.5 0.20 1 1087 . 174 MET H H 6.88 0.02 1 1088 . 174 MET CA C 57.9 0.20 1 1089 . 174 MET HA H 4.33 0.02 1 1090 . 174 MET CB C 32.7 0.20 1 1091 . 174 MET C C 177.0 0.20 1 1092 . 175 PHE N N 123.0 0.20 1 1093 . 175 PHE H H 7.93 0.02 1 1094 . 175 PHE CA C 59.1 0.20 1 1095 . 175 PHE HA H 4.24 0.02 1 1096 . 175 PHE CB C 37.4 0.20 1 1097 . 175 PHE C C 177.4 0.20 1 1098 . 176 LYS N N 114.8 0.20 1 1099 . 176 LYS H H 7.74 0.02 1 1100 . 176 LYS CA C 58.8 0.20 1 1101 . 176 LYS HA H 4.09 0.02 1 1102 . 176 LYS CB C 33.1 0.20 1 1103 . 176 LYS HB3 H 1.98 0.02 2 1104 . 176 LYS C C 177.5 0.20 1 1105 . 177 LYS N N 114.3 0.20 1 1106 . 177 LYS H H 6.86 0.02 1 1107 . 177 LYS CA C 54.5 0.20 1 1108 . 177 LYS HA H 4.46 0.02 1 1109 . 177 LYS CB C 35.6 0.20 1 1110 . 177 LYS HB3 H 1.76 0.02 2 1111 . 177 LYS C C 175.1 0.20 1 1112 . 178 ALA N N 119.4 0.20 1 1113 . 178 ALA H H 7.08 0.02 1 1114 . 178 ALA CA C 51.0 0.20 1 1115 . 178 ALA HA H 4.53 0.02 1 1116 . 178 ALA CB C 21.6 0.20 1 1117 . 178 ALA HB H 1.26 0.02 1 1118 . 178 ALA C C 177.6 0.20 1 1119 . 179 GLY N N 109.7 0.20 1 1120 . 179 GLY H H 7.81 0.02 1 1121 . 179 GLY CA C 46.4 0.20 1 1122 . 179 GLY HA2 H 4.02 0.02 2 1123 . 179 GLY C C 174.2 0.20 1 1124 . 180 LEU N N 122.4 0.20 1 1125 . 180 LEU H H 7.66 0.02 1 1126 . 180 LEU CA C 54.4 0.20 1 1127 . 180 LEU HA H 4.78 0.02 1 1128 . 180 LEU CB C 45.3 0.20 1 1129 . 180 LEU HB3 H 1.64 0.02 2 1130 . 180 LEU C C 174.7 0.20 1 1131 . 181 LYS N N 127.7 0.20 1 1132 . 181 LYS H H 9.31 0.02 1 1133 . 181 LYS CA C 55.4 0.20 1 1134 . 181 LYS HA H 4.11 0.02 1 1135 . 181 LYS CB C 31.4 0.20 1 1136 . 181 LYS C C 175.4 0.20 1 1137 . 182 ILE N N 125.5 0.20 1 1138 . 182 ILE H H 8.83 0.02 1 1139 . 182 ILE CA C 60.1 0.20 1 1140 . 182 ILE HA H 4.81 0.02 1 1141 . 182 ILE CB C 39.1 0.20 1 1142 . 182 ILE HB H 2.10 0.02 1 1143 . 182 ILE C C 174.0 0.20 1 1144 . 183 ALA N N 131.1 0.20 1 1145 . 183 ALA H H 9.00 0.02 1 1146 . 183 ALA CA C 49.9 0.20 1 1147 . 183 ALA HA H 5.15 0.02 1 1148 . 183 ALA CB C 20.3 0.20 1 1149 . 183 ALA HB H 1.51 0.02 1 1150 . 183 ALA C C 175.1 0.20 1 1151 . 184 PHE N N 129.7 0.20 1 1152 . 184 PHE H H 9.29 0.02 1 1153 . 184 PHE CA C 57.3 0.20 1 1154 . 184 PHE HA H 4.75 0.02 1 1155 . 184 PHE CB C 41.7 0.20 1 1156 . 184 PHE HB2 H 2.59 0.02 2 1157 . 184 PHE HB3 H 3.16 0.02 2 1158 . 184 PHE C C 171.1 0.20 1 1159 . 185 CYS N N 125.7 0.20 1 1160 . 185 CYS H H 8.97 0.02 1 1161 . 185 CYS CA C 59.7 0.20 1 1162 . 185 CYS HA H 3.77 0.02 1 1163 . 185 CYS CB C 26.6 0.20 1 1164 . 185 CYS HB3 H 2.65 0.02 2 1165 . 185 CYS C C 176.4 0.20 1 1166 . 186 ALA N N 118.1 0.20 1 1167 . 186 ALA H H 8.31 0.02 1 1168 . 186 ALA CA C 52.3 0.20 1 1169 . 186 ALA HA H 4.62 0.02 1 1170 . 186 ALA CB C 25.3 0.20 1 1171 . 186 ALA HB H 1.63 0.02 1 1172 . 186 ALA C C 177.9 0.20 1 1173 . 187 LYS N N 119.2 0.20 1 1174 . 187 LYS H H 8.48 0.02 1 1175 . 187 LYS CA C 54.1 0.20 1 1176 . 188 PRO CA C 67.0 0.20 1 1177 . 188 PRO HA H 4.08 0.02 1 1178 . 188 PRO CB C 32.4 0.20 1 1179 . 188 PRO C C 177.8 0.20 1 1180 . 189 ILE N N 114.5 0.20 1 1181 . 189 ILE H H 8.12 0.02 1 1182 . 189 ILE CA C 62.5 0.20 1 1183 . 189 ILE HA H 4.11 0.02 1 1184 . 189 ILE CB C 37.9 0.20 1 1185 . 189 ILE C C 174.9 0.20 1 1186 . 190 LEU N N 121.1 0.20 1 1187 . 190 LEU H H 7.08 0.02 1 1188 . 190 LEU CA C 55.2 0.20 1 1189 . 190 LEU HA H 4.16 0.02 1 1190 . 190 LEU CB C 44.0 0.20 1 1191 . 190 LEU C C 179.5 0.20 1 1192 . 191 LYS N N 118.2 0.20 1 1193 . 191 LYS H H 7.64 0.02 1 1194 . 191 LYS CA C 60.3 0.20 1 1195 . 191 LYS HA H 3.67 0.02 1 1196 . 191 LYS CB C 32.5 0.20 1 1197 . 191 LYS HB3 H 1.93 0.02 2 1198 . 191 LYS C C 179.2 0.20 1 1199 . 192 GLU N N 113.7 0.20 1 1200 . 192 GLU H H 7.42 0.02 1 1201 . 192 GLU CA C 57.9 0.20 1 1202 . 192 GLU HA H 4.14 0.02 1 1203 . 192 GLU CB C 30.2 0.20 1 1204 . 192 GLU HB3 H 2.12 0.02 2 1205 . 192 GLU C C 177.0 0.20 1 1206 . 193 LYS N N 115.8 0.20 1 1207 . 193 LYS H H 7.35 0.02 1 1208 . 193 LYS CA C 54.0 0.20 1 1209 . 193 LYS HA H 4.58 0.02 1 1210 . 193 LYS CB C 34.1 0.20 1 1211 . 193 LYS HB2 H 1.92 0.02 2 1212 . 193 LYS HB3 H 2.38 0.02 2 1213 . 193 LYS C C 175.7 0.20 1 1214 . 194 ALA N N 121.0 0.20 1 1215 . 194 ALA H H 7.18 0.02 1 1216 . 194 ALA CA C 51.7 0.20 1 1217 . 194 ALA HA H 4.01 0.02 1 1218 . 194 ALA CB C 22.9 0.20 1 1219 . 194 ALA HB H 0.59 0.02 1 1220 . 194 ALA C C 177.4 0.20 1 1221 . 195 ASP N N 119.0 0.20 1 1222 . 195 ASP H H 8.52 0.02 1 1223 . 195 ASP CA C 57.1 0.20 1 1224 . 195 ASP HA H 4.75 0.02 1 1225 . 195 ASP CB C 43.4 0.20 1 1226 . 195 ASP HB3 H 2.81 0.02 2 1227 . 195 ASP C C 176.2 0.20 1 1228 . 196 ILE N N 118.0 0.20 1 1229 . 196 ILE H H 7.45 0.02 1 1230 . 196 ILE CA C 58.5 0.20 1 1231 . 196 ILE HA H 4.31 0.02 1 1232 . 196 ILE CB C 42.8 0.20 1 1233 . 196 ILE HB H 1.45 0.02 1 1234 . 196 ILE C C 174.5 0.20 1 1235 . 197 CYS N N 124.2 0.20 1 1236 . 197 CYS H H 8.74 0.02 1 1237 . 197 CYS CA C 57.2 0.20 1 1238 . 197 CYS HA H 5.31 0.02 1 1239 . 197 CYS CB C 29.0 0.20 1 1240 . 197 CYS C C 173.9 0.20 1 1241 . 198 ILE N N 125.8 0.20 1 1242 . 198 ILE H H 8.85 0.02 1 1243 . 198 ILE CA C 60.2 0.20 1 1244 . 198 ILE HA H 4.33 0.02 1 1245 . 198 ILE C C 175.9 0.20 1 1246 . 199 GLU N N 126.2 0.20 1 1247 . 199 GLU H H 8.87 0.02 1 1248 . 199 GLU CA C 55.0 0.20 1 1249 . 199 GLU HA H 4.86 0.02 1 1250 . 199 GLU CB C 30.7 0.20 1 1251 . 199 GLU HB2 H 1.65 0.02 2 1252 . 199 GLU HB3 H 2.37 0.02 2 1253 . 199 GLU C C 175.6 0.20 1 1254 . 200 LYS N N 122.3 0.20 1 1255 . 200 LYS H H 6.98 0.02 1 1256 . 200 LYS CA C 54.3 0.20 1 1257 . 200 LYS HA H 4.78 0.02 1 1258 . 200 LYS CB C 35.0 0.20 1 1259 . 200 LYS HB3 H 1.77 0.02 2 1260 . 200 LYS C C 175.5 0.20 1 1261 . 201 ARG N N 127.0 0.20 1 1262 . 201 ARG H H 8.56 0.02 1 1263 . 201 ARG CA C 55.8 0.20 1 1264 . 201 ARG HA H 4.07 0.02 1 1265 . 201 ARG CB C 28.0 0.20 1 1266 . 201 ARG C C 174.6 0.20 1 1267 . 202 ASP N N 125.2 0.20 1 1268 . 202 ASP H H 8.32 0.02 1 1269 . 202 ASP CA C 53.4 0.20 1 1270 . 202 ASP HA H 4.76 0.02 1 1271 . 202 ASP CB C 42.8 0.20 1 1272 . 202 ASP HB3 H 2.68 0.02 2 1273 . 202 ASP C C 178.2 0.20 1 1274 . 203 LEU N N 127.2 0.20 1 1275 . 203 LEU H H 9.24 0.02 1 1276 . 203 LEU CA C 57.2 0.20 1 1277 . 203 LEU HA H 4.00 0.02 1 1278 . 203 LEU CB C 42.4 0.20 1 1279 . 203 LEU HB2 H 1.23 0.02 2 1280 . 203 LEU HB3 H 1.45 0.02 2 1281 . 203 LEU C C 177.7 0.20 1 1282 . 204 ARG N N 116.4 0.20 1 1283 . 204 ARG H H 8.68 0.02 1 1284 . 204 ARG CA C 58.1 0.20 1 1285 . 204 ARG HA H 4.21 0.02 1 1286 . 204 ARG CB C 29.7 0.20 1 1287 . 204 ARG C C 181.0 0.20 1 1288 . 205 GLU N N 118.9 0.20 1 1289 . 205 GLU H H 8.01 0.02 1 1290 . 205 GLU CA C 58.5 0.20 1 1291 . 205 GLU HA H 4.03 0.02 1 1292 . 205 GLU CB C 32.3 0.20 1 1293 . 205 GLU HB3 H 2.46 0.02 2 1294 . 205 GLU C C 179.1 0.20 1 1295 . 206 ILE N N 111.9 0.20 1 1296 . 206 ILE H H 7.98 0.02 1 1297 . 206 ILE CA C 64.6 0.20 1 1298 . 206 ILE HA H 4.03 0.02 1 1299 . 206 ILE CB C 38.1 0.20 1 1300 . 206 ILE HB H 2.12 0.02 1 1301 . 206 ILE C C 177.8 0.20 1 1302 . 207 LEU N N 116.5 0.20 1 1303 . 207 LEU H H 7.47 0.02 1 1304 . 207 LEU CA C 56.3 0.20 1 1305 . 207 LEU HA H 3.93 0.02 1 1306 . 207 LEU CB C 41.1 0.20 1 1307 . 207 LEU HB3 H 1.59 0.02 2 1308 . 207 LEU C C 178.2 0.20 1 1309 . 208 LYS N N 116.0 0.20 1 1310 . 208 LYS H H 7.26 0.02 1 1311 . 208 LYS CA C 57.7 0.20 1 1312 . 208 LYS HA H 4.01 0.02 1 1313 . 208 LYS CB C 32.3 0.20 1 1314 . 208 LYS HB3 H 1.34 0.02 2 1315 . 208 LYS C C 177.2 0.20 1 1316 . 209 TYR N N 115.0 0.20 1 1317 . 209 TYR H H 7.41 0.02 1 1318 . 209 TYR CA C 58.0 0.20 1 1319 . 209 TYR HA H 4.62 0.02 1 1320 . 209 TYR CB C 41.1 0.20 1 1321 . 209 TYR HB2 H 2.60 0.02 2 1322 . 209 TYR HB3 H 3.42 0.02 2 1323 . 209 TYR C C 174.9 0.20 1 1324 . 210 ILE N N 115.9 0.20 1 1325 . 210 ILE H H 6.93 0.02 1 1326 . 210 ILE CA C 59.6 0.20 1 1327 . 210 ILE HA H 4.32 0.02 1 1328 . 210 ILE CB C 38.8 0.20 1 1329 . 210 ILE HB H 1.99 0.02 1 1330 . 210 ILE C C 174.7 0.20 1 1331 . 211 LYS N N 129.7 0.20 1 1332 . 211 LYS H H 8.24 0.02 1 1333 . 211 LYS CA C 57.3 0.20 1 1334 . 211 LYS HA H 4.31 0.02 1 stop_ save_