data_5244 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Assignment of Endonuclease V from Bacteriophage T4 with deuterium labeling ; _BMRB_accession_number 5244 _BMRB_flat_file_name bmr5244.str _Entry_type original _Submission_date 2001-12-26 _Accession_date 2001-12-26 _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 Ahn Hee-Chul . . 2 Lee Sung-Yun . . 3 Lee Bong-Jin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 253 "13C chemical shifts" 395 "15N chemical shifts" 131 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone Assignments for Endonuclease V from Bacteriophage T4 with deuterium labeling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22012553 _PubMed_ID 12018491 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ahn Hee-Chul . . 2 Lee Sung-Yun . . 3 Lee Bong-Jin . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 383 _Page_last 384 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_endo_V _Saveframe_category molecular_system _Mol_system_name 'endonuclease V' _Abbreviation_common 'endo V' _Enzyme_commission_number 3.1.25.1 loop_ _Mol_system_component_name _Mol_label 'endonuclease V' $endonuclease_V stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA repair' stop_ _Database_query_date . _Details ; 2END is crystal structure of endonuclease V from Bacteriophage T4. 1VAS is crystal structure of mutant endonuclease V (E23Q) complexed with DNA substrate. ; save_ ######################## # Monomeric polymers # ######################## save_endonuclease_V _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'endonuclease V' _Abbreviation_common 'endo V' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 138 _Mol_residue_sequence ; MTRINLTLVSELADQHLMAE YRELPRVFGAVRKHVANGKR VRDFKISPTFILGAGHVTFF YDKLEFLRKRQIELIAECLK RGFNIKDTTVQDISDIPQEF RGDYIPHEASIAISQARLDE KIAQRPTWYKYYGKAIYA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 ARG 4 ILE 5 ASN 6 LEU 7 THR 8 LEU 9 VAL 10 SER 11 GLU 12 LEU 13 ALA 14 ASP 15 GLN 16 HIS 17 LEU 18 MET 19 ALA 20 GLU 21 TYR 22 ARG 23 GLU 24 LEU 25 PRO 26 ARG 27 VAL 28 PHE 29 GLY 30 ALA 31 VAL 32 ARG 33 LYS 34 HIS 35 VAL 36 ALA 37 ASN 38 GLY 39 LYS 40 ARG 41 VAL 42 ARG 43 ASP 44 PHE 45 LYS 46 ILE 47 SER 48 PRO 49 THR 50 PHE 51 ILE 52 LEU 53 GLY 54 ALA 55 GLY 56 HIS 57 VAL 58 THR 59 PHE 60 PHE 61 TYR 62 ASP 63 LYS 64 LEU 65 GLU 66 PHE 67 LEU 68 ARG 69 LYS 70 ARG 71 GLN 72 ILE 73 GLU 74 LEU 75 ILE 76 ALA 77 GLU 78 CYS 79 LEU 80 LYS 81 ARG 82 GLY 83 PHE 84 ASN 85 ILE 86 LYS 87 ASP 88 THR 89 THR 90 VAL 91 GLN 92 ASP 93 ILE 94 SER 95 ASP 96 ILE 97 PRO 98 GLN 99 GLU 100 PHE 101 ARG 102 GLY 103 ASP 104 TYR 105 ILE 106 PRO 107 HIS 108 GLU 109 ALA 110 SER 111 ILE 112 ALA 113 ILE 114 SER 115 GLN 116 ALA 117 ARG 118 LEU 119 ASP 120 GLU 121 LYS 122 ILE 123 ALA 124 GLN 125 ARG 126 PRO 127 THR 128 TRP 129 TYR 130 LYS 131 TYR 132 TYR 133 GLY 134 LYS 135 ALA 136 ILE 137 TYR 138 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-07-28 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 1ENI "Crystal Structure Of A Pyrimidine Dimer Specific Excision Repair Enzyme From Bacteriophage T4: Refinement At 1.45 Angstroms And" 100.00 138 99.28 100.00 3.26e-96 PDB 1ENJ "Crystal Structure Of A Pyrimidine Dimer Specific Excision Repair Enzyme From Bacteriophage T4: Refinement At 1.45 Angstroms And" 100.00 138 99.28 100.00 2.74e-96 PDB 1ENK "Crystal Structure Of A Pyrimidine Dimer Specific Excision Repair Enzyme From Bacteriophage T4: Refinement At 1.45 Angstroms And" 100.00 138 99.28 100.00 3.30e-96 PDB 1VAS "Atomic Model Of A Pyrimidine Dimer Specific Excision Repair Enzyme Complexed With A Dna Substrate: Structural Basis For Damaged" 99.28 137 99.27 100.00 2.33e-95 PDB 2END "Crystal Structure Of A Pyrimidine Dimer Specific Excision Repair Enzyme From Bacteriophage T4: Refinement At 1.45 Angstroms And" 100.00 138 100.00 100.00 8.32e-97 PDB 2FCC "Crystal Structure Of T4 Pyrimidine Dimer Glycosylase (T4-Pdg) Covalently Complexed With A Dna Substrate Containing Abasic Site" 99.28 137 100.00 100.00 8.62e-96 EMBL CAA28215 "unnamed protein product [Enterobacteria phage T4]" 100.00 138 100.00 100.00 8.32e-97 GB AAA72721 "T4 endonuclease V [synthetic construct]" 100.00 138 100.00 100.00 8.32e-97 GB AAC42096 "T4 endonuclease V (T4endV) [synthetic construct]" 100.00 138 100.00 100.00 8.32e-97 GB AAD42563 "DenV endonuclease V, N-glycosylase UV repair enzyme [Enterobacteria phage T4]" 100.00 138 100.00 100.00 8.32e-97 GB ABX11097 "DenV endonuclease V N-glycosylase UV repair enzyme [Enterobacteria phage JS98]" 100.00 138 97.83 99.28 2.54e-95 GB ACL78337 "DenV endonuclease V, N-glycosylase UV repair enzyme [Enterobacteria phage JS10]" 100.00 138 97.83 99.28 2.54e-95 REF NP_049733 "DenV endonuclease V, N-glycosylase UV repair enzyme [Enterobacteria phage T4]" 100.00 138 100.00 100.00 8.32e-97 REF YP_001595242 "DenV endonuclease V N-glycosylase UV repair enzyme [Enterobacteria phage JS98]" 100.00 138 97.83 99.28 2.54e-95 REF YP_002922460 "DenV endonuclease V, N-glycosylase UV repair enzyme [Enterobacteria phage JS10]" 100.00 138 97.83 99.28 2.54e-95 REF YP_003734258 "denV gene product [Enterobacteria phage IME08]" 100.00 143 97.10 98.55 1.51e-94 SP P04418 "RecName: Full=Endonuclease V [Enterobacteria phage T4]" 100.00 138 100.00 100.00 8.32e-97 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $endonuclease_V T4 10665 Viruses . 'T4-like phages' 'Bacteriophage T4' 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 $endonuclease_V 'recombinant technology' 'E. coli' Escherichia coli 'BL 21 (DE 3)' plasmid pET-15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $endonuclease_V 1.0 mM '[U-15N]-Ala, Asp, Arg, Gly, Lys, Ser, Thr, Tyr, Val' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $endonuclease_V 2.0 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $endonuclease_V 1.5 mM '[U-70% 2H ; U-15N]' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $endonuclease_V 1.5 mM '[U-90% 2H; U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'data processing' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Task 'data processing' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Task 'peak assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label . save_ save_3D_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label . save_ save_3D_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_HN(CO)CACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label . save_ save_3D_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions _Details 'Sample has a tendency to become gelation above 293K.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 293 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 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'endonuclease V' _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 THR CA C 62.067 0.2 1 2 . 2 THR CB C 69.019 0.2 1 3 . 2 THR C C 171.21 0.2 1 4 . 3 ARG N N 129.481 0.05 1 5 . 3 ARG H H 8.252 0.02 1 6 . 3 ARG CA C 53.304 0.2 1 7 . 3 ARG HA H 4.586 0.02 1 8 . 3 ARG CB C 30.02 0.2 1 9 . 3 ARG C C 173.033 0.2 1 10 . 4 ILE N N 131.361 0.05 1 11 . 4 ILE H H 11.494 0.02 1 12 . 4 ILE CA C 57.459 0.2 1 13 . 4 ILE CB C 34.959 0.2 1 14 . 4 ILE C C 176.666 0.2 1 15 . 5 ASN N N 124.705 0.05 1 16 . 5 ASN H H 9.071 0.02 1 17 . 5 ASN CA C 50.279 0.2 1 18 . 5 ASN HA H 4.611 0.02 1 19 . 5 ASN CB C 39.825 0.2 1 20 . 5 ASN C C 172.173 0.2 1 21 . 6 LEU N N 109.992 0.05 1 22 . 6 LEU H H 7.748 0.02 1 23 . 6 LEU CA C 51.386 0.2 1 24 . 6 LEU HA H 3.823 0.02 1 25 . 6 LEU CB C 43.355 0.2 1 26 . 6 LEU C C 177.577 0.2 1 27 . 7 THR N N 108.787 0.05 1 28 . 7 THR H H 7.003 0.02 1 29 . 7 THR CA C 60.141 0.2 1 30 . 7 THR HA H 4.067 0.02 1 31 . 7 THR CB C 67.7 0.2 1 32 . 7 THR C C 174.71 0.2 1 33 . 8 LEU N N 120.247 0.05 1 34 . 8 LEU H H 8.297 0.02 1 35 . 8 LEU CA C 54.684 0.2 1 36 . 8 LEU HA H 4.205 0.02 1 37 . 8 LEU CB C 39.984 0.2 1 38 . 8 LEU C C 180.328 0.2 1 39 . 9 VAL N N 127.227 0.05 1 40 . 9 VAL H H 9.06 0.02 1 41 . 9 VAL CA C 64.605 0.2 1 42 . 9 VAL HA H 3.604 0.02 1 43 . 9 VAL CB C 29.441 0.2 1 44 . 9 VAL C C 177.717 0.2 1 45 . 10 SER N N 110.061 0.05 1 46 . 10 SER H H 8.019 0.02 1 47 . 10 SER CA C 59.129 0.2 1 48 . 10 SER HA H 4.072 0.02 1 49 . 10 SER C C 175.166 0.2 1 50 . 11 GLU N N 118.802 0.05 1 51 . 11 GLU H H 7.423 0.02 1 52 . 11 GLU CA C 54.632 0.2 1 53 . 11 GLU HA H 4.441 0.02 1 54 . 11 GLU CB C 29.143 0.2 1 55 . 11 GLU C C 176.14 0.2 1 56 . 12 LEU N N 121.558 0.05 1 57 . 12 LEU H H 7.405 0.02 1 58 . 12 LEU CA C 54.394 0.2 1 59 . 12 LEU HA H 4.451 0.02 1 60 . 12 LEU CB C 42.407 0.2 1 61 . 12 LEU C C 178.669 0.2 1 62 . 13 ALA N N 124.956 0.05 1 63 . 13 ALA H H 10.375 0.02 1 64 . 13 ALA CA C 52.309 0.2 1 65 . 13 ALA CB C 17.412 0.2 1 66 . 13 ALA C C 178.855 0.2 1 67 . 14 ASP N N 124.254 0.05 1 68 . 14 ASP H H 10.439 0.02 1 69 . 14 ASP CA C 57.757 0.2 1 70 . 14 ASP HA H 4.361 0.02 1 71 . 14 ASP CB C 38.879 0.2 1 72 . 14 ASP C C 178.532 0.2 1 73 . 15 GLN N N 114.285 0.05 1 74 . 15 GLN H H 9.28 0.02 1 75 . 15 GLN CA C 59.741 0.2 1 76 . 15 GLN HA H 3.952 0.02 1 77 . 15 GLN CB C 25.244 0.2 1 78 . 15 GLN C C 180.316 0.2 1 79 . 16 HIS N N 119.083 0.05 1 80 . 16 HIS H H 7.188 0.02 1 81 . 16 HIS CA C 57.034 0.2 1 82 . 16 HIS CB C 31.096 0.2 1 83 . 16 HIS C C 178.025 0.2 1 84 . 17 LEU N N 124.333 0.05 1 85 . 17 LEU H H 9.048 0.02 1 86 . 17 LEU CA C 57.333 0.2 1 87 . 17 LEU HA H 4.262 0.02 1 88 . 17 LEU CB C 39.187 0.2 1 89 . 17 LEU C C 177.174 0.2 1 90 . 18 MET N N 115.207 0.05 1 91 . 18 MET H H 8.237 0.02 1 92 . 18 MET CA C 56.077 0.2 1 93 . 18 MET HA H 4.415 0.02 1 94 . 18 MET CB C 29.795 0.2 1 95 . 18 MET C C 178.412 0.2 1 96 . 19 ALA N N 118.818 0.05 1 97 . 19 ALA H H 7.575 0.02 1 98 . 19 ALA CA C 54.133 0.2 1 99 . 19 ALA HA H 4.23 0.02 1 100 . 19 ALA CB C 16.316 0.2 1 101 . 19 ALA C C 178.318 0.2 1 102 . 20 GLU N N 120.641 0.05 1 103 . 20 GLU H H 7.977 0.02 1 104 . 20 GLU CA C 59.556 0.2 1 105 . 20 GLU HA H 4.239 0.02 1 106 . 20 GLU CB C 27.174 0.2 1 107 . 20 GLU C C 178.545 0.2 1 108 . 21 TYR N N 117.921 0.05 1 109 . 21 TYR H H 8.421 0.02 1 110 . 21 TYR CA C 59.673 0.2 1 111 . 21 TYR HA H 4.262 0.02 1 112 . 21 TYR CB C 37.034 0.2 1 113 . 21 TYR C C 177.379 0.2 1 114 . 22 ARG N N 116.318 0.05 1 115 . 22 ARG H H 7.728 0.02 1 116 . 22 ARG CA C 57.289 0.2 1 117 . 22 ARG HA H 3.728 0.02 1 118 . 22 ARG CB C 29.322 0.2 1 119 . 22 ARG C C 178.436 0.2 1 120 . 23 GLU N N 117.812 0.05 1 121 . 23 GLU H H 8.548 0.02 1 122 . 23 GLU CA C 57.145 0.2 1 123 . 23 GLU HA H 3.56 0.02 1 124 . 23 GLU CB C 29.25 0.2 1 125 . 23 GLU C C 177.81 0.2 1 126 . 24 LEU N N 122.205 0.05 1 127 . 24 LEU H H 8.888 0.02 1 128 . 24 LEU CA C 60.256 0.2 1 129 . 24 LEU HA H 3.901 0.02 1 130 . 24 LEU CB C 37.944 0.2 1 131 . 25 PRO CA C 64.082 0.2 1 132 . 25 PRO CB C 29.408 0.2 1 133 . 25 PRO C C 178.649 0.2 1 134 . 26 ARG N N 117.437 0.05 1 135 . 26 ARG H H 8.051 0.02 1 136 . 26 ARG CA C 56.749 0.2 1 137 . 26 ARG HA H 4.462 0.02 1 138 . 26 ARG CB C 26.659 0.2 1 139 . 26 ARG C C 179.224 0.2 1 140 . 27 VAL N N 118.268 0.05 1 141 . 27 VAL H H 8.177 0.02 1 142 . 27 VAL CA C 65.552 0.2 1 143 . 27 VAL HA H 3.51 0.02 1 144 . 27 VAL CB C 29.302 0.2 1 145 . 27 VAL C C 177.478 0.2 1 146 . 28 PHE N N 115.453 0.05 1 147 . 28 PHE H H 6.381 0.02 1 148 . 28 PHE CA C 58.025 0.2 1 149 . 28 PHE HA H 4.188 0.02 1 150 . 28 PHE CB C 36.331 0.2 1 151 . 28 PHE C C 178.126 0.2 1 152 . 29 GLY N N 102.572 0.05 1 153 . 29 GLY H H 7.469 0.02 1 154 . 29 GLY CA C 46.259 0.2 1 155 . 29 GLY HA3 H 3.762 0.02 2 156 . 29 GLY HA2 H 3.934 0.02 2 157 . 29 GLY C C 176.295 0.2 1 158 . 30 ALA N N 124.815 0.05 1 159 . 30 ALA H H 7.879 0.02 1 160 . 30 ALA CA C 53.519 0.2 1 161 . 30 ALA HA H 3.936 0.02 1 162 . 30 ALA CB C 16.102 0.2 1 163 . 30 ALA C C 179.874 0.2 1 164 . 31 VAL N N 117.396 0.05 1 165 . 31 VAL H H 7.862 0.02 1 166 . 31 VAL CA C 66.216 0.2 1 167 . 31 VAL HA H 2.96 0.02 1 168 . 31 VAL CB C 29.137 0.2 1 169 . 31 VAL C C 177.362 0.2 1 170 . 32 ARG N N 118.252 0.05 1 171 . 32 ARG H H 8.173 0.02 1 172 . 32 ARG CA C 60.279 0.2 1 173 . 32 ARG HA H 4.211 0.02 1 174 . 32 ARG CB C 28.158 0.2 1 175 . 32 ARG C C 179.308 0.2 1 176 . 33 LYS N N 119.795 0.05 1 177 . 33 LYS H H 7.518 0.02 1 178 . 33 LYS CA C 58.322 0.2 1 179 . 33 LYS HA H 3.939 0.02 1 180 . 33 LYS CB C 29.679 0.2 1 181 . 33 LYS C C 178.885 0.2 1 182 . 34 HIS N N 119.101 0.05 1 183 . 34 HIS H H 7.76 0.02 1 184 . 34 HIS CA C 58.463 0.2 1 185 . 34 HIS HA H 4.717 0.02 1 186 . 34 HIS CB C 29.049 0.2 1 187 . 34 HIS C C 179.555 0.2 1 188 . 35 VAL N N 122.061 0.05 1 189 . 35 VAL H H 8.969 0.02 1 190 . 35 VAL CA C 64.867 0.2 1 191 . 35 VAL HA H 3.892 0.02 1 192 . 35 VAL CB C 29.876 0.2 1 193 . 35 VAL C C 180.975 0.2 1 194 . 36 ALA N N 124.922 0.05 1 195 . 36 ALA H H 8.044 0.02 1 196 . 36 ALA CA C 53.632 0.2 1 197 . 36 ALA HA H 4.224 0.02 1 198 . 36 ALA CB C 15.892 0.2 1 199 . 36 ALA C C 178.633 0.2 1 200 . 37 ASN N N 115.183 0.05 1 201 . 37 ASN H H 7.55 0.02 1 202 . 37 ASN CA C 51.827 0.2 1 203 . 37 ASN HA H 4.721 0.02 1 204 . 37 ASN CB C 38.135 0.2 1 205 . 37 ASN C C 175.532 0.2 1 206 . 38 GLY N N 107.905 0.05 1 207 . 38 GLY H H 8.163 0.02 1 208 . 38 GLY CA C 45.066 0.2 1 209 . 38 GLY HA3 H 3.864 0.02 2 210 . 38 GLY HA2 H 4.198 0.02 2 211 . 38 GLY C C 174.985 0.2 1 212 . 39 LYS N N 118.75 0.05 1 213 . 39 LYS H H 8.08 0.02 1 214 . 39 LYS CA C 54.075 0.2 1 215 . 39 LYS HA H 4.445 0.02 1 216 . 39 LYS CB C 31.409 0.2 1 217 . 39 LYS C C 175.5 0.2 1 218 . 40 ARG N N 120.617 0.05 1 219 . 40 ARG H H 9.245 0.02 1 220 . 40 ARG CA C 52.283 0.2 1 221 . 40 ARG CB C 30.945 0.2 1 222 . 40 ARG C C 177.529 0.2 1 223 . 41 VAL N N 123.371 0.05 1 224 . 41 VAL H H 8.444 0.02 1 225 . 41 VAL CA C 66.289 0.2 1 226 . 41 VAL HA H 3.54 0.02 1 227 . 41 VAL CB C 29.396 0.2 1 228 . 41 VAL C C 178.113 0.2 1 229 . 42 ARG N N 114.528 0.05 1 230 . 42 ARG H H 7.949 0.02 1 231 . 42 ARG CA C 55.775 0.2 1 232 . 42 ARG HA H 4.295 0.02 1 233 . 42 ARG CB C 27.039 0.2 1 234 . 42 ARG C C 176.327 0.2 1 235 . 43 ASP N N 119.198 0.05 1 236 . 43 ASP H H 7.931 0.02 1 237 . 43 ASP CA C 54.86 0.2 1 238 . 43 ASP HA H 4.345 0.02 1 239 . 43 ASP CB C 39.97 0.2 1 240 . 43 ASP C C 175.097 0.2 1 241 . 44 PHE N N 118.045 0.05 1 242 . 44 PHE H H 7.634 0.02 1 243 . 44 PHE CA C 56.603 0.2 1 244 . 44 PHE HA H 4.557 0.02 1 245 . 44 PHE CB C 40.096 0.2 1 246 . 44 PHE C C 174.366 0.2 1 247 . 45 LYS N N 123.583 0.05 1 248 . 45 LYS H H 8.683 0.02 1 249 . 45 LYS CA C 53.777 0.2 1 250 . 45 LYS HA H 4.35 0.02 1 251 . 45 LYS CB C 28.472 0.2 1 252 . 45 LYS C C 174.887 0.2 1 253 . 46 ILE N N 127.242 0.05 1 254 . 46 ILE H H 8.107 0.02 1 255 . 46 ILE CA C 60.368 0.2 1 256 . 46 ILE HA H 3.66 0.02 1 257 . 46 ILE CB C 36.639 0.2 1 258 . 46 ILE C C 176.591 0.2 1 259 . 47 SER N N 124.418 0.05 1 260 . 47 SER H H 8.584 0.02 1 261 . 47 SER CA C 55.336 0.2 1 262 . 47 SER HA H 4.562 0.02 1 263 . 47 SER CB C 62.55 0.2 1 264 . 48 PRO CA C 63.114 0.2 1 265 . 48 PRO CB C 30.278 0.2 1 266 . 48 PRO C C 176.436 0.2 1 267 . 49 THR N N 108.109 0.05 1 268 . 49 THR H H 7.302 0.02 1 269 . 49 THR CA C 57.996 0.2 1 270 . 49 THR CB C 70.205 0.2 1 271 . 49 THR C C 172.573 0.2 1 272 . 50 PHE N N 126.26 0.05 1 273 . 50 PHE H H 8.043 0.02 1 274 . 50 PHE CA C 59.121 0.2 1 275 . 50 PHE HA H 3.929 0.02 1 276 . 50 PHE CB C 37.156 0.2 1 277 . 50 PHE C C 173.326 0.2 1 278 . 51 ILE N N 120.906 0.05 1 279 . 51 ILE H H 5.284 0.02 1 280 . 51 ILE CA C 57.508 0.2 1 281 . 51 ILE HA H 4.091 0.02 1 282 . 51 ILE CB C 39.843 0.2 1 283 . 51 ILE C C 174.074 0.2 1 284 . 52 LEU N N 119.123 0.05 1 285 . 52 LEU H H 8.205 0.02 1 286 . 52 LEU CA C 53.343 0.2 1 287 . 52 LEU HA H 4.079 0.02 1 288 . 52 LEU CB C 41.584 0.2 1 289 . 52 LEU C C 177.428 0.2 1 290 . 53 GLY N N 108.335 0.05 1 291 . 53 GLY H H 7.906 0.02 1 292 . 53 GLY CA C 43.588 0.2 1 293 . 53 GLY HA3 H 3.803 0.02 2 294 . 53 GLY HA2 H 3.935 0.02 2 295 . 53 GLY C C 173.712 0.2 1 296 . 54 ALA N N 127.07 0.05 1 297 . 54 ALA H H 8.563 0.02 1 298 . 54 ALA CA C 53.455 0.2 1 299 . 54 ALA HA H 4.64 0.02 1 300 . 54 ALA CB C 16.317 0.2 1 301 . 54 ALA C C 178.991 0.2 1 302 . 55 GLY N N 110.309 0.05 1 303 . 55 GLY H H 8.843 0.02 1 304 . 55 GLY CA C 44.455 0.2 1 305 . 55 GLY HA3 H 3.837 0.02 2 306 . 55 GLY HA2 H 4.094 0.02 2 307 . 55 GLY C C 174.913 0.2 1 308 . 56 HIS N N 122.226 0.05 1 309 . 56 HIS H H 8.28 0.02 1 310 . 56 HIS CA C 59.435 0.2 1 311 . 56 HIS HA H 3.907 0.02 1 312 . 56 HIS CB C 28.614 0.2 1 313 . 56 HIS C C 174.67 0.2 1 314 . 57 VAL N N 114.518 0.05 1 315 . 57 VAL H H 8.11 0.02 1 316 . 57 VAL CA C 65.855 0.2 1 317 . 57 VAL HA H 3.552 0.02 1 318 . 57 VAL CB C 29.388 0.2 1 319 . 57 VAL C C 177.908 0.2 1 320 . 58 THR N N 113.714 0.05 1 321 . 58 THR H H 7.241 0.02 1 322 . 58 THR CA C 63.234 0.2 1 323 . 58 THR HA H 2.141 0.02 1 324 . 58 THR CB C 67.056 0.2 1 325 . 58 THR C C 175.126 0.2 1 326 . 59 PHE N N 118.834 0.05 1 327 . 59 PHE H H 7.497 0.02 1 328 . 59 PHE CA C 59.376 0.2 1 329 . 59 PHE HA H 3.874 0.02 1 330 . 59 PHE CB C 37.154 0.2 1 331 . 59 PHE C C 174.27 0.2 1 332 . 60 PHE N N 110.233 0.05 1 333 . 60 PHE H H 7.664 0.02 1 334 . 60 PHE CA C 58.307 0.2 1 335 . 60 PHE HA H 4.015 0.02 1 336 . 60 PHE CB C 38.13 0.2 1 337 . 60 PHE C C 176.662 0.2 1 338 . 61 TYR N N 120.153 0.05 1 339 . 61 TYR H H 8.249 0.02 1 340 . 61 TYR CA C 57.423 0.2 1 341 . 61 TYR CB C 34.858 0.2 1 342 . 61 TYR C C 174.103 0.2 1 343 . 62 ASP N N 108.976 0.05 1 344 . 62 ASP H H 7.301 0.02 1 345 . 62 ASP CA C 51.361 0.2 1 346 . 62 ASP HA H 4.252 0.02 1 347 . 62 ASP CB C 38.85 0.2 1 348 . 62 ASP C C 176.607 0.2 1 349 . 63 LYS N N 120.892 0.05 1 350 . 63 LYS H H 7.919 0.02 1 351 . 63 LYS CA C 53.997 0.2 1 352 . 63 LYS HA H 4.344 0.02 1 353 . 63 LYS CB C 31.577 0.2 1 354 . 63 LYS C C 178.952 0.2 1 355 . 64 LEU N N 115.052 0.05 1 356 . 64 LEU H H 8.585 0.02 1 357 . 64 LEU CA C 57.757 0.2 1 358 . 64 LEU HA H 4.275 0.02 1 359 . 64 LEU CB C 40.293 0.2 1 360 . 64 LEU C C 179.4 0.2 1 361 . 65 GLU N N 118.278 0.05 1 362 . 65 GLU H H 8.059 0.02 1 363 . 65 GLU CA C 56.971 0.2 1 364 . 65 GLU CB C 26.799 0.2 1 365 . 65 GLU C C 178.576 0.2 1 366 . 66 PHE N N 120.944 0.05 1 367 . 66 PHE H H 7.463 0.02 1 368 . 66 PHE CA C 60.807 0.2 1 369 . 66 PHE HA H 4.455 0.02 1 370 . 66 PHE CB C 37.69 0.2 1 371 . 66 PHE C C 178.441 0.2 1 372 . 67 LEU N N 116.903 0.05 1 373 . 67 LEU H H 7.895 0.02 1 374 . 67 LEU CA C 56.406 0.2 1 375 . 67 LEU HA H 3.848 0.02 1 376 . 67 LEU CB C 39.308 0.2 1 377 . 67 LEU C C 177.856 0.2 1 378 . 68 ARG N N 121.88 0.05 1 379 . 68 ARG H H 8.719 0.02 1 380 . 68 ARG CA C 59.442 0.2 1 381 . 68 ARG HA H 3.977 0.02 1 382 . 68 ARG CB C 28.611 0.2 1 383 . 68 ARG C C 177.638 0.2 1 384 . 69 LYS N N 115.464 0.05 1 385 . 69 LYS H H 7.86 0.02 1 386 . 69 LYS CA C 59.239 0.2 1 387 . 69 LYS HA H 3.866 0.02 1 388 . 69 LYS CB C 30.309 0.2 1 389 . 69 LYS C C 179.704 0.2 1 390 . 70 ARG N N 121.461 0.05 1 391 . 70 ARG H H 7.987 0.02 1 392 . 70 ARG CA C 58.504 0.2 1 393 . 70 ARG HA H 3.895 0.02 1 394 . 70 ARG CB C 30.158 0.2 1 395 . 70 ARG C C 177.932 0.2 1 396 . 71 GLN N N 121.799 0.05 1 397 . 71 GLN H H 8.936 0.02 1 398 . 71 GLN CA C 58.177 0.2 1 399 . 71 GLN HA H 4.24 0.02 1 400 . 71 GLN CB C 25.31 0.2 1 401 . 71 GLN C C 178.509 0.2 1 402 . 72 ILE N N 118.164 0.05 1 403 . 72 ILE H H 7.644 0.02 1 404 . 72 ILE CA C 65.056 0.2 1 405 . 72 ILE HA H 3.53 0.02 1 406 . 72 ILE CB C 36.544 0.2 1 407 . 72 ILE C C 179.285 0.2 1 408 . 73 GLU N N 118.462 0.05 1 409 . 73 GLU H H 7.247 0.02 1 410 . 73 GLU CA C 58.206 0.2 1 411 . 73 GLU HA H 4.108 0.02 1 412 . 73 GLU CB C 28.351 0.2 1 413 . 73 GLU C C 180.111 0.2 1 414 . 74 LEU N N 122.572 0.05 1 415 . 74 LEU H H 9.171 0.02 1 416 . 74 LEU CA C 57.602 0.2 1 417 . 74 LEU HA H 3.928 0.02 1 418 . 74 LEU CB C 40.676 0.2 1 419 . 74 LEU C C 179.454 0.2 1 420 . 75 ILE N N 119.897 0.05 1 421 . 75 ILE H H 8.682 0.02 1 422 . 75 ILE CA C 65.166 0.2 1 423 . 75 ILE CB C 37.098 0.2 1 424 . 75 ILE C C 177.363 0.2 1 425 . 76 ALA N N 118.715 0.05 1 426 . 76 ALA H H 7.571 0.02 1 427 . 76 ALA CA C 54.169 0.2 1 428 . 76 ALA HA H 3.983 0.02 1 429 . 76 ALA CB C 16.316 0.2 1 430 . 76 ALA C C 180.867 0.2 1 431 . 77 GLU N N 120.403 0.05 1 432 . 77 GLU H H 8.264 0.02 1 433 . 77 GLU CA C 57.215 0.2 1 434 . 77 GLU HA H 4.07 0.02 1 435 . 77 GLU CB C 26.748 0.2 1 436 . 77 GLU C C 178.171 0.2 1 437 . 78 CYS N N 118.355 0.05 1 438 . 78 CYS H H 8.361 0.02 1 439 . 78 CYS CA C 63.774 0.2 1 440 . 78 CYS CB C 25.568 0.2 1 441 . 78 CYS C C 177.21 0.2 1 442 . 79 LEU N N 117.214 0.05 1 443 . 79 LEU H H 7.895 0.02 1 444 . 79 LEU CA C 56.53 0.2 1 445 . 79 LEU HA H 3.984 0.02 1 446 . 79 LEU CB C 38.903 0.2 1 447 . 79 LEU C C 181.545 0.2 1 448 . 80 LYS N N 124.114 0.05 1 449 . 80 LYS H H 8.143 0.02 1 450 . 80 LYS CA C 58.505 0.2 1 451 . 80 LYS HA H 3.9 0.02 1 452 . 80 LYS CB C 30.764 0.2 1 453 . 80 LYS C C 178.448 0.2 1 454 . 81 ARG N N 114.238 0.05 1 455 . 81 ARG H H 7.115 0.02 1 456 . 81 ARG CA C 55.219 0.2 1 457 . 81 ARG HA H 3.598 0.02 1 458 . 81 ARG CB C 27.189 0.2 1 459 . 81 ARG C C 175.563 0.2 1 460 . 82 GLY N N 106.467 0.05 1 461 . 82 GLY H H 7.59 0.02 1 462 . 82 GLY CA C 44.547 0.2 1 463 . 82 GLY HA3 H 3.63 0.02 2 464 . 82 GLY HA2 H 3.895 0.02 2 465 . 82 GLY C C 174.879 0.2 1 466 . 83 PHE N N 118.675 0.05 1 467 . 83 PHE H H 7.718 0.02 1 468 . 83 PHE CA C 53.193 0.2 1 469 . 83 PHE HA H 4.668 0.02 1 470 . 83 PHE CB C 36.066 0.2 1 471 . 83 PHE C C 176.17 0.2 1 472 . 84 ASN N N 123.158 0.05 1 473 . 84 ASN H H 8.831 0.02 1 474 . 84 ASN CA C 51.595 0.2 1 475 . 84 ASN HA H 4.468 0.02 1 476 . 84 ASN CB C 35.908 0.2 1 477 . 84 ASN C C 175.233 0.2 1 478 . 85 ILE N N 116.307 0.05 1 479 . 85 ILE H H 7.396 0.02 1 480 . 85 ILE CA C 58.973 0.2 1 481 . 85 ILE HA H 4.335 0.02 1 482 . 85 ILE CB C 36.677 0.2 1 483 . 85 ILE C C 176.09 0.2 1 484 . 86 LYS N N 120.627 0.05 1 485 . 86 LYS H H 8.584 0.02 1 486 . 86 LYS CA C 56.428 0.2 1 487 . 86 LYS HA H 4.241 0.02 1 488 . 86 LYS CB C 31.266 0.2 1 489 . 86 LYS C C 176.688 0.2 1 490 . 87 ASP N N 116.818 0.05 1 491 . 87 ASP H H 7.476 0.02 1 492 . 87 ASP CA C 52.443 0.2 1 493 . 87 ASP HA H 4.517 0.02 1 494 . 87 ASP CB C 39.948 0.2 1 495 . 87 ASP C C 177.247 0.2 1 496 . 88 THR N N 115.467 0.05 1 497 . 88 THR H H 8.753 0.02 1 498 . 88 THR CA C 60.041 0.2 1 499 . 88 THR HA H 4.401 0.02 1 500 . 88 THR CB C 67.298 0.2 1 501 . 88 THR C C 173.29 0.2 1 502 . 89 THR N N 115.996 0.05 1 503 . 89 THR H H 7.969 0.02 1 504 . 89 THR CA C 59.913 0.2 1 505 . 89 THR HA H 4.45 0.02 1 506 . 89 THR CB C 69.634 0.2 1 507 . 89 THR C C 173.633 0.2 1 508 . 90 VAL N N 125.684 0.05 1 509 . 90 VAL H H 8.544 0.02 1 510 . 90 VAL CA C 60.11 0.2 1 511 . 90 VAL HA H 3.878 0.02 1 512 . 90 VAL CB C 30.434 0.2 1 513 . 90 VAL C C 175.161 0.2 1 514 . 91 GLN N N 127.208 0.05 1 515 . 91 GLN H H 8.585 0.02 1 516 . 91 GLN CA C 55.575 0.2 1 517 . 91 GLN HA H 3.878 0.02 1 518 . 91 GLN CB C 27.843 0.2 1 519 . 91 GLN C C 174.805 0.2 1 520 . 92 ASP N N 122.755 0.05 1 521 . 92 ASP H H 8.324 0.02 1 522 . 92 ASP CA C 52.949 0.2 1 523 . 92 ASP HA H 4.437 0.02 1 524 . 92 ASP CB C 39.678 0.2 1 525 . 92 ASP C C 176.812 0.2 1 526 . 93 ILE N N 118.474 0.05 1 527 . 93 ILE H H 8.232 0.02 1 528 . 93 ILE CA C 59.278 0.2 1 529 . 93 ILE HA H 4.444 0.02 1 530 . 93 ILE CB C 36.256 0.2 1 531 . 93 ILE C C 176.569 0.2 1 532 . 94 SER N N 117.618 0.05 1 533 . 94 SER H H 8.453 0.02 1 534 . 94 SER CA C 60.501 0.2 1 535 . 94 SER CB C 61.863 0.2 1 536 . 94 SER C C 173.817 0.2 1 537 . 95 ASP N N 117.761 0.05 1 538 . 95 ASP H H 8.929 0.02 1 539 . 95 ASP CA C 53.044 0.2 1 540 . 95 ASP HA H 4.314 0.02 1 541 . 95 ASP CB C 38.427 0.2 1 542 . 95 ASP C C 176.094 0.2 1 543 . 96 ILE N N 124.984 0.05 1 544 . 96 ILE H H 7.704 0.02 1 545 . 96 ILE CA C 58.096 0.2 1 546 . 96 ILE HA H 4.147 0.02 1 547 . 96 ILE CB C 37.307 0.2 1 548 . 97 PRO CA C 63.3 0.2 1 549 . 97 PRO CB C 31.344 0.2 1 550 . 97 PRO C C 176.834 0.2 1 551 . 98 GLN N N 123.148 0.05 1 552 . 98 GLN H H 8.839 0.02 1 553 . 98 GLN CA C 58.267 0.2 1 554 . 98 GLN CB C 26.988 0.2 1 555 . 98 GLN C C 178.433 0.2 1 556 . 99 GLU N N 117.152 0.05 1 557 . 99 GLU H H 8.981 0.02 1 558 . 99 GLU CA C 57.258 0.2 1 559 . 99 GLU HA H 4.189 0.02 1 560 . 99 GLU CB C 26.521 0.2 1 561 . 99 GLU C C 176.659 0.2 1 562 . 100 PHE N N 115.858 0.05 1 563 . 100 PHE H H 7.954 0.02 1 564 . 100 PHE CA C 58.609 0.2 1 565 . 100 PHE CB C 38.112 0.2 1 566 . 100 PHE C C 178.832 0.2 1 567 . 101 ARG N N 121.078 0.05 1 568 . 101 ARG H H 7.918 0.02 1 569 . 101 ARG CA C 54.687 0.2 1 570 . 101 ARG CB C 27.347 0.2 1 571 . 101 ARG C C 174.676 0.2 1 572 . 102 GLY N N 106.818 0.05 1 573 . 102 GLY H H 7.121 0.02 1 574 . 102 GLY CA C 43.907 0.2 1 575 . 102 GLY HA3 H 4.076 0.02 2 576 . 102 GLY HA2 H 4.366 0.02 2 577 . 102 GLY C C 174.25 0.2 1 578 . 103 ASP N N 122.147 0.05 1 579 . 103 ASP H H 8.736 0.02 1 580 . 103 ASP CA C 51.542 0.2 1 581 . 103 ASP HA H 5.045 0.02 1 582 . 103 ASP CB C 42.334 0.2 1 583 . 103 ASP C C 174.949 0.2 1 584 . 104 TYR N N 120.55 0.05 1 585 . 104 TYR H H 9.373 0.02 1 586 . 104 TYR CA C 56.071 0.2 1 587 . 104 TYR HA H 4.702 0.02 1 588 . 104 TYR CB C 39.343 0.2 1 589 . 104 TYR C C 172.174 0.2 1 590 . 105 ILE N N 128.41 0.05 1 591 . 105 ILE H H 8.071 0.02 1 592 . 105 ILE CA C 56.141 0.2 1 593 . 105 ILE HA H 4.206 0.02 1 594 . 105 ILE CB C 36.456 0.2 1 595 . 106 PRO CA C 60.828 0.2 1 596 . 106 PRO CB C 30.521 0.2 1 597 . 106 PRO C C 176.414 0.2 1 598 . 107 HIS N N 120.249 0.05 1 599 . 107 HIS H H 8.103 0.02 1 600 . 107 HIS CA C 55.016 0.2 1 601 . 107 HIS HA H 4.588 0.02 1 602 . 107 HIS CB C 29.709 0.2 1 603 . 107 HIS C C 176.744 0.2 1 604 . 108 GLU N N 124.603 0.05 1 605 . 108 GLU H H 9.017 0.02 1 606 . 108 GLU CA C 59.477 0.2 1 607 . 108 GLU HA H 4.59 0.02 1 608 . 108 GLU CB C 27.561 0.2 1 609 . 108 GLU C C 178.979 0.2 1 610 . 109 ALA N N 122.82 0.05 1 611 . 109 ALA H H 9.847 0.02 1 612 . 109 ALA CA C 54.15 0.2 1 613 . 109 ALA HA H 4.225 0.02 1 614 . 109 ALA CB C 16.577 0.2 1 615 . 109 ALA C C 180.982 0.2 1 616 . 110 SER N N 115.185 0.05 1 617 . 110 SER H H 7.576 0.02 1 618 . 110 SER CA C 60.491 0.2 1 619 . 110 SER HA H 4.397 0.02 1 620 . 110 SER C C 175.412 0.2 1 621 . 111 ILE N N 122.51 0.05 1 622 . 111 ILE H H 7.764 0.02 1 623 . 111 ILE CA C 64.933 0.2 1 624 . 111 ILE HA H 3.883 0.02 1 625 . 111 ILE CB C 36.042 0.2 1 626 . 111 ILE C C 177.467 0.2 1 627 . 112 ALA N N 120.004 0.05 1 628 . 112 ALA H H 7.959 0.02 1 629 . 112 ALA CA C 54.123 0.2 1 630 . 112 ALA HA H 4.216 0.02 1 631 . 112 ALA CB C 16.013 0.2 1 632 . 112 ALA C C 181.338 0.2 1 633 . 113 ILE N N 119.848 0.05 1 634 . 113 ILE H H 7.516 0.02 1 635 . 113 ILE CA C 63.8 0.2 1 636 . 113 ILE CB C 36.26 0.2 1 637 . 113 ILE C C 178.424 0.2 1 638 . 114 SER N N 115.04 0.05 1 639 . 114 SER H H 7.654 0.02 1 640 . 114 SER CA C 60.208 0.2 1 641 . 114 SER HA H 4.195 0.02 1 642 . 114 SER CB C 61.977 0.2 1 643 . 114 SER C C 178.03 0.2 1 644 . 115 GLN N N 119.482 0.05 1 645 . 115 GLN H H 9.111 0.02 1 646 . 115 GLN CA C 56.889 0.2 1 647 . 115 GLN HA H 3.823 0.02 1 648 . 115 GLN CB C 27.499 0.2 1 649 . 115 GLN C C 177.32 0.2 1 650 . 116 ALA N N 120.073 0.05 1 651 . 116 ALA H H 8.237 0.02 1 652 . 116 ALA CA C 53.842 0.2 1 653 . 116 ALA HA H 4.207 0.02 1 654 . 116 ALA CB C 16.075 0.2 1 655 . 116 ALA C C 180.378 0.2 1 656 . 117 ARG N N 117.906 0.05 1 657 . 117 ARG H H 7.311 0.02 1 658 . 117 ARG CA C 56.697 0.2 1 659 . 117 ARG HA H 4.198 0.02 1 660 . 117 ARG CB C 26.957 0.2 1 661 . 117 ARG C C 178.028 0.2 1 662 . 118 LEU N N 118.898 0.05 1 663 . 118 LEU H H 7.123 0.02 1 664 . 118 LEU CA C 57.053 0.2 1 665 . 118 LEU HA H 3.592 0.02 1 666 . 118 LEU CB C 38.249 0.2 1 667 . 118 LEU C C 179.407 0.2 1 668 . 119 ASP N N 119.09 0.05 1 669 . 119 ASP H H 8.69 0.02 1 670 . 119 ASP CA C 56.43 0.2 1 671 . 119 ASP HA H 4.183 0.02 1 672 . 119 ASP CB C 38.488 0.2 1 673 . 119 ASP C C 179.623 0.2 1 674 . 120 GLU N N 121.928 0.05 1 675 . 120 GLU H H 8.184 0.02 1 676 . 120 GLU CA C 57.892 0.2 1 677 . 120 GLU HA H 4.032 0.02 1 678 . 120 GLU CB C 27.823 0.2 1 679 . 120 GLU C C 179.189 0.2 1 680 . 121 LYS N N 118.031 0.05 1 681 . 121 LYS H H 7.695 0.02 1 682 . 121 LYS CA C 57.021 0.2 1 683 . 121 LYS HA H 4.056 0.02 1 684 . 121 LYS CB C 29.305 0.2 1 685 . 121 LYS C C 180.317 0.2 1 686 . 122 ILE N N 121.245 0.05 1 687 . 122 ILE H H 7.952 0.02 1 688 . 122 ILE CA C 63.526 0.2 1 689 . 122 ILE HA H 3.391 0.02 1 690 . 122 ILE CB C 35.378 0.2 1 691 . 122 ILE C C 177.866 0.2 1 692 . 123 ALA N N 117.84 0.05 1 693 . 123 ALA H H 7.777 0.02 1 694 . 123 ALA CA C 52.897 0.2 1 695 . 123 ALA HA H 4.079 0.02 1 696 . 123 ALA CB C 16.424 0.2 1 697 . 123 ALA C C 179.63 0.2 1 698 . 124 GLN N N 114.776 0.05 1 699 . 124 GLN H H 7.409 0.02 1 700 . 124 GLN CA C 56.595 0.2 1 701 . 124 GLN HA H 4.156 0.02 1 702 . 124 GLN CB C 27.731 0.2 1 703 . 124 GLN C C 177.799 0.2 1 704 . 125 ARG N N 114.921 0.05 1 705 . 125 ARG H H 7.594 0.02 1 706 . 125 ARG CA C 53.174 0.2 1 707 . 125 ARG HA H 4.732 0.02 1 708 . 125 ARG CB C 29.417 0.2 1 709 . 126 PRO CA C 65.374 0.2 1 710 . 126 PRO CB C 30.21 0.2 1 711 . 126 PRO C C 178.323 0.2 1 712 . 127 THR N N 104.685 0.05 1 713 . 127 THR H H 7.864 0.02 1 714 . 127 THR CA C 61.589 0.2 1 715 . 127 THR HA H 4.364 0.02 1 716 . 127 THR CB C 68.123 0.2 1 717 . 127 THR C C 174.468 0.2 1 718 . 128 TRP N N 122.689 0.05 1 719 . 128 TRP H H 8.02 0.02 1 720 . 128 TRP CA C 58.523 0.2 1 721 . 128 TRP HA H 4.334 0.02 1 722 . 128 TRP C C 177.469 0.2 1 723 . 129 TYR N N 114.89 0.05 1 724 . 129 TYR H H 6.903 0.02 1 725 . 129 TYR CA C 59.569 0.2 1 726 . 129 TYR HA H 3.89 0.02 1 727 . 129 TYR CB C 39.841 0.2 1 728 . 129 TYR C C 174.498 0.2 1 729 . 130 LYS N N 119.457 0.05 1 730 . 130 LYS H H 8.733 0.02 1 731 . 130 LYS CA C 52.535 0.2 1 732 . 130 LYS HA H 4.45 0.02 1 733 . 130 LYS CB C 36.33 0.2 1 734 . 130 LYS C C 174.552 0.2 1 735 . 131 TYR N N 122.115 0.05 1 736 . 131 TYR H H 9.404 0.02 1 737 . 131 TYR CA C 57.483 0.2 1 738 . 131 TYR HA H 4.731 0.02 1 739 . 131 TYR CB C 40.356 0.2 1 740 . 131 TYR C C 176.693 0.2 1 741 . 132 TYR N N 133.334 0.05 1 742 . 132 TYR H H 11.366 0.02 1 743 . 132 TYR CA C 58.795 0.2 1 744 . 132 TYR CB C 40.19 0.2 1 745 . 132 TYR C C 177.602 0.2 1 746 . 133 GLY N N 103.159 0.05 1 747 . 133 GLY H H 9.949 0.02 1 748 . 133 GLY CA C 45.035 0.2 1 749 . 133 GLY HA3 H 3.483 0.02 2 750 . 133 GLY HA2 H 4.188 0.02 2 751 . 133 GLY C C 173.95 0.2 1 752 . 134 LYS N N 120.566 0.05 1 753 . 134 LYS H H 7.801 0.02 1 754 . 134 LYS CA C 53.684 0.2 1 755 . 134 LYS HA H 4.663 0.02 1 756 . 134 LYS CB C 32.572 0.2 1 757 . 134 LYS C C 176.565 0.2 1 758 . 135 ALA N N 130.333 0.05 1 759 . 135 ALA H H 9.131 0.02 1 760 . 135 ALA CA C 51.101 0.2 1 761 . 135 ALA CB C 15.291 0.2 1 762 . 135 ALA C C 177.946 0.2 1 763 . 136 ILE N N 114.668 0.05 1 764 . 136 ILE H H 6.927 0.02 1 765 . 136 ILE CA C 61.177 0.2 1 766 . 136 ILE HA H 4.264 0.02 1 767 . 136 ILE CB C 36.537 0.2 1 768 . 136 ILE C C 176.862 0.2 1 769 . 137 TYR N N 123.215 0.05 1 770 . 137 TYR H H 8.994 0.02 1 771 . 137 TYR CA C 57.576 0.2 1 772 . 137 TYR HA H 4.463 0.02 1 773 . 137 TYR CB C 36.531 0.2 1 774 . 137 TYR C C 174.321 0.2 1 775 . 138 ALA N N 127.071 0.05 1 776 . 138 ALA H H 7.289 0.02 1 777 . 138 ALA CA C 52.416 0.2 1 778 . 138 ALA HA H 4.055 0.02 1 779 . 138 ALA CB C 19.24 0.2 1 stop_ save_