data_5270 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13C resonance assignments of YqgF, an Escherichia coli protein of unknown structure and function ; _BMRB_accession_number 5270 _BMRB_flat_file_name bmr5270.str _Entry_type original _Submission_date 2002-01-31 _Accession_date 2002-01-31 _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 Liu Dingjiang . . 2 Repaka Prasanti . . 3 Taremi Shane S . 4 Wyss Daniel F . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 213 "13C chemical shifts" 340 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-04-09 update BMRB 'addition of relation loop' 2003-01-06 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5758 'full assignment of YqgF' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C Resonance Assignments of YqgF, an Escherichia coli Protein of unknown Structure and Function ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22147548 _PubMed_ID 12153044 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Repaka Prasanti . . 3 Taremi Shane S . 4 Wyss Daniel F . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 159 _Page_last 160 _Year 2002 _Details . loop_ _Keyword YqgF 'structural genomics' 'NMR assignments' 'antibiotics resistance' anti-microbial stop_ save_ ################################## # Molecular system description # ################################## save_system_YqgF _Saveframe_category molecular_system _Mol_system_name YqgF _Abbreviation_common YqgF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label YqgF $YqgF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YqgF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YqgF _Abbreviation_common YqgF _Molecular_mass . _Mol_thiol_state 'not present' _Details ; The construct used here including a N-terminal RGSMADIGS sequence which is not included in chemical shift data. ; ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; RGSMADIGSMSGTLLAFDFG TKSIGVAVGQRITGTARPLP AIKAQDGTPDWNIIERLLKE WQPDEIIVGLPLNMDGTEQP LTARARKFANRIHGRFGVEV KLHDERLSTVEARSGLFEQG GYRALNKGKVDSASAVIILE SYFEQGY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -9 ARG 2 -8 GLY 3 -7 SER 4 -6 MET 5 -5 ALA 6 -4 ASP 7 -3 ILE 8 -2 GLY 9 -1 SER 10 1 MET 11 2 SER 12 3 GLY 13 4 THR 14 5 LEU 15 6 LEU 16 7 ALA 17 8 PHE 18 9 ASP 19 10 PHE 20 11 GLY 21 12 THR 22 13 LYS 23 14 SER 24 15 ILE 25 16 GLY 26 17 VAL 27 18 ALA 28 19 VAL 29 20 GLY 30 21 GLN 31 22 ARG 32 23 ILE 33 24 THR 34 25 GLY 35 26 THR 36 27 ALA 37 28 ARG 38 29 PRO 39 30 LEU 40 31 PRO 41 32 ALA 42 33 ILE 43 34 LYS 44 35 ALA 45 36 GLN 46 37 ASP 47 38 GLY 48 39 THR 49 40 PRO 50 41 ASP 51 42 TRP 52 43 ASN 53 44 ILE 54 45 ILE 55 46 GLU 56 47 ARG 57 48 LEU 58 49 LEU 59 50 LYS 60 51 GLU 61 52 TRP 62 53 GLN 63 54 PRO 64 55 ASP 65 56 GLU 66 57 ILE 67 58 ILE 68 59 VAL 69 60 GLY 70 61 LEU 71 62 PRO 72 63 LEU 73 64 ASN 74 65 MET 75 66 ASP 76 67 GLY 77 68 THR 78 69 GLU 79 70 GLN 80 71 PRO 81 72 LEU 82 73 THR 83 74 ALA 84 75 ARG 85 76 ALA 86 77 ARG 87 78 LYS 88 79 PHE 89 80 ALA 90 81 ASN 91 82 ARG 92 83 ILE 93 84 HIS 94 85 GLY 95 86 ARG 96 87 PHE 97 88 GLY 98 89 VAL 99 90 GLU 100 91 VAL 101 92 LYS 102 93 LEU 103 94 HIS 104 95 ASP 105 96 GLU 106 97 ARG 107 98 LEU 108 99 SER 109 100 THR 110 101 VAL 111 102 GLU 112 103 ALA 113 104 ARG 114 105 SER 115 106 GLY 116 107 LEU 117 108 PHE 118 109 GLU 119 110 GLN 120 111 GLY 121 112 GLY 122 113 TYR 123 114 ARG 124 115 ALA 125 116 LEU 126 117 ASN 127 118 LYS 128 119 GLY 129 120 LYS 130 121 VAL 131 122 ASP 132 123 SER 133 124 ALA 134 125 SER 135 126 ALA 136 127 VAL 137 128 ILE 138 129 ILE 139 130 LEU 140 131 GLU 141 132 SER 142 133 TYR 143 134 PHE 144 135 GLU 145 136 GLN 146 137 GLY 147 138 TYR 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 BMRB 5758 YqgF 100.00 147 100.00 100.00 8.07e-102 PDB 1NMN "Structure Of Yqgf From Escherichia Coli, A Hypothetical Protein" 93.88 138 100.00 100.00 3.72e-95 PDB 1NU0 "Structure Of The Double Mutant (L6m; F134m, Semet Form) Of Yqgf From Escherichia Coli, A Hypothetical Protein" 93.20 138 97.81 97.81 5.14e-91 PDB 1OVQ "Solution Structure Of The Hypothetical Protein Yqgf From Escherichia Coli" 93.20 138 100.00 100.00 5.23e-94 DBJ BAB37248 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 93.88 138 98.55 100.00 1.68e-94 DBJ BAE77012 "predicted Holliday junction resolvase [Escherichia coli str. K-12 substr. W3110]" 93.88 138 100.00 100.00 3.72e-95 DBJ BAG78741 "conserved hypothetical protein [Escherichia coli SE11]" 93.88 138 99.28 100.00 1.52e-94 DBJ BAI27233 "predicted Holliday junction resolvase [Escherichia coli O26:H11 str. 11368]" 93.88 138 99.28 100.00 9.11e-95 DBJ BAI32263 "predicted Holliday junction resolvase [Escherichia coli O103:H2 str. 12009]" 93.88 138 99.28 100.00 9.11e-95 EMBL CAP77386 "Holliday junction resolvase [Escherichia coli LF82]" 93.88 138 100.00 100.00 3.72e-95 EMBL CAQ33259 "predicted Holliday junction resolvase [Escherichia coli BL21(DE3)]" 93.88 138 99.28 99.28 4.25e-94 EMBL CAQ90381 "Holliday junction resolvase [Escherichia fergusonii ATCC 35469]" 93.88 138 99.28 100.00 9.11e-95 EMBL CAQ99897 "Holliday junction resolvase [Escherichia coli IAI1]" 93.88 138 99.28 100.00 9.11e-95 EMBL CAR04466 "Holliday junction resolvase [Escherichia coli S88]" 93.88 138 100.00 100.00 3.72e-95 GB AAA69116 "ORF_o180; was also ORF_o62p before splice [Escherichia coli str. K-12 substr. MG1655]" 93.88 180 100.00 100.00 1.99e-94 GB AAC75986 "putative Holliday junction resolvase [Escherichia coli str. K-12 substr. MG1655]" 93.88 138 100.00 100.00 3.72e-95 GB AAG58080 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 93.88 138 98.55 100.00 1.68e-94 GB AAN44421 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 93.88 138 99.28 100.00 9.11e-95 GB AAN81983 "Hypothetical protein yqgF [Escherichia coli CFT073]" 93.88 138 100.00 100.00 3.72e-95 REF NP_289521 "Holliday junction resolvase-like protein [Escherichia coli O157:H7 str. EDL933]" 93.88 138 98.55 100.00 1.68e-94 REF NP_311852 "Holliday junction resolvase-like protein [Escherichia coli O157:H7 str. Sakai]" 93.88 138 98.55 100.00 1.68e-94 REF NP_417424 "putative Holliday junction resolvase [Escherichia coli str. K-12 substr. MG1655]" 93.88 138 100.00 100.00 3.72e-95 REF NP_708714 "Holliday junction resolvase-like protein [Shigella flexneri 2a str. 301]" 93.88 138 99.28 100.00 9.11e-95 REF NP_755410 "Holliday junction resolvase-like protein [Escherichia coli CFT073]" 93.88 138 100.00 100.00 3.72e-95 SP A1AFD5 "RecName: Full=Putative Holliday junction resolvase [Escherichia coli APEC O1]" 93.88 138 100.00 100.00 3.72e-95 SP A7ZR72 "RecName: Full=Putative Holliday junction resolvase [Escherichia coli E24377A]" 93.88 138 99.28 100.00 9.11e-95 SP A8A489 "RecName: Full=Putative Holliday junction resolvase [Escherichia coli HS]" 93.88 138 100.00 100.00 3.72e-95 SP B1IT58 "RecName: Full=Putative Holliday junction resolvase [Escherichia coli ATCC 8739]" 93.88 138 100.00 100.00 3.72e-95 SP B1LDF8 "RecName: Full=Putative Holliday junction resolvase [Escherichia coli SMS-3-5]" 93.88 138 99.28 100.00 9.11e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YqgF 'E. coli' 562 Eubacteria . Escherichia coli 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 $YqgF 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $YqgF . mM 0.3 1.0 [U-15N] KiPO4 75 mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $YqgF . mM 0.5 1.0 '[U-13C; U-15N]' KiPO4 75 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2000 loop_ _Task process stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HN(CO)_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO) _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONNH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONNH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO) _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONNH _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 7.5 0.1 n/a temperature 298 0.5 K 'ionic strength' 0.45 0.05 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_cs_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name YqgF _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 . 10 MET N N 121.79 0.2 1 2 . 10 MET CA C 55.29 0.2 1 3 . 10 MET HA H 4.18 0.02 1 4 . 10 MET CB C 32.96 0.2 1 5 . 10 MET C C 176.36 0.2 1 6 . 11 SER N N 119.32 0.2 1 7 . 11 SER H H 9.46 0.02 1 8 . 11 SER CA C 59.00 0.2 1 9 . 11 SER HA H 4.53 0.02 1 10 . 11 SER CB C 64.50 0.2 1 11 . 11 SER C C 176.34 0.2 1 12 . 12 GLY N N 113.66 0.2 1 13 . 12 GLY H H 9.60 0.02 1 14 . 12 GLY CA C 46.08 0.2 1 15 . 12 GLY C C 174.23 0.2 1 16 . 13 THR N N 119.10 0.2 1 17 . 13 THR H H 8.59 0.02 1 18 . 13 THR CA C 62.02 0.2 1 19 . 13 THR HA H 5.02 0.02 1 20 . 13 THR CB C 69.97 0.2 1 21 . 13 THR C C 172.96 0.2 1 22 . 14 LEU N N 126.14 0.2 1 23 . 14 LEU H H 9.00 0.02 1 24 . 14 LEU CA C 54.75 0.2 1 25 . 14 LEU HA H 5.07 0.02 1 26 . 14 LEU CB C 46.18 0.2 1 27 . 14 LEU C C 174.83 0.2 1 28 . 15 LEU N N 118.02 0.2 1 29 . 15 LEU H H 7.01 0.02 1 30 . 15 LEU CA C 52.61 0.2 1 31 . 15 LEU HA H 5.10 0.02 1 32 . 15 LEU CB C 47.02 0.2 1 33 . 15 LEU C C 174.37 0.2 1 34 . 16 ALA N N 122.44 0.2 1 35 . 16 ALA H H 8.66 0.02 1 36 . 16 ALA CA C 48.84 0.2 1 37 . 16 ALA HA H 5.71 0.02 1 38 . 16 ALA CB C 24.66 0.2 1 39 . 16 ALA C C 175.04 0.2 1 40 . 17 PHE N N 115.16 0.2 1 41 . 17 PHE H H 8.83 0.02 1 42 . 17 PHE CA C 54.92 0.2 1 43 . 17 PHE HA H 5.79 0.02 1 44 . 17 PHE CB C 43.66 0.2 1 45 . 17 PHE C C 174.12 0.2 1 46 . 18 ASP N N 121.03 0.2 1 47 . 18 ASP H H 8.56 0.02 1 48 . 18 ASP CA C 51.40 0.2 1 49 . 18 ASP HA H 5.11 0.02 1 50 . 18 ASP CB C 43.48 0.2 1 51 . 18 ASP C C 175.14 0.2 1 52 . 19 PHE N N 126.58 0.2 1 53 . 19 PHE H H 9.86 0.02 1 54 . 19 PHE CA C 60.89 0.2 1 55 . 19 PHE HA H 3.69 0.02 1 56 . 19 PHE CB C 39.47 0.2 1 57 . 19 PHE C C 173.43 0.2 1 58 . 20 GLY N N 114.56 0.2 1 59 . 20 GLY H H 5.99 0.02 1 60 . 20 GLY CA C 43.70 0.2 1 61 . 20 GLY C C 170.74 0.2 1 62 . 21 THR N N 106.40 0.2 1 63 . 21 THR H H 7.89 0.02 1 64 . 21 THR CA C 63.78 0.2 1 65 . 21 THR HA H 3.46 0.02 1 66 . 21 THR CB C 68.15 0.2 1 67 . 22 LYS CA C 55.98 0.2 1 68 . 22 LYS CB C 34.23 0.2 1 69 . 22 LYS C C 176.99 0.2 1 70 . 23 SER N N 114.30 0.2 1 71 . 23 SER H H 7.05 0.02 1 72 . 23 SER CA C 56.46 0.2 1 73 . 23 SER HA H 4.74 0.02 1 74 . 23 SER CB C 63.95 0.2 1 75 . 23 SER C C 171.86 0.2 1 76 . 24 ILE N N 125.48 0.2 1 77 . 24 ILE H H 9.07 0.02 1 78 . 24 ILE CA C 58.88 0.2 1 79 . 24 ILE HA H 4.49 0.02 1 80 . 24 ILE CB C 40.27 0.2 1 81 . 24 ILE C C 176.09 0.2 1 82 . 25 GLY N N 114.58 0.2 1 83 . 25 GLY H H 8.83 0.02 1 84 . 25 GLY CA C 45.38 0.2 1 85 . 25 GLY C C 173.23 0.2 1 86 . 26 VAL N N 120.75 0.2 1 87 . 26 VAL H H 8.76 0.02 1 88 . 26 VAL CA C 60.59 0.2 1 89 . 26 VAL HA H 5.01 0.02 1 90 . 26 VAL CB C 34.71 0.2 1 91 . 26 VAL C C 173.36 0.2 1 92 . 27 ALA N N 126.43 0.2 1 93 . 27 ALA H H 8.52 0.02 1 94 . 27 ALA CA C 49.78 0.2 1 95 . 27 ALA HA H 4.93 0.02 1 96 . 27 ALA CB C 23.59 0.2 1 97 . 27 ALA C C 173.95 0.2 1 98 . 28 VAL N N 116.35 0.2 1 99 . 28 VAL H H 8.42 0.02 1 100 . 28 VAL CA C 57.73 0.2 1 101 . 28 VAL HA H 5.00 0.02 1 102 . 28 VAL CB C 35.02 0.2 1 103 . 28 VAL C C 173.66 0.2 1 104 . 29 GLY N N 112.30 0.2 1 105 . 29 GLY H H 8.50 0.02 1 106 . 29 GLY CA C 45.44 0.2 1 107 . 29 GLY C C 171.40 0.2 1 108 . 30 GLN N N 118.14 0.2 1 109 . 30 GLN H H 8.03 0.02 1 110 . 30 GLN CA C 53.95 0.2 1 111 . 30 GLN HA H 5.25 0.02 1 112 . 30 GLN CB C 31.18 0.2 1 113 . 30 GLN C C 175.51 0.2 1 114 . 31 ARG N N 124.84 0.2 1 115 . 31 ARG H H 8.61 0.02 1 116 . 31 ARG CA C 59.11 0.2 1 117 . 31 ARG HA H 4.05 0.02 1 118 . 31 ARG CB C 30.22 0.2 1 119 . 31 ARG C C 178.21 0.2 1 120 . 32 ILE N N 115.16 0.2 1 121 . 32 ILE H H 8.48 0.02 1 122 . 32 ILE CA C 63.59 0.2 1 123 . 32 ILE HA H 3.95 0.02 1 124 . 32 ILE CB C 37.56 0.2 1 125 . 32 ILE C C 176.43 0.2 1 126 . 33 THR N N 107.56 0.2 1 127 . 33 THR H H 6.78 0.02 1 128 . 33 THR CA C 61.46 0.2 1 129 . 33 THR HA H 4.36 0.02 1 130 . 33 THR CB C 69.76 0.2 1 131 . 33 THR C C 176.23 0.2 1 132 . 34 GLY N N 111.27 0.2 1 133 . 34 GLY H H 7.83 0.02 1 134 . 34 GLY CA C 46.27 0.2 1 135 . 34 GLY C C 173.61 0.2 1 136 . 35 THR N N 110.26 0.2 1 137 . 35 THR H H 7.34 0.02 1 138 . 35 THR CA C 59.80 0.2 1 139 . 35 THR HA H 4.69 0.02 1 140 . 35 THR CB C 72.09 0.2 1 141 . 35 THR C C 172.97 0.2 1 142 . 36 ALA N N 125.29 0.2 1 143 . 36 ALA H H 9.41 0.02 1 144 . 36 ALA CA C 50.17 0.2 1 145 . 36 ALA HA H 5.32 0.02 1 146 . 36 ALA CB C 24.85 0.2 1 147 . 36 ALA C C 175.30 0.2 1 148 . 37 ARG N N 118.75 0.2 1 149 . 37 ARG H H 9.05 0.02 1 150 . 37 ARG CA C 52.34 0.2 1 151 . 37 ARG HA H 4.89 0.02 1 152 . 37 ARG CB C 31.55 0.2 1 153 . 38 PRO CA C 62.70 0.2 1 154 . 38 PRO HA H 4.52 0.02 1 155 . 38 PRO CB C 32.83 0.2 1 156 . 38 PRO C C 175.87 0.2 1 157 . 39 LEU N N 122.84 0.2 1 158 . 39 LEU H H 8.31 0.02 1 159 . 39 LEU CA C 51.93 0.2 1 160 . 39 LEU HA H 4.89 0.02 1 161 . 39 LEU CB C 41.34 0.2 1 162 . 40 PRO CA C 64.23 0.2 1 163 . 40 PRO CB C 31.62 0.2 1 164 . 40 PRO C C 175.34 0.2 1 165 . 41 ALA N N 124.23 0.2 1 166 . 41 ALA H H 8.12 0.02 1 167 . 41 ALA CA C 52.04 0.2 1 168 . 41 ALA HA H 4.39 0.02 1 169 . 41 ALA CB C 19.00 0.2 1 170 . 41 ALA C C 177.93 0.2 1 171 . 42 ILE N N 121.00 0.2 1 172 . 42 ILE H H 8.88 0.02 1 173 . 42 ILE CA C 60.04 0.2 1 174 . 42 ILE HA H 4.18 0.02 1 175 . 42 ILE CB C 40.46 0.2 1 176 . 42 ILE C C 175.56 0.2 1 177 . 43 LYS N N 127.05 0.2 1 178 . 43 LYS H H 8.58 0.02 1 179 . 43 LYS CA C 57.28 0.2 1 180 . 43 LYS HA H 4.07 0.02 1 181 . 43 LYS CB C 32.53 0.2 1 182 . 43 LYS C C 175.08 0.2 1 183 . 44 ALA N N 124.09 0.2 1 184 . 44 ALA H H 7.51 0.02 1 185 . 44 ALA CA C 49.83 0.2 1 186 . 44 ALA HA H 4.48 0.02 1 187 . 44 ALA CB C 20.85 0.2 1 188 . 44 ALA C C 174.90 0.2 1 189 . 45 GLN N N 118.55 0.2 1 190 . 45 GLN H H 7.94 0.02 1 191 . 45 GLN CA C 54.70 0.2 1 192 . 45 GLN HA H 4.49 0.02 1 193 . 45 GLN CB C 29.83 0.2 1 194 . 46 ASP CA C 55.38 0.2 1 195 . 46 ASP CB C 39.88 0.2 1 196 . 46 ASP C C 176.75 0.2 1 197 . 47 GLY N N 106.41 0.2 1 198 . 47 GLY H H 8.82 0.02 1 199 . 47 GLY CA C 45.13 0.2 1 200 . 47 GLY C C 173.03 0.2 1 201 . 48 THR N N 117.35 0.2 1 202 . 48 THR H H 7.81 0.02 1 203 . 48 THR CA C 59.47 0.2 1 204 . 48 THR HA H 4.69 0.02 1 205 . 48 THR CB C 69.51 0.2 1 206 . 49 PRO CA C 61.06 0.2 1 207 . 49 PRO HA H 4.59 0.02 1 208 . 49 PRO CB C 32.41 0.2 1 209 . 49 PRO C C 173.77 0.2 1 210 . 50 ASP N N 115.77 0.2 1 211 . 50 ASP H H 7.45 0.02 1 212 . 50 ASP CA C 53.26 0.2 1 213 . 50 ASP HA H 4.57 0.02 1 214 . 50 ASP CB C 39.58 0.2 1 215 . 50 ASP C C 177.56 0.2 1 216 . 51 TRP N N 128.24 0.2 1 217 . 51 TRP H H 8.05 0.02 1 218 . 51 TRP CA C 59.87 0.2 1 219 . 51 TRP HA H 4.36 0.02 1 220 . 51 TRP CB C 29.40 0.2 1 221 . 51 TRP C C 178.21 0.2 1 222 . 52 ASN N N 117.37 0.2 1 223 . 52 ASN H H 8.72 0.02 1 224 . 52 ASN CA C 56.50 0.2 1 225 . 52 ASN HA H 4.64 0.02 1 226 . 52 ASN CB C 37.83 0.2 1 227 . 52 ASN C C 178.46 0.2 1 228 . 53 ILE N N 120.93 0.2 1 229 . 53 ILE H H 7.64 0.02 1 230 . 53 ILE CA C 64.17 0.2 1 231 . 53 ILE HA H 3.74 0.02 1 232 . 53 ILE CB C 37.24 0.2 1 233 . 53 ILE C C 178.37 0.2 1 234 . 54 ILE N N 118.65 0.2 1 235 . 54 ILE H H 6.98 0.02 1 236 . 54 ILE CA C 65.24 0.2 1 237 . 54 ILE HA H 3.69 0.02 1 238 . 54 ILE CB C 36.79 0.2 1 239 . 54 ILE C C 176.67 0.2 1 240 . 55 GLU N N 119.76 0.2 1 241 . 55 GLU H H 8.47 0.02 1 242 . 55 GLU CA C 60.05 0.2 1 243 . 55 GLU HA H 3.41 0.02 1 244 . 55 GLU CB C 29.57 0.2 1 245 . 55 GLU C C 178.32 0.2 1 246 . 56 ARG N N 118.01 0.2 1 247 . 56 ARG H H 7.68 0.02 1 248 . 56 ARG CA C 59.60 0.2 1 249 . 56 ARG HA H 4.00 0.02 1 250 . 56 ARG CB C 29.61 0.2 1 251 . 56 ARG C C 179.05 0.2 1 252 . 57 LEU N N 120.83 0.2 1 253 . 57 LEU H H 8.10 0.02 1 254 . 57 LEU CA C 58.17 0.2 1 255 . 57 LEU HA H 4.38 0.02 1 256 . 57 LEU CB C 42.87 0.2 1 257 . 57 LEU C C 179.37 0.2 1 258 . 58 LEU N N 118.91 0.2 1 259 . 58 LEU H H 8.11 0.02 1 260 . 58 LEU CA C 57.91 0.2 1 261 . 58 LEU HA H 3.76 0.02 1 262 . 58 LEU CB C 39.16 0.2 1 263 . 58 LEU C C 180.64 0.2 1 264 . 59 LYS N N 120.18 0.2 1 265 . 59 LYS H H 8.00 0.02 1 266 . 59 LYS CA C 58.98 0.2 1 267 . 59 LYS CB C 32.66 0.2 1 268 . 59 LYS C C 178.34 0.2 1 269 . 60 GLU N N 118.29 0.2 1 270 . 60 GLU H H 8.16 0.02 1 271 . 60 GLU CA C 58.96 0.2 1 272 . 60 GLU HA H 3.82 0.02 1 273 . 60 GLU CB C 30.27 0.2 1 274 . 60 GLU C C 178.34 0.2 1 275 . 61 TRP N N 115.16 0.2 1 276 . 61 TRP H H 7.94 0.02 1 277 . 61 TRP CA C 57.90 0.2 1 278 . 61 TRP HA H 4.56 0.02 1 279 . 61 TRP CB C 30.51 0.2 1 280 . 61 TRP C C 175.41 0.2 1 281 . 62 GLN N N 113.76 0.2 1 282 . 62 GLN H H 8.00 0.02 1 283 . 62 GLN CA C 55.43 0.2 1 284 . 62 GLN HA H 4.12 0.02 1 285 . 62 GLN CB C 27.82 0.2 1 286 . 63 PRO CA C 62.41 0.2 1 287 . 63 PRO HA H 4.43 0.02 1 288 . 63 PRO CB C 32.80 0.2 1 289 . 63 PRO C C 176.98 0.2 1 290 . 64 ASP N N 120.23 0.2 1 291 . 64 ASP H H 9.15 0.02 1 292 . 64 ASP CA C 56.45 0.2 1 293 . 64 ASP HA H 4.56 0.02 1 294 . 64 ASP CB C 41.94 0.2 1 295 . 64 ASP C C 176.77 0.2 1 296 . 65 GLU N N 111.98 0.2 1 297 . 65 GLU H H 7.30 0.02 1 298 . 65 GLU CA C 54.35 0.2 1 299 . 65 GLU HA H 4.67 0.02 1 300 . 65 GLU CB C 33.79 0.2 1 301 . 65 GLU C C 173.62 0.2 1 302 . 66 ILE N N 120.55 0.2 1 303 . 66 ILE H H 8.49 0.02 1 304 . 66 ILE CA C 58.59 0.2 1 305 . 66 ILE HA H 4.93 0.02 1 306 . 66 ILE CB C 40.09 0.2 1 307 . 66 ILE C C 173.31 0.2 1 308 . 67 ILE N N 127.04 0.2 1 309 . 67 ILE H H 8.92 0.02 1 310 . 67 ILE CA C 57.79 0.2 1 311 . 67 ILE HA H 4.86 0.02 1 312 . 67 ILE CB C 37.93 0.2 1 313 . 67 ILE C C 175.06 0.2 1 314 . 68 VAL N N 126.60 0.2 1 315 . 68 VAL H H 8.91 0.02 1 316 . 68 VAL CA C 60.17 0.2 1 317 . 68 VAL HA H 5.11 0.02 1 318 . 68 VAL CB C 34.70 0.2 1 319 . 68 VAL C C 176.42 0.2 1 320 . 69 GLY N N 113.05 0.2 1 321 . 69 GLY H H 8.33 0.02 1 322 . 69 GLY CA C 46.06 0.2 1 323 . 69 GLY C C 172.50 0.2 1 324 . 70 LEU N N 125.73 0.2 1 325 . 70 LEU H H 8.51 0.02 1 326 . 70 LEU CA C 50.52 0.2 1 327 . 70 LEU HA H 5.03 0.02 1 328 . 70 LEU CB C 43.70 0.2 1 329 . 71 PRO CA C 62.34 0.2 1 330 . 71 PRO HA H 4.17 0.02 1 331 . 71 PRO CB C 31.45 0.2 1 332 . 71 PRO C C 176.04 0.2 1 333 . 72 LEU N N 123.76 0.2 1 334 . 72 LEU H H 7.90 0.02 1 335 . 72 LEU CA C 54.03 0.2 1 336 . 72 LEU HA H 4.55 0.02 1 337 . 72 LEU CB C 47.54 0.2 1 338 . 72 LEU C C 177.08 0.2 1 339 . 73 ASN N N 116.56 0.2 1 340 . 73 ASN H H 8.60 0.02 1 341 . 73 ASN CA C 53.51 0.2 1 342 . 73 ASN HA H 4.78 0.02 1 343 . 73 ASN CB C 39.14 0.2 1 344 . 74 MET CA C 58.31 0.2 1 345 . 74 MET HA H 4.13 0.02 1 346 . 74 MET CB C 31.61 0.2 1 347 . 74 MET C C 176.97 0.2 1 348 . 75 ASP N N 115.79 0.2 1 349 . 75 ASP H H 7.81 0.02 1 350 . 75 ASP CA C 53.06 0.2 1 351 . 75 ASP HA H 4.47 0.02 1 352 . 75 ASP CB C 39.67 0.2 1 353 . 75 ASP C C 177.23 0.2 1 354 . 76 GLY N N 108.28 0.2 1 355 . 76 GLY H H 8.21 0.02 1 356 . 76 GLY CA C 45.13 0.2 1 357 . 76 GLY C C 174.14 0.2 1 358 . 77 THR N N 110.96 0.2 1 359 . 77 THR H H 7.87 0.02 1 360 . 77 THR CA C 61.39 0.2 1 361 . 77 THR HA H 4.35 0.02 1 362 . 77 THR CB C 71.23 0.2 1 363 . 77 THR C C 174.15 0.2 1 364 . 78 GLU N N 117.75 0.2 1 365 . 78 GLU H H 8.44 0.02 1 366 . 78 GLU CA C 57.32 0.2 1 367 . 78 GLU HA H 4.22 0.02 1 368 . 78 GLU CB C 30.12 0.2 1 369 . 78 GLU C C 176.27 0.2 1 370 . 79 GLN N N 118.83 0.2 1 371 . 79 GLN H H 8.71 0.02 1 372 . 79 GLN CA C 53.68 0.2 1 373 . 79 GLN HA H 4.93 0.02 1 374 . 79 GLN CB C 28.80 0.2 1 375 . 80 PRO CA C 66.45 0.2 1 376 . 80 PRO HA H 4.32 0.02 1 377 . 80 PRO CB C 32.12 0.2 1 378 . 80 PRO C C 178.68 0.2 1 379 . 81 LEU N N 112.63 0.2 1 380 . 81 LEU H H 8.11 0.02 1 381 . 81 LEU CA C 55.92 0.2 1 382 . 81 LEU HA H 4.28 0.02 1 383 . 81 LEU CB C 42.29 0.2 1 384 . 81 LEU C C 177.86 0.2 1 385 . 82 THR N N 117.94 0.2 1 386 . 82 THR H H 8.14 0.02 1 387 . 82 THR CA C 68.51 0.2 1 388 . 82 THR HA H 4.22 0.02 1 389 . 82 THR CB C 68.86 0.2 1 390 . 82 THR C C 175.91 0.2 1 391 . 83 ALA N N 121.11 0.2 1 392 . 83 ALA H H 8.46 0.02 1 393 . 83 ALA CA C 55.05 0.2 1 394 . 83 ALA HA H 4.03 0.02 1 395 . 83 ALA CB C 18.17 0.2 1 396 . 83 ALA C C 181.00 0.2 1 397 . 84 ARG N N 117.22 0.2 1 398 . 84 ARG H H 7.43 0.02 1 399 . 84 ARG CA C 58.46 0.2 1 400 . 84 ARG HA H 3.88 0.02 1 401 . 84 ARG CB C 30.17 0.2 1 402 . 84 ARG C C 178.29 0.2 1 403 . 85 ALA N N 125.33 0.2 1 404 . 85 ALA H H 8.22 0.02 1 405 . 85 ALA CA C 55.23 0.2 1 406 . 85 ALA HA H 3.35 0.02 1 407 . 85 ALA CB C 17.64 0.2 1 408 . 85 ALA C C 179.17 0.2 1 409 . 86 ARG N N 116.03 0.2 1 410 . 86 ARG H H 7.89 0.02 1 411 . 86 ARG CA C 60.05 0.2 1 412 . 86 ARG HA H 3.88 0.02 1 413 . 86 ARG CB C 29.92 0.2 1 414 . 86 ARG C C 178.95 0.2 1 415 . 87 LYS N N 119.53 0.2 1 416 . 87 LYS H H 7.79 0.02 1 417 . 87 LYS CA C 59.39 0.2 1 418 . 87 LYS HA H 4.07 0.02 1 419 . 87 LYS CB C 31.95 0.2 1 420 . 87 LYS C C 178.50 0.2 1 421 . 88 PHE N N 121.38 0.2 1 422 . 88 PHE H H 7.90 0.02 1 423 . 88 PHE CA C 60.56 0.2 1 424 . 88 PHE HA H 4.42 0.02 1 425 . 88 PHE CB C 39.07 0.2 1 426 . 88 PHE C C 179.05 0.2 1 427 . 89 ALA N N 120.40 0.2 1 428 . 89 ALA H H 8.11 0.02 1 429 . 89 ALA CA C 55.36 0.2 1 430 . 89 ALA HA H 3.71 0.02 1 431 . 89 ALA CB C 18.60 0.2 1 432 . 89 ALA C C 179.08 0.2 1 433 . 90 ASN N N 115.51 0.2 1 434 . 90 ASN H H 7.97 0.02 1 435 . 90 ASN CA C 55.89 0.2 1 436 . 90 ASN HA H 4.44 0.02 1 437 . 90 ASN CB C 38.56 0.2 1 438 . 90 ASN C C 178.59 0.2 1 439 . 91 ARG N N 122.30 0.2 1 440 . 91 ARG H H 8.58 0.02 1 441 . 91 ARG CA C 58.58 0.2 1 442 . 91 ARG HA H 4.03 0.02 1 443 . 91 ARG CB C 30.12 0.2 1 444 . 91 ARG C C 178.96 0.2 1 445 . 92 ILE N N 119.63 0.2 1 446 . 92 ILE H H 8.13 0.02 1 447 . 92 ILE CA C 65.06 0.2 1 448 . 92 ILE HA H 3.65 0.02 1 449 . 92 ILE CB C 37.31 0.2 1 450 . 92 ILE C C 178.03 0.2 1 451 . 93 HIS N N 119.16 0.2 1 452 . 93 HIS H H 7.78 0.02 1 453 . 93 HIS CA C 59.94 0.2 1 454 . 93 HIS HA H 4.32 0.02 1 455 . 93 HIS CB C 29.60 0.2 1 456 . 93 HIS C C 178.78 0.2 1 457 . 94 GLY N N 106.23 0.2 1 458 . 94 GLY H H 8.54 0.02 1 459 . 94 GLY CA C 46.48 0.2 1 460 . 94 GLY C C 175.16 0.2 1 461 . 95 ARG N N 118.28 0.2 1 462 . 95 ARG H H 7.79 0.02 1 463 . 95 ARG CA C 57.74 0.2 1 464 . 95 ARG HA H 3.72 0.02 1 465 . 95 ARG CB C 30.22 0.2 1 466 . 95 ARG C C 177.97 0.2 1 467 . 96 PHE N N 112.17 0.2 1 468 . 96 PHE H H 7.55 0.02 1 469 . 96 PHE CA C 57.53 0.2 1 470 . 96 PHE HA H 4.87 0.02 1 471 . 96 PHE CB C 40.50 0.2 1 472 . 96 PHE C C 176.96 0.2 1 473 . 97 GLY N N 109.28 0.2 1 474 . 97 GLY H H 8.06 0.02 1 475 . 97 GLY CA C 46.48 0.2 1 476 . 97 GLY C C 173.56 0.2 1 477 . 98 VAL N N 115.04 0.2 1 478 . 98 VAL H H 6.57 0.02 1 479 . 98 VAL CA C 59.32 0.2 1 480 . 98 VAL HA H 4.34 0.02 1 481 . 98 VAL CB C 33.48 0.2 1 482 . 98 VAL C C 174.60 0.2 1 483 . 99 GLU N N 126.59 0.2 1 484 . 99 GLU H H 8.68 0.02 1 485 . 99 GLU CA C 57.48 0.2 1 486 . 99 GLU HA H 4.20 0.02 1 487 . 99 GLU CB C 29.78 0.2 1 488 . 99 GLU C C 175.00 0.2 1 489 . 100 VAL N N 124.58 0.2 1 490 . 100 VAL H H 8.03 0.02 1 491 . 100 VAL CA C 59.83 0.2 1 492 . 100 VAL HA H 5.09 0.02 1 493 . 100 VAL CB C 34.25 0.2 1 494 . 100 VAL C C 175.81 0.2 1 495 . 101 LYS N N 126.98 0.2 1 496 . 101 LYS H H 9.10 0.02 1 497 . 101 LYS CA C 53.83 0.2 1 498 . 101 LYS HA H 4.60 0.02 1 499 . 101 LYS CB C 34.74 0.2 1 500 . 101 LYS C C 174.85 0.2 1 501 . 102 LEU N N 122.62 0.2 1 502 . 102 LEU H H 8.41 0.02 1 503 . 102 LEU CA C 53.13 0.2 1 504 . 102 LEU HA H 5.31 0.02 1 505 . 102 LEU CB C 42.76 0.2 1 506 . 102 LEU C C 177.07 0.2 1 507 . 103 HIS N N 123.77 0.2 1 508 . 103 HIS H H 8.51 0.02 1 509 . 103 HIS CA C 55.37 0.2 1 510 . 103 HIS HA H 4.96 0.02 1 511 . 103 HIS CB C 33.90 0.2 1 512 . 103 HIS C C 173.58 0.2 1 513 . 104 ASP N N 128.94 0.2 1 514 . 104 ASP H H 8.18 0.02 1 515 . 104 ASP CA C 54.36 0.2 1 516 . 104 ASP HA H 4.46 0.02 1 517 . 104 ASP CB C 40.98 0.2 1 518 . 104 ASP C C 175.85 0.2 1 519 . 105 GLU N N 126.13 0.2 1 520 . 105 GLU H H 8.36 0.02 1 521 . 105 GLU CA C 57.17 0.2 1 522 . 105 GLU HA H 4.06 0.02 1 523 . 105 GLU CB C 30.49 0.2 1 524 . 105 GLU C C 176.99 0.2 1 525 . 106 ARG N N 120.42 0.2 1 526 . 106 ARG H H 8.61 0.02 1 527 . 106 ARG CA C 56.86 0.2 1 528 . 106 ARG HA H 4.21 0.02 1 529 . 106 ARG CB C 30.05 0.2 1 530 . 106 ARG C C 177.66 0.2 1 531 . 107 LEU N N 119.45 0.2 1 532 . 107 LEU H H 7.89 0.02 1 533 . 107 LEU CA C 55.73 0.2 1 534 . 107 LEU HA H 4.25 0.02 1 535 . 107 LEU CB C 42.20 0.2 1 536 . 107 LEU C C 177.57 0.2 1 537 . 108 SER N N 114.86 0.2 1 538 . 108 SER H H 8.01 0.02 1 539 . 108 SER CA C 58.23 0.2 1 540 . 108 SER CB C 63.73 0.2 1 541 . 108 SER C C 174.88 0.2 1 542 . 109 THR N N 114.58 0.2 1 543 . 109 THR H H 7.97 0.02 1 544 . 109 THR CA C 61.48 0.2 1 545 . 109 THR HA H 4.40 0.02 1 546 . 109 THR CB C 69.50 0.2 1 547 . 109 THR C C 174.93 0.2 1 548 . 110 VAL N N 121.44 0.2 1 549 . 110 VAL H H 8.06 0.02 1 550 . 110 VAL CA C 63.23 0.2 1 551 . 110 VAL HA H 3.97 0.02 1 552 . 110 VAL CB C 32.25 0.2 1 553 . 110 VAL C C 176.90 0.2 1 554 . 111 GLU N N 123.06 0.2 1 555 . 111 GLU H H 8.46 0.02 1 556 . 111 GLU CA C 57.27 0.2 1 557 . 111 GLU HA H 4.15 0.02 1 558 . 111 GLU CB C 29.67 0.2 1 559 . 111 GLU C C 176.94 0.2 1 560 . 112 ALA N N 124.24 0.2 1 561 . 112 ALA H H 8.17 0.02 1 562 . 112 ALA CA C 53.21 0.2 1 563 . 112 ALA HA H 4.18 0.02 1 564 . 112 ALA CB C 19.00 0.2 1 565 . 114 SER CA C 59.34 0.2 1 566 . 114 SER CB C 63.81 0.2 1 567 . 115 GLY N N 110.38 0.2 1 568 . 115 GLY H H 8.26 0.02 1 569 . 115 GLY CA C 45.53 0.2 1 570 . 115 GLY C C 174.29 0.2 1 571 . 116 LEU N N 120.93 0.2 1 572 . 116 LEU H H 7.86 0.02 1 573 . 116 LEU CA C 55.63 0.2 1 574 . 116 LEU HA H 4.15 0.02 1 575 . 116 LEU CB C 41.98 0.2 1 576 . 132 SER CA C 58.89 0.2 1 577 . 132 SER CB C 64.03 0.2 1 578 . 132 SER C C 174.36 0.2 1 579 . 133 ALA N N 123.98 0.2 1 580 . 133 ALA H H 7.97 0.02 1 581 . 133 ALA CA C 55.21 0.2 1 582 . 133 ALA HA H 3.91 0.02 1 583 . 133 ALA CB C 18.99 0.2 1 584 . 133 ALA C C 180.49 0.2 1 585 . 134 SER N N 113.68 0.2 1 586 . 134 SER H H 8.43 0.02 1 587 . 134 SER CA C 61.89 0.2 1 588 . 134 SER HA H 4.14 0.02 1 589 . 134 SER C C 176.16 0.2 1 590 . 135 ALA N N 124.31 0.2 1 591 . 135 ALA H H 7.62 0.02 1 592 . 135 ALA CA C 54.74 0.2 1 593 . 135 ALA HA H 3.74 0.02 1 594 . 135 ALA CB C 17.12 0.2 1 595 . 135 ALA C C 177.90 0.2 1 596 . 136 VAL N N 117.45 0.2 1 597 . 136 VAL H H 7.15 0.02 1 598 . 136 VAL CA C 66.05 0.2 1 599 . 136 VAL HA H 2.92 0.02 1 600 . 136 VAL CB C 31.16 0.2 1 601 . 136 VAL C C 176.69 0.2 1 602 . 137 ILE N N 118.80 0.2 1 603 . 137 ILE H H 6.97 0.02 1 604 . 137 ILE CA C 64.36 0.2 1 605 . 137 ILE HA H 3.68 0.02 1 606 . 137 ILE CB C 37.07 0.2 1 607 . 137 ILE C C 179.15 0.2 1 608 . 138 ILE N N 120.52 0.2 1 609 . 138 ILE H H 7.86 0.02 1 610 . 138 ILE CA C 65.05 0.2 1 611 . 138 ILE HA H 3.48 0.02 1 612 . 138 ILE CB C 38.07 0.2 1 613 . 138 ILE C C 176.97 0.2 1 614 . 139 LEU N N 119.51 0.2 1 615 . 139 LEU H H 7.37 0.02 1 616 . 139 LEU CA C 56.94 0.2 1 617 . 139 LEU HA H 3.48 0.02 1 618 . 139 LEU CB C 39.73 0.2 1 619 . 139 LEU C C 177.62 0.2 1 620 . 140 GLU N N 116.69 0.2 1 621 . 140 GLU H H 8.47 0.02 1 622 . 140 GLU CA C 60.34 0.2 1 623 . 140 GLU HA H 3.81 0.02 1 624 . 140 GLU CB C 28.69 0.2 1 625 . 140 GLU C C 179.71 0.2 1 626 . 141 SER N N 114.51 0.2 1 627 . 141 SER H H 8.15 0.02 1 628 . 141 SER CA C 60.37 0.2 1 629 . 141 SER HA H 4.31 0.02 1 630 . 141 SER CB C 62.28 0.2 1 631 . 141 SER C C 176.94 0.2 1 632 . 142 TYR N N 124.17 0.2 1 633 . 142 TYR H H 8.14 0.02 1 634 . 142 TYR CA C 62.36 0.2 1 635 . 142 TYR HA H 3.47 0.02 1 636 . 142 TYR CB C 37.94 0.2 1 637 . 142 TYR C C 179.00 0.2 1 638 . 143 PHE N N 118.29 0.2 1 639 . 143 PHE H H 8.36 0.02 1 640 . 143 PHE CA C 57.71 0.2 1 641 . 143 PHE HA H 4.39 0.02 1 642 . 143 PHE CB C 37.56 0.2 1 643 . 143 PHE C C 178.49 0.2 1 644 . 144 GLU N N 119.07 0.2 1 645 . 144 GLU H H 7.90 0.02 1 646 . 144 GLU CA C 58.23 0.2 1 647 . 144 GLU HA H 4.07 0.02 1 648 . 144 GLU CB C 29.66 0.2 1 649 . 144 GLU C C 178.04 0.2 1 650 . 145 GLN N N 116.65 0.2 1 651 . 145 GLN H H 7.92 0.02 1 652 . 145 GLN CA C 56.72 0.2 1 653 . 145 GLN HA H 4.13 0.02 1 654 . 145 GLN CB C 28.55 0.2 1 655 . 145 GLN C C 177.54 0.2 1 656 . 146 GLY N N 107.38 0.2 1 657 . 146 GLY H H 7.83 0.02 1 658 . 146 GLY CA C 45.74 0.2 1 659 . 146 GLY C C 174.53 0.2 1 660 . 147 TYR N N 119.89 0.2 1 661 . 147 TYR H H 7.74 0.02 1 662 . 147 TYR CA C 58.28 0.2 1 663 . 147 TYR HA H 4.45 0.02 1 664 . 147 TYR CB C 38.09 0.2 1 stop_ save_