data_10096 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonance Assignments for LolB ; _BMRB_accession_number 10096 _BMRB_flat_file_name bmr10096.str _Entry_type original _Submission_date 2007-01-31 _Accession_date 2007-01-31 _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 Nakada Shingo . . 2 Sakakura Masayoshi . . 3 Takahashi Hideo . . 4 Tokuda Hajime . . 5 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 159 "13C chemical shifts" 476 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-31 update BMRB 'complete entry citation' 2007-08-22 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignment for the outer membrane lipoprotein receptor LolB from Escherichia coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636844 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shingo Nakada . . 2 Masayoshi Sakakura . . 3 Hideo Takahashi . . 4 Hajime Tokuda . . 5 Ichio Shimada . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 121 _Page_last 123 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LolB monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LolB monomer' $LolB stop_ _System_molecular_weight 21200 _System_physical_state native _System_oligomer_state 'protein monomer' _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Outer-membrane lipoprotein receptor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LolB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LolB _Molecular_mass 21300 _Mol_thiol_state 'not present' loop_ _Biological_function 'Outer-membrane lipoprotein receptor' stop_ _Details ; The signal peptides (21 aa)at the N-terminus and the next Cys residue of LolB were removed in this recombinant protein. Instead, Met and Ala residues were attached to the N-terminus. ; ############################## # Polymer residue sequence # ############################## _Residue_count 187 _Mol_residue_sequence ; MASVTTPKGPGKSPDSPQWR QHQQDVRNLNQYQTRGAFAY ISDQQKVYARFFWQQTGQDR YRLLLTNPLGSTELELNAQP GNVQLVDNKGQRYTADDAEE MIGKLTGMPIPLNSLRQWIL GLPGDATDYKLDDQYRLSEI TYSQNGKNWKVVYGGYDTKT QPAMPANMELTDGGQRIKLK MDNWIVK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 0 ALA 3 1 SER 4 2 VAL 5 3 THR 6 4 THR 7 5 PRO 8 6 LYS 9 7 GLY 10 8 PRO 11 9 GLY 12 10 LYS 13 11 SER 14 12 PRO 15 13 ASP 16 14 SER 17 15 PRO 18 16 GLN 19 17 TRP 20 18 ARG 21 19 GLN 22 20 HIS 23 21 GLN 24 22 GLN 25 23 ASP 26 24 VAL 27 25 ARG 28 26 ASN 29 27 LEU 30 28 ASN 31 29 GLN 32 30 TYR 33 31 GLN 34 32 THR 35 33 ARG 36 34 GLY 37 35 ALA 38 36 PHE 39 37 ALA 40 38 TYR 41 39 ILE 42 40 SER 43 41 ASP 44 42 GLN 45 43 GLN 46 44 LYS 47 45 VAL 48 46 TYR 49 47 ALA 50 48 ARG 51 49 PHE 52 50 PHE 53 51 TRP 54 52 GLN 55 53 GLN 56 54 THR 57 55 GLY 58 56 GLN 59 57 ASP 60 58 ARG 61 59 TYR 62 60 ARG 63 61 LEU 64 62 LEU 65 63 LEU 66 64 THR 67 65 ASN 68 66 PRO 69 67 LEU 70 68 GLY 71 69 SER 72 70 THR 73 71 GLU 74 72 LEU 75 73 GLU 76 74 LEU 77 75 ASN 78 76 ALA 79 77 GLN 80 78 PRO 81 79 GLY 82 80 ASN 83 81 VAL 84 82 GLN 85 83 LEU 86 84 VAL 87 85 ASP 88 86 ASN 89 87 LYS 90 88 GLY 91 89 GLN 92 90 ARG 93 91 TYR 94 92 THR 95 93 ALA 96 94 ASP 97 95 ASP 98 96 ALA 99 97 GLU 100 98 GLU 101 99 MET 102 100 ILE 103 101 GLY 104 102 LYS 105 103 LEU 106 104 THR 107 105 GLY 108 106 MET 109 107 PRO 110 108 ILE 111 109 PRO 112 110 LEU 113 111 ASN 114 112 SER 115 113 LEU 116 114 ARG 117 115 GLN 118 116 TRP 119 117 ILE 120 118 LEU 121 119 GLY 122 120 LEU 123 121 PRO 124 122 GLY 125 123 ASP 126 124 ALA 127 125 THR 128 126 ASP 129 127 TYR 130 128 LYS 131 129 LEU 132 130 ASP 133 131 ASP 134 132 GLN 135 133 TYR 136 134 ARG 137 135 LEU 138 136 SER 139 137 GLU 140 138 ILE 141 139 THR 142 140 TYR 143 141 SER 144 142 GLN 145 143 ASN 146 144 GLY 147 145 LYS 148 146 ASN 149 147 TRP 150 148 LYS 151 149 VAL 152 150 VAL 153 151 TYR 154 152 GLY 155 153 GLY 156 154 TYR 157 155 ASP 158 156 THR 159 157 LYS 160 158 THR 161 159 GLN 162 160 PRO 163 161 ALA 164 162 MET 165 163 PRO 166 164 ALA 167 165 ASN 168 166 MET 169 167 GLU 170 168 LEU 171 169 THR 172 170 ASP 173 171 GLY 174 172 GLY 175 173 GLN 176 174 ARG 177 175 ILE 178 176 LYS 179 177 LEU 180 178 LYS 181 179 MET 182 180 ASP 183 181 ASN 184 182 TRP 185 183 ILE 186 184 VAL 187 185 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-17 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 1IWM "Crystal Structure Of The Outer Membrane Lipoprotein Receptor, Lolb" 99.47 186 100.00 100.00 1.40e-132 PDB 1IWN "Crystal Structure Of The Outer Membrane Lipoprotein Receptor Lolb Complexed With Pegmme2000" 99.47 186 100.00 100.00 1.40e-132 PDB 3WJT "Crystal Structure Of The L68d Variant Of Mlolb" 95.19 178 99.44 99.44 2.93e-125 PDB 3WJU "Crystal Structure Of The L68d Variant Of Mlolb From Escherichia Coli" 95.19 178 99.44 99.44 2.93e-125 PDB 3WJV "Crystal Structure Of The L68e Variant Of Mlolb" 99.47 186 99.46 99.46 1.22e-131 DBJ BAA01105 "5-aminolevulinate synthase [Escherichia coli]" 99.47 207 99.46 99.46 4.85e-132 DBJ BAA36067 "chaperone for lipoproteins [Escherichia coli str. K12 substr. W3110]" 99.47 207 99.46 99.46 4.95e-132 DBJ BAB35137 "5-aminolevulinate synthase HemM [Escherichia coli O157:H7 str. Sakai]" 99.47 207 99.46 99.46 4.95e-132 DBJ BAG76783 "conserved hypothetical protein [Escherichia coli SE11]" 99.47 207 99.46 99.46 4.95e-132 DBJ BAI25021 "chaperone LolB [Escherichia coli O26:H11 str. 11368]" 99.47 207 99.46 99.46 4.95e-132 EMBL CAP75748 "Outer-membrane lipoprotein lolB [Escherichia coli LF82]" 99.47 207 98.92 99.46 1.49e-131 EMBL CAQ31711 "outer membrane lipoprotein, localization of lipoproteins in the outer membrane [Escherichia coli BL21(DE3)]" 99.47 207 99.46 99.46 4.95e-132 EMBL CAQ89267 "chaperone for lipoproteins [Escherichia fergusonii ATCC 35469]" 99.47 207 97.31 99.46 1.59e-130 EMBL CAQ98089 "chaperone for lipoproteins [Escherichia coli IAI1]" 99.47 207 99.46 99.46 4.95e-132 EMBL CAR02603 "chaperone for lipoproteins [Escherichia coli S88]" 99.47 207 98.92 99.46 1.15e-131 GB AAA24433 "ORF1 [Escherichia coli]" 99.47 207 99.46 99.46 4.95e-132 GB AAC74293 "lipoprotein localization factor [Escherichia coli str. K-12 substr. MG1655]" 99.47 207 99.46 99.46 4.95e-132 GB AAG56067 "an enzyme in main pathway of synthesis of 5-aminolevulinate, possibly glutamyl-tRNA dehydrogenase [Escherichia coli O157:H7 str" 99.47 207 99.46 99.46 4.95e-132 GB AAN42825 "carrier of lipoproteins to outer membrane [Shigella flexneri 2a str. 301]" 99.47 207 99.46 99.46 4.95e-132 GB AAN80132 "Outer-membrane lipoprotein lolB precursor [Escherichia coli CFT073]" 99.47 229 98.39 99.46 1.57e-131 REF NP_309741 "outer membrane lipoprotein LolB [Escherichia coli O157:H7 str. Sakai]" 99.47 207 99.46 99.46 4.95e-132 REF NP_415727 "lipoprotein localization factor [Escherichia coli str. K-12 substr. MG1655]" 99.47 207 99.46 99.46 4.95e-132 REF NP_707118 "molecular chaperone LolB [Shigella flexneri 2a str. 301]" 99.47 207 99.46 99.46 4.95e-132 REF WP_000174480 "MULTISPECIES: outer membrane lipoprotein LolB [Enterobacteriaceae]" 99.47 207 99.46 99.46 3.49e-132 REF WP_001130605 "outer membrane lipoprotein LolB [Escherichia coli]" 99.47 207 98.92 99.46 1.78e-131 SP A7ZKY3 "RecName: Full=Outer-membrane lipoprotein LolB; Flags: Precursor" 99.47 207 99.46 99.46 4.95e-132 SP A7ZZE5 "RecName: Full=Outer-membrane lipoprotein LolB; Flags: Precursor" 99.47 207 99.46 99.46 4.95e-132 SP B1IU84 "RecName: Full=Outer-membrane lipoprotein LolB; Flags: Precursor" 99.47 207 99.46 99.46 4.95e-132 SP B1LH91 "RecName: Full=Outer-membrane lipoprotein LolB; Flags: Precursor" 99.47 207 98.92 99.46 1.15e-131 SP B1XAQ0 "RecName: Full=Outer-membrane lipoprotein LolB; Flags: Precursor" 99.47 207 99.46 99.46 4.95e-132 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction $LolB 'Escherichia coli K-12' 83333 Bacteria . Escherichia coli K12 no 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 $LolB 'recombinant technology' 'E. coli' Esherichia coli K12 . 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 $LolB . mM 0.5 1.0 '[U-2H; U-13C; U-15N]' MES 38 mM . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address 'Bruker Japan' 'Ninomiya 3-21-5, Tsukuba, Ibaraki 305-0051' info@bruker-biospin.jp stop_ loop_ _Task 'data collection' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address 'T. D. Goddard and D. G. Kneller' 'University of California, San Francisco' sparky@cgl.ucsf.edu stop_ loop_ _Task 'peak assignments' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance600 _Field_strength 600 _Details ; The address and e-mail address of the machine's vendor are listed below. Address: Ninomiya 3-21-5, Tsukuba, Ibaraki 305-0051 E-mail: info@bruker-biospin.jp ; save_ ############################# # NMR applied experiments # ############################# save_1H15N_TROSY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N TROSY-HSQC' _Sample_label $sample_1 save_ save_TROSY-HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label $sample_1 save_ save_TROSY-HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label $sample_1 save_ save_TROSY-HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label $sample_1 save_ save_TROSY-HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label $sample_1 save_ save_TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label $sample_1 save_ save_1H15N_TROSY-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N TROSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HN(CO)CACB _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY-HNCO _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.2 pH temperature 310 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H15N TROSY-HSQC' TROSY-HNCACB TROSY-HN(CO)CACB TROSY-HNCA TROSY-HN(CO)CA TROSY-HNCO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_referencing_1 _Mol_system_component_name 'LolB 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 12 14 PRO C C 176.060 0.344 1 2 12 14 PRO CA C 63.468 0.484 1 3 12 14 PRO CB C 31.509 0.484 1 4 13 15 ASP H H 8.138 0.004 1 5 13 15 ASP C C 175.849 0.344 1 6 13 15 ASP CA C 53.442 0.484 1 7 13 15 ASP CB C 40.889 0.484 1 8 13 15 ASP N N 120.066 0.125 1 9 14 16 SER H H 7.934 0.004 1 10 14 16 SER CA C 56.626 0.484 1 11 14 16 SER CB C 63.743 0.484 1 12 14 16 SER N N 117.926 0.125 1 13 16 18 GLN C C 179.325 0.344 1 14 16 18 GLN CA C 59.403 0.484 1 15 16 18 GLN CB C 26.913 0.484 1 16 17 19 TRP H H 7.340 0.004 1 17 17 19 TRP C C 178.434 0.344 1 18 17 19 TRP CA C 57.503 0.484 1 19 17 19 TRP CB C 31.131 0.484 1 20 17 19 TRP N N 122.854 0.125 1 21 18 20 ARG H H 7.741 0.004 1 22 18 20 ARG C C 179.252 0.344 1 23 18 20 ARG CA C 59.821 0.484 1 24 18 20 ARG CB C 28.711 0.484 1 25 18 20 ARG N N 120.630 0.125 1 26 19 21 GLN H H 8.188 0.004 1 27 19 21 GLN C C 176.850 0.344 1 28 19 21 GLN CA C 57.971 0.484 1 29 19 21 GLN CB C 27.688 0.484 1 30 19 21 GLN N N 119.970 0.125 1 31 20 22 HIS H H 7.903 0.004 1 32 20 22 HIS C C 176.854 0.344 1 33 20 22 HIS CA C 60.421 0.484 1 34 20 22 HIS CB C 30.072 0.484 1 35 20 22 HIS N N 120.813 0.125 1 36 21 23 GLN H H 7.513 0.004 1 37 21 23 GLN C C 177.907 0.344 1 38 21 23 GLN CA C 58.938 0.484 1 39 21 23 GLN CB C 30.174 0.484 1 40 21 23 GLN N N 114.377 0.125 1 41 22 24 GLN H H 7.440 0.004 1 42 22 24 GLN C C 177.498 0.344 1 43 22 24 GLN CA C 58.318 0.484 1 44 22 24 GLN CB C 27.730 0.484 1 45 22 24 GLN N N 119.041 0.125 1 46 23 25 ASP H H 8.522 0.004 1 47 23 25 ASP C C 179.486 0.344 1 48 23 25 ASP CA C 56.830 0.484 1 49 23 25 ASP CB C 39.652 0.484 1 50 23 25 ASP N N 121.180 0.125 1 51 24 26 VAL H H 7.750 0.004 1 52 24 26 VAL C C 179.808 0.344 1 53 24 26 VAL CA C 65.821 0.484 1 54 24 26 VAL N N 120.128 0.125 1 55 25 27 ARG H H 8.232 0.004 1 56 25 27 ARG C C 176.531 0.344 1 57 25 27 ARG CA C 58.637 0.484 1 58 25 27 ARG CB C 29.494 0.484 1 59 25 27 ARG N N 121.350 0.125 1 60 26 28 ASN H H 7.733 0.004 1 61 26 28 ASN C C 176.391 0.344 1 62 26 28 ASN CA C 53.102 0.484 1 63 26 28 ASN CB C 38.243 0.484 1 64 26 28 ASN N N 117.518 0.125 1 65 27 29 LEU H H 6.969 0.004 1 66 27 29 LEU C C 174.816 0.344 1 67 27 29 LEU CA C 54.859 0.484 1 68 27 29 LEU CB C 41.044 0.484 1 69 27 29 LEU N N 122.507 0.125 1 70 28 30 ASN H H 9.450 0.004 1 71 28 30 ASN C C 174.822 0.344 1 72 28 30 ASN CA C 54.770 0.484 1 73 28 30 ASN CB C 42.031 0.484 1 74 28 30 ASN N N 117.649 0.125 1 75 29 31 GLN H H 8.280 0.004 1 76 29 31 GLN C C 173.283 0.344 1 77 29 31 GLN CA C 54.590 0.484 1 78 29 31 GLN CB C 31.954 0.484 1 79 29 31 GLN N N 120.072 0.125 1 80 30 32 TYR H H 8.922 0.004 1 81 30 32 TYR C C 175.835 0.344 1 82 30 32 TYR CA C 55.419 0.484 1 83 30 32 TYR CB C 41.450 0.484 1 84 30 32 TYR N N 120.227 0.125 1 85 31 33 GLN H H 9.190 0.004 1 86 31 33 GLN C C 173.956 0.344 1 87 31 33 GLN CA C 54.589 0.484 1 88 31 33 GLN CB C 32.333 0.484 1 89 31 33 GLN N N 123.234 0.125 1 90 32 34 THR H H 9.070 0.004 1 91 32 34 THR C C 171.008 0.344 1 92 32 34 THR CA C 59.401 0.484 1 93 32 34 THR CB C 68.996 0.484 1 94 32 34 THR N N 120.641 0.125 1 95 33 35 ARG H H 7.559 0.004 1 96 33 35 ARG C C 174.096 0.344 1 97 33 35 ARG CA C 52.860 0.484 1 98 33 35 ARG CB C 32.448 0.484 1 99 33 35 ARG N N 121.458 0.125 1 100 34 36 GLY H H 7.380 0.004 1 101 34 36 GLY C C 172.292 0.344 1 102 34 36 GLY CA C 46.056 0.484 1 103 34 36 GLY N N 108.073 0.125 1 104 35 37 ALA H H 9.059 0.004 1 105 35 37 ALA C C 175.008 0.344 1 106 35 37 ALA CA C 51.438 0.484 1 107 35 37 ALA CB C 21.215 0.484 1 108 35 37 ALA N N 128.522 0.125 1 109 36 38 PHE H H 9.181 0.004 1 110 36 38 PHE C C 173.407 0.344 1 111 36 38 PHE CA C 55.861 0.484 1 112 36 38 PHE CB C 42.518 0.484 1 113 36 38 PHE N N 125.354 0.125 1 114 37 39 ALA H H 8.287 0.004 1 115 37 39 ALA C C 174.072 0.344 1 116 37 39 ALA CA C 50.436 0.484 1 117 37 39 ALA CB C 21.699 0.484 1 118 37 39 ALA N N 132.021 0.125 1 119 38 40 TYR H H 8.814 0.004 1 120 38 40 TYR C C 173.561 0.344 1 121 38 40 TYR CA C 56.275 0.484 1 122 38 40 TYR CB C 41.643 0.484 1 123 38 40 TYR N N 124.130 0.125 1 124 39 41 ILE H H 8.574 0.004 1 125 39 41 ILE C C 174.000 0.344 1 126 39 41 ILE CA C 59.909 0.484 1 127 39 41 ILE CB C 40.394 0.484 1 128 39 41 ILE N N 127.825 0.125 1 129 40 42 SER H H 8.347 0.004 1 130 40 42 SER CA C 56.103 0.484 1 131 40 42 SER CB C 66.497 0.484 1 132 40 42 SER N N 123.700 0.125 1 133 41 43 ASP C C 177.055 0.344 1 134 41 43 ASP CA C 56.680 0.484 1 135 41 43 ASP CB C 39.739 0.484 1 136 42 44 GLN H H 8.115 0.004 1 137 42 44 GLN C C 175.856 0.344 1 138 42 44 GLN CA C 56.359 0.484 1 139 42 44 GLN CB C 29.811 0.484 1 140 42 44 GLN N N 116.673 0.125 1 141 43 45 GLN H H 7.582 0.004 1 142 43 45 GLN C C 173.189 0.344 1 143 43 45 GLN CA C 55.363 0.484 1 144 43 45 GLN CB C 30.925 0.484 1 145 43 45 GLN N N 118.736 0.125 1 146 44 46 LYS H H 8.276 0.004 1 147 44 46 LYS C C 175.482 0.344 1 148 44 46 LYS CA C 55.236 0.484 1 149 44 46 LYS CB C 33.846 0.484 1 150 44 46 LYS N N 123.533 0.125 1 151 45 47 VAL H H 9.289 0.004 1 152 45 47 VAL C C 173.569 0.344 1 153 45 47 VAL CA C 61.405 0.484 1 154 45 47 VAL CB C 35.179 0.484 1 155 45 47 VAL N N 126.492 0.125 1 156 46 48 TYR H H 8.442 0.004 1 157 46 48 TYR C C 175.284 0.344 1 158 46 48 TYR CA C 56.256 0.484 1 159 46 48 TYR CB C 39.512 0.484 1 160 46 48 TYR N N 126.787 0.125 1 161 47 49 ALA H H 9.267 0.004 1 162 47 49 ALA C C 176.861 0.344 1 163 47 49 ALA CA C 51.149 0.484 1 164 47 49 ALA CB C 22.327 0.484 1 165 47 49 ALA N N 125.989 0.125 1 166 48 50 ARG H H 8.652 0.004 1 167 48 50 ARG C C 176.046 0.344 1 168 48 50 ARG CA C 54.510 0.484 1 169 48 50 ARG CB C 29.251 0.484 1 170 48 50 ARG N N 121.485 0.125 1 171 49 51 PHE H H 8.936 0.004 1 172 49 51 PHE C C 172.843 0.344 1 173 49 51 PHE CA C 54.371 0.484 1 174 49 51 PHE CB C 44.009 0.484 1 175 49 51 PHE N N 120.666 0.125 1 176 50 52 PHE H H 8.844 0.004 1 177 50 52 PHE C C 172.899 0.344 1 178 50 52 PHE CA C 56.275 0.484 1 179 50 52 PHE CB C 41.643 0.484 1 180 50 52 PHE N N 124.277 0.125 1 181 51 53 TRP H H 8.698 0.004 1 182 51 53 TRP C C 174.114 0.344 1 183 51 53 TRP CA C 55.766 0.484 1 184 51 53 TRP CB C 31.622 0.484 1 185 51 53 TRP N N 130.321 0.125 1 186 52 54 GLN H H 8.343 0.004 1 187 52 54 GLN C C 173.753 0.344 1 188 52 54 GLN CA C 53.898 0.484 1 189 52 54 GLN CB C 31.714 0.484 1 190 52 54 GLN N N 127.394 0.125 1 191 53 55 GLN H H 9.478 0.004 1 192 53 55 GLN C C 174.796 0.344 1 193 53 55 GLN CA C 55.040 0.484 1 194 53 55 GLN CB C 31.852 0.484 1 195 53 55 GLN N N 129.477 0.125 1 196 54 56 THR H H 8.786 0.004 1 197 54 56 THR C C 174.539 0.344 1 198 54 56 THR CA C 61.357 0.484 1 199 54 56 THR CB C 70.293 0.484 1 200 54 56 THR N N 124.115 0.125 1 201 55 57 GLY H H 8.675 0.004 1 202 55 57 GLY C C 172.769 0.344 1 203 55 57 GLY CA C 45.503 0.484 1 204 55 57 GLY N N 115.373 0.125 1 205 56 58 GLN H H 8.544 0.004 1 206 56 58 GLN C C 177.756 0.344 1 207 56 58 GLN CA C 56.062 0.484 1 208 56 58 GLN CB C 29.257 0.484 1 209 56 58 GLN N N 117.825 0.125 1 210 57 59 ASP H H 8.171 0.004 1 211 57 59 ASP C C 174.999 0.344 1 212 57 59 ASP CA C 54.325 0.484 1 213 57 59 ASP CB C 42.279 0.484 1 214 57 59 ASP N N 115.763 0.125 1 215 58 60 ARG H H 7.112 0.004 1 216 58 60 ARG C C 174.314 0.344 1 217 58 60 ARG CA C 54.564 0.484 1 218 58 60 ARG CB C 31.645 0.484 1 219 58 60 ARG N N 119.527 0.125 1 220 59 61 TYR H H 8.012 0.004 1 221 59 61 TYR C C 171.789 0.344 1 222 59 61 TYR CA C 55.829 0.484 1 223 59 61 TYR CB C 39.529 0.484 1 224 59 61 TYR N N 119.871 0.125 1 225 60 62 ARG H H 8.541 0.004 1 226 60 62 ARG C C 173.088 0.344 1 227 60 62 ARG CA C 53.636 0.484 1 228 60 62 ARG CB C 33.454 0.484 1 229 60 62 ARG N N 122.376 0.125 1 230 61 63 LEU H H 8.780 0.004 1 231 61 63 LEU C C 173.773 0.344 1 232 61 63 LEU CA C 52.607 0.484 1 233 61 63 LEU CB C 44.491 0.484 1 234 61 63 LEU N N 126.573 0.125 1 235 62 64 LEU H H 9.121 0.004 1 236 62 64 LEU C C 176.041 0.344 1 237 62 64 LEU CA C 53.568 0.484 1 238 62 64 LEU CB C 45.390 0.484 1 239 62 64 LEU N N 128.983 0.125 1 240 63 65 LEU H H 9.099 0.004 1 241 63 65 LEU C C 176.853 0.344 1 242 63 65 LEU CA C 53.083 0.484 1 243 63 65 LEU CB C 43.302 0.484 1 244 63 65 LEU N N 125.452 0.125 1 245 64 66 THR H H 9.273 0.004 1 246 64 66 THR C C 173.790 0.344 1 247 64 66 THR CA C 59.925 0.484 1 248 64 66 THR CB C 71.275 0.484 1 249 64 66 THR N N 117.701 0.125 1 250 65 67 ASN H H 8.628 0.004 1 251 65 67 ASN CA C 51.651 0.484 1 252 65 67 ASN CB C 37.658 0.484 1 253 65 67 ASN N N 123.280 0.125 1 254 66 68 PRO C C 177.251 0.344 1 255 66 68 PRO CA C 64.985 0.484 1 256 67 69 LEU H H 7.658 0.004 1 257 67 69 LEU C C 178.152 0.344 1 258 67 69 LEU CA C 54.779 0.484 1 259 67 69 LEU CB C 40.443 0.484 1 260 67 69 LEU N N 116.913 0.125 1 261 68 70 GLY H H 8.276 0.004 1 262 68 70 GLY C C 174.399 0.344 1 263 68 70 GLY CA C 44.772 0.484 1 264 68 70 GLY N N 108.364 0.125 1 265 69 71 SER H H 7.729 0.004 1 266 69 71 SER CA C 57.288 0.484 1 267 69 71 SER CB C 63.534 0.484 1 268 69 71 SER N N 117.812 0.125 1 269 72 74 LEU C C 174.289 0.344 1 270 72 74 LEU CA C 54.676 0.484 1 271 72 74 LEU CB C 44.563 0.484 1 272 73 75 GLU H H 8.747 0.004 1 273 73 75 GLU C C 173.790 0.344 1 274 73 75 GLU CA C 54.895 0.484 1 275 73 75 GLU CB C 31.846 0.484 1 276 73 75 GLU N N 126.040 0.125 1 277 74 76 LEU H H 9.344 0.004 1 278 74 76 LEU C C 174.143 0.344 1 279 74 76 LEU CA C 53.574 0.484 1 280 74 76 LEU CB C 45.127 0.484 1 281 74 76 LEU N N 131.102 0.125 1 282 75 77 ASN H H 9.057 0.004 1 283 75 77 ASN C C 172.915 0.344 1 284 75 77 ASN CA C 52.638 0.484 1 285 75 77 ASN CB C 41.107 0.484 1 286 75 77 ASN N N 125.722 0.125 1 287 76 78 ALA H H 8.926 0.004 1 288 76 78 ALA C C 174.814 0.344 1 289 76 78 ALA CA C 51.314 0.484 1 290 76 78 ALA CB C 20.395 0.484 1 291 76 78 ALA N N 129.617 0.125 1 292 77 79 GLN H H 7.957 0.004 1 293 77 79 GLN CA C 52.944 0.484 1 294 77 79 GLN CB C 29.320 0.484 1 295 77 79 GLN N N 120.722 0.125 1 296 78 80 PRO C C 178.181 0.344 1 297 78 80 PRO CA C 64.708 0.484 1 298 79 81 GLY H H 8.812 0.004 1 299 79 81 GLY C C 174.122 0.344 1 300 79 81 GLY CA C 45.920 0.484 1 301 79 81 GLY N N 115.565 0.125 1 302 80 82 ASN H H 7.908 0.004 1 303 80 82 ASN C C 171.887 0.344 1 304 80 82 ASN CA C 54.437 0.484 1 305 80 82 ASN CB C 40.448 0.484 1 306 80 82 ASN N N 119.335 0.125 1 307 81 83 VAL H H 8.604 0.004 1 308 81 83 VAL C C 173.793 0.344 1 309 81 83 VAL CA C 60.382 0.484 1 310 81 83 VAL CB C 32.287 0.484 1 311 81 83 VAL N N 126.949 0.125 1 312 82 84 GLN H H 8.523 0.004 1 313 82 84 GLN C C 174.348 0.344 1 314 82 84 GLN CA C 53.691 0.484 1 315 82 84 GLN CB C 31.925 0.484 1 316 82 84 GLN N N 125.484 0.125 1 317 83 85 LEU H H 9.019 0.004 1 318 83 85 LEU C C 174.621 0.344 1 319 83 85 LEU CA C 53.878 0.484 1 320 83 85 LEU CB C 45.539 0.484 1 321 83 85 LEU N N 127.628 0.125 1 322 84 86 VAL H H 9.207 0.004 1 323 84 86 VAL C C 175.889 0.344 1 324 84 86 VAL CA C 60.556 0.484 1 325 84 86 VAL CB C 33.349 0.484 1 326 84 86 VAL N N 127.282 0.125 1 327 85 87 ASP H H 8.350 0.004 1 328 85 87 ASP C C 177.759 0.344 1 329 85 87 ASP CA C 52.106 0.484 1 330 85 87 ASP CB C 42.270 0.484 1 331 85 87 ASP N N 126.996 0.125 1 332 86 88 ASN H H 8.285 0.004 1 333 86 88 ASN C C 176.696 0.344 1 334 86 88 ASN CA C 54.593 0.484 1 335 86 88 ASN CB C 36.959 0.484 1 336 86 88 ASN N N 116.615 0.125 1 337 87 89 LYS H H 8.140 0.004 1 338 87 89 LYS C C 177.380 0.344 1 339 87 89 LYS CA C 54.839 0.484 1 340 87 89 LYS CB C 31.910 0.484 1 341 87 89 LYS N N 120.993 0.125 1 342 88 90 GLY H H 8.058 0.004 1 343 88 90 GLY C C 174.519 0.344 1 344 88 90 GLY CA C 45.203 0.484 1 345 88 90 GLY N N 110.384 0.125 1 346 89 91 GLN H H 8.482 0.004 1 347 89 91 GLN C C 173.617 0.344 1 348 89 91 GLN CA C 55.397 0.484 1 349 89 91 GLN CB C 28.109 0.484 1 350 89 91 GLN N N 124.108 0.125 1 351 90 92 ARG H H 7.773 0.004 1 352 90 92 ARG C C 175.808 0.344 1 353 90 92 ARG CA C 54.591 0.484 1 354 90 92 ARG CB C 31.780 0.484 1 355 90 92 ARG N N 122.991 0.125 1 356 91 93 TYR H H 9.246 0.004 1 357 91 93 TYR C C 175.237 0.344 1 358 91 93 TYR CA C 56.355 0.484 1 359 91 93 TYR CB C 41.509 0.484 1 360 91 93 TYR N N 124.773 0.125 1 361 92 94 THR H H 8.474 0.004 1 362 92 94 THR C C 173.447 0.344 1 363 92 94 THR CA C 60.633 0.484 1 364 92 94 THR CB C 71.064 0.484 1 365 92 94 THR N N 117.265 0.125 1 366 93 95 ALA H H 8.673 0.004 1 367 93 95 ALA C C 175.519 0.344 1 368 93 95 ALA CA C 51.727 0.484 1 369 93 95 ALA CB C 20.122 0.484 1 370 93 95 ALA N N 127.845 0.125 1 371 94 96 ASP H H 8.130 0.004 1 372 94 96 ASP C C 175.672 0.344 1 373 94 96 ASP CA C 54.603 0.484 1 374 94 96 ASP CB C 41.195 0.484 1 375 94 96 ASP N N 117.583 0.125 1 376 95 97 ASP H H 7.399 0.004 1 377 95 97 ASP C C 175.827 0.344 1 378 95 97 ASP CA C 52.944 0.484 1 379 95 97 ASP CB C 43.189 0.484 1 380 95 97 ASP N N 119.452 0.125 1 381 96 98 ALA H H 9.086 0.004 1 382 96 98 ALA C C 178.770 0.344 1 383 96 98 ALA CA C 55.215 0.484 1 384 96 98 ALA CB C 19.623 0.484 1 385 96 98 ALA N N 129.245 0.125 1 386 97 99 GLU H H 7.979 0.004 1 387 97 99 GLU C C 179.608 0.344 1 388 97 99 GLU CA C 59.709 0.484 1 389 97 99 GLU CB C 28.675 0.484 1 390 97 99 GLU N N 117.528 0.125 1 391 98 100 GLU H H 8.211 0.004 1 392 98 100 GLU C C 179.238 0.344 1 393 98 100 GLU CA C 58.475 0.484 1 394 98 100 GLU CB C 28.816 0.484 1 395 98 100 GLU N N 123.006 0.125 1 396 99 101 MET H H 7.655 0.004 1 397 99 101 MET C C 178.048 0.344 1 398 99 101 MET CA C 58.163 0.484 1 399 99 101 MET CB C 32.883 0.484 1 400 99 101 MET N N 117.300 0.125 1 401 100 102 ILE H H 8.262 0.004 1 402 100 102 ILE C C 178.927 0.344 1 403 100 102 ILE CA C 64.623 0.484 1 404 100 102 ILE N N 119.590 0.125 1 405 101 103 GLY H H 7.589 0.004 1 406 101 103 GLY C C 175.979 0.344 1 407 101 103 GLY CA C 46.957 0.484 1 408 101 103 GLY N N 112.895 0.125 1 409 102 104 LYS H H 7.691 0.004 1 410 102 104 LYS C C 177.401 0.344 1 411 102 104 LYS CA C 58.573 0.484 1 412 102 104 LYS CB C 32.079 0.484 1 413 102 104 LYS N N 122.659 0.125 1 414 103 105 LEU H H 7.956 0.004 1 415 103 105 LEU C C 178.612 0.344 1 416 103 105 LEU CA C 56.365 0.484 1 417 103 105 LEU CB C 41.524 0.484 1 418 103 105 LEU N N 116.298 0.125 1 419 104 106 THR H H 7.374 0.004 1 420 104 106 THR C C 175.683 0.344 1 421 104 106 THR CA C 61.354 0.484 1 422 104 106 THR CB C 71.885 0.484 1 423 104 106 THR N N 105.831 0.125 1 424 105 107 GLY H H 7.414 0.004 1 425 105 107 GLY C C 172.851 0.344 1 426 105 107 GLY CA C 45.549 0.484 1 427 105 107 GLY N N 111.313 0.125 1 428 106 108 MET H H 7.528 0.004 1 429 106 108 MET CA C 52.100 0.484 1 430 106 108 MET CB C 34.258 0.484 1 431 106 108 MET N N 119.483 0.125 1 432 107 109 PRO C C 175.707 0.344 1 433 107 109 PRO CA C 61.291 0.484 1 434 107 109 PRO CB C 27.189 0.484 1 435 108 110 ILE H H 7.856 0.004 1 436 108 110 ILE CA C 58.667 0.484 1 437 108 110 ILE CB C 38.532 0.484 1 438 108 110 ILE N N 123.424 0.125 1 439 109 111 PRO C C 176.396 0.344 1 440 109 111 PRO CA C 61.594 0.484 1 441 110 112 LEU H H 8.311 0.004 1 442 110 112 LEU C C 176.486 0.344 1 443 110 112 LEU CA C 58.023 0.484 1 444 110 112 LEU CB C 42.270 0.484 1 445 110 112 LEU N N 126.375 0.125 1 446 111 113 ASN H H 9.508 0.004 1 447 111 113 ASN C C 177.862 0.344 1 448 111 113 ASN CA C 55.640 0.484 1 449 111 113 ASN CB C 36.786 0.484 1 450 111 113 ASN N N 116.118 0.125 1 451 112 114 SER H H 6.922 0.004 1 452 112 114 SER C C 175.176 0.344 1 453 112 114 SER CA C 60.213 0.484 1 454 112 114 SER CB C 60.878 0.484 1 455 112 114 SER N N 115.250 0.125 1 456 113 115 LEU H H 8.032 0.004 1 457 113 115 LEU C C 175.257 0.344 1 458 113 115 LEU CA C 57.245 0.484 1 459 113 115 LEU CB C 41.645 0.484 1 460 113 115 LEU N N 125.207 0.125 1 461 114 116 ARG H H 6.959 0.004 1 462 114 116 ARG C C 174.989 0.344 1 463 114 116 ARG CA C 57.617 0.484 1 464 114 116 ARG CB C 27.756 0.484 1 465 114 116 ARG N N 113.423 0.125 1 466 115 117 GLN H H 6.705 0.004 1 467 115 117 GLN C C 177.166 0.344 1 468 115 117 GLN CA C 57.446 0.484 1 469 115 117 GLN CB C 27.824 0.484 1 470 115 117 GLN N N 115.977 0.125 1 471 116 118 TRP H H 8.021 0.004 1 472 116 118 TRP C C 181.887 0.344 1 473 116 118 TRP CA C 57.024 0.484 1 474 116 118 TRP CB C 28.744 0.484 1 475 116 118 TRP N N 121.243 0.125 1 476 117 119 ILE H H 9.334 0.004 1 477 117 119 ILE C C 171.759 0.344 1 478 117 119 ILE N N 124.240 0.125 1 479 118 120 LEU H H 6.627 0.004 1 480 118 120 LEU C C 177.814 0.344 1 481 118 120 LEU CA C 52.473 0.484 1 482 118 120 LEU CB C 40.610 0.484 1 483 118 120 LEU N N 113.353 0.125 1 484 119 121 GLY H H 7.983 0.004 1 485 119 121 GLY C C 172.914 0.344 1 486 119 121 GLY CA C 44.208 0.484 1 487 119 121 GLY N N 104.447 0.125 1 488 120 122 LEU H H 7.181 0.004 1 489 120 122 LEU CA C 50.184 0.484 1 490 120 122 LEU CB C 41.517 0.484 1 491 120 122 LEU N N 117.971 0.125 1 492 121 123 PRO C C 178.431 0.344 1 493 121 123 PRO CA C 63.613 0.484 1 494 121 123 PRO CB C 31.030 0.484 1 495 122 124 GLY H H 7.902 0.004 1 496 122 124 GLY C C 174.924 0.344 1 497 122 124 GLY CA C 46.169 0.484 1 498 122 124 GLY N N 111.257 0.125 1 499 123 125 ASP H H 8.677 0.004 1 500 123 125 ASP C C 176.017 0.344 1 501 123 125 ASP CA C 53.889 0.484 1 502 123 125 ASP CB C 40.320 0.484 1 503 123 125 ASP N N 127.376 0.125 1 504 124 126 ALA H H 7.679 0.004 1 505 124 126 ALA C C 177.377 0.344 1 506 124 126 ALA CA C 53.162 0.484 1 507 124 126 ALA CB C 19.811 0.484 1 508 124 126 ALA N N 123.299 0.125 1 509 125 127 THR H H 8.401 0.004 1 510 125 127 THR C C 174.526 0.344 1 511 125 127 THR CA C 61.643 0.484 1 512 125 127 THR CB C 69.858 0.484 1 513 125 127 THR N N 112.372 0.125 1 514 126 128 ASP H H 8.511 0.004 1 515 126 128 ASP C C 173.085 0.344 1 516 126 128 ASP CA C 52.940 0.484 1 517 126 128 ASP CB C 40.326 0.484 1 518 126 128 ASP N N 126.693 0.125 1 519 127 129 TYR H H 7.143 0.004 1 520 127 129 TYR C C 173.635 0.344 1 521 127 129 TYR CA C 55.033 0.484 1 522 127 129 TYR CB C 40.060 0.484 1 523 127 129 TYR N N 118.126 0.125 1 524 128 130 LYS H H 8.800 0.004 1 525 128 130 LYS C C 175.197 0.344 1 526 128 130 LYS CA C 54.048 0.484 1 527 128 130 LYS CB C 36.151 0.484 1 528 128 130 LYS N N 119.246 0.125 1 529 129 131 LEU H H 8.451 0.004 1 530 129 131 LEU C C 177.396 0.344 1 531 129 131 LEU CA C 52.252 0.484 1 532 129 131 LEU CB C 43.416 0.484 1 533 129 131 LEU N N 122.608 0.125 1 534 130 132 ASP H H 8.885 0.004 1 535 130 132 ASP C C 178.761 0.344 1 536 130 132 ASP CA C 51.713 0.484 1 537 130 132 ASP CB C 40.572 0.484 1 538 130 132 ASP N N 121.730 0.125 1 539 131 133 ASP H H 7.956 0.004 1 540 131 133 ASP C C 176.023 0.344 1 541 131 133 ASP CA C 55.659 0.484 1 542 131 133 ASP CB C 39.827 0.484 1 543 131 133 ASP N N 116.298 0.125 1 544 132 134 GLN H H 8.063 0.004 1 545 132 134 GLN C C 174.640 0.344 1 546 132 134 GLN CA C 54.344 0.484 1 547 132 134 GLN CB C 27.468 0.484 1 548 132 134 GLN N N 119.348 0.125 1 549 133 135 TYR H H 7.455 0.004 1 550 133 135 TYR CA C 60.169 0.484 1 551 133 135 TYR CB C 33.763 0.484 1 552 133 135 TYR N N 113.751 0.125 1 553 134 136 ARG H H 7.456 0.004 1 554 134 136 ARG C C 175.837 0.344 1 555 134 136 ARG CA C 53.083 0.484 1 556 134 136 ARG CB C 30.573 0.484 1 557 134 136 ARG N N 114.959 0.125 1 558 135 137 LEU H H 8.348 0.004 1 559 135 137 LEU C C 177.468 0.344 1 560 135 137 LEU CA C 56.421 0.484 1 561 135 137 LEU CB C 41.750 0.484 1 562 135 137 LEU N N 122.883 0.125 1 563 136 138 SER H H 8.950 0.004 1 564 136 138 SER C C 175.125 0.344 1 565 136 138 SER CA C 58.657 0.484 1 566 136 138 SER CB C 64.843 0.484 1 567 136 138 SER N N 118.187 0.125 1 568 137 139 GLU H H 7.521 0.004 1 569 137 139 GLU C C 174.305 0.344 1 570 137 139 GLU CA C 54.869 0.484 1 571 137 139 GLU CB C 34.044 0.484 1 572 137 139 GLU N N 121.070 0.125 1 573 138 140 ILE H H 8.994 0.004 1 574 138 140 ILE C C 175.472 0.344 1 575 138 140 ILE CA C 60.621 0.484 1 576 138 140 ILE CB C 42.208 0.484 1 577 138 140 ILE N N 122.859 0.125 1 578 139 141 THR H H 8.523 0.004 1 579 139 141 THR C C 173.280 0.344 1 580 139 141 THR CA C 61.808 0.484 1 581 139 141 THR CB C 70.008 0.484 1 582 139 141 THR N N 123.602 0.125 1 583 140 142 TYR H H 9.154 0.004 1 584 140 142 TYR C C 173.280 0.344 1 585 140 142 TYR CA C 57.185 0.484 1 586 140 142 TYR CB C 41.870 0.484 1 587 140 142 TYR N N 129.091 0.125 1 588 141 143 SER H H 8.162 0.004 1 589 141 143 SER C C 173.470 0.344 1 590 141 143 SER CA C 56.562 0.484 1 591 141 143 SER CB C 63.765 0.484 1 592 141 143 SER N N 124.602 0.125 1 593 142 144 GLN H H 8.284 0.004 1 594 142 144 GLN CA C 55.197 0.484 1 595 142 144 GLN CB C 30.698 0.484 1 596 142 144 GLN N N 124.746 0.125 1 597 143 145 ASN H H 8.108 0.004 1 598 143 145 ASN N N 129.808 0.125 1 599 144 146 GLY C C 173.759 0.344 1 600 144 146 GLY CA C 45.260 0.484 1 601 145 147 LYS H H 7.689 0.004 1 602 145 147 LYS C C 174.797 0.344 1 603 145 147 LYS CA C 54.315 0.484 1 604 145 147 LYS CB C 33.095 0.484 1 605 145 147 LYS N N 121.919 0.125 1 606 146 148 ASN H H 8.466 0.004 1 607 146 148 ASN C C 173.911 0.344 1 608 146 148 ASN CA C 52.313 0.484 1 609 146 148 ASN CB C 39.543 0.484 1 610 146 148 ASN N N 123.602 0.125 1 611 147 149 TRP H H 8.882 0.004 1 612 147 149 TRP C C 175.682 0.344 1 613 147 149 TRP CA C 57.036 0.484 1 614 147 149 TRP CB C 31.584 0.484 1 615 147 149 TRP N N 122.723 0.125 1 616 148 150 LYS H H 9.091 0.004 1 617 148 150 LYS C C 175.703 0.344 1 618 148 150 LYS CA C 54.316 0.484 1 619 148 150 LYS CB C 33.444 0.484 1 620 148 150 LYS N N 124.492 0.125 1 621 149 151 VAL H H 8.981 0.004 1 622 149 151 VAL C C 174.987 0.344 1 623 149 151 VAL CA C 59.998 0.484 1 624 149 151 VAL CB C 32.943 0.484 1 625 149 151 VAL N N 128.471 0.125 1 626 150 152 VAL H H 8.771 0.004 1 627 150 152 VAL C C 175.465 0.344 1 628 150 152 VAL CA C 60.534 0.484 1 629 150 152 VAL CB C 34.533 0.484 1 630 150 152 VAL N N 125.266 0.125 1 631 151 153 TYR H H 8.320 0.004 1 632 151 153 TYR C C 176.365 0.344 1 633 151 153 TYR CA C 57.412 0.484 1 634 151 153 TYR CB C 38.416 0.484 1 635 151 153 TYR N N 127.185 0.125 1 636 152 154 GLY H H 8.214 0.004 1 637 152 154 GLY C C 174.452 0.344 1 638 152 154 GLY CA C 45.205 0.484 1 639 152 154 GLY N N 113.958 0.125 1 640 153 155 GLY H H 7.332 0.004 1 641 153 155 GLY C C 171.900 0.344 1 642 153 155 GLY CA C 44.960 0.484 1 643 153 155 GLY N N 107.200 0.125 1 644 154 156 TYR H H 8.790 0.004 1 645 154 156 TYR C C 174.530 0.344 1 646 154 156 TYR CA C 58.169 0.484 1 647 154 156 TYR CB C 41.245 0.484 1 648 154 156 TYR N N 121.102 0.125 1 649 155 157 ASP H H 9.745 0.004 1 650 155 157 ASP C C 177.043 0.344 1 651 155 157 ASP CA C 53.216 0.484 1 652 155 157 ASP CB C 41.001 0.484 1 653 155 157 ASP N N 124.606 0.125 1 654 156 158 THR H H 8.144 0.004 1 655 156 158 THR C C 175.822 0.344 1 656 156 158 THR CA C 61.298 0.484 1 657 156 158 THR CB C 68.017 0.484 1 658 156 158 THR N N 115.081 0.125 1 659 157 159 LYS H H 8.658 0.004 1 660 157 159 LYS C C 177.576 0.344 1 661 157 159 LYS CA C 57.770 0.484 1 662 157 159 LYS CB C 31.146 0.484 1 663 157 159 LYS N N 123.589 0.125 1 664 158 160 THR H H 7.144 0.004 1 665 158 160 THR C C 171.948 0.344 1 666 158 160 THR CA C 60.723 0.484 1 667 158 160 THR CB C 70.462 0.484 1 668 158 160 THR N N 113.103 0.125 1 669 159 161 GLN H H 7.707 0.004 1 670 159 161 GLN CA C 51.937 0.484 1 671 159 161 GLN CB C 29.900 0.484 1 672 159 161 GLN N N 122.161 0.125 1 673 160 162 PRO C C 174.177 0.344 1 674 160 162 PRO CA C 62.112 0.484 1 675 160 162 PRO CB C 33.747 0.484 1 676 161 163 ALA H H 8.230 0.004 1 677 161 163 ALA C C 176.195 0.344 1 678 161 163 ALA CA C 52.435 0.484 1 679 161 163 ALA CB C 18.773 0.484 1 680 161 163 ALA N N 122.358 0.125 1 681 162 164 MET H H 6.895 0.004 1 682 162 164 MET CA C 50.322 0.484 1 683 162 164 MET CB C 28.760 0.484 1 684 162 164 MET N N 117.866 0.125 1 685 163 165 PRO C C 174.616 0.344 1 686 163 165 PRO CA C 64.088 0.484 1 687 163 165 PRO CB C 31.972 0.484 1 688 164 166 ALA H H 8.786 0.004 1 689 164 166 ALA C C 178.197 0.344 1 690 164 166 ALA CA C 51.937 0.484 1 691 164 166 ALA CB C 19.801 0.484 1 692 164 166 ALA N N 123.874 0.125 1 693 165 167 ASN H H 7.188 0.004 1 694 165 167 ASN C C 174.272 0.344 1 695 165 167 ASN CA C 53.053 0.484 1 696 165 167 ASN CB C 40.953 0.484 1 697 165 167 ASN N N 115.065 0.125 1 698 166 168 MET H H 9.147 0.004 1 699 166 168 MET C C 173.494 0.344 1 700 166 168 MET CA C 54.924 0.484 1 701 166 168 MET CB C 37.640 0.484 1 702 166 168 MET N N 121.619 0.125 1 703 167 169 GLU H H 8.505 0.004 1 704 167 169 GLU C C 174.343 0.344 1 705 167 169 GLU CA C 54.832 0.484 1 706 167 169 GLU CB C 32.582 0.484 1 707 167 169 GLU N N 122.116 0.125 1 708 168 170 LEU H H 9.430 0.004 1 709 168 170 LEU C C 176.052 0.344 1 710 168 170 LEU CA C 54.354 0.484 1 711 168 170 LEU CB C 43.746 0.484 1 712 168 170 LEU N N 126.313 0.125 1 713 169 171 THR H H 9.212 0.004 1 714 169 171 THR C C 172.256 0.344 1 715 169 171 THR CA C 59.849 0.484 1 716 169 171 THR CB C 71.481 0.484 1 717 169 171 THR N N 115.878 0.125 1 718 170 172 ASP H H 7.765 0.004 1 719 170 172 ASP C C 177.694 0.344 1 720 170 172 ASP CA C 52.636 0.484 1 721 170 172 ASP CB C 39.932 0.484 1 722 170 172 ASP N N 127.594 0.125 1 723 171 173 GLY H H 8.451 0.004 1 724 171 173 GLY C C 174.614 0.344 1 725 171 173 GLY CA C 45.700 0.484 1 726 171 173 GLY N N 113.002 0.125 1 727 172 174 GLY H H 8.388 0.004 1 728 172 174 GLY C C 173.427 0.344 1 729 172 174 GLY CA C 45.407 0.484 1 730 172 174 GLY N N 112.620 0.125 1 731 173 175 GLN H H 8.566 0.004 1 732 173 175 GLN C C 175.139 0.344 1 733 173 175 GLN CA C 54.070 0.484 1 734 173 175 GLN CB C 30.426 0.484 1 735 173 175 GLN N N 121.874 0.125 1 736 174 176 ARG H H 8.625 0.004 1 737 174 176 ARG C C 173.775 0.344 1 738 174 176 ARG CA C 54.366 0.484 1 739 174 176 ARG CB C 33.272 0.484 1 740 174 176 ARG N N 123.686 0.125 1 741 175 177 ILE H H 9.186 0.004 1 742 175 177 ILE C C 174.563 0.344 1 743 175 177 ILE CA C 59.400 0.484 1 744 175 177 ILE CB C 40.091 0.484 1 745 175 177 ILE N N 124.745 0.125 1 746 176 178 LYS H H 9.101 0.004 1 747 176 178 LYS C C 174.782 0.344 1 748 176 178 LYS CA C 54.642 0.484 1 749 176 178 LYS CB C 34.441 0.484 1 750 176 178 LYS N N 127.458 0.125 1 751 177 179 LEU H H 8.565 0.004 1 752 177 179 LEU C C 175.318 0.344 1 753 177 179 LEU CA C 54.016 0.484 1 754 177 179 LEU CB C 44.167 0.484 1 755 177 179 LEU N N 124.059 0.125 1 756 178 180 LYS H H 8.616 0.004 1 757 178 180 LYS C C 174.834 0.344 1 758 178 180 LYS CA C 55.572 0.484 1 759 178 180 LYS CB C 34.556 0.484 1 760 178 180 LYS N N 125.036 0.125 1 761 179 181 MET H H 8.768 0.004 1 762 179 181 MET C C 176.128 0.344 1 763 179 181 MET CA C 57.273 0.484 1 764 179 181 MET CB C 32.238 0.484 1 765 179 181 MET N N 130.230 0.125 1 766 180 182 ASP H H 9.481 0.004 1 767 180 182 ASP C C 176.402 0.344 1 768 180 182 ASP CA C 55.637 0.484 1 769 180 182 ASP CB C 41.414 0.484 1 770 180 182 ASP N N 125.098 0.125 1 771 181 183 ASN H H 7.128 0.004 1 772 181 183 ASN C C 172.912 0.344 1 773 181 183 ASN CA C 53.032 0.484 1 774 181 183 ASN CB C 40.918 0.484 1 775 181 183 ASN N N 113.358 0.125 1 776 182 184 TRP H H 8.952 0.004 1 777 182 184 TRP C C 175.950 0.344 1 778 182 184 TRP CA C 57.500 0.484 1 779 182 184 TRP CB C 33.308 0.484 1 780 182 184 TRP N N 123.652 0.125 1 781 183 185 ILE H H 9.210 0.004 1 782 183 185 ILE C C 176.316 0.344 1 783 183 185 ILE CA C 61.399 0.484 1 784 183 185 ILE CB C 39.882 0.484 1 785 183 185 ILE N N 123.018 0.125 1 786 184 186 VAL H H 8.609 0.004 1 787 184 186 VAL C C 174.475 0.344 1 788 184 186 VAL CA C 58.288 0.484 1 789 184 186 VAL CB C 34.363 0.484 1 790 184 186 VAL N N 122.212 0.125 1 791 185 187 LYS H H 8.407 0.004 1 792 185 187 LYS CA C 57.753 0.484 1 793 185 187 LYS CB C 34.511 0.484 1 794 185 187 LYS N N 127.963 0.125 1 stop_ save_