data_4773 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments for OspA N-terminal fragment[27-163] ; _BMRB_accession_number 4773 _BMRB_flat_file_name bmr4773.str _Entry_type original _Submission_date 2000-06-30 _Accession_date 2000-06-30 _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 Huang Xiaolin . . 2 Nakagawa Tomoko . . 3 Tamura Atsuo . . 4 Link Karl . . 5 Koide Akiko . . 6 Koide Shohei . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 138 "13C chemical shifts" 406 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-08-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4076 'Outer Surface Protein A' stop_ _Original_release_date 2001-08-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Formation of the Single-layer Beta-sheet of Borrelia burgdorferi OspA in the Absence of the C-terminal Capping Globular Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21226873 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Xiaolin . . 2 Nakagawa Tomoko . . 3 Tamura Atsuo . . 4 Link Karl . . 5 Koide Akiko . . 6 Koide Shohei . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 308 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 367 _Page_last 375 _Year 2001 _Details . loop_ _Keyword 'outer surface protein A' 'protein folding' 'protein stability' 'Lyme disease' stop_ save_ ################################## # Molecular system description # ################################## save_system_OspA-NTF _Saveframe_category molecular_system _Mol_system_name 'OspA N-terminal fragment' _Abbreviation_common OspA-NTF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'OspA fragment residue 27-163' $OspA-NTF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'major surface antigen' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OspA-NTF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'outer surface protein A' _Name_variant 'residues 27-163' _Abbreviation_common OspA-NTF _Molecular_mass . _Mol_thiol_state 'not present' _Details 'This fragment contains three additional residues (GSH) at the N-terminus from the expression vector (pET15b).' ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; GSHMKNSVSVDLPGEMKVLV SKEKNKDGKYDLIATVDKLE LKGTSDKNNGSGVLEGVKAD KSKVKLTISDDLGQTTLEVF KEDGKTLVSKKVTSKDKSST EEKFNEKGEVSEKIITRADG TRLEYTGIKSDGSGKAKEVL K ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 . HIS 4 26 MET 5 27 LYS 6 28 ASN 7 29 SER 8 30 VAL 9 31 SER 10 32 VAL 11 33 ASP 12 34 LEU 13 35 PRO 14 36 GLY 15 37 GLU 16 38 MET 17 39 LYS 18 40 VAL 19 41 LEU 20 42 VAL 21 43 SER 22 44 LYS 23 45 GLU 24 46 LYS 25 47 ASN 26 48 LYS 27 49 ASP 28 50 GLY 29 51 LYS 30 52 TYR 31 53 ASP 32 54 LEU 33 55 ILE 34 56 ALA 35 57 THR 36 58 VAL 37 59 ASP 38 60 LYS 39 61 LEU 40 62 GLU 41 63 LEU 42 64 LYS 43 65 GLY 44 66 THR 45 67 SER 46 68 ASP 47 69 LYS 48 70 ASN 49 71 ASN 50 72 GLY 51 73 SER 52 74 GLY 53 75 VAL 54 76 LEU 55 77 GLU 56 78 GLY 57 79 VAL 58 80 LYS 59 81 ALA 60 82 ASP 61 83 LYS 62 84 SER 63 85 LYS 64 86 VAL 65 87 LYS 66 88 LEU 67 89 THR 68 90 ILE 69 91 SER 70 92 ASP 71 93 ASP 72 94 LEU 73 95 GLY 74 96 GLN 75 97 THR 76 98 THR 77 99 LEU 78 100 GLU 79 101 VAL 80 102 PHE 81 103 LYS 82 104 GLU 83 105 ASP 84 106 GLY 85 107 LYS 86 108 THR 87 109 LEU 88 110 VAL 89 111 SER 90 112 LYS 91 113 LYS 92 114 VAL 93 115 THR 94 116 SER 95 117 LYS 96 118 ASP 97 119 LYS 98 120 SER 99 121 SER 100 122 THR 101 123 GLU 102 124 GLU 103 125 LYS 104 126 PHE 105 127 ASN 106 128 GLU 107 129 LYS 108 130 GLY 109 131 GLU 110 132 VAL 111 133 SER 112 134 GLU 113 135 LYS 114 136 ILE 115 137 ILE 116 138 THR 117 139 ARG 118 140 ALA 119 141 ASP 120 142 GLY 121 143 THR 122 144 ARG 123 145 LEU 124 146 GLU 125 147 TYR 126 148 THR 127 149 GLY 128 150 ILE 129 151 LYS 130 152 SER 131 153 ASP 132 154 GLY 133 155 SER 134 156 GLY 135 157 LYS 136 158 ALA 137 159 LYS 138 160 GLU 139 161 VAL 140 162 LEU 141 163 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 4076 OspA 97.16 257 100.00 100.00 1.84e-84 PDB 1FJ1 "Lyme Disease Antigen Ospa In Complex With Neutralizing Antibody Fab La-2" 97.16 257 99.27 99.27 7.73e-84 PDB 1OSP "Crystal Structure Of Outer Surface Protein A Of Borrelia Burgdorferi Complexed With A Murine Monoclonal Antibody Fab" 97.16 257 99.27 99.27 7.73e-84 EMBL CAA32579 "ospA [Borrelia burgdorferi]" 97.16 273 100.00 100.00 6.39e-84 EMBL CAA34487 "unnamed protein product [Borrelia burgdorferi ZS7]" 97.16 273 98.54 98.54 3.68e-82 EMBL CAA49314 "0spA [Borrelia burgdorferi]" 97.16 273 100.00 100.00 6.39e-84 EMBL CAA56467 "ospA [Borrelia burgdorferi]" 97.16 273 100.00 100.00 6.39e-84 EMBL CAA59729 "outer surface protein A [Borrelia burgdorferi 297]" 97.16 273 99.27 99.27 1.23e-82 GB AAA20947 "OspA, partial [Borrelia burgdorferi]" 97.16 250 100.00 100.00 2.48e-84 GB AAA20949 "OspA, partial [Borrelia burgdorferi]" 97.16 250 98.54 98.54 3.81e-82 GB AAA20951 "OspA, partial [Borrelia burgdorferi]" 97.16 250 100.00 100.00 2.48e-84 GB AAA20953 "OspA, partial [Borrelia burgdorferi]" 97.16 250 98.54 99.27 6.00e-83 GB AAA20955 "OspA, partial [Borrelia burgdorferi]" 97.16 250 100.00 100.00 2.48e-84 REF NP_045688 "outer surface protein A [Borrelia burgdorferi B31]" 97.16 273 100.00 100.00 6.39e-84 REF WP_010258120 "outer surface protein A (ospA) [Borrelia burgdorferi]" 97.16 273 99.27 99.27 1.23e-82 REF WP_010890378 "outer surface protein A (OspA) [Borrelia burgdorferi]" 97.16 273 100.00 100.00 6.39e-84 REF WP_012615002 "outer surface protein A (OspA) [Borrelia burgdorferi]" 97.16 273 98.54 98.54 3.68e-82 REF WP_012665570 "outer surfce protein A [Borrelia burgdorferi]" 97.16 273 98.54 98.54 4.57e-82 SP B7IZU3 "RecName: Full=Outer surface protein A; Flags: Precursor [Borrelia burgdorferi ZS7]" 97.16 273 98.54 98.54 3.68e-82 SP C6C2D6 "RecName: Full=Outer surface protein A; Flags: Precursor [Borrelia burgdorferi N40]" 97.16 273 98.54 98.54 4.57e-82 SP P0CL66 "RecName: Full=Outer surface protein A; Flags: Precursor [Borrelia burgdorferi B31]" 97.16 273 100.00 100.00 6.39e-84 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 _Gene_mnemonic $OspA-NTF Spirochete 139 Eubacteria Bacteria Borrelia burgdorferi B31 ospA 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 $OspA-NTF '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 _Isotopic_labeling $OspA-NTF 1.5 mM '[U-13C; U-15N]' 'sodium phosphate' 10 mM . 'sodium chloride' 50 mM . stop_ 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_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 308 0.5 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP C 13 'methyl protons' ppm 0.00 external indirect . external_to_the_sample . 0.25144954 $entry_citation $entry_citation ammonia N 15 nitrogen ppm 0.00 external indirect . external_to_the_sample . 0.10132900 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation 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_backbone _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC HNCO CBCA(CO)NH HNCACB stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'OspA fragment residue 27-163' _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 . 1 GLY CA C 45.6 0.5 1 2 . 2 SER CA C 58.2 0.5 1 3 . 2 SER CB C 64.0 0.5 1 4 . 2 SER C C 174.3 0.1 1 5 . 3 HIS N N 124.9 0.2 1 6 . 3 HIS H H 8.41 0.015 1 7 . 3 HIS CA C 55.9 0.5 1 8 . 3 HIS CB C 30.4 0.5 1 9 . 3 HIS C C 173.5 0.1 1 10 . 4 MET N N 122.6 0.2 1 11 . 4 MET H H 8.25 0.015 1 12 . 4 MET CA C 55.6 0.5 1 13 . 4 MET CB C 33.4 0.5 1 14 . 4 MET C C 176.5 0.1 1 15 . 5 LYS N N 124.9 0.2 1 16 . 5 LYS H H 8.46 0.015 1 17 . 5 LYS CA C 57.1 0.5 1 18 . 5 LYS CB C 32.8 0.5 1 19 . 5 LYS C C 176.5 0.1 1 20 . 6 ASN N N 120.2 0.2 1 21 . 6 ASN H H 8.55 0.015 1 22 . 6 ASN CA C 53.1 0.5 1 23 . 6 ASN CB C 38.6 0.5 1 24 . 6 ASN C C 174.2 0.1 1 25 . 7 SER N N 115.7 0.2 1 26 . 7 SER H H 7.98 0.015 1 27 . 7 SER CA C 57.6 0.5 1 28 . 7 SER CB C 67.1 0.5 1 29 . 7 SER C C 172.9 0.1 1 30 . 8 VAL N N 121.5 0.2 1 31 . 8 VAL H H 9.05 0.015 1 32 . 8 VAL CA C 60.9 0.5 1 33 . 8 VAL CB C 34.5 0.5 1 34 . 8 VAL C C 174.3 0.1 1 35 . 9 SER N N 120.1 0.2 1 36 . 9 SER H H 8.29 0.015 1 37 . 9 SER CA C 57.1 0.5 1 38 . 9 SER CB C 64.0 0.5 1 39 . 9 SER C C 174.4 0.1 1 40 . 10 VAL N N 131.0 0.2 1 41 . 10 VAL H H 9.36 0.015 1 42 . 10 VAL CA C 61.9 0.5 1 43 . 10 VAL CB C 34.3 0.5 1 44 . 10 VAL C C 175.0 0.1 1 45 . 11 ASP N N 127.3 0.2 1 46 . 11 ASP H H 8.27 0.015 1 47 . 11 ASP CA C 55.3 0.5 1 48 . 11 ASP CB C 41.8 0.5 1 49 . 11 ASP C C 175.4 0.1 1 50 . 12 LEU N N 123.1 0.2 1 51 . 12 LEU H H 8.33 0.015 1 52 . 12 LEU CA C 51.8 0.5 1 53 . 12 LEU CB C 44.1 0.5 1 54 . 13 PRO CA C 63.6 0.5 1 55 . 13 PRO CB C 32.0 0.5 1 56 . 13 PRO C C 176.2 0.1 1 57 . 14 GLY N N 111.4 0.2 1 58 . 14 GLY H H 8.78 0.015 1 59 . 14 GLY CA C 45.7 0.5 1 60 . 14 GLY C C 174.4 0.1 1 61 . 15 GLU N N 115.7 0.2 1 62 . 15 GLU H H 8.38 0.015 1 63 . 15 GLU CA C 56.9 0.5 1 64 . 15 GLU CB C 26.7 0.5 1 65 . 15 GLU C C 175.4 0.1 1 66 . 16 MET N N 117.9 0.2 1 67 . 16 MET H H 6.80 0.015 1 68 . 16 MET CA C 54.5 0.5 1 69 . 16 MET CB C 36.3 0.5 1 70 . 16 MET C C 174.3 0.1 1 71 . 17 LYS N N 122.0 0.2 1 72 . 17 LYS H H 8.14 0.015 1 73 . 17 LYS CA C 55.1 0.5 1 74 . 17 LYS CB C 36.2 0.5 1 75 . 17 LYS C C 175.0 0.1 1 76 . 18 VAL N N 122.6 0.2 1 77 . 18 VAL H H 8.77 0.015 1 78 . 18 VAL CA C 58.8 0.5 1 79 . 18 VAL CB C 35.8 0.5 1 80 . 18 VAL C C 171.8 0.1 1 81 . 19 LEU N N 128.7 0.2 1 82 . 19 LEU H H 9.18 0.015 1 83 . 19 LEU CA C 53.3 0.5 1 84 . 19 LEU CB C 42.8 0.5 1 85 . 19 LEU C C 175.9 0.1 1 86 . 20 VAL N N 124.1 0.2 1 87 . 20 VAL H H 8.96 0.015 1 88 . 20 VAL CA C 59.3 0.5 1 89 . 20 VAL CB C 34.5 0.5 1 90 . 20 VAL C C 176.1 0.1 1 91 . 21 SER N N 124.4 0.2 1 92 . 21 SER H H 8.91 0.015 1 93 . 21 SER CA C 59.7 0.5 1 94 . 21 SER CB C 64.2 0.5 1 95 . 21 SER C C 174.1 0.1 1 96 . 22 LYS N N 121.4 0.2 1 97 . 22 LYS H H 8.30 0.015 1 98 . 22 LYS CA C 58.2 0.5 1 99 . 22 LYS CB C 33.3 0.5 1 100 . 22 LYS C C 177.3 0.1 1 101 . 23 GLU N N 116.5 0.2 1 102 . 23 GLU H H 8.16 0.015 1 103 . 23 GLU CA C 53.8 0.5 1 104 . 23 GLU CB C 32.5 0.5 1 105 . 23 GLU C C 176.5 0.1 1 106 . 24 LYS N N 124.1 0.2 1 107 . 24 LYS H H 8.54 0.015 1 108 . 24 LYS CA C 56.5 0.5 1 109 . 24 LYS CB C 34.2 0.5 1 110 . 24 LYS C C 176.7 0.1 1 111 . 25 ASN N N 121.2 0.2 1 112 . 25 ASN H H 9.22 0.015 1 113 . 25 ASN CA C 51.0 0.5 1 114 . 25 ASN CB C 38.8 0.5 1 115 . 25 ASN C C 176.6 0.1 1 116 . 26 LYS N N 118.8 0.2 1 117 . 26 LYS H H 8.39 0.015 1 118 . 26 LYS CA C 58.7 0.5 1 119 . 26 LYS CB C 31.8 0.5 1 120 . 26 LYS C C 176.8 0.1 1 121 . 27 ASP N N 119.3 0.2 1 122 . 27 ASP H H 7.95 0.015 1 123 . 27 ASP CA C 54.2 0.5 1 124 . 27 ASP CB C 41.6 0.5 1 125 . 27 ASP C C 176.2 0.1 1 126 . 28 GLY N N 108.8 0.2 1 127 . 28 GLY H H 8.23 0.015 1 128 . 28 GLY CA C 45.7 0.5 1 129 . 28 GLY C C 173.2 0.1 1 130 . 29 LYS N N 119.4 0.2 1 131 . 29 LYS H H 7.35 0.015 1 132 . 29 LYS CA C 53.7 0.5 1 133 . 29 LYS CB C 36.0 0.5 1 134 . 29 LYS C C 173.8 0.1 1 135 . 30 TYR N N 119.8 0.2 1 136 . 30 TYR H H 9.19 0.015 1 137 . 30 TYR CA C 58.8 0.5 1 138 . 30 TYR CB C 38.6 0.5 1 139 . 30 TYR C C 175.7 0.1 1 140 . 31 ASP N N 123.1 0.2 1 141 . 31 ASP H H 8.54 0.015 1 142 . 31 ASP CA C 55.1 0.5 1 143 . 31 ASP CB C 43.7 0.5 1 144 . 31 ASP C C 174.8 0.1 1 145 . 32 LEU N N 121.7 0.2 1 146 . 32 LEU H H 8.48 0.015 1 147 . 32 LEU CA C 53.6 0.5 1 148 . 32 LEU CB C 46.2 0.5 1 149 . 32 LEU C C 177.3 0.1 1 150 . 33 ILE N N 122.6 0.2 1 151 . 33 ILE H H 8.72 0.015 1 152 . 33 ILE CA C 60.3 0.5 1 153 . 33 ILE CB C 42.8 0.5 1 154 . 33 ILE C C 173.6 0.1 1 155 . 34 ALA N N 127.4 0.2 1 156 . 34 ALA H H 8.58 0.015 1 157 . 34 ALA CA C 51.2 0.5 1 158 . 34 ALA CB C 23.6 0.5 1 159 . 34 ALA C C 175.4 0.1 1 160 . 35 THR N N 118.3 0.2 1 161 . 35 THR H H 8.86 0.015 1 162 . 35 THR CA C 61.7 0.5 1 163 . 35 THR CB C 69.8 0.5 1 164 . 35 THR C C 174.4 0.1 1 165 . 36 VAL N N 127.8 0.2 1 166 . 36 VAL H H 8.71 0.015 1 167 . 36 VAL CA C 61.0 0.5 1 168 . 36 VAL CB C 34.5 0.5 1 169 . 36 VAL C C 175.3 0.1 1 170 . 37 ASP N N 130.1 0.2 1 171 . 37 ASP H H 9.24 0.015 1 172 . 37 ASP CA C 56.0 0.5 1 173 . 37 ASP CB C 39.4 0.5 1 174 . 37 ASP C C 175.1 0.1 1 175 . 38 LYS N N 111.5 0.2 1 176 . 38 LYS H H 8.32 0.015 1 177 . 38 LYS CA C 58.1 0.5 1 178 . 38 LYS CB C 30.6 0.5 1 179 . 38 LYS C C 174.9 0.1 1 180 . 39 LEU N N 125.4 0.2 1 181 . 39 LEU H H 8.10 0.015 1 182 . 39 LEU CA C 54.1 0.5 1 183 . 39 LEU CB C 44.3 0.5 1 184 . 39 LEU C C 174.8 0.1 1 185 . 40 GLU N N 126.8 0.2 1 186 . 40 GLU H H 8.44 0.015 1 187 . 40 GLU CA C 56.4 0.5 1 188 . 40 GLU CB C 30.8 0.5 1 189 . 40 GLU C C 175.0 0.1 1 190 . 41 LEU N N 128.7 0.2 1 191 . 41 LEU H H 9.41 0.015 1 192 . 41 LEU CA C 53.3 0.5 1 193 . 41 LEU CB C 44.4 0.5 1 194 . 41 LEU C C 175.4 0.1 1 195 . 42 LYS N N 119.0 0.2 1 196 . 42 LYS H H 8.41 0.015 1 197 . 42 LYS CA C 55.0 0.5 1 198 . 42 LYS CB C 37.4 0.5 1 199 . 42 LYS C C 176.8 0.1 1 200 . 43 GLY N N 112.3 0.2 1 201 . 43 GLY H H 8.90 0.015 1 202 . 43 GLY CA C 45.6 0.5 1 203 . 43 GLY C C 172.2 0.1 1 204 . 44 THR N N 112.2 0.2 1 205 . 44 THR H H 8.57 0.015 1 206 . 44 THR CA C 59.8 0.5 1 207 . 44 THR CB C 73.6 0.5 1 208 . 44 THR C C 173.9 0.1 1 209 . 45 SER N N 113.7 0.2 1 210 . 45 SER H H 8.98 0.015 1 211 . 45 SER CA C 56.4 0.5 1 212 . 45 SER CB C 65.4 0.5 1 213 . 45 SER C C 173.6 0.1 1 214 . 46 ASP N N 125.4 0.2 1 215 . 46 ASP H H 8.91 0.015 1 216 . 46 ASP CA C 55.8 0.5 1 217 . 46 ASP CB C 41.0 0.5 1 218 . 46 ASP C C 176.2 0.1 1 219 . 47 LYS N N 120.7 0.2 1 220 . 47 LYS H H 8.72 0.015 1 221 . 47 LYS CA C 55.0 0.5 1 222 . 47 LYS CB C 35.5 0.5 1 223 . 47 LYS C C 176.1 0.1 1 224 . 48 ASN N N 117.4 0.2 1 225 . 48 ASN H H 7.81 0.015 1 226 . 48 ASN CA C 50.8 0.5 1 227 . 48 ASN CB C 36.4 0.5 1 228 . 48 ASN C C 174.6 0.1 1 229 . 49 ASN N N 116.1 0.2 1 230 . 49 ASN H H 7.61 0.015 1 231 . 49 ASN CA C 52.8 0.5 1 232 . 49 ASN CB C 38.1 0.5 1 233 . 49 ASN C C 173.8 0.1 1 234 . 50 GLY N N 110.6 0.2 1 235 . 50 GLY H H 9.13 0.015 1 236 . 50 GLY CA C 44.4 0.5 1 237 . 50 GLY C C 170.0 0.1 1 238 . 51 SER N N 110.4 0.2 1 239 . 51 SER H H 7.04 0.015 1 240 . 51 SER CA C 57.3 0.5 1 241 . 51 SER CB C 66.1 0.5 1 242 . 51 SER C C 174.1 0.1 1 243 . 52 GLY N N 107.1 0.2 1 244 . 52 GLY H H 7.74 0.015 1 245 . 52 GLY CA C 44.1 0.5 1 246 . 52 GLY C C 170.8 0.1 1 247 . 53 VAL N N 120.2 0.2 1 248 . 53 VAL H H 8.19 0.015 1 249 . 53 VAL CA C 61.1 0.5 1 250 . 53 VAL CB C 34.6 0.5 1 251 . 53 VAL C C 175.3 0.1 1 252 . 54 LEU N N 127.5 0.2 1 253 . 54 LEU H H 9.55 0.015 1 254 . 54 LEU CA C 54.8 0.5 1 255 . 54 LEU CB C 46.5 0.5 1 256 . 54 LEU C C 175.2 0.1 1 257 . 55 GLU N N 118.8 0.2 1 258 . 55 GLU H H 8.69 0.015 1 259 . 55 GLU CA C 54.8 0.5 1 260 . 55 GLU CB C 35.9 0.5 1 261 . 55 GLU C C 176.4 0.1 1 262 . 56 GLY N N 110.8 0.2 1 263 . 56 GLY H H 8.86 0.015 1 264 . 56 GLY CA C 45.3 0.5 1 265 . 56 GLY C C 171.0 0.1 1 266 . 57 VAL N N 121.3 0.2 1 267 . 57 VAL H H 8.62 0.015 1 268 . 57 VAL CA C 60.9 0.5 1 269 . 57 VAL CB C 35.0 0.5 1 270 . 57 VAL C C 175.4 0.1 1 271 . 58 LYS N N 125.3 0.2 1 272 . 58 LYS H H 8.75 0.015 1 273 . 58 LYS CA C 56.4 0.5 1 274 . 58 LYS CB C 34.6 0.5 1 275 . 58 LYS C C 178.8 0.1 1 276 . 59 ALA N N 125.9 0.2 1 277 . 59 ALA H H 8.83 0.015 1 278 . 59 ALA CA C 55.0 0.5 1 279 . 59 ALA CB C 18.1 0.5 1 280 . 59 ALA C C 178.1 0.1 1 281 . 60 ASP N N 115.7 0.2 1 282 . 60 ASP H H 7.50 0.015 1 283 . 60 ASP CA C 53.2 0.5 1 284 . 60 ASP CB C 39.5 0.5 1 285 . 60 ASP C C 176.5 0.1 1 286 . 61 LYS N N 111.9 0.2 1 287 . 61 LYS H H 8.01 0.015 1 288 . 61 LYS CA C 58.9 0.5 1 289 . 61 LYS CB C 29.6 0.5 1 290 . 61 LYS C C 175.6 0.1 1 291 . 62 SER N N 116.5 0.2 1 292 . 62 SER H H 8.18 0.015 1 293 . 62 SER CA C 60.5 0.5 1 294 . 62 SER CB C 63.0 0.5 1 295 . 62 SER C C 172.7 0.1 1 296 . 63 LYS N N 123.7 0.2 1 297 . 63 LYS H H 7.82 0.015 1 298 . 63 LYS CA C 55.5 0.5 1 299 . 63 LYS CB C 35.0 0.5 1 300 . 63 LYS C C 174.7 0.1 1 301 . 64 VAL N N 124.1 0.2 1 302 . 64 VAL H H 8.70 0.015 1 303 . 64 VAL CA C 60.9 0.5 1 304 . 64 VAL CB C 34.5 0.5 1 305 . 64 VAL C C 174.5 0.1 1 306 . 65 LYS N N 129.2 0.2 1 307 . 65 LYS H H 9.52 0.015 1 308 . 65 LYS CA C 55.1 0.5 1 309 . 65 LYS CB C 37.8 0.5 1 310 . 65 LYS C C 174.0 0.1 1 311 . 66 LEU N N 132.6 0.2 1 312 . 66 LEU H H 9.61 0.015 1 313 . 66 LEU CA C 52.8 0.5 1 314 . 66 LEU CB C 46.0 0.5 1 315 . 66 LEU C C 174.0 0.1 1 316 . 67 THR N N 124.1 0.2 1 317 . 67 THR H H 9.43 0.015 1 318 . 67 THR CA C 62.5 0.5 1 319 . 67 THR CB C 70.0 0.5 1 320 . 67 THR C C 174.2 0.1 1 321 . 68 ILE N N 132.5 0.2 1 322 . 68 ILE H H 9.56 0.015 1 323 . 68 ILE CA C 60.9 0.5 1 324 . 68 ILE CB C 40.3 0.5 1 325 . 68 ILE C C 176.5 0.1 1 326 . 69 SER N N 124.9 0.2 1 327 . 69 SER H H 8.46 0.015 1 328 . 69 SER CA C 59.7 0.5 1 329 . 69 SER CB C 64.1 0.5 1 330 . 69 SER C C 174.8 0.1 1 331 . 70 ASP N N 121.1 0.2 1 332 . 70 ASP H H 8.57 0.015 1 333 . 70 ASP CA C 57.7 0.5 1 334 . 70 ASP CB C 41.2 0.5 1 335 . 70 ASP C C 176.3 0.1 1 336 . 71 ASP N N 115.6 0.2 1 337 . 71 ASP H H 7.82 0.015 1 338 . 71 ASP CA C 52.2 0.5 1 339 . 71 ASP CB C 43.8 0.5 1 340 . 71 ASP C C 176.8 0.1 1 341 . 72 LEU N N 117.5 0.2 1 342 . 72 LEU H H 8.37 0.015 1 343 . 72 LEU CA C 56.5 0.5 1 344 . 72 LEU CB C 39.1 0.5 1 345 . 72 LEU C C 176.1 0.1 1 346 . 73 GLY N N 105.8 0.2 1 347 . 73 GLY H H 8.16 0.015 1 348 . 73 GLY CA C 46.2 0.5 1 349 . 73 GLY C C 173.6 0.1 1 350 . 74 GLN N N 118.9 0.2 1 351 . 74 GLN H H 7.86 0.015 1 352 . 74 GLN CA C 54.8 0.5 1 353 . 74 GLN CB C 33.8 0.5 1 354 . 74 GLN C C 174.7 0.1 1 355 . 75 THR N N 114.1 0.2 1 356 . 75 THR H H 8.89 0.015 1 357 . 75 THR CA C 58.8 0.5 1 358 . 75 THR CB C 71.3 0.5 1 359 . 75 THR C C 173.5 0.1 1 360 . 76 THR N N 119.8 0.2 1 361 . 76 THR H H 9.05 0.015 1 362 . 76 THR CA C 62.3 0.5 1 363 . 76 THR CB C 71.0 0.5 1 364 . 76 THR C C 172.4 0.1 1 365 . 77 LEU N N 132.7 0.2 1 366 . 77 LEU H H 9.55 0.015 1 367 . 77 LEU CA C 53.4 0.5 1 368 . 77 LEU CB C 44.7 0.5 1 369 . 77 LEU C C 175.9 0.1 1 370 . 78 GLU N N 131.0 0.2 1 371 . 78 GLU H H 9.68 0.015 1 372 . 78 GLU CA C 55.0 0.5 1 373 . 78 GLU CB C 35.2 0.5 1 374 . 78 GLU C C 174.6 0.1 1 375 . 79 VAL N N 122.6 0.2 1 376 . 79 VAL H H 8.25 0.015 1 377 . 79 VAL CA C 61.3 0.5 1 378 . 79 VAL CB C 33.3 0.5 1 379 . 79 VAL C C 174.4 0.1 1 380 . 80 PHE N N 126.8 0.2 1 381 . 80 PHE H H 9.71 0.015 1 382 . 80 PHE CA C 56.2 0.5 1 383 . 80 PHE CB C 40.0 0.5 1 384 . 80 PHE C C 176.8 0.1 1 385 . 81 LYS N N 117.5 0.2 1 386 . 81 LYS H H 8.37 0.015 1 387 . 81 LYS CA C 56.5 0.5 1 388 . 81 LYS CB C 33.8 0.5 1 389 . 81 LYS C C 176.6 0.1 1 390 . 82 GLU N N 119.9 0.2 1 391 . 82 GLU H H 8.82 0.015 1 392 . 82 GLU CA C 58.5 0.5 1 393 . 82 GLU CB C 29.6 0.5 1 394 . 82 GLU C C 176.1 0.1 1 395 . 83 ASP N N 117.4 0.2 1 396 . 83 ASP H H 7.36 0.015 1 397 . 83 ASP CA C 54.6 0.5 1 398 . 83 ASP CB C 39.8 0.5 1 399 . 83 ASP C C 177.6 0.1 1 400 . 84 GLY N N 110.6 0.2 1 401 . 84 GLY H H 8.74 0.015 1 402 . 84 GLY CA C 46.0 0.5 1 403 . 84 GLY C C 172.1 0.1 1 404 . 85 LYS N N 118.8 0.2 1 405 . 85 LYS H H 8.50 0.015 1 406 . 85 LYS CA C 56.7 0.5 1 407 . 85 LYS CB C 36.0 0.5 1 408 . 85 LYS C C 175.8 0.1 1 409 . 86 THR N N 123.1 0.2 1 410 . 86 THR H H 9.74 0.015 1 411 . 86 THR CA C 63.5 0.5 1 412 . 86 THR CB C 67.6 0.5 1 413 . 86 THR C C 173.7 0.1 1 414 . 87 LEU N N 132.5 0.2 1 415 . 87 LEU H H 8.40 0.015 1 416 . 87 LEU CA C 56.3 0.5 1 417 . 87 LEU CB C 43.0 0.5 1 418 . 87 LEU C C 176.3 0.1 1 419 . 88 VAL N N 122.6 0.2 1 420 . 88 VAL H H 9.26 0.015 1 421 . 88 VAL CA C 64.0 0.5 1 422 . 88 VAL CB C 33.8 0.5 1 423 . 88 VAL C C 176.8 0.1 1 424 . 89 SER N N 113.7 0.2 1 425 . 89 SER H H 7.84 0.015 1 426 . 89 SER CA C 57.7 0.5 1 427 . 89 SER CB C 65.4 0.5 1 428 . 89 SER C C 171.7 0.1 1 429 . 90 LYS N N 123.1 0.2 1 430 . 90 LYS H H 8.95 0.015 1 431 . 90 LYS CA C 55.9 0.5 1 432 . 90 LYS CB C 37.5 0.5 1 433 . 90 LYS C C 174.2 0.1 1 434 . 91 LYS N N 130.7 0.2 1 435 . 91 LYS H H 9.30 0.015 1 436 . 91 LYS CA C 55.0 0.5 1 437 . 91 LYS CB C 36.2 0.5 1 438 . 91 LYS C C 175.3 0.1 1 439 . 92 VAL N N 133.3 0.2 1 440 . 92 VAL H H 9.23 0.015 1 441 . 92 VAL CA C 61.2 0.5 1 442 . 92 VAL CB C 34.1 0.5 1 443 . 92 VAL C C 175.9 0.1 1 444 . 93 THR N N 125.9 0.2 1 445 . 93 THR H H 9.10 0.015 1 446 . 93 THR CA C 62.1 0.5 1 447 . 93 THR CB C 70.0 0.5 1 448 . 93 THR C C 173.1 0.1 1 449 . 94 SER N N 120.8 0.2 1 450 . 94 SER H H 8.56 0.015 1 451 . 94 SER CA C 56.9 0.5 1 452 . 94 SER CB C 64.7 0.5 1 453 . 94 SER C C 176.5 0.1 1 454 . 95 LYS N N 125.4 0.2 1 455 . 95 LYS H H 8.29 0.015 1 456 . 95 LYS CA C 58.9 0.5 1 457 . 95 LYS CB C 32.7 0.5 1 458 . 95 LYS C C 175.8 0.1 1 459 . 96 ASP N N 120.2 0.2 1 460 . 96 ASP H H 7.96 0.015 1 461 . 96 ASP CA C 54.0 0.5 1 462 . 96 ASP CB C 39.5 0.5 1 463 . 96 ASP C C 175.4 0.1 1 464 . 97 LYS N N 111.3 0.2 1 465 . 97 LYS H H 7.99 0.015 1 466 . 97 LYS CA C 59.5 0.5 1 467 . 97 LYS CB C 30.1 0.5 1 468 . 97 LYS C C 176.3 0.1 1 469 . 98 SER N N 118.4 0.2 1 470 . 98 SER H H 8.37 0.015 1 471 . 98 SER CA C 58.5 0.5 1 472 . 98 SER CB C 64.7 0.5 1 473 . 98 SER C C 173.2 0.1 1 474 . 99 SER N N 114.6 0.2 1 475 . 99 SER H H 8.99 0.015 1 476 . 99 SER CA C 57.3 0.5 1 477 . 99 SER CB C 67.4 0.5 1 478 . 99 SER C C 174.1 0.1 1 479 . 100 THR N N 117.9 0.2 1 480 . 100 THR H H 8.89 0.015 1 481 . 100 THR CA C 61.9 0.5 1 482 . 100 THR CB C 71.6 0.5 1 483 . 100 THR C C 172.9 0.1 1 484 . 101 GLU N N 129.1 0.2 1 485 . 101 GLU H H 9.27 0.015 1 486 . 101 GLU CA C 54.7 0.5 1 487 . 101 GLU CB C 33.2 0.5 1 488 . 101 GLU C C 174.4 0.1 1 489 . 102 GLU N N 126.4 0.2 1 490 . 102 GLU H H 9.19 0.015 1 491 . 102 GLU CA C 54.7 0.5 1 492 . 102 GLU CB C 34.8 0.5 1 493 . 102 GLU C C 174.6 0.1 1 494 . 103 LYS N N 122.2 0.2 1 495 . 103 LYS H H 8.28 0.015 1 496 . 103 LYS CA C 54.7 0.5 1 497 . 103 LYS CB C 34.8 0.5 1 498 . 103 LYS C C 175.1 0.1 1 499 . 104 PHE N N 121.2 0.2 1 500 . 104 PHE H H 7.85 0.015 1 501 . 104 PHE CA C 56.9 0.5 1 502 . 104 PHE CB C 42.6 0.5 1 503 . 104 PHE C C 176.7 0.1 1 504 . 105 ASN N N 120.3 0.2 1 505 . 105 ASN H H 8.87 0.015 1 506 . 105 ASN CA C 50.7 0.5 1 507 . 105 ASN CB C 39.0 0.5 1 508 . 105 ASN C C 177.8 0.1 1 509 . 106 GLU N N 119.8 0.2 1 510 . 106 GLU H H 9.20 0.015 1 511 . 106 GLU CA C 59.0 0.5 1 512 . 106 GLU CB C 28.9 0.5 1 513 . 106 GLU C C 177.0 0.1 1 514 . 107 LYS N N 118.8 0.2 1 515 . 107 LYS H H 7.64 0.015 1 516 . 107 LYS CA C 55.6 0.5 1 517 . 107 LYS CB C 32.7 0.5 1 518 . 107 LYS C C 176.9 0.1 1 519 . 108 GLY N N 109.0 0.2 1 520 . 108 GLY H H 8.28 0.015 1 521 . 108 GLY CA C 45.7 0.5 1 522 . 108 GLY C C 174.2 0.1 1 523 . 109 GLU N N 120.7 0.2 1 524 . 109 GLU H H 7.81 0.015 1 525 . 109 GLU CA C 54.3 0.5 1 526 . 109 GLU CB C 30.8 0.5 1 527 . 109 GLU C C 176.1 0.1 1 528 . 110 VAL N N 124.0 0.2 1 529 . 110 VAL H H 8.54 0.015 1 530 . 110 VAL CA C 63.7 0.5 1 531 . 110 VAL CB C 31.8 0.5 1 532 . 110 VAL C C 176.0 0.1 1 533 . 111 SER N N 125.4 0.2 1 534 . 111 SER H H 9.19 0.015 1 535 . 111 SER CA C 58.4 0.5 1 536 . 111 SER CB C 64.8 0.5 1 537 . 111 SER C C 174.7 0.1 1 538 . 112 GLU N N 121.9 0.2 1 539 . 112 GLU H H 7.38 0.015 1 540 . 112 GLU CA C 55.9 0.5 1 541 . 112 GLU CB C 33.9 0.5 1 542 . 112 GLU C C 173.3 0.1 1 543 . 113 LYS N N 125.0 0.2 1 544 . 113 LYS H H 8.65 0.015 1 545 . 113 LYS CA C 55.0 0.5 1 546 . 113 LYS CB C 36.2 0.5 1 547 . 113 LYS C C 173.9 0.1 1 548 . 114 ILE N N 127.3 0.2 1 549 . 114 ILE H H 9.36 0.015 1 550 . 114 ILE CA C 60.3 0.5 1 551 . 114 ILE CB C 41.0 0.5 1 552 . 114 ILE C C 176.3 0.1 1 553 . 115 ILE N N 132.8 0.2 1 554 . 115 ILE H H 9.41 0.015 1 555 . 115 ILE CA C 60.3 0.5 1 556 . 115 ILE CB C 40.7 0.5 1 557 . 115 ILE C C 175.0 0.1 1 558 . 116 THR N N 124.5 0.2 1 559 . 116 THR H H 9.15 0.015 1 560 . 116 THR CA C 61.7 0.5 1 561 . 116 THR CB C 69.6 0.5 1 562 . 116 THR C C 175.0 0.1 1 563 . 117 ARG N N 125.4 0.2 1 564 . 117 ARG H H 8.89 0.015 1 565 . 117 ARG CA C 55.6 0.5 1 566 . 117 ARG CB C 31.9 0.5 1 567 . 117 ARG C C 177.7 0.1 1 568 . 118 ALA N N 125.0 0.2 1 569 . 118 ALA H H 8.88 0.015 1 570 . 118 ALA CA C 54.7 0.5 1 571 . 118 ALA CB C 18.6 0.5 1 572 . 118 ALA C C 177.6 0.1 1 573 . 119 ASP N N 114.6 0.2 1 574 . 119 ASP H H 7.53 0.015 1 575 . 119 ASP CA C 53.2 0.5 1 576 . 119 ASP CB C 40.0 0.5 1 577 . 119 ASP C C 177.1 0.1 1 578 . 120 GLY N N 109.9 0.2 1 579 . 120 GLY H H 8.17 0.015 1 580 . 120 GLY CA C 44.9 0.5 1 581 . 120 GLY C C 174.8 0.1 1 582 . 121 THR N N 117.9 0.2 1 583 . 121 THR H H 8.08 0.015 1 584 . 121 THR CA C 63.9 0.5 1 585 . 121 THR CB C 69.8 0.5 1 586 . 121 THR C C 173.1 0.1 1 587 . 122 ARG N N 125.8 0.2 1 588 . 122 ARG H H 8.45 0.015 1 589 . 122 ARG CA C 54.9 0.5 1 590 . 122 ARG CB C 33.3 0.5 1 591 . 122 ARG C C 175.4 0.1 1 592 . 123 LEU N N 128.1 0.2 1 593 . 123 LEU H H 9.23 0.015 1 594 . 123 LEU CA C 54.3 0.5 1 595 . 123 LEU CB C 44.3 0.5 1 596 . 123 LEU C C 175.0 0.1 1 597 . 124 GLU N N 123.5 0.2 1 598 . 124 GLU H H 8.39 0.015 1 599 . 124 GLU CA C 55.1 0.5 1 600 . 124 GLU CB C 31.8 0.5 1 601 . 124 GLU C C 175.1 0.1 1 602 . 125 TYR N N 124.8 0.2 1 603 . 125 TYR H H 8.96 0.015 1 604 . 125 TYR CA C 57.1 0.5 1 605 . 125 TYR CB C 39.9 0.5 1 606 . 125 TYR C C 175.6 0.1 1 607 . 126 THR N N 117.4 0.2 1 608 . 126 THR H H 8.38 0.015 1 609 . 126 THR CA C 61.0 0.5 1 610 . 126 THR CB C 70.4 0.5 1 611 . 126 THR C C 174.4 0.1 1 612 . 127 GLY N N 112.2 0.2 1 613 . 127 GLY H H 8.11 0.015 1 614 . 127 GLY CA C 45.6 0.5 1 615 . 127 GLY C C 174.1 0.1 1 616 . 128 ILE N N 121.2 0.2 1 617 . 128 ILE H H 7.91 0.015 1 618 . 128 ILE CA C 61.5 0.5 1 619 . 128 ILE CB C 38.6 0.5 1 620 . 128 ILE C C 176.3 0.1 1 621 . 129 LYS N N 126.8 0.2 1 622 . 129 LYS H H 8.39 0.015 1 623 . 129 LYS CA C 56.0 0.5 1 624 . 129 LYS CB C 33.3 0.5 1 625 . 129 LYS C C 178.0 0.1 1 626 . 130 SER N N 118.9 0.2 1 627 . 130 SER H H 8.38 0.015 1 628 . 130 SER CA C 58.4 0.5 1 629 . 130 SER CB C 63.9 0.5 1 630 . 130 SER C C 174.4 0.1 1 631 . 131 ASP N N 123.1 0.2 1 632 . 131 ASP H H 8.30 0.015 1 633 . 131 ASP CA C 54.1 0.5 1 634 . 131 ASP CB C 41.1 0.5 1 635 . 131 ASP C C 176.9 0.1 1 636 . 132 GLY N N 110.4 0.2 1 637 . 132 GLY H H 8.36 0.015 1 638 . 132 GLY CA C 45.6 0.5 1 639 . 132 GLY C C 174.7 0.1 1 640 . 133 SER N N 117.4 0.2 1 641 . 133 SER H H 8.29 0.015 1 642 . 133 SER CA C 58.9 0.5 1 643 . 133 SER CB C 63.9 0.5 1 644 . 133 SER C C 175.2 0.1 1 645 . 134 GLY N N 111.5 0.2 1 646 . 134 GLY H H 8.41 0.015 1 647 . 134 GLY CA C 45.4 0.5 1 648 . 134 GLY C C 174.0 0.1 1 649 . 135 LYS N N 122.1 0.2 1 650 . 135 LYS H H 8.04 0.015 1 651 . 135 LYS CA C 56.1 0.5 1 652 . 135 LYS CB C 33.3 0.5 1 653 . 135 LYS C C 176.3 0.1 1 654 . 136 ALA N N 126.4 0.2 1 655 . 136 ALA H H 8.27 0.015 1 656 . 136 ALA CA C 52.5 0.5 1 657 . 136 ALA CB C 19.4 0.5 1 658 . 136 ALA C C 177.6 0.1 1 659 . 137 LYS N N 121.7 0.2 1 660 . 137 LYS H H 8.21 0.015 1 661 . 137 LYS CA C 56.4 0.5 1 662 . 137 LYS CB C 33.2 0.5 1 663 . 137 LYS C C 176.3 0.1 1 664 . 138 GLU N N 123.5 0.2 1 665 . 138 GLU H H 8.32 0.015 1 666 . 138 GLU CA C 56.4 0.5 1 667 . 138 GLU CB C 30.6 0.5 1 668 . 138 GLU C C 176.1 0.1 1 669 . 139 VAL N N 123.0 0.2 1 670 . 139 VAL H H 8.17 0.015 1 671 . 139 VAL CA C 62.1 0.5 1 672 . 139 VAL CB C 32.8 0.5 1 673 . 139 VAL C C 175.7 0.1 1 674 . 140 LEU N N 128.2 0.2 1 675 . 140 LEU H H 8.26 0.015 1 676 . 140 LEU CA C 55.1 0.5 1 677 . 140 LEU CB C 42.2 0.5 1 678 . 140 LEU C C 176.0 0.1 1 679 . 141 LYS N N 128.6 0.2 1 680 . 141 LYS H H 7.80 0.015 1 681 . 141 LYS CA C 57.5 0.5 1 682 . 141 LYS CB C 34.0 0.5 1 stop_ save_