data_25281 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR STRUCTURE OF YERSINIA PESTIS AIL (ATTACHMENT INVASION LOCUS) IN DECYLPHOSPHOCHOLINE MICELLES ; _BMRB_accession_number 25281 _BMRB_flat_file_name bmr25281.str _Entry_type original _Submission_date 2014-10-10 _Accession_date 2014-10-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'MEMBRANE PROTEIN STRUCTURES BY SOLUTION NMR' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ding Yi . . 2 Yao Yong . . 3 Fujimoto Lynn M. . 4 Marassi Francesca M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "13C chemical shifts" 280 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-07-20 original BMRB . stop_ _Original_release_date 2015-07-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Marassi Francesca M. . 2 Ding Yi . . 3 Schwieters C. D. . 4 Tian Y. . . 5 Yao Yong . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'YERSINIA PESTIS AIL (ATTACHMENT INVASION LOCUS)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ATTACHMENT_INVASION_LOCUS_PROTEIN _Molecular_mass 17492.549 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; EGESSISIGYAQSRVKEDGY KLDKNPRGFNLKYRYEFNND WGVIGSFAQTRRGFEESVDG FKLIDGDFKYYSVTAGPVFR INEYVSLYGLLGAGHGKAKF SSIFGQSESRSKTSLAYGAG LQFNPHPNFVIDASYEYSKL DDVKVGTWMLGAGYRF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLU 2 2 GLY 3 3 GLU 4 4 SER 5 5 SER 6 6 ILE 7 7 SER 8 8 ILE 9 9 GLY 10 10 TYR 11 11 ALA 12 12 GLN 13 13 SER 14 14 ARG 15 15 VAL 16 16 LYS 17 17 GLU 18 18 ASP 19 19 GLY 20 20 TYR 21 21 LYS 22 22 LEU 23 23 ASP 24 24 LYS 25 25 ASN 26 26 PRO 27 27 ARG 28 28 GLY 29 29 PHE 30 30 ASN 31 31 LEU 32 32 LYS 33 33 TYR 34 34 ARG 35 35 TYR 36 36 GLU 37 37 PHE 38 38 ASN 39 39 ASN 40 40 ASP 41 41 TRP 42 42 GLY 43 43 VAL 44 44 ILE 45 45 GLY 46 46 SER 47 47 PHE 48 48 ALA 49 49 GLN 50 50 THR 51 51 ARG 52 52 ARG 53 53 GLY 54 54 PHE 55 55 GLU 56 56 GLU 57 57 SER 58 58 VAL 59 59 ASP 60 60 GLY 61 61 PHE 62 62 LYS 63 63 LEU 64 64 ILE 65 65 ASP 66 66 GLY 67 67 ASP 68 68 PHE 69 69 LYS 70 70 TYR 71 71 TYR 72 72 SER 73 73 VAL 74 74 THR 75 75 ALA 76 76 GLY 77 77 PRO 78 78 VAL 79 79 PHE 80 80 ARG 81 81 ILE 82 82 ASN 83 83 GLU 84 84 TYR 85 85 VAL 86 86 SER 87 87 LEU 88 88 TYR 89 89 GLY 90 90 LEU 91 91 LEU 92 92 GLY 93 93 ALA 94 94 GLY 95 95 HIS 96 96 GLY 97 97 LYS 98 98 ALA 99 99 LYS 100 100 PHE 101 101 SER 102 102 SER 103 103 ILE 104 104 PHE 105 105 GLY 106 106 GLN 107 107 SER 108 108 GLU 109 109 SER 110 110 ARG 111 111 SER 112 112 LYS 113 113 THR 114 114 SER 115 115 LEU 116 116 ALA 117 117 TYR 118 118 GLY 119 119 ALA 120 120 GLY 121 121 LEU 122 122 GLN 123 123 PHE 124 124 ASN 125 125 PRO 126 126 HIS 127 127 PRO 128 128 ASN 129 129 PHE 130 130 VAL 131 131 ILE 132 132 ASP 133 133 ALA 134 134 SER 135 135 TYR 136 136 GLU 137 137 TYR 138 138 SER 139 139 LYS 140 140 LEU 141 141 ASP 142 142 ASP 143 143 VAL 144 144 LYS 145 145 VAL 146 146 GLY 147 147 THR 148 148 TRP 149 149 MET 150 150 LEU 151 151 GLY 152 152 ALA 153 153 GLY 154 154 TYR 155 155 ARG 156 156 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 2N2L "Nmr Structure Of Yersinia Pestis Ail (attachment Invasion Locus) In Decylphosphocholine Micelles Calculated With Implicit Membr" 100.00 156 100.00 100.00 1.39e-107 PDB 2N2M "Nmr Structure Of Yersinia Pestis Ail (attachment Invasion Locus) In Decylphosphocholine Micelles" 100.00 156 100.00 100.00 1.39e-107 PDB 3QRA "The Crystal Structure Of Ail, The Attachment Invasion Locus Protein Of Yersinia Pestis" 100.00 157 100.00 100.00 1.30e-107 PDB 3QRC "The Crystal Structure Of Ail, The Attachment Invasion Locus Protein Of Yersinia Pestis, In Complex With The Heparin Analogue Su" 100.00 157 100.00 100.00 1.30e-107 DBJ GAE10604 "hypothetical protein YP1_012_00180 [Yersinia pseudotuberculosis NBRC 105692]" 100.00 179 99.36 99.36 1.66e-107 EMBL CAH22105 "attachment invasion locus protein [Yersinia pseudotuberculosis IP 32953]" 100.00 182 99.36 99.36 1.99e-107 EMBL CAL21516 "attachment invasion locus protein [Yersinia pestis CO92]" 100.00 182 100.00 100.00 2.94e-108 EMBL CCC18813 "attachment-invasion locus protein precursor [Yersinia pseudotuberculosis]" 100.00 179 99.36 99.36 1.66e-107 EMBL CFQ79902 "attachment invasion locus protein [Yersinia pseudotuberculosis]" 100.00 179 100.00 100.00 3.13e-108 EMBL CFU96389 "attachment invasion locus protein [Yersinia pseudotuberculosis]" 100.00 179 99.36 99.36 1.66e-107 GB AAB36601 "ail [Yersinia pseudotuberculosis]" 100.00 182 98.72 99.36 1.14e-106 GB AAM84897 "outer membrane protein X [Yersinia pestis KIM10+]" 100.00 194 100.00 100.00 2.48e-108 GB AAS62746 "attachment invasion locus protein [Yersinia pestis biovar Microtus str. 91001]" 100.00 182 98.08 98.08 3.30e-105 GB ABG14310 "attachment invasion locus protein [Yersinia pestis Antiqua]" 100.00 182 100.00 100.00 2.94e-108 GB ABG17563 "attachment invasion locus protein [Yersinia pestis Nepal516]" 100.00 182 99.36 99.36 1.64e-107 REF WP_002222198 "MULTISPECIES: attachment protein [Yersinia]" 100.00 179 100.00 100.00 3.13e-108 REF WP_002227864 "attachment invasion locus protein [Yersinia pestis]" 100.00 182 100.00 100.00 2.94e-108 REF WP_012104793 "MULTISPECIES: attachment protein [Yersinia pseudotuberculosis complex]" 100.00 179 99.36 99.36 1.66e-107 REF WP_012229027 "attachment protein [Yersinia pestis]" 100.00 179 97.44 98.08 4.28e-105 REF WP_012303842 "attachment protein [Yersinia pseudotuberculosis]" 100.00 179 98.72 99.36 8.20e-107 SP Q56957 "RecName: Full=Attachment invasion locus protein; Flags: Precursor" 100.00 182 99.36 99.36 1.99e-107 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 $entity enterobacteria 187410 Bacteria . Yersinia pestis KIM10+ y1324 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 $entity 'recombinant technology' . Escherichia coli BL21(DE3) pET-30b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-13C; U-15N]' 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 5 mM 'natural abundance' decylphosphocholine 170 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version 2.36 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version TALOS+ loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'chemical shift calculation' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_WhatIF _Saveframe_category software _Name WhatIF _Version . loop_ _Vendor _Address _Electronic_address Vriend . . stop_ loop_ _Task 'structure validation' stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task 'structure validation' stop_ _Details . save_ save_MolProbity _Saveframe_category software _Name MolProbity _Version . loop_ _Vendor _Address _Electronic_address 'Chen, Arendall, Headd, Keedy, Immormino, Kapral, Murray, Richardson and Richardson' . . stop_ loop_ _Task 'structure validation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.8 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 GLY H H 8.46 . . 2 2 2 GLY CA C 44.83 . . 3 2 2 GLY N N 112.28 . . 4 3 3 GLU H H 7.63 . . 5 3 3 GLU CA C 56.84 . . 6 3 3 GLU CB C 29.98 . . 7 3 3 GLU N N 118.46 . . 8 4 4 SER H H 8.82 . . 9 4 4 SER CA C 57.28 . . 10 4 4 SER CB C 65.86 . . 11 4 4 SER N N 119.00 . . 12 5 5 SER H H 8.70 . . 13 5 5 SER CA C 57.56 . . 14 5 5 SER CB C 65.48 . . 15 5 5 SER N N 118.30 . . 16 6 6 ILE H H 9.08 . . 17 6 6 ILE CA C 54.11 . . 18 6 6 ILE CB C 33.87 . . 19 6 6 ILE N N 123.24 . . 20 7 7 SER H H 8.57 . . 21 7 7 SER CA C 57.13 . . 22 7 7 SER CB C 65.71 . . 23 7 7 SER N N 116.10 . . 24 8 8 ILE H H 8.30 . . 25 8 8 ILE CA C 58.46 . . 26 8 8 ILE CB C 40.88 . . 27 8 8 ILE N N 114.14 . . 28 9 9 GLY H H 9.06 . . 29 9 9 GLY CA C 45.55 . . 30 9 9 GLY N N 109.20 . . 31 10 10 TYR H H 8.87 . . 32 10 10 TYR CA C 56.97 . . 33 10 10 TYR CB C 41.52 . . 34 10 10 TYR N N 121.41 . . 35 11 11 ALA H H 7.21 . . 36 11 11 ALA CA C 48.74 . . 37 11 11 ALA CB C 21.61 . . 38 11 11 ALA N N 125.25 . . 39 12 12 GLN H H 8.33 . . 40 12 12 GLN CA C 54.69 . . 41 12 12 GLN CB C 32.00 . . 42 12 12 GLN N N 119.18 . . 43 13 13 SER H H 8.61 . . 44 13 13 SER CA C 57.78 . . 45 13 13 SER CB C 64.54 . . 46 13 13 SER N N 122.79 . . 47 14 14 ARG H H 8.52 . . 48 14 14 ARG CA C 54.96 . . 49 14 14 ARG CB C 32.37 . . 50 14 14 ARG N N 121.14 . . 51 15 15 VAL H H 8.44 . . 52 15 15 VAL CA C 60.97 . . 53 15 15 VAL CB C 34.32 . . 54 15 15 VAL N N 115.89 . . 55 16 16 LYS H H 8.85 . . 56 16 16 LYS CA C 55.12 . . 57 16 16 LYS CB C 34.35 . . 58 16 16 LYS N N 126.01 . . 59 17 17 GLU H H 8.03 . . 60 17 17 GLU CA C 54.46 . . 61 17 17 GLU CB C 33.43 . . 62 17 17 GLU N N 119.14 . . 63 18 18 ASP H H 8.12 . . 64 18 18 ASP CA C 56.50 . . 65 18 18 ASP CB C 33.78 . . 66 18 18 ASP N N 120.28 . . 67 19 19 GLY H H 8.43 . . 68 19 19 GLY CA C 44.13 . . 69 19 19 GLY N N 118.75 . . 70 20 20 TYR H H 8.61 . . 71 20 20 TYR CA C 60.94 . . 72 20 20 TYR CB C 42.01 . . 73 20 20 TYR N N 117.08 . . 74 21 21 LYS H H 7.97 . . 75 21 21 LYS CA C 56.76 . . 76 21 21 LYS CB C 29.10 . . 77 21 21 LYS N N 127.24 . . 78 22 22 LEU H H 8.37 . . 79 22 22 LEU CA C 59.17 . . 80 22 22 LEU CB C 40.03 . . 81 22 22 LEU N N 122.27 . . 82 23 23 ASP H H 8.21 . . 83 23 23 ASP CA C 51.84 . . 84 23 23 ASP CB C 37.73 . . 85 23 23 ASP N N 114.79 . . 86 24 24 LYS H H 9.23 . . 87 24 24 LYS CA C 58.86 . . 88 24 24 LYS CB C 28.33 . . 89 24 24 LYS N N 115.47 . . 90 25 25 ASN H H 8.15 . . 91 25 25 ASN CA C 54.43 . . 92 25 25 ASN CB C 42.50 . . 93 25 25 ASN N N 121.61 . . 94 26 26 PRO CA C 63.34 . . 95 26 26 PRO CB C 30.94 . . 96 27 27 ARG H H 8.29 . . 97 27 27 ARG CA C 54.34 . . 98 27 27 ARG CB C 33.50 . . 99 27 27 ARG N N 120.73 . . 100 28 28 GLY H H 8.81 . . 101 28 28 GLY CA C 46.94 . . 102 28 28 GLY N N 112.00 . . 103 29 29 PHE H H 8.47 . . 104 29 29 PHE CA C 55.23 . . 105 29 29 PHE CB C 43.70 . . 106 29 29 PHE N N 121.23 . . 107 30 30 ASN H H 8.63 . . 108 30 30 ASN CA C 50.22 . . 109 30 30 ASN CB C 45.81 . . 110 30 30 ASN N N 117.25 . . 111 31 31 LEU H H 9.08 . . 112 31 31 LEU CA C 53.93 . . 113 31 31 LEU CB C 45.81 . . 114 31 31 LEU N N 128.18 . . 115 32 32 LYS H H 8.78 . . 116 32 32 LYS CA C 55.73 . . 117 32 32 LYS CB C 36.07 . . 118 32 32 LYS N N 119.98 . . 119 33 33 TYR H H 8.64 . . 120 33 33 TYR CA C 55.83 . . 121 33 33 TYR CB C 42.11 . . 122 33 33 TYR N N 121.50 . . 123 34 34 ARG H H 8.83 . . 124 34 34 ARG CA C 52.69 . . 125 34 34 ARG CB C 34.32 . . 126 34 34 ARG N N 128.98 . . 127 35 35 TYR H H 8.84 . . 128 35 35 TYR CA C 56.64 . . 129 35 35 TYR CB C 41.98 . . 130 35 35 TYR N N 124.82 . . 131 39 39 ASN H H 7.99 . . 132 39 39 ASN CA C 54.85 . . 133 39 39 ASN CB C 38.29 . . 134 39 39 ASN N N 127.69 . . 135 40 40 ASP H H 8.37 . . 136 40 40 ASP CA C 55.21 . . 137 40 40 ASP CB C 44.01 . . 138 40 40 ASP N N 115.20 . . 139 41 41 TRP H H 9.13 . . 140 41 41 TRP CA C 55.84 . . 141 41 41 TRP CB C 33.54 . . 142 41 41 TRP N N 124.21 . . 143 42 42 GLY H H 8.61 . . 144 42 42 GLY CA C 45.87 . . 145 42 42 GLY N N 107.80 . . 146 43 43 VAL H H 8.88 . . 147 43 43 VAL CA C 58.98 . . 148 43 43 VAL CB C 35.43 . . 149 43 43 VAL N N 116.26 . . 150 44 44 ILE H H 9.11 . . 151 44 44 ILE CA C 58.39 . . 152 44 44 ILE CB C 42.89 . . 153 44 44 ILE N N 124.72 . . 154 45 45 GLY H H 8.91 . . 155 45 45 GLY CA C 43.15 . . 156 45 45 GLY N N 110.61 . . 157 46 46 SER H H 9.25 . . 158 46 46 SER CA C 56.25 . . 159 46 46 SER CB C 63.72 . . 160 46 46 SER N N 116.21 . . 161 47 47 PHE H H 8.94 . . 162 47 47 PHE CA C 55.09 . . 163 47 47 PHE CB C 42.56 . . 164 47 47 PHE N N 126.40 . . 165 48 48 ALA H H 8.79 . . 166 48 48 ALA CA C 50.35 . . 167 48 48 ALA CB C 21.28 . . 168 48 48 ALA N N 131.93 . . 169 49 49 GLN H H 7.72 . . 170 49 49 GLN CA C 54.11 . . 171 49 49 GLN CB C 31.14 . . 172 49 49 GLN N N 116.07 . . 173 50 50 THR H H 9.47 . . 174 50 50 THR CA C 59.27 . . 175 50 50 THR CB C 70.98 . . 176 50 50 THR N N 115.99 . . 177 51 51 ARG H H 8.60 . . 178 51 51 ARG CA C 55.35 . . 179 51 51 ARG CB C 33.61 . . 180 51 51 ARG N N 117.60 . . 181 52 52 ARG H H 8.38 . . 182 52 52 ARG CA C 56.91 . . 183 52 52 ARG CB C 29.37 . . 184 52 52 ARG N N 121.40 . . 185 53 53 GLY H H 8.33 . . 186 53 53 GLY CA C 45.19 . . 187 53 53 GLY N N 111.04 . . 188 54 54 PHE H H 7.72 . . 189 54 54 PHE CA C 55.67 . . 190 54 54 PHE CB C 29.22 . . 191 54 54 PHE N N 119.21 . . 192 55 55 GLU H H 8.40 . . 193 55 55 GLU CA C 55.58 . . 194 55 55 GLU CB C 32.92 . . 195 55 55 GLU N N 123.47 . . 196 56 56 GLU H H 8.50 . . 197 56 56 GLU CA C 56.69 . . 198 56 56 GLU CB C 29.45 . . 199 56 56 GLU N N 121.95 . . 200 57 57 SER H H 8.64 . . 201 57 57 SER CA C 55.09 . . 202 57 57 SER CB C 64.89 . . 203 57 57 SER N N 123.33 . . 204 58 58 VAL H H 8.48 . . 205 58 58 VAL CA C 57.66 . . 206 58 58 VAL CB C 31.64 . . 207 58 58 VAL N N 122.06 . . 208 59 59 ASP H H 9.36 . . 209 59 59 ASP CA C 54.96 . . 210 59 59 ASP CB C 42.84 . . 211 59 59 ASP N N 123.39 . . 212 60 60 GLY H H 8.21 . . 213 60 60 GLY CA C 45.13 . . 214 60 60 GLY N N 105.23 . . 215 61 61 PHE H H 8.33 . . 216 61 61 PHE CA C 57.33 . . 217 61 61 PHE CB C 39.42 . . 218 61 61 PHE N N 121.44 . . 219 62 62 LYS H H 8.48 . . 220 62 62 LYS CA C 56.34 . . 221 62 62 LYS CB C 33.85 . . 222 62 62 LYS N N 119.87 . . 223 63 63 LEU H H 8.91 . . 224 63 63 LEU CA C 56.22 . . 225 63 63 LEU CB C 41.52 . . 226 63 63 LEU N N 125.16 . . 227 64 64 ILE H H 8.21 . . 228 64 64 ILE CA C 62.42 . . 229 64 64 ILE CB C 37.70 . . 230 64 64 ILE N N 119.66 . . 231 65 65 ASP H H 7.71 . . 232 65 65 ASP CA C 57.42 . . 233 65 65 ASP CB C 38.35 . . 234 65 65 ASP N N 117.08 . . 235 66 66 GLY H H 7.92 . . 236 66 66 GLY CA C 45.17 . . 237 66 66 GLY N N 106.44 . . 238 67 67 ASP H H 7.82 . . 239 67 67 ASP CA C 57.34 . . 240 67 67 ASP CB C 29.87 . . 241 67 67 ASP N N 118.49 . . 242 68 68 PHE H H 8.31 . . 243 68 68 PHE CA C 56.09 . . 244 68 68 PHE CB C 41.94 . . 245 68 68 PHE N N 125.32 . . 246 69 69 LYS H H 8.73 . . 247 69 69 LYS CA C 54.88 . . 248 69 69 LYS CB C 36.92 . . 249 69 69 LYS N N 124.77 . . 250 70 70 TYR H H 8.68 . . 251 70 70 TYR CA C 55.54 . . 252 70 70 TYR CB C 40.15 . . 253 70 70 TYR N N 123.74 . . 254 71 71 TYR H H 8.62 . . 255 71 71 TYR CA C 54.50 . . 256 71 71 TYR CB C 42.42 . . 257 71 71 TYR N N 123.92 . . 258 72 72 SER H H 8.80 . . 259 72 72 SER CA C 56.32 . . 260 72 72 SER CB C 65.79 . . 261 72 72 SER N N 113.82 . . 262 73 73 VAL H H 8.17 . . 263 73 73 VAL CA C 60.73 . . 264 73 73 VAL CB C 33.87 . . 265 73 73 VAL N N 119.26 . . 266 74 74 THR H H 9.20 . . 267 74 74 THR CA C 59.04 . . 268 74 74 THR CB C 73.25 . . 269 74 74 THR N N 115.36 . . 270 75 75 ALA H H 9.13 . . 271 75 75 ALA CA C 51.39 . . 272 75 75 ALA CB C 22.38 . . 273 75 75 ALA N N 119.33 . . 274 76 76 GLY H H 8.76 . . 275 76 76 GLY CA C 45.90 . . 276 76 76 GLY N N 103.13 . . 277 77 77 PRO CA C 61.25 . . 278 77 77 PRO CB C 32.59 . . 279 78 78 VAL H H 8.24 . . 280 78 78 VAL CA C 58.43 . . 281 78 78 VAL CB C 32.70 . . 282 78 78 VAL N N 115.25 . . 283 79 79 PHE H H 9.54 . . 284 79 79 PHE CA C 55.09 . . 285 79 79 PHE CB C 41.59 . . 286 79 79 PHE N N 130.61 . . 287 80 80 ARG H H 8.81 . . 288 80 80 ARG CA C 55.49 . . 289 80 80 ARG CB C 29.52 . . 290 80 80 ARG N N 130.35 . . 291 81 81 ILE H H 8.26 . . 292 81 81 ILE CA C 62.85 . . 293 81 81 ILE CB C 37.65 . . 294 81 81 ILE N N 127.48 . . 295 82 82 ASN H H 7.97 . . 296 82 82 ASN CA C 55.63 . . 297 82 82 ASN CB C 43.21 . . 298 82 82 ASN N N 113.11 . . 299 85 85 VAL H H 7.84 . . 300 85 85 VAL CA C 61.12 . . 301 85 85 VAL CB C 34.91 . . 302 85 85 VAL N N 118.09 . . 303 86 86 SER H H 8.24 . . 304 86 86 SER CA C 57.10 . . 305 86 86 SER CB C 65.40 . . 306 86 86 SER N N 119.05 . . 307 87 87 LEU H H 9.13 . . 308 87 87 LEU CA C 53.75 . . 309 87 87 LEU CB C 46.32 . . 310 87 87 LEU N N 124.64 . . 311 88 88 TYR H H 8.74 . . 312 88 88 TYR CA C 55.08 . . 313 88 88 TYR CB C 42.63 . . 314 88 88 TYR N N 118.74 . . 315 89 89 GLY H H 7.72 . . 316 89 89 GLY CA C 43.25 . . 317 89 89 GLY N N 103.92 . . 318 90 90 LEU H H 8.52 . . 319 90 90 LEU CA C 53.20 . . 320 90 90 LEU CB C 45.81 . . 321 90 90 LEU N N 117.53 . . 322 91 91 LEU H H 9.25 . . 323 91 91 LEU CA C 53.59 . . 324 91 91 LEU CB C 46.33 . . 325 91 91 LEU N N 120.67 . . 326 92 92 GLY H H 8.48 . . 327 92 92 GLY CA C 46.52 . . 328 92 92 GLY N N 108.77 . . 329 93 93 ALA H H 8.86 . . 330 93 93 ALA CA C 49.89 . . 331 93 93 ALA CB C 21.86 . . 332 93 93 ALA N N 126.76 . . 333 94 94 GLY H H 8.88 . . 334 94 94 GLY CA C 42.76 . . 335 94 94 GLY N N 107.51 . . 336 95 95 HIS H H 9.20 . . 337 95 95 HIS CA C 54.57 . . 338 95 95 HIS CB C 32.70 . . 339 95 95 HIS N N 122.34 . . 340 96 96 GLY H H 8.62 . . 341 96 96 GLY CA C 43.15 . . 342 96 96 GLY N N 112.17 . . 343 97 97 LYS H H 9.01 . . 344 97 97 LYS CA C 54.89 . . 345 97 97 LYS CB C 35.56 . . 346 97 97 LYS N N 120.58 . . 347 98 98 ALA H H 9.12 . . 348 98 98 ALA CA C 50.02 . . 349 98 98 ALA CB C 22.38 . . 350 98 98 ALA N N 126.74 . . 351 99 99 LYS H H 8.58 . . 352 99 99 LYS CA C 55.09 . . 353 99 99 LYS CB C 34.97 . . 354 99 99 LYS N N 122.36 . . 355 100 100 PHE H H 8.75 . . 356 100 100 PHE CA C 56.39 . . 357 100 100 PHE CB C 42.11 . . 358 100 100 PHE N N 121.17 . . 359 101 101 SER H H 8.99 . . 360 101 101 SER CA C 57.07 . . 361 101 101 SER CB C 65.83 . . 362 101 101 SER N N 117.28 . . 363 102 102 SER H H 8.68 . . 364 102 102 SER CA C 56.50 . . 365 102 102 SER CB C 67.54 . . 366 102 102 SER N N 117.60 . . 367 103 103 ILE H H 7.70 . . 368 103 103 ILE CA C 59.18 . . 369 103 103 ILE CB C 40.55 . . 370 103 103 ILE N N 114.98 . . 371 104 104 PHE H H 8.59 . . 372 104 104 PHE CA C 53.19 . . 373 104 104 PHE CB C 43.90 . . 374 104 104 PHE N N 123.71 . . 375 105 105 GLY H H 8.40 . . 376 105 105 GLY CA C 45.42 . . 377 105 105 GLY N N 109.08 . . 378 106 106 GLN H H 8.53 . . 379 106 106 GLN CA C 53.72 . . 380 106 106 GLN CB C 30.10 . . 381 106 106 GLN N N 119.68 . . 382 107 107 SER H H 8.80 . . 383 107 107 SER CA C 57.36 . . 384 107 107 SER CB C 66.05 . . 385 107 107 SER N N 119.16 . . 386 108 108 GLU H H 8.96 . . 387 108 108 GLU CA C 58.91 . . 388 108 108 GLU CB C 40.88 . . 389 108 108 GLU N N 125.36 . . 390 109 109 SER H H 9.08 . . 391 109 109 SER CA C 56.71 . . 392 109 109 SER CB C 66.18 . . 393 109 109 SER N N 118.89 . . 394 110 110 ARG H H 8.85 . . 395 110 110 ARG CA C 58.39 . . 396 110 110 ARG CB C 40.94 . . 397 110 110 ARG N N 119.83 . . 398 111 111 SER H H 8.74 . . 399 111 111 SER CA C 57.29 . . 400 111 111 SER CB C 66.11 . . 401 111 111 SER N N 114.87 . . 402 112 112 LYS H H 8.52 . . 403 112 112 LYS CA C 55.15 . . 404 112 112 LYS CB C 36.33 . . 405 112 112 LYS N N 120.87 . . 406 113 113 THR H H 8.44 . . 407 113 113 THR CA C 61.25 . . 408 113 113 THR CB C 70.01 . . 409 113 113 THR N N 121.39 . . 410 114 114 SER H H 9.35 . . 411 114 114 SER CA C 56.19 . . 412 114 114 SER CB C 66.38 . . 413 114 114 SER N N 120.73 . . 414 115 115 LEU H H 8.20 . . 415 115 115 LEU CA C 55.48 . . 416 115 115 LEU CB C 42.89 . . 417 115 115 LEU N N 121.54 . . 418 116 116 ALA H H 8.60 . . 419 116 116 ALA CA C 49.96 . . 420 116 116 ALA CB C 20.31 . . 421 116 116 ALA N N 129.06 . . 422 117 117 TYR H H 8.45 . . 423 117 117 TYR CA C 55.15 . . 424 117 117 TYR CB C 41.20 . . 425 117 117 TYR N N 115.89 . . 426 118 118 GLY H H 9.34 . . 427 118 118 GLY CA C 45.94 . . 428 118 118 GLY N N 107.33 . . 429 119 119 ALA H H 8.77 . . 430 119 119 ALA CA C 51.32 . . 431 119 119 ALA CB C 22.12 . . 432 119 119 ALA N N 118.88 . . 433 120 120 GLY H H 7.94 . . 434 120 120 GLY CA C 45.65 . . 435 120 120 GLY N N 105.73 . . 436 121 121 LEU H H 9.01 . . 437 121 121 LEU CA C 52.98 . . 438 121 121 LEU CB C 46.46 . . 439 121 121 LEU N N 115.48 . . 440 122 122 GLN H H 8.09 . . 441 122 122 GLN CA C 54.78 . . 442 122 122 GLN CB C 31.40 . . 443 122 122 GLN N N 112.53 . . 444 123 123 PHE H H 10.02 . . 445 123 123 PHE CA C 54.18 . . 446 123 123 PHE CB C 42.56 . . 447 123 123 PHE N N 126.05 . . 448 124 124 ASN H H 9.52 . . 449 124 124 ASN CA C 50.94 . . 450 124 124 ASN CB C 40.36 . . 451 124 124 ASN N N 121.91 . . 452 125 125 PRO CA C 63.39 . . 453 125 125 PRO CB C 31.21 . . 454 126 126 HIS H H 7.63 . . 455 126 126 HIS CA C 54.11 . . 456 126 126 HIS CB C 34.91 . . 457 126 126 HIS N N 116.83 . . 458 127 127 PRO CA C 65.37 . . 459 127 127 PRO CB C 31.03 . . 460 128 128 ASN H H 10.46 . . 461 128 128 ASN CA C 53.99 . . 462 128 128 ASN CB C 40.55 . . 463 128 128 ASN N N 114.68 . . 464 129 129 PHE H H 8.34 . . 465 129 129 PHE CA C 56.53 . . 466 129 129 PHE CB C 44.31 . . 467 129 129 PHE N N 119.63 . . 468 130 130 VAL H H 7.82 . . 469 130 130 VAL CA C 60.34 . . 470 130 130 VAL CB C 34.97 . . 471 130 130 VAL N N 123.00 . . 472 131 131 ILE H H 8.83 . . 473 131 131 ILE CA C 60.21 . . 474 131 131 ILE CB C 39.51 . . 475 131 131 ILE N N 124.47 . . 476 132 132 ASP H H 9.04 . . 477 132 132 ASP CA C 53.53 . . 478 132 132 ASP CB C 47.62 . . 479 132 132 ASP N N 130.70 . . 480 133 133 ALA H H 8.80 . . 481 133 133 ALA CA C 51.39 . . 482 133 133 ALA CB C 21.73 . . 483 133 133 ALA N N 126.90 . . 484 134 134 SER H H 9.16 . . 485 134 134 SER CA C 58.14 . . 486 134 134 SER CB C 67.02 . . 487 134 134 SER N N 113.76 . . 488 135 135 TYR H H 8.82 . . 489 135 135 TYR CA C 55.69 . . 490 135 135 TYR CB C 43.15 . . 491 135 135 TYR N N 118.50 . . 492 136 136 GLU H H 8.38 . . 493 136 136 GLU CA C 53.53 . . 494 136 136 GLU CB C 34.45 . . 495 136 136 GLU N N 126.29 . . 496 137 137 TYR H H 9.30 . . 497 137 137 TYR CA C 55.67 . . 498 137 137 TYR CB C 43.15 . . 499 137 137 TYR N N 123.63 . . 500 138 138 SER H H 7.98 . . 501 138 138 SER CA C 58.27 . . 502 138 138 SER CB C 67.09 . . 503 138 138 SER N N 118.30 . . 504 139 139 LYS H H 8.63 . . 505 139 139 LYS CA C 55.16 . . 506 139 139 LYS CB C 32.64 . . 507 139 139 LYS N N 127.45 . . 508 140 140 LEU H H 9.06 . . 509 140 140 LEU CA C 52.50 . . 510 140 140 LEU CB C 40.00 . . 511 140 140 LEU N N 129.65 . . 512 141 141 ASP H H 8.59 . . 513 141 141 ASP CA C 57.19 . . 514 141 141 ASP CB C 39.73 . . 515 141 141 ASP N N 121.47 . . 516 142 142 ASP H H 8.43 . . 517 142 142 ASP CA C 55.18 . . 518 142 142 ASP CB C 41.09 . . 519 142 142 ASP N N 121.51 . . 520 143 143 VAL H H 8.02 . . 521 143 143 VAL CA C 62.24 . . 522 143 143 VAL CB C 31.28 . . 523 143 143 VAL N N 121.42 . . 524 144 144 LYS H H 8.66 . . 525 144 144 LYS CA C 55.44 . . 526 144 144 LYS CB C 32.64 . . 527 144 144 LYS N N 127.95 . . 528 145 145 VAL H H 8.72 . . 529 145 145 VAL CA C 55.91 . . 530 145 145 VAL CB C 32.57 . . 531 145 145 VAL N N 124.12 . . 532 146 146 GLY H H 8.40 . . 533 146 146 GLY CA C 44.08 . . 534 146 146 GLY N N 116.24 . . 535 147 147 THR H H 9.08 . . 536 147 147 THR CA C 61.45 . . 537 147 147 THR CB C 70.26 . . 538 147 147 THR N N 124.62 . . 539 148 148 TRP H H 8.51 . . 540 148 148 TRP CA C 54.77 . . 541 148 148 TRP CB C 33.09 . . 542 148 148 TRP N N 124.79 . . 543 149 149 MET H H 9.15 . . 544 149 149 MET CA C 54.54 . . 545 149 149 MET CB C 34.64 . . 546 149 149 MET N N 118.88 . . 547 150 150 LEU H H 8.48 . . 548 150 150 LEU CA C 54.10 . . 549 150 150 LEU CB C 45.80 . . 550 150 150 LEU N N 122.83 . . 551 151 151 GLY H H 9.82 . . 552 151 151 GLY CA C 45.94 . . 553 151 151 GLY N N 112.73 . . 554 152 152 ALA H H 8.84 . . 555 152 152 ALA CA C 49.76 . . 556 152 152 ALA CB C 22.70 . . 557 152 152 ALA N N 119.46 . . 558 153 153 GLY H H 8.54 . . 559 153 153 GLY CA C 46.44 . . 560 153 153 GLY N N 104.36 . . 561 154 154 TYR H H 8.31 . . 562 154 154 TYR CA C 55.37 . . 563 154 154 TYR CB C 44.25 . . 564 154 154 TYR N N 120.68 . . 565 155 155 ARG H H 7.64 . . 566 155 155 ARG CA C 53.48 . . 567 155 155 ARG CB C 32.16 . . 568 155 155 ARG N N 127.05 . . 569 156 156 PHE H H 8.77 . . 570 156 156 PHE CA C 57.97 . . 571 156 156 PHE CB C 39.90 . . 572 156 156 PHE N N 127.48 . . stop_ save_