data_15206 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Differences in the electrostatic surfaces of the type III secretion needle proteins ; _BMRB_accession_number 15206 _BMRB_flat_file_name bmr15206.str _Entry_type original _Submission_date 2007-04-06 _Accession_date 2007-04-06 _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 Wang Yu . . 2 Ouellette Andrew N. . 3 Egan Chet W. . 4 'De Guzman' Roberto N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 383 "13C chemical shifts" 297 "15N chemical shifts" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-26 update BMRB 'update entity name' 2007-10-24 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17617421 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Yu . . 2 Ouellette Andrew N. . 3 Egana Chet W. . 4 Rathinavelana Thenmalarchelvi . . 5 Ima Wonpil . . 6 'De Guzman' Roberto N. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 371 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1304 _Page_last 1314 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Needle Monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'needle monomer' $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 'needle monomer' _Molecular_mass 9279.383 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; MATPWSGYLDDVSAKFDTGV DNLQTQVTEALDKLAAKPSD PALLAAYQSKLSEYNLYRNA QSNTVKVFKDIDAAILEHHH HHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 PRO 5 TRP 6 SER 7 GLY 8 TYR 9 LEU 10 ASP 11 ASP 12 VAL 13 SER 14 ALA 15 LYS 16 PHE 17 ASP 18 THR 19 GLY 20 VAL 21 ASP 22 ASN 23 LEU 24 GLN 25 THR 26 GLN 27 VAL 28 THR 29 GLU 30 ALA 31 LEU 32 ASP 33 LYS 34 LEU 35 ALA 36 ALA 37 LYS 38 PRO 39 SER 40 ASP 41 PRO 42 ALA 43 LEU 44 LEU 45 ALA 46 ALA 47 TYR 48 GLN 49 SER 50 LYS 51 LEU 52 SER 53 GLU 54 TYR 55 ASN 56 LEU 57 TYR 58 ARG 59 ASN 60 ALA 61 GLN 62 SER 63 ASN 64 THR 65 VAL 66 LYS 67 VAL 68 PHE 69 LYS 70 ASP 71 ILE 72 ASP 73 ALA 74 ALA 75 ILE 76 LEU 77 GLU 78 HIS 79 HIS 80 HIS 81 HIS 82 HIS 83 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 2JOW "Differences In The Electrostatic Surfaces Of The Type Iii Secretion Needle Proteins" 100.00 83 100.00 100.00 1.07e-52 GB AHS51581 "type III secretion system needle complex protein PrgI, partial [Salmonella enterica subsp. enterica serovar Enteritidis str. EC" 91.57 76 98.68 100.00 2.68e-46 GB ERF90330 "type III secretion system needle complex protein PrgI [Salmonella enterica subsp. enterica serovar Heidelberg str. SARA33]" 92.77 83 97.40 100.00 1.10e-46 GB ERG01985 "type III secretion system needle complex protein PrgI [Salmonella enterica subsp. enterica serovar Muenchen str. RKS4129]" 92.77 83 97.40 100.00 1.10e-46 GB KLT33237 "type III secretion system needle complex protein PrgI [Salmonella enterica subsp. enterica serovar Typhimurium]" 92.77 83 97.40 100.00 1.10e-46 GB KMJ71568 "type III secretion system needle complex protein PrgI [Salmonella enterica subsp. enterica serovar Typhimurium]" 92.77 83 97.40 100.00 1.10e-46 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'Salmonella typhimurium' 602 Bacteria . Salmonella typhimurium 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 . pET22b 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 $entity 0.8 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version . loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _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' 70 . mM pH 6.0 . pH pressure 1 . atm temperature 298 . 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 protons ppm 0 external indirect . . . 0.251449530 DSS H 1 protons ppm 0 external indirect . . . 1 DSS N 15 protons ppm 0 external 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 HNCO' '3D CBCA(CO)NH' '3D HNCACB' '3D HBHA(CO)NH' '3D 1H-15N NOESY' '3D 1H-13C NOESY' 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 'needle 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 2 2 ALA HA H 4.113 . 1 2 2 2 ALA HB H 1.464 . 1 3 2 2 ALA CA C 51.484 . 1 4 2 2 ALA CB C 19.395 . 1 5 3 3 THR HA H 4.545 . 1 6 3 3 THR HB H 3.936 . 1 7 3 3 THR HG2 H 1.174 . 1 8 3 3 THR CA C 59.673 . 1 9 3 3 THR CB C 69.530 . 1 10 3 3 THR CG2 C 21.437 . 1 11 4 4 PRO HA H 4.342 . 1 12 4 4 PRO HB2 H 2.177 . 2 13 4 4 PRO HB3 H 1.710 . 2 14 4 4 PRO HG2 H 1.860 . 1 15 4 4 PRO HG3 H 1.860 . 1 16 4 4 PRO HD2 H 3.729 . 2 17 4 4 PRO HD3 H 3.484 . 2 18 4 4 PRO C C 176.530 . 1 19 4 4 PRO CA C 63.437 . 1 20 4 4 PRO CB C 31.933 . 1 21 4 4 PRO CG C 27.271 . 1 22 4 4 PRO CD C 50.955 . 1 23 5 5 TRP H H 8.045 . 1 24 5 5 TRP HA H 4.637 . 1 25 5 5 TRP HB2 H 3.243 . 1 26 5 5 TRP HB3 H 3.243 . 1 27 5 5 TRP HE1 H 10.161 . 1 28 5 5 TRP C C 176.296 . 1 29 5 5 TRP CA C 57.425 . 1 30 5 5 TRP CB C 29.306 . 1 31 5 5 TRP N N 120.439 . 1 32 5 5 TRP NE1 N 129.886 . 1 33 6 6 SER H H 8.026 . 1 34 6 6 SER HA H 4.220 . 1 35 6 6 SER HB2 H 3.732 . 2 36 6 6 SER HB3 H 3.654 . 2 37 6 6 SER C C 174.474 . 1 38 6 6 SER CA C 58.576 . 1 39 6 6 SER CB C 63.844 . 1 40 6 6 SER N N 118.616 . 1 41 7 7 GLY H H 7.309 . 1 42 7 7 GLY HA2 H 3.651 . 2 43 7 7 GLY HA3 H 3.513 . 2 44 7 7 GLY C C 173.516 . 1 45 7 7 GLY CA C 45.133 . 1 46 7 7 GLY N N 109.694 . 1 47 8 8 TYR H H 7.804 . 1 48 8 8 TYR HA H 4.456 . 1 49 8 8 TYR HB2 H 2.963 . 2 50 8 8 TYR HB3 H 2.856 . 2 51 8 8 TYR C C 175.651 . 1 52 8 8 TYR CA C 58.093 . 1 53 8 8 TYR CB C 38.799 . 1 54 8 8 TYR N N 119.638 . 1 55 9 9 LEU H H 8.086 . 1 56 9 9 LEU HA H 4.219 . 1 57 9 9 LEU HB2 H 1.533 . 2 58 9 9 LEU HB3 H 1.479 . 2 59 9 9 LEU HG H 1.418 . 1 60 9 9 LEU HD1 H 0.770 . 2 61 9 9 LEU HD2 H 0.820 . 2 62 9 9 LEU C C 176.637 . 1 63 9 9 LEU CA C 55.099 . 1 64 9 9 LEU CB C 42.448 . 1 65 9 9 LEU CG C 26.688 . 1 66 9 9 LEU CD1 C 23.479 . 2 67 9 9 LEU CD2 C 24.937 . 2 68 9 9 LEU N N 123.369 . 1 69 10 10 ASP H H 8.060 . 1 70 10 10 ASP HA H 4.490 . 1 71 10 10 ASP HB2 H 2.653 . 2 72 10 10 ASP HB3 H 2.585 . 2 73 10 10 ASP C C 175.830 . 1 74 10 10 ASP CA C 54.404 . 1 75 10 10 ASP CB C 41.193 . 1 76 10 10 ASP N N 120.437 . 1 77 11 11 ASP H H 8.152 . 1 78 11 11 ASP HA H 4.554 . 1 79 11 11 ASP HB2 H 2.696 . 2 80 11 11 ASP HB3 H 2.629 . 2 81 11 11 ASP C C 176.864 . 1 82 11 11 ASP CA C 54.461 . 1 83 11 11 ASP CB C 41.161 . 1 84 11 11 ASP N N 120.253 . 1 85 12 12 VAL H H 8.079 . 1 86 12 12 VAL HA H 4.038 . 1 87 12 12 VAL HB H 2.153 . 1 88 12 12 VAL HG1 H 0.894 . 2 89 12 12 VAL C C 176.789 . 1 90 12 12 VAL CA C 63.107 . 1 91 12 12 VAL CB C 32.149 . 1 92 12 12 VAL CG1 C 20.416 . 2 93 12 12 VAL N N 119.947 . 1 94 13 13 SER H H 8.302 . 1 95 13 13 SER HA H 4.287 . 1 96 13 13 SER HB2 H 3.858 . 1 97 13 13 SER HB3 H 3.858 . 1 98 13 13 SER C C 174.648 . 1 99 13 13 SER CA C 59.278 . 1 100 13 13 SER CB C 61.477 . 1 101 13 13 SER N N 118.036 . 1 102 14 14 ALA H H 8.032 . 1 103 14 14 ALA HA H 4.223 . 1 104 14 14 ALA HB H 1.321 . 1 105 14 14 ALA C C 177.556 . 1 106 14 14 ALA CA C 52.751 . 1 107 14 14 ALA CB C 19.100 . 1 108 14 14 ALA N N 125.125 . 1 109 15 15 LYS H H 7.930 . 1 110 15 15 LYS HA H 4.184 . 1 111 15 15 LYS HB2 H 1.649 . 1 112 15 15 LYS HB3 H 1.649 . 1 113 15 15 LYS HG2 H 1.314 . 2 114 15 15 LYS HG3 H 1.250 . 2 115 15 15 LYS HD2 H 1.571 . 1 116 15 15 LYS HD3 H 1.571 . 1 117 15 15 LYS C C 176.442 . 1 118 15 15 LYS CA C 56.282 . 1 119 15 15 LYS CB C 33.012 . 1 120 15 15 LYS CG C 24.646 . 1 121 15 15 LYS CD C 28.875 . 1 122 15 15 LYS N N 119.409 . 1 123 16 16 PHE H H 8.104 . 1 124 16 16 PHE HA H 4.615 . 1 125 16 16 PHE HB2 H 3.132 . 2 126 16 16 PHE HB3 H 2.966 . 2 127 16 16 PHE C C 175.401 . 1 128 16 16 PHE CA C 57.662 . 1 129 16 16 PHE CB C 39.688 . 1 130 16 16 PHE N N 120.679 . 1 131 17 17 ASP H H 8.303 . 1 132 17 17 ASP HA H 4.632 . 1 133 17 17 ASP HB2 H 2.713 . 2 134 17 17 ASP HB3 H 2.623 . 2 135 17 17 ASP C C 176.485 . 1 136 17 17 ASP CA C 54.328 . 1 137 17 17 ASP CB C 41.396 . 1 138 17 17 ASP N N 121.968 . 1 139 18 18 THR H H 8.172 . 1 140 18 18 THR HA H 4.240 . 1 141 18 18 THR HB H 4.282 . 1 142 18 18 THR HG2 H 1.212 . 1 143 18 18 THR C C 175.533 . 1 144 18 18 THR CA C 62.619 . 1 145 18 18 THR CB C 69.531 . 1 146 18 18 THR CG2 C 21.583 . 1 147 18 18 THR N N 114.589 . 1 148 19 19 GLY H H 8.429 . 1 149 19 19 GLY HA2 H 3.959 . 2 150 19 19 GLY HA3 H 3.909 . 2 151 19 19 GLY C C 174.883 . 1 152 19 19 GLY CA C 45.788 . 1 153 19 19 GLY N N 110.979 . 1 154 20 20 VAL H H 7.989 . 1 155 20 20 VAL HA H 3.872 . 1 156 20 20 VAL HB H 2.061 . 1 157 20 20 VAL HG1 H 0.916 . 1 158 20 20 VAL HG2 H 0.916 . 1 159 20 20 VAL C C 176.249 . 1 160 20 20 VAL CA C 63.763 . 1 161 20 20 VAL CB C 32.353 . 1 162 20 20 VAL CG1 C 21.291 . 2 163 20 20 VAL N N 119.768 . 1 164 21 21 ASP H H 8.252 . 1 165 21 21 ASP HA H 4.510 . 1 166 21 21 ASP HB2 H 2.692 . 2 167 21 21 ASP HB3 H 2.623 . 2 168 21 21 ASP C C 177.092 . 1 169 21 21 ASP CA C 55.571 . 1 170 21 21 ASP CB C 41.055 . 1 171 21 21 ASP N N 122.290 . 1 172 22 22 ASN H H 8.256 . 1 173 22 22 ASN HA H 4.544 . 1 174 22 22 ASN HB2 H 2.815 . 2 175 22 22 ASN HB3 H 2.771 . 2 176 22 22 ASN C C 180.593 . 1 177 22 22 ASN CA C 54.800 . 1 178 22 22 ASN CB C 38.648 . 1 179 22 22 ASN N N 119.207 . 1 180 23 23 LEU H H 8.099 . 1 181 23 23 LEU HA H 4.044 . 1 182 23 23 LEU HB2 H 1.829 . 2 183 23 23 LEU HB3 H 1.462 . 2 184 23 23 LEU HG H 1.590 . 1 185 23 23 LEU HD1 H 0.745 . 2 186 23 23 LEU HD2 H 0.797 . 2 187 23 23 LEU C C 178.523 . 1 188 23 23 LEU CA C 57.754 . 1 189 23 23 LEU CB C 42.508 . 1 190 23 23 LEU CG C 27.563 . 1 191 23 23 LEU CD1 C 25.375 . 2 192 23 23 LEU CD2 C 23.771 . 2 193 23 23 LEU N N 121.230 . 1 194 24 24 GLN H H 8.481 . 1 195 24 24 GLN HA H 3.466 . 1 196 24 24 GLN HB2 H 2.153 . 1 197 24 24 GLN HB3 H 2.153 . 1 198 24 24 GLN HG2 H 2.178 . 1 199 24 24 GLN HG3 H 2.178 . 1 200 24 24 GLN C C 178.370 . 1 201 24 24 GLN CA C 59.244 . 1 202 24 24 GLN CB C 28.328 . 1 203 24 24 GLN CG C 34.126 . 1 204 24 24 GLN N N 119.770 . 1 205 25 25 THR H H 8.017 . 1 206 25 25 THR HA H 3.971 . 1 207 25 25 THR HB H 4.285 . 1 208 25 25 THR HG2 H 1.220 . 1 209 25 25 THR C C 176.111 . 1 210 25 25 THR CA C 65.870 . 1 211 25 25 THR CB C 68.549 . 1 212 25 25 THR CG2 C 21.678 . 1 213 25 25 THR N N 115.927 . 1 214 26 26 GLN H H 7.895 . 1 215 26 26 GLN HA H 4.133 . 1 216 26 26 GLN HB2 H 2.265 . 2 217 26 26 GLN HB3 H 1.989 . 2 218 26 26 GLN HG2 H 2.604 . 2 219 26 26 GLN HG3 H 2.387 . 2 220 26 26 GLN C C 179.571 . 1 221 26 26 GLN CA C 58.835 . 1 222 26 26 GLN CB C 28.730 . 1 223 26 26 GLN CG C 34.125 . 1 224 26 26 GLN N N 120.302 . 1 225 27 27 VAL H H 8.197 . 1 226 27 27 VAL HA H 3.514 . 1 227 27 27 VAL HB H 2.099 . 1 228 27 27 VAL HG1 H 0.791 . 2 229 27 27 VAL HG2 H 0.841 . 2 230 27 27 VAL C C 177.010 . 1 231 27 27 VAL CA C 66.937 . 1 232 27 27 VAL CB C 31.501 . 1 233 27 27 VAL CG1 C 23.333 . 2 234 27 27 VAL CG2 C 22.166 . 2 235 27 27 VAL N N 122.122 . 1 236 28 28 THR H H 8.043 . 1 237 28 28 THR HA H 3.850 . 1 238 28 28 THR HB H 4.259 . 1 239 28 28 THR HG2 H 1.222 . 1 240 28 28 THR C C 176.052 . 1 241 28 28 THR CA C 66.383 . 1 242 28 28 THR CB C 68.549 . 1 243 28 28 THR CG2 C 22.020 . 1 244 28 28 THR N N 116.625 . 1 245 29 29 GLU H H 8.382 . 1 246 29 29 GLU HA H 4.102 . 1 247 29 29 GLU HB2 H 2.084 . 2 248 29 29 GLU HB3 H 1.985 . 2 249 29 29 GLU HG2 H 2.447 . 2 250 29 29 GLU HG3 H 2.195 . 2 251 29 29 GLU C C 178.528 . 1 252 29 29 GLU CA C 59.194 . 1 253 29 29 GLU CB C 29.605 . 1 254 29 29 GLU CG C 36.606 . 1 255 29 29 GLU N N 121.395 . 1 256 30 30 ALA H H 7.884 . 1 257 30 30 ALA HA H 4.170 . 1 258 30 30 ALA HB H 1.645 . 1 259 30 30 ALA C C 180.644 . 1 260 30 30 ALA CA C 54.658 . 1 261 30 30 ALA CB C 18.035 . 1 262 30 30 ALA N N 121.248 . 1 263 31 31 LEU H H 8.570 . 1 264 31 31 LEU HA H 3.663 . 1 265 31 31 LEU HB2 H 1.834 . 2 266 31 31 LEU HB3 H 1.586 . 2 267 31 31 LEU HG H 1.394 . 1 268 31 31 LEU HD1 H 0.412 . 2 269 31 31 LEU HD2 H 0.661 . 2 270 31 31 LEU C C 178.214 . 1 271 31 31 LEU CA C 57.462 . 1 272 31 31 LEU CB C 41.164 . 1 273 31 31 LEU CG C 26.688 . 1 274 31 31 LEU CD1 C 22.604 . 2 275 31 31 LEU CD2 C 25.083 . 2 276 31 31 LEU N N 123.142 . 1 277 32 32 ASP H H 8.406 . 1 278 32 32 ASP HA H 4.316 . 1 279 32 32 ASP HB2 H 2.788 . 2 280 32 32 ASP HB3 H 2.598 . 2 281 32 32 ASP C C 179.462 . 1 282 32 32 ASP CA C 57.069 . 1 283 32 32 ASP CB C 40.107 . 1 284 32 32 ASP N N 120.434 . 1 285 33 33 LYS H H 7.804 . 1 286 33 33 LYS HA H 4.021 . 1 287 33 33 LYS HB2 H 1.839 . 1 288 33 33 LYS HB3 H 1.839 . 1 289 33 33 LYS HG2 H 1.695 . 2 290 33 33 LYS HG3 H 1.456 . 2 291 33 33 LYS HD2 H 1.653 . 1 292 33 33 LYS HD3 H 1.653 . 1 293 33 33 LYS HE2 H 2.926 . 1 294 33 33 LYS HE3 H 2.926 . 1 295 33 33 LYS C C 178.951 . 1 296 33 33 LYS CA C 59.108 . 1 297 33 33 LYS CB C 32.713 . 1 298 33 33 LYS CG C 25.667 . 1 299 33 33 LYS CD C 28.876 . 1 300 33 33 LYS CE C 41.857 . 1 301 33 33 LYS N N 118.915 . 1 302 34 34 LEU H H 7.637 . 1 303 34 34 LEU HA H 3.962 . 1 304 34 34 LEU HB2 H 1.838 . 2 305 34 34 LEU HB3 H 1.228 . 2 306 34 34 LEU HG H 1.388 . 1 307 34 34 LEU HD1 H 0.690 . 2 308 34 34 LEU HD2 H 0.842 . 2 309 34 34 LEU CA C 56.972 . 1 310 34 34 LEU CB C 42.294 . 1 311 34 34 LEU CG C 26.834 . 1 312 34 34 LEU CD1 C 26.250 . 2 313 34 34 LEU CD2 C 23.625 . 2 314 34 34 LEU N N 120.868 . 1 315 35 35 ALA HA H 3.863 . 1 316 35 35 ALA HB H 1.379 . 1 317 35 35 ALA CA C 53.963 . 1 318 35 35 ALA CB C 18.228 . 1 319 36 36 ALA HA H 4.243 . 1 320 36 36 ALA HB H 1.445 . 1 321 36 36 ALA C C 178.081 . 1 322 36 36 ALA CA C 52.960 . 1 323 36 36 ALA CB C 19.278 . 1 324 37 37 LYS H H 7.484 . 1 325 37 37 LYS HA H 4.555 . 1 326 37 37 LYS HB2 H 1.935 . 2 327 37 37 LYS HB3 H 1.586 . 2 328 37 37 LYS HG2 H 1.365 . 1 329 37 37 LYS HG3 H 1.365 . 1 330 37 37 LYS HD2 H 1.723 . 1 331 37 37 LYS HD3 H 1.723 . 1 332 37 37 LYS HE2 H 2.995 . 2 333 37 37 LYS HE3 H 2.954 . 2 334 37 37 LYS CA C 54.377 . 1 335 37 37 LYS CB C 33.397 . 1 336 37 37 LYS CG C 25.375 . 1 337 37 37 LYS CD C 29.459 . 1 338 37 37 LYS CE C 42.002 . 1 339 37 37 LYS N N 119.664 . 1 340 38 38 PRO HA H 4.536 . 1 341 38 38 PRO HB2 H 2.185 . 2 342 38 38 PRO HB3 H 1.864 . 2 343 38 38 PRO HG2 H 1.920 . 1 344 38 38 PRO HG3 H 1.920 . 1 345 38 38 PRO HD2 H 3.539 . 2 346 38 38 PRO HD3 H 3.445 . 2 347 38 38 PRO C C 177.584 . 1 348 38 38 PRO CA C 64.696 . 1 349 38 38 PRO CB C 31.939 . 1 350 38 38 PRO CG C 27.125 . 1 351 38 38 PRO CD C 49.693 . 1 352 39 39 SER H H 8.031 . 1 353 39 39 SER HA H 4.427 . 1 354 39 39 SER HB2 H 4.008 . 2 355 39 39 SER HB3 H 3.807 . 2 356 39 39 SER C C 174.393 . 1 357 39 39 SER CA C 57.676 . 1 358 39 39 SER CB C 63.702 . 1 359 39 39 SER N N 112.062 . 1 360 40 40 ASP H H 7.802 . 1 361 40 40 ASP HA H 4.877 . 1 362 40 40 ASP HB2 H 3.092 . 2 363 40 40 ASP HB3 H 2.504 . 2 364 40 40 ASP CA C 52.365 . 1 365 40 40 ASP CB C 42.878 . 1 366 40 40 ASP N N 124.947 . 1 367 41 41 PRO HA H 4.307 . 1 368 41 41 PRO HB2 H 2.390 . 2 369 41 41 PRO HB3 H 2.027 . 2 370 41 41 PRO HG2 H 2.142 . 2 371 41 41 PRO HG3 H 2.077 . 2 372 41 41 PRO HD2 H 4.335 . 2 373 41 41 PRO HD3 H 3.901 . 2 374 41 41 PRO CA C 64.900 . 1 375 41 41 PRO CB C 32.084 . 1 376 41 41 PRO CG C 27.271 . 1 377 41 41 PRO CD C 51.257 . 1 378 42 42 ALA H H 8.221 . 1 379 42 42 ALA HA H 4.294 . 1 380 42 42 ALA HB H 1.495 . 1 381 42 42 ALA CA C 54.785 . 1 382 42 42 ALA CB C 17.936 . 1 383 42 42 ALA N N 122.627 . 1 384 43 43 LEU HA H 4.205 . 1 385 43 43 LEU HB2 H 1.997 . 2 386 43 43 LEU HB3 H 1.370 . 2 387 43 43 LEU HG H 1.718 . 1 388 43 43 LEU HD1 H 0.832 . 2 389 43 43 LEU HD2 H 1.014 . 2 390 43 43 LEU CA C 56.734 . 1 391 43 43 LEU CB C 41.565 . 1 392 43 43 LEU CG C 26.688 . 1 393 43 43 LEU CD1 C 22.166 . 2 394 43 43 LEU CD2 C 26.542 . 2 395 44 44 LEU HA H 4.235 . 1 396 44 44 LEU HB2 H 1.793 . 2 397 44 44 LEU HB3 H 1.749 . 2 398 44 44 LEU HG H 1.571 . 1 399 44 44 LEU HD1 H 0.962 . 2 400 44 44 LEU HD2 H 1.012 . 2 401 44 44 LEU C C 178.196 . 1 402 44 44 LEU CA C 58.334 . 1 403 44 44 LEU CB C 41.520 . 1 404 44 44 LEU CG C 27.125 . 1 405 44 44 LEU CD1 C 25.285 . 2 406 44 44 LEU CD2 C 23.801 . 2 407 45 45 ALA H H 7.885 . 1 408 45 45 ALA HA H 4.189 . 1 409 45 45 ALA HB H 1.498 . 1 410 45 45 ALA C C 180.527 . 1 411 45 45 ALA CA C 54.907 . 1 412 45 45 ALA CB C 17.848 . 1 413 45 45 ALA N N 121.241 . 1 414 46 46 ALA H H 8.018 . 1 415 46 46 ALA HA H 4.198 . 1 416 46 46 ALA HB H 1.530 . 1 417 46 46 ALA C C 180.072 . 1 418 46 46 ALA CA C 54.932 . 1 419 46 46 ALA CB C 18.495 . 1 420 46 46 ALA N N 120.792 . 1 421 47 47 TYR H H 7.804 . 1 422 47 47 TYR HA H 4.173 . 1 423 47 47 TYR HB2 H 3.111 . 2 424 47 47 TYR HB3 H 3.022 . 2 425 47 47 TYR C C 176.012 . 1 426 47 47 TYR CA C 60.984 . 1 427 47 47 TYR CB C 38.316 . 1 428 47 47 TYR N N 118.549 . 1 429 48 48 GLN H H 8.531 . 1 430 48 48 GLN HA H 3.554 . 1 431 48 48 GLN HB2 H 2.175 . 2 432 48 48 GLN HB3 H 1.994 . 2 433 48 48 GLN HG2 H 2.577 . 2 434 48 48 GLN HG3 H 2.304 . 2 435 48 48 GLN C C 179.279 . 1 436 48 48 GLN CA C 59.042 . 1 437 48 48 GLN CB C 27.990 . 1 438 48 48 GLN CG C 34.126 . 1 439 48 48 GLN N N 117.399 . 1 440 49 49 SER H H 8.316 . 1 441 49 49 SER HA H 4.194 . 1 442 49 49 SER HB2 H 3.976 . 1 443 49 49 SER HB3 H 3.976 . 1 444 49 49 SER C C 176.978 . 1 445 49 49 SER CA C 61.444 . 1 446 49 49 SER CB C 62.915 . 1 447 49 49 SER N N 114.905 . 1 448 50 50 LYS H H 7.904 . 1 449 50 50 LYS HA H 4.202 . 1 450 50 50 LYS HB2 H 1.928 . 2 451 50 50 LYS HB3 H 1.694 . 2 452 50 50 LYS HG2 H 1.536 . 2 453 50 50 LYS HG3 H 1.493 . 2 454 50 50 LYS HD2 H 1.821 . 1 455 50 50 LYS HD3 H 1.821 . 1 456 50 50 LYS HE2 H 2.934 . 2 457 50 50 LYS HE3 H 2.903 . 2 458 50 50 LYS C C 178.282 . 1 459 50 50 LYS CA C 57.181 . 1 460 50 50 LYS CB C 30.726 . 1 461 50 50 LYS CG C 24.062 . 1 462 50 50 LYS CD C 26.979 . 1 463 50 50 LYS CE C 41.419 . 1 464 50 50 LYS N N 122.392 . 1 465 51 51 LEU H H 8.593 . 1 466 51 51 LEU HA H 3.968 . 1 467 51 51 LEU HB2 H 1.509 . 2 468 51 51 LEU HB3 H 1.020 . 2 469 51 51 LEU HG H 1.443 . 1 470 51 51 LEU HD1 H 0.781 . 2 471 51 51 LEU HD2 H 0.856 . 2 472 51 51 LEU C C 178.637 . 1 473 51 51 LEU CA C 57.811 . 1 474 51 51 LEU CB C 41.761 . 1 475 51 51 LEU CG C 26.542 . 1 476 51 51 LEU CD1 C 24.937 . 2 477 51 51 LEU CD2 C 23.479 . 2 478 51 51 LEU N N 121.244 . 1 479 52 52 SER H H 7.966 . 1 480 52 52 SER HA H 4.233 . 1 481 52 52 SER HB2 H 3.995 . 1 482 52 52 SER HB3 H 3.995 . 1 483 52 52 SER C C 176.783 . 1 484 52 52 SER CA C 61.636 . 1 485 52 52 SER CB C 62.796 . 1 486 52 52 SER N N 113.807 . 1 487 53 53 GLU H H 7.868 . 1 488 53 53 GLU HA H 4.003 . 1 489 53 53 GLU HB2 H 2.193 . 1 490 53 53 GLU HB3 H 2.193 . 1 491 53 53 GLU HG2 H 2.462 . 2 492 53 53 GLU HG3 H 2.218 . 2 493 53 53 GLU C C 178.781 . 1 494 53 53 GLU CA C 59.518 . 1 495 53 53 GLU CB C 30.079 . 1 496 53 53 GLU CG C 36.314 . 1 497 53 53 GLU N N 122.086 . 1 498 54 54 TYR H H 8.426 . 1 499 54 54 TYR HA H 4.259 . 1 500 54 54 TYR HB2 H 3.198 . 2 501 54 54 TYR HB3 H 2.936 . 2 502 54 54 TYR C C 176.677 . 1 503 54 54 TYR CA C 60.887 . 1 504 54 54 TYR CB C 38.650 . 1 505 54 54 TYR N N 120.402 . 1 506 55 55 ASN H H 8.674 . 1 507 55 55 ASN HA H 4.255 . 1 508 55 55 ASN HB2 H 2.846 . 2 509 55 55 ASN HB3 H 2.735 . 2 510 55 55 ASN C C 177.561 . 1 511 55 55 ASN CA C 55.647 . 1 512 55 55 ASN CB C 38.004 . 1 513 55 55 ASN N N 118.089 . 1 514 56 56 LEU H H 8.053 . 1 515 56 56 LEU HA H 4.037 . 1 516 56 56 LEU HB2 H 1.759 . 2 517 56 56 LEU HB3 H 1.533 . 2 518 56 56 LEU HG H 1.630 . 1 519 56 56 LEU HD1 H 0.809 . 2 520 56 56 LEU HD2 H 0.850 . 2 521 56 56 LEU C C 179.149 . 1 522 56 56 LEU CA C 57.800 . 1 523 56 56 LEU CB C 41.905 . 1 524 56 56 LEU CG C 26.834 . 1 525 56 56 LEU CD1 C 23.771 . 2 526 56 56 LEU CD2 C 24.792 . 2 527 56 56 LEU N N 121.071 . 1 528 57 57 TYR H H 7.783 . 1 529 57 57 TYR HA H 4.209 . 1 530 57 57 TYR HB2 H 3.055 . 2 531 57 57 TYR HB3 H 2.978 . 2 532 57 57 TYR C C 177.619 . 1 533 57 57 TYR CA C 60.408 . 1 534 57 57 TYR CB C 38.605 . 1 535 57 57 TYR N N 119.618 . 1 536 58 58 ARG H H 8.226 . 1 537 58 58 ARG HA H 3.847 . 1 538 58 58 ARG HB2 H 1.571 . 1 539 58 58 ARG HB3 H 1.571 . 1 540 58 58 ARG HG2 H 1.353 . 1 541 58 58 ARG HG3 H 1.353 . 1 542 58 58 ARG HD2 H 2.932 . 2 543 58 58 ARG HD3 H 2.845 . 2 544 58 58 ARG C C 177.756 . 1 545 58 58 ARG CA C 57.785 . 1 546 58 58 ARG CB C 29.637 . 1 547 58 58 ARG CG C 26.688 . 1 548 58 58 ARG CD C 42.877 . 1 549 58 58 ARG N N 118.950 . 1 550 59 59 ASN H H 8.036 . 1 551 59 59 ASN HA H 4.529 . 1 552 59 59 ASN HB2 H 2.784 . 2 553 59 59 ASN C C 175.851 . 1 554 59 59 ASN CA C 54.331 . 1 555 59 59 ASN CB C 38.576 . 1 556 59 59 ASN N N 117.639 . 1 557 60 60 ALA H H 7.800 . 1 558 60 60 ALA HA H 4.208 . 1 559 60 60 ALA HB H 1.385 . 1 560 60 60 ALA C C 178.431 . 1 561 60 60 ALA CA C 53.432 . 1 562 60 60 ALA CB C 23.875 . 1 563 60 60 ALA N N 122.801 . 1 564 61 61 GLN H H 7.955 . 1 565 61 61 GLN HA H 4.161 . 1 566 61 61 GLN HB2 H 2.090 . 2 567 61 61 GLN HB3 H 1.895 . 2 568 61 61 GLN HG2 H 2.198 . 1 569 61 61 GLN HG3 H 2.198 . 1 570 61 61 GLN C C 176.528 . 1 571 61 61 GLN CA C 56.215 . 1 572 61 61 GLN CB C 28.875 . 1 573 61 61 GLN CG C 33.543 . 1 574 61 61 GLN N N 117.587 . 1 575 62 62 SER H H 8.047 . 1 576 62 62 SER HA H 4.342 . 1 577 62 62 SER HB2 H 3.882 . 2 578 62 62 SER HB3 H 3.825 . 2 579 62 62 SER C C 174.510 . 1 580 62 62 SER CA C 58.933 . 1 581 62 62 SER CB C 63.652 . 1 582 62 62 SER N N 115.292 . 1 583 63 63 ASN H H 8.289 . 1 584 63 63 ASN HA H 4.725 . 1 585 63 63 ASN HB2 H 2.823 . 2 586 63 63 ASN HB3 H 2.762 . 2 587 63 63 ASN C C 175.376 . 1 588 63 63 ASN CA C 53.525 . 1 589 63 63 ASN CB C 38.813 . 1 590 63 63 ASN N N 120.221 . 1 591 64 64 THR H H 7.993 . 1 592 64 64 THR HA H 4.265 . 1 593 64 64 THR HB H 4.174 . 1 594 64 64 THR HG2 H 1.161 . 1 595 64 64 THR C C 174.487 . 1 596 64 64 THR CA C 62.346 . 1 597 64 64 THR CB C 69.765 . 1 598 64 64 THR CG2 C 21.583 . 1 599 64 64 THR N N 114.038 . 1 600 65 65 VAL H H 8.018 . 1 601 65 65 VAL HA H 4.017 . 1 602 65 65 VAL HB H 2.030 . 1 603 65 65 VAL HG1 H 0.863 . 2 604 65 65 VAL HG2 H 0.907 . 2 605 65 65 VAL C C 175.864 . 1 606 65 65 VAL CA C 62.617 . 1 607 65 65 VAL CB C 32.491 . 1 608 65 65 VAL CG1 C 20.853 . 2 609 65 65 VAL CG2 C 21.145 . 2 610 65 65 VAL N N 122.556 . 1 611 66 66 LYS H H 8.269 . 1 612 66 66 LYS HA H 4.230 . 1 613 66 66 LYS HB2 H 1.667 . 1 614 66 66 LYS HB3 H 1.667 . 1 615 66 66 LYS HG2 H 1.331 . 2 616 66 66 LYS HG3 H 1.255 . 2 617 66 66 LYS HD2 H 1.609 . 1 618 66 66 LYS HD3 H 1.609 . 1 619 66 66 LYS C C 175.969 . 1 620 66 66 LYS CA C 56.208 . 1 621 66 66 LYS CB C 33.107 . 1 622 66 66 LYS CG C 24.792 . 1 623 66 66 LYS CD C 28.875 . 1 624 66 66 LYS N N 125.408 . 1 625 67 67 VAL H H 8.001 . 1 626 67 67 VAL HA H 4.018 . 1 627 67 67 VAL HB H 1.924 . 1 628 67 67 VAL HG1 H 0.778 . 2 629 67 67 VAL HG2 H 0.834 . 2 630 67 67 VAL C C 175.652 . 1 631 67 67 VAL CA C 62.158 . 1 632 67 67 VAL CB C 32.951 . 1 633 67 67 VAL CG1 C 20.999 . 2 634 67 67 VAL CG2 C 20.562 . 2 635 67 67 VAL N N 121.375 . 1 636 68 68 PHE H H 8.340 . 1 637 68 68 PHE HA H 4.572 . 1 638 68 68 PHE HB2 H 3.083 . 2 639 68 68 PHE HB3 H 2.941 . 2 640 68 68 PHE C C 175.462 . 1 641 68 68 PHE CA C 57.720 . 1 642 68 68 PHE CB C 39.765 . 1 643 68 68 PHE N N 124.212 . 1 644 69 69 LYS H H 8.236 . 1 645 69 69 LYS HA H 4.239 . 1 646 69 69 LYS HB2 H 1.754 . 2 647 69 69 LYS HB3 H 1.672 . 2 648 69 69 LYS HG2 H 1.381 . 2 649 69 69 LYS HG3 H 1.339 . 2 650 69 69 LYS HD2 H 1.622 . 1 651 69 69 LYS HD3 H 1.622 . 1 652 69 69 LYS C C 175.818 . 1 653 69 69 LYS CA C 56.286 . 1 654 69 69 LYS CB C 33.448 . 1 655 69 69 LYS CG C 24.500 . 1 656 69 69 LYS CD C 28.875 . 1 657 69 69 LYS N N 123.117 . 1 658 70 70 ASP H H 8.256 . 1 659 70 70 ASP HA H 4.528 . 1 660 70 70 ASP HB2 H 2.703 . 2 661 70 70 ASP HB3 H 2.579 . 2 662 70 70 ASP C C 176.465 . 1 663 70 70 ASP CA C 54.553 . 1 664 70 70 ASP CB C 41.098 . 1 665 70 70 ASP N N 121.494 . 1 666 71 71 ILE H H 8.100 . 1 667 71 71 ILE HA H 4.020 . 1 668 71 71 ILE HB H 1.834 . 1 669 71 71 ILE HG12 H 1.435 . 9 670 71 71 ILE HG13 H 1.140 . 9 671 71 71 ILE HG2 H 0.856 . 1 672 71 71 ILE HD1 H 0.787 . 1 673 71 71 ILE C C 175.997 . 1 674 71 71 ILE CA C 61.831 . 1 675 71 71 ILE CB C 38.694 . 1 676 71 71 ILE CG1 C 27.563 . 1 677 71 71 ILE CG2 C 17.499 . 1 678 71 71 ILE CD1 C 13.269 . 1 679 71 71 ILE N N 120.643 . 1 680 72 72 ASP H H 8.180 . 1 681 72 72 ASP HA H 4.491 . 1 682 72 72 ASP HB2 H 2.679 . 2 683 72 72 ASP HB3 H 2.605 . 2 684 72 72 ASP C C 176.680 . 1 685 72 72 ASP CA C 55.021 . 1 686 72 72 ASP CB C 41.122 . 1 687 72 72 ASP N N 123.265 . 1 688 73 73 ALA H H 8.116 . 1 689 73 73 ALA HA H 4.130 . 1 690 73 73 ALA HB H 1.396 . 1 691 73 73 ALA C C 178.312 . 1 692 73 73 ALA CA C 53.513 . 1 693 73 73 ALA CB C 18.947 . 1 694 73 73 ALA N N 124.310 . 1 695 74 74 ALA H H 8.138 . 1 696 74 74 ALA HA H 4.149 . 1 697 74 74 ALA HB H 1.362 . 1 698 74 74 ALA C C 178.750 . 1 699 74 74 ALA CA C 53.464 . 1 700 74 74 ALA CB C 18.755 . 1 701 74 74 ALA N N 121.606 . 1 702 75 75 ILE H H 7.841 . 1 703 75 75 ILE HA H 3.947 . 1 704 75 75 ILE HB H 1.875 . 1 705 75 75 ILE HG12 H 1.485 . 9 706 75 75 ILE HG13 H 1.139 . 9 707 75 75 ILE HG2 H 0.835 . 1 708 75 75 ILE HD1 H 0.806 . 1 709 75 75 ILE C C 176.893 . 1 710 75 75 ILE CA C 62.174 . 1 711 75 75 ILE CB C 38.214 . 1 712 75 75 ILE CG1 C 27.709 . 1 713 75 75 ILE CG2 C 17.499 . 1 714 75 75 ILE CD1 C 12.977 . 1 715 75 75 ILE N N 118.632 . 1 716 76 76 LEU H H 7.919 . 1 717 76 76 LEU HA H 4.189 . 1 718 76 76 LEU HB2 H 1.620 . 2 719 76 76 LEU HB3 H 1.494 . 2 720 76 76 LEU HG H 1.560 . 1 721 76 76 LEU HD1 H 0.789 . 2 722 76 76 LEU HD2 H 0.843 . 2 723 76 76 LEU C C 177.743 . 1 724 76 76 LEU CA C 55.804 . 1 725 76 76 LEU CB C 42.174 . 1 726 76 76 LEU CG C 26.979 . 1 727 76 76 LEU CD1 C 23.479 . 2 728 76 76 LEU CD2 C 24.937 . 2 729 76 76 LEU N N 123.571 . 1 730 77 77 GLU H H 8.050 . 1 731 77 77 GLU HA H 4.104 . 1 732 77 77 GLU HB2 H 1.892 . 1 733 77 77 GLU HB3 H 1.892 . 1 734 77 77 GLU HG2 H 2.196 . 2 735 77 77 GLU HG3 H 2.118 . 2 736 77 77 GLU C C 176.605 . 1 737 77 77 GLU CA C 57.046 . 1 738 77 77 GLU CB C 30.118 . 1 739 77 77 GLU CG C 36.023 . 1 740 77 77 GLU N N 119.985 . 1 741 78 78 HIS H H 8.099 . 1 742 78 78 HIS HA H 4.479 . 1 743 78 78 HIS C C 175.241 . 1 744 78 78 HIS CA C 56.455 . 1 745 78 78 HIS N N 118.922 . 1 746 79 79 HIS H H 8.172 . 1 747 79 79 HIS CA C 56.306 . 1 748 79 79 HIS N N 119.297 . 1 749 79 82 HIS C C 173.823 . 1 750 83 83 HIS H H 8.079 . 1 751 83 83 HIS N N 125.276 . 1 stop_ save_