data_28050 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H 15N 13C Resonance Assignments of Receptor Binding Domain 1 of CDTb ; _BMRB_accession_number 28050 _BMRB_flat_file_name bmr28050.str _Entry_type original _Submission_date 2019-11-27 _Accession_date 2019-11-27 _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 Cook Mary E. . 2 Varney Kristen M. . 3 Godoy-Ruiz Raquel J. . 4 Weber David J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 "13C chemical shifts" 437 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-04-17 update BMRB 'update entry citation' 2019-12-04 original author 'original release' stop_ _Original_release_date 2019-11-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a novel macromolecular assembly ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31896582 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weber David J. . 2 Xu Xingjian . . 3 Godoy-Ruiz Raquel . . 4 Adipietro 'Kaylin A. Adipietro' A . 5 Peralta Christopher . . 6 Ben-Hail Danya . . 7 Varney Kristen M. . 8 Cook Mary E. . 9 Roth Braden M. . 10 Wilder Paul T. . 11 Cleveland Thomas . . 12 Grishaev Alexander . . 13 Neu 'Heather M. Neu' M . 14 Michel Sarah . . 15 Yu Wenbo . . 16 Beckett Dorothy . . 17 Rustandi Richard R. . 18 Lancaster Catherine . . 19 Loughney John W. . 20 Kristopeit Adam . . 21 Christanti Sianny . . 22 Olson Jessica W. . 23 MacKerell Alex D. . 24 'des Georges' Amedee . . 25 Pozharski Edwin . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 117 _Journal_issue 2 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1049 _Page_last 1058 _Year 2020 _Details . loop_ _Keyword 'Clostridium difficile' NMR 'X-ray crystallography' 'binary toxin' cryoEM 'protein structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name RBD1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RBD1, chain 1' $CDTb_receptor_binding_domain_1 'RBD1, chain 2' $CDTb_receptor_binding_domain_1 'RBD1, chain 3' $CDTb_receptor_binding_domain_1 'RBD1, chain 4' $CDTb_receptor_binding_domain_1 'CALCIUM ION' $entity_CA 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_CDTb_receptor_binding_domain_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CDTb_receptor_binding_domain_1 _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 136 _Mol_residue_sequence ; DDDDKPTYFTNFDDYNNYPS TWSNVNTTNQDGLQGSANKL NGETKIKIPMSELKPYKRYV FSGYSKDPLTSNSIIVKIKA KEEKTDYLVPEQGYTKFSYE FETTEKDSSNIEITLIGSGT TYLDNLSITELNSTPE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 611 ASP 2 612 ASP 3 613 ASP 4 614 ASP 5 615 LYS 6 616 PRO 7 617 THR 8 618 TYR 9 619 PHE 10 620 THR 11 621 ASN 12 622 PHE 13 623 ASP 14 624 ASP 15 625 TYR 16 626 ASN 17 627 ASN 18 628 TYR 19 629 PRO 20 630 SER 21 631 THR 22 632 TRP 23 633 SER 24 634 ASN 25 635 VAL 26 636 ASN 27 637 THR 28 638 THR 29 639 ASN 30 640 GLN 31 641 ASP 32 642 GLY 33 643 LEU 34 644 GLN 35 645 GLY 36 646 SER 37 647 ALA 38 648 ASN 39 649 LYS 40 650 LEU 41 651 ASN 42 652 GLY 43 653 GLU 44 654 THR 45 655 LYS 46 656 ILE 47 657 LYS 48 658 ILE 49 659 PRO 50 660 MET 51 661 SER 52 662 GLU 53 663 LEU 54 664 LYS 55 665 PRO 56 666 TYR 57 667 LYS 58 668 ARG 59 669 TYR 60 670 VAL 61 671 PHE 62 672 SER 63 673 GLY 64 674 TYR 65 675 SER 66 676 LYS 67 677 ASP 68 678 PRO 69 679 LEU 70 680 THR 71 681 SER 72 682 ASN 73 683 SER 74 684 ILE 75 685 ILE 76 686 VAL 77 687 LYS 78 688 ILE 79 689 LYS 80 690 ALA 81 691 LYS 82 692 GLU 83 693 GLU 84 694 LYS 85 695 THR 86 696 ASP 87 697 TYR 88 698 LEU 89 699 VAL 90 700 PRO 91 701 GLU 92 702 GLN 93 703 GLY 94 704 TYR 95 705 THR 96 706 LYS 97 707 PHE 98 708 SER 99 709 TYR 100 710 GLU 101 711 PHE 102 712 GLU 103 713 THR 104 714 THR 105 715 GLU 106 716 LYS 107 717 ASP 108 718 SER 109 719 SER 110 720 ASN 111 721 ILE 112 722 GLU 113 723 ILE 114 724 THR 115 725 LEU 116 726 ILE 117 727 GLY 118 728 SER 119 729 GLY 120 730 THR 121 731 THR 122 732 TYR 123 733 LEU 124 734 ASP 125 735 ASN 126 736 LEU 127 737 SER 128 738 ILE 129 739 THR 130 740 GLU 131 741 LEU 132 742 ASN 133 743 SER 134 744 THR 135 745 PRO 136 746 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CA (CALCIUM ION)" _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CDTb_receptor_binding_domain_1 'Clostridium difficile' 1496 Bacteria . Clostridium difficile 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 $CDTb_receptor_binding_domain_1 'recombinant technology' . Escherichia coli . pET21 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Added calcium to stabilize protein' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CDTb_receptor_binding_domain_1 0.5 mM '[U-13C; U-15N]' HEPES 15 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 10 % 'natural abundance' $entity_CA 13 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TopSpin _Saveframe_category software _Name TopSpin _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 9.7 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version 3.0.0 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III' _Field_strength 950 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III' _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_TROSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC TROSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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' 0.189 . M pH 7.0 . 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 TSP C 13 'methyl carbons' na 0.0 external indirect . . . 0.251449530 TSP H 1 protons ppm 0.0 external indirect . . . 1.0 TSP N 15 nitrogen na 0.0 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 CBCA(CO)NH' '3D C(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(CA)CO' 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 'RBD1, chain 1' _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 1 611 1 ASP H H 8.36 0.00 1 2 611 1 ASP C C 175.49 0.00 1 3 611 1 ASP CA C 53.96 0.00 1 4 611 1 ASP CB C 40.69 0.00 1 5 611 1 ASP N N 122.94 0.00 1 6 613 3 ASP H H 8.17 0.00 1 7 613 3 ASP C C 174.20 0.00 1 8 613 3 ASP CA C 54.82 0.00 1 9 613 3 ASP CB C 42.86 0.00 1 10 613 3 ASP N N 118.67 0.00 1 11 614 4 ASP H H 8.55 0.00 1 12 614 4 ASP C C 174.91 0.00 1 13 614 4 ASP CA C 53.18 0.00 1 14 614 4 ASP CB C 40.78 0.00 1 15 614 4 ASP N N 120.29 0.00 1 16 615 5 LYS H H 8.10 0.00 1 17 615 5 LYS C C 173.43 0.00 1 18 615 5 LYS CA C 53.46 0.00 1 19 615 5 LYS CB C 31.76 0.00 1 20 615 5 LYS N N 123.17 0.00 1 21 617 7 THR H H 8.05 0.00 1 22 617 7 THR CA C 61.32 0.00 1 23 617 7 THR CB C 69.28 0.00 1 24 617 7 THR N N 114.77 0.00 1 25 619 9 PHE H H 9.47 0.00 1 26 619 9 PHE C C 171.52 0.00 1 27 619 9 PHE CA C 56.91 0.00 1 28 619 9 PHE CB C 43.45 0.00 1 29 619 9 PHE N N 123.48 0.00 1 30 620 10 THR H H 7.24 0.00 1 31 620 10 THR C C 169.66 0.00 1 32 620 10 THR CA C 58.39 0.00 1 33 620 10 THR CB C 70.21 0.00 1 34 620 10 THR CG2 C 18.17 0.00 1 35 620 10 THR N N 118.60 0.00 1 36 621 11 ASN H H 7.47 0.00 1 37 621 11 ASN C C 174.56 0.00 1 38 621 11 ASN CA C 49.90 0.00 1 39 621 11 ASN CB C 38.66 0.00 1 40 621 11 ASN N N 121.14 0.00 1 41 622 12 PHE H H 8.31 0.00 1 42 622 12 PHE C C 170.78 0.00 1 43 622 12 PHE CA C 61.35 0.00 1 44 622 12 PHE CB C 35.19 0.00 1 45 622 12 PHE N N 114.62 0.00 1 46 624 14 ASP H H 8.16 0.00 1 47 624 14 ASP C C 175.48 0.00 1 48 624 14 ASP CA C 52.79 0.00 1 49 624 14 ASP CB C 40.54 0.00 1 50 624 14 ASP N N 121.05 0.00 1 51 625 15 TYR H H 8.62 0.00 1 52 625 15 TYR C C 174.60 0.00 1 53 625 15 TYR CA C 57.76 0.00 1 54 625 15 TYR CB C 41.65 0.00 1 55 625 15 TYR N N 123.96 0.00 1 56 627 17 ASN H H 8.49 0.00 1 57 627 17 ASN C C 176.19 0.00 1 58 627 17 ASN CA C 51.08 0.00 1 59 627 17 ASN CB C 38.53 0.00 1 60 627 17 ASN N N 126.89 0.00 1 61 628 18 TYR H H 8.39 0.00 1 62 628 18 TYR C C 175.44 0.00 1 63 628 18 TYR CA C 58.58 0.00 1 64 628 18 TYR CB C 36.81 0.00 1 65 628 18 TYR N N 119.02 0.00 1 66 630 20 SER H H 7.00 0.00 1 67 630 20 SER C C 172.33 0.00 1 68 630 20 SER CA C 54.73 0.00 1 69 630 20 SER CB C 64.36 0.00 1 70 630 20 SER N N 113.21 0.00 1 71 631 21 THR H H 8.04 0.00 1 72 631 21 THR C C 174.83 0.00 1 73 631 21 THR CA C 60.86 0.00 1 74 631 21 THR CB C 69.96 0.00 1 75 631 21 THR CG2 C 21.57 0.00 1 76 631 21 THR N N 113.80 0.00 1 77 632 22 TRP H H 8.46 0.00 1 78 632 22 TRP C C 176.14 0.00 1 79 632 22 TRP CA C 56.70 0.00 1 80 632 22 TRP CB C 28.71 0.00 1 81 632 22 TRP N N 127.64 0.00 1 82 633 23 SER H H 9.06 0.00 1 83 633 23 SER C C 174.20 0.00 1 84 633 23 SER CA C 57.01 0.00 1 85 633 23 SER CB C 64.30 0.00 1 86 633 23 SER N N 118.43 0.00 1 87 634 24 ASN H H 8.68 0.00 1 88 634 24 ASN C C 173.32 0.00 1 89 634 24 ASN CA C 53.23 0.00 1 90 634 24 ASN CB C 37.09 0.00 1 91 634 24 ASN N N 118.03 0.00 1 92 636 26 ASN H H 8.18 0.00 1 93 636 26 ASN CA C 51.52 0.00 1 94 636 26 ASN CB C 38.75 0.00 1 95 636 26 ASN N N 127.43 0.00 1 96 637 27 THR H H 8.55 0.00 1 97 637 27 THR C C 175.61 0.00 1 98 637 27 THR CA C 59.89 0.00 1 99 637 27 THR CB C 67.65 0.00 1 100 637 27 THR CG2 C 22.15 0.00 1 101 637 27 THR N N 112.75 0.00 1 102 638 28 THR H H 7.73 0.00 1 103 638 28 THR C C 173.67 0.00 1 104 638 28 THR CA C 59.76 0.00 1 105 638 28 THR CB C 66.52 0.00 1 106 638 28 THR CG2 C 21.74 0.00 1 107 638 28 THR N N 118.91 0.00 1 108 639 29 ASN H H 8.62 0.00 1 109 639 29 ASN C C 172.77 0.00 1 110 639 29 ASN CA C 52.61 0.00 1 111 639 29 ASN CB C 40.71 0.00 1 112 639 29 ASN N N 119.65 0.00 1 113 640 30 GLN H H 8.79 0.00 1 114 640 30 GLN C C 175.54 0.00 1 115 640 30 GLN CA C 53.62 0.00 1 116 640 30 GLN CB C 27.77 0.00 1 117 640 30 GLN CG C 33.23 0.00 1 118 640 30 GLN N N 121.12 0.00 1 119 641 31 ASP H H 8.57 0.00 1 120 641 31 ASP C C 176.09 0.00 1 121 641 31 ASP CA C 54.30 0.00 1 122 641 31 ASP CB C 43.13 0.00 1 123 641 31 ASP N N 120.78 0.00 1 124 642 32 GLY H H 8.43 0.00 1 125 642 32 GLY C C 173.47 0.00 1 126 642 32 GLY CA C 45.07 0.00 1 127 642 32 GLY N N 109.68 0.00 1 128 643 33 LEU H H 9.52 0.00 1 129 643 33 LEU CA C 57.90 0.00 1 130 643 33 LEU CB C 41.39 0.00 1 131 643 33 LEU CG C 25.77 0.00 1 132 643 33 LEU CD1 C 23.73 0.00 1 133 643 33 LEU CD2 C 23.73 0.00 1 134 643 33 LEU N N 130.61 0.00 1 135 644 34 GLN H H 6.48 0.00 1 136 644 34 GLN C C 175.73 0.00 1 137 644 34 GLN CA C 55.00 0.00 1 138 644 34 GLN CB C 30.26 0.00 1 139 644 34 GLN CG C 32.89 0.00 1 140 644 34 GLN N N 110.40 0.00 1 141 645 35 GLY H H 9.07 0.00 1 142 645 35 GLY C C 174.12 0.00 1 143 645 35 GLY CA C 46.80 0.00 1 144 645 35 GLY N N 117.67 0.00 1 145 646 36 SER H H 11.69 0.00 1 146 646 36 SER C C 173.70 0.00 1 147 646 36 SER CA C 58.35 0.00 1 148 646 36 SER CB C 64.50 0.00 1 149 646 36 SER N N 128.22 0.00 1 150 647 37 ALA H H 9.00 0.00 1 151 647 37 ALA C C 176.07 0.00 1 152 647 37 ALA CA C 48.97 0.00 1 153 647 37 ALA CB C 22.52 0.00 1 154 647 37 ALA N N 130.09 0.00 1 155 648 38 ASN H H 8.41 0.00 1 156 648 38 ASN C C 174.16 0.00 1 157 648 38 ASN CA C 51.45 0.00 1 158 648 38 ASN CB C 36.67 0.00 1 159 648 38 ASN N N 117.00 0.00 1 160 649 39 LYS H H 8.45 0.00 1 161 649 39 LYS C C 172.91 0.00 1 162 649 39 LYS CA C 55.23 0.00 1 163 649 39 LYS CB C 32.19 0.00 1 164 649 39 LYS CE C 41.58 0.00 1 165 649 39 LYS N N 130.86 0.00 1 166 650 40 LEU H H 8.65 0.00 1 167 650 40 LEU C C 174.10 0.00 1 168 650 40 LEU CA C 54.23 0.00 1 169 650 40 LEU CB C 42.74 0.00 1 170 650 40 LEU CG C 26.66 0.00 1 171 650 40 LEU CD1 C 24.02 0.00 2 172 650 40 LEU N N 133.48 0.00 1 173 651 41 ASN H H 8.11 0.00 1 174 651 41 ASN C C 173.27 0.00 1 175 651 41 ASN CA C 52.57 0.00 1 176 651 41 ASN CB C 40.09 0.00 1 177 651 41 ASN N N 127.30 0.00 1 178 652 42 GLY H H 7.95 0.00 1 179 652 42 GLY C C 171.28 0.00 1 180 652 42 GLY CA C 44.87 0.00 1 181 652 42 GLY N N 113.68 0.00 1 182 653 43 GLU H H 8.38 0.00 1 183 653 43 GLU C C 176.21 0.00 1 184 653 43 GLU CA C 54.28 0.00 1 185 653 43 GLU CB C 32.66 0.00 1 186 653 43 GLU CG C 36.25 0.00 1 187 653 43 GLU N N 124.38 0.00 1 188 654 44 THR H H 9.17 0.00 1 189 654 44 THR C C 170.52 0.00 1 190 654 44 THR CA C 59.80 0.00 1 191 654 44 THR CB C 69.51 0.00 1 192 654 44 THR CG2 C 20.26 0.00 1 193 654 44 THR N N 122.54 0.00 1 194 655 45 LYS H H 8.61 0.00 1 195 655 45 LYS C C 174.21 0.00 1 196 655 45 LYS CA C 53.71 0.00 1 197 655 45 LYS CB C 37.38 0.00 1 198 655 45 LYS CG C 23.57 0.00 1 199 655 45 LYS CD C 29.33 0.00 1 200 655 45 LYS CE C 41.27 0.00 1 201 655 45 LYS N N 129.98 0.00 1 202 656 46 ILE H H 8.66 0.00 1 203 656 46 ILE C C 170.74 0.00 1 204 656 46 ILE CA C 58.77 0.00 1 205 656 46 ILE CB C 41.25 0.00 1 206 656 46 ILE CG1 C 24.368 0.00 1 207 656 46 ILE CG2 C 14.69 0.00 1 208 656 46 ILE CD1 C 13.47 0.00 1 209 656 46 ILE N N 126.18 0.00 1 210 657 47 LYS H H 7.72 0.00 1 211 657 47 LYS C C 175.14 0.00 1 212 657 47 LYS CA C 53.58 0.00 1 213 657 47 LYS CB C 33.28 0.00 1 214 657 47 LYS CE C 41.09 0.00 1 215 657 47 LYS N N 125.88 0.00 1 216 658 48 ILE H H 9.04 0.00 1 217 658 48 ILE C C 172.00 0.00 1 218 658 48 ILE CA C 56.94 0.00 1 219 658 48 ILE CB C 40.21 0.00 1 220 658 48 ILE N N 126.03 0.00 1 221 660 50 MET H H 8.77 0.00 1 222 660 50 MET C C 178.00 0.00 1 223 660 50 MET CA C 54.86 0.00 1 224 660 50 MET CB C 29.13 0.00 1 225 660 50 MET CG C 31.58 0.00 1 226 660 50 MET N N 123.21 0.00 1 227 661 51 SER H H 8.09 0.00 1 228 661 51 SER C C 175.33 0.00 1 229 661 51 SER CA C 60.25 0.00 1 230 661 51 SER CB C 61.93 0.00 1 231 661 51 SER N N 113.24 0.00 1 232 662 52 GLU H H 7.83 0.00 1 233 662 52 GLU C C 175.90 0.00 1 234 662 52 GLU CA C 54.28 0.00 1 235 662 52 GLU CB C 28.49 0.00 1 236 662 52 GLU CG C 35.10 0.00 1 237 662 52 GLU N N 119.80 0.00 1 238 663 53 LEU H H 7.59 0.00 1 239 663 53 LEU C C 173.88 0.00 1 240 663 53 LEU CA C 52.61 0.00 1 241 663 53 LEU CB C 44.54 0.00 1 242 663 53 LEU CG C 29.478 0.00 1 243 663 53 LEU CD1 C 24.64 0.00 1 244 663 53 LEU CD2 C 24.64 0.00 1 245 663 53 LEU N N 122.53 0.00 1 246 664 54 LYS H H 7.99 0.00 1 247 664 54 LYS C C 174.77 0.00 1 248 664 54 LYS CA C 56.82 0.00 1 249 664 54 LYS CB C 32.82 0.00 1 250 664 54 LYS N N 113.65 0.00 1 251 666 56 TYR H H 7.65 0.00 1 252 666 56 TYR C C 174.72 0.00 1 253 666 56 TYR CA C 58.08 0.00 1 254 666 56 TYR CB C 35.29 0.00 1 255 666 56 TYR N N 118.64 0.00 1 256 667 57 LYS H H 8.10 0.00 1 257 667 57 LYS C C 173.92 0.00 1 258 667 57 LYS CA C 52.65 0.00 1 259 667 57 LYS CB C 35.46 0.00 1 260 667 57 LYS N N 120.11 0.00 1 261 668 58 ARG H H 8.00 0.00 1 262 668 58 ARG C C 173.47 0.00 1 263 668 58 ARG CA C 54.82 0.00 1 264 668 58 ARG CB C 31.49 0.00 1 265 668 58 ARG CD C 43.06 0.00 1 266 668 58 ARG N N 122.22 0.00 1 267 669 59 TYR H H 8.73 0.00 1 268 669 59 TYR C C 173.92 0.00 1 269 669 59 TYR CA C 55.89 0.00 1 270 669 59 TYR CB C 44.63 0.00 1 271 669 59 TYR N N 122.60 0.00 1 272 670 60 VAL H H 9.02 0.00 1 273 670 60 VAL C C 175.76 0.00 1 274 670 60 VAL CA C 59.67 0.00 1 275 670 60 VAL CB C 34.92 0.00 1 276 670 60 VAL CG1 C 21.50 0.00 1 277 670 60 VAL CG2 C 21.50 0.00 1 278 670 60 VAL N N 115.42 0.00 1 279 671 61 PHE H H 9.90 0.00 1 280 671 61 PHE C C 173.15 0.00 1 281 671 61 PHE CA C 54.29 0.00 1 282 671 61 PHE CB C 40.35 0.00 1 283 671 61 PHE N N 132.57 0.00 1 284 672 62 SER H H 9.20 0.00 1 285 672 62 SER C C 170.41 0.00 1 286 672 62 SER CA C 54.80 0.00 1 287 672 62 SER CB C 67.06 0.00 1 288 672 62 SER N N 123.26 0.00 1 289 673 63 GLY H H 6.51 0.00 1 290 673 63 GLY C C 168.54 0.00 1 291 673 63 GLY CA C 45.06 0.00 1 292 673 63 GLY N N 106.75 0.00 1 293 674 64 TYR H H 7.93 0.00 1 294 674 64 TYR C C 174.65 0.00 1 295 674 64 TYR CA C 55.69 0.00 1 296 674 64 TYR CB C 41.11 0.00 1 297 674 64 TYR N N 116.01 0.00 1 298 675 65 SER H H 8.54 0.00 1 299 675 65 SER C C 174.08 0.00 1 300 675 65 SER CA C 56.73 0.00 1 301 675 65 SER CB C 69.19 0.00 1 302 675 65 SER N N 116.94 0.00 1 303 676 66 LYS H H 8.65 0.00 1 304 676 66 LYS C C 173.15 0.00 1 305 676 66 LYS CA C 56.31 0.00 1 306 676 66 LYS CB C 35.21 0.00 1 307 676 66 LYS N N 117.82 0.00 1 308 677 67 ASP H H 8.27 0.00 1 309 677 67 ASP C C 174.22 0.00 1 310 677 67 ASP CA C 50.72 0.00 1 311 677 67 ASP CB C 42.88 0.00 1 312 677 67 ASP N N 117.00 0.00 1 313 679 69 LEU H H 8.20 0.00 1 314 679 69 LEU C C 177.03 0.00 1 315 679 69 LEU CA C 54.01 0.00 1 316 679 69 LEU CB C 42.05 0.00 1 317 679 69 LEU CG C 26.82 0.00 1 318 679 69 LEU CD1 C 23.43 0.00 1 319 679 69 LEU CD2 C 23.43 0.00 1 320 679 69 LEU N N 117.04 0.00 1 321 680 70 THR H H 8.05 0.00 1 322 680 70 THR C C 172.92 0.00 1 323 680 70 THR CA C 60.87 0.00 1 324 680 70 THR CB C 69.07 0.00 1 325 680 70 THR N N 113.74 0.00 1 326 683 73 SER H H 8.00 0.00 1 327 683 73 SER C C 172.22 0.00 1 328 683 73 SER CA C 56.87 0.00 1 329 683 73 SER CB C 65.18 0.00 1 330 683 73 SER N N 113.25 0.00 1 331 684 74 ILE H H 9.32 0.00 1 332 684 74 ILE C C 174.20 0.00 1 333 684 74 ILE CA C 59.56 0.00 1 334 684 74 ILE CB C 41.15 0.00 1 335 684 74 ILE CG1 C 27.30 0.00 1 336 684 74 ILE CG2 C 17.16 0.00 1 337 684 74 ILE CD1 C 13.39 0.00 1 338 684 74 ILE N N 123.27 0.00 1 339 685 75 ILE H H 8.66 0.00 1 340 685 75 ILE C C 174.00 0.00 1 341 685 75 ILE CA C 60.57 0.00 1 342 685 75 ILE CB C 38.55 0.00 1 343 685 75 ILE CG1 C 27.42 0.00 1 344 685 75 ILE CG2 C 17.10 0.00 1 345 685 75 ILE CD1 C 13.20 0.00 1 346 685 75 ILE N N 128.72 0.00 1 347 686 76 VAL H H 8.65 0.00 1 348 686 76 VAL C C 173.99 0.00 1 349 686 76 VAL CA C 60.60 0.00 1 350 686 76 VAL CB C 32.36 0.00 1 351 686 76 VAL CG1 C 19.50 0.00 2 352 686 76 VAL CG2 C 20.99 0.00 2 353 686 76 VAL N N 129.49 0.00 1 354 687 77 LYS H H 9.18 0.00 1 355 687 77 LYS C C 174.69 0.00 1 356 687 77 LYS CA C 54.01 0.00 1 357 687 77 LYS CB C 34.49 0.00 1 358 687 77 LYS CG C 24.35 0.00 1 359 687 77 LYS CD C 28.97 0.00 1 360 687 77 LYS CE C 41.11 0.00 1 361 687 77 LYS N N 128.63 0.00 1 362 688 78 ILE H H 8.43 0.00 1 363 688 78 ILE C C 173.87 0.00 1 364 688 78 ILE CA C 60.19 0.00 1 365 688 78 ILE CB C 39.70 0.00 1 366 688 78 ILE CG1 C 15.82 0.00 1 367 688 78 ILE CG2 C 13.38 0.00 1 368 688 78 ILE N N 125.09 0.00 1 369 689 79 LYS H H 9.04 0.00 1 370 689 79 LYS C C 172.81 0.00 1 371 689 79 LYS CA C 55.18 0.00 1 372 689 79 LYS CB C 33.86 0.00 1 373 689 79 LYS CE C 41.73 0.00 1 374 689 79 LYS N N 130.66 0.00 1 375 690 80 ALA H H 7.92 0.00 1 376 690 80 ALA C C 175.36 0.00 1 377 690 80 ALA CA C 51.28 0.00 1 378 690 80 ALA CB C 19.01 0.00 1 379 690 80 ALA N N 133.13 0.00 1 380 691 81 LYS H H 8.89 0.00 1 381 691 81 LYS C C 176.77 0.00 1 382 691 81 LYS CA C 60.11 0.00 1 383 691 81 LYS CB C 32.61 0.00 1 384 691 81 LYS N N 129.13 0.00 1 385 693 83 GLU H H 8.78 0.00 1 386 693 83 GLU C C 174.81 0.00 1 387 693 83 GLU CA C 54.84 0.00 1 388 693 83 GLU CB C 30.11 0.00 1 389 693 83 GLU CG C 36.40 0.00 1 390 693 83 GLU N N 124.60 0.00 1 391 694 84 LYS H H 8.58 0.00 1 392 694 84 LYS C C 174.75 0.00 1 393 694 84 LYS CA C 54.84 0.00 1 394 694 84 LYS CB C 35.60 0.00 1 395 694 84 LYS CG C 24.54 0.00 1 396 694 84 LYS CD C 28.11 0.00 1 397 694 84 LYS CE C 41.68 0.00 1 398 694 84 LYS N N 127.99 0.00 1 399 695 85 THR H H 8.45 0.00 1 400 695 85 THR C C 172.37 0.00 1 401 695 85 THR CA C 60.97 0.00 1 402 695 85 THR CB C 70.30 0.00 1 403 695 85 THR CG2 C 21.04 0.00 1 404 695 85 THR N N 121.24 0.00 1 405 696 86 ASP H H 9.23 0.00 1 406 696 86 ASP C C 172.54 0.00 1 407 696 86 ASP CA C 52.39 0.00 1 408 696 86 ASP CB C 46.00 0.00 1 409 696 86 ASP N N 128.28 0.00 1 410 697 87 TYR H H 8.56 0.00 1 411 697 87 TYR C C 173.75 0.00 1 412 697 87 TYR CA C 56.85 0.00 1 413 697 87 TYR CB C 39.31 0.00 1 414 697 87 TYR N N 120.66 0.00 1 415 698 88 LEU H H 9.26 0.00 1 416 698 88 LEU C C 174.11 0.00 1 417 698 88 LEU CA C 53.43 0.00 1 418 698 88 LEU CB C 43.29 0.00 1 419 698 88 LEU CG C 26.94 0.00 1 420 698 88 LEU CD1 C 25.13 0.00 2 421 698 88 LEU CD2 C 22.61 0.00 2 422 698 88 LEU N N 130.93 0.00 1 423 699 89 VAL H H 8.80 0.00 1 424 699 89 VAL C C 173.76 0.00 1 425 699 89 VAL CA C 59.16 0.00 1 426 699 89 VAL CB C 31.39 0.00 1 427 699 89 VAL N N 129.45 0.00 1 428 701 91 GLU H H 8.87 0.00 1 429 701 91 GLU C C 174.39 0.00 1 430 701 91 GLU CA C 54.07 0.00 1 431 701 91 GLU CB C 30.68 0.00 1 432 701 91 GLU CG C 35.84 0.00 1 433 701 91 GLU N N 120.73 0.00 1 434 702 92 GLN H H 8.40 0.00 1 435 702 92 GLN C C 175.98 0.00 1 436 702 92 GLN CA C 57.54 0.00 1 437 702 92 GLN CB C 28.61 0.00 1 438 702 92 GLN CG C 33.64 0.00 1 439 702 92 GLN N N 118.85 0.00 1 440 703 93 GLY H H 7.51 0.00 1 441 703 93 GLY C C 172.68 0.00 1 442 703 93 GLY CA C 41.62 0.00 1 443 703 93 GLY N N 104.18 0.00 1 444 704 94 TYR H H 8.51 0.00 1 445 704 94 TYR C C 177.78 0.00 1 446 704 94 TYR CA C 60.24 0.00 1 447 704 94 TYR CB C 39.33 0.00 1 448 704 94 TYR N N 117.55 0.00 1 449 705 95 THR H H 8.24 0.00 1 450 705 95 THR C C 173.16 0.00 1 451 705 95 THR CA C 60.06 0.00 1 452 705 95 THR CB C 73.17 0.00 1 453 705 95 THR CG2 C 21.90 0.00 1 454 705 95 THR N N 113.17 0.00 1 455 706 96 LYS H H 8.74 0.00 1 456 706 96 LYS C C 175.43 0.00 1 457 706 96 LYS CA C 55.12 0.00 1 458 706 96 LYS CB C 34.18 0.00 1 459 706 96 LYS CD C 29.34 0.00 1 460 706 96 LYS CE C 41.61 0.00 1 461 706 96 LYS N N 127.71 0.00 1 462 707 97 PHE H H 8.54 0.00 1 463 707 97 PHE C C 173.44 0.00 1 464 707 97 PHE CA C 54.80 0.00 1 465 707 97 PHE CB C 40.96 0.00 1 466 707 97 PHE N N 126.12 0.00 1 467 708 98 SER H H 7.79 0.00 1 468 708 98 SER C C 171.47 0.00 1 469 708 98 SER CA C 57.63 0.00 1 470 708 98 SER CB C 65.55 0.00 1 471 708 98 SER N N 113.91 0.00 1 472 709 99 TYR H H 9.47 0.00 1 473 709 99 TYR C C 174.04 0.00 1 474 709 99 TYR CA C 57.54 0.00 1 475 709 99 TYR CB C 43.02 0.00 1 476 709 99 TYR N N 123.86 0.00 1 477 710 100 GLU H H 8.96 0.00 1 478 710 100 GLU C C 176.10 0.00 1 479 710 100 GLU CA C 54.98 0.00 1 480 710 100 GLU CB C 31.63 0.00 1 481 710 100 GLU CG C 36.55 0.00 1 482 710 100 GLU N N 124.80 0.00 1 483 711 101 PHE H H 9.18 0.00 1 484 711 101 PHE C C 171.12 0.00 1 485 711 101 PHE CA C 55.96 0.00 1 486 711 101 PHE CB C 41.39 0.00 1 487 711 101 PHE N N 120.25 0.00 1 488 712 102 GLU H H 8.89 0.00 1 489 712 102 GLU C C 174.55 0.00 1 490 712 102 GLU CA C 53.70 0.00 1 491 712 102 GLU CB C 34.36 0.00 1 492 712 102 GLU CG C 36.62 0.00 1 493 712 102 GLU N N 120.72 0.00 1 494 713 103 THR H H 8.99 0.00 1 495 713 103 THR C C 175.28 0.00 1 496 713 103 THR CA C 58.70 0.00 1 497 713 103 THR CB C 70.74 0.00 1 498 713 103 THR CG2 C 23.53 0.00 1 499 713 103 THR N N 111.51 0.00 1 500 714 104 THR H H 8.51 0.00 1 501 714 104 THR C C 172.22 0.00 1 502 714 104 THR CA C 58.80 0.00 1 503 714 104 THR CB C 67.49 0.00 1 504 714 104 THR CG2 C 21.37 0.00 1 505 714 104 THR N N 112.60 0.00 1 506 715 105 GLU H H 7.98 0.00 1 507 715 105 GLU C C 176.02 0.00 1 508 715 105 GLU CA C 53.20 0.00 1 509 715 105 GLU CB C 30.15 0.00 1 510 715 105 GLU CG C 39.35 0.00 1 511 715 105 GLU N N 119.42 0.00 1 512 716 106 LYS H H 8.67 0.00 1 513 716 106 LYS C C 174.54 0.00 1 514 716 106 LYS CA C 56.84 0.00 1 515 716 106 LYS CB C 31.30 0.00 1 516 716 106 LYS CG C 24.64 0.00 1 517 716 106 LYS CD C 31.56 0.00 1 518 716 106 LYS CE C 41.70 0.00 1 519 716 106 LYS N N 122.44 0.00 1 520 717 107 ASP H H 7.65 0.00 1 521 717 107 ASP C C 175.44 0.00 1 522 717 107 ASP CA C 52.72 0.00 1 523 717 107 ASP CB C 40.04 0.00 1 524 717 107 ASP N N 123.97 0.00 1 525 718 108 SER H H 7.55 0.00 1 526 718 108 SER CA C 57.79 0.00 1 527 718 108 SER CB C 63.18 0.00 1 528 718 108 SER N N 113.65 0.00 1 529 719 109 SER H H 8.01 0.00 1 530 719 109 SER C C 172.08 0.00 1 531 719 109 SER CA C 58.29 0.00 1 532 719 109 SER CB C 63.78 0.00 1 533 719 109 SER N N 118.28 0.00 1 534 720 110 ASN H H 8.20 0.00 1 535 720 110 ASN C C 174.94 0.00 1 536 720 110 ASN CA C 52.10 0.00 1 537 720 110 ASN CB C 40.14 0.00 1 538 720 110 ASN N N 115.90 0.00 1 539 721 111 ILE H H 8.68 0.00 1 540 721 111 ILE C C 175.04 0.00 1 541 721 111 ILE CA C 58.83 0.00 1 542 721 111 ILE CB C 37.20 0.00 1 543 721 111 ILE CG1 C 24.111 0.00 1 544 721 111 ILE CG2 C 17.194 0.00 1 545 721 111 ILE CD1 C 12.73 0.00 1 546 721 111 ILE N N 123.24 0.00 1 547 722 112 GLU H H 8.16 0.00 1 548 722 112 GLU C C 174.34 0.00 1 549 722 112 GLU CA C 53.85 0.00 1 550 722 112 GLU CB C 32.31 0.00 1 551 722 112 GLU CG C 35.94 0.00 1 552 722 112 GLU N N 125.89 0.00 1 553 723 113 ILE H H 8.14 0.00 1 554 723 113 ILE C C 173.23 0.00 1 555 723 113 ILE CA C 60.39 0.00 1 556 723 113 ILE CB C 39.508 0.00 1 557 723 113 ILE CG2 C 16.114 0.00 1 558 723 113 ILE CD1 C 12.73 0.00 1 559 723 113 ILE N N 126.65 0.00 1 560 724 114 THR H H 8.96 0.00 1 561 724 114 THR C C 172.13 0.00 1 562 724 114 THR CA C 61.02 0.00 1 563 724 114 THR CB C 70.44 0.00 1 564 724 114 THR CG2 C 21.43 0.00 1 565 724 114 THR N N 123.29 0.00 1 566 725 115 LEU H H 9.20 0.00 1 567 725 115 LEU C C 174.68 0.00 1 568 725 115 LEU CA C 54.18 0.00 1 569 725 115 LEU CB C 42.44 0.00 1 570 725 115 LEU CG C 28.60 0.00 1 571 725 115 LEU CD1 C 26.16 0.00 1 572 725 115 LEU CD2 C 26.16 0.00 1 573 725 115 LEU N N 127.18 0.00 1 574 726 116 ILE H H 9.00 0.00 1 575 726 116 ILE C C 175.85 0.00 1 576 726 116 ILE CA C 60.08 0.00 1 577 726 116 ILE CB C 39.37 0.00 1 578 726 116 ILE CG1 C 22.33 0.00 1 579 726 116 ILE CD1 C 13.66 0.00 1 580 726 116 ILE N N 122.26 0.00 1 581 727 117 GLY H H 8.88 0.00 1 582 727 117 GLY C C 173.92 0.00 1 583 727 117 GLY CA C 44.04 0.00 1 584 727 117 GLY N N 117.41 0.00 1 585 728 118 SER H H 8.25 0.00 1 586 728 118 SER C C 174.25 0.00 1 587 728 118 SER CA C 57.13 0.00 1 588 728 118 SER CB C 64.87 0.00 1 589 728 118 SER N N 117.85 0.00 1 590 729 119 GLY H H 8.47 0.00 1 591 729 119 GLY C C 173.48 0.00 1 592 729 119 GLY CA C 46.09 0.00 1 593 729 119 GLY N N 111.28 0.00 1 594 730 120 THR H H 7.80 0.00 1 595 730 120 THR C C 172.23 0.00 1 596 730 120 THR CA C 61.41 0.00 1 597 730 120 THR CB C 68.94 0.00 1 598 730 120 THR CG2 C 21.84 0.00 1 599 730 120 THR N N 119.17 0.00 1 600 731 121 THR H H 8.05 0.00 1 601 731 121 THR C C 174.90 0.00 1 602 731 121 THR CA C 57.06 0.00 1 603 731 121 THR CB C 65.06 0.00 1 604 731 121 THR N N 112.96 0.00 1 605 733 123 LEU H H 8.46 0.00 1 606 733 123 LEU CA C 51.64 0.00 1 607 733 123 LEU CB C 47.12 0.00 1 608 733 123 LEU CG C 27.24 0.00 1 609 733 123 LEU CD1 C 24.53 0.00 1 610 733 123 LEU CD2 C 24.53 0.00 1 611 733 123 LEU N N 119.76 0.00 1 612 734 124 ASP H H 9.14 0.00 1 613 734 124 ASP C C 174.14 0.00 1 614 734 124 ASP CA C 51.45 0.00 1 615 734 124 ASP CB C 43.78 0.00 1 616 734 124 ASP N N 118.30 0.00 1 617 735 125 ASN H H 8.65 0.00 1 618 735 125 ASN C C 173.75 0.00 1 619 735 125 ASN CA C 53.49 0.00 1 620 735 125 ASN CB C 35.75 0.00 1 621 735 125 ASN N N 120.25 0.00 1 622 736 126 LEU H H 6.82 0.00 1 623 736 126 LEU C C 178.61 0.00 1 624 736 126 LEU CA C 53.68 0.00 1 625 736 126 LEU CB C 42.22 0.00 1 626 736 126 LEU CG C 26.86 0.00 1 627 736 126 LEU CD1 C 24.38 0.00 1 628 736 126 LEU CD2 C 24.38 0.00 1 629 736 126 LEU N N 117.01 0.00 1 630 737 127 SER H H 10.20 0.00 1 631 737 127 SER C C 172.67 0.00 1 632 737 127 SER CA C 57.10 0.00 1 633 737 127 SER CB C 67.45 0.00 1 634 737 127 SER N N 125.12 0.00 1 635 738 128 ILE H H 9.12 0.00 1 636 738 128 ILE C C 175.35 0.00 1 637 738 128 ILE CA C 60.17 0.00 1 638 738 128 ILE CB C 40.72 0.00 1 639 738 128 ILE CG1 C 22.51 0.00 1 640 738 128 ILE CD1 C 13.50 0.00 1 641 738 128 ILE N N 121.45 0.00 1 642 739 129 THR H H 9.07 0.00 1 643 739 129 THR C C 172.00 0.00 1 644 739 129 THR CA C 61.58 0.00 1 645 739 129 THR CB C 70.84 0.00 1 646 739 129 THR N N 125.32 0.00 1 647 740 130 GLU H H 8.87 0.00 1 648 740 130 GLU C C 174.81 0.00 1 649 740 130 GLU CA C 56.21 0.00 1 650 740 130 GLU CB C 30.18 0.00 1 651 740 130 GLU CG C 35.287 0.00 1 652 740 130 GLU N N 129.77 0.00 1 653 741 131 LEU H H 8.21 0.00 1 654 741 131 LEU C C 175.86 0.00 1 655 741 131 LEU CA C 53.85 0.00 1 656 741 131 LEU CB C 41.74 0.00 1 657 741 131 LEU CG C 26.56 0.00 1 658 741 131 LEU CD1 C 23.93 0.00 1 659 741 131 LEU CD2 C 23.93 0.00 1 660 741 131 LEU N N 127.45 0.00 1 661 742 132 ASN H H 8.53 0.00 1 662 742 132 ASN C C 174.50 0.00 1 663 742 132 ASN CA C 52.52 0.00 1 664 742 132 ASN CB C 38.80 0.00 1 665 742 132 ASN N N 122.13 0.00 1 666 744 134 THR H H 8.21 0.00 1 667 744 134 THR C C 172.29 0.00 1 668 744 134 THR CA C 59.28 0.00 1 669 744 134 THR CB C 69.27 0.00 1 670 744 134 THR N N 119.19 0.00 1 671 746 136 GLU H H 7.97 0.00 1 672 746 136 GLU C C 180.72 0.00 1 673 746 136 GLU CA C 57.59 0.00 1 674 746 136 GLU CB C 30.79 0.00 1 675 746 136 GLU N N 127.41 0.00 1 stop_ save_