data_6779 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the type 1 pilus assembly platform FimD(25-125) ; _BMRB_accession_number 6779 _BMRB_flat_file_name bmr6779.str _Entry_type original _Submission_date 2005-08-17 _Accession_date 2005-08-17 _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 Nishiyama M. . . 2 Horst R. . . 3 Herrmann R. . . 4 Vetsch M. . . 5 Bettendorff P. . . 6 Ignatov O. . . 7 Grutter M. . . 8 Wuthrich K. . . 9 Glockshuber R. . . 10 Capitani G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 525 "13C chemical shifts" 310 "15N chemical shifts" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-18 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6629 FimD(25-139) stop_ _Original_release_date 2005-10-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15920478 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishiyama M. . . 2 Horst R. . . 3 Herrmann R. . . 4 Vetsch M. . . 5 Bettendorff P. . . 6 Ignatov O. . . 7 Grutter M. . . 8 Wuthrich K. . . 9 Glockshuber R. . . 10 Capitani G. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 24 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2075 _Page_last 2086 _Year 2005 _Details . loop_ _Keyword 'BETA SHEET' 'ALPHA HELIX' FimD stop_ save_ ################################## # Molecular system description # ################################## save_system_FimD _Saveframe_category molecular_system _Mol_system_name 'Outer membrane usher protein fimD' _Abbreviation_common FimD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Outer membrane usher protein FimD' $FimD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FimD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FimD _Abbreviation_common FimD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; GQELPPGTYRVDIYLNNGYM ATRDVTFNTGDSEQGIVPCL TRAQLASMGLNTASVAGMNL LADDACVPLTTMVQDATAHL DVGQQRLNLTIPQAFMSNRA R ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 25 GLY 2 26 GLN 3 27 GLU 4 28 LEU 5 29 PRO 6 30 PRO 7 31 GLY 8 32 THR 9 33 TYR 10 34 ARG 11 35 VAL 12 36 ASP 13 37 ILE 14 38 TYR 15 39 LEU 16 40 ASN 17 41 ASN 18 42 GLY 19 43 TYR 20 44 MET 21 45 ALA 22 46 THR 23 47 ARG 24 48 ASP 25 49 VAL 26 50 THR 27 51 PHE 28 52 ASN 29 53 THR 30 54 GLY 31 55 ASP 32 56 SER 33 57 GLU 34 58 GLN 35 59 GLY 36 60 ILE 37 61 VAL 38 62 PRO 39 63 CYS 40 64 LEU 41 65 THR 42 66 ARG 43 67 ALA 44 68 GLN 45 69 LEU 46 70 ALA 47 71 SER 48 72 MET 49 73 GLY 50 74 LEU 51 75 ASN 52 76 THR 53 77 ALA 54 78 SER 55 79 VAL 56 80 ALA 57 81 GLY 58 82 MET 59 83 ASN 60 84 LEU 61 85 LEU 62 86 ALA 63 87 ASP 64 88 ASP 65 89 ALA 66 90 CYS 67 91 VAL 68 92 PRO 69 93 LEU 70 94 THR 71 95 THR 72 96 MET 73 97 VAL 74 98 GLN 75 99 ASP 76 100 ALA 77 101 THR 78 102 ALA 79 103 HIS 80 104 LEU 81 105 ASP 82 106 VAL 83 107 GLY 84 108 GLN 85 109 GLN 86 110 ARG 87 111 LEU 88 112 ASN 89 113 LEU 90 114 THR 91 115 ILE 92 116 PRO 93 117 GLN 94 118 ALA 95 119 PHE 96 120 MET 97 121 SER 98 122 ASN 99 123 ARG 100 124 ALA 101 125 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 6629 FimD 100.00 115 100.00 100.00 5.00e-66 PDB 1ZDV "Solution Structure Of The Type 1 Pilus Assembly Platform Fimd(25-139)" 100.00 115 100.00 100.00 5.00e-66 PDB 1ZDX "Solution Structure Of The Type 1 Pilus Assembly Platform Fimd(25-125)" 100.00 101 100.00 100.00 1.20e-66 PDB 1ZE3 "Crystal Structure Of The Ternary Complex Of Fimd (N- Terminal Domain) With Fimc And The Pilin Domain Of Fimh" 100.00 125 100.00 100.00 3.75e-66 PDB 3BWU "Crystal Structure Of The Ternary Complex Of Fimd (n-terminal Domain, Fimdn) With Fimc And The N-terminally Truncated Pilus Subu" 100.00 125 100.00 100.00 3.75e-66 PDB 3RFZ "Crystal Structure Of The Fimd Usher Bound To Its Cognate Fimc:fimh Substrate" 100.00 843 100.00 100.00 2.06e-61 PDB 4J3O "Crystal Structure Of The Fimd Usher Traversed By The Pilus Tip Complex Assembly Composed Of Fimc:fimf:fimg:fimh" 100.00 843 100.00 100.00 2.06e-61 DBJ BAB38699 "export and assembly outer membrane protein of type 1 fimbriae [Escherichia coli O157:H7 str. Sakai]" 100.00 878 100.00 100.00 2.96e-61 DBJ BAE78310 "outer membrane usher protein, type 1 fimbrial synthesis [Escherichia coli str. K-12 substr. W3110]" 100.00 878 100.00 100.00 2.90e-61 DBJ BAI28636 "outer membrane usher protein FimD [Escherichia coli O26:H11 str. 11368]" 100.00 878 100.00 100.00 3.29e-61 DBJ BAI33777 "outer membrane usher protein FimD [Escherichia coli O103:H2 str. 12009]" 100.00 878 98.02 100.00 1.02e-60 DBJ BAJ46031 "outer membrane protein; export and assembly of type 1 fimbriae [Escherichia coli DH1]" 100.00 878 100.00 100.00 2.90e-61 EMBL CAQ34665 "outer membrane protein; export and assembly of type 1 fimbriae [Escherichia coli BL21(DE3)]" 100.00 878 100.00 100.00 3.39e-61 EMBL CAR16035 "outer membrane usher protein, type 1 fimbrial synthesis [Escherichia coli UMN026]" 100.00 878 100.00 100.00 3.39e-61 EMBL CCP96085 "type 1 fimbriae anchoring protein FimD [Escherichia coli O10:K5(L):H4 str. ATCC 23506]" 100.00 856 100.00 100.00 3.10e-61 EMBL CCQ07908 "type 1 fimbriae anchoring protein FimD [Escherichia coli Nissle 1917]" 100.00 856 99.01 99.01 1.67e-60 EMBL CCW23202 "outer membrane usher protein FimD precursor [Escherichia coli O25b:H4-ST131 str. EC958]" 100.00 878 99.01 99.01 2.08e-60 GB AAA97213 "CG Site No. 18349 [Escherichia coli str. K-12 substr. MG1655]" 100.00 878 100.00 100.00 2.90e-61 GB AAC77273 "fimbrial usher outer membrane porin protein; FimCD chaperone-usher [Escherichia coli str. K-12 substr. MG1655]" 100.00 878 100.00 100.00 2.90e-61 GB AAG59499 "outer membrane protein; export and assembly of type 1 fimbriae, interrupted [Escherichia coli O157:H7 str. EDL933]" 100.00 878 100.00 100.00 3.20e-61 GB AAY89700 "FimD [Escherichia coli LW1655F+]" 100.00 148 100.00 100.00 3.58e-66 GB ABF06193 "Outer membrane usher protein fimD precursor [Shigella flexneri 5 str. 8401]" 100.00 878 99.01 99.01 7.35e-60 REF NP_290933 "outer membrane protein; export and assembly of type 1 fimbriae, interrupted [Escherichia coli O157:H7 str. EDL933]" 100.00 878 100.00 100.00 3.20e-61 REF NP_313303 "protein FimD [Escherichia coli O157:H7 str. Sakai]" 100.00 878 100.00 100.00 2.96e-61 REF NP_418737 "fimbrial usher outer membrane porin protein; FimCD chaperone-usher [Escherichia coli str. K-12 substr. MG1655]" 100.00 878 100.00 100.00 2.90e-61 REF WP_000120908 "fimbrial protein FimD [Escherichia coli]" 100.00 878 99.01 99.01 1.67e-60 REF WP_000120909 "fimbrial protein FimD [Escherichia coli]" 100.00 878 99.01 99.01 1.92e-60 SP P30130 "RecName: Full=Outer membrane usher protein FimD; Flags: Precursor [Escherichia coli K-12]" 100.00 878 100.00 100.00 2.90e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FimD 'E. coli' 562 Eubacteria . Escherichia coli 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 $FimD 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FimD 2 mM '[U-13C; U-15N]' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task collection stop_ _Details Bruker save_ save_ATHNOS-CANDID _Saveframe_category software _Name ATHNOS-CANDID _Version . loop_ _Task 'structure solution' refinement stop_ _Details Herrmann save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 293 0.5 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 15N-separated NOESY' '3D 13C-separated NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Outer membrane usher protein FimD' _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 GLN CA C 54.745 . . 2 . 2 GLN HA H 4.284 . . 3 . 2 GLN CB C 28.828 . . 4 . 2 GLN HB2 H 1.870 . . 5 . 2 GLN HB3 H 2.000 . . 6 . 2 GLN CG C 33.193 . . 7 . 2 GLN HG2 H 2.225 . . 8 . 2 GLN NE2 N 112.451 . . 9 . 2 GLN HE21 H 6.831 . . 10 . 2 GLN HE22 H 7.544 . . 11 . 3 GLU H H 8.555 . . 12 . 3 GLU N N 122.605 . . 13 . 3 GLU CA C 55.998 . . 14 . 3 GLU HA H 4.083 . . 15 . 3 GLU CB C 29.101 . . 16 . 3 GLU HB2 H 1.870 . . 17 . 3 GLU HB3 H 1.801 . . 18 . 3 GLU CG C 35.460 . . 19 . 3 GLU HG2 H 2.082 . . 20 . 3 GLU HG3 H 2.154 . . 21 . 4 LEU H H 8.115 . . 22 . 4 LEU N N 124.085 . . 23 . 4 LEU CA C 51.254 . . 24 . 4 LEU HA H 4.580 . . 25 . 4 LEU CB C 42.668 . . 26 . 4 LEU HB2 H 1.197 . . 27 . 4 LEU HB3 H 1.459 . . 28 . 4 LEU CG C 26.237 . . 29 . 4 LEU CD1 C 25.325 . . 30 . 4 LEU HD1 H 0.463 . . 31 . 4 LEU CD2 C 22.497 . . 32 . 4 LEU HD2 H 0.645 . . 33 . 4 LEU HG H 3.062 . . 34 . 5 PRO CG C 25.977 . . 35 . 5 PRO HG2 H 1.466 . . 36 . 5 PRO HG3 H 1.902 . . 37 . 5 PRO CD C 49.377 . . 38 . 5 PRO HD2 H 3.464 . . 39 . 5 PRO HD3 H 3.631 . . 40 . 6 PRO CA C 62.333 . . 41 . 6 PRO HA H 4.163 . . 42 . 6 PRO CB C 31.697 . . 43 . 6 PRO HB2 H 2.116 . . 44 . 6 PRO HB3 H 2.165 . . 45 . 6 PRO CG C 26.587 . . 46 . 6 PRO HG2 H 1.899 . . 47 . 6 PRO HG3 H 1.966 . . 48 . 6 PRO CD C 49.397 . . 49 . 6 PRO HD2 H 3.581 . . 50 . 6 PRO HD3 H 3.465 . . 51 . 7 GLY H H 8.205 . . 52 . 7 GLY N N 107.291 . . 53 . 7 GLY CA C 43.988 . . 54 . 7 GLY HA2 H 4.067 . . 55 . 7 GLY HA3 H 3.820 . . 56 . 8 THR H H 8.425 . . 57 . 8 THR N N 118.325 . . 58 . 8 THR CA C 61.712 . . 59 . 8 THR HA H 4.913 . . 60 . 8 THR CB C 68.662 . . 61 . 8 THR HB H 3.678 . . 62 . 8 THR CG2 C 20.899 . . 63 . 8 THR HG2 H 0.863 . . 64 . 9 TYR H H 9.010 . . 65 . 9 TYR N N 126.933 . . 66 . 9 TYR CA C 55.669 . . 67 . 9 TYR HA H 4.575 . . 68 . 9 TYR CB C 40.512 . . 69 . 9 TYR HB2 H 2.514 . . 70 . 9 TYR HB3 H 2.661 . . 71 . 9 TYR CD1 C 133.295 . . 72 . 9 TYR HD1 H 6.821 . . 73 . 9 TYR CE1 C 130.550 . . 74 . 9 TYR HE1 H 7.051 . . 75 . 10 ARG H H 8.612 . . 76 . 10 ARG N N 126.383 . . 77 . 10 ARG CA C 55.624 . . 78 . 10 ARG HA H 4.574 . . 79 . 10 ARG CB C 27.867 . . 80 . 10 ARG HB2 H 1.664 . . 81 . 10 ARG CG C 26.558 . . 82 . 10 ARG HG2 H 1.265 . . 83 . 10 ARG HG3 H 1.122 . . 84 . 10 ARG CD C 42.085 . . 85 . 10 ARG HD2 H 2.923 . . 86 . 10 ARG HD3 H 3.017 . . 87 . 10 ARG NE N 84.957 . . 88 . 10 ARG HE H 7.526 . . 89 . 11 VAL H H 8.547 . . 90 . 11 VAL N N 119.626 . . 91 . 11 VAL CA C 57.268 . . 92 . 11 VAL HA H 4.828 . . 93 . 11 VAL CB C 35.104 . . 94 . 11 VAL HB H 1.823 . . 95 . 11 VAL CG1 C 22.452 . . 96 . 11 VAL HG1 H 0.522 . . 97 . 11 VAL CG2 C 17.747 . . 98 . 11 VAL HG2 H 0.874 . . 99 . 12 ASP H H 8.482 . . 100 . 12 ASP N N 120.046 . . 101 . 12 ASP CA C 53.158 . . 102 . 12 ASP HA H 5.189 . . 103 . 12 ASP CB C 41.742 . . 104 . 12 ASP HB2 H 2.987 . . 105 . 12 ASP HB3 H 2.676 . . 106 . 13 ILE H H 9.515 . . 107 . 13 ILE N N 125.056 . . 108 . 13 ILE CA C 61.125 . . 109 . 13 ILE HA H 4.690 . . 110 . 13 ILE CB C 38.299 . . 111 . 13 ILE HB H 1.481 . . 112 . 13 ILE CG2 C 16.752 . . 113 . 13 ILE CG1 C 27.495 . . 114 . 13 ILE HG12 H 1.734 . . 115 . 13 ILE HG13 H 0.666 . . 116 . 13 ILE CD1 C 12.975 . . 117 . 13 ILE HD1 H 0.525 . . 118 . 13 ILE HG2 H 0.593 . . 119 . 14 TYR H H 9.317 . . 120 . 14 TYR N N 129.245 . . 121 . 14 TYR CA C 55.328 . . 122 . 14 TYR HA H 4.996 . . 123 . 14 TYR CB C 41.134 . . 124 . 14 TYR HB2 H 2.362 . . 125 . 14 TYR HB3 H 3.198 . . 126 . 14 TYR CD1 C 132.294 . . 127 . 14 TYR HD1 H 6.688 . . 128 . 14 TYR CE1 C 132.377 . . 129 . 14 TYR HE1 H 6.438 . . 130 . 15 LEU H H 8.950 . . 131 . 15 LEU N N 123.221 . . 132 . 15 LEU CA C 52.543 . . 133 . 15 LEU HA H 5.107 . . 134 . 15 LEU CB C 43.981 . . 135 . 15 LEU HB2 H 1.147 . . 136 . 15 LEU HB3 H 1.872 . . 137 . 15 LEU CG C 27.867 . . 138 . 15 LEU CD1 C 25.319 . . 139 . 15 LEU HD1 H 0.786 . . 140 . 15 LEU CD2 C 24.655 . . 141 . 15 LEU HD2 H 0.670 . . 142 . 15 LEU HG H 1.325 . . 143 . 16 ASN H H 9.453 . . 144 . 16 ASN N N 129.378 . . 145 . 16 ASN CA C 53.498 . . 146 . 16 ASN HA H 4.487 . . 147 . 16 ASN CB C 34.819 . . 148 . 16 ASN HB2 H 2.898 . . 149 . 16 ASN ND2 N 109.147 . . 150 . 16 ASN HD21 H 7.784 . . 151 . 16 ASN HD22 H 7.349 . . 152 . 17 ASN H H 9.305 . . 153 . 17 ASN N N 108.206 . . 154 . 17 ASN CA C 54.431 . . 155 . 17 ASN HA H 4.176 . . 156 . 17 ASN CB C 37.310 . . 157 . 17 ASN HB2 H 2.994 . . 158 . 17 ASN HB3 H 3.033 . . 159 . 17 ASN ND2 N 113.009 . . 160 . 17 ASN HD21 H 7.475 . . 161 . 17 ASN HD22 H 6.777 . . 162 . 18 GLY H H 8.068 . . 163 . 18 GLY N N 108.290 . . 164 . 18 GLY CA C 43.437 . . 165 . 18 GLY HA2 H 4.594 . . 166 . 18 GLY HA3 H 3.481 . . 167 . 19 TYR H H 8.781 . . 168 . 19 TYR N N 127.336 . . 169 . 19 TYR CA C 58.543 . . 170 . 19 TYR HA H 2.885 . . 171 . 19 TYR CB C 36.742 . . 172 . 19 TYR HB2 H 2.496 . . 173 . 19 TYR HB3 H 2.421 . . 174 . 19 TYR CD1 C 132.395 . . 175 . 19 TYR HD1 H 6.436 . . 176 . 19 TYR CE1 C 117.137 . . 177 . 19 TYR HE1 H 6.371 . . 178 . 20 MET H H 8.400 . . 179 . 20 MET N N 125.356 . . 180 . 20 MET CA C 53.468 . . 181 . 20 MET HA H 4.482 . . 182 . 20 MET CB C 33.861 . . 183 . 20 MET HB2 H 1.508 . . 184 . 20 MET HB3 H 1.460 . . 185 . 20 MET CG C 31.613 . . 186 . 20 MET HG2 H 2.524 . . 187 . 20 MET HG3 H 2.323 . . 188 . 20 MET CE C 17.374 . . 189 . 20 MET HE H 1.959 . . 190 . 21 ALA H H 6.531 . . 191 . 21 ALA N N 117.196 . . 192 . 21 ALA CA C 51.277 . . 193 . 21 ALA HA H 4.072 . . 194 . 21 ALA CB C 20.922 . . 195 . 21 ALA HB H 1.076 . . 196 . 22 THR H H 8.653 . . 197 . 22 THR N N 118.757 . . 198 . 22 THR CA C 61.416 . . 199 . 22 THR HA H 5.439 . . 200 . 22 THR CB C 70.297 . . 201 . 22 THR HB H 3.768 . . 202 . 22 THR CG2 C 19.327 . . 203 . 22 THR HG2 H 1.080 . . 204 . 23 ARG H H 8.810 . . 205 . 23 ARG N N 122.557 . . 206 . 23 ARG CA C 53.167 . . 207 . 23 ARG HA H 4.549 . . 208 . 23 ARG CB C 33.551 . . 209 . 23 ARG HB2 H 1.851 . . 210 . 23 ARG HB3 H 1.429 . . 211 . 23 ARG CG C 25.634 . . 212 . 23 ARG HG2 H 1.267 . . 213 . 23 ARG HG3 H 1.184 . . 214 . 23 ARG CD C 42.277 . . 215 . 23 ARG HD2 H 2.989 . . 216 . 23 ARG HD3 H 2.963 . . 217 . 24 ASP H H 8.358 . . 218 . 24 ASP N N 120.915 . . 219 . 24 ASP CA C 53.804 . . 220 . 24 ASP HA H 4.849 . . 221 . 24 ASP CB C 39.574 . . 222 . 24 ASP HB2 H 2.090 . . 223 . 24 ASP HB3 H 2.403 . . 224 . 25 VAL H H 9.058 . . 225 . 25 VAL N N 127.435 . . 226 . 25 VAL CA C 60.447 . . 227 . 25 VAL HA H 4.124 . . 228 . 25 VAL CB C 34.204 . . 229 . 25 VAL HB H 1.946 . . 230 . 25 VAL CG1 C 20.879 . . 231 . 25 VAL HG1 H 0.237 . . 232 . 25 VAL CG2 C 21.860 . . 233 . 25 VAL HG2 H 0.675 . . 234 . 26 THR H H 9.290 . . 235 . 26 THR N N 126.055 . . 236 . 26 THR CA C 62.942 . . 237 . 26 THR HA H 4.444 . . 238 . 26 THR CB C 68.680 . . 239 . 26 THR HB H 3.846 . . 240 . 26 THR CG2 C 21.215 . . 241 . 26 THR HG2 H 0.994 . . 242 . 27 PHE H H 9.456 . . 243 . 27 PHE N N 125.903 . . 244 . 27 PHE CA C 55.072 . . 245 . 27 PHE HA H 4.989 . . 246 . 27 PHE CB C 40.827 . . 247 . 27 PHE HB2 H 2.465 . . 248 . 27 PHE HB3 H 3.096 . . 249 . 27 PHE CD1 C 132.688 . . 250 . 27 PHE HD1 H 7.046 . . 251 . 27 PHE CE1 C 133.299 . . 252 . 27 PHE HE1 H 6.820 . . 253 . 27 PHE CZ C 116.458 . . 254 . 27 PHE HZ H 6.307 . . 255 . 28 ASN H H 8.317 . . 256 . 28 ASN N N 120.044 . . 257 . 28 ASN CA C 50.642 . . 258 . 28 ASN HA H 5.158 . . 259 . 28 ASN CB C 41.475 . . 260 . 28 ASN HB2 H 2.437 . . 261 . 28 ASN HB3 H 2.775 . . 262 . 28 ASN ND2 N 113.738 . . 263 . 28 ASN HD21 H 7.745 . . 264 . 28 ASN HD22 H 6.893 . . 265 . 29 THR H H 8.857 . . 266 . 29 THR N N 116.514 . . 267 . 29 THR CA C 63.292 . . 268 . 29 THR HA H 4.517 . . 269 . 29 THR CB C 68.397 . . 270 . 29 THR HB H 3.981 . . 271 . 29 THR CG2 C 21.239 . . 272 . 29 THR HG2 H 1.217 . . 273 . 30 GLY H H 7.928 . . 274 . 30 GLY N N 111.310 . . 275 . 30 GLY CA C 44.976 . . 276 . 30 GLY HA2 H 3.653 . . 277 . 30 GLY HA3 H 4.041 . . 278 . 31 ASP H H 8.255 . . 279 . 31 ASP N N 119.459 . . 280 . 31 ASP CA C 53.171 . . 281 . 31 ASP HA H 4.532 . . 282 . 31 ASP CB C 39.243 . . 283 . 31 ASP HB2 H 2.565 . . 284 . 31 ASP HB3 H 2.423 . . 285 . 32 SER H H 7.675 . . 286 . 32 SER N N 117.330 . . 287 . 32 SER CA C 56.374 . . 288 . 32 SER HA H 4.685 . . 289 . 32 SER CB C 64.899 . . 290 . 32 SER HB2 H 3.623 . . 291 . 32 SER HB3 H 4.174 . . 292 . 33 GLU CA C 58.509 . . 293 . 33 GLU HA H 4.092 . . 294 . 33 GLU CB C 28.792 . . 295 . 33 GLU HB2 H 2.054 . . 296 . 33 GLU HB3 H 2.251 . . 297 . 33 GLU CG C 35.760 . . 298 . 33 GLU HG2 H 2.282 . . 299 . 33 GLU HG3 H 2.255 . . 300 . 34 GLN H H 8.063 . . 301 . 34 GLN N N 113.614 . . 302 . 34 GLN CA C 55.651 . . 303 . 34 GLN HA H 4.420 . . 304 . 34 GLN CB C 29.756 . . 305 . 34 GLN HB2 H 1.919 . . 306 . 34 GLN HB3 H 2.030 . . 307 . 34 GLN CG C 34.518 . . 308 . 34 GLN HG2 H 2.367 . . 309 . 34 GLN HG3 H 2.267 . . 310 . 34 GLN NE2 N 114.473 . . 311 . 34 GLN HE21 H 7.669 . . 312 . 34 GLN HE22 H 7.594 . . 313 . 35 GLY H H 7.834 . . 314 . 35 GLY N N 108.131 . . 315 . 35 GLY CA C 44.942 . . 316 . 35 GLY HA2 H 3.854 . . 317 . 35 GLY HA3 H 4.203 . . 318 . 36 ILE H H 6.738 . . 319 . 36 ILE N N 109.728 . . 320 . 36 ILE CA C 57.592 . . 321 . 36 ILE HA H 5.219 . . 322 . 36 ILE CB C 43.029 . . 323 . 36 ILE HB H 1.545 . . 324 . 36 ILE CG2 C 17.099 . . 325 . 36 ILE CG1 C 23.082 . . 326 . 36 ILE HG12 H 1.025 . . 327 . 36 ILE HG13 H 0.684 . . 328 . 36 ILE CD1 C 12.671 . . 329 . 36 ILE HD1 H 0.101 . . 330 . 36 ILE HG2 H 0.600 . . 331 . 37 VAL H H 9.303 . . 332 . 37 VAL N N 117.035 . . 333 . 37 VAL CA C 56.690 . . 334 . 37 VAL HA H 4.759 . . 335 . 37 VAL CB C 33.796 . . 336 . 37 VAL HB H 2.048 . . 337 . 37 VAL CG1 C 21.146 . . 338 . 37 VAL HG1 H 0.788 . . 339 . 37 VAL CG2 C 17.723 . . 340 . 37 VAL HG2 H 0.662 . . 341 . 38 PRO CA C 60.804 . . 342 . 38 PRO HA H 3.361 . . 343 . 38 PRO CB C 31.054 . . 344 . 38 PRO HB2 H 0.973 . . 345 . 38 PRO HB3 H 1.105 . . 346 . 38 PRO CG C 25.290 . . 347 . 38 PRO HG2 H 1.575 . . 348 . 38 PRO HG3 H 1.896 . . 349 . 38 PRO CD C 48.749 . . 350 . 38 PRO HD2 H 3.578 . . 351 . 38 PRO HD3 H 3.686 . . 352 . 39 CYS H H 8.343 . . 353 . 39 CYS N N 122.484 . . 354 . 39 CYS CA C 56.055 . . 355 . 39 CYS HA H 4.584 . . 356 . 39 CYS CB C 44.632 . . 357 . 39 CYS HB2 H 3.323 . . 358 . 39 CYS HB3 H 2.571 . . 359 . 40 LEU H H 9.125 . . 360 . 40 LEU N N 130.763 . . 361 . 40 LEU CA C 52.212 . . 362 . 40 LEU HA H 4.856 . . 363 . 40 LEU CB C 43.299 . . 364 . 40 LEU HB2 H 1.600 . . 365 . 40 LEU HB3 H 1.039 . . 366 . 40 LEU CG C 26.570 . . 367 . 40 LEU CD1 C 25.942 . . 368 . 40 LEU HD1 H 0.592 . . 369 . 40 LEU HG H 1.201 . . 370 . 41 THR H H 8.159 . . 371 . 41 THR N N 111.716 . . 372 . 41 THR CA C 59.400 . . 373 . 41 THR HA H 4.686 . . 374 . 41 THR CB C 70.781 . . 375 . 41 THR HB H 4.697 . . 376 . 41 THR CG2 C 20.558 . . 377 . 41 THR HG2 H 0.959 . . 378 . 42 ARG H H 9.565 . . 379 . 42 ARG N N 122.330 . . 380 . 42 ARG CA C 59.811 . . 381 . 42 ARG HA H 3.626 . . 382 . 42 ARG CB C 28.795 . . 383 . 42 ARG HB2 H 1.947 . . 384 . 42 ARG HB3 H 1.497 . . 385 . 42 ARG CG C 26.600 . . 386 . 42 ARG HG2 H 1.485 . . 387 . 42 ARG HG3 H 0.861 . . 388 . 42 ARG CD C 43.055 . . 389 . 42 ARG HD2 H 3.186 . . 390 . 42 ARG HD3 H 2.908 . . 391 . 43 ALA H H 8.922 . . 392 . 43 ALA N N 119.759 . . 393 . 43 ALA CA C 53.819 . . 394 . 43 ALA HA H 4.044 . . 395 . 43 ALA CB C 17.415 . . 396 . 43 ALA HB H 1.285 . . 397 . 44 GLN H H 7.623 . . 398 . 44 GLN N N 118.706 . . 399 . 44 GLN CA C 57.945 . . 400 . 44 GLN HA H 3.750 . . 401 . 44 GLN CB C 27.214 . . 402 . 44 GLN HB2 H 1.580 . . 403 . 44 GLN HB3 H 2.233 . . 404 . 44 GLN CG C 33.528 . . 405 . 44 GLN HG2 H 2.196 . . 406 . 44 GLN HG3 H 2.318 . . 407 . 44 GLN NE2 N 109.023 . . 408 . 44 GLN HE21 H 6.651 . . 409 . 44 GLN HE22 H 7.252 . . 410 . 45 LEU H H 8.263 . . 411 . 45 LEU N N 120.053 . . 412 . 45 LEU CA C 57.278 . . 413 . 45 LEU HA H 3.797 . . 414 . 45 LEU CB C 40.199 . . 415 . 45 LEU HB2 H 1.745 . . 416 . 45 LEU HB3 H 1.135 . . 417 . 45 LEU CG C 26.276 . . 418 . 45 LEU CD1 C 25.325 . . 419 . 45 LEU HD1 H 0.577 . . 420 . 45 LEU CD2 C 21.846 . . 421 . 45 LEU HD2 H 0.582 . . 422 . 45 LEU HG H 1.535 . . 423 . 46 ALA H H 8.941 . . 424 . 46 ALA N N 123.638 . . 425 . 46 ALA CA C 53.833 . . 426 . 46 ALA HA H 4.555 . . 427 . 46 ALA CB C 17.113 . . 428 . 46 ALA HB H 1.436 . . 429 . 47 SER H H 7.994 . . 430 . 47 SER N N 114.761 . . 431 . 47 SER CA C 60.445 . . 432 . 47 SER HA H 4.178 . . 433 . 47 SER CB C 62.030 . . 434 . 47 SER HB2 H 3.867 . . 435 . 47 SER HB3 H 3.906 . . 436 . 48 MET H H 7.168 . . 437 . 48 MET N N 118.743 . . 438 . 48 MET CA C 55.400 . . 439 . 48 MET HA H 4.258 . . 440 . 48 MET CB C 32.908 . . 441 . 48 MET HB2 H 1.911 . . 442 . 48 MET HB3 H 2.201 . . 443 . 48 MET CG C 31.959 . . 444 . 48 MET HG2 H 2.693 . . 445 . 48 MET HG3 H 2.203 . . 446 . 48 MET CE C 16.010 . . 447 . 48 MET HE H 1.686 . . 448 . 49 GLY H H 7.473 . . 449 . 49 GLY N N 103.138 . . 450 . 49 GLY CA C 43.992 . . 451 . 49 GLY HA2 H 4.278 . . 452 . 49 GLY HA3 H 3.509 . . 453 . 50 LEU H H 7.586 . . 454 . 50 LEU N N 122.640 . . 455 . 50 LEU CA C 55.428 . . 456 . 50 LEU HA H 4.340 . . 457 . 50 LEU CB C 42.133 . . 458 . 50 LEU HB2 H 1.217 . . 459 . 50 LEU HB3 H 0.903 . . 460 . 50 LEU CG C 26.612 . . 461 . 50 LEU CD1 C 24.659 . . 462 . 50 LEU HD1 H 0.757 . . 463 . 50 LEU CD2 C 26.878 . . 464 . 50 LEU HD2 H 0.581 . . 465 . 50 LEU HG H 1.273 . . 466 . 51 ASN H H 9.186 . . 467 . 51 ASN N N 124.624 . . 468 . 51 ASN CA C 50.644 . . 469 . 51 ASN HA H 4.748 . . 470 . 51 ASN CB C 35.458 . . 471 . 51 ASN HB2 H 2.958 . . 472 . 51 ASN HB3 H 2.329 . . 473 . 51 ASN ND2 N 110.432 . . 474 . 51 ASN HD21 H 6.858 . . 475 . 51 ASN HD22 H 7.657 . . 476 . 52 THR H H 8.370 . . 477 . 52 THR N N 118.764 . . 478 . 52 THR CA C 64.566 . . 479 . 52 THR HA H 3.622 . . 480 . 52 THR CB C 66.843 . . 481 . 52 THR HB H 4.083 . . 482 . 52 THR CG2 C 21.514 . . 483 . 52 THR HG2 H 1.121 . . 484 . 53 ALA H H 7.692 . . 485 . 53 ALA N N 121.565 . . 486 . 53 ALA CA C 52.836 . . 487 . 53 ALA HA H 4.111 . . 488 . 53 ALA CB C 17.414 . . 489 . 53 ALA HB H 1.331 . . 490 . 54 SER H H 7.579 . . 491 . 54 SER N N 112.024 . . 492 . 54 SER CA C 58.553 . . 493 . 54 SER HA H 4.279 . . 494 . 54 SER CB C 63.596 . . 495 . 54 SER HB2 H 3.818 . . 496 . 54 SER HB3 H 4.011 . . 497 . 55 VAL H H 7.002 . . 498 . 55 VAL N N 122.623 . . 499 . 55 VAL CA C 60.145 . . 500 . 55 VAL HA H 4.035 . . 501 . 55 VAL CB C 31.354 . . 502 . 55 VAL HB H 1.972 . . 503 . 55 VAL CG1 C 19.926 . . 504 . 55 VAL HG1 H 0.645 . . 505 . 55 VAL CG2 C 21.845 . . 506 . 55 VAL HG2 H 0.643 . . 507 . 56 ALA H H 8.772 . . 508 . 56 ALA N N 132.954 . . 509 . 56 ALA CA C 53.225 . . 510 . 56 ALA HA H 4.025 . . 511 . 56 ALA CB C 16.787 . . 512 . 56 ALA HB H 1.299 . . 513 . 57 GLY H H 8.718 . . 514 . 57 GLY N N 109.149 . . 515 . 57 GLY CA C 44.930 . . 516 . 57 GLY HA2 H 4.140 . . 517 . 57 GLY HA3 H 3.511 . . 518 . 58 MET H H 7.908 . . 519 . 58 MET N N 122.907 . . 520 . 58 MET CA C 58.225 . . 521 . 58 MET HA H 3.807 . . 522 . 58 MET CB C 31.659 . . 523 . 58 MET HB2 H 2.124 . . 524 . 58 MET HB3 H 1.950 . . 525 . 58 MET CG C 33.207 . . 526 . 58 MET HG2 H 2.398 . . 527 . 58 MET HG3 H 2.343 . . 528 . 58 MET CE C 17.097 . . 529 . 58 MET HE H 1.732 . . 530 . 59 ASN H H 8.715 . . 531 . 59 ASN N N 115.617 . . 532 . 59 ASN CA C 53.808 . . 533 . 59 ASN HA H 4.224 . . 534 . 59 ASN CB C 36.058 . . 535 . 59 ASN HB2 H 2.706 . . 536 . 59 ASN ND2 N 112.153 . . 537 . 59 ASN HD21 H 7.521 . . 538 . 59 ASN HD22 H 6.750 . . 539 . 60 LEU H H 7.007 . . 540 . 60 LEU N N 117.400 . . 541 . 60 LEU CA C 53.825 . . 542 . 60 LEU HA H 4.158 . . 543 . 60 LEU CB C 41.298 . . 544 . 60 LEU HB2 H 1.490 . . 545 . 60 LEU HB3 H 1.570 . . 546 . 60 LEU CG C 25.948 . . 547 . 60 LEU CD1 C 24.348 . . 548 . 60 LEU HD1 H 0.802 . . 549 . 60 LEU CD2 C 21.514 . . 550 . 60 LEU HD2 H 0.670 . . 551 . 60 LEU HG H 1.423 . . 552 . 61 LEU H H 6.763 . . 553 . 61 LEU N N 117.937 . . 554 . 61 LEU CA C 53.544 . . 555 . 61 LEU HA H 4.097 . . 556 . 61 LEU CB C 41.894 . . 557 . 61 LEU HB2 H 1.434 . . 558 . 61 LEU HB3 H 1.607 . . 559 . 61 LEU CG C 26.287 . . 560 . 61 LEU CD1 C 26.565 . . 561 . 61 LEU HD1 H 0.860 . . 562 . 61 LEU CD2 C 21.943 . . 563 . 61 LEU HD2 H 0.720 . . 564 . 61 LEU HG H 1.661 . . 565 . 62 ALA H H 8.458 . . 566 . 62 ALA N N 124.348 . . 567 . 62 ALA CA C 51.277 . . 568 . 62 ALA HA H 4.247 . . 569 . 62 ALA CB C 18.392 . . 570 . 62 ALA HB H 1.396 . . 571 . 63 ASP H H 8.684 . . 572 . 63 ASP N N 120.102 . . 573 . 63 ASP CA C 56.330 . . 574 . 63 ASP HA H 4.153 . . 575 . 63 ASP CB C 39.990 . . 576 . 63 ASP HB3 H 2.494 . . 577 . 64 ASP H H 8.064 . . 578 . 64 ASP N N 112.462 . . 579 . 64 ASP CA C 51.694 . . 580 . 64 ASP HA H 4.520 . . 581 . 64 ASP CB C 39.257 . . 582 . 64 ASP HB2 H 2.448 . . 583 . 64 ASP HB3 H 2.681 . . 584 . 65 ALA H H 7.138 . . 585 . 65 ALA N N 122.370 . . 586 . 65 ALA CA C 51.317 . . 587 . 65 ALA HA H 4.053 . . 588 . 65 ALA CB C 19.244 . . 589 . 65 ALA HB H 1.298 . . 590 . 66 CYS H H 8.350 . . 591 . 66 CYS N N 118.196 . . 592 . 66 CYS CA C 52.216 . . 593 . 66 CYS HA H 4.143 . . 594 . 66 CYS CB C 39.225 . . 595 . 66 CYS HB2 H 3.218 . . 596 . 66 CYS HB3 H 2.570 . . 597 . 67 VAL H H 9.028 . . 598 . 67 VAL N N 128.000 . . 599 . 67 VAL CA C 60.123 . . 600 . 67 VAL HA H 3.820 . . 601 . 67 VAL CB C 31.707 . . 602 . 67 VAL HB H 1.843 . . 603 . 67 VAL CG1 C 19.306 . . 604 . 67 VAL HG1 H 0.504 . . 605 . 67 VAL CG2 C 21.496 . . 606 . 67 VAL HG2 H 0.841 . . 607 . 68 PRO CA C 60.491 . . 608 . 68 PRO HA H 4.823 . . 609 . 68 PRO CB C 26.582 . . 610 . 68 PRO HB2 H 1.973 . . 611 . 68 PRO HB3 H 1.835 . . 612 . 68 PRO CG C 32.716 . . 613 . 68 PRO HG2 H 2.238 . . 614 . 68 PRO HG3 H 2.479 . . 615 . 68 PRO CD C 50.020 . . 616 . 68 PRO HD2 H 3.531 . . 617 . 68 PRO HD3 H 3.859 . . 618 . 69 LEU H H 7.912 . . 619 . 69 LEU N N 127.482 . . 620 . 69 LEU CA C 58.588 . . 621 . 69 LEU HA H 3.420 . . 622 . 69 LEU CB C 42.704 . . 623 . 69 LEU HB2 H 1.643 . . 624 . 69 LEU HB3 H 1.244 . . 625 . 69 LEU CG C 25.339 . . 626 . 69 LEU CD1 C 19.293 . . 627 . 69 LEU HD1 H 0.500 . . 628 . 69 LEU CD2 C 22.188 . . 629 . 69 LEU HD2 H 0.578 . . 630 . 69 LEU HG H 0.579 . . 631 . 70 THR H H 7.831 . . 632 . 70 THR N N 103.022 . . 633 . 70 THR CA C 62.994 . . 634 . 70 THR HA H 3.957 . . 635 . 70 THR CB C 67.436 . . 636 . 70 THR HB H 4.376 . . 637 . 70 THR CG2 C 20.887 . . 638 . 70 THR HG2 H 1.121 . . 639 . 71 THR H H 7.162 . . 640 . 71 THR N N 112.195 . . 641 . 71 THR CA C 62.372 . . 642 . 71 THR HA H 4.226 . . 643 . 71 THR CB C 68.348 . . 644 . 71 THR HB H 4.040 . . 645 . 71 THR CG2 C 20.941 . . 646 . 71 THR HG2 H 1.077 . . 647 . 72 MET H H 7.789 . . 648 . 72 MET N N 118.937 . . 649 . 72 MET CA C 56.986 . . 650 . 72 MET HA H 4.105 . . 651 . 72 MET CB C 34.752 . . 652 . 72 MET HB2 H 1.648 . . 653 . 72 MET HB3 H 2.476 . . 654 . 72 MET CG C 32.910 . . 655 . 72 MET HG2 H 2.236 . . 656 . 72 MET HG3 H 2.487 . . 657 . 72 MET CE C 16.524 . . 658 . 72 MET HE H 1.861 . . 659 . 73 VAL H H 7.599 . . 660 . 73 VAL N N 119.132 . . 661 . 73 VAL CA C 59.756 . . 662 . 73 VAL HA H 3.544 . . 663 . 73 VAL CB C 29.419 . . 664 . 73 VAL HB H 1.928 . . 665 . 73 VAL CG1 C 21.213 . . 666 . 73 VAL HG1 H 0.091 . . 667 . 73 VAL CG2 C 19.964 . . 668 . 73 VAL HG2 H 0.326 . . 669 . 74 GLN H H 7.851 . . 670 . 74 GLN N N 126.055 . . 671 . 74 GLN CA C 57.283 . . 672 . 74 GLN HA H 3.752 . . 673 . 74 GLN CB C 27.846 . . 674 . 74 GLN HB2 H 1.873 . . 675 . 74 GLN HB3 H 1.966 . . 676 . 74 GLN CG C 32.890 . . 677 . 74 GLN HG2 H 2.219 . . 678 . 74 GLN HG3 H 2.251 . . 679 . 74 GLN NE2 N 113.049 . . 680 . 74 GLN HE21 H 6.771 . . 681 . 74 GLN HE22 H 7.548 . . 682 . 75 ASP H H 8.500 . . 683 . 75 ASP N N 116.465 . . 684 . 75 ASP CA C 55.376 . . 685 . 75 ASP HA H 4.169 . . 686 . 75 ASP CB C 38.619 . . 687 . 75 ASP HB2 H 2.780 . . 688 . 75 ASP HB3 H 2.984 . . 689 . 76 ALA H H 7.972 . . 690 . 76 ALA N N 122.361 . . 691 . 76 ALA CA C 51.567 . . 692 . 76 ALA HA H 4.685 . . 693 . 76 ALA CB C 19.003 . . 694 . 76 ALA HB H 1.225 . . 695 . 77 THR H H 8.597 . . 696 . 77 THR N N 108.864 . . 697 . 77 THR CA C 59.848 . . 698 . 77 THR HA H 4.688 . . 699 . 77 THR CB C 72.170 . . 700 . 77 THR HB H 4.049 . . 701 . 77 THR CG2 C 20.258 . . 702 . 77 THR HG2 H 0.978 . . 703 . 78 ALA H H 8.518 . . 704 . 78 ALA N N 121.210 . . 705 . 78 ALA CA C 50.623 . . 706 . 78 ALA HA H 5.105 . . 707 . 78 ALA CB C 21.218 . . 708 . 78 ALA HB H 1.097 . . 709 . 79 HIS H H 8.434 . . 710 . 79 HIS N N 121.207 . . 711 . 79 HIS CA C 55.672 . . 712 . 79 HIS HA H 4.588 . . 713 . 79 HIS CB C 33.553 . . 714 . 79 HIS HB2 H 2.886 . . 715 . 79 HIS HB3 H 2.947 . . 716 . 79 HIS HD1 H 9.213 . . 717 . 79 HIS CD2 C 119.289 . . 718 . 79 HIS HD2 H 6.710 . . 719 . 79 HIS CE1 C 138.155 . . 720 . 79 HIS HE1 H 7.611 . . 721 . 80 LEU H H 8.944 . . 722 . 80 LEU N N 130.520 . . 723 . 80 LEU CA C 52.865 . . 724 . 80 LEU HA H 4.550 . . 725 . 80 LEU CB C 42.084 . . 726 . 80 LEU HB2 H 1.290 . . 727 . 80 LEU HB3 H 0.754 . . 728 . 80 LEU CG C 25.975 . . 729 . 80 LEU CD1 C 23.431 . . 730 . 80 LEU HD1 H -0.762 . . 731 . 80 LEU CD2 C 21.524 . . 732 . 80 LEU HD2 H 0.149 . . 733 . 80 LEU HG H 0.630 . . 734 . 81 ASP H H 9.123 . . 735 . 81 ASP N N 128.069 . . 736 . 81 ASP CA C 51.256 . . 737 . 81 ASP HA H 4.643 . . 738 . 81 ASP CB C 40.577 . . 739 . 81 ASP HB2 H 2.879 . . 740 . 81 ASP HB3 H 2.265 . . 741 . 82 VAL H H 8.321 . . 742 . 82 VAL N N 123.490 . . 743 . 82 VAL CA C 64.859 . . 744 . 82 VAL HA H 3.408 . . 745 . 82 VAL CB C 31.023 . . 746 . 82 VAL HB H 1.857 . . 747 . 82 VAL CG1 C 20.734 . . 748 . 82 VAL HG1 H 0.729 . . 749 . 83 GLY H H 8.450 . . 750 . 83 GLY N N 109.597 . . 751 . 83 GLY CA C 46.186 . . 752 . 83 GLY HA2 H 3.771 . . 753 . 83 GLY HA3 H 3.835 . . 754 . 84 GLN H H 7.341 . . 755 . 84 GLN N N 115.600 . . 756 . 84 GLN CA C 53.807 . . 757 . 84 GLN HA H 4.294 . . 758 . 84 GLN CB C 29.114 . . 759 . 84 GLN HB2 H 1.358 . . 760 . 84 GLN HB3 H 2.075 . . 761 . 84 GLN CG C 33.863 . . 762 . 84 GLN HG2 H 2.274 . . 763 . 84 GLN HG3 H 2.040 . . 764 . 84 GLN NE2 N 112.008 . . 765 . 84 GLN HE21 H 7.494 . . 766 . 84 GLN HE22 H 6.580 . . 767 . 85 GLN H H 7.785 . . 768 . 85 GLN N N 118.309 . . 769 . 85 GLN CA C 56.011 . . 770 . 85 GLN HA H 3.626 . . 771 . 85 GLN CB C 25.664 . . 772 . 85 GLN HB2 H 2.287 . . 773 . 85 GLN HB3 H 2.242 . . 774 . 85 GLN CG C 33.854 . . 775 . 85 GLN HG2 H 2.201 . . 776 . 85 GLN HG3 H 2.329 . . 777 . 85 GLN NE2 N 110.995 . . 778 . 85 GLN HE21 H 7.478 . . 779 . 85 GLN HE22 H 6.573 . . 780 . 86 ARG H H 7.931 . . 781 . 86 ARG N N 116.618 . . 782 . 86 ARG CA C 53.520 . . 783 . 86 ARG HA H 5.359 . . 784 . 86 ARG CB C 34.812 . . 785 . 86 ARG HB2 H 1.583 . . 786 . 86 ARG HB3 H 1.682 . . 787 . 86 ARG CG C 25.931 . . 788 . 86 ARG HG2 H 1.587 . . 789 . 86 ARG HG3 H 1.404 . . 790 . 86 ARG CD C 42.765 . . 791 . 86 ARG HD2 H 2.594 . . 792 . 86 ARG HD3 H 2.787 . . 793 . 86 ARG NE N 83.910 . . 794 . 86 ARG HE H 7.306 . . 795 . 87 LEU H H 9.173 . . 796 . 87 LEU N N 126.353 . . 797 . 87 LEU CA C 52.213 . . 798 . 87 LEU HA H 4.926 . . 799 . 87 LEU CB C 44.308 . . 800 . 87 LEU HB2 H 1.884 . . 801 . 87 LEU HB3 H 1.120 . . 802 . 87 LEU CG C 26.899 . . 803 . 87 LEU CD1 C 21.552 . . 804 . 87 LEU HD1 H 0.838 . . 805 . 87 LEU CD2 C 24.453 . . 806 . 87 LEU HD2 H 0.757 . . 807 . 87 LEU HG H 1.438 . . 808 . 88 ASN H H 9.202 . . 809 . 88 ASN N N 125.171 . . 810 . 88 ASN CA C 51.910 . . 811 . 88 ASN HA H 5.268 . . 812 . 88 ASN CB C 39.563 . . 813 . 88 ASN HB2 H 2.711 . . 814 . 88 ASN HB3 H 2.506 . . 815 . 88 ASN ND2 N 113.607 . . 816 . 88 ASN HD21 H 7.029 . . 817 . 88 ASN HD22 H 7.452 . . 818 . 89 LEU H H 9.486 . . 819 . 89 LEU N N 126.812 . . 820 . 89 LEU CA C 51.920 . . 821 . 89 LEU HA H 5.266 . . 822 . 89 LEU CB C 44.339 . . 823 . 89 LEU HB2 H 1.978 . . 824 . 89 LEU HB3 H 1.119 . . 825 . 89 LEU CG C 26.270 . . 826 . 89 LEU CD1 C 25.015 . . 827 . 89 LEU HD1 H 0.565 . . 828 . 89 LEU CD2 C 22.816 . . 829 . 89 LEU HD2 H 0.700 . . 830 . 89 LEU HG H 1.600 . . 831 . 90 THR H H 8.853 . . 832 . 90 THR N N 119.042 . . 833 . 90 THR CA C 60.445 . . 834 . 90 THR HA H 4.982 . . 835 . 90 THR CB C 69.628 . . 836 . 90 THR HB H 4.128 . . 837 . 90 THR CG2 C 20.260 . . 838 . 90 THR HG2 H 1.019 . . 839 . 91 ILE H H 9.228 . . 840 . 91 ILE N N 123.777 . . 841 . 91 ILE CA C 56.657 . . 842 . 91 ILE HA H 4.420 . . 843 . 91 ILE CB C 41.762 . . 844 . 91 ILE HB H 1.770 . . 845 . 91 ILE CG2 C 16.133 . . 846 . 91 ILE CG1 C 26.880 . . 847 . 91 ILE HG12 H 0.916 . . 848 . 91 ILE HG13 H 1.336 . . 849 . 91 ILE CD1 C 12.041 . . 850 . 91 ILE HD1 H 0.626 . . 851 . 91 ILE HG2 H 0.834 . . 852 . 92 PRO CA C 62.669 . . 853 . 92 PRO HA H 4.287 . . 854 . 92 PRO CB C 31.673 . . 855 . 92 PRO HB2 H 1.863 . . 856 . 92 PRO HB3 H 2.450 . . 857 . 92 PRO CG C 27.250 . . 858 . 92 PRO HG2 H 1.870 . . 859 . 92 PRO HG3 H 2.513 . . 860 . 92 PRO CD C 51.226 . . 861 . 92 PRO HD2 H 3.359 . . 862 . 92 PRO HD3 H 3.556 . . 863 . 93 GLN H H 8.473 . . 864 . 93 GLN N N 122.327 . . 865 . 93 GLN CA C 57.912 . . 866 . 93 GLN HA H 3.620 . . 867 . 93 GLN CB C 27.531 . . 868 . 93 GLN HB2 H 1.914 . . 869 . 93 GLN HB3 H 1.966 . . 870 . 93 GLN CG C 32.621 . . 871 . 93 GLN HG2 H 2.349 . . 872 . 93 GLN NE2 N 112.631 . . 873 . 93 GLN HE21 H 7.513 . . 874 . 93 GLN HE22 H 6.825 . . 875 . 94 ALA H H 8.306 . . 876 . 94 ALA N N 119.344 . . 877 . 94 ALA CA C 53.236 . . 878 . 94 ALA HA H 3.836 . . 879 . 94 ALA CB C 17.228 . . 880 . 94 ALA HB H 0.797 . . 881 . 95 PHE H H 7.545 . . 882 . 95 PHE N N 113.874 . . 883 . 95 PHE CA C 56.063 . . 884 . 95 PHE HA H 4.771 . . 885 . 95 PHE CB C 38.303 . . 886 . 95 PHE HB2 H 2.298 . . 887 . 95 PHE HB3 H 3.198 . . 888 . 95 PHE CD1 C 131.332 . . 889 . 95 PHE HD1 H 7.052 . . 890 . 95 PHE CE1 C 131.175 . . 891 . 95 PHE HE1 H 7.353 . . 892 . 95 PHE CZ C 129.866 . . 893 . 95 PHE HZ H 7.266 . . 894 . 96 MET H H 7.522 . . 895 . 96 MET N N 117.164 . . 896 . 96 MET CA C 51.935 . . 897 . 96 MET HA H 4.992 . . 898 . 96 MET CB C 30.157 . . 899 . 96 MET HB3 H 2.015 . . 900 . 96 MET CG C 30.406 . . 901 . 96 MET HG2 H 2.332 . . 902 . 96 MET HG3 H 2.355 . . 903 . 96 MET CE C 14.921 . . 904 . 96 MET HE H 1.831 . . 905 . 97 SER H H 8.785 . . 906 . 97 SER N N 117.469 . . 907 . 97 SER CA C 58.225 . . 908 . 97 SER HA H 4.305 . . 909 . 97 SER CB C 62.960 . . 910 . 97 SER HB3 H 3.685 . . 911 . 98 ASN CA C 52.840 . . 912 . 98 ASN HA H 4.598 . . 913 . 98 ASN CB C 37.974 . . 914 . 98 ASN HB3 H 2.663 . . 915 . 99 ARG H H 8.170 . . 916 . 99 ARG N N 121.479 . . 917 . 99 ARG CA C 55.052 . . 918 . 99 ARG HA H 4.185 . . 919 . 99 ARG CB C 30.068 . . 920 . 99 ARG HB2 H 1.622 . . 921 . 99 ARG HB3 H 1.739 . . 922 . 99 ARG CG C 25.966 . . 923 . 99 ARG HG2 H 1.487 . . 924 . 99 ARG CD C 43.042 . . 925 . 99 ARG HD2 H 2.908 . . 926 . 100 ALA H H 8.253 . . 927 . 100 ALA N N 125.934 . . 928 . 100 ALA CA C 51.920 . . 929 . 100 ALA HA H 4.180 . . 930 . 100 ALA CB C 18.345 . . 931 . 100 ALA HB H 1.268 . . 932 . 101 ARG H H 7.822 . . 933 . 101 ARG N N 125.459 . . 934 . 101 ARG CA C 56.352 . . 935 . 101 ARG HA H 4.019 . . 936 . 101 ARG CB C 30.692 . . 937 . 101 ARG HB2 H 1.583 . . 938 . 101 ARG HB3 H 1.715 . . 939 . 101 ARG CG C 26.266 . . 940 . 101 ARG HG2 H 1.469 . . 941 . 101 ARG CD C 42.718 . . 942 . 101 ARG HD2 H 3.064 . . stop_ save_