data_6709 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C resonance assignment of the N-terminal domain of PilB from Neisseria meningitidis ; _BMRB_accession_number 6709 _BMRB_flat_file_name bmr6709.str _Entry_type original _Submission_date 2005-06-29 _Accession_date 2005-06-29 _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 Beaufils Chrystel . . 2 Neiers Fabrice . . 3 Coudevylle Nicolas . . 4 Boschi-Muller Sandrine . . 5 Averlant-Petit Marie-Christine . . 6 Branlant Guy . . 7 Cung Manh-Thong . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 512 "13C chemical shifts" 469 "15N chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-06-11 update BMRB 'add related entry loop' 2007-02-05 update BMRB 'complete entry citation' 2006-03-10 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C and 15N Resonance Assignment of the N-terminal Domain of PilB from Neisseria Meningitidis. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16424993 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Beaufils Chrystel . . 2 Neiers Fabrice . . 3 Coudevylle Nicolas . . 4 Boschi-Muller Sandrine . . 5 Averlant-Petit Marie-Christine . . 6 Branlant Guy . . 7 Cung Manh-Thong . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 36 _Journal_issue 'Suppl. 5' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6 _Page_last 6 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Dsbe _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Dsbe $Dsbe stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Dsbe _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dsbe _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; MVPHTLSTLKTADNRPASVY LKKDKPTLIKFWASWCPLCL SELGQTEKWAQDAKFSSANL ITVASPGFLHEKKDGDFQKW YAGLNYPKLPVVTDNGGTIA QSLNISVYPSWALIGKDGDV QRIVKGSINEAQALALIRDP NADL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 32 MET 2 33 VAL 3 34 PRO 4 35 HIS 5 36 THR 6 37 LEU 7 38 SER 8 39 THR 9 40 LEU 10 41 LYS 11 42 THR 12 43 ALA 13 44 ASP 14 45 ASN 15 46 ARG 16 47 PRO 17 48 ALA 18 49 SER 19 50 VAL 20 51 TYR 21 52 LEU 22 53 LYS 23 54 LYS 24 55 ASP 25 56 LYS 26 57 PRO 27 58 THR 28 59 LEU 29 60 ILE 30 61 LYS 31 62 PHE 32 63 TRP 33 64 ALA 34 65 SER 35 66 TRP 36 67 CYS 37 68 PRO 38 69 LEU 39 70 CYS 40 71 LEU 41 72 SER 42 73 GLU 43 74 LEU 44 75 GLY 45 76 GLN 46 77 THR 47 78 GLU 48 79 LYS 49 80 TRP 50 81 ALA 51 82 GLN 52 83 ASP 53 84 ALA 54 85 LYS 55 86 PHE 56 87 SER 57 88 SER 58 89 ALA 59 90 ASN 60 91 LEU 61 92 ILE 62 93 THR 63 94 VAL 64 95 ALA 65 96 SER 66 97 PRO 67 98 GLY 68 99 PHE 69 100 LEU 70 101 HIS 71 102 GLU 72 103 LYS 73 104 LYS 74 105 ASP 75 106 GLY 76 107 ASP 77 108 PHE 78 109 GLN 79 110 LYS 80 111 TRP 81 112 TYR 82 113 ALA 83 114 GLY 84 115 LEU 85 116 ASN 86 117 TYR 87 118 PRO 88 119 LYS 89 120 LEU 90 121 PRO 91 122 VAL 92 123 VAL 93 124 THR 94 125 ASP 95 126 ASN 96 127 GLY 97 128 GLY 98 129 THR 99 130 ILE 100 131 ALA 101 132 GLN 102 133 SER 103 134 LEU 104 135 ASN 105 136 ILE 106 137 SER 107 138 VAL 108 139 TYR 109 140 PRO 110 141 SER 111 142 TRP 112 143 ALA 113 144 LEU 114 145 ILE 115 146 GLY 116 147 LYS 117 148 ASP 118 149 GLY 119 150 ASP 120 151 VAL 121 152 GLN 122 153 ARG 123 154 ILE 124 155 VAL 125 156 LYS 126 157 GLY 127 158 SER 128 159 ILE 129 160 ASN 130 161 GLU 131 162 ALA 132 163 GLN 133 164 ALA 134 165 LEU 135 166 ALA 136 167 LEU 137 168 ILE 138 169 ARG 139 170 ASP 140 171 PRO 141 172 ASN 142 173 ALA 143 174 ASP 144 175 LEU 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 15280 Dsbe_ox 100.00 144 100.00 100.00 3.64e-100 PDB 2FY6 "Structure Of The N-Terminal Domain Of Neisseria Meningitidis Pilb" 99.31 143 100.00 100.00 2.84e-99 PDB 2JZR "Solution Structure Of The Oxidized Form (Cys67-Cys70) Of The N-Terminal Domain Of Pilb From N. Meningitidis." 100.00 144 100.00 100.00 3.64e-100 PDB 2JZS "Solution Structure Of The Reduced Form Of The N-Terminal Domain Of Pilb From N. Meningitidis." 100.00 144 100.00 100.00 3.64e-100 PDB 2K9F "Structural Features Of The Complex Between The Dsbd N- Terminal And The Pilb N-Terminal Domains From Neisseria Meningitidis" 100.00 144 100.00 100.00 3.64e-100 EMBL CAA32146 "unnamed protein product [Neisseria gonorrhoeae]" 99.31 521 97.20 99.30 4.65e-93 EMBL CAM07595 "peptide methionine sulfoxide reductase [Neisseria meningitidis Z2491]" 99.31 522 100.00 100.00 7.49e-96 EMBL CAM09346 "peptide methionine sulfoxide reductase [Neisseria meningitidis FAM18]" 99.31 522 100.00 100.00 7.49e-96 EMBL CAX49031 "peptide methionine sulfoxide reductase MsrA/MsrB [includes: thioredoxin, peptide methionine sulfoxide reductase MsrA (protein-m" 99.31 522 100.00 100.00 7.49e-96 EMBL CBA03711 "Peptide methionine sulfoxide reductase [Neisseria meningitidis alpha153]" 52.78 422 98.68 100.00 1.78e-43 GB AAB97511 "putative gonococcal sensor kinase [Neisseria meningitidis]" 99.31 351 100.00 100.00 2.07e-97 GB AAF40515 "peptide methionine sulfoxide reductase [Neisseria meningitidis MC58]" 99.31 522 99.30 99.30 7.10e-95 GB AAL89752 "methionine sulfoxide reductase PilB [Neisseria gonorrhoeae]" 99.31 522 97.20 99.30 2.70e-93 GB AAW90666 "putative peptide methionine sulfoxide reductase [Neisseria gonorrhoeae FA 1090]" 99.31 522 97.20 99.30 2.88e-93 GB ABX72275 "peptide methionine sulfoxide reductase [Neisseria meningitidis 053442]" 99.31 522 100.00 100.00 7.49e-96 REF NP_273110 "trifunctional thioredoxin/methionine sulfoxide reductase A/B protein [Neisseria meningitidis MC58]" 99.31 522 99.30 99.30 7.10e-95 REF WP_002216163 "methionine sulfoxide reductase [Neisseria meningitidis]" 99.31 522 100.00 100.00 7.49e-96 REF WP_002218473 "peptide methionine sulfoxide reductase msrA/msrB, partial [Neisseria meningitidis]" 98.61 488 99.30 100.00 6.73e-95 REF WP_002221795 "methionine sulfoxide reductase [Neisseria meningitidis]" 99.31 522 100.00 100.00 8.70e-96 REF WP_002223263 "methionine sulfoxide reductase [Neisseria meningitidis]" 99.31 522 100.00 100.00 8.16e-96 SP P14930 "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" 99.31 522 97.20 99.30 2.70e-93 SP Q9JWM8 "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" 99.31 522 100.00 100.00 7.49e-96 SP Q9K1N8 "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" 99.31 522 99.30 99.30 7.10e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Dsbe 'Neisseria meningitidis' 487 Eubacteria . Neisseria meningitidis 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 $Dsbe '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 $Dsbe 1 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600.13 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_trosy_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N trosy' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_1H15N_trosy _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_trosy _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_CBCACONH _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_HCCH-TOCSY _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0.05 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 TMPS C 13 'methyl protons' ppm 0.0 internal indirect . . . 0.251449530 TMPS H 1 'methy protons' ppm 0 internal direct . . . 1.0 TMPS N 15 'methyl protons' ppm 0.0 internal 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Dsbe _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 36 5 THR C C 177.881 . 1 2 36 5 THR CA C 67.015 . 1 3 36 5 THR CB C 68.344 . 1 4 37 6 LEU H H 8.746 . 1 5 37 6 LEU HA H 3.826 . 1 6 37 6 LEU HB2 H 1.749 . 1 7 37 6 LEU HB3 H 1.749 . 1 8 37 6 LEU HG H 1.316 . 1 9 37 6 LEU HD1 H 0.694 . 1 10 37 6 LEU HD2 H 0.694 . 1 11 37 6 LEU C C 177.565 . 1 12 37 6 LEU CA C 58.456 . 1 13 37 6 LEU CB C 42.101 . 1 14 37 6 LEU CG C 24.063 . 1 15 37 6 LEU CD1 C 22.056 . 1 16 37 6 LEU CD2 C 22.956 . 1 17 37 6 LEU N N 122.503 . 1 18 38 7 SER H H 7.581 . 1 19 38 7 SER HA H 3.993 . 1 20 38 7 SER C C 174.912 . 1 21 38 7 SER CA C 61.506 . 1 22 38 7 SER CB C 63.205 . 1 23 38 7 SER N N 111.136 . 1 24 39 8 THR H H 7.612 . 1 25 39 8 THR HA H 4.578 . 1 26 39 8 THR HB H 4.485 . 1 27 39 8 THR HG2 H 1.189 . 1 28 39 8 THR C C 174.849 . 1 29 39 8 THR CA C 61.804 . 1 30 39 8 THR CB C 70.026 . 1 31 39 8 THR CG2 C 21.597 . 1 32 39 8 THR N N 111.485 . 1 33 40 9 LEU H H 7.303 . 1 34 40 9 LEU HA H 4.682 . 1 35 40 9 LEU HB2 H 1.734 . 1 36 40 9 LEU HB3 H 1.734 . 1 37 40 9 LEU HD1 H 0.952 . 1 38 40 9 LEU HD2 H 0.732 . 1 39 40 9 LEU C C 176.190 . 1 40 40 9 LEU CA C 54.264 . 1 41 40 9 LEU CB C 42.475 . 1 42 40 9 LEU CD1 C 25.020 . 1 43 40 9 LEU CD2 C 25.020 . 1 44 40 9 LEU N N 122.834 . 1 45 41 10 LYS H H 8.882 . 1 46 41 10 LYS HA H 5.344 . 1 47 41 10 LYS HB2 H 1.941 . 1 48 41 10 LYS HB3 H 1.941 . 1 49 41 10 LYS HG2 H 1.380 . 1 50 41 10 LYS HG3 H 1.380 . 1 51 41 10 LYS HD2 H 1.542 . 1 52 41 10 LYS HD3 H 1.542 . 1 53 41 10 LYS HE2 H 2.976 . 1 54 41 10 LYS HE3 H 2.976 . 1 55 41 10 LYS C C 176.775 . 1 56 41 10 LYS CA C 54.040 . 1 57 41 10 LYS CB C 36.258 . 1 58 41 10 LYS CG C 24.949 . 1 59 41 10 LYS CD C 25.871 . 1 60 41 10 LYS CE C 42.180 . 1 61 41 10 LYS N N 120.449 . 1 62 42 11 THR H H 9.414 . 1 63 42 11 THR HA H 5.408 . 1 64 42 11 THR HB H 5.007 . 1 65 42 11 THR HG2 H 1.068 . 1 66 42 11 THR C C 178.793 . 1 67 42 11 THR CA C 60.964 . 1 68 42 11 THR CB C 71.119 . 1 69 42 11 THR N N 109.284 . 1 70 43 12 ALA H H 8.762 . 1 71 43 12 ALA HA H 4.296 . 1 72 43 12 ALA HB H 1.492 . 1 73 43 12 ALA C C 178.818 . 1 74 43 12 ALA CA C 54.927 . 1 75 43 12 ALA CB C 17.533 . 1 76 43 12 ALA N N 124.166 . 1 77 44 13 ASP H H 8.215 . 1 78 44 13 ASP HA H 4.772 . 1 79 44 13 ASP HB2 H 3.147 . 1 80 44 13 ASP HB3 H 2.657 . 1 81 44 13 ASP C C 174.983 . 1 82 44 13 ASP CA C 52.561 . 1 83 44 13 ASP CB C 39.089 . 1 84 44 13 ASP N N 114.128 . 1 85 45 14 ASN H H 8.175 . 1 86 45 14 ASN HA H 4.279 . 1 87 45 14 ASN HB2 H 3.072 . 1 88 45 14 ASN HB3 H 2.681 . 1 89 45 14 ASN C C 174.463 . 1 90 45 14 ASN CA C 54.900 . 1 91 45 14 ASN CB C 36.958 . 1 92 45 14 ASN N N 114.979 . 1 93 46 15 ARG H H 8.290 . 1 94 46 15 ARG HA H 4.749 . 1 95 46 15 ARG C C 173.578 . 1 96 46 15 ARG CA C 54.380 . 1 97 46 15 ARG CB C 29.820 . 1 98 46 15 ARG N N 120.452 . 1 99 47 16 PRO C C 177.904 . 1 100 47 16 PRO CA C 63.578 . 1 101 47 16 PRO CB C 31.787 . 1 102 48 17 ALA H H 8.610 . 1 103 48 17 ALA HA H 3.790 . 1 104 48 17 ALA HB H 1.321 . 1 105 48 17 ALA C C 177.902 . 1 106 48 17 ALA CA C 55.021 . 1 107 48 17 ALA CB C 19.159 . 1 108 48 17 ALA N N 125.903 . 1 109 49 18 SER H H 7.980 . 1 110 49 18 SER HA H 3.944 . 1 111 49 18 SER HB2 H 3.512 . 1 112 49 18 SER HB3 H 3.206 . 1 113 49 18 SER C C 176.449 . 1 114 49 18 SER CA C 60.575 . 1 115 49 18 SER CB C 62.525 . 1 116 49 18 SER N N 109.973 . 1 117 50 19 VAL H H 7.639 . 1 118 50 19 VAL HA H 3.955 . 1 119 50 19 VAL HB H 1.996 . 1 120 50 19 VAL HG1 H 0.764 . 1 121 50 19 VAL HG2 H 0.528 . 1 122 50 19 VAL C C 177.313 . 1 123 50 19 VAL CA C 64.570 . 1 124 50 19 VAL CB C 30.981 . 1 125 50 19 VAL CG1 C 19.630 . 1 126 50 19 VAL N N 120.008 . 1 127 51 20 TYR C C 175.033 . 1 128 51 20 TYR CA C 56.914 . 1 129 51 20 TYR CB C 39.887 . 1 130 52 21 LEU H H 7.289 . 1 131 52 21 LEU HA H 4.349 . 1 132 52 21 LEU HB2 H 1.668 . 1 133 52 21 LEU HB3 H 1.668 . 1 134 52 21 LEU HG H 1.301 . 1 135 52 21 LEU C C 175.156 . 1 136 52 21 LEU CA C 53.155 . 1 137 52 21 LEU CB C 42.334 . 1 138 52 21 LEU CG C 22.598 . 1 139 52 21 LEU N N 120.042 . 1 140 53 22 LYS H H 8.259 . 1 141 53 22 LYS HA H 4.480 . 1 142 53 22 LYS C C 178.156 . 1 143 53 22 LYS CA C 55.293 . 1 144 53 22 LYS CB C 32.455 . 1 145 53 22 LYS N N 123.320 . 1 146 54 23 LYS H H 8.585 . 1 147 54 23 LYS C C 175.797 . 1 148 54 23 LYS CA C 57.264 . 1 149 54 23 LYS CB C 32.680 . 1 150 54 23 LYS N N 123.827 . 1 151 55 24 ASP H H 8.781 . 1 152 55 24 ASP HA H 4.336 . 1 153 55 24 ASP HB2 H 3.276 . 1 154 55 24 ASP HB3 H 3.276 . 1 155 55 24 ASP C C 174.460 . 1 156 55 24 ASP CA C 55.222 . 1 157 55 24 ASP CB C 39.295 . 1 158 55 24 ASP N N 115.923 . 1 159 56 25 LYS H H 7.302 . 1 160 56 25 LYS HA H 4.929 . 1 161 56 25 LYS HB2 H 1.970 . 1 162 56 25 LYS HB3 H 1.970 . 1 163 56 25 LYS HG2 H 1.369 . 1 164 56 25 LYS HG3 H 1.369 . 1 165 56 25 LYS HD2 H 1.536 . 1 166 56 25 LYS HD3 H 1.536 . 1 167 56 25 LYS HE2 H 2.912 . 1 168 56 25 LYS HE3 H 2.912 . 1 169 56 25 LYS C C 173.569 . 1 170 56 25 LYS CA C 53.827 . 1 171 56 25 LYS CB C 35.303 . 1 172 56 25 LYS CG C 24.889 . 1 173 56 25 LYS CD C 25.309 . 1 174 56 25 LYS CE C 42.243 . 1 175 56 25 LYS N N 117.430 . 1 176 57 26 PRO C C 175.018 . 1 177 57 26 PRO CA C 62.148 . 1 178 57 26 PRO CB C 33.370 . 1 179 58 27 THR H H 9.446 . 1 180 58 27 THR HA H 5.021 . 1 181 58 27 THR HB H 3.841 . 1 182 58 27 THR HG2 H 0.957 . 1 183 58 27 THR C C 172.327 . 1 184 58 27 THR CA C 62.379 . 1 185 58 27 THR CB C 71.158 . 1 186 58 27 THR CG2 C 21.191 . 1 187 58 27 THR N N 117.271 . 1 188 59 28 LEU H H 9.305 . 1 189 59 28 LEU HA H 5.298 . 1 190 59 28 LEU HB2 H 2.072 . 1 191 59 28 LEU HB3 H 1.935 . 1 192 59 28 LEU HG H 1.367 . 1 193 59 28 LEU HD1 H 1.022 . 1 194 59 28 LEU HD2 H 0.893 . 1 195 59 28 LEU C C 174.049 . 1 196 59 28 LEU CA C 53.613 . 1 197 59 28 LEU CB C 44.248 . 1 198 59 28 LEU N N 131.742 . 1 199 60 29 ILE H H 9.493 . 1 200 60 29 ILE HA H 4.670 . 1 201 60 29 ILE HB H 1.579 . 1 202 60 29 ILE HG2 H 0.655 . 1 203 60 29 ILE HD1 H -0.169 . 1 204 60 29 ILE C C 175.060 . 1 205 60 29 ILE CA C 59.725 . 1 206 60 29 ILE CB C 40.790 . 1 207 60 29 ILE N N 124.195 . 1 208 61 30 LYS H H 8.032 . 1 209 61 30 LYS HA H 4.064 . 1 210 61 30 LYS HB2 H 1.956 . 1 211 61 30 LYS HB3 H 1.956 . 1 212 61 30 LYS HE2 H 3.008 . 1 213 61 30 LYS HE3 H 3.008 . 1 214 61 30 LYS C C 175.684 . 1 215 61 30 LYS CA C 54.063 . 1 216 61 30 LYS CB C 34.146 . 1 217 61 30 LYS N N 126.370 . 1 218 62 31 PHE H H 9.455 . 1 219 62 31 PHE HA H 5.071 . 1 220 62 31 PHE HB2 H 3.327 . 1 221 62 31 PHE HB3 H 2.904 . 1 222 62 31 PHE C C 174.681 . 1 223 62 31 PHE CA C 57.535 . 1 224 62 31 PHE CB C 40.191 . 1 225 62 31 PHE N N 129.423 . 1 226 63 32 TRP H H 7.842 . 1 227 63 32 TRP HA H 4.507 . 1 228 63 32 TRP HB2 H 3.665 . 1 229 63 32 TRP HB3 H 3.665 . 1 230 63 32 TRP C C 172.096 . 1 231 63 32 TRP CA C 54.206 . 1 232 63 32 TRP CB C 31.611 . 1 233 63 32 TRP N N 117.484 . 1 234 64 33 ALA H H 6.578 . 1 235 64 33 ALA HA H 3.854 . 1 236 64 33 ALA HB H 0.107 . 1 237 64 33 ALA C C 177.523 . 1 238 64 33 ALA CA C 50.599 . 1 239 64 33 ALA CB C 22.783 . 1 240 64 33 ALA N N 117.059 . 1 241 65 34 SER H H 9.975 . 1 242 65 34 SER HA H 3.907 . 1 243 65 34 SER C C 173.875 . 1 244 65 34 SER CA C 60.621 . 1 245 65 34 SER CB C 62.221 . 1 246 65 34 SER N N 117.129 . 1 247 66 35 TRP H H 6.252 . 1 248 66 35 TRP HA H 4.506 . 1 249 66 35 TRP HB2 H 3.663 . 1 250 66 35 TRP HB3 H 3.101 . 1 251 66 35 TRP C C 176.028 . 1 252 66 35 TRP CA C 53.417 . 1 253 66 35 TRP CB C 29.582 . 1 254 66 35 TRP N N 114.507 . 1 255 67 36 CYS H H 6.946 . 1 256 67 36 CYS HA H 5.041 . 1 257 67 36 CYS HB2 H 2.584 . 1 258 67 36 CYS HB3 H 2.371 . 1 259 67 36 CYS C C 174.449 . 1 260 67 36 CYS CA C 56.454 . 1 261 67 36 CYS CB C 28.730 . 1 262 67 36 CYS N N 128.574 . 1 263 68 37 PRO C C 180.324 . 1 264 68 37 PRO CA C 64.798 . 1 265 68 37 PRO CB C 32.234 . 1 266 69 38 LEU H H 8.670 . 1 267 69 38 LEU HA H 4.281 . 1 268 69 38 LEU HB2 H 1.934 . 1 269 69 38 LEU HB3 H 1.934 . 1 270 69 38 LEU HG H 1.750 . 1 271 69 38 LEU HD1 H 0.994 . 1 272 69 38 LEU HD2 H 0.994 . 1 273 69 38 LEU C C 180.240 . 1 274 69 38 LEU CA C 58.105 . 1 275 69 38 LEU CB C 41.736 . 1 276 69 38 LEU CG C 29.160 . 1 277 69 38 LEU CD1 C 24.359 . 1 278 69 38 LEU CD2 C 24.359 . 1 279 69 38 LEU N N 126.966 . 1 280 70 39 CYS H H 10.254 . 1 281 70 39 CYS HA H 4.550 . 1 282 70 39 CYS HB2 H 3.607 . 1 283 70 39 CYS HB3 H 3.607 . 1 284 70 39 CYS C C 180.170 . 1 285 70 39 CYS CA C 64.861 . 1 286 70 39 CYS CB C 29.664 . 1 287 70 39 CYS N N 127.134 . 1 288 71 40 LEU H H 8.683 . 1 289 71 40 LEU HA H 3.877 . 1 290 71 40 LEU HB2 H 1.903 . 1 291 71 40 LEU HB3 H 1.903 . 1 292 71 40 LEU HG H 1.587 . 1 293 71 40 LEU HD1 H 1.267 . 1 294 71 40 LEU HD2 H 1.159 . 1 295 71 40 LEU C C 177.169 . 1 296 71 40 LEU CA C 57.976 . 1 297 71 40 LEU CB C 41.076 . 1 298 71 40 LEU N N 120.316 . 1 299 72 41 SER H H 8.048 . 1 300 72 41 SER HA H 4.305 . 1 301 72 41 SER HB2 H 3.936 . 1 302 72 41 SER HB3 H 3.697 . 1 303 72 41 SER C C 177.391 . 1 304 72 41 SER CA C 60.906 . 1 305 72 41 SER CB C 62.919 . 1 306 72 41 SER N N 116.923 . 1 307 73 42 GLU H H 7.228 . 1 308 73 42 GLU HA H 4.201 . 1 309 73 42 GLU HB2 H 2.112 . 1 310 73 42 GLU HB3 H 2.112 . 1 311 73 42 GLU HG2 H 2.627 . 1 312 73 42 GLU HG3 H 2.627 . 1 313 73 42 GLU C C 177.271 . 1 314 73 42 GLU CA C 56.091 . 1 315 73 42 GLU CB C 31.792 . 1 316 73 42 GLU CG C 31.410 . 1 317 73 42 GLU N N 118.037 . 1 318 74 43 LEU H H 7.118 . 1 319 74 43 LEU HA H 3.109 . 1 320 74 43 LEU HB2 H 1.003 . 1 321 74 43 LEU HB3 H -0.168 . 1 322 74 43 LEU HG H 0.553 . 1 323 74 43 LEU HD1 H -0.779 . 1 324 74 43 LEU HD2 H -0.779 . 1 325 74 43 LEU C C 177.629 . 1 326 74 43 LEU CA C 59.195 . 1 327 74 43 LEU CB C 39.602 . 1 328 74 43 LEU CG C 26.320 . 1 329 74 43 LEU CD1 C 20.148 . 1 330 74 43 LEU CD2 C 20.148 . 1 331 74 43 LEU N N 124.194 . 1 332 75 44 GLY H H 8.397 . 1 333 75 44 GLY HA2 H 3.901 . 1 334 75 44 GLY HA3 H 3.901 . 1 335 75 44 GLY C C 177.081 . 1 336 75 44 GLY CA C 47.127 . 1 337 75 44 GLY N N 105.958 . 1 338 76 45 GLN H H 8.079 . 1 339 76 45 GLN HA H 3.861 . 1 340 76 45 GLN HB2 H 1.909 . 1 341 76 45 GLN HB3 H 1.909 . 1 342 76 45 GLN HG2 H 2.336 . 1 343 76 45 GLN HG3 H 2.336 . 1 344 76 45 GLN C C 176.214 . 1 345 76 45 GLN CA C 58.149 . 1 346 76 45 GLN CB C 28.624 . 1 347 76 45 GLN N N 124.076 . 1 348 77 46 THR H H 7.606 . 1 349 77 46 THR HA H 3.608 . 1 350 77 46 THR HB H 2.897 . 1 351 77 46 THR HG2 H 0.861 . 1 352 77 46 THR C C 175.144 . 1 353 77 46 THR CA C 66.762 . 1 354 77 46 THR CB C 67.590 . 1 355 77 46 THR N N 114.843 . 1 356 78 47 GLU H H 8.030 . 1 357 78 47 GLU HA H 3.408 . 1 358 78 47 GLU HB2 H 1.793 . 1 359 78 47 GLU HB3 H 1.793 . 1 360 78 47 GLU HG2 H 2.334 . 1 361 78 47 GLU HG3 H 2.334 . 1 362 78 47 GLU C C 177.790 . 1 363 78 47 GLU CA C 59.784 . 1 364 78 47 GLU CB C 29.582 . 1 365 78 47 GLU CG C 34.227 . 1 366 78 47 GLU N N 122.300 . 1 367 79 48 LYS H H 7.431 . 1 368 79 48 LYS HA H 3.976 . 1 369 79 48 LYS HB2 H 2.087 . 1 370 79 48 LYS HB3 H 2.087 . 1 371 79 48 LYS HG2 H 1.337 . 1 372 79 48 LYS HG3 H 1.337 . 1 373 79 48 LYS HD2 H 1.885 . 1 374 79 48 LYS HD3 H 1.885 . 1 375 79 48 LYS HE2 H 3.058 . 1 376 79 48 LYS HE3 H 3.058 . 1 377 79 48 LYS C C 180.556 . 1 378 79 48 LYS CA C 59.773 . 1 379 79 48 LYS CB C 31.518 . 1 380 79 48 LYS CG C 24.509 . 1 381 79 48 LYS CD C 27.252 . 1 382 79 48 LYS CE C 42.094 . 1 383 79 48 LYS N N 119.693 . 1 384 80 49 TRP H H 8.248 . 1 385 80 49 TRP HA H 4.360 . 1 386 80 49 TRP HB2 H 3.146 . 1 387 80 49 TRP HB3 H 2.935 . 1 388 80 49 TRP C C 177.945 . 1 389 80 49 TRP CA C 58.014 . 1 390 80 49 TRP CB C 28.202 . 1 391 80 49 TRP N N 122.495 . 1 392 81 50 ALA H H 7.862 . 1 393 81 50 ALA HA H 4.003 . 1 394 81 50 ALA HB H 1.524 . 1 395 81 50 ALA C C 179.018 . 1 396 81 50 ALA CA C 54.585 . 1 397 81 50 ALA CB C 17.442 . 1 398 81 50 ALA N N 116.831 . 1 399 82 51 GLN H H 7.383 . 1 400 82 51 GLN HA H 4.562 . 1 401 82 51 GLN HB2 H 2.098 . 1 402 82 51 GLN HB3 H 2.098 . 1 403 82 51 GLN HG2 H 2.380 . 1 404 82 51 GLN HG3 H 2.380 . 1 405 82 51 GLN C C 175.085 . 1 406 82 51 GLN CA C 54.857 . 1 407 82 51 GLN CB C 31.753 . 1 408 82 51 GLN CG C 31.343 . 1 409 82 51 GLN N N 114.283 . 1 410 83 52 ASP H H 7.828 . 1 411 83 52 ASP HA H 4.701 . 1 412 83 52 ASP HB2 H 3.056 . 1 413 83 52 ASP HB3 H 3.364 . 1 414 83 52 ASP C C 178.463 . 1 415 83 52 ASP CA C 54.647 . 1 416 83 52 ASP CB C 43.939 . 1 417 83 52 ASP N N 124.187 . 1 418 84 53 ALA C C 180.724 . 1 419 84 53 ALA CA C 55.311 . 1 420 84 53 ALA CB C 18.530 . 1 421 85 54 LYS H H 9.616 . 1 422 85 54 LYS HA H 4.103 . 1 423 85 54 LYS HB2 H 1.949 . 1 424 85 54 LYS HB3 H 1.949 . 1 425 85 54 LYS HE2 H 3.005 . 1 426 85 54 LYS HE3 H 3.005 . 1 427 85 54 LYS C C 177.839 . 1 428 85 54 LYS CA C 59.386 . 1 429 85 54 LYS CB C 31.479 . 1 430 85 54 LYS CE C 42.046 . 1 431 85 54 LYS N N 119.777 . 1 432 86 55 PHE H H 7.932 . 1 433 86 55 PHE HA H 4.245 . 1 434 86 55 PHE HB2 H 3.371 . 1 435 86 55 PHE HB3 H 3.261 . 1 436 86 55 PHE C C 176.299 . 1 437 86 55 PHE CA C 58.838 . 1 438 86 55 PHE CB C 39.413 . 1 439 86 55 PHE N N 117.283 . 1 440 87 56 SER H H 7.631 . 1 441 87 56 SER HA H 4.122 . 1 442 87 56 SER C C 174.870 . 1 443 87 56 SER CA C 61.558 . 1 444 87 56 SER CB C 63.614 . 1 445 87 56 SER N N 114.112 . 1 446 88 57 SER H H 8.084 . 1 447 88 57 SER C C 172.685 . 1 448 88 57 SER CA C 59.348 . 1 449 88 57 SER CB C 62.919 . 1 450 88 57 SER N N 116.938 . 1 451 89 58 ALA H H 8.183 . 1 452 89 58 ALA HA H 4.952 . 1 453 89 58 ALA HB H 1.295 . 1 454 89 58 ALA C C 176.497 . 1 455 89 58 ALA CA C 50.207 . 1 456 89 58 ALA CB C 22.585 . 1 457 89 58 ALA N N 123.045 . 1 458 90 59 ASN H H 9.256 . 1 459 90 59 ASN HA H 5.048 . 1 460 90 59 ASN HB2 H 3.032 . 1 461 90 59 ASN HB3 H 2.763 . 1 462 90 59 ASN C C 173.801 . 1 463 90 59 ASN CA C 52.536 . 1 464 90 59 ASN CB C 39.676 . 1 465 90 59 ASN N N 117.332 . 1 466 91 60 LEU H H 8.534 . 1 467 91 60 LEU HA H 5.502 . 1 468 91 60 LEU HB2 H 1.832 . 1 469 91 60 LEU HB3 H 1.575 . 1 470 91 60 LEU HG H 1.699 . 1 471 91 60 LEU HD1 H 0.978 . 1 472 91 60 LEU HD2 H 0.781 . 1 473 91 60 LEU C C 175.588 . 1 474 91 60 LEU CA C 55.252 . 1 475 91 60 LEU CB C 43.969 . 1 476 91 60 LEU CG C 29.060 . 1 477 91 60 LEU CD1 C 24.874 . 1 478 91 60 LEU CD2 C 24.874 . 1 479 91 60 LEU N N 128.543 . 1 480 92 61 ILE H H 8.681 . 1 481 92 61 ILE HA H 4.504 . 1 482 92 61 ILE HB H 1.483 . 1 483 92 61 ILE HG12 H 1.117 . 1 484 92 61 ILE HG2 H 0.681 . 1 485 92 61 ILE HD1 H 0.605 . 1 486 92 61 ILE C C 173.121 . 1 487 92 61 ILE CA C 58.672 . 1 488 92 61 ILE CB C 43.446 . 1 489 92 61 ILE CG1 C 26.107 . 1 490 92 61 ILE CG2 C 18.080 . 1 491 92 61 ILE CD1 C 14.003 . 1 492 92 61 ILE N N 118.693 . 1 493 93 62 THR HA H 5.458 . 1 494 93 62 THR HB H 4.195 . 1 495 93 62 THR HG2 H 0.861 . 1 496 93 62 THR C C 172.222 . 1 497 93 62 THR CA C 58.710 . 1 498 93 62 THR CB C 70.159 . 1 499 93 62 THR CG2 C 20.548 . 1 500 93 62 THR N N 112.211 . 1 501 94 63 VAL H H 8.878 . 1 502 94 63 VAL HA H 4.206 . 1 503 94 63 VAL HB H 1.878 . 1 504 94 63 VAL HG1 H 0.879 . 1 505 94 63 VAL HG2 H 0.879 . 1 506 94 63 VAL C C 174.049 . 1 507 94 63 VAL CA C 60.738 . 1 508 94 63 VAL CB C 35.255 . 1 509 94 63 VAL CG1 C 20.593 . 1 510 94 63 VAL N N 123.135 . 1 511 95 64 ALA H H 8.069 . 1 512 95 64 ALA HA H 4.096 . 1 513 95 64 ALA HB H -0.192 . 1 514 95 64 ALA C C 176.769 . 1 515 95 64 ALA CA C 48.991 . 1 516 95 64 ALA CB C 21.993 . 1 517 95 64 ALA N N 129.829 . 1 518 96 65 SER H H 9.117 . 1 519 96 65 SER HA H 4.889 . 1 520 96 65 SER C C 171.232 . 1 521 96 65 SER CA C 55.021 . 1 522 96 65 SER CB C 64.727 . 1 523 96 65 SER N N 119.045 . 1 524 97 66 PRO C C 176.471 . 1 525 97 66 PRO CA C 64.097 . 1 526 97 66 PRO CB C 31.499 . 1 527 98 67 GLY H H 7.113 . 1 528 98 67 GLY HA2 H 3.580 . 1 529 98 67 GLY HA3 H 3.580 . 1 530 98 67 GLY C C 173.233 . 1 531 98 67 GLY CA C 45.682 . 1 532 98 67 GLY N N 110.139 . 1 533 99 68 PHE H H 8.064 . 1 534 99 68 PHE HA H 4.835 . 1 535 99 68 PHE HB2 H 3.139 . 1 536 99 68 PHE HB3 H 3.139 . 1 537 99 68 PHE C C 175.712 . 1 538 99 68 PHE CA C 55.836 . 1 539 99 68 PHE CB C 40.943 . 1 540 99 68 PHE N N 123.435 . 1 541 100 69 LEU H H 8.894 . 1 542 100 69 LEU HA H 3.211 . 1 543 100 69 LEU HB2 H 1.662 . 1 544 100 69 LEU HB3 H 1.031 . 1 545 100 69 LEU HD1 H 0.410 . 1 546 100 69 LEU HD2 H 0.410 . 1 547 100 69 LEU C C 175.628 . 1 548 100 69 LEU CA C 55.502 . 1 549 100 69 LEU CB C 40.256 . 1 550 100 69 LEU N N 132.634 . 1 551 101 70 HIS H H 8.120 . 1 552 101 70 HIS HA H 3.931 . 1 553 101 70 HIS HB2 H 2.927 . 1 554 101 70 HIS HB3 H 2.927 . 1 555 101 70 HIS C C 175.128 . 1 556 101 70 HIS CA C 57.437 . 1 557 101 70 HIS CB C 26.971 . 1 558 101 70 HIS N N 107.450 . 1 559 102 71 GLU H H 7.972 . 1 560 102 71 GLU HA H 4.453 . 1 561 102 71 GLU C C 175.627 . 1 562 102 71 GLU CA C 55.945 . 1 563 102 71 GLU CB C 30.772 . 1 564 102 71 GLU N N 121.635 . 1 565 103 72 LYS H H 10.181 . 1 566 103 72 LYS HA H 4.145 . 1 567 103 72 LYS C C 176.260 . 1 568 103 72 LYS CA C 57.728 . 1 569 103 72 LYS CB C 34.705 . 1 570 103 72 LYS N N 129.641 . 1 571 104 73 LYS H H 8.644 . 1 572 104 73 LYS HA H 4.063 . 1 573 104 73 LYS C C 176.281 . 1 574 104 73 LYS CA C 56.231 . 1 575 104 73 LYS CB C 33.426 . 1 576 104 73 LYS N N 120.021 . 1 577 105 74 ASP H H 9.092 . 1 578 105 74 ASP HA H 4.420 . 1 579 105 74 ASP HB2 H 2.645 . 1 580 105 74 ASP HB3 H 2.511 . 1 581 105 74 ASP C C 177.523 . 1 582 105 74 ASP CA C 57.375 . 1 583 105 74 ASP CB C 41.171 . 1 584 105 74 ASP N N 123.257 . 1 585 106 75 GLY H H 9.620 . 1 586 106 75 GLY HA2 H 4.709 . 1 587 106 75 GLY HA3 H 4.709 . 1 588 106 75 GLY C C 176.102 . 1 589 106 75 GLY CA C 46.471 . 1 590 106 75 GLY N N 119.322 . 1 591 107 76 ASP H H 7.417 . 1 592 107 76 ASP HA H 4.514 . 1 593 107 76 ASP HB2 H 3.029 . 1 594 107 76 ASP HB3 H 2.728 . 1 595 107 76 ASP C C 179.997 . 1 596 107 76 ASP CA C 57.041 . 1 597 107 76 ASP CB C 40.075 . 1 598 107 76 ASP N N 123.977 . 1 599 108 77 PHE H H 9.106 . 1 600 108 77 PHE HA H 3.902 . 1 601 108 77 PHE HB2 H 3.083 . 1 602 108 77 PHE HB3 H 2.803 . 1 603 108 77 PHE C C 176.195 . 1 604 108 77 PHE CA C 63.505 . 1 605 108 77 PHE CB C 38.154 . 1 606 108 77 PHE N N 121.879 . 1 607 109 78 GLN H H 10.318 . 1 608 109 78 GLN HA H 3.783 . 1 609 109 78 GLN C C 178.787 . 1 610 109 78 GLN CA C 61.963 . 1 611 109 78 GLN CB C 26.868 . 1 612 109 78 GLN N N 121.765 . 1 613 110 79 LYS H H 7.815 . 1 614 110 79 LYS HA H 4.068 . 1 615 110 79 LYS C C 178.682 . 1 616 110 79 LYS CA C 59.363 . 1 617 110 79 LYS CB C 32.422 . 1 618 110 79 LYS N N 121.128 . 1 619 111 80 TRP H H 7.854 . 1 620 111 80 TRP HA H 4.119 . 1 621 111 80 TRP HB2 H 3.500 . 1 622 111 80 TRP HB3 H 3.299 . 1 623 111 80 TRP C C 178.471 . 1 624 111 80 TRP CA C 61.014 . 1 625 111 80 TRP CB C 27.181 . 1 626 111 80 TRP N N 121.678 . 1 627 112 81 TYR H H 8.990 . 1 628 112 81 TYR HA H 4.279 . 1 629 112 81 TYR HB2 H 3.095 . 1 630 112 81 TYR HB3 H 2.705 . 1 631 112 81 TYR C C 177.123 . 1 632 112 81 TYR CA C 61.201 . 1 633 112 81 TYR CB C 38.043 . 1 634 112 81 TYR N N 121.843 . 1 635 113 82 ALA H H 7.609 . 1 636 113 82 ALA HA H 4.009 . 1 637 113 82 ALA HB H 1.523 . 1 638 113 82 ALA C C 178.333 . 1 639 113 82 ALA CA C 53.715 . 1 640 113 82 ALA CB C 17.948 . 1 641 113 82 ALA N N 121.023 . 1 642 114 83 GLY H H 7.235 . 1 643 114 83 GLY HA2 H 3.962 . 1 644 114 83 GLY HA3 H 3.544 . 1 645 114 83 GLY C C 174.133 . 1 646 114 83 GLY CA C 44.887 . 1 647 114 83 GLY N N 103.619 . 1 648 115 84 LEU H H 7.179 . 1 649 115 84 LEU HA H 4.011 . 1 650 115 84 LEU C C 175.923 . 1 651 115 84 LEU CA C 54.098 . 1 652 115 84 LEU CB C 41.695 . 1 653 115 84 LEU N N 122.390 . 1 654 116 85 ASN C C 173.212 . 1 655 116 85 ASN CA C 51.510 . 1 656 116 85 ASN CB C 38.423 . 1 657 117 86 TYR H H 8.149 . 1 658 117 86 TYR HA H 4.829 . 1 659 117 86 TYR HB2 H 3.118 . 1 660 117 86 TYR HB3 H 2.653 . 1 661 117 86 TYR C C 174.935 . 1 662 117 86 TYR CA C 55.798 . 1 663 117 86 TYR CB C 38.583 . 1 664 117 86 TYR N N 120.181 . 1 665 118 87 PRO C C 178.471 . 1 666 118 87 PRO CA C 64.984 . 1 667 118 87 PRO CB C 32.198 . 1 668 119 88 LYS H H 9.218 . 1 669 119 88 LYS HA H 4.489 . 1 670 119 88 LYS C C 175.799 . 1 671 119 88 LYS CA C 54.536 . 1 672 119 88 LYS CB C 31.476 . 1 673 119 88 LYS N N 118.359 . 1 674 120 89 LEU H H 7.753 . 1 675 120 89 LEU HA H 4.331 . 1 676 120 89 LEU HB2 H 2.270 . 1 677 120 89 LEU HB3 H 2.270 . 1 678 120 89 LEU HG H 0.861 . 1 679 120 89 LEU HD1 H 0.469 . 1 680 120 89 LEU HD2 H 0.469 . 1 681 120 89 LEU C C 174.134 . 1 682 120 89 LEU CA C 51.832 . 1 683 120 89 LEU CB C 44.104 . 1 684 120 89 LEU N N 124.114 . 1 685 121 90 PRO C C 177.165 . 1 686 121 90 PRO CA C 62.312 . 1 687 121 90 PRO CB C 31.420 . 1 688 122 91 VAL H H 8.569 . 1 689 122 91 VAL HA H 4.253 . 1 690 122 91 VAL HB H 1.867 . 1 691 122 91 VAL HG1 H 0.884 . 1 692 122 91 VAL HG2 H 0.628 . 1 693 122 91 VAL C C 174.154 . 1 694 122 91 VAL CA C 62.128 . 1 695 122 91 VAL CB C 33.953 . 1 696 122 91 VAL CG1 C 21.218 . 1 697 122 91 VAL N N 130.226 . 1 698 123 92 VAL H H 9.010 . 1 699 123 92 VAL HA H 4.385 . 1 700 123 92 VAL HB H 2.044 . 1 701 123 92 VAL HG1 H 0.842 . 1 702 123 92 VAL HG2 H 0.842 . 1 703 123 92 VAL C C 174.836 . 1 704 123 92 VAL CA C 62.248 . 1 705 123 92 VAL CB C 33.394 . 1 706 123 92 VAL CG1 C 21.136 . 1 707 123 92 VAL N N 128.984 . 1 708 124 93 THR H H 8.636 . 1 709 124 93 THR HA H 4.911 . 1 710 124 93 THR HB H 3.790 . 1 711 124 93 THR HG2 H 0.832 . 1 712 124 93 THR C C 173.591 . 1 713 124 93 THR CA C 58.307 . 1 714 124 93 THR CB C 68.899 . 1 715 124 93 THR CG2 C 21.984 . 1 716 124 93 THR N N 115.021 . 1 717 125 94 ASP H H 8.579 . 1 718 125 94 ASP HA H 4.845 . 1 719 125 94 ASP HB2 H 2.825 . 1 720 125 94 ASP HB3 H 2.063 . 1 721 125 94 ASP C C 176.070 . 1 722 125 94 ASP CA C 50.647 . 1 723 125 94 ASP CB C 41.594 . 1 724 125 94 ASP N N 124.596 . 1 725 126 95 ASN H H 8.435 . 1 726 126 95 ASN HA H 4.475 . 1 727 126 95 ASN HB2 H 2.855 . 1 728 126 95 ASN HB3 H 2.855 . 1 729 126 95 ASN C C 177.002 . 1 730 126 95 ASN CA C 55.348 . 1 731 126 95 ASN CB C 37.612 . 1 732 126 95 ASN N N 124.952 . 1 733 127 96 GLY H H 9.514 . 1 734 127 96 GLY HA2 H 4.198 . 1 735 127 96 GLY HA3 H 4.198 . 1 736 127 96 GLY C C 175.019 . 1 737 127 96 GLY CA C 44.972 . 1 738 127 96 GLY N N 116.737 . 1 739 128 97 GLY H H 8.748 . 1 740 128 97 GLY HA2 H 3.589 . 1 741 128 97 GLY HA3 H 3.589 . 1 742 128 97 GLY C C 173.799 . 1 743 128 97 GLY CA C 47.792 . 1 744 128 97 GLY N N 110.418 . 1 745 129 98 THR H H 7.467 . 1 746 129 98 THR HA H 4.027 . 1 747 129 98 THR HB H 3.559 . 1 748 129 98 THR HG2 H 1.182 . 1 749 129 98 THR C C 178.273 . 1 750 129 98 THR CA C 66.335 . 1 751 129 98 THR CB C 68.129 . 1 752 129 98 THR N N 114.300 . 1 753 130 99 ILE H H 10.680 . 1 754 130 99 ILE HA H 3.544 . 1 755 130 99 ILE C C 178.638 . 1 756 130 99 ILE CA C 65.684 . 1 757 130 99 ILE CB C 38.876 . 1 758 130 99 ILE N N 128.033 . 1 759 131 100 ALA H H 9.256 . 1 760 131 100 ALA HA H 3.201 . 1 761 131 100 ALA HB H 1.048 . 1 762 131 100 ALA C C 180.319 . 1 763 131 100 ALA CA C 55.593 . 1 764 131 100 ALA CB C 17.007 . 1 765 131 100 ALA N N 125.258 . 1 766 132 101 GLN H H 8.284 . 1 767 132 101 GLN HA H 4.072 . 1 768 132 101 GLN C C 180.050 . 1 769 132 101 GLN CA C 59.441 . 1 770 132 101 GLN CB C 29.757 . 1 771 132 101 GLN N N 115.401 . 1 772 133 102 SER H H 7.639 . 1 773 133 102 SER HA H 4.177 . 1 774 133 102 SER C C 175.333 . 1 775 133 102 SER CA C 61.427 . 1 776 133 102 SER CB C 62.923 . 1 777 133 102 SER N N 118.298 . 1 778 134 103 LEU H H 7.519 . 1 779 134 103 LEU HA H 4.303 . 1 780 134 103 LEU HB2 H 1.679 . 1 781 134 103 LEU HB3 H 1.679 . 1 782 134 103 LEU HG H 1.320 . 1 783 134 103 LEU HD1 H 0.805 . 1 784 134 103 LEU HD2 H 0.725 . 1 785 134 103 LEU C C 175.411 . 1 786 134 103 LEU CA C 54.384 . 1 787 134 103 LEU CB C 41.428 . 1 788 134 103 LEU CG C 24.031 . 1 789 134 103 LEU CD1 C 23.109 . 1 790 134 103 LEU CD2 C 23.109 . 1 791 134 103 LEU N N 120.511 . 1 792 135 104 ASN H H 7.806 . 1 793 135 104 ASN HA H 4.251 . 1 794 135 104 ASN HB2 H 3.095 . 1 795 135 104 ASN HB3 H 2.713 . 1 796 135 104 ASN C C 174.552 . 1 797 135 104 ASN CA C 54.148 . 1 798 135 104 ASN CB C 37.067 . 1 799 135 104 ASN N N 116.946 . 1 800 136 105 ILE H H 8.190 . 1 801 136 105 ILE HA H 3.926 . 1 802 136 105 ILE HB H 1.426 . 1 803 136 105 ILE HG2 H 0.558 . 1 804 136 105 ILE HD1 H 0.231 . 1 805 136 105 ILE C C 175.813 . 1 806 136 105 ILE CA C 60.331 . 1 807 136 105 ILE CB C 36.696 . 1 808 136 105 ILE CG2 C 16.416 . 1 809 136 105 ILE N N 120.543 . 1 810 137 106 SER C C 172.749 . 1 811 137 106 SER CA C 57.138 . 1 812 137 106 SER CB C 64.751 . 1 813 138 107 VAL H H 7.161 . 1 814 138 107 VAL HA H 4.191 . 1 815 138 107 VAL HB H 1.886 . 1 816 138 107 VAL HG1 H 0.896 . 1 817 138 107 VAL HG2 H 0.896 . 1 818 138 107 VAL C C 173.549 . 1 819 138 107 VAL CA C 60.179 . 1 820 138 107 VAL CB C 35.329 . 1 821 138 107 VAL CG1 C 20.531 . 1 822 138 107 VAL N N 120.442 . 1 823 139 108 TYR H H 8.631 . 1 824 139 108 TYR HA H 5.164 . 1 825 139 108 TYR HB2 H 2.850 . 1 826 139 108 TYR HB3 H 2.470 . 1 827 139 108 TYR C C 175.333 . 1 828 139 108 TYR CA C 52.992 . 1 829 139 108 TYR CB C 40.951 . 1 830 139 108 TYR N N 122.595 . 1 831 140 109 PRO C C 176.028 . 1 832 140 109 PRO CA C 63.158 . 1 833 140 109 PRO CB C 34.813 . 1 834 141 110 SER H H 8.101 . 1 835 141 110 SER HA H 5.502 . 1 836 141 110 SER HB2 H 4.075 . 1 837 141 110 SER HB3 H 3.831 . 1 838 141 110 SER C C 171.759 . 1 839 141 110 SER CA C 60.605 . 1 840 141 110 SER CB C 70.547 . 1 841 141 110 SER N N 113.702 . 1 842 142 111 TRP H H 9.966 . 1 843 142 111 TRP HA H 6.228 . 1 844 142 111 TRP HB2 H 3.143 . 1 845 142 111 TRP HB3 H 2.904 . 1 846 142 111 TRP C C 175.204 . 1 847 142 111 TRP CA C 55.798 . 1 848 142 111 TRP CB C 32.612 . 1 849 142 111 TRP N N 123.957 . 1 850 143 112 ALA H H 9.820 . 1 851 143 112 ALA HA H 5.648 . 1 852 143 112 ALA HB H 1.485 . 1 853 143 112 ALA C C 174.501 . 1 854 143 112 ALA CA C 50.178 . 1 855 143 112 ALA CB C 23.542 . 1 856 143 112 ALA N N 122.511 . 1 857 144 113 LEU H H 9.173 . 1 858 144 113 LEU HA H 5.320 . 1 859 144 113 LEU HB2 H 2.090 . 1 860 144 113 LEU HB3 H 2.090 . 1 861 144 113 LEU HG H 1.376 . 1 862 144 113 LEU HD1 H 1.023 . 1 863 144 113 LEU HD2 H 0.892 . 1 864 144 113 LEU C C 174.512 . 1 865 144 113 LEU CA C 53.164 . 1 866 144 113 LEU CB C 45.128 . 1 867 144 113 LEU N N 124.757 . 1 868 145 114 ILE H H 9.734 . 1 869 145 114 ILE HA H 4.828 . 1 870 145 114 ILE HB H 2.105 . 1 871 145 114 ILE HG2 H 0.977 . 1 872 145 114 ILE HD1 H 0.782 . 1 873 145 114 ILE C C 176.365 . 1 874 145 114 ILE CA C 57.462 . 1 875 145 114 ILE CB C 37.512 . 1 876 145 114 ILE N N 130.085 . 1 877 146 115 GLY H H 9.157 . 1 878 146 115 GLY HA2 H 4.133 . 1 879 146 115 GLY HA3 H 4.133 . 1 880 146 115 GLY C C 176.789 . 1 881 146 115 GLY CA C 45.123 . 1 882 146 115 GLY N N 113.159 . 1 883 147 116 LYS H H 9.154 . 1 884 147 116 LYS HA H 3.935 . 1 885 147 116 LYS C C 176.913 . 1 886 147 116 LYS CA C 59.100 . 1 887 147 116 LYS CB C 31.686 . 1 888 147 116 LYS N N 122.835 . 1 889 148 117 ASP H H 8.736 . 1 890 148 117 ASP HA H 4.830 . 1 891 148 117 ASP HB2 H 2.905 . 1 892 148 117 ASP HB3 H 2.659 . 1 893 148 117 ASP C C 177.144 . 1 894 148 117 ASP CA C 54.501 . 1 895 148 117 ASP CB C 40.667 . 1 896 148 117 ASP N N 118.132 . 1 897 149 118 GLY H H 8.133 . 1 898 149 118 GLY HA2 H 4.253 . 1 899 149 118 GLY HA3 H 3.328 . 1 900 149 118 GLY C C 172.587 . 1 901 149 118 GLY CA C 45.985 . 1 902 149 118 GLY N N 108.650 . 1 903 150 119 ASP H H 9.380 . 1 904 150 119 ASP HA H 4.556 . 1 905 150 119 ASP HB2 H 2.632 . 1 906 150 119 ASP HB3 H 2.447 . 1 907 150 119 ASP C C 176.082 . 1 908 150 119 ASP CA C 52.312 . 1 909 150 119 ASP CB C 39.408 . 1 910 150 119 ASP N N 119.951 . 1 911 151 120 VAL H H 8.949 . 1 912 151 120 VAL HA H 3.954 . 1 913 151 120 VAL HB H 2.004 . 1 914 151 120 VAL HG1 H 0.772 . 1 915 151 120 VAL HG2 H 0.519 . 1 916 151 120 VAL C C 176.559 . 1 917 151 120 VAL CA C 64.054 . 1 918 151 120 VAL CB C 30.809 . 1 919 151 120 VAL CG1 C 19.740 . 1 920 151 120 VAL N N 124.957 . 1 921 152 121 GLN H H 9.138 . 1 922 152 121 GLN HA H 4.443 . 1 923 152 121 GLN C C 176.449 . 1 924 152 121 GLN CA C 57.058 . 1 925 152 121 GLN CB C 30.491 . 1 926 152 121 GLN N N 129.016 . 1 927 153 122 ARG H H 7.615 . 1 928 153 122 ARG C C 173.838 . 1 929 153 122 ARG CA C 55.308 . 1 930 153 122 ARG CB C 33.811 . 1 931 153 122 ARG N N 118.090 . 1 932 154 123 ILE H H 8.179 . 1 933 154 123 ILE HA H 5.053 . 1 934 154 123 ILE HB H 1.800 . 1 935 154 123 ILE HG12 H 1.626 . 1 936 154 123 ILE HG2 H 1.022 . 1 937 154 123 ILE HD1 H 0.889 . 1 938 154 123 ILE C C 175.799 . 1 939 154 123 ILE CA C 60.736 . 1 940 154 123 ILE CB C 40.195 . 1 941 154 123 ILE CG1 C 27.625 . 1 942 154 123 ILE CG2 C 14.172 . 1 943 154 123 ILE CD1 C 16.862 . 1 944 154 123 ILE N N 127.038 . 1 945 155 124 VAL H H 9.883 . 1 946 155 124 VAL HA H 4.365 . 1 947 155 124 VAL HB H 2.025 . 1 948 155 124 VAL HG1 H 0.836 . 1 949 155 124 VAL HG2 H 0.836 . 1 950 155 124 VAL C C 174.702 . 1 951 155 124 VAL CA C 61.116 . 1 952 155 124 VAL CB C 34.957 . 1 953 155 124 VAL CG1 C 21.377 . 1 954 155 124 VAL N N 130.703 . 1 955 156 125 LYS H H 8.685 . 1 956 156 125 LYS HA H 4.848 . 1 957 156 125 LYS C C 177.102 . 1 958 156 125 LYS CA C 56.049 . 1 959 156 125 LYS CB C 33.046 . 1 960 156 125 LYS N N 128.643 . 1 961 157 126 GLY H H 8.417 . 1 962 157 126 GLY HA2 H 4.385 . 1 963 157 126 GLY HA3 H 4.385 . 1 964 157 126 GLY C C 171.590 . 1 965 157 126 GLY CA C 44.613 . 1 966 157 126 GLY N N 116.459 . 1 967 158 127 SER H H 7.851 . 1 968 158 127 SER HA H 4.583 . 1 969 158 127 SER HB2 H 3.829 . 1 970 158 127 SER HB3 H 3.742 . 1 971 158 127 SER C C 176.131 . 1 972 158 127 SER CA C 59.407 . 1 973 158 127 SER CB C 63.246 . 1 974 158 127 SER N N 109.343 . 1 975 159 128 ILE H H 7.994 . 1 976 159 128 ILE HA H 4.836 . 1 977 159 128 ILE C C 174.867 . 1 978 159 128 ILE CA C 59.378 . 1 979 159 128 ILE CB C 40.937 . 1 980 159 128 ILE N N 117.904 . 1 981 160 129 ASN H H 8.796 . 1 982 160 129 ASN HA H 5.090 . 1 983 160 129 ASN HB2 H 3.379 . 1 984 160 129 ASN HB3 H 2.833 . 1 985 160 129 ASN C C 174.870 . 1 986 160 129 ASN CA C 50.431 . 1 987 160 129 ASN CB C 39.393 . 1 988 160 129 ASN N N 120.331 . 1 989 161 130 GLU H H 8.477 . 1 990 161 130 GLU C C 176.762 . 1 991 161 130 GLU CA C 60.183 . 1 992 161 130 GLU CB C 30.608 . 1 993 161 130 GLU N N 120.331 . 1 994 162 131 ALA H H 7.817 . 1 995 162 131 ALA HA H 3.797 . 1 996 162 131 ALA HB H 1.328 . 1 997 162 131 ALA C C 181.669 . 1 998 162 131 ALA CA C 54.854 . 1 999 162 131 ALA CB C 17.646 . 1 1000 162 131 ALA N N 120.256 . 1 1001 163 132 GLN H H 8.336 . 1 1002 163 132 GLN HA H 3.839 . 1 1003 163 132 GLN C C 177.173 . 1 1004 163 132 GLN CA C 58.284 . 1 1005 163 132 GLN CB C 29.371 . 1 1006 163 132 GLN N N 119.908 . 1 1007 164 133 ALA H H 7.817 . 1 1008 164 133 ALA HA H 3.436 . 1 1009 164 133 ALA HB H 0.774 . 1 1010 164 133 ALA C C 178.787 . 1 1011 164 133 ALA CA C 54.854 . 1 1012 164 133 ALA CB C 17.646 . 1 1013 164 133 ALA N N 122.300 . 1 1014 165 134 LEU H H 8.110 . 1 1015 165 134 LEU HA H 3.525 . 1 1016 165 134 LEU HB2 H 1.432 . 1 1017 165 134 LEU HB3 H 1.432 . 1 1018 165 134 LEU HG H 1.008 . 1 1019 165 134 LEU HD1 H -.86 . 1 1020 165 134 LEU HD2 H -.86 . 1 1021 165 134 LEU C C 179.698 . 1 1022 165 134 LEU CA C 55.312 . 1 1023 165 134 LEU CB C 41.297 . 1 1024 165 134 LEU CG C 27.166 . 1 1025 165 134 LEU CD1 C 22.492 . 1 1026 165 134 LEU CD2 C 22.492 . 1 1027 165 134 LEU N N 122.300 . 1 1028 166 135 ALA H H 8.110 . 1 1029 166 135 ALA HA H 3.855 . 1 1030 166 135 ALA HB H 1.360 . 1 1031 166 135 ALA C C 179.823 . 1 1032 166 135 ALA CA C 55.312 . 1 1033 166 135 ALA CB C 17.827 . 1 1034 166 135 ALA N N 122.300 . 1 1035 167 136 LEU H H 7.719 . 1 1036 167 136 LEU HA H 4.066 . 1 1037 167 136 LEU HB2 H 1.784 . 1 1038 167 136 LEU HB3 H 1.784 . 1 1039 167 136 LEU HG H 1.396 . 1 1040 167 136 LEU HD1 H 0.705 . 1 1041 167 136 LEU HD2 H 0.705 . 1 1042 167 136 LEU C C 177.383 . 1 1043 167 136 LEU CA C 56.526 . 1 1044 167 136 LEU CB C 42.383 . 1 1045 167 136 LEU CG C 29.914 . 1 1046 167 136 LEU CD1 C 24.425 . 1 1047 167 136 LEU CD2 C 24.425 . 1 1048 167 136 LEU N N 119.029 . 1 1049 168 137 ILE H H 7.235 . 1 1050 168 137 ILE HA H 3.623 . 1 1051 168 137 ILE C C 177.966 . 1 1052 168 137 ILE CA C 64.295 . 1 1053 168 137 ILE CB C 37.784 . 1 1054 168 137 ILE N N 112.366 . 1 1055 169 138 ARG H H 7.306 . 1 1056 169 138 ARG HA H 4.103 . 1 1057 169 138 ARG C C 176.733 . 1 1058 169 138 ARG CA C 57.801 . 1 1059 169 138 ARG CB C 30.617 . 1 1060 169 138 ARG N N 120.873 . 1 1061 170 139 ASP H H 8.170 . 1 1062 170 139 ASP HA H 4.859 . 1 1063 170 139 ASP HB2 H 2.750 . 1 1064 170 139 ASP HB3 H 2.531 . 1 1065 170 139 ASP C C 173.466 . 1 1066 170 139 ASP CA C 50.987 . 1 1067 170 139 ASP CB C 42.478 . 1 1068 170 139 ASP N N 119.901 . 1 1069 171 140 PRO C C 176.734 . 1 1070 171 140 PRO CA C 64.063 . 1 1071 171 140 PRO CB C 32.676 . 1 1072 172 141 ASN H H 8.054 . 1 1073 172 141 ASN HA H 4.792 . 1 1074 172 141 ASN HB2 H 2.957 . 1 1075 172 141 ASN HB3 H 2.632 . 1 1076 172 141 ASN C C 175.422 . 1 1077 172 141 ASN CA C 52.496 . 1 1078 172 141 ASN CB C 38.945 . 1 1079 172 141 ASN N N 114.125 . 1 1080 173 142 ALA H H 7.786 . 1 1081 173 142 ALA HA H 3.916 . 1 1082 173 142 ALA HB H 1.321 . 1 1083 173 142 ALA C C 177.418 . 1 1084 173 142 ALA CA C 53.288 . 1 1085 173 142 ALA CB C 19.199 . 1 1086 173 142 ALA N N 124.058 . 1 1087 174 143 ASP H H 8.392 . 1 1088 174 143 ASP HA H 4.618 . 1 1089 174 143 ASP HB2 H 2.710 . 1 1090 174 143 ASP HB3 H 2.517 . 1 1091 174 143 ASP C C 175.123 . 1 1092 174 143 ASP CA C 54.443 . 1 1093 174 143 ASP CB C 40.637 . 1 1094 174 143 ASP N N 122.362 . 1 1095 175 144 LEU H H 8.158 . 1 1096 175 144 LEU HA H 4.179 . 1 1097 175 144 LEU HB2 H 1.624 . 1 1098 175 144 LEU HB3 H 1.624 . 1 1099 175 144 LEU HG H 1.483 . 1 1100 175 144 LEU HD1 H 0.684 . 1 1101 175 144 LEU HD2 H 0.684 . 1 1102 175 144 LEU C C 182.556 . 1 1103 175 144 LEU CA C 56.106 . 1 1104 175 144 LEU CB C 42.991 . 1 1105 175 144 LEU CG C 29.444 . 1 1106 175 144 LEU CD1 C 18.032 . 1 1107 175 144 LEU CD2 C 18.032 . 1 1108 175 144 LEU N N 130.778 . 1 stop_ save_