data_15280 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignment of the oxidized form (Cys67-Cys70) of the N-terminal domain of PilB from Neisseria meningitidis ; _BMRB_accession_number 15280 _BMRB_flat_file_name bmr15280.str _Entry_type original _Submission_date 2007-06-05 _Accession_date 2007-06-05 _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 Quinternet Marc . . 2 Beaufils Chrystel . . 3 Neiers Fabrice . . 4 Tsan Pascale . . 5 Boschi-Muller Sandrine . . 6 Averlant-petit Marie-Christine . . 7 Branlant Guy . . 8 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" 690 "13C chemical shifts" 541 "15N chemical shifts" 134 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-12 update BMRB 'added PubMed ID' 2008-10-17 update BMRB 'complete entry citation' 2007-07-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6709 'reduced form of the N-terminal domain of PilB' 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 oxidized form (Cys(67)-Cys (70)) of the N-terminal domain of PilB from Neisseria meningitidis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636850 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Quinternet Marc . . 2 Beaufils Chrystel . . 3 Neiers Fabrice . . 4 Tsan Pascale . . 5 Boschi-Muller Sandrine . . 6 Averlant-Petit Marie-Christine . . 7 Branlant Guy . . 8 Cung Manh-Thong . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 143 _Page_last 145 _Year 2007 _Details . loop_ _Keyword 'Neisseria meningitidis' 'N-terminal domain of PilB' 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Dsbe_ox _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Dsbe_ox $Dsbe_ox 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_Dsbe_ox _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dsbe_ox _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _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 2015-07-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2FY6 "Structure Of The N-Terminal Domain Of Neisseria Meningitidis Pilb" 99.31 143 100.00 100.00 3.29e-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 4.22e-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 4.22e-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 4.22e-100 EMBL CAA32146 "unnamed protein product [Neisseria gonorrhoeae]" 99.31 521 97.20 99.30 5.38e-93 EMBL CAM07595 "peptide methionine sulfoxide reductase [Neisseria meningitidis Z2491]" 99.31 522 100.00 100.00 8.67e-96 EMBL CAM09346 "peptide methionine sulfoxide reductase [Neisseria meningitidis FAM18]" 99.31 522 100.00 100.00 8.67e-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 8.67e-96 EMBL CBA03711 "Peptide methionine sulfoxide reductase [Neisseria meningitidis alpha153]" 52.78 422 98.68 100.00 2.06e-43 GB AAB97511 "putative gonococcal sensor kinase [Neisseria meningitidis]" 99.31 351 100.00 100.00 2.40e-97 GB AAF40515 "peptide methionine sulfoxide reductase [Neisseria meningitidis MC58]" 99.31 522 99.30 99.30 8.22e-95 GB AAL89752 "methionine sulfoxide reductase PilB [Neisseria gonorrhoeae]" 99.31 522 97.20 99.30 3.12e-93 GB AAW90666 "trifunctional thioredoxin/methionine sulfoxide reductase A/B protein [Neisseria gonorrhoeae FA 1090]" 99.31 522 97.20 99.30 3.33e-93 GB ABX72275 "peptide methionine sulfoxide reductase [Neisseria meningitidis 053442]" 99.31 522 100.00 100.00 8.67e-96 REF NP_273110 "trifunctional thioredoxin/methionine sulfoxide reductase A/B protein [Neisseria meningitidis MC58]" 99.31 522 99.30 99.30 8.22e-95 REF WP_002216163 "peptide methionine sulfoxide reductase MsrA/MsrB [Neisseria meningitidis]" 99.31 522 100.00 100.00 8.67e-96 REF WP_002218473 "peptide methionine sulfoxide reductase msrA/msrB, partial [Neisseria meningitidis]" 98.61 488 99.30 100.00 7.79e-95 REF WP_002221795 "methionine sulfoxide reductase [Neisseria meningitidis]" 99.31 522 100.00 100.00 1.01e-95 REF WP_002223263 "peptide methionine sulfoxide reductase MsrA/MsrB [Neisseria meningitidis]" 99.31 522 100.00 100.00 9.45e-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 3.12e-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 8.67e-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 8.22e-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_ox '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_ox 'recombinant technology' . Escherichia coli . pET 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_ox 50 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'with cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_HNHB_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_11 _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 pH 7 0.05 pH pressure 1 . atm temperature 298 0.1 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 TMS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TMS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 TMS N 15 'methyl protons' ppm 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $XEASY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HCCH-TOCSY' '3D HNHA' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '3D HNHB' 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 Dsbe_ox _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 35 4 HIS C C 178.406 0.020 1 2 35 4 HIS CA C 59.076 0.020 1 3 35 4 HIS CB C 30.614 0.020 1 4 36 5 THR H H 8.007 0.010 1 5 36 5 THR HA H 3.78 0.010 1 6 36 5 THR HB H 3.953 0.010 1 7 36 5 THR HG2 H 1.016 0.010 1 8 36 5 THR C C 177.664 0.020 1 9 36 5 THR CA C 66.145 0.020 1 10 36 5 THR CB C 68.888 0.020 1 11 36 5 THR CG2 C 22.577 0.020 1 12 36 5 THR N N 116.883 0.020 1 13 37 6 LEU H H 8.486 0.010 1 14 37 6 LEU HA H 3.722 0.010 1 15 37 6 LEU HB2 H 1.229 0.010 1 16 37 6 LEU HB3 H 1.635 0.010 1 17 37 6 LEU HD1 H 0.613 0.010 1 18 37 6 LEU HD2 H 0.553 0.010 1 19 37 6 LEU HG H 1.502 0.010 1 20 37 6 LEU C C 178.104 0.020 1 21 37 6 LEU CA C 58.525 0.020 1 22 37 6 LEU CB C 42.752 0.020 1 23 37 6 LEU CD1 C 25.453 0.020 1 24 37 6 LEU CD2 C 24.672 0.020 1 25 37 6 LEU CG C 27.22 0.020 1 26 37 6 LEU N N 121.567 0.020 1 27 38 7 SER H H 7.436 0.010 1 28 38 7 SER HA H 3.941 0.010 1 29 38 7 SER C C 175.267 0.020 1 30 38 7 SER CA C 61.954 0.020 1 31 38 7 SER CB C 63.402 0.020 1 32 38 7 SER N N 110.835 0.020 1 33 39 8 THR H H 7.5 0.010 1 34 39 8 THR HA H 4.457 0.010 1 35 39 8 THR HB H 3.854 0.010 1 36 39 8 THR HG2 H 1.085 0.010 1 37 39 8 THR C C 175.132 0.020 1 38 39 8 THR CA C 62.03 0.020 1 39 39 8 THR CB C 70.336 0.020 1 40 39 8 THR N N 110.448 0.020 1 41 40 9 LEU H H 7.193 0.010 1 42 40 9 LEU HA H 4.608 0.010 1 43 40 9 LEU HB2 H 1.595 0.010 1 44 40 9 LEU HB3 H 1.595 0.010 1 45 40 9 LEU HD1 H 0.84 0.010 1 46 40 9 LEU HD2 H 0.615 0.010 1 47 40 9 LEU C C 176.438 0.020 1 48 40 9 LEU CA C 54.563 0.020 1 49 40 9 LEU CB C 43.057 0.020 1 50 40 9 LEU CD1 C 22.119 0.020 1 51 40 9 LEU CD2 C 26.232 0.020 1 52 40 9 LEU N N 122.085 0.020 1 53 41 10 LYS H H 8.775 0.010 1 54 41 10 LYS HA H 5.246 0.010 1 55 41 10 LYS HB2 H 1.838 0.010 1 56 41 10 LYS HB3 H 1.838 0.010 1 57 41 10 LYS HD2 H 1.536 0.010 1 58 41 10 LYS HD3 H 1.448 0.010 1 59 41 10 LYS HE2 H 2.857 0.010 1 60 41 10 LYS HE3 H 2.857 0.010 1 61 41 10 LYS HG2 H 1.277 0.010 1 62 41 10 LYS HG3 H 1.277 0.010 1 63 41 10 LYS C C 177.157 0.020 1 64 41 10 LYS CA C 54.384 0.020 1 65 41 10 LYS CB C 36.885 0.020 1 66 41 10 LYS CD C 29.337 0.020 1 67 41 10 LYS CE C 42.674 0.020 1 68 41 10 LYS CG C 25.436 0.020 1 69 41 10 LYS N N 119.804 0.020 1 70 42 11 THR H H 9.303 0.010 1 71 42 11 THR HA H 5.325 0.010 1 72 42 11 THR HB H 4.892 0.010 1 73 42 11 THR HG1 H 6.179 0.010 1 74 42 11 THR HG2 H 0.964 0.010 1 75 42 11 THR C C 179.174 0.020 1 76 42 11 THR CA C 61.344 0.020 1 77 42 11 THR CB C 71.555 0.020 1 78 42 11 THR CG2 C 23.826 0.020 1 79 42 11 THR N N 108.52 0.020 1 80 43 12 ALA H H 8.603 0.010 1 81 43 12 ALA HA H 4.184 0.010 1 82 43 12 ALA HB H 1.384 0.010 1 83 43 12 ALA C C 177.232 0.020 1 84 43 12 ALA CA C 55.401 0.020 1 85 43 12 ALA CB C 18.292 0.020 1 86 43 12 ALA N N 123.487 0.020 1 87 44 13 ASP H H 8.116 0.010 1 88 44 13 ASP HA H 4.672 0.010 1 89 44 13 ASP HB2 H 3.035 0.010 1 90 44 13 ASP HB3 H 2.533 0.010 1 91 44 13 ASP C C 175.283 0.020 1 92 44 13 ASP CA C 53.076 0.020 1 93 44 13 ASP CB C 39.643 0.020 1 94 44 13 ASP N N 113.48 0.020 1 95 45 14 ASN H H 8.083 0.010 1 96 45 14 ASN HA H 4.228 0.010 1 97 45 14 ASN HB2 H 3.144 0.010 1 98 45 14 ASN HB3 H 2.712 0.010 1 99 45 14 ASN C C 174.81 0.020 1 100 45 14 ASN CA C 55.325 0.020 1 101 45 14 ASN CB C 37.494 0.020 1 102 45 14 ASN N N 114.262 0.020 1 103 46 15 ARG H H 8.166 0.010 1 104 46 15 ARG HA H 4.635 0.010 1 105 46 15 ARG HB2 H 1.632 0.010 1 106 46 15 ARG HB3 H 1.632 0.010 1 107 46 15 ARG C C 173.524 0.020 1 108 46 15 ARG CA C 54.666 0.020 1 109 46 15 ARG CB C 30.331 0.020 1 110 46 15 ARG N N 119.703 0.020 1 111 47 16 PRO HA H 4.46 0.010 1 112 47 16 PRO HB2 H 2.366 0.010 1 113 47 16 PRO HB3 H 1.985 0.010 1 114 47 16 PRO HD2 H 3.511 0.010 1 115 47 16 PRO HD3 H 3.732 0.010 1 116 47 16 PRO HG2 H 1.903 0.010 1 117 47 16 PRO HG3 H 2.061 0.010 1 118 47 16 PRO C C 178.125 0.020 1 119 47 16 PRO CA C 64.023 0.020 1 120 47 16 PRO CB C 32.236 0.020 1 121 47 16 PRO CD C 50.511 0.020 1 122 47 16 PRO CG C 28.517 0.020 1 123 48 17 ALA H H 8.53 0.010 1 124 48 17 ALA HA H 3.697 0.010 1 125 48 17 ALA HB H 1.207 0.010 1 126 48 17 ALA C C 178.387 0.020 1 127 48 17 ALA CA C 55.401 0.020 1 128 48 17 ALA CB C 19.664 0.020 1 129 48 17 ALA N N 125.272 0.020 1 130 49 18 SER H H 7.827 0.010 1 131 49 18 SER HA H 3.821 0.010 1 132 49 18 SER HB2 H 3.883 0.010 1 133 49 18 SER HB3 H 3.883 0.010 1 134 49 18 SER CA C 61.036 0.020 1 135 49 18 SER CB C 62.595 0.020 1 136 49 18 SER N N 108.504 0.020 1 137 50 19 VAL C C 177.429 0.020 1 138 50 19 VAL CA C 64.532 0.020 1 139 51 20 TYR H H 7.513 0.010 1 140 51 20 TYR HA H 4.698 0.010 1 141 51 20 TYR HB2 H 3.304 0.010 1 142 51 20 TYR HB3 H 2.477 0.010 1 143 51 20 TYR C C 175.319 0.020 1 144 51 20 TYR CA C 57.41 0.020 1 145 51 20 TYR CB C 40.618 0.020 1 146 51 20 TYR N N 117.419 0.020 1 147 52 21 LEU H H 7.187 0.010 1 148 52 21 LEU HA H 4.278 0.010 1 149 52 21 LEU HB2 H 1.175 0.010 1 150 52 21 LEU HB3 H 1.546 0.010 1 151 52 21 LEU HD1 H 0.611 0.010 1 152 52 21 LEU HD2 H 0.701 0.010 1 153 52 21 LEU HG H 1.451 0.010 1 154 52 21 LEU C C 175.884 0.020 1 155 52 21 LEU CA C 53.572 0.020 1 156 52 21 LEU CB C 42.752 0.020 1 157 52 21 LEU CD1 C 21.343 0.020 1 158 52 21 LEU CD2 C 24.017 0.020 1 159 52 21 LEU CG C 26.275 0.020 1 160 52 21 LEU N N 119.475 0.020 1 161 53 22 LYS H H 8.171 0.010 1 162 53 22 LYS HA H 4.411 0.010 1 163 53 22 LYS HB2 H 1.794 0.010 1 164 53 22 LYS HB3 H 1.794 0.010 1 165 53 22 LYS HG2 H 1.429 0.010 1 166 53 22 LYS HG3 H 1.429 0.010 1 167 53 22 LYS C C 178.595 0.020 1 168 53 22 LYS CA C 55.706 0.020 1 169 53 22 LYS CB C 32.998 0.020 1 170 53 22 LYS CG C 25.495 0.020 1 171 53 22 LYS N N 122.63 0.020 1 172 54 23 LYS H H 8.505 0.010 1 173 54 23 LYS HA H 4.029 0.010 1 174 54 23 LYS HB2 H 1.712 0.010 1 175 54 23 LYS HB3 H 1.712 0.010 1 176 54 23 LYS HD2 H 1.618 0.010 1 177 54 23 LYS HD3 H 1.618 0.010 1 178 54 23 LYS HE2 H 2.923 0.010 1 179 54 23 LYS HE3 H 2.923 0.010 1 180 54 23 LYS HG2 H 1.384 0.010 1 181 54 23 LYS HG3 H 1.384 0.010 1 182 54 23 LYS C C 176.211 0.020 1 183 54 23 LYS CA C 57.687 0.020 1 184 54 23 LYS CB C 33.303 0.020 1 185 54 23 LYS CD C 29.631 0.020 1 186 54 23 LYS CE C 42.484 0.020 1 187 54 23 LYS CG C 25.079 0.020 1 188 54 23 LYS N N 123.135 0.020 1 189 55 24 ASP H H 8.681 0.010 1 190 55 24 ASP HA H 4.251 0.010 1 191 55 24 ASP HB2 H 2.734 0.010 1 192 55 24 ASP HB3 H 2.734 0.010 1 193 55 24 ASP C C 174.716 0.020 1 194 55 24 ASP CA C 55.629 0.020 1 195 55 24 ASP CB C 39.78 0.020 1 196 55 24 ASP N N 115.209 0.020 1 197 56 25 LYS H H 7.189 0.010 1 198 56 25 LYS HA H 4.842 0.010 1 199 56 25 LYS HB2 H 1.849 0.010 1 200 56 25 LYS HB3 H 1.433 0.010 1 201 56 25 LYS HD2 H 1.25 0.010 1 202 56 25 LYS HD3 H 1.25 0.010 1 203 56 25 LYS HE2 H 2.827 0.010 1 204 56 25 LYS HE3 H 2.779 0.010 1 205 56 25 LYS HG2 H 1.2 0.010 1 206 56 25 LYS HG3 H 1.2 0.010 1 207 56 25 LYS C C 173.788 0.020 1 208 56 25 LYS CA C 54.362 0.020 1 209 56 25 LYS CB C 35.808 0.020 1 210 56 25 LYS CD C 30.163 0.020 1 211 56 25 LYS CE C 43.074 0.020 1 212 56 25 LYS CG C 25.491 0.020 1 213 56 25 LYS N N 116.725 0.020 1 214 57 26 PRO HA H 4.513 0.010 1 215 57 26 PRO HB2 H 1.836 0.010 1 216 57 26 PRO HB3 H 2.462 0.010 1 217 57 26 PRO HD2 H 3.697 0.010 1 218 57 26 PRO HD3 H 4.184 0.010 1 219 57 26 PRO HG2 H 1.919 0.010 1 220 57 26 PRO HG3 H 2.11 0.010 1 221 57 26 PRO C C 175.365 0.020 1 222 57 26 PRO CA C 63.137 0.020 1 223 57 26 PRO CB C 33.837 0.020 1 224 57 26 PRO CD C 50.844 0.020 1 225 57 26 PRO CG C 26.977 0.020 1 226 58 27 THR H H 9.347 0.010 1 227 58 27 THR HA H 4.916 0.010 1 228 58 27 THR HB H 3.716 0.010 1 229 58 27 THR HG2 H 0.84 0.010 1 230 58 27 THR C C 172.544 0.020 1 231 58 27 THR CA C 62.792 0.020 1 232 58 27 THR CB C 71.631 0.020 1 233 58 27 THR CG2 C 21.564 0.020 1 234 58 27 THR N N 116.485 0.020 1 235 59 28 LEU H H 9.2 0.010 1 236 59 28 LEU HA H 5.22 0.010 1 237 59 28 LEU HB2 H 1.963 0.010 1 238 59 28 LEU HB3 H 1.282 0.010 1 239 59 28 LEU HD1 H 0.896 0.010 1 240 59 28 LEU HD2 H 0.777 0.010 1 241 59 28 LEU HG H 1.809 0.010 1 242 59 28 LEU C C 174.318 0.020 1 243 59 28 LEU CA C 54.105 0.020 1 244 59 28 LEU CB C 44.809 0.020 1 245 59 28 LEU CD1 C 24.209 0.020 1 246 59 28 LEU CD2 C 25.707 0.020 1 247 59 28 LEU CG C 27.517 0.020 1 248 59 28 LEU N N 130.986 0.020 1 249 60 29 ILE H H 9.376 0.010 1 250 60 29 ILE HA H 4.539 0.010 1 251 60 29 ILE HB H 1.452 0.010 1 252 60 29 ILE HD1 H -0.297 0.010 1 253 60 29 ILE HG12 H 0.379 0.010 1 254 60 29 ILE HG13 H 0.379 0.010 1 255 60 29 ILE HG2 H 0.557 0.010 1 256 60 29 ILE C C 175.265 0.020 1 257 60 29 ILE CA C 60.201 0.020 1 258 60 29 ILE CB C 41.282 0.020 1 259 60 29 ILE CD1 C 18.387 0.020 1 260 60 29 ILE CG1 C 27.493 0.020 1 261 60 29 ILE CG2 C 14.475 0.020 1 262 60 29 ILE N N 123.169 0.020 1 263 61 30 LYS H H 7.899 0.010 1 264 61 30 LYS HA H 3.989 0.010 1 265 61 30 LYS HB2 H 0.735 0.010 1 266 61 30 LYS HB3 H -0.409 0.010 1 267 61 30 LYS C C 176.02 0.020 1 268 61 30 LYS CA C 54.41 0.020 1 269 61 30 LYS CB C 34.446 0.020 1 270 61 30 LYS N N 125.725 0.020 1 271 62 31 PHE H H 9.353 0.010 1 272 62 31 PHE HA H 4.939 0.010 1 273 62 31 PHE HB2 H 3.181 0.010 1 274 62 31 PHE HB3 H 2.767 0.010 1 275 62 31 PHE C C 175.254 0.020 1 276 62 31 PHE CA C 57.992 0.020 1 277 62 31 PHE CB C 40.771 0.020 1 278 62 31 PHE N N 128.456 0.020 1 279 63 32 TRP H H 7.781 0.010 1 280 63 32 TRP HA H 4.066 0.010 1 281 63 32 TRP HB2 H 2.586 0.010 1 282 63 32 TRP HB3 H 2.586 0.010 1 283 63 32 TRP HD1 H 6.737 0.010 1 284 63 32 TRP HE1 H 9.208 0.010 1 285 63 32 TRP HZ2 H 6.97 0.010 1 286 63 32 TRP C C 171.732 0.020 1 287 63 32 TRP CA C 54.944 0.020 1 288 63 32 TRP CB C 31.474 0.020 1 289 63 32 TRP N N 115.783 0.020 1 290 63 32 TRP NE1 N 127.73 0.020 1 291 64 33 ALA H H 6.047 0.010 1 292 64 33 ALA HA H 3.789 0.010 1 293 64 33 ALA HB H -0.023 0.010 1 294 64 33 ALA C C 178.182 0.020 1 295 64 33 ALA CA C 50.829 0.020 1 296 64 33 ALA CB C 23.778 0.020 1 297 64 33 ALA N N 114.63 0.020 1 298 65 34 SER H H 10.179 0.010 1 299 65 34 SER HA H 3.864 0.010 1 300 65 34 SER HB2 H 2.173 0.010 1 301 65 34 SER HB3 H 2.928 0.010 1 302 65 34 SER C C 174.425 0.020 1 303 65 34 SER CA C 61.229 0.020 1 304 65 34 SER CB C 61.637 0.020 1 305 65 34 SER N N 118.547 0.020 1 306 66 35 TRP H H 6.125 0.010 1 307 66 35 TRP HA H 4.521 0.010 1 308 66 35 TRP HB2 H 3.66 0.010 1 309 66 35 TRP HB3 H 2.993 0.010 1 310 66 35 TRP HD1 H 6.833 0.010 1 311 66 35 TRP HE1 H 9.304 0.010 1 312 66 35 TRP HZ2 H 7.738 0.010 1 313 66 35 TRP C C 175.666 0.020 1 314 66 35 TRP CA C 53.877 0.020 1 315 66 35 TRP CB C 30.06 0.020 1 316 66 35 TRP N N 114.871 0.020 1 317 66 35 TRP NE1 N 128.74 0.020 1 318 67 36 CYS H H 6.946 0.010 1 319 67 36 CYS HA H 5.229 0.010 1 320 67 36 CYS HB2 H 3.292 0.010 1 321 67 36 CYS HB3 H 3.145 0.010 1 322 67 36 CYS C C 172.624 0.020 1 323 67 36 CYS CA C 51.972 0.020 1 324 67 36 CYS CB C 45.266 0.020 1 325 67 36 CYS N N 123.775 0.020 1 326 68 37 PRO HA H 4.251 0.010 1 327 68 37 PRO HB2 H 2.013 0.010 1 328 68 37 PRO HB3 H 2.417 0.010 1 329 68 37 PRO HD2 H 4.06 0.010 1 330 68 37 PRO HD3 H 4.06 0.010 1 331 68 37 PRO HG2 H 2.191 0.010 1 332 68 37 PRO HG3 H 2.191 0.010 1 333 68 37 PRO C C 181.266 0.020 1 334 68 37 PRO CA C 66.907 0.020 1 335 68 37 PRO CB C 32.539 0.020 1 336 68 37 PRO CD C 52.253 0.020 1 337 68 37 PRO CG C 28.584 0.020 1 338 69 38 LEU H H 8.974 0.010 1 339 69 38 LEU HA H 4.201 0.010 1 340 69 38 LEU HB2 H 1.656 0.010 1 341 69 38 LEU HB3 H 1.549 0.010 1 342 69 38 LEU HD1 H 0.865 0.010 1 343 69 38 LEU HD2 H 0.906 0.010 1 344 69 38 LEU HG H 1.459 0.010 1 345 69 38 LEU C C 179.564 0.020 1 346 69 38 LEU CA C 57.915 0.020 1 347 69 38 LEU CB C 42.447 0.020 1 348 69 38 LEU CD1 C 23.9 0.020 1 349 69 38 LEU CD2 C 25.717 0.020 1 350 69 38 LEU CG C 27.612 0.020 1 351 69 38 LEU N N 120.561 0.020 1 352 70 39 CYS H H 8.375 0.010 1 353 70 39 CYS HA H 3.863 0.010 1 354 70 39 CYS HB2 H 2.729 0.010 1 355 70 39 CYS HB3 H 4.475 0.010 1 356 70 39 CYS C C 178.022 0.020 1 357 70 39 CYS CA C 63.859 0.020 1 358 70 39 CYS CB C 34.141 0.020 1 359 70 39 CYS N N 111.935 0.020 1 360 71 40 LEU H H 7.892 0.010 1 361 71 40 LEU HA H 3.84 0.010 1 362 71 40 LEU HB2 H 1.578 0.010 1 363 71 40 LEU HB3 H 2.035 0.010 1 364 71 40 LEU HD1 H 1.166 0.010 1 365 71 40 LEU HD2 H 1.18 0.010 1 366 71 40 LEU HG H 2.849 0.010 1 367 71 40 LEU C C 180.536 0.020 1 368 71 40 LEU CA C 57.915 0.020 1 369 71 40 LEU CB C 40.923 0.020 1 370 71 40 LEU CD1 C 23.616 0.020 1 371 71 40 LEU CD2 C 25.674 0.020 1 372 71 40 LEU CG C 27.256 0.020 1 373 71 40 LEU N N 120.086 0.020 1 374 72 41 SER H H 8.085 0.010 1 375 72 41 SER HA H 4.201 0.010 1 376 72 41 SER HB2 H 3.941 0.010 1 377 72 41 SER HB3 H 3.941 0.010 1 378 72 41 SER C C 176.242 0.020 1 379 72 41 SER CA C 61.649 0.020 1 380 72 41 SER CB C 63.021 0.020 1 381 72 41 SER N N 116.51 0.020 1 382 73 42 GLU H H 7.231 0.010 1 383 73 42 GLU HA H 4.076 0.010 1 384 73 42 GLU HB2 H 1.791 0.010 1 385 73 42 GLU HB3 H 1.349 0.010 1 386 73 42 GLU HG2 H 2.573 0.010 1 387 73 42 GLU HG3 H 2.02 0.010 1 388 73 42 GLU C C 177.621 0.020 1 389 73 42 GLU CA C 56.738 0.020 1 390 73 42 GLU CB C 32.236 0.020 1 391 73 42 GLU CG C 36.472 0.020 1 392 73 42 GLU N N 116.067 0.020 1 393 74 43 LEU H H 7.006 0.010 1 394 74 43 LEU HA H 2.999 0.010 1 395 74 43 LEU HB2 H -0.313 0.010 1 396 74 43 LEU HB3 H 0.879 0.010 1 397 74 43 LEU HD1 H -0.845 0.010 1 398 74 43 LEU HD2 H 0.378 0.010 1 399 74 43 LEU HG H 1.467 0.010 1 400 74 43 LEU C C 177.832 0.020 1 401 74 43 LEU CA C 59.668 0.020 1 402 74 43 LEU CB C 39.856 0.020 1 403 74 43 LEU CD1 C 20.751 0.020 1 404 74 43 LEU CD2 C 26.552 0.020 1 405 74 43 LEU CG C 25.64 0.020 1 406 74 43 LEU N N 123.179 0.020 1 407 75 44 GLY H H 8.304 0.010 1 408 75 44 GLY HA2 H 3.61 0.010 1 409 75 44 GLY HA3 H 3.835 0.010 1 410 75 44 GLY C C 177.41 0.020 1 411 75 44 GLY CA C 47.483 0.020 1 412 75 44 GLY N N 105.202 0.020 1 413 76 45 GLN H H 7.94 0.010 1 414 76 45 GLN HA H 3.765 0.010 1 415 76 45 GLN HB2 H 1.663 0.010 1 416 76 45 GLN HB3 H 1.787 0.010 1 417 76 45 GLN HG2 H 1.83 0.010 1 418 76 45 GLN HG3 H 1.496 0.010 1 419 76 45 GLN C C 176.438 0.020 1 420 76 45 GLN CA C 58.601 0.020 1 421 76 45 GLN CB C 29.188 0.020 1 422 76 45 GLN CG C 34.423 0.020 1 423 76 45 GLN N N 123.478 0.020 1 424 77 46 THR H H 7.546 0.010 1 425 77 46 THR HA H 2.774 0.010 1 426 77 46 THR HB H 3.486 0.010 1 427 77 46 THR HG2 H 0.749 0.010 1 428 77 46 THR C C 175.519 0.020 1 429 77 46 THR CA C 66.983 0.020 1 430 77 46 THR CB C 68.126 0.020 1 431 77 46 THR CG2 C 23.29 0.020 1 432 77 46 THR N N 114.337 0.020 1 433 78 47 GLU H H 7.996 0.010 1 434 78 47 GLU HA H 3.316 0.010 1 435 78 47 GLU HB2 H 2.233 0.010 1 436 78 47 GLU HB3 H 1.669 0.010 1 437 78 47 GLU HG2 H 1.943 0.010 1 438 78 47 GLU HG3 H 1.943 0.010 1 439 78 47 GLU C C 178.022 0.020 1 440 78 47 GLU CA C 60.294 0.020 1 441 78 47 GLU CB C 30.255 0.020 1 442 78 47 GLU CG C 37.079 0.020 1 443 78 47 GLU N N 121.53 0.020 1 444 79 48 LYS H H 7.324 0.010 1 445 79 48 LYS HA H 3.893 0.010 1 446 79 48 LYS HB2 H 1.985 0.010 1 447 79 48 LYS HB3 H 1.985 0.010 1 448 79 48 LYS C C 180.938 0.020 1 449 79 48 LYS CA C 60.278 0.020 1 450 79 48 LYS CB C 32.084 0.020 1 451 79 48 LYS N N 119.119 0.020 1 452 80 49 TRP H H 8.195 0.010 1 453 80 49 TRP HA H 4.277 0.010 1 454 80 49 TRP HB2 H 1.53 0.010 1 455 80 49 TRP HB3 H 2.813 0.010 1 456 80 49 TRP HE1 H 9.994 0.010 1 457 80 49 TRP C C 178.213 0.020 1 458 80 49 TRP CA C 58.601 0.020 1 459 80 49 TRP CB C 28.655 0.020 1 460 80 49 TRP N N 121.806 0.020 1 461 80 49 TRP NE1 N 126.673 0.020 1 462 81 50 ALA H H 7.757 0.010 1 463 81 50 ALA HA H 3.91 0.010 1 464 81 50 ALA HB H 1.422 0.010 1 465 81 50 ALA C C 179.374 0.020 1 466 81 50 ALA CA C 54.944 0.020 1 467 81 50 ALA CB C 18.216 0.020 1 468 81 50 ALA N N 116.063 0.020 1 469 82 51 GLN H H 7.266 0.010 1 470 82 51 GLN HA H 4.475 0.010 1 471 82 51 GLN HB2 H 2.276 0.010 1 472 82 51 GLN HB3 H 1.99 0.010 1 473 82 51 GLN HG2 H 2.393 0.010 1 474 82 51 GLN HG3 H 2.393 0.010 1 475 82 51 GLN C C 175.361 0.020 1 476 82 51 GLN CA C 55.325 0.020 1 477 82 51 GLN CB C 32.236 0.020 1 478 82 51 GLN CG C 34.799 0.020 1 479 82 51 GLN N N 113.689 0.020 1 480 83 52 ASP H H 7.729 0.010 1 481 83 52 ASP HA H 4.567 0.010 1 482 83 52 ASP HB2 H 2.926 0.010 1 483 83 52 ASP HB3 H 3.24 0.010 1 484 83 52 ASP C C 178.783 0.020 1 485 83 52 ASP CA C 54.944 0.020 1 486 83 52 ASP CB C 44.352 0.020 1 487 83 52 ASP N N 123.431 0.020 1 488 84 53 ALA H H 9.242 0.010 1 489 84 53 ALA HA H 4.17 0.010 1 490 84 53 ALA HB H 1.449 0.010 1 491 84 53 ALA C C 181.106 0.020 1 492 84 53 ALA CA C 55.706 0.020 1 493 84 53 ALA CB C 18.978 0.020 1 494 84 53 ALA N N 133.599 0.020 1 495 85 54 LYS H H 9.511 0.010 1 496 85 54 LYS HA H 3.903 0.010 1 497 85 54 LYS HB2 H 1.315 0.010 1 498 85 54 LYS HB3 H 1.477 0.010 1 499 85 54 LYS HE2 H 2.764 0.010 1 500 85 54 LYS HE3 H 2.694 0.010 1 501 85 54 LYS C C 178.191 0.020 1 502 85 54 LYS CA C 59.82 0.020 1 503 85 54 LYS CB C 32.084 0.020 1 504 85 54 LYS CE C 41.477 0.020 1 505 85 54 LYS N N 119.002 0.020 1 506 86 55 PHE H H 7.836 0.010 1 507 86 55 PHE HA H 4.17 0.010 1 508 86 55 PHE HB2 H 3.209 0.010 1 509 86 55 PHE HB3 H 3.209 0.010 1 510 86 55 PHE C C 176.628 0.020 1 511 86 55 PHE CA C 59.211 0.020 1 512 86 55 PHE CB C 39.856 0.020 1 513 86 55 PHE N N 116.604 0.020 1 514 87 56 SER H H 7.528 0.010 1 515 87 56 SER HA H 4.216 0.010 1 516 87 56 SER HB2 H 3.987 0.010 1 517 87 56 SER HB3 H 3.987 0.010 1 518 87 56 SER C C 175.128 0.020 1 519 87 56 SER CA C 61.954 0.020 1 520 87 56 SER CB C 63.935 0.020 1 521 87 56 SER N N 113.462 0.020 1 522 88 57 SER H H 7.995 0.010 1 523 88 57 SER HA H 4.246 0.010 1 524 88 57 SER HB2 H 3.746 0.010 1 525 88 57 SER HB3 H 3.857 0.010 1 526 88 57 SER C C 172.699 0.020 1 527 88 57 SER CA C 59.744 0.020 1 528 88 57 SER CB C 63.478 0.020 1 529 88 57 SER N N 116.22 0.020 1 530 89 58 ALA H H 8.089 0.010 1 531 89 58 ALA HA H 4.826 0.010 1 532 89 58 ALA HB H 1.181 0.010 1 533 89 58 ALA C C 176.692 0.020 1 534 89 58 ALA CA C 50.676 0.020 1 535 89 58 ALA CB C 23.093 0.020 1 536 89 58 ALA N N 122.334 0.020 1 537 90 59 ASN H H 9.152 0.010 1 538 90 59 ASN HA H 4.963 0.010 1 539 90 59 ASN HB2 H 2.63 0.010 1 540 90 59 ASN HB3 H 2.904 0.010 1 541 90 59 ASN C C 174.093 0.020 1 542 90 59 ASN CA C 52.962 0.020 1 543 90 59 ASN CB C 40.161 0.020 1 544 90 59 ASN N N 116.698 0.020 1 545 91 60 LEU H H 8.462 0.010 1 546 91 60 LEU HA H 5.39 0.010 1 547 91 60 LEU HB2 H 1.447 0.010 1 548 91 60 LEU HB3 H 1.708 0.010 1 549 91 60 LEU HD1 H 0.673 0.010 1 550 91 60 LEU HD2 H 0.868 0.010 1 551 91 60 LEU HG H 1.574 0.010 1 552 91 60 LEU C C 175.762 0.020 1 553 91 60 LEU CA C 55.629 0.020 1 554 91 60 LEU CB C 44.504 0.020 1 555 91 60 LEU CD1 C 25.303 0.020 1 556 91 60 LEU CD2 C 26.326 0.020 1 557 91 60 LEU CG C 29.754 0.020 1 558 91 60 LEU N N 127.76 0.020 1 559 92 61 ILE H H 8.552 0.010 1 560 92 61 ILE HA H 4.432 0.010 1 561 92 61 ILE HB H 1.365 0.010 1 562 92 61 ILE HD1 H 0.497 0.010 1 563 92 61 ILE HG12 H 0.994 0.010 1 564 92 61 ILE HG13 H 0.994 0.010 1 565 92 61 ILE HG2 H 0.592 0.010 1 566 92 61 ILE C C 173.122 0.020 1 567 92 61 ILE CA C 59.058 0.020 1 568 92 61 ILE CB C 43.819 0.020 1 569 92 61 ILE CD1 C 14.683 0.020 1 570 92 61 ILE CG1 C 27.047 0.020 1 571 92 61 ILE CG2 C 18.609 0.020 1 572 92 61 ILE N N 117.511 0.020 1 573 93 62 THR H H 6.859 0.010 1 574 93 62 THR HA H 5.328 0.010 1 575 93 62 THR HB H 4.073 0.010 1 576 93 62 THR HG2 H 0.741 0.010 1 577 93 62 THR C C 172.256 0.020 1 578 93 62 THR CA C 59.202 0.020 1 579 93 62 THR CB C 70.641 0.020 1 580 93 62 THR CG2 C 21.605 0.020 1 581 93 62 THR N N 111.24 0.020 1 582 94 63 VAL H H 8.672 0.010 1 583 94 63 VAL HA H 4.694 0.010 1 584 94 63 VAL HB H 0.922 0.010 1 585 94 63 VAL HG1 H 0.584 0.010 1 586 94 63 VAL HG2 H 0.175 0.010 1 587 94 63 VAL C C 174.283 0.020 1 588 94 63 VAL CA C 61.04 0.020 1 589 94 63 VAL CB C 35.97 0.020 1 590 94 63 VAL CG1 C 22.262 0.020 1 591 94 63 VAL CG2 C 22.262 0.020 1 592 94 63 VAL N N 122.198 0.020 1 593 95 64 ALA H H 7.974 0.010 1 594 95 64 ALA HA H 3.957 0.010 1 595 95 64 ALA HB H -0.343 0.010 1 596 95 64 ALA C C 176.839 0.020 1 597 95 64 ALA CA C 49.457 0.020 1 598 95 64 ALA CB C 22.559 0.020 1 599 95 64 ALA N N 129.104 0.020 1 600 96 65 SER H H 8.931 0.010 1 601 96 65 SER HA H 4.795 0.010 1 602 96 65 SER HB2 H 3.395 0.010 1 603 96 65 SER HB3 H 4.124 0.010 1 604 96 65 SER CA C 55.401 0.020 1 605 96 65 SER CB C 65.154 0.020 1 606 96 65 SER N N 118.115 0.020 1 607 97 66 PRO HA H 4.053 0.010 1 608 97 66 PRO HB2 H 2.312 0.010 1 609 97 66 PRO HB3 H 2.312 0.010 1 610 97 66 PRO HD2 H 2.923 0.010 1 611 97 66 PRO HD3 H 2.923 0.010 1 612 97 66 PRO C C 176.782 0.020 1 613 97 66 PRO CA C 64.392 0.020 1 614 97 66 PRO CB C 32.008 0.020 1 615 97 66 PRO CD C 50.144 0.020 1 616 98 67 GLY H H 7.022 0.010 1 617 98 67 GLY HA2 H 3.484 0.010 1 618 98 67 GLY HA3 H 4.148 0.010 1 619 98 67 GLY C C 173.454 0.020 1 620 98 67 GLY CA C 46.257 0.020 1 621 98 67 GLY N N 109.457 0.020 1 622 99 68 PHE H H 7.929 0.010 1 623 99 68 PHE HA H 4.795 0.010 1 624 99 68 PHE HB2 H 2.257 0.010 1 625 99 68 PHE HB3 H 3.028 0.010 1 626 99 68 PHE C C 176.248 0.020 1 627 99 68 PHE CA C 56.115 0.020 1 628 99 68 PHE CB C 41.304 0.020 1 629 99 68 PHE N N 122.503 0.020 1 630 100 69 LEU H H 8.875 0.010 1 631 100 69 LEU HA H 3.169 0.010 1 632 100 69 LEU HB2 H 1.536 0.010 1 633 100 69 LEU HB3 H 0.987 0.010 1 634 100 69 LEU HD1 H 0.306 0.010 1 635 100 69 LEU HD2 H 0.038 0.010 1 636 100 69 LEU HG H 0.306 0.010 1 637 100 69 LEU C C 176.375 0.020 1 638 100 69 LEU CA C 55.706 0.020 1 639 100 69 LEU CB C 40.237 0.020 1 640 100 69 LEU CD1 C 22.834 0.020 1 641 100 69 LEU CD2 C 25.909 0.020 1 642 100 69 LEU CG C 25.193 0.020 1 643 100 69 LEU N N 132.024 0.020 1 644 101 70 HIS H H 8.16 0.010 1 645 101 70 HIS HA H 3.847 0.010 1 646 101 70 HIS HB2 H 2.895 0.010 1 647 101 70 HIS HB3 H 2.895 0.010 1 648 101 70 HIS C C 175.826 0.020 1 649 101 70 HIS CA C 57.915 0.020 1 650 101 70 HIS CB C 27.283 0.020 1 651 101 70 HIS N N 106.93 0.020 1 652 102 71 GLU H H 7.809 0.010 1 653 102 71 GLU HA H 4.397 0.010 1 654 102 71 GLU HB2 H 2.356 0.010 1 655 102 71 GLU HB3 H 1.974 0.010 1 656 102 71 GLU C C 175.889 0.020 1 657 102 71 GLU CA C 56.304 0.020 1 658 102 71 GLU CB C 31.246 0.020 1 659 102 71 GLU CG C 35.468 0.020 1 660 102 71 GLU N N 120.338 0.020 1 661 103 72 LYS H H 10.095 0.010 1 662 103 72 LYS HA H 4.048 0.010 1 663 103 72 LYS HD2 H 1.392 0.010 1 664 103 72 LYS HD3 H 1.029 0.010 1 665 103 72 LYS HE2 H 2.173 0.010 1 666 103 72 LYS HE3 H 2.173 0.010 1 667 103 72 LYS C C 176.659 0.020 1 668 103 72 LYS CA C 58.144 0.020 1 669 103 72 LYS CB C 35.208 0.020 1 670 103 72 LYS CD C 30.682 0.020 1 671 103 72 LYS CE C 41.516 0.020 1 672 103 72 LYS N N 129.089 0.020 1 673 104 73 LYS H H 8.573 0.010 1 674 104 73 LYS HA H 3.962 0.010 1 675 104 73 LYS HB2 H 1.868 0.010 1 676 104 73 LYS HB3 H 1.868 0.010 1 677 104 73 LYS HD2 H 1.669 0.010 1 678 104 73 LYS HD3 H 1.669 0.010 1 679 104 73 LYS HE2 H 2.982 0.010 1 680 104 73 LYS HE3 H 2.982 0.010 1 681 104 73 LYS HG2 H 1.504 0.010 1 682 104 73 LYS HG3 H 1.504 0.010 1 683 104 73 LYS C C 176.435 0.020 1 684 104 73 LYS CA C 56.62 0.020 1 685 104 73 LYS CB C 33.989 0.020 1 686 104 73 LYS CD C 29.662 0.020 1 687 104 73 LYS CE C 42.517 0.020 1 688 104 73 LYS CG C 25.48 0.020 1 689 104 73 LYS N N 119.846 0.020 1 690 105 74 ASP H H 9.008 0.010 1 691 105 74 ASP HA H 4.322 0.010 1 692 105 74 ASP HB2 H 2.371 0.010 1 693 105 74 ASP HB3 H 2.523 0.010 1 694 105 74 ASP C C 177.811 0.020 1 695 105 74 ASP CA C 57.763 0.020 1 696 105 74 ASP CB C 41.761 0.020 1 697 105 74 ASP N N 122.554 0.020 1 698 106 75 GLY H H 9.526 0.010 1 699 106 75 GLY HA2 H 4.612 0.010 1 700 106 75 GLY HA3 H 3.362 0.010 1 701 106 75 GLY C C 176.44 0.020 1 702 106 75 GLY CA C 46.867 0.020 1 703 106 75 GLY N N 118.737 0.020 1 704 107 76 ASP H H 7.31 0.010 1 705 107 76 ASP HA H 4.429 0.010 1 706 107 76 ASP HB2 H 2.645 0.010 1 707 107 76 ASP HB3 H 2.904 0.010 1 708 107 76 ASP C C 180.379 0.020 1 709 107 76 ASP CA C 57.611 0.020 1 710 107 76 ASP CB C 40.542 0.020 1 711 107 76 ASP N N 123.289 0.020 1 712 108 77 PHE H H 9.023 0.010 1 713 108 77 PHE HA H 3.804 0.010 1 714 108 77 PHE HB2 H 2.645 0.010 1 715 108 77 PHE HB3 H 2.95 0.010 1 716 108 77 PHE C C 176.44 0.020 1 717 108 77 PHE CA C 63.935 0.020 1 718 108 77 PHE CB C 38.561 0.020 1 719 108 77 PHE N N 121.015 0.020 1 720 109 78 GLN H H 10.253 0.010 1 721 109 78 GLN HA H 3.664 0.010 1 722 109 78 GLN HB2 H 2.218 0.010 1 723 109 78 GLN HB3 H 2.218 0.010 1 724 109 78 GLN HG2 H 3.362 0.010 1 725 109 78 GLN HG3 H 2.246 0.010 1 726 109 78 GLN C C 179.175 0.020 1 727 109 78 GLN CA C 62.411 0.020 1 728 109 78 GLN CB C 27.36 0.020 1 729 109 78 GLN CG C 36.747 0.020 1 730 109 78 GLN N N 121.105 0.020 1 731 110 79 LYS H H 7.704 0.010 1 732 110 79 LYS HA H 3.992 0.010 1 733 110 79 LYS HB2 H 1.864 0.010 1 734 110 79 LYS HB3 H 1.864 0.010 1 735 110 79 LYS HD2 H 1.629 0.010 1 736 110 79 LYS HD3 H 1.629 0.010 1 737 110 79 LYS HE2 H 2.899 0.010 1 738 110 79 LYS HE3 H 2.899 0.010 1 739 110 79 LYS HG2 H 1.374 0.010 1 740 110 79 LYS HG3 H 1.374 0.010 1 741 110 79 LYS C C 178.991 0.020 1 742 110 79 LYS CA C 59.92 0.020 1 743 110 79 LYS CB C 33.075 0.020 1 744 110 79 LYS CD C 29.752 0.020 1 745 110 79 LYS CE C 42.517 0.020 1 746 110 79 LYS CG C 24.692 0.020 1 747 110 79 LYS N N 120.487 0.020 1 748 111 80 TRP H H 7.759 0.010 1 749 111 80 TRP HA H 4.022 0.010 1 750 111 80 TRP HB2 H 3.375 0.010 1 751 111 80 TRP HB3 H 3.187 0.010 1 752 111 80 TRP HE1 H 10.15 0.010 1 753 111 80 TRP C C 178.787 0.020 1 754 111 80 TRP CA C 61.421 0.020 1 755 111 80 TRP CB C 27.741 0.020 1 756 111 80 TRP N N 121.02 0.020 1 757 111 80 TRP NE1 N 131.199 0.020 1 758 112 81 TYR H H 8.892 0.010 1 759 112 81 TYR HA H 2.676 0.010 1 760 112 81 TYR HB2 H 2.424 0.010 1 761 112 81 TYR HB3 H 2.424 0.010 1 762 112 81 TYR C C 177.419 0.020 1 763 112 81 TYR CA C 61.421 0.020 1 764 112 81 TYR CB C 38.561 0.020 1 765 112 81 TYR N N 121.07 0.020 1 766 113 82 ALA H H 7.513 0.010 1 767 113 82 ALA HA H 3.828 0.010 1 768 113 82 ALA HB H 1.336 0.010 1 769 113 82 ALA C C 178.766 0.020 1 770 113 82 ALA CA C 54.105 0.020 1 771 113 82 ALA CB C 18.368 0.020 1 772 113 82 ALA N N 119.428 0.020 1 773 114 83 GLY H H 7.134 0.010 1 774 114 83 GLY HA2 H 3.865 0.010 1 775 114 83 GLY HA3 H 3.453 0.010 1 776 114 83 GLY C C 174.113 0.020 1 777 114 83 GLY CA C 45.419 0.020 1 778 114 83 GLY N N 102.936 0.020 1 779 115 84 LEU H H 7.135 0.010 1 780 115 84 LEU HA H 3.955 0.010 1 781 115 84 LEU HB2 H 1.107 0.010 1 782 115 84 LEU HB3 H 1.107 0.010 1 783 115 84 LEU HD1 H 0.214 0.010 1 784 115 84 LEU HD2 H 0.443 0.010 1 785 115 84 LEU HG H 0.929 0.010 1 786 115 84 LEU C C 176.236 0.020 1 787 115 84 LEU CA C 54.639 0.020 1 788 115 84 LEU CB C 42.066 0.020 1 789 115 84 LEU CD1 C 25.087 0.020 1 790 115 84 LEU CD2 C 23.215 0.020 1 791 115 84 LEU CG C 28.047 0.020 1 792 115 84 LEU N N 121.828 0.020 1 793 116 85 ASN H H 7.454 0.010 1 794 116 85 ASN HA H 4.561 0.010 1 795 116 85 ASN HB2 H 2.382 0.010 1 796 116 85 ASN HB3 H 2.081 0.010 1 797 116 85 ASN C C 173.113 0.020 1 798 116 85 ASN CA C 52.124 0.020 1 799 116 85 ASN CB C 38.866 0.020 1 800 116 85 ASN N N 117.411 0.020 1 801 117 86 TYR H H 8.13 0.010 1 802 117 86 TYR HA H 4.665 0.010 1 803 117 86 TYR HB2 H 2.587 0.010 1 804 117 86 TYR HB3 H 2.587 0.010 1 805 117 86 TYR C C 175.174 0.020 1 806 117 86 TYR CA C 56.239 0.020 1 807 117 86 TYR CB C 37.342 0.020 1 808 117 86 TYR N N 119.557 0.020 1 809 118 87 PRO HA H 4.265 0.010 1 810 118 87 PRO HB2 H 1.866 0.010 1 811 118 87 PRO HB3 H 2.229 0.010 1 812 118 87 PRO HD2 H 3.627 0.010 1 813 118 87 PRO HD3 H 3.096 0.010 1 814 118 87 PRO HG2 H 1.757 0.010 1 815 118 87 PRO HG3 H 1.851 0.010 1 816 118 87 PRO C C 177.533 0.020 1 817 118 87 PRO CA C 65.459 0.020 1 818 118 87 PRO CB C 32.667 0.020 1 819 118 87 PRO CD C 50.443 0.020 1 820 118 87 PRO CG C 27.682 0.020 1 821 119 88 LYS H H 9.115 0.010 1 822 119 88 LYS HA H 4.414 0.010 1 823 119 88 LYS HB2 H 1.865 0.010 1 824 119 88 LYS HB3 H 1.667 0.010 1 825 119 88 LYS C C 176.032 0.020 1 826 119 88 LYS CA C 54.944 0.020 1 827 119 88 LYS CB C 32.008 0.020 1 828 119 88 LYS N N 117.653 0.020 1 829 120 89 LEU H H 7.654 0.010 1 830 120 89 LEU HA H 4.26 0.010 1 831 120 89 LEU HB2 H 2.166 0.010 1 832 120 89 LEU HB3 H 0.751 0.010 1 833 120 89 LEU HD1 H 0.346 0.010 1 834 120 89 LEU HD2 H 0.373 0.010 1 835 120 89 LEU C C 174.48 0.020 1 836 120 89 LEU CA C 52.277 0.020 1 837 120 89 LEU CB C 44.733 0.020 1 838 120 89 LEU CD1 C 24.162 0.020 1 839 120 89 LEU CD2 C 27.271 0.020 1 840 120 89 LEU N N 123.348 0.020 1 841 121 90 PRO HA H 4.05 0.010 1 842 121 90 PRO HB2 H 1.317 0.010 1 843 121 90 PRO HB3 H 1.317 0.010 1 844 121 90 PRO HD2 H 3.064 0.010 1 845 121 90 PRO HD3 H 3.064 0.010 1 846 121 90 PRO HG2 H 2.159 0.010 1 847 121 90 PRO HG3 H 1.413 0.010 1 848 121 90 PRO C C 177.553 0.020 1 849 121 90 PRO CA C 62.846 0.020 1 850 121 90 PRO CB C 32.16 0.020 1 851 121 90 PRO CD C 51.734 0.020 1 852 121 90 PRO CG C 28.671 0.020 1 853 122 91 VAL H H 8.521 0.010 1 854 122 91 VAL HA H 4.112 0.010 1 855 122 91 VAL HB H 1.755 0.010 1 856 122 91 VAL HG1 H 0.473 0.010 1 857 122 91 VAL HG2 H 0.746 0.010 1 858 122 91 VAL C C 174.399 0.020 1 859 122 91 VAL CA C 62.64 0.020 1 860 122 91 VAL CB C 34.294 0.020 1 861 122 91 VAL CG1 C 21.426 0.020 1 862 122 91 VAL CG2 C 21.534 0.020 1 863 122 91 VAL N N 129.734 0.020 1 864 123 92 VAL H H 8.883 0.010 1 865 123 92 VAL HA H 4.265 0.010 1 866 123 92 VAL HB H 1.913 0.010 1 867 123 92 VAL HG1 H 0.719 0.010 1 868 123 92 VAL HG2 H 0.784 0.010 1 869 123 92 VAL C C 175.072 0.020 1 870 123 92 VAL CA C 61.725 0.020 1 871 123 92 VAL CB C 33.76 0.020 1 872 123 92 VAL CG1 C 21.316 0.020 1 873 123 92 VAL CG2 C 23.043 0.020 1 874 123 92 VAL N N 128.277 0.020 1 875 124 93 THR H H 8.58 0.010 1 876 124 93 THR HA H 4.81 0.010 1 877 124 93 THR HB H 3.68 0.010 1 878 124 93 THR HG2 H 0.73 0.010 1 879 124 93 THR C C 173.521 0.020 1 880 124 93 THR CA C 58.754 0.020 1 881 124 93 THR CB C 69.193 0.020 1 882 124 93 THR CG2 C 22.234 0.020 1 883 124 93 THR N N 114.523 0.020 1 884 125 94 ASP H H 8.448 0.010 1 885 125 94 ASP HA H 4.771 0.010 1 886 125 94 ASP HB2 H 2.708 0.010 1 887 125 94 ASP HB3 H 1.95 0.010 1 888 125 94 ASP C C 176.358 0.020 1 889 125 94 ASP CA C 51.134 0.020 1 890 125 94 ASP CB C 42.064 0.020 1 891 125 94 ASP N N 123.879 0.020 1 892 126 95 ASN H H 8.34 0.010 1 893 126 95 ASN HA H 4.414 0.010 1 894 126 95 ASN HB2 H 2.731 0.010 1 895 126 95 ASN HB3 H 2.731 0.010 1 896 126 95 ASN C C 177.419 0.020 1 897 126 95 ASN CA C 55.782 0.020 1 898 126 95 ASN CB C 38.104 0.020 1 899 126 95 ASN N N 124.334 0.020 1 900 127 96 GLY H H 9.387 0.010 1 901 127 96 GLY HA2 H 4.155 0.010 1 902 127 96 GLY HA3 H 3.423 0.010 1 903 127 96 GLY C C 175.442 0.020 1 904 127 96 GLY CA C 45.495 0.020 1 905 127 96 GLY N N 115.983 0.020 1 906 128 97 GLY H H 8.645 0.010 1 907 128 97 GLY HA2 H 2.695 0.010 1 908 128 97 GLY HA3 H 3.499 0.010 1 909 128 97 GLY C C 173.987 0.020 1 910 128 97 GLY CA C 48.238 0.020 1 911 128 97 GLY N N 109.758 0.020 1 912 129 98 THR H H 7.38 0.010 1 913 129 98 THR HA H 3.469 0.010 1 914 129 98 THR HB H 3.953 0.010 1 915 129 98 THR HG2 H 1.068 0.010 1 916 129 98 THR C C 178.613 0.020 1 917 129 98 THR CA C 66.754 0.020 1 918 129 98 THR CB C 68.583 0.020 1 919 129 98 THR CG2 C 22.341 0.020 1 920 129 98 THR N N 113.603 0.020 1 921 130 99 ILE H H 10.546 0.010 1 922 130 99 ILE HA H 3.453 0.010 1 923 130 99 ILE HB H 1.752 0.010 1 924 130 99 ILE HD1 H 0.572 0.010 1 925 130 99 ILE HG12 H 0.794 0.010 1 926 130 99 ILE HG13 H 0.794 0.010 1 927 130 99 ILE HG2 H 1.071 0.010 1 928 130 99 ILE C C 178.979 0.020 1 929 130 99 ILE CA C 65.916 0.020 1 930 130 99 ILE CB C 37.418 0.020 1 931 130 99 ILE CD1 C 14.135 0.020 1 932 130 99 ILE CG1 C 18.711 0.020 1 933 130 99 ILE CG2 C 22.117 0.020 1 934 130 99 ILE N N 127.138 0.020 1 935 131 100 ALA H H 9.209 0.010 1 936 131 100 ALA HA H 3.118 0.010 1 937 131 100 ALA HB H 0.968 0.010 1 938 131 100 ALA C C 180.732 0.020 1 939 131 100 ALA CA C 56.087 0.020 1 940 131 100 ALA CB C 17.606 0.020 1 941 131 100 ALA N N 124.587 0.020 1 942 132 101 GLN H H 8.17 0.010 1 943 132 101 GLN HA H 3.987 0.010 1 944 132 101 GLN HB2 H 1.88 0.010 1 945 132 101 GLN HB3 H 1.775 0.010 1 946 132 101 GLN HG2 H 2.085 0.010 1 947 132 101 GLN HG3 H 2.085 0.010 1 948 132 101 GLN C C 180.531 0.020 1 949 132 101 GLN CA C 59.82 0.020 1 950 132 101 GLN CB C 30.255 0.020 1 951 132 101 GLN N N 114.649 0.020 1 952 133 102 SER H H 7.53 0.010 1 953 133 102 SER HA H 4.101 0.010 1 954 133 102 SER HB2 H 3.893 0.010 1 955 133 102 SER HB3 H 3.893 0.010 1 956 133 102 SER C C 175.672 0.020 1 957 133 102 SER CA C 61.878 0.020 1 958 133 102 SER CB C 63.173 0.020 1 959 133 102 SER N N 117.622 0.020 1 960 134 103 LEU H H 7.415 0.010 1 961 134 103 LEU HA H 4.184 0.010 1 962 134 103 LEU HB2 H 1.574 0.010 1 963 134 103 LEU HB3 H 1.191 0.010 1 964 134 103 LEU HD1 H 0.621 0.010 1 965 134 103 LEU HD2 H 0.701 0.010 1 966 134 103 LEU C C 175.786 0.020 1 967 134 103 LEU CA C 54.957 0.020 1 968 134 103 LEU CB C 41.954 0.020 1 969 134 103 LEU CD1 C 25.907 0.020 1 970 134 103 LEU CD2 C 26.007 0.020 1 971 134 103 LEU N N 119.859 0.020 1 972 135 104 ASN H H 7.707 0.010 1 973 135 104 ASN HA H 4.169 0.010 1 974 135 104 ASN HB2 H 2.586 0.010 1 975 135 104 ASN HB3 H 2.982 0.010 1 976 135 104 ASN C C 174.809 0.020 1 977 135 104 ASN CA C 54.486 0.020 1 978 135 104 ASN CB C 37.57 0.020 1 979 135 104 ASN N N 116.343 0.020 1 980 136 105 ILE H H 8.069 0.010 1 981 136 105 ILE HA H 3.837 0.010 1 982 136 105 ILE HB H 1.33 0.010 1 983 136 105 ILE HD1 H 0.13 0.010 1 984 136 105 ILE HG12 H 0.486 0.010 1 985 136 105 ILE HG13 H 0.486 0.010 1 986 136 105 ILE HG2 H 0.878 0.010 1 987 136 105 ILE C C 176.144 0.020 1 988 136 105 ILE CA C 60.735 0.020 1 989 136 105 ILE CB C 37.113 0.020 1 990 136 105 ILE CD1 C 11.584 0.020 1 991 136 105 ILE CG1 C 17.193 0.020 1 992 136 105 ILE CG2 C 27.118 0.020 1 993 136 105 ILE N N 119.711 0.020 1 994 137 106 SER HA H 3.453 0.010 1 995 137 106 SER HB2 H 3.842 0.010 1 996 137 106 SER HB3 H 3.842 0.010 1 997 137 106 SER C C 172.736 0.020 1 998 137 106 SER CA C 57.642 0.020 1 999 137 106 SER CB C 65.052 0.020 1 1000 138 107 VAL H H 7.036 0.010 1 1001 138 107 VAL HA H 4.144 0.010 1 1002 138 107 VAL HB H 1.803 0.010 1 1003 138 107 VAL HG1 H 0.788 0.010 1 1004 138 107 VAL HG2 H 0.788 0.010 1 1005 138 107 VAL C C 173.887 0.020 1 1006 138 107 VAL CA C 60.506 0.020 1 1007 138 107 VAL CB C 35.742 0.020 1 1008 138 107 VAL CG1 C 20.992 0.020 1 1009 138 107 VAL CG2 C 20.992 0.020 1 1010 138 107 VAL N N 118.886 0.020 1 1011 139 108 TYR H H 8.582 0.010 1 1012 139 108 TYR HA H 5.154 0.010 1 1013 139 108 TYR HB2 H 2.847 0.010 1 1014 139 108 TYR HB3 H 2.499 0.010 1 1015 139 108 TYR C C 175.279 0.020 1 1016 139 108 TYR CA C 52.81 0.020 1 1017 139 108 TYR CB C 40.999 0.020 1 1018 139 108 TYR N N 121.646 0.020 1 1019 140 109 PRO HA H 5.126 0.010 1 1020 140 109 PRO HB2 H 2.097 0.010 1 1021 140 109 PRO HB3 H 1.783 0.010 1 1022 140 109 PRO HD2 H 3.307 0.010 1 1023 140 109 PRO HD3 H 3.598 0.010 1 1024 140 109 PRO HG2 H 1.897 0.010 1 1025 140 109 PRO HG3 H 1.897 0.010 1 1026 140 109 PRO C C 177.059 0.020 1 1027 140 109 PRO CA C 63.741 0.020 1 1028 140 109 PRO CB C 35.445 0.020 1 1029 140 109 PRO CD C 50.554 0.020 1 1030 140 109 PRO CG C 25.214 0.020 1 1031 141 110 SER H H 7.938 0.010 1 1032 141 110 SER HA H 5.422 0.010 1 1033 141 110 SER HB2 H 3.991 0.010 1 1034 141 110 SER HB3 H 3.728 0.010 1 1035 141 110 SER C C 175.749 0.020 1 1036 141 110 SER CA C 60.963 0.020 1 1037 141 110 SER CB C 70.641 0.020 1 1038 141 110 SER N N 113.284 0.020 1 1039 142 111 TRP H H 9.911 0.010 1 1040 142 111 TRP HA H 6.152 0.010 1 1041 142 111 TRP HB2 H 3.011 0.010 1 1042 142 111 TRP HB3 H 2.782 0.010 1 1043 142 111 TRP HD1 H 7.716 0.010 1 1044 142 111 TRP HE1 H 10.065 0.010 1 1045 142 111 TRP HZ2 H 7.577 0.010 1 1046 142 111 TRP C C 175.467 0.020 1 1047 142 111 TRP CA C 56.315 0.020 1 1048 142 111 TRP CB C 33.227 0.020 1 1049 142 111 TRP N N 123.415 0.020 1 1050 142 111 TRP NE1 N 129 0.020 1 1051 143 112 ALA H H 9.699 0.010 1 1052 143 112 ALA HA H 5.542 0.010 1 1053 143 112 ALA HB H 1.395 0.010 1 1054 143 112 ALA C C 174.677 0.020 1 1055 143 112 ALA CA C 50.676 0.020 1 1056 143 112 ALA CB C 24.312 0.020 1 1057 143 112 ALA N N 121.57 0.020 1 1058 144 113 LEU H H 9.074 0.010 1 1059 144 113 LEU HA H 5.245 0.010 1 1060 144 113 LEU HB2 H 1.885 0.010 1 1061 144 113 LEU HB3 H 1.057 0.010 1 1062 144 113 LEU HD1 H 0.743 0.010 1 1063 144 113 LEU HD2 H 0.811 0.010 1 1064 144 113 LEU HG H 1.521 0.010 1 1065 144 113 LEU C C 174.79 0.020 1 1066 144 113 LEU CA C 53.724 0.020 1 1067 144 113 LEU CB C 45.8 0.020 1 1068 144 113 LEU CD1 C 23.414 0.020 1 1069 144 113 LEU CD2 C 27.322 0.020 1 1070 144 113 LEU CG C 28.008 0.020 1 1071 144 113 LEU N N 123.926 0.020 1 1072 145 114 ILE H H 9.619 0.010 1 1073 145 114 ILE HA H 4.739 0.010 1 1074 145 114 ILE HB H 1.985 0.010 1 1075 145 114 ILE HD1 H 0.675 0.010 1 1076 145 114 ILE HG12 H 1.454 0.010 1 1077 145 114 ILE HG13 H 1.207 0.010 1 1078 145 114 ILE HG2 H 0.866 0.010 1 1079 145 114 ILE C C 176.633 0.020 1 1080 145 114 ILE CA C 57.915 0.020 1 1081 145 114 ILE CB C 38.18 0.020 1 1082 145 114 ILE CD1 C 11.929 0.020 1 1083 145 114 ILE CG1 C 28.003 0.020 1 1084 145 114 ILE CG2 C 17.682 0.020 1 1085 145 114 ILE N N 129.353 0.020 1 1086 146 115 GLY H H 9.28 0.010 1 1087 146 115 GLY HA2 H 4.048 0.010 1 1088 146 115 GLY HA3 H 4.048 0.010 1 1089 146 115 GLY C C 177.196 0.020 1 1090 146 115 GLY CA C 45.571 0.020 1 1091 146 115 GLY N N 112.42 0.020 1 1092 147 116 LYS H H 9.064 0.010 1 1093 147 116 LYS HA H 3.85 0.010 1 1094 147 116 LYS HB2 H 1.603 0.010 1 1095 147 116 LYS HB3 H 1.338 0.010 1 1096 147 116 LYS HD2 H 1.497 0.010 1 1097 147 116 LYS HD3 H 1.497 0.010 1 1098 147 116 LYS HE2 H 2.872 0.010 1 1099 147 116 LYS HE3 H 2.872 0.010 1 1100 147 116 LYS HG2 H 1.221 0.010 1 1101 147 116 LYS HG3 H 1.221 0.010 1 1102 147 116 LYS C C 177.385 0.020 1 1103 147 116 LYS CA C 59.516 0.020 1 1104 147 116 LYS CB C 32.16 0.020 1 1105 147 116 LYS CD C 29.944 0.020 1 1106 147 116 LYS CE C 42.44 0.020 1 1107 147 116 LYS CG C 24.39 0.020 1 1108 147 116 LYS N N 122.179 0.020 1 1109 148 117 ASP H H 8.634 0.010 1 1110 148 117 ASP HA H 4.765 0.010 1 1111 148 117 ASP HB2 H 2.782 0.010 1 1112 148 117 ASP HB3 H 2.554 0.010 1 1113 148 117 ASP C C 177.534 0.020 1 1114 148 117 ASP CA C 54.944 0.020 1 1115 148 117 ASP CB C 41.152 0.020 1 1116 148 117 ASP N N 117.436 0.020 1 1117 149 118 GLY H H 8.027 0.010 1 1118 149 118 GLY HA2 H 4.17 0.010 1 1119 149 118 GLY HA3 H 3.278 0.010 1 1120 149 118 GLY C C 172.714 0.020 1 1121 149 118 GLY CA C 46.486 0.020 1 1122 149 118 GLY N N 107.963 0.020 1 1123 150 119 ASP H H 9.266 0.010 1 1124 150 119 ASP HA H 4.459 0.010 1 1125 150 119 ASP HB2 H 2.318 0.010 1 1126 150 119 ASP HB3 H 2.527 0.010 1 1127 150 119 ASP C C 176.362 0.020 1 1128 150 119 ASP CA C 52.734 0.020 1 1129 150 119 ASP CB C 40.009 0.020 1 1130 150 119 ASP N N 117.293 0.020 1 1131 151 120 VAL H H 8.854 0.010 1 1132 151 120 VAL HA H 3.88 0.010 1 1133 151 120 VAL HB H 2.02 0.010 1 1134 151 120 VAL HG1 H 0.947 0.010 1 1135 151 120 VAL HG2 H 0.798 0.010 1 1136 151 120 VAL C C 176.931 0.020 1 1137 151 120 VAL CA C 64.468 0.020 1 1138 151 120 VAL CB C 31.398 0.020 1 1139 151 120 VAL CG1 C 22.207 0.020 1 1140 151 120 VAL CG2 C 21.528 0.020 1 1141 151 120 VAL N N 124.26 0.020 1 1142 152 121 GLN H H 9.015 0.010 1 1143 152 121 GLN HA H 4.384 0.010 1 1144 152 121 GLN HB2 H 1.862 0.010 1 1145 152 121 GLN HB3 H 1.862 0.010 1 1146 152 121 GLN C C 176.722 0.020 1 1147 152 121 GLN CA C 57.382 0.020 1 1148 152 121 GLN CB C 31.017 0.020 1 1149 152 121 GLN N N 128.261 0.020 1 1150 153 122 ARG H H 7.506 0.010 1 1151 153 122 ARG HA H 4.441 0.010 1 1152 153 122 ARG HB2 H 1.979 0.010 1 1153 153 122 ARG HB3 H 1.564 0.010 1 1154 153 122 ARG C C 174.125 0.020 1 1155 153 122 ARG CA C 55.705 0.020 1 1156 153 122 ARG CB C 34.383 0.020 1 1157 153 122 ARG N N 117.173 0.020 1 1158 154 123 ILE H H 8.635 0.010 1 1159 154 123 ILE HA H 4.917 0.010 1 1160 154 123 ILE HB H 1.692 0.010 1 1161 154 123 ILE HD1 H 0.794 0.010 1 1162 154 123 ILE HG12 H 1.526 0.010 1 1163 154 123 ILE HG13 H 0.97 0.010 1 1164 154 123 ILE HG2 H 0.908 0.010 1 1165 154 123 ILE C C 176.052 0.020 1 1166 154 123 ILE CA C 61.116 0.020 1 1167 154 123 ILE CB C 40.694 0.020 1 1168 154 123 ILE CD1 C 17.498 0.020 1 1169 154 123 ILE CG1 C 28.329 0.020 1 1170 154 123 ILE CG2 C 14.774 0.020 1 1171 154 123 ILE N N 126.361 0.020 1 1172 155 124 VAL H H 9.769 0.010 1 1173 155 124 VAL HA H 4.258 0.010 1 1174 155 124 VAL HB H 1.913 0.010 1 1175 155 124 VAL HG1 H 0.716 0.010 1 1176 155 124 VAL HG2 H 0.784 0.010 1 1177 155 124 VAL C C 175.067 0.020 1 1178 155 124 VAL CA C 61.754 0.020 1 1179 155 124 VAL CB C 35.437 0.020 1 1180 155 124 VAL CG1 C 21.279 0.020 1 1181 155 124 VAL CG2 C 23 0.020 1 1182 155 124 VAL N N 130 0.020 1 1183 156 125 LYS H H 8.641 0.010 1 1184 156 125 LYS HA H 4.795 0.010 1 1185 156 125 LYS HB2 H 1.631 0.010 1 1186 156 125 LYS HB3 H 1.631 0.010 1 1187 156 125 LYS HE2 H 2.9 0.010 1 1188 156 125 LYS HE3 H 2.9 0.010 1 1189 156 125 LYS C C 177.392 0.020 1 1190 156 125 LYS CA C 56.468 0.020 1 1191 156 125 LYS CB C 33.349 0.020 1 1192 156 125 LYS CE C 42.616 0.020 1 1193 156 125 LYS N N 128.199 0.020 1 1194 157 126 GLY H H 8.225 0.010 1 1195 157 126 GLY HA2 H 4.292 0.010 1 1196 157 126 GLY HA3 H 3.804 0.010 1 1197 157 126 GLY C C 171.611 0.020 1 1198 157 126 GLY CA C 45.114 0.020 1 1199 157 126 GLY N N 115.401 0.020 1 1200 158 127 SER H H 7.689 0.010 1 1201 158 127 SER HA H 4.507 0.010 1 1202 158 127 SER HB2 H 3.688 0.010 1 1203 158 127 SER HB3 H 3.688 0.010 1 1204 158 127 SER C C 176.324 0.020 1 1205 158 127 SER CA C 59.668 0.020 1 1206 158 127 SER CB C 63.783 0.020 1 1207 158 127 SER N N 108.731 0.020 1 1208 159 128 ILE H H 7.797 0.010 1 1209 159 128 ILE HA H 4.765 0.010 1 1210 159 128 ILE HB H 1.617 0.010 1 1211 159 128 ILE HD1 H -0.648 0.010 1 1212 159 128 ILE HG12 H -0.221 0.010 1 1213 159 128 ILE HG13 H 0.694 0.010 1 1214 159 128 ILE HG2 H 0.429 0.010 1 1215 159 128 ILE C C 175.088 0.020 1 1216 159 128 ILE CA C 59.82 0.020 1 1217 159 128 ILE CB C 41.38 0.020 1 1218 159 128 ILE CD1 C 12.491 0.020 1 1219 159 128 ILE CG1 C 23.299 0.020 1 1220 159 128 ILE CG2 C 17.291 0.020 1 1221 159 128 ILE N N 116.827 0.020 1 1222 160 129 ASN H H 8.704 0.010 1 1223 160 129 ASN HA H 4.963 0.010 1 1224 160 129 ASN HB2 H 3.286 0.010 1 1225 160 129 ASN HB3 H 2.691 0.010 1 1226 160 129 ASN C C 175.193 0.020 1 1227 160 129 ASN CA C 50.981 0.020 1 1228 160 129 ASN CB C 39.932 0.020 1 1229 160 129 ASN N N 119.729 0.020 1 1230 161 130 GLU H H 8.388 0.010 1 1231 161 130 GLU HA H 2.564 0.010 1 1232 161 130 GLU HB2 H 1.968 0.010 1 1233 161 130 GLU HB3 H 1.968 0.010 1 1234 161 130 GLU HG2 H 1.715 0.010 1 1235 161 130 GLU HG3 H 1.39 0.010 1 1236 161 130 GLU C C 177.078 0.020 1 1237 161 130 GLU CA C 60.659 0.020 1 1238 161 130 GLU CB C 31.093 0.020 1 1239 161 130 GLU CG C 36.649 0.020 1 1240 161 130 GLU N N 119.092 0.020 1 1241 162 131 ALA H H 7.728 0.010 1 1242 162 131 ALA HA H 3.728 0.010 1 1243 162 131 ALA HB H 1.21 0.010 1 1244 162 131 ALA C C 182.105 0.020 1 1245 162 131 ALA CA C 55.325 0.020 1 1246 162 131 ALA CB C 18.368 0.020 1 1247 162 131 ALA N N 119.606 0.020 1 1248 163 132 GLN H H 8.258 0.010 1 1249 163 132 GLN HA H 3.746 0.010 1 1250 163 132 GLN HB2 H 1.432 0.010 1 1251 163 132 GLN HB3 H 2.223 0.010 1 1252 163 132 GLN HG2 H 2.656 0.010 1 1253 163 132 GLN HG3 H 2.656 0.010 1 1254 163 132 GLN C C 177.413 0.020 1 1255 163 132 GLN CA C 58.601 0.020 1 1256 163 132 GLN CB C 29.874 0.020 1 1257 163 132 GLN CG C 34.961 0.020 1 1258 163 132 GLN N N 119.147 0.020 1 1259 164 133 ALA H H 8.025 0.010 1 1260 164 133 ALA HA H 3.347 0.010 1 1261 164 133 ALA HB H 0.678 0.010 1 1262 164 133 ALA C C 179.193 0.020 1 1263 164 133 ALA CA C 55.858 0.020 1 1264 164 133 ALA CB C 18.292 0.020 1 1265 164 133 ALA N N 121.576 0.020 1 1266 165 134 LEU H H 7.781 0.010 1 1267 165 134 LEU HA H 3.437 0.010 1 1268 165 134 LEU HB2 H 1.317 0.010 1 1269 165 134 LEU HB3 H 0.929 0.010 1 1270 165 134 LEU HD1 H 0.275 0.010 1 1271 165 134 LEU HD2 H -0.411 0.010 1 1272 165 134 LEU HG H 1.005 0.010 1 1273 165 134 LEU C C 180.178 0.020 1 1274 165 134 LEU CA C 57.458 0.020 1 1275 165 134 LEU CB C 41.685 0.020 1 1276 165 134 LEU CD1 C 25.763 0.020 1 1277 165 134 LEU CD2 C 22.462 0.020 1 1278 165 134 LEU CG C 26.772 0.020 1 1279 165 134 LEU N N 115.164 0.020 1 1280 166 135 ALA H H 7.637 0.010 1 1281 166 135 ALA HA H 3.761 0.010 1 1282 166 135 ALA HB H 1.253 0.010 1 1283 166 135 ALA C C 180.283 0.020 1 1284 166 135 ALA CA C 55.401 0.020 1 1285 166 135 ALA CB C 18.216 0.020 1 1286 166 135 ALA N N 122.276 0.020 1 1287 167 136 LEU H H 7.637 0.010 1 1288 167 136 LEU HA H 3.994 0.010 1 1289 167 136 LEU HB2 H 1.255 0.010 1 1290 167 136 LEU HB3 H 1.672 0.010 1 1291 167 136 LEU HD1 H 0.566 0.010 1 1292 167 136 LEU HD2 H 0.606 0.010 1 1293 167 136 LEU C C 177.748 0.020 1 1294 167 136 LEU CA C 57.001 0.020 1 1295 167 136 LEU CB C 42.828 0.020 1 1296 167 136 LEU CD1 C 25.057 0.020 1 1297 167 136 LEU CD2 C 24.96 0.020 1 1298 167 136 LEU N N 118.36 0.020 1 1299 168 137 ILE H H 7.146 0.010 1 1300 168 137 ILE HA H 3.525 0.010 1 1301 168 137 ILE HB H 1.648 0.010 1 1302 168 137 ILE HD1 H 0.655 0.010 1 1303 168 137 ILE HG12 H 1.498 0.010 1 1304 168 137 ILE HG13 H 0.88 0.010 1 1305 168 137 ILE HG2 H 0.702 0.010 1 1306 168 137 ILE C C 178.293 0.020 1 1307 168 137 ILE CA C 64.697 0.020 1 1308 168 137 ILE CB C 38.332 0.020 1 1309 168 137 ILE CD1 C 14.821 0.020 1 1310 168 137 ILE CG1 C 28.72 0.020 1 1311 168 137 ILE CG2 C 18.345 0.020 1 1312 168 137 ILE N N 111.89 0.020 1 1313 169 138 ARG H H 7.187 0.010 1 1314 169 138 ARG HA H 4.028 0.010 1 1315 169 138 ARG HB2 H 1.706 0.010 1 1316 169 138 ARG HB3 H 1.706 0.010 1 1317 169 138 ARG HD2 H 3.024 0.010 1 1318 169 138 ARG HD3 H 3.024 0.010 1 1319 169 138 ARG HG2 H 1.45 0.010 1 1320 169 138 ARG HG3 H 1.45 0.010 1 1321 169 138 ARG C C 177.015 0.020 1 1322 169 138 ARG CA C 58.22 0.020 1 1323 169 138 ARG CB C 31.17 0.020 1 1324 169 138 ARG CD C 43.776 0.020 1 1325 169 138 ARG CG C 27.7 0.020 1 1326 169 138 ARG N N 120.106 0.020 1 1327 170 139 ASP H H 8.076 0.010 1 1328 170 139 ASP HA H 4.81 0.010 1 1329 170 139 ASP HB2 H 2.64 0.010 1 1330 170 139 ASP HB3 H 2.424 0.010 1 1331 170 139 ASP C C 173.371 0.020 1 1332 170 139 ASP CA C 51.362 0.020 1 1333 170 139 ASP CB C 42.98 0.020 1 1334 170 139 ASP N N 119.215 0.020 1 1335 172 141 ASN C C 175.842 0.020 1 1336 172 141 ASN CA C 52.568 0.020 1 1337 172 141 ASN CB C 39.393 0.020 1 1338 173 142 ALA H H 7.683 0.010 1 1339 173 142 ALA HA H 3.801 0.010 1 1340 173 142 ALA HB H 1.202 0.010 1 1341 173 142 ALA C C 177.727 0.020 1 1342 173 142 ALA CA C 53.648 0.020 1 1343 173 142 ALA CB C 19.74 0.020 1 1344 173 142 ALA N N 123.347 0.020 1 1345 174 143 ASP H H 8.307 0.010 1 1346 174 143 ASP HA H 4.536 0.010 1 1347 174 143 ASP HB2 H 2.386 0.010 1 1348 174 143 ASP HB3 H 2.584 0.010 1 1349 174 143 ASP C C 175.465 0.020 1 1350 174 143 ASP CA C 54.867 0.020 1 1351 174 143 ASP CB C 41.228 0.020 1 1352 174 143 ASP N N 121.617 0.020 1 1353 175 144 LEU H H 8.078 0.010 1 1354 175 144 LEU HA H 4.058 0.010 1 1355 175 144 LEU HB2 H 1.503 0.010 1 1356 175 144 LEU HB3 H 1.35 0.010 1 1357 175 144 LEU HD1 H 0.702 0.010 1 1358 175 144 LEU HD2 H 0.593 0.010 1 1359 175 144 LEU C C 182.943 0.020 1 1360 175 144 LEU CA C 56.696 0.020 1 1361 175 144 LEU CB C 43.438 0.020 1 1362 175 144 LEU CD1 C 26.386 0.020 1 1363 175 144 LEU CD2 C 23.873 0.020 1 1364 175 144 LEU CG C 32.163 0.020 1 1365 175 144 LEU N N 130.098 0.020 1 stop_ save_