data_17830 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Resonance Assignments for Oxidised and Reduced nDsbD fromm Escherichia coli ; _BMRB_accession_number 17830 _BMRB_flat_file_name bmr17830.str _Entry_type original _Submission_date 2011-08-04 _Accession_date 2011-08-04 _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 Mavridou Despoina A.I. . 2 Stelzl Lukas S. . 3 Ferguson Stuart J. . 4 Redfield Christina . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 625 "13C chemical shifts" 489 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-10-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17831 'oxidized nDsbD' stop_ _Original_release_date 2011-10-25 save_ ############################# # Citation for this entry # ############################# save_JBC_paper _Saveframe_category entry_citation _Citation_full . _Citation_title 'Oxidation state-dependent protein-protein interactions in disulfide cascades.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21543317 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mavridou Despoina A.I. . 2 Saridakis Emmanuel . . 3 Kritsiligkou Paraskevi . . 4 Goddard Alan D. . 5 Stevens Julie M. . 6 Ferguson Stuart J. . 7 Redfield Christina . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 24943 _Page_last 24956 _Year 2011 _Details . loop_ _Keyword 'E. coli DsbD' 'NMR resonance assignments' oxidation/reduction 'thiol:disulfide exchange reaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name nDsbD-red _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label nDsbD-red $nDsbD-red stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function oxidoreductase stop_ _Database_query_date . _Details 'N-terminal domain of DsbD' save_ ######################## # Monomeric polymers # ######################## save_nDsbD-red _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common nDsbD-red _Molecular_mass 15604.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'thiol-disulfide oxidoreductase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; MDTLFDAPGRSQFVPADQAF AFDFQQNQHDLNLTWQIKDG YYLYRKQIRITPEHAKIADV QLPQGVWHEDEFYGKSEIYR DRLTLPVTINQASAGATLTV TYQGCADAGFCYPPETKTVP LSEVVANNAAPQPVGLVPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 0 ASP 3 1 THR 4 2 LEU 5 3 PHE 6 4 ASP 7 5 ALA 8 6 PRO 9 7 GLY 10 8 ARG 11 9 SER 12 10 GLN 13 11 PHE 14 12 VAL 15 13 PRO 16 14 ALA 17 15 ASP 18 16 GLN 19 17 ALA 20 18 PHE 21 19 ALA 22 20 PHE 23 21 ASP 24 22 PHE 25 23 GLN 26 24 GLN 27 25 ASN 28 26 GLN 29 27 HIS 30 28 ASP 31 29 LEU 32 30 ASN 33 31 LEU 34 32 THR 35 33 TRP 36 34 GLN 37 35 ILE 38 36 LYS 39 37 ASP 40 38 GLY 41 39 TYR 42 40 TYR 43 41 LEU 44 42 TYR 45 43 ARG 46 44 LYS 47 45 GLN 48 46 ILE 49 47 ARG 50 48 ILE 51 49 THR 52 50 PRO 53 51 GLU 54 52 HIS 55 53 ALA 56 54 LYS 57 55 ILE 58 56 ALA 59 57 ASP 60 58 VAL 61 59 GLN 62 60 LEU 63 61 PRO 64 62 GLN 65 63 GLY 66 64 VAL 67 65 TRP 68 66 HIS 69 67 GLU 70 68 ASP 71 69 GLU 72 70 PHE 73 71 TYR 74 72 GLY 75 73 LYS 76 74 SER 77 75 GLU 78 76 ILE 79 77 TYR 80 78 ARG 81 79 ASP 82 80 ARG 83 81 LEU 84 82 THR 85 83 LEU 86 84 PRO 87 85 VAL 88 86 THR 89 87 ILE 90 88 ASN 91 89 GLN 92 90 ALA 93 91 SER 94 92 ALA 95 93 GLY 96 94 ALA 97 95 THR 98 96 LEU 99 97 THR 100 98 VAL 101 99 THR 102 100 TYR 103 101 GLN 104 102 GLY 105 103 CYS 106 104 ALA 107 105 ASP 108 106 ALA 109 107 GLY 110 108 PHE 111 109 CYS 112 110 TYR 113 111 PRO 114 112 PRO 115 113 GLU 116 114 THR 117 115 LYS 118 116 THR 119 117 VAL 120 118 PRO 121 119 LEU 122 120 SER 123 121 GLU 124 122 VAL 125 123 VAL 126 124 ALA 127 125 ASN 128 126 ASN 129 127 ALA 130 128 ALA 131 129 PRO 132 130 GLN 133 131 PRO 134 132 VAL 135 133 GLY 136 134 LEU 137 135 VAL 138 136 PRO 139 137 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 17831 nDsbD-ox 100.00 139 100.00 100.00 3.89e-98 PDB 1JPE "Crystal Structure Of Dsbd-Alpha; The N-Terminal Domain Of Dsbd" 94.24 151 100.00 100.00 9.30e-92 PDB 1JZD "Dsbc-Dsbdalpha Complex" 94.24 132 99.24 99.24 2.42e-90 PDB 1L6P "N-Terminal Of Dsbd (Residues 20-144) From E. Coli" 89.21 125 100.00 100.00 2.28e-86 PDB 1VRS "Crystal Structure Of The Disulfide-Linked Complex Between The N- Terminal And C-Terminal Domain Of The Electron Transfer Cataly" 95.68 143 97.74 98.50 1.33e-90 PDB 1Z5Y "Crystal Structure Of The Disulfide-linked Complex Between The N-terminal Domain Of The Electron Transfer Catalyst Dsbd And The " 95.68 143 97.74 98.50 1.33e-90 PDB 3PFU "N-terminal Domain Of Thiol:disulfide Interchange Protein Dsbd In Its Reduced Form" 100.00 139 100.00 100.00 3.89e-98 DBJ BAB38540 "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" 95.68 565 96.99 97.74 9.96e-87 DBJ BAE78138 "fused thiol:disulfide interchange protein [Escherichia coli str. K12 substr. W3110]" 95.68 565 98.50 99.25 3.39e-88 DBJ BAG66862 "fused thiol:disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O111:H-]" 95.68 565 96.99 97.74 7.71e-87 DBJ BAG79959 "thiol:disulfide interchange protein [Escherichia coli SE11]" 95.68 565 96.99 97.74 1.06e-86 DBJ BAI28440 "fused thiol: disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O26:H11 str. 11368]" 95.68 565 96.99 97.74 1.40e-86 EMBL CAA54781 "disulphide isomerase like protein [Escherichia coli K-12]" 53.96 489 98.67 100.00 4.36e-43 EMBL CAA85375 "inner membrane copper tolerance protein [Escherichia coli str. K-12 substr. W3110]" 53.96 489 98.67 100.00 4.36e-43 EMBL CAQ34485 "DsbD[reduced] [Escherichia coli BL21(DE3)]" 95.68 565 97.74 98.50 2.76e-87 EMBL CAR01112 "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli IAI1]" 95.68 565 97.74 98.50 2.07e-87 EMBL CAR05872 "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli S88]" 95.68 565 96.99 97.74 2.37e-86 GB AAA97035 "cycZ [Escherichia coli str. K-12 substr. MG1655]" 95.68 565 98.50 99.25 3.39e-88 GB AAC77096 "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" 95.68 565 98.50 99.25 3.39e-88 GB AAG59335 "thiol:disulfide interchange protein; copper tolerance [Escherichia coli O157:H7 str. EDL933]" 95.68 565 96.99 97.74 9.96e-87 GB AAN45708 "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" 95.68 565 96.99 97.74 2.50e-86 GB AAN83640 "Thiol:disulfide interchange protein dsbD precursor [Escherichia coli CFT073]" 95.68 565 96.99 97.74 2.04e-86 REF NP_313144 "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" 95.68 565 96.99 97.74 9.96e-87 REF NP_418559 "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" 95.68 565 98.50 99.25 3.39e-88 REF NP_710001 "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" 95.68 565 96.99 97.74 2.50e-86 REF WP_000068901 "thiol:disulfide interchange protein DsbD [Shigella sonnei]" 95.68 565 96.99 97.74 1.48e-86 REF WP_000068902 "MULTISPECIES: thiol:disulfide interchange protein [Enterobacteriaceae]" 95.68 565 96.99 97.74 1.63e-86 SP P36655 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=C-type cytochrome biogenesis protein CycZ; AltName: Full=" 95.68 565 98.50 99.25 3.39e-88 SP P58162 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 95.68 565 96.99 97.74 9.96e-87 SP Q0SXE3 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 95.68 565 97.74 98.50 2.07e-87 SP Q0T9Q5 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 95.68 565 96.99 97.74 2.37e-86 SP Q1R3C4 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 95.68 565 96.99 97.74 2.37e-86 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic _Details $nDsbD-red 'E. coli' 562 Eubacteria . Escherichia coli K12 dsbd 'Located in the periplasm' 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 $nDsbD-red 'recombinant technology' . Escherichia coli BL21(DE3) pET22b(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $nDsbD-red . mM 0.5 1.0 '[U-98% 15N]' DTT 20 mM . . 'natural abundance' D2O 5 % . . 'natural abundance' H2O 95 % . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $nDsbD-red . mM 0.5 1.0 '[U-98% 13C; U-98% 15N]' DTT 20 mM . . 'natural abundance' D2O 5 % . . 'natural abundance' H2O 95 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer home-built _Model 'home-built using GE Omega software' _Field_strength 750 _Details 'home-built spectrometer with triple-axis gradient probe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'with TCI CryoProbe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_NH2_only_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC NH2 only' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_HBHA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HN(CA)CO_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2 save_ save_3D_1H-15N_HSQC-NOESY-HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'Water was used as the reference for 1H (4.75 ppm at 298K). The gamma ratios were used for 13C and 15N.' 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 water C 13 protons ppm 4.75 internal indirect . . . 0.251449530 water H 1 protons ppm 4.75 internal direct . . . 1.0 water N 15 protons ppm 4.75 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_ _Experiment_label '3D HNCO' '3D HNCA' '3D HCCH-TOCSY' '3D CBCA(CO)NH' '3D HBHA(CO)NH' '2D 1H-15N HSQC' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name nDsbD-red _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 4 LEU H H 8.247 0.02 1 2 2 4 LEU HA H 4.280 0.02 1 3 2 4 LEU HB2 H 1.408 0.02 2 4 2 4 LEU HB3 H 1.514 0.02 2 5 2 4 LEU HG H 1.462 0.02 1 6 2 4 LEU HD1 H 0.863 0.02 2 7 2 4 LEU HD2 H 0.804 0.02 2 8 2 4 LEU C C 177.030 0.2 1 9 2 4 LEU CA C 55.368 0.2 1 10 2 4 LEU CB C 42.274 0.2 1 11 2 4 LEU CG C 26.989 0.2 1 12 2 4 LEU CD1 C 24.743 0.2 2 13 2 4 LEU CD2 C 23.634 0.2 2 14 2 4 LEU N N 124.068 0.2 1 15 3 5 PHE H H 8.101 0.02 1 16 3 5 PHE HA H 4.570 0.02 1 17 3 5 PHE HB2 H 3.155 0.02 2 18 3 5 PHE HB3 H 2.952 0.02 2 19 3 5 PHE C C 175.252 0.2 1 20 3 5 PHE CA C 57.796 0.2 1 21 3 5 PHE CB C 39.586 0.2 1 22 3 5 PHE N N 120.094 0.2 1 23 4 6 ASP H H 8.153 0.02 1 24 4 6 ASP HA H 4.552 0.02 1 25 4 6 ASP HB2 H 2.545 0.02 2 26 4 6 ASP HB3 H 2.621 0.02 2 27 4 6 ASP C C 175.182 0.2 1 28 4 6 ASP CA C 53.896 0.2 1 29 4 6 ASP CB C 41.247 0.2 1 30 4 6 ASP N N 121.292 0.2 1 31 5 7 ALA H H 7.976 0.02 1 32 5 7 ALA HA H 4.536 0.02 1 33 5 7 ALA HB H 1.345 0.02 1 34 5 7 ALA CA C 50.724 0.2 1 35 5 7 ALA CB C 18.229 0.2 1 36 5 7 ALA N N 124.898 0.2 1 37 6 8 PRO HA H 4.381 0.02 1 38 6 8 PRO HB2 H 1.921 0.02 2 39 6 8 PRO HB3 H 2.276 0.02 2 40 6 8 PRO C C 177.870 0.2 1 41 6 8 PRO CA C 63.811 0.2 1 42 6 8 PRO CB C 32.041 0.2 1 43 7 9 GLY H H 8.479 0.02 1 44 7 9 GLY HA2 H 3.911 0.02 2 45 7 9 GLY HA3 H 3.952 0.02 2 46 7 9 GLY C C 174.444 0.2 1 47 7 9 GLY CA C 45.327 0.2 1 48 7 9 GLY N N 108.853 0.2 1 49 8 10 ARG H H 8.045 0.02 1 50 8 10 ARG HA H 4.314 0.02 1 51 8 10 ARG HB2 H 1.768 0.02 2 52 8 10 ARG HB3 H 1.856 0.02 2 53 8 10 ARG HG2 H 1.620 0.02 2 54 8 10 ARG HG3 H 1.611 0.02 2 55 8 10 ARG HD2 H 3.174 0.02 2 56 8 10 ARG HD3 H 3.163 0.02 2 57 8 10 ARG C C 176.460 0.2 1 58 8 10 ARG CA C 56.281 0.2 1 59 8 10 ARG CB C 30.760 0.2 1 60 8 10 ARG CG C 26.969 0.2 1 61 8 10 ARG CD C 43.347 0.2 1 62 8 10 ARG N N 120.035 0.2 1 63 9 11 SER H H 8.238 0.02 1 64 9 11 SER HA H 4.323 0.02 1 65 9 11 SER HB2 H 3.761 0.02 2 66 9 11 SER HB3 H 3.816 0.02 2 67 9 11 SER C C 174.203 0.2 1 68 9 11 SER CA C 58.573 0.2 1 69 9 11 SER CB C 63.780 0.2 1 70 9 11 SER N N 116.243 0.2 1 71 10 12 GLN H H 8.187 0.02 1 72 10 12 GLN HA H 4.114 0.02 1 73 10 12 GLN HB2 H 1.776 0.02 2 74 10 12 GLN HB3 H 1.705 0.02 2 75 10 12 GLN HG2 H 1.992 0.02 2 76 10 12 GLN HG3 H 1.963 0.02 2 77 10 12 GLN C C 174.913 0.2 1 78 10 12 GLN CA C 55.945 0.2 1 79 10 12 GLN CB C 28.684 0.2 1 80 10 12 GLN CG C 33.013 0.2 1 81 10 12 GLN N N 121.345 0.2 1 82 11 13 PHE H H 7.770 0.02 1 83 11 13 PHE HA H 4.689 0.02 1 84 11 13 PHE HB2 H 2.543 0.02 2 85 11 13 PHE HB3 H 3.175 0.02 2 86 11 13 PHE C C 175.530 0.2 1 87 11 13 PHE CA C 57.223 0.2 1 88 11 13 PHE CB C 39.202 0.2 1 89 11 13 PHE N N 120.877 0.2 1 90 12 14 VAL H H 7.511 0.02 1 91 12 14 VAL HA H 4.426 0.02 1 92 12 14 VAL HB H 2.101 0.02 1 93 12 14 VAL HG1 H 0.864 0.02 2 94 12 14 VAL HG2 H 0.613 0.02 2 95 12 14 VAL C C 173.433 0.2 1 96 12 14 VAL CA C 59.751 0.2 1 97 12 14 VAL CB C 30.988 0.2 1 98 12 14 VAL CG1 C 21.407 0.2 2 99 12 14 VAL CG2 C 19.356 0.2 2 100 12 14 VAL N N 118.881 0.2 1 101 13 15 PRO HA H 4.557 0.02 1 102 13 15 PRO HB2 H 1.877 0.02 2 103 13 15 PRO HB3 H 2.523 0.02 2 104 13 15 PRO C C 177.441 0.2 1 105 13 15 PRO CA C 63.314 0.2 1 106 13 15 PRO CB C 32.437 0.2 1 107 14 16 ALA H H 9.403 0.02 1 108 14 16 ALA HA H 3.591 0.02 1 109 14 16 ALA HB H 1.613 0.02 1 110 14 16 ALA C C 178.412 0.2 1 111 14 16 ALA CA C 56.254 0.2 1 112 14 16 ALA CB C 18.403 0.2 1 113 14 16 ALA N N 126.793 0.2 1 114 15 17 ASP H H 8.607 0.02 1 115 15 17 ASP HA H 4.444 0.02 1 116 15 17 ASP HB2 H 2.591 0.02 2 117 15 17 ASP HB3 H 2.792 0.02 2 118 15 17 ASP C C 176.647 0.2 1 119 15 17 ASP CA C 56.301 0.2 1 120 15 17 ASP CB C 40.234 0.2 1 121 15 17 ASP N N 112.510 0.2 1 122 16 18 GLN H H 7.453 0.02 1 123 16 18 GLN HA H 4.156 0.02 1 124 16 18 GLN HB2 H 1.772 0.02 2 125 16 18 GLN HB3 H 1.912 0.02 2 126 16 18 GLN HG2 H 2.337 0.02 2 127 16 18 GLN HG3 H 2.263 0.02 2 128 16 18 GLN C C 176.384 0.2 1 129 16 18 GLN CA C 56.549 0.2 1 130 16 18 GLN CB C 29.404 0.2 1 131 16 18 GLN CG C 34.008 0.2 1 132 16 18 GLN N N 115.259 0.2 1 133 17 19 ALA H H 7.229 0.02 1 134 17 19 ALA HA H 3.074 0.02 1 135 17 19 ALA HB H -0.428 0.02 1 136 17 19 ALA C C 175.453 0.2 1 137 17 19 ALA CA C 54.005 0.2 1 138 17 19 ALA CB C 17.163 0.2 1 139 17 19 ALA N N 123.186 0.2 1 140 18 20 PHE H H 7.994 0.02 1 141 18 20 PHE HA H 4.909 0.02 1 142 18 20 PHE HB2 H 3.435 0.02 2 143 18 20 PHE HB3 H 2.700 0.02 2 144 18 20 PHE C C 173.329 0.2 1 145 18 20 PHE CA C 53.147 0.2 1 146 18 20 PHE CB C 38.887 0.2 1 147 18 20 PHE N N 115.281 0.2 1 148 19 21 ALA H H 8.106 0.02 1 149 19 21 ALA HA H 4.618 0.02 1 150 19 21 ALA HB H 1.368 0.02 1 151 19 21 ALA C C 176.463 0.2 1 152 19 21 ALA CA C 52.375 0.2 1 153 19 21 ALA CB C 19.020 0.2 1 154 19 21 ALA N N 125.952 0.2 1 155 20 22 PHE H H 8.709 0.02 1 156 20 22 PHE HA H 4.938 0.02 1 157 20 22 PHE HB2 H 2.655 0.02 2 158 20 22 PHE HB3 H 2.762 0.02 2 159 20 22 PHE C C 174.120 0.2 1 160 20 22 PHE CA C 56.683 0.2 1 161 20 22 PHE CB C 42.113 0.2 1 162 20 22 PHE N N 129.155 0.2 1 163 21 23 ASP H H 8.338 0.02 1 164 21 23 ASP HA H 4.223 0.02 1 165 21 23 ASP HB2 H 2.272 0.02 2 166 21 23 ASP HB3 H 2.109 0.02 2 167 21 23 ASP C C 171.309 0.2 1 168 21 23 ASP CA C 52.516 0.2 1 169 21 23 ASP CB C 44.684 0.2 1 170 21 23 ASP N N 128.379 0.2 1 171 22 24 PHE H H 7.600 0.02 1 172 22 24 PHE HA H 5.299 0.02 1 173 22 24 PHE HB2 H 2.548 0.02 2 174 22 24 PHE HB3 H 2.561 0.02 2 175 22 24 PHE C C 173.586 0.2 1 176 22 24 PHE CA C 55.145 0.2 1 177 22 24 PHE CB C 42.755 0.2 1 178 22 24 PHE N N 112.800 0.2 1 179 23 25 GLN H H 8.049 0.02 1 180 23 25 GLN HA H 4.331 0.02 1 181 23 25 GLN HB2 H 1.883 0.02 2 182 23 25 GLN HB3 H 1.876 0.02 2 183 23 25 GLN HG2 H 2.106 0.02 2 184 23 25 GLN HG3 H 2.168 0.02 2 185 23 25 GLN C C 173.929 0.2 1 186 23 25 GLN CA C 55.747 0.2 1 187 23 25 GLN CB C 32.313 0.2 1 188 23 25 GLN CG C 33.513 0.2 1 189 23 25 GLN N N 116.815 0.2 1 190 24 26 GLN H H 9.377 0.02 1 191 24 26 GLN HA H 4.997 0.02 1 192 24 26 GLN HB2 H 1.830 0.02 2 193 24 26 GLN HB3 H 2.118 0.02 2 194 24 26 GLN HG2 H 2.371 0.02 2 195 24 26 GLN HG3 H 2.110 0.02 2 196 24 26 GLN C C 174.267 0.2 1 197 24 26 GLN CA C 54.372 0.2 1 198 24 26 GLN CB C 30.722 0.2 1 199 24 26 GLN CG C 32.748 0.2 1 200 24 26 GLN N N 128.860 0.2 1 201 25 27 ASN H H 9.170 0.02 1 202 25 27 ASN HA H 4.801 0.02 1 203 25 27 ASN HB2 H 2.634 0.02 2 204 25 27 ASN HB3 H 2.875 0.02 2 205 25 27 ASN C C 174.363 0.2 1 206 25 27 ASN CA C 52.530 0.2 1 207 25 27 ASN CB C 39.331 0.2 1 208 25 27 ASN N N 126.113 0.2 1 209 26 28 GLN H H 9.417 0.02 1 210 26 28 GLN HA H 3.604 0.02 1 211 26 28 GLN HB2 H 2.070 0.02 2 212 26 28 GLN HB3 H 2.448 0.02 2 213 26 28 GLN HG2 H 2.471 0.02 2 214 26 28 GLN HG3 H 2.326 0.02 2 215 26 28 GLN C C 174.562 0.2 1 216 26 28 GLN CA C 58.553 0.2 1 217 26 28 GLN CB C 26.602 0.2 1 218 26 28 GLN CG C 34.040 0.2 1 219 26 28 GLN N N 122.156 0.2 1 220 27 29 HIS H H 8.212 0.02 1 221 27 29 HIS HA H 4.481 0.02 1 222 27 29 HIS HB2 H 3.390 0.02 2 223 27 29 HIS HB3 H 3.384 0.02 2 224 27 29 HIS C C 173.790 0.2 1 225 27 29 HIS CA C 57.785 0.2 1 226 27 29 HIS CB C 29.192 0.2 1 227 27 29 HIS N N 117.871 0.2 1 228 28 30 ASP H H 8.021 0.02 1 229 28 30 ASP HA H 5.003 0.02 1 230 28 30 ASP HB2 H 2.667 0.02 1 231 28 30 ASP HB3 H 2.667 0.02 1 232 28 30 ASP C C 173.819 0.2 1 233 28 30 ASP CA C 54.390 0.2 1 234 28 30 ASP CB C 42.309 0.2 1 235 28 30 ASP N N 118.812 0.2 1 236 29 31 LEU H H 8.730 0.02 1 237 29 31 LEU HA H 5.081 0.02 1 238 29 31 LEU HB2 H 1.135 0.02 2 239 29 31 LEU HB3 H 1.950 0.02 2 240 29 31 LEU HG H 1.289 0.02 1 241 29 31 LEU HD1 H 0.737 0.02 2 242 29 31 LEU HD2 H 0.663 0.02 2 243 29 31 LEU C C 173.742 0.2 1 244 29 31 LEU CA C 53.268 0.2 1 245 29 31 LEU CB C 44.774 0.2 1 246 29 31 LEU CG C 27.157 0.2 1 247 29 31 LEU CD1 C 24.462 0.2 2 248 29 31 LEU CD2 C 27.819 0.2 2 249 29 31 LEU N N 126.739 0.2 1 250 30 32 ASN H H 8.786 0.02 1 251 30 32 ASN HA H 5.316 0.02 1 252 30 32 ASN HB2 H 2.315 0.02 2 253 30 32 ASN HB3 H 2.528 0.02 2 254 30 32 ASN C C 174.289 0.2 1 255 30 32 ASN CA C 52.616 0.2 1 256 30 32 ASN CB C 41.342 0.2 1 257 30 32 ASN N N 124.822 0.2 1 258 31 33 LEU H H 8.342 0.02 1 259 31 33 LEU HA H 4.555 0.02 1 260 31 33 LEU HB2 H 1.072 0.02 2 261 31 33 LEU HB3 H 2.162 0.02 2 262 31 33 LEU HG H 1.695 0.02 1 263 31 33 LEU HD1 H 0.833 0.02 2 264 31 33 LEU HD2 H 0.931 0.02 2 265 31 33 LEU C C 174.996 0.2 1 266 31 33 LEU CA C 53.102 0.2 1 267 31 33 LEU CB C 43.004 0.2 1 268 31 33 LEU CG C 26.578 0.2 1 269 31 33 LEU CD1 C 23.884 0.2 2 270 31 33 LEU CD2 C 27.017 0.2 2 271 31 33 LEU N N 125.343 0.2 1 272 32 34 THR H H 8.316 0.02 1 273 32 34 THR HA H 5.468 0.02 1 274 32 34 THR HB H 3.705 0.02 1 275 32 34 THR HG2 H 0.934 0.02 1 276 32 34 THR C C 172.019 0.2 1 277 32 34 THR CA C 60.381 0.2 1 278 32 34 THR CB C 72.062 0.2 1 279 32 34 THR CG2 C 24.901 0.2 1 280 32 34 THR N N 115.827 0.2 1 281 33 35 TRP H H 9.345 0.02 1 282 33 35 TRP HA H 5.409 0.02 1 283 33 35 TRP HB2 H 2.434 0.02 2 284 33 35 TRP HB3 H 2.929 0.02 2 285 33 35 TRP HE1 H 5.621 0.02 1 286 33 35 TRP C C 175.725 0.2 1 287 33 35 TRP CA C 57.424 0.2 1 288 33 35 TRP CB C 33.984 0.2 1 289 33 35 TRP N N 122.200 0.2 1 290 33 35 TRP NE1 N 121.607 0.2 1 291 34 36 GLN H H 8.815 0.02 1 292 34 36 GLN HA H 4.632 0.02 1 293 34 36 GLN HB2 H 2.128 0.02 2 294 34 36 GLN HB3 H 1.955 0.02 2 295 34 36 GLN HG2 H 2.266 0.02 1 296 34 36 GLN HG3 H 2.266 0.02 1 297 34 36 GLN C C 175.468 0.2 1 298 34 36 GLN CA C 55.146 0.2 1 299 34 36 GLN CB C 29.205 0.2 1 300 34 36 GLN CG C 33.493 0.2 1 301 34 36 GLN N N 122.746 0.2 1 302 35 37 ILE H H 8.453 0.02 1 303 35 37 ILE HA H 4.708 0.02 1 304 35 37 ILE HB H 1.778 0.02 1 305 35 37 ILE HG12 H 0.671 0.02 2 306 35 37 ILE HG13 H 1.507 0.02 2 307 35 37 ILE HG2 H 1.121 0.02 1 308 35 37 ILE HD1 H 0.553 0.02 1 309 35 37 ILE C C 175.073 0.2 1 310 35 37 ILE CA C 61.040 0.2 1 311 35 37 ILE CB C 38.602 0.2 1 312 35 37 ILE CG1 C 28.052 0.2 1 313 35 37 ILE CG2 C 18.939 0.2 1 314 35 37 ILE CD1 C 13.794 0.2 1 315 35 37 ILE N N 129.939 0.2 1 316 36 38 LYS H H 8.672 0.02 1 317 36 38 LYS HA H 4.059 0.02 1 318 36 38 LYS HB2 H 1.637 0.02 2 319 36 38 LYS HB3 H 1.422 0.02 2 320 36 38 LYS HG2 H 1.616 0.02 2 321 36 38 LYS HG3 H 1.794 0.02 2 322 36 38 LYS HD2 H 1.353 0.02 1 323 36 38 LYS HD3 H 1.353 0.02 1 324 36 38 LYS HE2 H 3.037 0.02 2 325 36 38 LYS HE3 H 3.060 0.02 2 326 36 38 LYS C C 175.362 0.2 1 327 36 38 LYS CA C 57.410 0.2 1 328 36 38 LYS CB C 33.667 0.2 1 329 36 38 LYS CG C 24.694 0.2 1 330 36 38 LYS CD C 29.297 0.2 1 331 36 38 LYS CE C 41.886 0.2 1 332 36 38 LYS N N 131.313 0.2 1 333 37 39 ASP H H 8.457 0.02 1 334 37 39 ASP HA H 4.669 0.02 1 335 37 39 ASP HB2 H 2.707 0.02 2 336 37 39 ASP HB3 H 2.802 0.02 2 337 37 39 ASP C C 177.528 0.2 1 338 37 39 ASP CA C 56.701 0.2 1 339 37 39 ASP CB C 41.321 0.2 1 340 37 39 ASP N N 124.693 0.2 1 341 38 40 GLY H H 9.203 0.02 1 342 38 40 GLY HA2 H 3.973 0.02 2 343 38 40 GLY HA3 H 4.277 0.02 2 344 38 40 GLY C C 174.090 0.2 1 345 38 40 GLY CA C 45.072 0.2 1 346 38 40 GLY N N 113.018 0.2 1 347 39 41 TYR H H 8.289 0.02 1 348 39 41 TYR HA H 5.320 0.02 1 349 39 41 TYR HB2 H 2.847 0.02 2 350 39 41 TYR HB3 H 3.055 0.02 2 351 39 41 TYR C C 173.868 0.2 1 352 39 41 TYR CA C 56.949 0.2 1 353 39 41 TYR CB C 40.688 0.2 1 354 39 41 TYR N N 120.821 0.2 1 355 40 42 TYR H H 8.815 0.02 1 356 40 42 TYR HA H 5.363 0.02 1 357 40 42 TYR HB2 H 2.582 0.02 2 358 40 42 TYR HB3 H 2.806 0.02 2 359 40 42 TYR C C 173.677 0.2 1 360 40 42 TYR CA C 55.989 0.2 1 361 40 42 TYR CB C 41.372 0.2 1 362 40 42 TYR N N 113.119 0.2 1 363 41 43 LEU H H 8.460 0.02 1 364 41 43 LEU HA H 4.564 0.02 1 365 41 43 LEU HB2 H 1.156 0.02 2 366 41 43 LEU HB3 H 1.394 0.02 2 367 41 43 LEU HG H 1.215 0.02 1 368 41 43 LEU HD1 H -0.129 0.02 2 369 41 43 LEU HD2 H -0.216 0.02 2 370 41 43 LEU C C 177.260 0.2 1 371 41 43 LEU CA C 52.611 0.2 1 372 41 43 LEU CB C 46.968 0.2 1 373 41 43 LEU CG C 26.424 0.2 1 374 41 43 LEU CD1 C 23.728 0.2 2 375 41 43 LEU CD2 C 24.710 0.2 2 376 41 43 LEU N N 115.722 0.2 1 377 42 44 TYR H H 7.532 0.02 1 378 42 44 TYR HA H 4.505 0.02 1 379 42 44 TYR HB2 H 2.350 0.02 2 380 42 44 TYR HB3 H 2.987 0.02 2 381 42 44 TYR C C 176.817 0.2 1 382 42 44 TYR CA C 58.310 0.2 1 383 42 44 TYR CB C 39.594 0.2 1 384 42 44 TYR N N 116.483 0.2 1 385 43 45 ARG H H 8.272 0.02 1 386 43 45 ARG HA H 3.824 0.02 1 387 43 45 ARG HB2 H 1.299 0.02 2 388 43 45 ARG HB3 H 0.645 0.02 2 389 43 45 ARG HD2 H 2.789 0.02 2 390 43 45 ARG HD3 H 2.626 0.02 2 391 43 45 ARG C C 177.411 0.2 1 392 43 45 ARG CA C 60.374 0.2 1 393 43 45 ARG CB C 30.826 0.2 1 394 43 45 ARG CD C 43.778 0.2 1 395 43 45 ARG N N 127.988 0.2 1 396 44 46 LYS H H 9.090 0.02 1 397 44 46 LYS HA H 4.077 0.02 1 398 44 46 LYS HB2 H 1.744 0.02 2 399 44 46 LYS HB3 H 1.740 0.02 2 400 44 46 LYS HG2 H 1.362 0.02 2 401 44 46 LYS HG3 H 1.456 0.02 2 402 44 46 LYS HD2 H 1.617 0.02 1 403 44 46 LYS HD3 H 1.617 0.02 1 404 44 46 LYS HE2 H 2.901 0.02 2 405 44 46 LYS HE3 H 2.923 0.02 2 406 44 46 LYS C C 176.285 0.2 1 407 44 46 LYS CA C 57.688 0.2 1 408 44 46 LYS CB C 32.064 0.2 1 409 44 46 LYS CG C 25.262 0.2 1 410 44 46 LYS CD C 29.303 0.2 1 411 44 46 LYS CE C 41.927 0.2 1 412 44 46 LYS N N 113.235 0.2 1 413 45 47 GLN H H 6.685 0.02 1 414 45 47 GLN HA H 4.412 0.02 1 415 45 47 GLN HB2 H 1.844 0.02 2 416 45 47 GLN HB3 H 2.469 0.02 2 417 45 47 GLN C C 174.877 0.2 1 418 45 47 GLN CA C 53.731 0.2 1 419 45 47 GLN CB C 29.117 0.2 1 420 45 47 GLN N N 112.457 0.2 1 421 46 48 ILE H H 6.802 0.02 1 422 46 48 ILE HA H 4.862 0.02 1 423 46 48 ILE HB H 1.777 0.02 1 424 46 48 ILE HG12 H 1.767 0.02 2 425 46 48 ILE HG13 H 0.743 0.02 2 426 46 48 ILE HG2 H 0.766 0.02 1 427 46 48 ILE HD1 H 0.455 0.02 1 428 46 48 ILE C C 176.042 0.2 1 429 46 48 ILE CA C 61.795 0.2 1 430 46 48 ILE CB C 37.803 0.2 1 431 46 48 ILE CG1 C 28.163 0.2 1 432 46 48 ILE CG2 C 16.315 0.2 1 433 46 48 ILE CD1 C 13.662 0.2 1 434 46 48 ILE N N 119.020 0.2 1 435 47 49 ARG H H 8.955 0.02 1 436 47 49 ARG HA H 4.666 0.02 1 437 47 49 ARG HB2 H 1.734 0.02 2 438 47 49 ARG HB3 H 1.639 0.02 2 439 47 49 ARG HG2 H 1.495 0.02 2 440 47 49 ARG HG3 H 1.540 0.02 2 441 47 49 ARG HD2 H 3.129 0.02 2 442 47 49 ARG HD3 H 3.181 0.02 2 443 47 49 ARG C C 174.511 0.2 1 444 47 49 ARG CA C 55.249 0.2 1 445 47 49 ARG CB C 33.655 0.2 1 446 47 49 ARG CG C 26.920 0.2 1 447 47 49 ARG CD C 43.086 0.2 1 448 47 49 ARG N N 129.481 0.2 1 449 48 50 ILE H H 8.749 0.02 1 450 48 50 ILE HA H 4.933 0.02 1 451 48 50 ILE HB H 1.775 0.02 1 452 48 50 ILE HG12 H 1.069 0.02 2 453 48 50 ILE HG13 H 1.577 0.02 2 454 48 50 ILE HG2 H 0.749 0.02 1 455 48 50 ILE HD1 H 0.855 0.02 1 456 48 50 ILE C C 175.319 0.2 1 457 48 50 ILE CA C 60.525 0.2 1 458 48 50 ILE CB C 40.733 0.2 1 459 48 50 ILE CG1 C 28.093 0.2 1 460 48 50 ILE CG2 C 19.016 0.2 1 461 48 50 ILE CD1 C 14.482 0.2 1 462 48 50 ILE N N 125.042 0.2 1 463 49 51 THR H H 9.024 0.02 1 464 49 51 THR HA H 5.007 0.02 1 465 49 51 THR HB H 3.999 0.02 1 466 49 51 THR HG2 H 1.217 0.02 1 467 49 51 THR C C 173.177 0.2 1 468 49 51 THR CA C 59.129 0.2 1 469 49 51 THR CB C 71.624 0.2 1 470 49 51 THR CG2 C 21.529 0.2 1 471 49 51 THR N N 122.272 0.2 1 472 50 52 PRO HA H 5.134 0.02 1 473 50 52 PRO HB2 H 1.732 0.02 2 474 50 52 PRO HB3 H 2.063 0.02 2 475 50 52 PRO C C 175.271 0.2 1 476 50 52 PRO CA C 62.102 0.2 1 477 50 52 PRO CB C 33.436 0.2 1 478 51 53 GLU H H 8.798 0.02 1 479 51 53 GLU HA H 4.433 0.02 1 480 51 53 GLU HB2 H 1.819 0.02 1 481 51 53 GLU HB3 H 1.819 0.02 1 482 51 53 GLU HG2 H 1.784 0.02 2 483 51 53 GLU HG3 H 1.876 0.02 2 484 51 53 GLU C C 174.828 0.2 1 485 51 53 GLU CA C 56.294 0.2 1 486 51 53 GLU CB C 31.608 0.2 1 487 51 53 GLU CG C 35.650 0.2 1 488 51 53 GLU N N 120.874 0.2 1 489 52 54 HIS H H 8.873 0.02 1 490 52 54 HIS HA H 4.185 0.02 1 491 52 54 HIS HB2 H 3.336 0.02 2 492 52 54 HIS HB3 H 3.336 0.02 2 493 52 54 HIS C C 171.963 0.2 1 494 52 54 HIS CA C 56.779 0.2 1 495 52 54 HIS CB C 26.511 0.2 1 496 52 54 HIS N N 117.976 0.2 1 497 53 55 ALA H H 7.271 0.02 1 498 53 55 ALA HA H 4.908 0.02 1 499 53 55 ALA HB H 1.206 0.02 1 500 53 55 ALA C C 174.961 0.2 1 501 53 55 ALA CA C 50.715 0.2 1 502 53 55 ALA CB C 23.053 0.2 1 503 53 55 ALA N N 114.451 0.2 1 504 54 56 LYS H H 8.859 0.02 1 505 54 56 LYS HA H 4.746 0.02 1 506 54 56 LYS HB2 H 1.919 0.02 2 507 54 56 LYS HB3 H 1.633 0.02 2 508 54 56 LYS HG2 H 1.461 0.02 2 509 54 56 LYS HG3 H 1.380 0.02 2 510 54 56 LYS HD2 H 1.621 0.02 2 511 54 56 LYS HD3 H 1.664 0.02 2 512 54 56 LYS HE2 H 2.927 0.02 2 513 54 56 LYS HE3 H 2.942 0.02 2 514 54 56 LYS C C 175.797 0.2 1 515 54 56 LYS CA C 54.922 0.2 1 516 54 56 LYS CB C 35.287 0.2 1 517 54 56 LYS CG C 24.559 0.2 1 518 54 56 LYS CD C 28.938 0.2 1 519 54 56 LYS CE C 42.259 0.2 1 520 54 56 LYS N N 119.631 0.2 1 521 55 57 ILE H H 8.783 0.02 1 522 55 57 ILE HA H 5.219 0.02 1 523 55 57 ILE HB H 2.021 0.02 1 524 55 57 ILE HG12 H 0.878 0.02 2 525 55 57 ILE HG13 H 1.532 0.02 2 526 55 57 ILE HG2 H 0.692 0.02 1 527 55 57 ILE HD1 H 0.724 0.02 1 528 55 57 ILE C C 175.313 0.2 1 529 55 57 ILE CA C 58.617 0.2 1 530 55 57 ILE CB C 40.944 0.2 1 531 55 57 ILE CG1 C 25.156 0.2 1 532 55 57 ILE CG2 C 17.492 0.2 1 533 55 57 ILE CD1 C 13.753 0.2 1 534 55 57 ILE N N 117.800 0.2 1 535 56 58 ALA H H 8.224 0.02 1 536 56 58 ALA HA H 4.436 0.02 1 537 56 58 ALA HB H 1.539 0.02 1 538 56 58 ALA C C 177.585 0.2 1 539 56 58 ALA CA C 51.152 0.2 1 540 56 58 ALA CB C 19.487 0.2 1 541 56 58 ALA N N 125.352 0.2 1 542 57 59 ASP H H 8.345 0.02 1 543 57 59 ASP HA H 4.402 0.02 1 544 57 59 ASP HB2 H 2.550 0.02 2 545 57 59 ASP HB3 H 2.569 0.02 2 546 57 59 ASP C C 176.636 0.2 1 547 57 59 ASP CA C 55.661 0.2 1 548 57 59 ASP CB C 40.609 0.2 1 549 57 59 ASP N N 120.354 0.2 1 550 58 60 VAL H H 8.354 0.02 1 551 58 60 VAL HA H 4.067 0.02 1 552 58 60 VAL HB H 2.040 0.02 1 553 58 60 VAL HG1 H 0.905 0.02 2 554 58 60 VAL HG2 H 1.114 0.02 2 555 58 60 VAL C C 176.002 0.2 1 556 58 60 VAL CA C 62.793 0.2 1 557 58 60 VAL CB C 32.864 0.2 1 558 58 60 VAL CG1 C 21.640 0.2 2 559 58 60 VAL CG2 C 22.307 0.2 2 560 58 60 VAL N N 124.773 0.2 1 561 59 61 GLN H H 8.702 0.02 1 562 59 61 GLN HA H 4.524 0.02 1 563 59 61 GLN HB2 H 2.002 0.02 2 564 59 61 GLN HB3 H 1.976 0.02 2 565 59 61 GLN HG2 H 2.288 0.02 1 566 59 61 GLN HG3 H 2.288 0.02 1 567 59 61 GLN C C 174.833 0.2 1 568 59 61 GLN CA C 53.908 0.2 1 569 59 61 GLN CB C 28.884 0.2 1 570 59 61 GLN CG C 33.458 0.2 1 571 59 61 GLN N N 128.142 0.2 1 572 60 62 LEU H H 8.611 0.02 1 573 60 62 LEU HA H 4.504 0.02 1 574 60 62 LEU HB2 H 1.744 0.02 2 575 60 62 LEU HB3 H 1.582 0.02 2 576 60 62 LEU HG H 1.664 0.02 1 577 60 62 LEU HD1 H 0.910 0.02 2 578 60 62 LEU HD2 H 1.004 0.02 2 579 60 62 LEU C C 175.862 0.2 1 580 60 62 LEU CA C 52.841 0.2 1 581 60 62 LEU CB C 40.009 0.2 1 582 60 62 LEU CG C 27.876 0.2 1 583 60 62 LEU CD1 C 24.972 0.2 2 584 60 62 LEU CD2 C 26.568 0.2 2 585 60 62 LEU N N 127.216 0.2 1 586 61 63 PRO HA H 4.646 0.02 1 587 61 63 PRO HB2 H 2.113 0.02 2 588 61 63 PRO HB3 H 2.421 0.02 2 589 61 63 PRO C C 177.328 0.2 1 590 61 63 PRO CA C 62.181 0.2 1 591 61 63 PRO CB C 32.740 0.2 1 592 62 64 GLN H H 8.998 0.02 1 593 62 64 GLN HA H 4.119 0.02 1 594 62 64 GLN HB2 H 2.156 0.02 2 595 62 64 GLN HB3 H 2.143 0.02 2 596 62 64 GLN HG2 H 2.573 0.02 2 597 62 64 GLN HG3 H 2.603 0.02 2 598 62 64 GLN C C 176.938 0.2 1 599 62 64 GLN CA C 57.536 0.2 1 600 62 64 GLN CB C 29.391 0.2 1 601 62 64 GLN CG C 34.028 0.2 1 602 62 64 GLN N N 123.363 0.2 1 603 63 65 GLY H H 9.603 0.02 1 604 63 65 GLY HA2 H 3.095 0.02 2 605 63 65 GLY HA3 H 4.684 0.02 2 606 63 65 GLY C C 173.079 0.2 1 607 63 65 GLY CA C 43.994 0.2 1 608 63 65 GLY N N 115.423 0.2 1 609 64 66 VAL H H 8.670 0.02 1 610 64 66 VAL HA H 4.536 0.02 1 611 64 66 VAL HB H 2.026 0.02 1 612 64 66 VAL HG1 H 0.830 0.02 2 613 64 66 VAL HG2 H 0.980 0.02 2 614 64 66 VAL C C 175.169 0.2 1 615 64 66 VAL CA C 59.961 0.2 1 616 64 66 VAL CB C 34.591 0.2 1 617 64 66 VAL CG1 C 19.616 0.2 2 618 64 66 VAL CG2 C 21.301 0.2 2 619 64 66 VAL N N 118.256 0.2 1 620 65 67 TRP H H 8.704 0.02 1 621 65 67 TRP HA H 4.781 0.02 1 622 65 67 TRP HB2 H 3.061 0.02 2 623 65 67 TRP HB3 H 3.082 0.02 2 624 65 67 TRP HE1 H 10.025 0.02 1 625 65 67 TRP C C 176.661 0.2 1 626 65 67 TRP CA C 58.434 0.2 1 627 65 67 TRP CB C 29.711 0.2 1 628 65 67 TRP N N 123.915 0.2 1 629 65 67 TRP NE1 N 129.000 0.2 1 630 66 68 HIS H H 9.356 0.02 1 631 66 68 HIS HA H 4.814 0.02 1 632 66 68 HIS HB2 H 2.578 0.02 2 633 66 68 HIS HB3 H 2.690 0.02 2 634 66 68 HIS C C 172.621 0.2 1 635 66 68 HIS CA C 55.239 0.2 1 636 66 68 HIS N N 124.992 0.2 1 637 67 69 GLU HA H 5.085 0.02 1 638 67 69 GLU HB2 H 1.783 0.02 2 639 67 69 GLU HB3 H 1.678 0.02 2 640 67 69 GLU HG2 H 1.959 0.02 1 641 67 69 GLU HG3 H 1.959 0.02 1 642 67 69 GLU C C 174.271 0.2 1 643 67 69 GLU CA C 55.120 0.2 1 644 67 69 GLU CB C 31.952 0.2 1 645 67 69 GLU CG C 36.393 0.2 1 646 68 70 ASP H H 8.098 0.02 1 647 68 70 ASP HA H 4.699 0.02 1 648 68 70 ASP HB2 H 3.022 0.02 2 649 68 70 ASP HB3 H 3.273 0.02 2 650 68 70 ASP C C 176.473 0.2 1 651 68 70 ASP CA C 52.891 0.2 1 652 68 70 ASP CB C 43.699 0.2 1 653 68 70 ASP N N 120.039 0.2 1 654 69 71 GLU H H 8.777 0.02 1 655 69 71 GLU HA H 4.058 0.02 1 656 69 71 GLU HB2 H 1.589 0.02 1 657 69 71 GLU HB3 H 1.589 0.02 1 658 69 71 GLU HG2 H 1.346 0.02 2 659 69 71 GLU HG3 H 1.408 0.02 2 660 69 71 GLU C C 175.516 0.2 1 661 69 71 GLU CA C 56.844 0.2 1 662 69 71 GLU CB C 29.327 0.2 1 663 69 71 GLU CG C 35.053 0.2 1 664 69 71 GLU N N 115.930 0.2 1 665 70 72 PHE H H 8.194 0.02 1 666 70 72 PHE HA H 4.208 0.02 1 667 70 72 PHE HB2 H 2.796 0.02 2 668 70 72 PHE HB3 H 2.994 0.02 2 669 70 72 PHE C C 176.930 0.2 1 670 70 72 PHE CA C 59.454 0.2 1 671 70 72 PHE CB C 39.219 0.2 1 672 70 72 PHE N N 122.158 0.2 1 673 71 73 TYR H H 8.448 0.02 1 674 71 73 TYR HA H 4.666 0.02 1 675 71 73 TYR HB2 H 2.348 0.02 2 676 71 73 TYR HB3 H 3.131 0.02 2 677 71 73 TYR C C 175.809 0.2 1 678 71 73 TYR CA C 57.610 0.2 1 679 71 73 TYR CB C 40.299 0.2 1 680 71 73 TYR N N 114.760 0.2 1 681 72 74 GLY H H 7.500 0.02 1 682 72 74 GLY HA2 H 4.008 0.02 2 683 72 74 GLY HA3 H 4.107 0.02 2 684 72 74 GLY C C 175.335 0.2 1 685 72 74 GLY CA C 46.121 0.2 1 686 72 74 GLY N N 109.910 0.2 1 687 73 75 LYS H H 8.885 0.02 1 688 73 75 LYS HA H 4.890 0.02 1 689 73 75 LYS HB2 H 1.902 0.02 2 690 73 75 LYS HB3 H 1.811 0.02 2 691 73 75 LYS HG2 H 1.433 0.02 1 692 73 75 LYS HG3 H 1.433 0.02 1 693 73 75 LYS HD2 H 1.511 0.02 2 694 73 75 LYS HD3 H 1.581 0.02 2 695 73 75 LYS HE2 H 2.587 0.02 2 696 73 75 LYS HE3 H 2.713 0.02 2 697 73 75 LYS C C 176.281 0.2 1 698 73 75 LYS CA C 57.254 0.2 1 699 73 75 LYS CB C 32.190 0.2 1 700 73 75 LYS CG C 26.062 0.2 1 701 73 75 LYS CD C 29.430 0.2 1 702 73 75 LYS CE C 41.895 0.2 1 703 73 75 LYS N N 129.404 0.2 1 704 74 76 SER H H 9.348 0.02 1 705 74 76 SER HA H 4.898 0.02 1 706 74 76 SER HB2 H 3.817 0.02 1 707 74 76 SER HB3 H 3.817 0.02 1 708 74 76 SER C C 170.972 0.2 1 709 74 76 SER CA C 58.637 0.2 1 710 74 76 SER CB C 67.213 0.2 1 711 74 76 SER N N 123.528 0.2 1 712 75 77 GLU H H 8.176 0.02 1 713 75 77 GLU HA H 3.835 0.02 1 714 75 77 GLU HB2 H 1.047 0.02 2 715 75 77 GLU HB3 H 0.674 0.02 2 716 75 77 GLU HG2 H 0.750 0.02 2 717 75 77 GLU HG3 H 0.833 0.02 2 718 75 77 GLU C C 176.913 0.2 1 719 75 77 GLU CA C 55.074 0.2 1 720 75 77 GLU CB C 30.861 0.2 1 721 75 77 GLU CG C 35.983 0.2 1 722 75 77 GLU N N 123.683 0.2 1 723 76 78 ILE H H 9.362 0.02 1 724 76 78 ILE HA H 5.039 0.02 1 725 76 78 ILE HB H 1.509 0.02 1 726 76 78 ILE HG12 H 0.699 0.02 2 727 76 78 ILE HG13 H 0.962 0.02 2 728 76 78 ILE HG2 H 0.558 0.02 1 729 76 78 ILE HD1 H -0.339 0.02 1 730 76 78 ILE C C 173.776 0.2 1 731 76 78 ILE CA C 59.376 0.2 1 732 76 78 ILE CB C 42.701 0.2 1 733 76 78 ILE CG1 C 25.694 0.2 1 734 76 78 ILE CG2 C 18.656 0.2 1 735 76 78 ILE CD1 C 13.157 0.2 1 736 76 78 ILE N N 122.062 0.2 1 737 77 79 TYR H H 8.700 0.02 1 738 77 79 TYR HA H 5.247 0.02 1 739 77 79 TYR HB2 H 2.221 0.02 2 740 77 79 TYR HB3 H 2.970 0.02 2 741 77 79 TYR C C 175.060 0.2 1 742 77 79 TYR CA C 55.610 0.2 1 743 77 79 TYR CB C 41.578 0.2 1 744 77 79 TYR N N 116.368 0.2 1 745 78 80 ARG H H 8.306 0.02 1 746 78 80 ARG HA H 4.639 0.02 1 747 78 80 ARG HB2 H 1.607 0.02 2 748 78 80 ARG HB3 H 1.973 0.02 2 749 78 80 ARG HG2 H 1.358 0.02 2 750 78 80 ARG HG3 H 1.806 0.02 2 751 78 80 ARG HD2 H 3.331 0.02 2 752 78 80 ARG HD3 H 3.018 0.02 2 753 78 80 ARG C C 176.292 0.2 1 754 78 80 ARG CA C 54.670 0.2 1 755 78 80 ARG CB C 34.110 0.2 1 756 78 80 ARG CD C 43.061 0.2 1 757 78 80 ARG N N 118.583 0.2 1 758 79 81 ASP H H 9.048 0.02 1 759 79 81 ASP HA H 4.395 0.02 1 760 79 81 ASP HB2 H 2.921 0.02 2 761 79 81 ASP HB3 H 3.104 0.02 2 762 79 81 ASP C C 174.810 0.2 1 763 79 81 ASP CA C 59.200 0.2 1 764 79 81 ASP CB C 40.412 0.2 1 765 79 81 ASP N N 115.392 0.2 1 766 80 82 ARG H H 9.048 0.02 1 767 80 82 ARG HA H 5.036 0.02 1 768 80 82 ARG HB2 H 1.861 0.02 2 769 80 82 ARG HB3 H 1.832 0.02 2 770 80 82 ARG HG2 H 1.552 0.02 2 771 80 82 ARG HG3 H 1.485 0.02 2 772 80 82 ARG HD2 H 3.128 0.02 1 773 80 82 ARG HD3 H 3.128 0.02 1 774 80 82 ARG C C 173.973 0.2 1 775 80 82 ARG CA C 55.526 0.2 1 776 80 82 ARG CB C 32.746 0.2 1 777 80 82 ARG CG C 27.129 0.2 1 778 80 82 ARG CD C 43.355 0.2 1 779 80 82 ARG N N 124.126 0.2 1 780 81 83 LEU H H 8.679 0.02 1 781 81 83 LEU HA H 4.566 0.02 1 782 81 83 LEU HB2 H 1.569 0.02 2 783 81 83 LEU HB3 H 0.744 0.02 2 784 81 83 LEU HG H 1.045 0.02 1 785 81 83 LEU HD1 H -0.245 0.02 2 786 81 83 LEU HD2 H -0.044 0.02 2 787 81 83 LEU C C 174.269 0.2 1 788 81 83 LEU CA C 54.040 0.2 1 789 81 83 LEU CB C 45.418 0.2 1 790 81 83 LEU CG C 27.073 0.2 1 791 81 83 LEU CD1 C 26.393 0.2 2 792 81 83 LEU CD2 C 21.019 0.2 2 793 81 83 LEU N N 125.820 0.2 1 794 82 84 THR H H 8.520 0.02 1 795 82 84 THR HA H 5.235 0.02 1 796 82 84 THR HB H 3.873 0.02 1 797 82 84 THR HG2 H 1.053 0.02 1 798 82 84 THR C C 172.521 0.2 1 799 82 84 THR CA C 61.212 0.2 1 800 82 84 THR CB C 70.568 0.2 1 801 82 84 THR CG2 C 21.261 0.2 1 802 82 84 THR N N 123.553 0.2 1 803 83 85 LEU H H 9.695 0.02 1 804 83 85 LEU HA H 5.080 0.02 1 805 83 85 LEU HB2 H 1.532 0.02 2 806 83 85 LEU HB3 H 1.796 0.02 2 807 83 85 LEU HG H 1.627 0.02 1 808 83 85 LEU HD1 H 0.940 0.02 2 809 83 85 LEU HD2 H 0.914 0.02 2 810 83 85 LEU C C 173.054 0.2 1 811 83 85 LEU CA C 50.777 0.2 1 812 83 85 LEU CB C 45.659 0.2 1 813 83 85 LEU CG C 27.099 0.2 1 814 83 85 LEU CD1 C 26.089 0.2 2 815 83 85 LEU CD2 C 25.945 0.2 2 816 83 85 LEU N N 128.038 0.2 1 817 84 86 PRO HA H 5.166 0.02 1 818 84 86 PRO HB2 H 1.986 0.02 2 819 84 86 PRO HB3 H 2.243 0.02 2 820 84 86 PRO C C 176.393 0.2 1 821 84 86 PRO CA C 61.890 0.2 1 822 84 86 PRO CB C 31.873 0.2 1 823 85 87 VAL H H 9.311 0.02 1 824 85 87 VAL HA H 4.447 0.02 1 825 85 87 VAL HB H 1.932 0.02 1 826 85 87 VAL HG1 H 0.879 0.02 2 827 85 87 VAL HG2 H 0.873 0.02 2 828 85 87 VAL C C 175.395 0.2 1 829 85 87 VAL CA C 60.708 0.2 1 830 85 87 VAL CB C 35.369 0.2 1 831 85 87 VAL CG1 C 21.597 0.2 2 832 85 87 VAL CG2 C 21.567 0.2 2 833 85 87 VAL N N 125.255 0.2 1 834 86 88 THR H H 9.331 0.02 1 835 86 88 THR HA H 4.920 0.02 1 836 86 88 THR HB H 3.949 0.02 1 837 86 88 THR HG2 H 1.128 0.02 1 838 86 88 THR C C 173.344 0.2 1 839 86 88 THR CA C 62.351 0.2 1 840 86 88 THR CB C 70.058 0.2 1 841 86 88 THR CG2 C 21.603 0.2 1 842 86 88 THR N N 125.305 0.2 1 843 87 89 ILE H H 9.878 0.02 1 844 87 89 ILE HA H 4.136 0.02 1 845 87 89 ILE HB H 1.988 0.02 1 846 87 89 ILE HG12 H 0.860 0.02 2 847 87 89 ILE HG13 H 1.466 0.02 2 848 87 89 ILE HG2 H 0.641 0.02 1 849 87 89 ILE HD1 H 0.755 0.02 1 850 87 89 ILE C C 175.289 0.2 1 851 87 89 ILE CA C 59.914 0.2 1 852 87 89 ILE CB C 38.297 0.2 1 853 87 89 ILE CG1 C 26.297 0.2 1 854 87 89 ILE CG2 C 18.899 0.2 1 855 87 89 ILE CD1 C 15.038 0.2 1 856 87 89 ILE N N 128.190 0.2 1 857 88 90 ASN H H 9.032 0.02 1 858 88 90 ASN HA H 4.737 0.02 1 859 88 90 ASN HB2 H 2.326 0.02 2 860 88 90 ASN HB3 H 2.854 0.02 2 861 88 90 ASN C C 175.120 0.2 1 862 88 90 ASN CA C 55.568 0.2 1 863 88 90 ASN CB C 39.246 0.2 1 864 88 90 ASN N N 127.528 0.2 1 865 89 91 GLN H H 7.728 0.02 1 866 89 91 GLN HA H 4.170 0.02 1 867 89 91 GLN HB2 H 2.018 0.02 2 868 89 91 GLN HB3 H 2.020 0.02 2 869 89 91 GLN HG2 H 2.307 0.02 2 870 89 91 GLN HG3 H 2.401 0.02 2 871 89 91 GLN C C 173.132 0.2 1 872 89 91 GLN CA C 55.807 0.2 1 873 89 91 GLN CB C 30.761 0.2 1 874 89 91 GLN CG C 33.082 0.2 1 875 89 91 GLN N N 115.458 0.2 1 876 90 92 ALA H H 9.341 0.02 1 877 90 92 ALA HA H 4.733 0.02 1 878 90 92 ALA HB H 1.271 0.02 1 879 90 92 ALA C C 176.134 0.2 1 880 90 92 ALA CA C 53.156 0.2 1 881 90 92 ALA CB C 21.306 0.2 1 882 90 92 ALA N N 125.700 0.2 1 883 91 93 SER H H 8.381 0.02 1 884 91 93 SER HA H 4.660 0.02 1 885 91 93 SER HB2 H 3.814 0.02 2 886 91 93 SER HB3 H 4.034 0.02 2 887 91 93 SER C C 172.756 0.2 1 888 91 93 SER CA C 57.842 0.2 1 889 91 93 SER CB C 64.568 0.2 1 890 91 93 SER N N 120.091 0.2 1 891 92 94 ALA H H 8.499 0.02 1 892 92 94 ALA HA H 4.184 0.02 1 893 92 94 ALA HB H 1.322 0.02 1 894 92 94 ALA C C 179.344 0.2 1 895 92 94 ALA CA C 53.852 0.2 1 896 92 94 ALA CB C 17.759 0.2 1 897 92 94 ALA N N 123.723 0.2 1 898 93 95 GLY H H 9.128 0.02 1 899 93 95 GLY HA2 H 3.732 0.02 2 900 93 95 GLY HA3 H 4.038 0.02 2 901 93 95 GLY C C 174.458 0.2 1 902 93 95 GLY CA C 45.285 0.2 1 903 93 95 GLY N N 112.501 0.2 1 904 94 96 ALA H H 7.873 0.02 1 905 94 96 ALA HA H 4.489 0.02 1 906 94 96 ALA HB H 1.646 0.02 1 907 94 96 ALA C C 177.097 0.2 1 908 94 96 ALA CA C 52.906 0.2 1 909 94 96 ALA CB C 22.044 0.2 1 910 94 96 ALA N N 122.540 0.2 1 911 95 97 THR H H 8.331 0.02 1 912 95 97 THR HA H 5.166 0.02 1 913 95 97 THR HB H 3.855 0.02 1 914 95 97 THR C C 173.526 0.2 1 915 95 97 THR CA C 59.601 0.2 1 916 95 97 THR CB C 74.119 0.2 1 917 95 97 THR N N 109.167 0.2 1 918 96 98 LEU H H 8.837 0.02 1 919 96 98 LEU HA H 4.849 0.02 1 920 96 98 LEU HB2 H 1.298 0.02 2 921 96 98 LEU HB3 H 1.306 0.02 2 922 96 98 LEU HG H 1.424 0.02 1 923 96 98 LEU HD1 H 0.651 0.02 2 924 96 98 LEU HD2 H 0.691 0.02 2 925 96 98 LEU C C 175.694 0.2 1 926 96 98 LEU CA C 53.552 0.2 1 927 96 98 LEU CB C 45.361 0.2 1 928 96 98 LEU CG C 26.458 0.2 1 929 96 98 LEU CD1 C 25.052 0.2 2 930 96 98 LEU CD2 C 25.785 0.2 2 931 96 98 LEU N N 117.279 0.2 1 932 97 99 THR H H 8.857 0.02 1 933 97 99 THR HA H 4.843 0.02 1 934 97 99 THR HB H 3.980 0.02 1 935 97 99 THR HG2 H 1.050 0.02 1 936 97 99 THR C C 173.922 0.2 1 937 97 99 THR CA C 62.998 0.2 1 938 97 99 THR CB C 69.246 0.2 1 939 97 99 THR CG2 C 21.685 0.2 1 940 97 99 THR N N 122.085 0.2 1 941 98 100 VAL H H 9.376 0.02 1 942 98 100 VAL HA H 4.931 0.02 1 943 98 100 VAL HB H 1.853 0.02 1 944 98 100 VAL HG1 H 0.880 0.02 2 945 98 100 VAL HG2 H 1.037 0.02 2 946 98 100 VAL C C 173.693 0.2 1 947 98 100 VAL CA C 60.979 0.2 1 948 98 100 VAL CB C 34.058 0.2 1 949 98 100 VAL CG1 C 21.342 0.2 2 950 98 100 VAL CG2 C 20.901 0.2 2 951 98 100 VAL N N 130.097 0.2 1 952 99 101 THR H H 9.207 0.02 1 953 99 101 THR HA H 5.767 0.02 1 954 99 101 THR HB H 3.790 0.02 1 955 99 101 THR HG2 H 1.135 0.02 1 956 99 101 THR C C 172.521 0.2 1 957 99 101 THR CA C 60.363 0.2 1 958 99 101 THR CB C 71.269 0.2 1 959 99 101 THR CG2 C 21.746 0.2 1 960 99 101 THR N N 124.433 0.2 1 961 100 102 TYR H H 8.306 0.02 1 962 100 102 TYR HA H 4.863 0.02 1 963 100 102 TYR HB2 H 2.504 0.02 2 964 100 102 TYR HB3 H 2.935 0.02 2 965 100 102 TYR C C 172.231 0.2 1 966 100 102 TYR CA C 55.607 0.2 1 967 100 102 TYR CB C 38.864 0.2 1 968 100 102 TYR N N 117.968 0.2 1 969 101 103 GLN H H 8.266 0.02 1 970 101 103 GLN HA H 5.007 0.02 1 971 101 103 GLN HB2 H 1.893 0.02 2 972 101 103 GLN HB3 H 1.551 0.02 2 973 101 103 GLN HG2 H 2.528 0.02 2 974 101 103 GLN HG3 H 2.372 0.02 2 975 101 103 GLN C C 173.867 0.2 1 976 101 103 GLN CA C 54.780 0.2 1 977 101 103 GLN CB C 32.732 0.2 1 978 101 103 GLN CG C 33.655 0.2 1 979 101 103 GLN N N 118.163 0.2 1 980 102 104 GLY H H 7.885 0.02 1 981 102 104 GLY HA2 H 4.601 0.02 2 982 102 104 GLY HA3 H 3.261 0.02 2 983 102 104 GLY C C 170.442 0.2 1 984 102 104 GLY CA C 44.962 0.2 1 985 102 104 GLY N N 115.034 0.2 1 986 103 105 CYS H H 8.615 0.02 1 987 103 105 CYS HA H 5.168 0.02 1 988 103 105 CYS HB2 H 1.765 0.02 2 989 103 105 CYS HB3 H 2.393 0.02 2 990 103 105 CYS C C 171.492 0.2 1 991 103 105 CYS CA C 56.961 0.2 1 992 103 105 CYS CB C 32.120 0.2 1 993 103 105 CYS N N 117.620 0.2 1 994 104 106 ALA H H 9.000 0.02 1 995 104 106 ALA HA H 4.802 0.02 1 996 104 106 ALA HB H 1.489 0.02 1 997 104 106 ALA C C 179.442 0.2 1 998 104 106 ALA CA C 50.351 0.2 1 999 104 106 ALA CB C 21.967 0.2 1 1000 104 106 ALA N N 125.034 0.2 1 1001 105 107 ASP H H 9.143 0.02 1 1002 105 107 ASP HA H 4.672 0.02 1 1003 105 107 ASP HB2 H 2.550 0.02 2 1004 105 107 ASP HB3 H 2.689 0.02 2 1005 105 107 ASP C C 177.385 0.2 1 1006 105 107 ASP CA C 58.264 0.2 1 1007 105 107 ASP CB C 40.876 0.2 1 1008 105 107 ASP N N 127.223 0.2 1 1009 106 108 ALA H H 8.157 0.02 1 1010 106 108 ALA HA H 4.373 0.02 1 1011 106 108 ALA HB H 1.517 0.02 1 1012 106 108 ALA C C 177.703 0.2 1 1013 106 108 ALA CA C 53.140 0.2 1 1014 106 108 ALA CB C 18.462 0.2 1 1015 106 108 ALA N N 117.220 0.2 1 1016 107 109 GLY H H 7.962 0.02 1 1017 107 109 GLY HA2 H 4.507 0.02 2 1018 107 109 GLY HA3 H 3.935 0.02 2 1019 107 109 GLY C C 172.708 0.2 1 1020 107 109 GLY CA C 46.511 0.2 1 1021 107 109 GLY N N 104.214 0.2 1 1022 108 110 PHE H H 6.699 0.02 1 1023 108 110 PHE HA H 4.437 0.02 1 1024 108 110 PHE HB2 H 2.191 0.02 2 1025 108 110 PHE HB3 H 2.025 0.02 2 1026 108 110 PHE C C 170.780 0.2 1 1027 108 110 PHE CA C 57.618 0.2 1 1028 108 110 PHE CB C 41.151 0.2 1 1029 108 110 PHE N N 119.753 0.2 1 1030 109 111 CYS H H 7.612 0.02 1 1031 109 111 CYS HA H 4.446 0.02 1 1032 109 111 CYS HB2 H 0.664 0.02 2 1033 109 111 CYS HB3 H 1.832 0.02 2 1034 109 111 CYS C C 173.861 0.2 1 1035 109 111 CYS CA C 58.272 0.2 1 1036 109 111 CYS CB C 25.840 0.2 1 1037 109 111 CYS N N 129.553 0.2 1 1038 110 112 TYR H H 8.630 0.02 1 1039 110 112 TYR HA H 4.235 0.02 1 1040 110 112 TYR HB2 H 3.156 0.02 2 1041 110 112 TYR HB3 H 3.174 0.02 2 1042 110 112 TYR C C 173.691 0.2 1 1043 110 112 TYR CA C 58.156 0.2 1 1044 110 112 TYR CB C 37.894 0.2 1 1045 110 112 TYR N N 129.617 0.2 1 1046 112 114 PRO HA H 4.342 0.02 1 1047 112 114 PRO HB2 H 1.637 0.02 2 1048 112 114 PRO HB3 H 1.973 0.02 2 1049 112 114 PRO C C 175.798 0.2 1 1050 112 114 PRO CA C 63.511 0.2 1 1051 112 114 PRO CB C 31.502 0.2 1 1052 113 115 GLU H H 8.677 0.02 1 1053 113 115 GLU HA H 4.337 0.02 1 1054 113 115 GLU HB2 H 0.898 0.02 2 1055 113 115 GLU HB3 H 1.320 0.02 2 1056 113 115 GLU HG2 H 2.025 0.02 2 1057 113 115 GLU HG3 H 2.107 0.02 2 1058 113 115 GLU C C 174.478 0.2 1 1059 113 115 GLU CA C 54.206 0.2 1 1060 113 115 GLU CB C 32.974 0.2 1 1061 113 115 GLU CG C 35.570 0.2 1 1062 113 115 GLU N N 124.991 0.2 1 1063 114 116 THR H H 8.255 0.02 1 1064 114 116 THR HA H 5.110 0.02 1 1065 114 116 THR HB H 3.701 0.02 1 1066 114 116 THR HG2 H 0.947 0.02 1 1067 114 116 THR C C 174.037 0.2 1 1068 114 116 THR CA C 61.743 0.2 1 1069 114 116 THR CB C 71.228 0.2 1 1070 114 116 THR CG2 C 21.514 0.2 1 1071 114 116 THR N N 117.017 0.2 1 1072 115 117 LYS H H 9.358 0.02 1 1073 115 117 LYS HA H 4.695 0.02 1 1074 115 117 LYS HB2 H 1.288 0.02 2 1075 115 117 LYS HB3 H 1.581 0.02 2 1076 115 117 LYS HG2 H 1.036 0.02 2 1077 115 117 LYS HG3 H 1.159 0.02 2 1078 115 117 LYS HD2 H 1.653 0.02 2 1079 115 117 LYS HD3 H 1.835 0.02 2 1080 115 117 LYS HE2 H 3.097 0.02 2 1081 115 117 LYS HE3 H 3.179 0.02 2 1082 115 117 LYS C C 175.140 0.2 1 1083 115 117 LYS CA C 52.750 0.2 1 1084 115 117 LYS CB C 35.647 0.2 1 1085 115 117 LYS CG C 24.694 0.2 1 1086 115 117 LYS CD C 28.727 0.2 1 1087 115 117 LYS CE C 42.750 0.2 1 1088 115 117 LYS N N 126.861 0.2 1 1089 116 118 THR H H 8.686 0.02 1 1090 116 118 THR HA H 4.745 0.02 1 1091 116 118 THR HB H 3.887 0.02 1 1092 116 118 THR C C 173.735 0.2 1 1093 116 118 THR CA C 62.465 0.2 1 1094 116 118 THR CB C 69.692 0.2 1 1095 116 118 THR N N 118.693 0.2 1 1096 117 119 VAL H H 9.252 0.02 1 1097 117 119 VAL HA H 3.965 0.02 1 1098 117 119 VAL HB H 1.751 0.02 1 1099 117 119 VAL HG1 H -0.140 0.02 2 1100 117 119 VAL HG2 H 0.556 0.02 2 1101 117 119 VAL C C 172.959 0.2 1 1102 117 119 VAL CA C 58.529 0.2 1 1103 117 119 VAL CB C 33.368 0.2 1 1104 117 119 VAL CG1 C 19.640 0.2 2 1105 117 119 VAL CG2 C 20.725 0.2 2 1106 117 119 VAL N N 129.373 0.2 1 1107 118 120 PRO HA H 4.518 0.02 1 1108 118 120 PRO HB2 H 1.963 0.02 2 1109 118 120 PRO HB3 H 2.182 0.02 2 1110 118 120 PRO C C 175.561 0.2 1 1111 118 120 PRO CA C 62.361 0.2 1 1112 118 120 PRO CB C 31.690 0.2 1 1113 119 121 LEU H H 7.768 0.02 1 1114 119 121 LEU HA H 4.576 0.02 1 1115 119 121 LEU HB2 H 1.395 0.02 2 1116 119 121 LEU HB3 H 1.071 0.02 2 1117 119 121 LEU HG H 1.375 0.02 1 1118 119 121 LEU HD1 H 0.493 0.02 2 1119 119 121 LEU HD2 H 0.524 0.02 2 1120 119 121 LEU C C 177.285 0.2 1 1121 119 121 LEU CA C 52.627 0.2 1 1122 119 121 LEU CB C 43.389 0.2 1 1123 119 121 LEU CG C 26.433 0.2 1 1124 119 121 LEU CD1 C 25.422 0.2 2 1125 119 121 LEU CD2 C 23.327 0.2 2 1126 119 121 LEU N N 120.912 0.2 1 1127 120 122 SER H H 9.295 0.02 1 1128 120 122 SER HA H 4.377 0.02 1 1129 120 122 SER HB2 H 3.660 0.02 2 1130 120 122 SER HB3 H 3.811 0.02 2 1131 120 122 SER C C 173.145 0.2 1 1132 120 122 SER CA C 58.131 0.2 1 1133 120 122 SER CB C 63.850 0.2 1 1134 120 122 SER N N 119.433 0.2 1 1135 121 123 GLU H H 8.201 0.02 1 1136 121 123 GLU HA H 3.648 0.02 1 1137 121 123 GLU HB2 H 1.875 0.02 2 1138 121 123 GLU HB3 H 1.796 0.02 2 1139 121 123 GLU HG2 H 2.012 0.02 2 1140 121 123 GLU HG3 H 2.401 0.02 2 1141 121 123 GLU C C 176.305 0.2 1 1142 121 123 GLU CA C 57.648 0.2 1 1143 121 123 GLU CB C 30.819 0.2 1 1144 121 123 GLU CG C 36.287 0.2 1 1145 121 123 GLU N N 121.021 0.2 1 1146 122 124 VAL H H 8.777 0.02 1 1147 122 124 VAL HA H 4.152 0.02 1 1148 122 124 VAL HB H 1.536 0.02 1 1149 122 124 VAL HG1 H 0.313 0.02 2 1150 122 124 VAL HG2 H 0.537 0.02 2 1151 122 124 VAL C C 175.243 0.2 1 1152 122 124 VAL CA C 61.461 0.2 1 1153 122 124 VAL CB C 35.367 0.2 1 1154 122 124 VAL CG1 C 20.971 0.2 2 1155 122 124 VAL CG2 C 20.986 0.2 2 1156 122 124 VAL N N 124.437 0.2 1 1157 123 125 VAL H H 8.643 0.02 1 1158 123 125 VAL HA H 4.193 0.02 1 1159 123 125 VAL HB H 2.041 0.02 1 1160 123 125 VAL HG1 H 0.996 0.02 2 1161 123 125 VAL HG2 H 0.950 0.02 2 1162 123 125 VAL C C 175.607 0.2 1 1163 123 125 VAL CA C 61.969 0.2 1 1164 123 125 VAL CB C 32.603 0.2 1 1165 123 125 VAL CG1 C 21.316 0.2 2 1166 123 125 VAL CG2 C 20.642 0.2 2 1167 123 125 VAL N N 127.639 0.2 1 1168 124 126 ALA H H 8.592 0.02 1 1169 124 126 ALA HA H 4.536 0.02 1 1170 124 126 ALA HB H 1.375 0.02 1 1171 124 126 ALA C C 177.806 0.2 1 1172 124 126 ALA CA C 52.352 0.2 1 1173 124 126 ALA CB C 19.169 0.2 1 1174 124 126 ALA N N 127.688 0.2 1 1175 125 127 ASN H H 8.627 0.02 1 1176 125 127 ASN HA H 4.671 0.02 1 1177 125 127 ASN HB2 H 2.755 0.02 1 1178 125 127 ASN HB3 H 2.755 0.02 1 1179 125 127 ASN C C 175.086 0.2 1 1180 125 127 ASN CA C 53.078 0.2 1 1181 125 127 ASN CB C 38.632 0.2 1 1182 125 127 ASN N N 119.330 0.2 1 1183 126 128 ASN H H 8.419 0.02 1 1184 126 128 ASN HA H 4.665 0.02 1 1185 126 128 ASN HB2 H 2.756 0.02 1 1186 126 128 ASN HB3 H 2.756 0.02 1 1187 126 128 ASN C C 174.688 0.2 1 1188 126 128 ASN CA C 53.121 0.2 1 1189 126 128 ASN CB C 38.632 0.2 1 1190 126 128 ASN N N 119.499 0.2 1 1191 127 129 ALA H H 8.121 0.02 1 1192 127 129 ALA HA H 4.265 0.02 1 1193 127 129 ALA HB H 1.323 0.02 1 1194 127 129 ALA C C 176.902 0.2 1 1195 127 129 ALA CA C 52.198 0.2 1 1196 127 129 ALA CB C 19.576 0.2 1 1197 127 129 ALA N N 124.050 0.2 1 1198 128 130 ALA H H 8.163 0.02 1 1199 128 130 ALA HA H 4.561 0.02 1 1200 128 130 ALA HB H 1.328 0.02 1 1201 128 130 ALA CA C 50.239 0.2 1 1202 128 130 ALA CB C 18.229 0.2 1 1203 128 130 ALA N N 124.724 0.2 1 1204 129 131 PRO HA H 4.444 0.02 1 1205 129 131 PRO HB2 H 1.862 0.02 2 1206 129 131 PRO HB3 H 2.252 0.02 2 1207 129 131 PRO C C 176.740 0.2 1 1208 129 131 PRO CA C 62.941 0.2 1 1209 129 131 PRO CB C 32.051 0.2 1 1210 130 132 GLN H H 8.416 0.02 1 1211 130 132 GLN HA H 4.579 0.02 1 1212 130 132 GLN HB2 H 2.076 0.02 2 1213 130 132 GLN HB3 H 1.902 0.02 2 1214 130 132 GLN HG2 H 2.378 0.02 2 1215 130 132 GLN HG3 H 2.396 0.02 2 1216 130 132 GLN CA C 53.480 0.2 1 1217 130 132 GLN CB C 29.031 0.2 1 1218 130 132 GLN CG C 33.529 0.2 1 1219 130 132 GLN N N 121.687 0.2 1 1220 131 133 PRO HA H 4.390 0.02 1 1221 131 133 PRO HB2 H 1.913 0.02 2 1222 131 133 PRO HB3 H 2.249 0.02 2 1223 131 133 PRO C C 176.833 0.2 1 1224 131 133 PRO CA C 62.944 0.2 1 1225 131 133 PRO CB C 32.037 0.2 1 1226 132 134 VAL H H 8.230 0.02 1 1227 132 134 VAL HA H 4.081 0.02 1 1228 132 134 VAL HB H 2.064 0.02 1 1229 132 134 VAL HG1 H 0.952 0.02 1 1230 132 134 VAL HG2 H 0.952 0.02 1 1231 132 134 VAL C C 176.734 0.2 1 1232 132 134 VAL CA C 62.640 0.2 1 1233 132 134 VAL CB C 32.884 0.2 1 1234 132 134 VAL CG1 C 20.990 0.2 1 1235 132 134 VAL CG2 C 20.990 0.2 1 1236 132 134 VAL N N 120.463 0.2 1 stop_ save_