data_17831 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments for oxidised and reduced nDsbD from Escherichia coli ; _BMRB_accession_number 17831 _BMRB_flat_file_name bmr17831.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" 610 "13C chemical shifts" 475 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-10-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17830 'reduced nDsbD' stop_ _Original_release_date 2011-10-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _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-ox _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label nDsbD-ox $nDsbD-ox 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-ox _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common nDsbD-ox _Molecular_mass 15604.5 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'thiol-disulfide oxidoreductase' stop_ _Details 'contains C103-C109 disulfide bond' ############################## # 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 17830 nDsbD-red 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-ox 'E. coli' 562 Bacteria . 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-ox '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-ox . mM 0.5 1.0 '[U-98% 15N]' H2O 95 % . . 'natural abundance' D2O 5 % . . '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-ox . mM 0.5 1.0 '[U-98% 13C; U-98% 15N]' H2O 95 % . . 'natural abundance' D2O 5 % . . '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-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 2 4 LEU H H 8.236 0.02 1 2 2 4 LEU HA H 4.274 0.02 1 3 2 4 LEU HB2 H 1.488 0.02 2 4 2 4 LEU HB3 H 1.413 0.02 2 5 2 4 LEU HG H 1.452 0.02 1 6 2 4 LEU HD1 H 0.810 0.02 2 7 2 4 LEU HD2 H 0.828 0.02 2 8 2 4 LEU C C 177.014 0.2 1 9 2 4 LEU CA C 55.390 0.2 1 10 2 4 LEU CB C 42.266 0.2 1 11 2 4 LEU CG C 27.153 0.2 1 12 2 4 LEU CD1 C 23.674 0.2 2 13 2 4 LEU CD2 C 24.684 0.2 2 14 2 4 LEU N N 124.176 0.2 1 15 3 5 PHE H H 8.089 0.02 1 16 3 5 PHE HA H 4.560 0.02 1 17 3 5 PHE HB2 H 3.142 0.02 2 18 3 5 PHE HB3 H 2.956 0.02 2 19 3 5 PHE C C 175.235 0.2 1 20 3 5 PHE CA C 57.813 0.2 1 21 3 5 PHE CB C 39.584 0.2 1 22 3 5 PHE N N 120.128 0.2 1 23 4 6 ASP H H 8.140 0.02 1 24 4 6 ASP HA H 4.543 0.02 1 25 4 6 ASP HB2 H 2.545 0.02 2 26 4 6 ASP HB3 H 2.572 0.02 2 27 4 6 ASP C C 175.172 0.2 1 28 4 6 ASP CA C 53.869 0.2 1 29 4 6 ASP CB C 41.587 0.2 1 30 4 6 ASP N N 121.390 0.2 1 31 5 7 ALA H H 7.957 0.02 1 32 5 7 ALA HA H 4.513 0.02 1 33 5 7 ALA HB H 1.327 0.02 1 34 5 7 ALA CA C 50.819 0.2 1 35 5 7 ALA CB C 18.080 0.2 1 36 5 7 ALA N N 124.903 0.2 1 37 6 8 PRO HA H 4.391 0.02 1 38 6 8 PRO HB2 H 2.259 0.02 2 39 6 8 PRO HB3 H 1.906 0.02 2 40 6 8 PRO C C 177.842 0.2 1 41 6 8 PRO CA C 63.825 0.2 1 42 6 8 PRO CB C 31.932 0.2 1 43 7 9 GLY H H 8.469 0.02 1 44 7 9 GLY HA2 H 3.931 0.02 1 45 7 9 GLY HA3 H 3.931 0.02 1 46 7 9 GLY C C 174.460 0.2 1 47 7 9 GLY CA C 45.345 0.2 1 48 7 9 GLY N N 109.130 0.2 1 49 8 10 ARG H H 8.035 0.02 1 50 8 10 ARG HA H 4.292 0.02 1 51 8 10 ARG HB2 H 1.857 0.02 2 52 8 10 ARG HB3 H 1.756 0.02 2 53 8 10 ARG HG2 H 1.567 0.02 1 54 8 10 ARG HG3 H 1.567 0.02 1 55 8 10 ARG HD2 H 3.127 0.02 1 56 8 10 ARG HD3 H 3.127 0.02 1 57 8 10 ARG C C 176.513 0.2 1 58 8 10 ARG CA C 56.317 0.2 1 59 8 10 ARG CB C 30.737 0.2 1 60 8 10 ARG CG C 26.990 0.2 1 61 8 10 ARG CD C 43.336 0.2 1 62 8 10 ARG N N 120.311 0.2 1 63 9 11 SER H H 8.262 0.02 1 64 9 11 SER HA H 4.346 0.02 1 65 9 11 SER HB2 H 3.794 0.02 1 66 9 11 SER HB3 H 3.794 0.02 1 67 9 11 SER C C 174.279 0.2 1 68 9 11 SER CA C 58.699 0.2 1 69 9 11 SER CB C 63.690 0.2 1 70 9 11 SER N N 116.336 0.2 1 71 10 12 GLN H H 8.218 0.02 1 72 10 12 GLN HA H 4.187 0.02 1 73 10 12 GLN HB2 H 1.758 0.02 2 74 10 12 GLN HB3 H 1.841 0.02 2 75 10 12 GLN HG2 H 2.040 0.02 2 76 10 12 GLN HG3 H 2.124 0.02 2 77 10 12 GLN C C 175.168 0.2 1 78 10 12 GLN CA C 55.908 0.2 1 79 10 12 GLN CB C 29.354 0.2 1 80 10 12 GLN CG C 33.649 0.2 1 81 10 12 GLN N N 121.278 0.2 1 82 11 13 PHE H H 7.953 0.02 1 83 11 13 PHE HA H 4.638 0.02 1 84 11 13 PHE HB2 H 3.175 0.02 2 85 11 13 PHE HB3 H 2.763 0.02 2 86 11 13 PHE C C 175.349 0.2 1 87 11 13 PHE CA C 57.624 0.2 1 88 11 13 PHE CB C 39.555 0.2 1 89 11 13 PHE N N 121.433 0.2 1 90 12 14 VAL H H 7.691 0.02 1 91 12 14 VAL HA H 4.409 0.02 1 92 12 14 VAL HB H 2.055 0.02 1 93 12 14 VAL HG1 H 0.921 0.02 2 94 12 14 VAL HG2 H 0.948 0.02 2 95 12 14 VAL C C 173.459 0.2 1 96 12 14 VAL CA C 59.502 0.2 1 97 12 14 VAL CB C 32.858 0.2 1 98 12 14 VAL CG1 C 20.337 0.2 2 99 12 14 VAL CG2 C 21.010 0.2 2 100 12 14 VAL N N 120.895 0.2 1 101 13 15 PRO HA H 4.547 0.02 1 102 13 15 PRO HB2 H 1.898 0.02 2 103 13 15 PRO HB3 H 2.507 0.02 2 104 13 15 PRO C C 177.382 0.2 1 105 13 15 PRO CA C 63.129 0.2 1 106 13 15 PRO CB C 32.550 0.2 1 107 14 16 ALA H H 9.227 0.02 1 108 14 16 ALA HA H 3.331 0.02 1 109 14 16 ALA HB H 1.409 0.02 1 110 14 16 ALA C C 178.440 0.2 1 111 14 16 ALA CA C 55.928 0.2 1 112 14 16 ALA CB C 18.185 0.2 1 113 14 16 ALA N N 126.708 0.2 1 114 15 17 ASP H H 8.450 0.02 1 115 15 17 ASP HA H 4.447 0.02 1 116 15 17 ASP HB2 H 2.604 0.02 2 117 15 17 ASP HB3 H 2.766 0.02 2 118 15 17 ASP C C 176.599 0.2 1 119 15 17 ASP CA C 56.386 0.2 1 120 15 17 ASP CB C 40.264 0.2 1 121 15 17 ASP N N 112.545 0.2 1 122 16 18 GLN H H 7.447 0.02 1 123 16 18 GLN HA H 4.154 0.02 1 124 16 18 GLN HB2 H 1.754 0.02 2 125 16 18 GLN HB3 H 1.901 0.02 2 126 16 18 GLN HG2 H 2.234 0.02 2 127 16 18 GLN HG3 H 2.309 0.02 2 128 16 18 GLN C C 176.326 0.2 1 129 16 18 GLN CA C 56.392 0.2 1 130 16 18 GLN CB C 29.400 0.2 1 131 16 18 GLN CG C 33.990 0.2 1 132 16 18 GLN N N 115.386 0.2 1 133 17 19 ALA H H 7.199 0.02 1 134 17 19 ALA HA H 3.079 0.02 1 135 17 19 ALA HB H -0.326 0.02 1 136 17 19 ALA C C 175.480 0.2 1 137 17 19 ALA CA C 54.002 0.2 1 138 17 19 ALA CB C 17.158 0.2 1 139 17 19 ALA N N 123.409 0.2 1 140 18 20 PHE H H 7.857 0.02 1 141 18 20 PHE HA H 4.929 0.02 1 142 18 20 PHE HB2 H 2.713 0.02 2 143 18 20 PHE HB3 H 3.396 0.02 2 144 18 20 PHE C C 173.305 0.2 1 145 18 20 PHE CA C 53.285 0.2 1 146 18 20 PHE CB C 39.220 0.2 1 147 18 20 PHE N N 114.612 0.2 1 148 19 21 ALA H H 8.147 0.02 1 149 19 21 ALA HA H 4.643 0.02 1 150 19 21 ALA HB H 1.362 0.02 1 151 19 21 ALA C C 176.407 0.2 1 152 19 21 ALA CA C 52.243 0.2 1 153 19 21 ALA CB C 18.968 0.2 1 154 19 21 ALA N N 126.059 0.2 1 155 20 22 PHE H H 8.705 0.02 1 156 20 22 PHE HA H 4.964 0.02 1 157 20 22 PHE HB2 H 2.640 0.02 2 158 20 22 PHE HB3 H 2.755 0.02 2 159 20 22 PHE C C 174.090 0.2 1 160 20 22 PHE CA C 56.604 0.2 1 161 20 22 PHE CB C 42.173 0.2 1 162 20 22 PHE N N 128.991 0.2 1 163 21 23 ASP H H 8.340 0.02 1 164 21 23 ASP HA H 4.235 0.02 1 165 21 23 ASP HB2 H 2.116 0.02 2 166 21 23 ASP HB3 H 2.268 0.02 2 167 21 23 ASP C C 171.316 0.2 1 168 21 23 ASP CA C 52.537 0.2 1 169 21 23 ASP CB C 44.688 0.2 1 170 21 23 ASP N N 128.388 0.2 1 171 22 24 PHE H H 7.593 0.02 1 172 22 24 PHE HA H 5.293 0.02 1 173 22 24 PHE HB2 H 2.562 0.02 1 174 22 24 PHE HB3 H 2.562 0.02 1 175 22 24 PHE C C 173.586 0.2 1 176 22 24 PHE CA C 55.105 0.2 1 177 22 24 PHE CB C 42.804 0.2 1 178 22 24 PHE N N 112.739 0.2 1 179 23 25 GLN H H 8.059 0.02 1 180 23 25 GLN HA H 4.334 0.02 1 181 23 25 GLN HB2 H 1.889 0.02 1 182 23 25 GLN HB3 H 1.889 0.02 1 183 23 25 GLN HG2 H 2.172 0.02 2 184 23 25 GLN HG3 H 2.086 0.02 2 185 23 25 GLN C C 173.922 0.2 1 186 23 25 GLN CA C 55.689 0.2 1 187 23 25 GLN CB C 32.305 0.2 1 188 23 25 GLN CG C 33.315 0.2 1 189 23 25 GLN N N 116.827 0.2 1 190 24 26 GLN H H 9.378 0.02 1 191 24 26 GLN HA H 5.006 0.02 1 192 24 26 GLN HB2 H 1.837 0.02 2 193 24 26 GLN HB3 H 2.078 0.02 2 194 24 26 GLN HG2 H 2.375 0.02 2 195 24 26 GLN HG3 H 2.115 0.02 2 196 24 26 GLN C C 174.265 0.2 1 197 24 26 GLN CA C 54.342 0.2 1 198 24 26 GLN CB C 30.712 0.2 1 199 24 26 GLN CG C 32.784 0.2 1 200 24 26 GLN N N 128.881 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 2.869 0.02 2 204 25 27 ASN HB3 H 2.631 0.02 2 205 25 27 ASN C C 174.356 0.2 1 206 25 27 ASN CA C 52.522 0.2 1 207 25 27 ASN CB C 39.326 0.2 1 208 25 27 ASN N N 126.141 0.2 1 209 26 28 GLN H H 9.410 0.02 1 210 26 28 GLN HA H 3.603 0.02 1 211 26 28 GLN HB2 H 2.466 0.02 2 212 26 28 GLN HB3 H 2.086 0.02 2 213 26 28 GLN HG2 H 2.313 0.02 2 214 26 28 GLN HG3 H 2.436 0.02 2 215 26 28 GLN C C 174.479 0.2 1 216 26 28 GLN CA C 58.453 0.2 1 217 26 28 GLN CB C 26.593 0.2 1 218 26 28 GLN CG C 34.081 0.2 1 219 26 28 GLN N N 122.178 0.2 1 220 27 29 HIS H H 8.209 0.02 1 221 27 29 HIS HA H 4.493 0.02 1 222 27 29 HIS HB2 H 3.385 0.02 1 223 27 29 HIS HB3 H 3.385 0.02 1 224 27 29 HIS C C 173.691 0.2 1 225 27 29 HIS CA C 57.798 0.2 1 226 27 29 HIS CB C 29.145 0.2 1 227 27 29 HIS N N 117.893 0.2 1 228 28 30 ASP H H 7.997 0.02 1 229 28 30 ASP HA H 4.999 0.02 1 230 28 30 ASP HB2 H 2.662 0.02 1 231 28 30 ASP HB3 H 2.662 0.02 1 232 28 30 ASP C C 173.831 0.2 1 233 28 30 ASP CA C 54.394 0.2 1 234 28 30 ASP CB C 42.294 0.2 1 235 28 30 ASP N N 118.632 0.2 1 236 29 31 LEU H H 8.726 0.02 1 237 29 31 LEU HA H 5.080 0.02 1 238 29 31 LEU HB2 H 1.932 0.02 2 239 29 31 LEU HB3 H 1.129 0.02 2 240 29 31 LEU HG H 1.292 0.02 1 241 29 31 LEU HD1 H 0.660 0.02 2 242 29 31 LEU HD2 H 0.742 0.02 2 243 29 31 LEU C C 173.752 0.2 1 244 29 31 LEU CA C 53.165 0.2 1 245 29 31 LEU CB C 44.832 0.2 1 246 29 31 LEU CG C 27.378 0.2 1 247 29 31 LEU CD1 C 27.715 0.2 2 248 29 31 LEU CD2 C 24.347 0.2 2 249 29 31 LEU N N 126.747 0.2 1 250 30 32 ASN H H 8.781 0.02 1 251 30 32 ASN HA H 5.314 0.02 1 252 30 32 ASN HB2 H 2.534 0.02 2 253 30 32 ASN HB3 H 2.303 0.02 2 254 30 32 ASN C C 174.294 0.2 1 255 30 32 ASN CA C 52.467 0.2 1 256 30 32 ASN CB C 41.323 0.2 1 257 30 32 ASN N N 124.808 0.2 1 258 31 33 LEU H H 8.346 0.02 1 259 31 33 LEU HA H 4.561 0.02 1 260 31 33 LEU HB2 H 1.068 0.02 2 261 31 33 LEU HB3 H 2.170 0.02 2 262 31 33 LEU HG H 1.699 0.02 1 263 31 33 LEU HD1 H 0.839 0.02 2 264 31 33 LEU HD2 H 0.939 0.02 2 265 31 33 LEU C C 175.007 0.2 1 266 31 33 LEU CA C 53.190 0.2 1 267 31 33 LEU CB C 43.140 0.2 1 268 31 33 LEU CG C 26.705 0.2 1 269 31 33 LEU CD1 C 24.010 0.2 2 270 31 33 LEU CD2 C 27.042 0.2 2 271 31 33 LEU N N 125.200 0.2 1 272 32 34 THR H H 8.325 0.02 1 273 32 34 THR HA H 5.469 0.02 1 274 32 34 THR HB H 3.700 0.02 1 275 32 34 THR HG2 H 0.933 0.02 1 276 32 34 THR C C 172.040 0.2 1 277 32 34 THR CA C 60.367 0.2 1 278 32 34 THR CB C 71.968 0.2 1 279 32 34 THR CG2 C 24.674 0.2 1 280 32 34 THR N N 115.837 0.2 1 281 33 35 TRP H H 9.368 0.02 1 282 33 35 TRP HA H 5.395 0.02 1 283 33 35 TRP HB2 H 2.456 0.02 2 284 33 35 TRP HB3 H 2.951 0.02 2 285 33 35 TRP HE1 H 5.661 0.02 1 286 33 35 TRP C C 175.739 0.2 1 287 33 35 TRP CA C 57.512 0.2 1 288 33 35 TRP CB C 34.024 0.2 1 289 33 35 TRP N N 122.333 0.2 1 290 33 35 TRP NE1 N 121.647 0.2 1 291 34 36 GLN H H 8.830 0.02 1 292 34 36 GLN HA H 4.640 0.02 1 293 34 36 GLN HB2 H 1.946 0.02 2 294 34 36 GLN HB3 H 2.112 0.02 2 295 34 36 GLN HG2 H 2.272 0.02 1 296 34 36 GLN HG3 H 2.272 0.02 1 297 34 36 GLN C C 175.440 0.2 1 298 34 36 GLN CA C 55.157 0.2 1 299 34 36 GLN CB C 29.209 0.2 1 300 34 36 GLN CG C 33.251 0.2 1 301 34 36 GLN N N 122.652 0.2 1 302 35 37 ILE H H 8.485 0.02 1 303 35 37 ILE HA H 4.661 0.02 1 304 35 37 ILE HB H 1.807 0.02 1 305 35 37 ILE HG12 H 0.684 0.02 2 306 35 37 ILE HG13 H 1.520 0.02 2 307 35 37 ILE HG2 H 1.103 0.02 1 308 35 37 ILE HD1 H 0.544 0.02 1 309 35 37 ILE C C 175.064 0.2 1 310 35 37 ILE CA C 61.046 0.2 1 311 35 37 ILE CB C 38.598 0.2 1 312 35 37 ILE CG1 C 27.979 0.2 1 313 35 37 ILE CG2 C 18.839 0.2 1 314 35 37 ILE CD1 C 14.028 0.2 1 315 35 37 ILE N N 130.017 0.2 1 316 36 38 LYS H H 8.662 0.02 1 317 36 38 LYS HA H 4.059 0.02 1 318 36 38 LYS HB2 H 1.472 0.02 2 319 36 38 LYS HB3 H 1.639 0.02 2 320 36 38 LYS HG2 H 1.622 0.02 2 321 36 38 LYS HG3 H 1.764 0.02 2 322 36 38 LYS HD2 H 1.368 0.02 2 323 36 38 LYS HD3 H 1.368 0.02 2 324 36 38 LYS HE2 H 3.027 0.02 2 325 36 38 LYS HE3 H 3.046 0.02 2 326 36 38 LYS C C 175.420 0.2 1 327 36 38 LYS CA C 57.452 0.2 1 328 36 38 LYS CB C 33.566 0.2 1 329 36 38 LYS CG C 24.674 0.2 1 330 36 38 LYS CD C 29.389 0.2 1 331 36 38 LYS CE C 41.830 0.2 1 332 36 38 LYS N N 131.135 0.2 1 333 37 39 ASP H H 8.450 0.02 1 334 37 39 ASP HA H 4.635 0.02 1 335 37 39 ASP HB2 H 2.783 0.02 2 336 37 39 ASP HB3 H 2.728 0.02 2 337 37 39 ASP C C 177.466 0.2 1 338 37 39 ASP CA C 56.646 0.2 1 339 37 39 ASP CB C 41.298 0.2 1 340 37 39 ASP N N 124.591 0.2 1 341 38 40 GLY H H 9.183 0.02 1 342 38 40 GLY HA2 H 4.225 0.02 2 343 38 40 GLY HA3 H 3.875 0.02 2 344 38 40 GLY C C 173.908 0.2 1 345 38 40 GLY CA C 44.952 0.2 1 346 38 40 GLY N N 112.948 0.2 1 347 39 41 TYR H H 8.234 0.02 1 348 39 41 TYR HA H 5.214 0.02 1 349 39 41 TYR HB2 H 3.002 0.02 2 350 39 41 TYR HB3 H 2.848 0.02 2 351 39 41 TYR C C 173.851 0.2 1 352 39 41 TYR CA C 56.804 0.2 1 353 39 41 TYR CB C 40.409 0.2 1 354 39 41 TYR N N 120.577 0.2 1 355 40 42 TYR H H 8.657 0.02 1 356 40 42 TYR HA H 5.382 0.02 1 357 40 42 TYR HB2 H 2.619 0.02 2 358 40 42 TYR HB3 H 2.741 0.02 2 359 40 42 TYR C C 173.424 0.2 1 360 40 42 TYR CA C 56.243 0.2 1 361 40 42 TYR CB C 41.661 0.2 1 362 40 42 TYR N N 113.026 0.2 1 363 41 43 LEU H H 8.483 0.02 1 364 41 43 LEU HA H 4.623 0.02 1 365 41 43 LEU HB2 H 1.196 0.02 2 366 41 43 LEU HB3 H 1.391 0.02 2 367 41 43 LEU HG H 1.212 0.02 1 368 41 43 LEU HD1 H -0.209 0.02 2 369 41 43 LEU HD2 H -0.157 0.02 2 370 41 43 LEU C C 177.781 0.2 1 371 41 43 LEU CA C 52.636 0.2 1 372 41 43 LEU CB C 46.745 0.2 1 373 41 43 LEU CG C 26.347 0.2 1 374 41 43 LEU CD1 C 24.497 0.2 2 375 41 43 LEU CD2 C 23.421 0.2 2 376 41 43 LEU N N 116.234 0.2 1 377 42 44 TYR H H 7.666 0.02 1 378 42 44 TYR HA H 4.675 0.02 1 379 42 44 TYR HB2 H 2.540 0.02 2 380 42 44 TYR HB3 H 3.082 0.02 2 381 42 44 TYR C C 176.864 0.2 1 382 42 44 TYR CA C 58.081 0.2 1 383 42 44 TYR CB C 39.895 0.2 1 384 42 44 TYR N N 116.762 0.2 1 385 43 45 ARG H H 8.243 0.02 1 386 43 45 ARG HA H 3.917 0.02 1 387 43 45 ARG HB2 H 1.342 0.02 2 388 43 45 ARG HB3 H 0.657 0.02 2 389 43 45 ARG HD2 H 2.804 0.02 2 390 43 45 ARG HD3 H 2.658 0.02 2 391 43 45 ARG C C 177.621 0.2 1 392 43 45 ARG CA C 60.182 0.2 1 393 43 45 ARG CB C 30.625 0.2 1 394 43 45 ARG CD C 43.763 0.2 1 395 43 45 ARG N N 127.112 0.2 1 396 44 46 LYS H H 9.110 0.02 1 397 44 46 LYS HA H 4.116 0.02 1 398 44 46 LYS HB2 H 1.776 0.02 2 399 44 46 LYS HB3 H 1.773 0.02 2 400 44 46 LYS HG2 H 1.359 0.02 2 401 44 46 LYS HG3 H 1.369 0.02 2 402 44 46 LYS HD2 H 1.579 0.02 1 403 44 46 LYS HD3 H 1.579 0.02 1 404 44 46 LYS HE2 H 2.790 0.02 2 405 44 46 LYS HE3 H 2.796 0.02 2 406 44 46 LYS C C 176.300 0.2 1 407 44 46 LYS CA C 57.824 0.2 1 408 44 46 LYS CB C 31.983 0.2 1 409 44 46 LYS CG C 25.174 0.2 1 410 44 46 LYS CD C 28.878 0.2 1 411 44 46 LYS CE C 41.857 0.2 1 412 44 46 LYS N N 113.180 0.2 1 413 45 47 GLN H H 6.605 0.02 1 414 45 47 GLN HA H 4.525 0.02 1 415 45 47 GLN HB2 H 1.956 0.02 2 416 45 47 GLN HB3 H 2.507 0.02 2 417 45 47 GLN C C 174.943 0.2 1 418 45 47 GLN CA C 54.087 0.2 1 419 45 47 GLN CB C 29.549 0.2 1 420 45 47 GLN N N 112.785 0.2 1 421 46 48 ILE H H 6.865 0.02 1 422 46 48 ILE HA H 4.852 0.02 1 423 46 48 ILE HB H 1.815 0.02 1 424 46 48 ILE HG12 H 0.794 0.02 2 425 46 48 ILE HG13 H 1.798 0.02 2 426 46 48 ILE HG2 H 0.781 0.02 1 427 46 48 ILE HD1 H 0.461 0.02 1 428 46 48 ILE C C 176.040 0.2 1 429 46 48 ILE CA C 61.841 0.2 1 430 46 48 ILE CB C 37.687 0.2 1 431 46 48 ILE CG1 C 28.010 0.2 1 432 46 48 ILE CG2 C 16.705 0.2 1 433 46 48 ILE CD1 C 13.680 0.2 1 434 46 48 ILE N N 119.118 0.2 1 435 47 49 ARG H H 8.868 0.02 1 436 47 49 ARG HA H 4.677 0.02 1 437 47 49 ARG HB2 H 1.634 0.02 2 438 47 49 ARG HB3 H 1.734 0.02 2 439 47 49 ARG HG2 H 1.499 0.02 2 440 47 49 ARG HG3 H 1.525 0.02 2 441 47 49 ARG HD2 H 3.120 0.02 2 442 47 49 ARG HD3 H 3.187 0.02 2 443 47 49 ARG C C 174.557 0.2 1 444 47 49 ARG CA C 55.201 0.2 1 445 47 49 ARG CB C 33.610 0.2 1 446 47 49 ARG CG C 26.847 0.2 1 447 47 49 ARG CD C 43.347 0.2 1 448 47 49 ARG N N 129.557 0.2 1 449 48 50 ILE H H 8.772 0.02 1 450 48 50 ILE HA H 4.923 0.02 1 451 48 50 ILE HB H 1.786 0.02 1 452 48 50 ILE HG12 H 1.059 0.02 2 453 48 50 ILE HG13 H 1.565 0.02 2 454 48 50 ILE HG2 H 0.760 0.02 1 455 48 50 ILE HD1 H 0.862 0.02 1 456 48 50 ILE C C 175.317 0.2 1 457 48 50 ILE CA C 60.493 0.2 1 458 48 50 ILE CB C 40.676 0.2 1 459 48 50 ILE CG1 C 28.010 0.2 1 460 48 50 ILE CG2 C 19.010 0.2 1 461 48 50 ILE CD1 C 14.681 0.2 1 462 48 50 ILE N N 124.911 0.2 1 463 49 51 THR H H 9.030 0.02 1 464 49 51 THR HA H 5.009 0.02 1 465 49 51 THR HB H 3.997 0.02 1 466 49 51 THR HG2 H 1.215 0.02 1 467 49 51 THR C C 173.229 0.2 1 468 49 51 THR CA C 59.139 0.2 1 469 49 51 THR CB C 71.594 0.2 1 470 49 51 THR CG2 C 21.511 0.2 1 471 49 51 THR N N 122.373 0.2 1 472 50 52 PRO HA H 5.122 0.02 1 473 50 52 PRO HB2 H 1.736 0.02 2 474 50 52 PRO HB3 H 2.088 0.02 2 475 50 52 PRO C C 175.275 0.2 1 476 50 52 PRO CA C 62.056 0.2 1 477 50 52 PRO CB C 33.477 0.2 1 478 51 53 GLU H H 8.797 0.02 1 479 51 53 GLU HA H 4.427 0.02 1 480 51 53 GLU HB2 H 1.812 0.02 1 481 51 53 GLU HB3 H 1.812 0.02 1 482 51 53 GLU HG2 H 1.866 0.02 2 483 51 53 GLU HG3 H 1.789 0.02 2 484 51 53 GLU C C 174.817 0.2 1 485 51 53 GLU CA C 56.525 0.2 1 486 51 53 GLU CB C 31.620 0.2 1 487 51 53 GLU CG C 36.184 0.2 1 488 51 53 GLU N N 120.918 0.2 1 489 52 54 HIS H H 8.879 0.02 1 490 52 54 HIS HA H 4.170 0.02 1 491 52 54 HIS HB2 H 3.333 0.02 2 492 52 54 HIS HB3 H 3.324 0.02 2 493 52 54 HIS C C 171.982 0.2 1 494 52 54 HIS CA C 56.776 0.2 1 495 52 54 HIS CB C 26.469 0.2 1 496 52 54 HIS N N 118.018 0.2 1 497 53 55 ALA H H 7.268 0.02 1 498 53 55 ALA HA H 4.910 0.02 1 499 53 55 ALA HB H 1.202 0.02 1 500 53 55 ALA C C 174.966 0.2 1 501 53 55 ALA CA C 50.678 0.2 1 502 53 55 ALA CB C 22.970 0.2 1 503 53 55 ALA N N 114.482 0.2 1 504 54 56 LYS H H 8.863 0.02 1 505 54 56 LYS HA H 4.755 0.02 1 506 54 56 LYS HB2 H 1.639 0.02 2 507 54 56 LYS HB3 H 1.903 0.02 2 508 54 56 LYS HG2 H 1.372 0.02 2 509 54 56 LYS HG3 H 1.451 0.02 2 510 54 56 LYS HD2 H 1.610 0.02 2 511 54 56 LYS HD3 H 1.682 0.02 2 512 54 56 LYS HE2 H 2.932 0.02 2 513 54 56 LYS HE3 H 2.932 0.02 2 514 54 56 LYS C C 175.801 0.2 1 515 54 56 LYS CA C 54.939 0.2 1 516 54 56 LYS CB C 35.265 0.2 1 517 54 56 LYS CG C 24.291 0.2 1 518 54 56 LYS CD C 29.010 0.2 1 519 54 56 LYS CE C 42.256 0.2 1 520 54 56 LYS N N 119.737 0.2 1 521 55 57 ILE H H 8.785 0.02 1 522 55 57 ILE HA H 5.208 0.02 1 523 55 57 ILE HB H 2.017 0.02 1 524 55 57 ILE HG12 H 1.534 0.02 2 525 55 57 ILE HG13 H 0.890 0.02 2 526 55 57 ILE HG2 H 0.688 0.02 1 527 55 57 ILE HD1 H 0.733 0.02 1 528 55 57 ILE C C 175.307 0.2 1 529 55 57 ILE CA C 58.571 0.2 1 530 55 57 ILE CB C 40.948 0.2 1 531 55 57 ILE CG1 C 25.420 0.2 1 532 55 57 ILE CG2 C 18.010 0.2 1 533 55 57 ILE CD1 C 13.997 0.2 1 534 55 57 ILE N N 117.825 0.2 1 535 56 58 ALA H H 8.235 0.02 1 536 56 58 ALA HA H 4.436 0.02 1 537 56 58 ALA HB H 1.532 0.02 1 538 56 58 ALA C C 177.580 0.2 1 539 56 58 ALA CA C 51.185 0.2 1 540 56 58 ALA CB C 19.526 0.2 1 541 56 58 ALA N N 125.369 0.2 1 542 57 59 ASP H H 8.357 0.02 1 543 57 59 ASP HA H 4.404 0.02 1 544 57 59 ASP HB2 H 2.604 0.02 2 545 57 59 ASP HB3 H 2.545 0.02 2 546 57 59 ASP C C 176.630 0.2 1 547 57 59 ASP CA C 55.665 0.2 1 548 57 59 ASP CB C 40.591 0.2 1 549 57 59 ASP N N 120.237 0.2 1 550 58 60 VAL H H 8.361 0.02 1 551 58 60 VAL HA H 4.065 0.02 1 552 58 60 VAL HB H 2.052 0.02 1 553 58 60 VAL HG1 H 0.956 0.02 2 554 58 60 VAL HG2 H 1.115 0.02 2 555 58 60 VAL C C 176.012 0.2 1 556 58 60 VAL CA C 62.856 0.2 1 557 58 60 VAL CB C 32.810 0.2 1 558 58 60 VAL CG1 C 21.010 0.2 2 559 58 60 VAL CG2 C 22.021 0.2 2 560 58 60 VAL N N 124.820 0.2 1 561 59 61 GLN H H 8.703 0.02 1 562 59 61 GLN HA H 4.524 0.02 1 563 59 61 GLN HB2 H 1.956 0.02 2 564 59 61 GLN HB3 H 1.978 0.02 2 565 59 61 GLN HG2 H 2.290 0.02 1 566 59 61 GLN HG3 H 2.290 0.02 1 567 59 61 GLN C C 174.849 0.2 1 568 59 61 GLN CA C 53.870 0.2 1 569 59 61 GLN CB C 28.882 0.2 1 570 59 61 GLN CG C 33.442 0.2 1 571 59 61 GLN N N 128.224 0.2 1 572 60 62 LEU H H 8.610 0.02 1 573 60 62 LEU HA H 4.512 0.02 1 574 60 62 LEU HB2 H 1.757 0.02 2 575 60 62 LEU HB3 H 1.587 0.02 2 576 60 62 LEU HG H 1.681 0.02 1 577 60 62 LEU HD1 H 1.000 0.02 2 578 60 62 LEU HD2 H 0.907 0.02 2 579 60 62 LEU C C 175.848 0.2 1 580 60 62 LEU CA C 52.859 0.2 1 581 60 62 LEU CB C 40.009 0.2 1 582 60 62 LEU CG C 28.042 0.2 1 583 60 62 LEU CD1 C 26.358 0.2 2 584 60 62 LEU CD2 C 25.010 0.2 2 585 60 62 LEU N N 127.363 0.2 1 586 61 63 PRO HA H 4.641 0.02 1 587 61 63 PRO HB2 H 2.112 0.02 2 588 61 63 PRO HB3 H 2.422 0.02 2 589 61 63 PRO C C 177.272 0.2 1 590 61 63 PRO CA C 62.127 0.2 1 591 61 63 PRO CB C 32.628 0.2 1 592 62 64 GLN H H 8.980 0.02 1 593 62 64 GLN HA H 4.116 0.02 1 594 62 64 GLN HB2 H 2.149 0.02 1 595 62 64 GLN HB3 H 2.149 0.02 1 596 62 64 GLN HG2 H 2.564 0.02 2 597 62 64 GLN HG3 H 2.588 0.02 2 598 62 64 GLN C C 176.989 0.2 1 599 62 64 GLN CA C 57.546 0.2 1 600 62 64 GLN CB C 29.354 0.2 1 601 62 64 GLN CG C 34.003 0.2 1 602 62 64 GLN N N 123.192 0.2 1 603 63 65 GLY H H 9.595 0.02 1 604 63 65 GLY HA2 H 3.143 0.02 2 605 63 65 GLY HA3 H 4.667 0.02 2 606 63 65 GLY C C 173.256 0.2 1 607 63 65 GLY CA C 44.008 0.2 1 608 63 65 GLY N N 115.580 0.2 1 609 64 66 VAL H H 8.706 0.02 1 610 64 66 VAL HA H 4.502 0.02 1 611 64 66 VAL HB H 2.106 0.02 1 612 64 66 VAL HG1 H 0.991 0.02 2 613 64 66 VAL HG2 H 0.825 0.02 2 614 64 66 VAL C C 175.124 0.2 1 615 64 66 VAL CA C 59.994 0.2 1 616 64 66 VAL CB C 34.264 0.2 1 617 64 66 VAL CG1 C 21.531 0.2 2 618 64 66 VAL CG2 C 19.510 0.2 2 619 64 66 VAL N N 117.637 0.2 1 620 65 67 TRP H H 8.622 0.02 1 621 65 67 TRP HA H 4.843 0.02 1 622 65 67 TRP HB2 H 3.069 0.02 2 623 65 67 TRP HB3 H 3.039 0.02 2 624 65 67 TRP HE1 H 10.034 0.02 1 625 65 67 TRP C C 176.449 0.2 1 626 65 67 TRP CA C 58.225 0.2 1 627 65 67 TRP CB C 30.090 0.2 1 628 65 67 TRP N N 122.710 0.2 1 629 65 67 TRP NE1 N 128.942 0.2 1 630 66 68 HIS H H 9.212 0.02 1 631 66 68 HIS C C 172.920 0.2 1 632 66 68 HIS CA C 55.084 0.2 1 633 66 68 HIS N N 124.593 0.2 1 634 67 69 GLU HA H 4.796 0.02 1 635 67 69 GLU HB2 H 1.675 0.02 2 636 67 69 GLU HB3 H 1.794 0.02 2 637 67 69 GLU HG2 H 1.967 0.02 1 638 67 69 GLU HG3 H 1.967 0.02 1 639 67 69 GLU C C 174.065 0.2 1 640 67 69 GLU CA C 55.490 0.2 1 641 67 69 GLU CB C 31.528 0.2 1 642 67 69 GLU CG C 36.298 0.2 1 643 68 70 ASP H H 8.019 0.02 1 644 68 70 ASP HA H 4.721 0.02 1 645 68 70 ASP HB2 H 2.851 0.02 2 646 68 70 ASP HB3 H 3.093 0.02 2 647 68 70 ASP C C 176.425 0.2 1 648 68 70 ASP CA C 53.089 0.2 1 649 68 70 ASP CB C 44.538 0.2 1 650 68 70 ASP N N 121.454 0.2 1 651 69 71 GLU H H 8.811 0.02 1 652 69 71 GLU HA H 4.079 0.02 1 653 69 71 GLU HB2 H 1.755 0.02 2 654 69 71 GLU HB3 H 1.766 0.02 2 655 69 71 GLU HG2 H 1.776 0.02 2 656 69 71 GLU HG3 H 1.882 0.02 2 657 69 71 GLU C C 175.857 0.2 1 658 69 71 GLU CA C 57.660 0.2 1 659 69 71 GLU CB C 29.422 0.2 1 660 69 71 GLU CG C 35.821 0.2 1 661 69 71 GLU N N 119.166 0.2 1 662 70 72 PHE H H 8.434 0.02 1 663 70 72 PHE HA H 4.346 0.02 1 664 70 72 PHE HB2 H 2.888 0.02 2 665 70 72 PHE HB3 H 2.873 0.02 2 666 70 72 PHE C C 176.979 0.2 1 667 70 72 PHE CA C 59.556 0.2 1 668 70 72 PHE CB C 39.877 0.2 1 669 70 72 PHE N N 121.090 0.2 1 670 71 73 TYR H H 8.835 0.02 1 671 71 73 TYR HA H 4.576 0.02 1 672 71 73 TYR HB2 H 2.680 0.02 2 673 71 73 TYR HB3 H 3.144 0.02 2 674 71 73 TYR C C 176.394 0.2 1 675 71 73 TYR CA C 57.784 0.2 1 676 71 73 TYR CB C 39.494 0.2 1 677 71 73 TYR N N 116.401 0.2 1 678 72 74 GLY H H 7.707 0.02 1 679 72 74 GLY HA2 H 3.978 0.02 2 680 72 74 GLY HA3 H 4.196 0.02 2 681 72 74 GLY C C 174.756 0.2 1 682 72 74 GLY CA C 45.529 0.2 1 683 72 74 GLY N N 109.794 0.2 1 684 73 75 LYS H H 8.738 0.02 1 685 73 75 LYS HA H 5.037 0.02 1 686 73 75 LYS HB2 H 1.781 0.02 2 687 73 75 LYS HB3 H 1.868 0.02 2 688 73 75 LYS HG2 H 1.400 0.02 2 689 73 75 LYS HG3 H 1.323 0.02 2 690 73 75 LYS HD2 H 1.453 0.02 1 691 73 75 LYS HD3 H 1.453 0.02 1 692 73 75 LYS HE2 H 2.525 0.02 2 693 73 75 LYS HE3 H 2.625 0.02 2 694 73 75 LYS C C 176.720 0.2 1 695 73 75 LYS CA C 56.820 0.2 1 696 73 75 LYS CB C 33.047 0.2 1 697 73 75 LYS CG C 25.347 0.2 1 698 73 75 LYS CD C 29.343 0.2 1 699 73 75 LYS CE C 41.800 0.2 1 700 73 75 LYS N N 126.972 0.2 1 701 74 76 SER H H 9.294 0.02 1 702 74 76 SER HA H 4.903 0.02 1 703 74 76 SER HB2 H 3.796 0.02 2 704 74 76 SER HB3 H 3.880 0.02 2 705 74 76 SER C C 171.364 0.2 1 706 74 76 SER CA C 58.446 0.2 1 707 74 76 SER CB C 66.978 0.2 1 708 74 76 SER N N 121.508 0.2 1 709 75 77 GLU H H 8.277 0.02 1 710 75 77 GLU HA H 3.951 0.02 1 711 75 77 GLU HB2 H 0.834 0.02 2 712 75 77 GLU HB3 H 1.164 0.02 2 713 75 77 GLU HG2 H 0.863 0.02 1 714 75 77 GLU HG3 H 0.863 0.02 1 715 75 77 GLU C C 176.918 0.2 1 716 75 77 GLU CA C 55.297 0.2 1 717 75 77 GLU CB C 30.848 0.2 1 718 75 77 GLU CG C 36.150 0.2 1 719 75 77 GLU N N 124.161 0.2 1 720 76 78 ILE H H 9.331 0.02 1 721 76 78 ILE HA H 5.055 0.02 1 722 76 78 ILE HB H 1.530 0.02 1 723 76 78 ILE HG12 H 0.970 0.02 2 724 76 78 ILE HG13 H 0.655 0.02 2 725 76 78 ILE HG2 H 0.423 0.02 1 726 76 78 ILE HD1 H -0.173 0.02 1 727 76 78 ILE C C 173.511 0.2 1 728 76 78 ILE CA C 59.347 0.2 1 729 76 78 ILE CB C 42.859 0.2 1 730 76 78 ILE CG1 C 25.784 0.2 1 731 76 78 ILE CG2 C 18.780 0.2 1 732 76 78 ILE CD1 C 13.476 0.2 1 733 76 78 ILE N N 121.887 0.2 1 734 77 79 TYR H H 8.736 0.02 1 735 77 79 TYR HA H 5.276 0.02 1 736 77 79 TYR HB2 H 2.216 0.02 2 737 77 79 TYR HB3 H 2.976 0.02 2 738 77 79 TYR C C 175.079 0.2 1 739 77 79 TYR CA C 55.670 0.2 1 740 77 79 TYR CB C 41.606 0.2 1 741 77 79 TYR N N 116.283 0.2 1 742 78 80 ARG H H 8.358 0.02 1 743 78 80 ARG HA H 4.630 0.02 1 744 78 80 ARG HB2 H 1.609 0.02 2 745 78 80 ARG HB3 H 1.966 0.02 2 746 78 80 ARG HD2 H 3.090 0.02 1 747 78 80 ARG HD3 H 3.090 0.02 1 748 78 80 ARG C C 176.088 0.2 1 749 78 80 ARG CA C 54.618 0.2 1 750 78 80 ARG CB C 34.343 0.2 1 751 78 80 ARG N N 118.543 0.2 1 752 79 81 ASP H H 9.009 0.02 1 753 79 81 ASP HA H 4.391 0.02 1 754 79 81 ASP HB2 H 2.928 0.02 2 755 79 81 ASP HB3 H 3.089 0.02 2 756 79 81 ASP C C 174.720 0.2 1 757 79 81 ASP CA C 59.065 0.2 1 758 79 81 ASP CB C 40.403 0.2 1 759 79 81 ASP N N 115.480 0.2 1 760 80 82 ARG H H 8.998 0.02 1 761 80 82 ARG HA H 5.040 0.02 1 762 80 82 ARG HB2 H 1.838 0.02 1 763 80 82 ARG HB3 H 1.838 0.02 1 764 80 82 ARG HG2 H 1.473 0.02 2 765 80 82 ARG HG3 H 1.508 0.02 2 766 80 82 ARG HD2 H 3.147 0.02 2 767 80 82 ARG HD3 H 3.137 0.02 2 768 80 82 ARG C C 174.057 0.2 1 769 80 82 ARG CA C 55.523 0.2 1 770 80 82 ARG CB C 32.628 0.2 1 771 80 82 ARG CG C 27.052 0.2 1 772 80 82 ARG CD C 43.379 0.2 1 773 80 82 ARG N N 124.062 0.2 1 774 81 83 LEU H H 8.713 0.02 1 775 81 83 LEU HA H 4.582 0.02 1 776 81 83 LEU HB2 H 0.756 0.02 2 777 81 83 LEU HB3 H 1.567 0.02 2 778 81 83 LEU HG H 1.051 0.02 1 779 81 83 LEU HD1 H -0.025 0.02 2 780 81 83 LEU HD2 H -0.259 0.02 2 781 81 83 LEU C C 174.281 0.2 1 782 81 83 LEU CA C 54.026 0.2 1 783 81 83 LEU CB C 45.405 0.2 1 784 81 83 LEU CG C 27.021 0.2 1 785 81 83 LEU CD1 C 21.278 0.2 2 786 81 83 LEU CD2 C 26.396 0.2 2 787 81 83 LEU N N 126.191 0.2 1 788 82 84 THR H H 8.532 0.02 1 789 82 84 THR HA H 5.235 0.02 1 790 82 84 THR HB H 3.875 0.02 1 791 82 84 THR HG2 H 1.046 0.02 1 792 82 84 THR C C 172.529 0.2 1 793 82 84 THR CA C 61.232 0.2 1 794 82 84 THR CB C 70.446 0.2 1 795 82 84 THR CG2 C 21.319 0.2 1 796 82 84 THR N N 123.547 0.2 1 797 83 85 LEU H H 9.701 0.02 1 798 83 85 LEU HA H 5.084 0.02 1 799 83 85 LEU HB2 H 1.533 0.02 2 800 83 85 LEU HB3 H 1.814 0.02 2 801 83 85 LEU HG H 1.620 0.02 1 802 83 85 LEU HD1 H 0.939 0.02 2 803 83 85 LEU HD2 H 0.894 0.02 2 804 83 85 LEU C C 173.095 0.2 1 805 83 85 LEU CA C 50.737 0.2 1 806 83 85 LEU CB C 45.668 0.2 1 807 83 85 LEU CG C 26.979 0.2 1 808 83 85 LEU CD1 C 25.969 0.2 2 809 83 85 LEU CD2 C 25.632 0.2 2 810 83 85 LEU N N 128.161 0.2 1 811 84 86 PRO HA H 5.172 0.02 1 812 84 86 PRO HB2 H 1.981 0.02 2 813 84 86 PRO HB3 H 2.243 0.02 2 814 84 86 PRO C C 176.393 0.2 1 815 84 86 PRO CA C 61.727 0.2 1 816 84 86 PRO CB C 31.862 0.2 1 817 85 87 VAL H H 9.315 0.02 1 818 85 87 VAL HA H 4.443 0.02 1 819 85 87 VAL HB H 1.934 0.02 1 820 85 87 VAL HG1 H 0.845 0.02 1 821 85 87 VAL HG2 H 0.845 0.02 1 822 85 87 VAL C C 175.392 0.2 1 823 85 87 VAL CA C 60.696 0.2 1 824 85 87 VAL CB C 35.443 0.2 1 825 85 87 VAL CG1 C 21.653 0.2 1 826 85 87 VAL CG2 C 21.653 0.2 1 827 85 87 VAL N N 125.245 0.2 1 828 86 88 THR H H 9.334 0.02 1 829 86 88 THR HA H 4.909 0.02 1 830 86 88 THR HB H 3.958 0.02 1 831 86 88 THR C C 173.342 0.2 1 832 86 88 THR CA C 62.301 0.2 1 833 86 88 THR CB C 70.017 0.2 1 834 86 88 THR N N 125.286 0.2 1 835 87 89 ILE H H 9.882 0.02 1 836 87 89 ILE HA H 4.129 0.02 1 837 87 89 ILE HB H 2.001 0.02 1 838 87 89 ILE HG12 H 0.867 0.02 2 839 87 89 ILE HG13 H 1.475 0.02 2 840 87 89 ILE HG2 H 0.636 0.02 1 841 87 89 ILE HD1 H 0.752 0.02 1 842 87 89 ILE C C 175.261 0.2 1 843 87 89 ILE CA C 59.880 0.2 1 844 87 89 ILE CB C 38.252 0.2 1 845 87 89 ILE CG1 C 26.222 0.2 1 846 87 89 ILE CG2 C 18.813 0.2 1 847 87 89 ILE CD1 C 14.771 0.2 1 848 87 89 ILE N N 128.207 0.2 1 849 88 90 ASN H H 9.026 0.02 1 850 88 90 ASN HA H 4.736 0.02 1 851 88 90 ASN HB2 H 2.857 0.02 2 852 88 90 ASN HB3 H 2.339 0.02 2 853 88 90 ASN C C 175.124 0.2 1 854 88 90 ASN CA C 55.551 0.2 1 855 88 90 ASN CB C 39.169 0.2 1 856 88 90 ASN N N 127.444 0.2 1 857 89 91 GLN H H 7.726 0.02 1 858 89 91 GLN HA H 4.176 0.02 1 859 89 91 GLN HB2 H 2.015 0.02 2 860 89 91 GLN HB3 H 2.016 0.02 2 861 89 91 GLN HG2 H 2.322 0.02 2 862 89 91 GLN HG3 H 2.397 0.02 2 863 89 91 GLN C C 173.145 0.2 1 864 89 91 GLN CA C 55.768 0.2 1 865 89 91 GLN CB C 30.797 0.2 1 866 89 91 GLN CG C 33.010 0.2 1 867 89 91 GLN N N 115.441 0.2 1 868 90 92 ALA H H 9.342 0.02 1 869 90 92 ALA HA H 4.740 0.02 1 870 90 92 ALA HB H 1.271 0.02 1 871 90 92 ALA C C 176.138 0.2 1 872 90 92 ALA CA C 53.158 0.2 1 873 90 92 ALA CB C 21.274 0.2 1 874 90 92 ALA N N 125.683 0.2 1 875 91 93 SER H H 8.390 0.02 1 876 91 93 SER HA H 4.653 0.02 1 877 91 93 SER HB2 H 3.816 0.02 2 878 91 93 SER HB3 H 4.025 0.02 2 879 91 93 SER C C 172.775 0.2 1 880 91 93 SER CA C 57.789 0.2 1 881 91 93 SER CB C 64.496 0.2 1 882 91 93 SER N N 120.048 0.2 1 883 92 94 ALA H H 8.498 0.02 1 884 92 94 ALA HA H 4.179 0.02 1 885 92 94 ALA HB H 1.322 0.02 1 886 92 94 ALA C C 179.320 0.2 1 887 92 94 ALA CA C 53.851 0.2 1 888 92 94 ALA CB C 17.729 0.2 1 889 92 94 ALA N N 123.702 0.2 1 890 93 95 GLY H H 9.109 0.02 1 891 93 95 GLY HA2 H 3.729 0.02 2 892 93 95 GLY HA3 H 4.033 0.02 2 893 93 95 GLY C C 174.449 0.2 1 894 93 95 GLY CA C 45.242 0.2 1 895 93 95 GLY N N 112.425 0.2 1 896 94 96 ALA H H 7.869 0.02 1 897 94 96 ALA HA H 4.497 0.02 1 898 94 96 ALA HB H 1.640 0.02 1 899 94 96 ALA C C 177.119 0.2 1 900 94 96 ALA CA C 52.950 0.2 1 901 94 96 ALA CB C 22.052 0.2 1 902 94 96 ALA N N 122.521 0.2 1 903 95 97 THR H H 8.333 0.02 1 904 95 97 THR HA H 5.155 0.02 1 905 95 97 THR HB H 3.848 0.02 1 906 95 97 THR C C 173.551 0.2 1 907 95 97 THR CA C 59.557 0.2 1 908 95 97 THR CB C 74.133 0.2 1 909 95 97 THR N N 109.165 0.2 1 910 96 98 LEU H H 8.830 0.02 1 911 96 98 LEU HA H 4.874 0.02 1 912 96 98 LEU HB2 H 1.308 0.02 2 913 96 98 LEU HB3 H 1.306 0.02 2 914 96 98 LEU HG H 1.438 0.02 1 915 96 98 LEU HD1 H 0.641 0.02 2 916 96 98 LEU HD2 H 0.684 0.02 2 917 96 98 LEU C C 175.713 0.2 1 918 96 98 LEU CA C 53.556 0.2 1 919 96 98 LEU CB C 45.352 0.2 1 920 96 98 LEU CG C 26.378 0.2 1 921 96 98 LEU CD1 C 25.705 0.2 2 922 96 98 LEU CD2 C 25.031 0.2 2 923 96 98 LEU N N 117.236 0.2 1 924 97 99 THR H H 8.849 0.02 1 925 97 99 THR HA H 4.872 0.02 1 926 97 99 THR HB H 3.973 0.02 1 927 97 99 THR HG2 H 1.049 0.02 1 928 97 99 THR C C 173.940 0.2 1 929 97 99 THR CA C 62.870 0.2 1 930 97 99 THR CB C 69.259 0.2 1 931 97 99 THR CG2 C 21.845 0.2 1 932 97 99 THR N N 121.892 0.2 1 933 98 100 VAL H H 9.371 0.02 1 934 98 100 VAL HA H 4.977 0.02 1 935 98 100 VAL HB H 1.848 0.02 1 936 98 100 VAL HG1 H 0.882 0.02 2 937 98 100 VAL HG2 H 1.031 0.02 2 938 98 100 VAL C C 173.756 0.2 1 939 98 100 VAL CA C 60.812 0.2 1 940 98 100 VAL CB C 34.174 0.2 1 941 98 100 VAL N N 129.946 0.2 1 942 99 101 THR H H 9.182 0.02 1 943 99 101 THR HA H 5.779 0.02 1 944 99 101 THR HB H 3.815 0.02 1 945 99 101 THR HG2 H 1.133 0.02 1 946 99 101 THR C C 172.579 0.2 1 947 99 101 THR CA C 60.262 0.2 1 948 99 101 THR CB C 71.326 0.2 1 949 99 101 THR CG2 C 21.526 0.2 1 950 99 101 THR N N 124.073 0.2 1 951 100 102 TYR H H 8.212 0.02 1 952 100 102 TYR HA H 4.833 0.02 1 953 100 102 TYR HB2 H 2.528 0.02 2 954 100 102 TYR HB3 H 2.982 0.02 2 955 100 102 TYR C C 172.397 0.2 1 956 100 102 TYR CA C 55.747 0.2 1 957 100 102 TYR CB C 38.787 0.2 1 958 100 102 TYR N N 117.427 0.2 1 959 101 103 GLN H H 8.337 0.02 1 960 101 103 GLN HA H 5.049 0.02 1 961 101 103 GLN HB2 H 1.660 0.02 2 962 101 103 GLN HB3 H 1.987 0.02 2 963 101 103 GLN HG2 H 2.265 0.02 2 964 101 103 GLN HG3 H 2.499 0.02 2 965 101 103 GLN C C 173.938 0.2 1 966 101 103 GLN CA C 54.820 0.2 1 967 101 103 GLN CB C 32.663 0.2 1 968 101 103 GLN CG C 33.635 0.2 1 969 101 103 GLN N N 117.968 0.2 1 970 102 104 GLY H H 8.103 0.02 1 971 102 104 GLY HA2 H 3.535 0.02 2 972 102 104 GLY HA3 H 4.411 0.02 2 973 102 104 GLY C C 171.340 0.2 1 974 102 104 GLY CA C 45.265 0.2 1 975 102 104 GLY N N 114.319 0.2 1 976 103 105 CYS HA H 5.257 0.02 1 977 103 105 CYS HB2 H 2.054 0.02 2 978 103 105 CYS HB3 H 2.727 0.02 2 979 103 105 CYS C C 175.704 0.2 1 980 103 105 CYS CA C 56.364 0.2 1 981 103 105 CYS CB C 51.937 0.2 1 982 104 106 ALA H H 8.858 0.02 1 983 104 106 ALA HA H 4.519 0.02 1 984 104 106 ALA HB H 0.975 0.02 1 985 104 106 ALA C C 179.132 0.2 1 986 104 106 ALA CA C 49.969 0.2 1 987 104 106 ALA CB C 21.706 0.2 1 988 104 106 ALA N N 120.705 0.2 1 989 105 107 ASP H H 8.916 0.02 1 990 105 107 ASP HA H 4.518 0.02 1 991 105 107 ASP HB2 H 2.465 0.02 2 992 105 107 ASP HB3 H 2.666 0.02 2 993 105 107 ASP C C 177.434 0.2 1 994 105 107 ASP CA C 57.771 0.2 1 995 105 107 ASP CB C 40.538 0.2 1 996 105 107 ASP N N 125.658 0.2 1 997 106 108 ALA H H 7.845 0.02 1 998 106 108 ALA HA H 4.293 0.02 1 999 106 108 ALA HB H 1.474 0.02 1 1000 106 108 ALA C C 178.195 0.2 1 1001 106 108 ALA CA C 53.359 0.2 1 1002 106 108 ALA CB C 18.726 0.2 1 1003 106 108 ALA N N 117.797 0.2 1 1004 107 109 GLY H H 7.728 0.02 1 1005 107 109 GLY HA2 H 3.873 0.02 2 1006 107 109 GLY HA3 H 4.487 0.02 2 1007 107 109 GLY C C 173.038 0.2 1 1008 107 109 GLY CA C 46.178 0.2 1 1009 107 109 GLY N N 103.819 0.2 1 1010 108 110 PHE H H 6.851 0.02 1 1011 108 110 PHE HA H 4.679 0.02 1 1012 108 110 PHE HB2 H 2.827 0.02 2 1013 108 110 PHE HB3 H 2.466 0.02 2 1014 108 110 PHE CA C 56.800 0.2 1 1015 108 110 PHE N N 117.941 0.2 1 1016 112 114 PRO HA H 4.327 0.02 1 1017 112 114 PRO HB2 H 1.984 0.02 2 1018 112 114 PRO HB3 H 1.658 0.02 2 1019 112 114 PRO C C 175.870 0.2 1 1020 112 114 PRO CA C 63.505 0.2 1 1021 112 114 PRO CB C 31.461 0.2 1 1022 113 115 GLU H H 8.621 0.02 1 1023 113 115 GLU HA H 4.360 0.02 1 1024 113 115 GLU HB2 H 0.935 0.02 2 1025 113 115 GLU HB3 H 1.256 0.02 2 1026 113 115 GLU HG2 H 1.969 0.02 2 1027 113 115 GLU HG3 H 2.067 0.02 2 1028 113 115 GLU C C 174.542 0.2 1 1029 113 115 GLU CA C 54.241 0.2 1 1030 113 115 GLU CB C 32.917 0.2 1 1031 113 115 GLU CG C 35.611 0.2 1 1032 113 115 GLU N N 125.351 0.2 1 1033 114 116 THR H H 8.240 0.02 1 1034 114 116 THR HA H 5.090 0.02 1 1035 114 116 THR HB H 3.701 0.02 1 1036 114 116 THR HG2 H 0.946 0.02 1 1037 114 116 THR C C 174.017 0.2 1 1038 114 116 THR CA C 61.672 0.2 1 1039 114 116 THR CB C 71.116 0.2 1 1040 114 116 THR CG2 C 21.493 0.2 1 1041 114 116 THR N N 117.242 0.2 1 1042 115 117 LYS H H 9.359 0.02 1 1043 115 117 LYS HA H 4.689 0.02 1 1044 115 117 LYS HB2 H 1.567 0.02 2 1045 115 117 LYS HB3 H 1.282 0.02 2 1046 115 117 LYS HG2 H 1.019 0.02 2 1047 115 117 LYS HG3 H 1.160 0.02 2 1048 115 117 LYS HD2 H 1.805 0.02 2 1049 115 117 LYS HD3 H 1.635 0.02 2 1050 115 117 LYS HE2 H 3.062 0.02 2 1051 115 117 LYS HE3 H 3.137 0.02 2 1052 115 117 LYS C C 175.169 0.2 1 1053 115 117 LYS CA C 52.730 0.2 1 1054 115 117 LYS CB C 35.474 0.2 1 1055 115 117 LYS CG C 24.510 0.2 1 1056 115 117 LYS CD C 28.705 0.2 1 1057 115 117 LYS CE C 42.750 0.2 1 1058 115 117 LYS N N 126.772 0.2 1 1059 116 118 THR H H 8.688 0.02 1 1060 116 118 THR HA H 4.735 0.02 1 1061 116 118 THR HB H 3.884 0.02 1 1062 116 118 THR C C 173.733 0.2 1 1063 116 118 THR CA C 62.410 0.2 1 1064 116 118 THR CB C 69.569 0.2 1 1065 116 118 THR N N 118.791 0.2 1 1066 117 119 VAL H H 9.261 0.02 1 1067 117 119 VAL HA H 3.967 0.02 1 1068 117 119 VAL HB H 1.755 0.02 1 1069 117 119 VAL HG1 H 0.551 0.02 2 1070 117 119 VAL HG2 H -0.140 0.02 2 1071 117 119 VAL C C 172.958 0.2 1 1072 117 119 VAL CA C 58.525 0.2 1 1073 117 119 VAL CB C 33.351 0.2 1 1074 117 119 VAL CG1 C 20.349 0.2 2 1075 117 119 VAL CG2 C 19.599 0.2 2 1076 117 119 VAL N N 129.408 0.2 1 1077 118 120 PRO HA H 4.511 0.02 1 1078 118 120 PRO HB2 H 2.178 0.02 2 1079 118 120 PRO HB3 H 1.955 0.02 2 1080 118 120 PRO C C 175.549 0.2 1 1081 118 120 PRO CA C 62.384 0.2 1 1082 118 120 PRO CB C 31.635 0.2 1 1083 119 121 LEU H H 7.774 0.02 1 1084 119 121 LEU HA H 4.577 0.02 1 1085 119 121 LEU HB2 H 1.078 0.02 2 1086 119 121 LEU HB3 H 1.390 0.02 2 1087 119 121 LEU HG H 1.387 0.02 1 1088 119 121 LEU HD1 H 0.498 0.02 2 1089 119 121 LEU HD2 H 0.527 0.02 2 1090 119 121 LEU C C 177.282 0.2 1 1091 119 121 LEU CA C 52.616 0.2 1 1092 119 121 LEU CB C 43.395 0.2 1 1093 119 121 LEU CG C 26.358 0.2 1 1094 119 121 LEU CD1 C 25.471 0.2 2 1095 119 121 LEU CD2 C 23.340 0.2 2 1096 119 121 LEU N N 120.917 0.2 1 1097 120 122 SER H H 9.297 0.02 1 1098 120 122 SER HA H 4.371 0.02 1 1099 120 122 SER HB2 H 3.811 0.02 2 1100 120 122 SER HB3 H 3.657 0.02 2 1101 120 122 SER C C 173.145 0.2 1 1102 120 122 SER CA C 58.127 0.2 1 1103 120 122 SER CB C 63.893 0.2 1 1104 120 122 SER N N 119.439 0.2 1 1105 121 123 GLU H H 8.205 0.02 1 1106 121 123 GLU HA H 3.641 0.02 1 1107 121 123 GLU HB2 H 1.819 0.02 2 1108 121 123 GLU HB3 H 1.888 0.02 2 1109 121 123 GLU HG2 H 2.399 0.02 2 1110 121 123 GLU HG3 H 2.017 0.02 2 1111 121 123 GLU C C 176.309 0.2 1 1112 121 123 GLU CA C 57.660 0.2 1 1113 121 123 GLU CB C 30.817 0.2 1 1114 121 123 GLU CG C 36.299 0.2 1 1115 121 123 GLU N N 121.007 0.2 1 1116 122 124 VAL H H 8.775 0.02 1 1117 122 124 VAL HA H 4.155 0.02 1 1118 122 124 VAL HB H 1.542 0.02 1 1119 122 124 VAL HG1 H 0.343 0.02 2 1120 122 124 VAL HG2 H 0.545 0.02 2 1121 122 124 VAL C C 175.241 0.2 1 1122 122 124 VAL CA C 61.361 0.2 1 1123 122 124 VAL CB C 35.351 0.2 1 1124 122 124 VAL CG1 C 21.004 0.2 2 1125 122 124 VAL CG2 C 21.001 0.2 2 1126 122 124 VAL N N 124.504 0.2 1 1127 123 125 VAL H H 8.641 0.02 1 1128 123 125 VAL HA H 4.187 0.02 1 1129 123 125 VAL HB H 2.035 0.02 1 1130 123 125 VAL HG1 H 0.966 0.02 2 1131 123 125 VAL HG2 H 0.920 0.02 2 1132 123 125 VAL C C 175.604 0.2 1 1133 123 125 VAL CA C 62.045 0.2 1 1134 123 125 VAL CB C 32.654 0.2 1 1135 123 125 VAL CG1 C 21.358 0.2 2 1136 123 125 VAL CG2 C 20.684 0.2 2 1137 123 125 VAL N N 127.676 0.2 1 1138 124 126 ALA H H 8.600 0.02 1 1139 124 126 ALA HA H 4.537 0.02 1 1140 124 126 ALA HB H 1.377 0.02 1 1141 124 126 ALA C C 177.806 0.2 1 1142 124 126 ALA CA C 52.379 0.2 1 1143 124 126 ALA CB C 19.475 0.2 1 1144 124 126 ALA N N 127.666 0.2 1 1145 125 127 ASN H H 8.622 0.02 1 1146 125 127 ASN HA H 4.684 0.02 1 1147 125 127 ASN HB2 H 2.747 0.02 1 1148 125 127 ASN HB3 H 2.747 0.02 1 1149 125 127 ASN C C 175.078 0.2 1 1150 125 127 ASN CA C 53.018 0.2 1 1151 125 127 ASN CB C 38.880 0.2 1 1152 125 127 ASN N N 119.392 0.2 1 1153 126 128 ASN H H 8.413 0.02 1 1154 126 128 ASN HA H 4.666 0.02 1 1155 126 128 ASN HB2 H 2.757 0.02 1 1156 126 128 ASN HB3 H 2.757 0.02 1 1157 126 128 ASN C C 174.688 0.2 1 1158 126 128 ASN CA C 53.122 0.2 1 1159 126 128 ASN CB C 38.880 0.2 1 1160 126 128 ASN N N 119.516 0.2 1 1161 127 129 ALA H H 8.121 0.02 1 1162 127 129 ALA HA H 4.271 0.02 1 1163 127 129 ALA HB H 1.318 0.02 1 1164 127 129 ALA C C 176.900 0.2 1 1165 127 129 ALA CA C 52.211 0.2 1 1166 127 129 ALA CB C 19.378 0.2 1 1167 127 129 ALA N N 124.059 0.2 1 1168 128 130 ALA H H 8.157 0.02 1 1169 128 130 ALA HA H 4.557 0.02 1 1170 128 130 ALA HB H 1.330 0.02 1 1171 128 130 ALA CA C 50.231 0.2 1 1172 128 130 ALA CB C 18.358 0.2 1 1173 128 130 ALA N N 124.742 0.2 1 1174 129 131 PRO HA H 4.407 0.02 1 1175 129 131 PRO HB2 H 2.259 0.02 2 1176 129 131 PRO HB3 H 1.854 0.02 2 1177 129 131 PRO C C 176.739 0.2 1 1178 129 131 PRO CA C 63.045 0.2 1 1179 130 132 GLN H H 8.418 0.02 1 1180 130 132 GLN HA H 4.580 0.02 1 1181 130 132 GLN HB2 H 2.065 0.02 2 1182 130 132 GLN HB3 H 1.896 0.02 2 1183 130 132 GLN HG2 H 2.410 0.02 1 1184 130 132 GLN HG3 H 2.410 0.02 1 1185 130 132 GLN CA C 53.478 0.2 1 1186 130 132 GLN CB C 29.120 0.2 1 1187 130 132 GLN CG C 33.527 0.2 1 1188 130 132 GLN N N 121.710 0.2 1 1189 131 133 PRO HA H 4.448 0.02 1 1190 131 133 PRO HB2 H 1.908 0.02 2 1191 131 133 PRO HB3 H 2.265 0.02 2 1192 131 133 PRO C C 176.837 0.2 1 1193 131 133 PRO CA C 62.857 0.2 1 1194 132 134 VAL H H 8.233 0.02 1 1195 132 134 VAL HA H 4.127 0.02 1 1196 132 134 VAL HB H 2.062 0.02 1 1197 132 134 VAL HG1 H 0.946 0.02 1 1198 132 134 VAL HG2 H 0.946 0.02 1 1199 132 134 VAL C C 176.734 0.2 1 1200 132 134 VAL CA C 62.699 0.2 1 1201 132 134 VAL CB C 32.808 0.2 1 1202 132 134 VAL CG1 C 20.500 0.2 1 1203 132 134 VAL CG2 C 20.500 0.2 1 1204 132 134 VAL N N 120.803 0.2 1 stop_ save_