data_18396 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; nanocrystalline DsbA 1H, 13C, 15N chemical shifts ; _BMRB_accession_number 18396 _BMRB_flat_file_name bmr18396.str _Entry_type original _Submission_date 2012-04-13 _Accession_date 2012-04-13 _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 Zhou Donghua . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 140 "13C chemical shifts" 427 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-09-24 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22986689 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Donghua H. . 2 Nieuwkoop Andrew J. . 3 Berthold Deborah A. . 4 Comellas Gemma . . 5 Sperling Lindsay J. . 6 Tang Ming . . 7 Shah Gautam J. . 8 Brea Elliott J. . 9 Lemkau Luisel R. . 10 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 54 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 305 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'nanocrystalline DsbA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'nanocrystalline DsbA' $oxidized_DsbA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_oxidized_DsbA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common oxidized_DsbA _Molecular_mass . _Mol_thiol_state 'free and disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHCYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQQK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 TYR 4 GLU 5 ASP 6 GLY 7 LYS 8 GLN 9 TYR 10 THR 11 THR 12 LEU 13 GLU 14 LYS 15 PRO 16 VAL 17 ALA 18 GLY 19 ALA 20 PRO 21 GLN 22 VAL 23 LEU 24 GLU 25 PHE 26 PHE 27 SER 28 PHE 29 PHE 30 CYS 31 PRO 32 HIS 33 CYS 34 TYR 35 GLN 36 PHE 37 GLU 38 GLU 39 VAL 40 LEU 41 HIS 42 ILE 43 SER 44 ASP 45 ASN 46 VAL 47 LYS 48 LYS 49 LYS 50 LEU 51 PRO 52 GLU 53 GLY 54 VAL 55 LYS 56 MET 57 THR 58 LYS 59 TYR 60 HIS 61 VAL 62 ASN 63 PHE 64 MET 65 GLY 66 GLY 67 ASP 68 LEU 69 GLY 70 LYS 71 ASP 72 LEU 73 THR 74 GLN 75 ALA 76 TRP 77 ALA 78 VAL 79 ALA 80 MET 81 ALA 82 LEU 83 GLY 84 VAL 85 GLU 86 ASP 87 LYS 88 VAL 89 THR 90 VAL 91 PRO 92 LEU 93 PHE 94 GLU 95 GLY 96 VAL 97 GLN 98 LYS 99 THR 100 GLN 101 THR 102 ILE 103 ARG 104 SER 105 ALA 106 SER 107 ASP 108 ILE 109 ARG 110 ASP 111 VAL 112 PHE 113 ILE 114 ASN 115 ALA 116 GLY 117 ILE 118 LYS 119 GLY 120 GLU 121 GLU 122 TYR 123 ASP 124 ALA 125 ALA 126 TRP 127 ASN 128 SER 129 PHE 130 VAL 131 VAL 132 LYS 133 SER 134 LEU 135 VAL 136 ALA 137 GLN 138 GLN 139 GLN 140 LYS 141 ALA 142 ALA 143 ALA 144 ASP 145 VAL 146 GLN 147 LEU 148 ARG 149 GLY 150 VAL 151 PRO 152 ALA 153 MET 154 PHE 155 VAL 156 ASN 157 GLY 158 LYS 159 TYR 160 GLN 161 LEU 162 ASN 163 PRO 164 GLN 165 GLY 166 MET 167 ASP 168 THR 169 SER 170 ASN 171 MET 172 ASP 173 VAL 174 PHE 175 VAL 176 GLN 177 GLN 178 TYR 179 ALA 180 ASP 181 THR 182 VAL 183 LYS 184 TYR 185 LEU 186 SER 187 GLU 188 LYS 189 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 16327 DsbA 100.00 189 99.47 100.00 4.95e-136 BMRB 17710 DsbA 99.47 188 99.47 100.00 3.04e-135 BMRB 18543 DsbA(C33S) 100.00 189 98.94 99.47 1.00e-134 BMRB 18544 DsbA(C33S) 100.00 189 98.94 99.47 1.00e-134 PDB 1A23 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" 100.00 189 99.47 100.00 4.95e-136 PDB 1A24 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" 100.00 189 99.47 100.00 4.95e-136 PDB 1A2J "Oxidized Dsba Crystal Form Ii" 100.00 189 99.47 100.00 4.95e-136 PDB 1A2L "Reduced Dsba At 2.7 Angstroms Resolution" 100.00 189 99.47 100.00 4.95e-136 PDB 1A2M "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" 100.00 189 99.47 100.00 4.95e-136 PDB 1AC1 "Dsba Mutant H32l" 100.00 189 98.94 99.47 2.25e-134 PDB 1ACV "Dsba Mutant H32s" 100.00 189 98.94 99.47 8.42e-135 PDB 1BQ7 "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" 100.00 189 98.94 99.47 4.09e-135 PDB 1DSB "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" 100.00 189 99.47 100.00 4.95e-136 PDB 1FVJ "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" 100.00 189 98.94 100.00 5.32e-135 PDB 1FVK "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" 100.00 189 99.47 100.00 4.95e-136 PDB 1TI1 "Crystal Structure Of A Mutant Dsba" 100.00 189 98.94 99.47 6.00e-135 PDB 1U3A "Mutant Dsba" 100.00 189 98.94 99.47 6.00e-135 PDB 2B3S "Structure Of The Dsba Mutant (P31g-C33a)" 100.00 189 98.41 98.94 1.94e-133 PDB 2B6M "Structure Of The Dsba Mutant (P31a-C33a)" 100.00 189 98.41 98.94 1.17e-133 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 189 98.94 99.47 6.00e-135 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 100.00 189 98.94 99.47 6.00e-135 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 189 98.94 99.47 6.00e-135 PDB 3DKS "Dsba Substrate Complex" 100.00 189 98.94 100.00 1.63e-135 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 189 98.94 99.47 6.00e-135 PDB 4TKY "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" 100.00 191 98.94 99.47 6.02e-135 PDB 4WET "Crystal Structure Of E.coli Dsba In Complex With Compound 16" 100.00 189 99.47 100.00 4.95e-136 PDB 4WEY "Crystal Structure Of E.coli Dsba In Complex With Compound 17" 100.00 189 99.47 100.00 4.95e-136 PDB 4WF4 "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" 100.00 189 99.47 100.00 4.95e-136 PDB 4WF5 "Crystal Structure Of E.coli Dsba Soaked With Compound 4" 100.00 189 99.47 100.00 4.95e-136 DBJ BAB38206 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 100.00 3.46e-136 DBJ BAE77448 "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 208 99.47 100.00 3.46e-136 DBJ BAG79665 "protein disulfide isomerase I [Escherichia coli SE11]" 100.00 208 99.47 100.00 3.46e-136 DBJ BAI27892 "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" 100.00 208 99.47 100.00 3.46e-136 DBJ BAI33015 "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" 100.00 208 99.47 100.00 3.46e-136 EMBL CAA44868 "PpfA protein [Escherichia coli K-12]" 100.00 208 99.47 100.00 3.46e-136 EMBL CAA56736 "dsbA [Escherichia coli K-12]" 100.00 208 99.47 100.00 3.46e-136 EMBL CAA90910 "DsbA protein [Escherichia coli]" 100.00 208 98.94 100.00 1.10e-135 EMBL CAP78318 "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" 100.00 208 98.94 100.00 1.10e-135 EMBL CAQ34212 "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" 100.00 208 99.47 100.00 3.46e-136 GB AAA23715 "putative [Escherichia coli]" 100.00 208 99.47 100.00 3.46e-136 GB AAB02995 "dsbA [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 100.00 3.46e-136 GB AAC43519 "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" 100.00 208 98.94 99.47 1.33e-134 GB AAC43520 "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" 100.00 208 98.41 98.94 3.85e-134 GB AAC43521 "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" 100.00 208 98.41 98.94 9.33e-134 REF NP_312810 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 100.00 3.46e-136 REF NP_418297 "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 100.00 3.46e-136 REF NP_709659 "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" 100.00 208 98.94 100.00 1.28e-135 REF WP_000725331 "thiol-disulfide isomerase [Shigella boydii]" 100.00 208 98.41 99.47 6.40e-135 REF WP_000725332 "thiol:disulfide interchange protein DsbA [Escherichia coli]" 100.00 208 98.94 100.00 5.12e-136 SP P0A4L5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 100.00 1.10e-135 SP P0A4L6 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 100.00 1.10e-135 SP P0AEG4 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 3.46e-136 SP P0AEG5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 3.46e-136 SP P52235 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 100.00 1.28e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $oxidized_DsbA 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $oxidized_DsbA 'recombinant technology' . Escherichia coli . pSS18 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'polycrystalline powder' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $oxidized_DsbA 3.3 mg '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_CANH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _Sample_label $sample_1 save_ save_CA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CA(CO)NH _Sample_label $sample_1 save_ save_NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name NH _Sample_label $sample_1 save_ save_CONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CONH _Sample_label $sample_1 save_ save_CO(CA)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CO(CA)NH _Sample_label $sample_1 save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 CANH CA(CO)NH NH CONH CO(CA)NH CBCANH CBCA(CO)NH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'nanocrystalline DsbA' _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 3 3 TYR C C 175.538 0.000 1 2 4 4 GLU H H 9.022 0.057 1 3 4 4 GLU C C 174.796 0.523 1 4 4 4 GLU CA C 54.470 0.017 1 5 4 4 GLU CB C 32.837 0.109 1 6 4 4 GLU N N 122.347 0.108 1 7 5 5 ASP H H 8.730 0.027 1 8 5 5 ASP C C 177.164 0.019 1 9 5 5 ASP CA C 54.988 0.036 1 10 5 5 ASP CB C 40.576 0.087 1 11 5 5 ASP N N 125.431 0.050 1 12 6 6 GLY H H 9.130 0.046 1 13 6 6 GLY C C 173.212 0.001 1 14 6 6 GLY CA C 44.530 0.010 1 15 6 6 GLY N N 116.835 0.048 1 16 7 7 LYS H H 8.241 0.027 1 17 7 7 LYS C C 175.335 0.016 1 18 7 7 LYS CA C 56.478 0.094 1 19 7 7 LYS CB C 30.851 0.000 1 20 7 7 LYS N N 122.206 0.038 1 21 8 8 GLN H H 8.765 0.044 1 22 8 8 GLN C C 174.070 0.022 1 23 8 8 GLN CA C 58.980 0.079 1 24 8 8 GLN CB C 26.195 0.041 1 25 8 8 GLN N N 115.263 0.149 1 26 9 9 TYR H H 7.562 0.031 1 27 9 9 TYR C C 172.052 0.053 1 28 9 9 TYR CA C 54.781 0.019 1 29 9 9 TYR CB C 40.550 0.184 1 30 9 9 TYR N N 111.468 0.055 1 31 10 10 THR H H 9.663 0.035 1 32 10 10 THR C C 174.412 0.026 1 33 10 10 THR CA C 59.953 0.054 1 34 10 10 THR CB C 71.140 0.122 1 35 10 10 THR CG2 C 21.197 0.038 1 36 10 10 THR N N 111.392 0.075 1 37 11 11 THR H H 9.262 0.027 1 38 11 11 THR C C 175.294 0.030 1 39 11 11 THR CA C 62.465 0.051 1 40 11 11 THR CB C 69.264 0.023 1 41 11 11 THR CG2 C 20.613 0.083 1 42 11 11 THR N N 120.753 0.179 1 43 12 12 LEU H H 8.706 0.028 1 44 12 12 LEU C C 177.441 0.009 1 45 12 12 LEU CA C 55.576 0.045 1 46 12 12 LEU CB C 40.412 0.110 1 47 12 12 LEU CG C 27.646 0.000 1 48 12 12 LEU CD2 C 23.441 0.000 1 49 12 12 LEU N N 129.041 0.065 1 50 13 13 GLU H H 8.875 0.049 1 51 13 13 GLU C C 176.607 0.009 1 52 13 13 GLU CA C 58.278 0.047 1 53 13 13 GLU CB C 28.877 0.019 1 54 13 13 GLU N N 123.302 0.040 1 55 14 14 LYS H H 8.122 0.035 1 56 14 14 LYS C C 172.385 0.000 1 57 14 14 LYS CA C 51.853 0.038 1 58 14 14 LYS CB C 31.810 0.000 1 59 14 14 LYS N N 117.725 0.103 1 60 15 15 PRO C C 176.354 0.000 1 61 15 15 PRO CA C 62.144 0.000 1 62 16 16 VAL H H 9.218 0.020 1 63 16 16 VAL C C 176.089 0.025 1 64 16 16 VAL CA C 61.164 0.013 1 65 16 16 VAL CB C 31.746 0.000 1 66 16 16 VAL CG1 C 20.480 0.000 2 67 16 16 VAL N N 123.614 0.046 1 68 17 17 ALA H H 8.846 0.009 1 69 17 17 ALA C C 178.915 0.026 1 70 17 17 ALA CA C 52.154 0.097 1 71 17 17 ALA CB C 17.895 0.015 1 72 17 17 ALA N N 132.355 0.058 1 73 18 18 GLY H H 9.085 0.037 1 74 18 18 GLY C C 174.034 0.031 1 75 18 18 GLY CA C 45.341 0.044 1 76 18 18 GLY N N 111.027 0.048 1 77 19 19 ALA H H 7.508 0.031 1 78 19 19 ALA CA C 50.151 0.001 1 79 19 19 ALA CB C 16.398 0.000 1 80 19 19 ALA N N 121.996 0.040 1 81 20 20 PRO C C 175.610 0.000 1 82 20 20 PRO CA C 61.931 0.000 1 83 20 20 PRO CB C 31.220 0.000 1 84 21 21 GLN H H 8.652 0.019 1 85 21 21 GLN C C 177.023 0.007 1 86 21 21 GLN CA C 59.568 0.027 1 87 21 21 GLN CB C 28.770 0.000 1 88 21 21 GLN N N 121.586 0.093 1 89 22 22 VAL H H 7.697 0.022 1 90 22 22 VAL C C 172.728 0.017 1 91 22 22 VAL CA C 62.256 0.076 1 92 22 22 VAL CB C 32.974 0.000 1 93 22 22 VAL N N 115.932 0.044 1 94 23 23 LEU H H 8.939 0.015 1 95 23 23 LEU CA C 52.359 0.000 1 96 23 23 LEU N N 128.556 0.000 1 97 26 26 PHE CA C 54.497 0.000 1 98 27 27 SER H H 6.609 0.011 1 99 27 27 SER C C 177.199 0.000 1 100 27 27 SER CA C 54.382 0.069 1 101 27 27 SER CB C 63.818 0.061 1 102 27 27 SER N N 108.676 0.010 1 103 28 28 PHE H H 11.457 0.036 1 104 28 28 PHE C C 176.368 0.013 1 105 28 28 PHE CA C 62.614 0.018 1 106 28 28 PHE CB C 37.735 0.120 1 107 28 28 PHE N N 131.531 0.106 1 108 29 29 PHE H H 8.782 0.098 1 109 29 29 PHE C C 175.480 0.042 1 110 29 29 PHE CA C 59.079 0.024 1 111 29 29 PHE CB C 39.445 0.000 1 112 29 29 PHE N N 116.210 0.973 1 113 30 30 CYS H H 7.329 0.029 1 114 30 30 CYS C C 174.227 0.000 1 115 30 30 CYS CA C 52.404 0.000 1 116 30 30 CYS CB C 45.431 0.000 1 117 30 30 CYS N N 120.481 0.091 1 118 33 33 CYS H H 8.933 0.011 1 119 33 33 CYS C C 175.533 0.000 1 120 33 33 CYS CA C 62.875 0.087 1 121 33 33 CYS CB C 33.041 0.109 1 122 33 33 CYS N N 116.459 0.099 1 123 34 34 TYR H H 7.705 0.039 1 124 34 34 TYR C C 177.325 0.015 1 125 34 34 TYR CA C 59.899 0.000 1 126 34 34 TYR CB C 36.703 0.080 1 127 34 34 TYR N N 124.078 0.047 1 128 35 35 GLN H H 7.847 0.024 1 129 35 35 GLN CA C 58.270 0.030 1 130 35 35 GLN CB C 27.211 0.000 1 131 35 35 GLN N N 118.117 0.080 1 132 37 37 GLU C C 177.637 0.000 1 133 37 37 GLU CA C 58.204 0.000 1 134 38 38 GLU H H 8.377 0.025 1 135 38 38 GLU C C 176.642 0.000 1 136 38 38 GLU CA C 58.164 0.080 1 137 38 38 GLU CB C 30.073 0.000 1 138 38 38 GLU N N 112.328 0.062 1 139 39 39 VAL H H 7.000 0.061 1 140 39 39 VAL C C 176.596 0.089 1 141 39 39 VAL CA C 63.389 0.033 1 142 39 39 VAL N N 116.425 0.080 1 143 40 40 LEU H H 8.090 0.034 1 144 40 40 LEU C C 176.736 0.000 1 145 40 40 LEU CA C 54.551 0.000 1 146 40 40 LEU CB C 41.129 0.000 1 147 40 40 LEU N N 114.728 0.096 1 148 43 43 SER H H 7.827 0.000 1 149 43 43 SER CB C 61.738 0.000 1 150 43 43 SER N N 113.721 0.000 1 151 47 47 LYS C C 179.138 0.000 1 152 47 47 LYS CA C 59.696 0.040 1 153 48 48 LYS H H 7.434 0.049 1 154 48 48 LYS C C 177.558 0.005 1 155 48 48 LYS CA C 58.064 0.103 1 156 48 48 LYS CB C 31.931 0.000 1 157 48 48 LYS N N 114.700 0.146 1 158 49 49 LYS H H 7.403 0.061 1 159 49 49 LYS CA C 55.087 0.000 1 160 49 49 LYS N N 116.284 0.049 1 161 50 50 LEU H H 7.181 0.058 1 162 50 50 LEU CA C 52.913 0.000 1 163 50 50 LEU CB C 42.367 0.000 1 164 50 50 LEU N N 120.755 0.154 1 165 53 53 GLY H H 8.607 0.002 1 166 53 53 GLY C C 176.782 0.000 1 167 53 53 GLY CA C 45.157 0.066 1 168 53 53 GLY N N 111.016 0.020 1 169 54 54 VAL H H 7.509 0.008 1 170 54 54 VAL CA C 62.178 0.000 1 171 54 54 VAL CB C 30.629 0.000 1 172 54 54 VAL N N 121.525 0.017 1 173 59 59 TYR CA C 51.767 0.000 1 174 59 59 TYR CB C 40.365 0.000 1 175 60 60 HIS H H 9.388 0.043 1 176 60 60 HIS C C 176.605 0.000 1 177 60 60 HIS CA C 54.698 0.000 1 178 60 60 HIS CB C 30.851 0.000 1 179 60 60 HIS N N 123.358 0.039 1 180 61 61 VAL H H 6.346 0.000 1 181 61 61 VAL C C 175.839 0.000 1 182 61 61 VAL CA C 56.984 1.269 1 183 61 61 VAL CB C 25.069 0.000 1 184 61 61 VAL N N 112.461 0.000 1 185 62 62 ASN H H 9.150 0.502 1 186 62 62 ASN CA C 52.243 0.000 1 187 62 62 ASN CB C 38.742 0.000 1 188 62 62 ASN N N 117.438 0.060 1 189 64 64 MET C C 177.198 0.000 1 190 64 64 MET CA C 54.759 0.000 1 191 65 65 GLY H H 7.533 0.016 1 192 65 65 GLY C C 176.503 0.000 1 193 65 65 GLY CA C 46.087 0.000 1 194 65 65 GLY N N 112.024 0.282 1 195 66 66 GLY C C 176.786 0.000 1 196 66 66 GLY CA C 45.218 0.067 1 197 67 67 ASP H H 9.354 0.026 1 198 67 67 ASP C C 178.083 0.000 1 199 67 67 ASP CA C 57.236 0.028 1 200 67 67 ASP CB C 39.149 0.000 1 201 67 67 ASP N N 128.010 0.040 1 202 68 68 LEU C C 179.150 0.000 1 203 68 68 LEU CA C 56.268 0.000 1 204 69 69 GLY H H 7.586 0.025 1 205 69 69 GLY C C 176.199 0.000 1 206 69 69 GLY CA C 47.785 0.071 1 207 69 69 GLY N N 106.933 0.039 1 208 70 70 LYS H H 7.648 0.037 1 209 70 70 LYS CA C 59.371 0.000 1 210 70 70 LYS CB C 30.882 0.000 1 211 70 70 LYS N N 121.814 0.027 1 212 73 73 THR C C 176.473 0.000 1 213 73 73 THR CA C 66.611 0.148 1 214 73 73 THR CB C 68.198 0.000 1 215 74 74 GLN H H 7.976 0.032 1 216 74 74 GLN C C 177.452 0.000 1 217 74 74 GLN CA C 58.988 0.010 1 218 74 74 GLN CB C 25.023 0.000 1 219 74 74 GLN CG C 30.131 0.000 1 220 74 74 GLN N N 125.125 0.039 1 221 76 76 TRP C C 178.043 0.000 1 222 77 77 ALA H H 8.373 0.043 1 223 77 77 ALA C C 179.358 0.052 1 224 77 77 ALA CA C 55.257 0.002 1 225 77 77 ALA N N 119.703 0.051 1 226 78 78 VAL H H 8.305 0.020 1 227 78 78 VAL C C 177.740 0.039 1 228 78 78 VAL CA C 66.920 0.000 1 229 78 78 VAL N N 120.240 0.021 1 230 79 79 ALA H H 7.521 0.151 1 231 79 79 ALA C C 179.880 0.000 1 232 79 79 ALA CA C 54.650 0.009 1 233 79 79 ALA N N 121.007 0.162 1 234 80 80 MET H H 7.840 0.000 1 235 82 82 LEU C C 177.430 0.015 1 236 82 82 LEU CA C 54.084 0.000 1 237 83 83 GLY H H 7.791 0.019 1 238 83 83 GLY C C 176.728 0.020 1 239 83 83 GLY CA C 46.877 0.041 1 240 83 83 GLY N N 111.396 0.084 1 241 84 84 VAL H H 8.244 0.028 1 242 84 84 VAL C C 176.764 0.039 1 243 84 84 VAL CA C 58.995 0.036 1 244 84 84 VAL N N 108.693 0.058 1 245 85 85 GLU H H 10.878 0.053 1 246 85 85 GLU C C 179.363 0.028 1 247 85 85 GLU CA C 61.430 0.031 1 248 85 85 GLU CB C 28.367 0.035 1 249 85 85 GLU N N 126.653 0.044 1 250 86 86 ASP H H 9.092 0.026 1 251 86 86 ASP C C 177.160 0.014 1 252 86 86 ASP CA C 55.640 0.037 1 253 86 86 ASP CB C 39.129 0.192 1 254 86 86 ASP N N 116.066 0.077 1 255 87 87 LYS H H 7.880 0.041 1 256 87 87 LYS C C 177.879 0.028 1 257 87 87 LYS CA C 56.922 0.125 1 258 87 87 LYS CB C 33.242 0.000 1 259 87 87 LYS N N 116.977 0.087 1 260 88 88 VAL H H 7.006 0.023 1 261 88 88 VAL C C 176.010 0.037 1 262 88 88 VAL CA C 60.463 0.021 1 263 88 88 VAL N N 103.995 0.068 1 264 89 89 THR H H 7.845 0.022 1 265 89 89 THR C C 175.006 0.007 1 266 89 89 THR CA C 69.292 0.169 1 267 89 89 THR CB C 68.541 0.074 1 268 89 89 THR N N 120.810 0.262 1 269 90 90 VAL H H 9.287 0.030 1 270 90 90 VAL C C 175.782 0.000 1 271 90 90 VAL CA C 68.798 0.085 1 272 90 90 VAL CB C 27.812 0.000 1 273 90 90 VAL N N 119.970 0.034 1 274 92 92 LEU CA C 56.975 0.000 1 275 92 92 LEU CB C 39.423 0.000 1 276 93 93 PHE H H 8.355 0.020 1 277 93 93 PHE CA C 62.944 0.000 1 278 93 93 PHE CB C 40.136 0.000 1 279 93 93 PHE N N 120.759 0.051 1 280 94 94 GLU C C 180.096 0.000 1 281 94 94 GLU CA C 58.807 0.000 1 282 95 95 GLY H H 8.494 0.020 1 283 95 95 GLY C C 175.634 0.000 1 284 95 95 GLY CA C 46.097 0.011 1 285 95 95 GLY N N 107.996 0.100 1 286 98 98 LYS C C 177.271 0.000 1 287 98 98 LYS CA C 56.847 0.000 1 288 98 98 LYS CB C 32.494 0.000 1 289 99 99 THR H H 8.696 0.064 1 290 99 99 THR C C 175.322 0.066 1 291 99 99 THR CA C 61.819 0.087 1 292 99 99 THR CB C 68.665 0.000 1 293 99 99 THR N N 107.550 0.107 1 294 100 100 GLN H H 6.640 0.053 1 295 100 100 GLN C C 175.167 0.087 1 296 100 100 GLN CA C 57.155 0.131 1 297 100 100 GLN N N 114.614 0.133 1 298 101 101 THR H H 8.170 0.040 1 299 101 101 THR C C 175.093 0.000 1 300 101 101 THR CA C 60.435 0.077 1 301 101 101 THR CB C 68.354 0.000 1 302 101 101 THR CG2 C 21.903 0.103 1 303 101 101 THR N N 105.973 0.089 1 304 102 102 ILE H H 7.132 0.029 1 305 102 102 ILE C C 173.921 0.024 1 306 102 102 ILE CA C 60.349 0.126 1 307 102 102 ILE CB C 35.789 0.000 1 308 102 102 ILE N N 120.904 0.093 1 309 103 103 ARG H H 9.679 0.022 1 310 103 103 ARG C C 175.422 0.009 1 311 103 103 ARG CA C 54.784 0.062 1 312 103 103 ARG CB C 31.369 0.000 1 313 103 103 ARG CD C 42.404 0.000 1 314 103 103 ARG N N 125.649 0.129 1 315 104 104 SER H H 8.256 0.027 1 316 104 104 SER C C 174.311 0.017 1 317 104 104 SER CA C 56.343 0.090 1 318 104 104 SER CB C 66.610 0.059 1 319 104 104 SER N N 114.970 0.044 1 320 105 105 ALA H H 9.391 0.033 1 321 105 105 ALA C C 180.741 0.013 1 322 105 105 ALA CA C 54.776 0.060 1 323 105 105 ALA CB C 15.927 0.031 1 324 105 105 ALA N N 123.357 0.038 1 325 106 106 SER H H 8.538 0.032 1 326 106 106 SER C C 176.187 0.060 1 327 106 106 SER CA C 60.915 0.004 1 328 106 106 SER CB C 61.496 0.080 1 329 106 106 SER N N 116.020 0.038 1 330 107 107 ASP H H 7.519 0.025 1 331 107 107 ASP C C 179.079 0.033 1 332 107 107 ASP CA C 56.537 0.032 1 333 107 107 ASP CB C 41.989 0.058 1 334 107 107 ASP N N 119.934 0.074 1 335 108 108 ILE H H 7.369 0.042 1 336 108 108 ILE C C 176.927 0.001 1 337 108 108 ILE CA C 65.223 0.027 1 338 108 108 ILE CB C 37.209 0.085 1 339 108 108 ILE N N 119.991 0.053 1 340 109 109 ARG H H 7.257 0.033 1 341 109 109 ARG C C 177.901 0.029 1 342 109 109 ARG CA C 58.766 0.013 1 343 109 109 ARG CB C 28.399 0.000 1 344 109 109 ARG N N 120.974 0.091 1 345 110 110 ASP H H 7.873 0.018 1 346 110 110 ASP CA C 57.212 0.000 1 347 110 110 ASP CB C 39.304 0.000 1 348 110 110 ASP N N 116.837 0.014 1 349 113 113 ILE C C 182.131 0.000 1 350 113 113 ILE CA C 63.015 0.000 1 351 113 113 ILE CB C 37.646 0.000 1 352 114 114 ASN H H 8.644 0.016 1 353 114 114 ASN C C 175.976 0.013 1 354 114 114 ASN CA C 55.207 0.039 1 355 114 114 ASN CB C 37.515 0.036 1 356 114 114 ASN N N 120.083 0.041 1 357 115 115 ALA H H 7.519 0.026 1 358 115 115 ALA C C 176.880 0.002 1 359 115 115 ALA CA C 51.513 0.110 1 360 115 115 ALA CB C 17.952 0.090 1 361 115 115 ALA N N 120.549 0.061 1 362 116 116 GLY H H 7.881 0.045 1 363 116 116 GLY C C 173.730 0.003 1 364 116 116 GLY CA C 44.831 0.054 1 365 116 116 GLY N N 105.727 0.052 1 366 117 117 ILE H H 8.215 0.033 1 367 117 117 ILE C C 174.993 0.011 1 368 117 117 ILE CA C 60.710 0.030 1 369 117 117 ILE CB C 36.534 0.014 1 370 117 117 ILE N N 125.339 0.036 1 371 118 118 LYS H H 8.829 0.028 1 372 118 118 LYS C C 179.077 0.013 1 373 118 118 LYS CA C 56.379 0.052 1 374 118 118 LYS CB C 31.563 0.000 1 375 118 118 LYS CG C 24.274 0.000 1 376 118 118 LYS N N 125.590 0.108 1 377 119 119 GLY H H 9.522 0.030 1 378 119 119 GLY C C 175.029 0.014 1 379 119 119 GLY CA C 47.823 0.055 1 380 119 119 GLY N N 113.148 0.078 1 381 120 120 GLU H H 9.392 0.030 1 382 120 120 GLU C C 179.978 0.000 1 383 120 120 GLU CA C 59.125 0.039 1 384 120 120 GLU CB C 27.824 0.085 1 385 120 120 GLU N N 117.139 0.045 1 386 121 121 GLU H H 7.129 0.035 1 387 121 121 GLU CA C 58.230 0.137 1 388 121 121 GLU CB C 28.761 0.075 1 389 121 121 GLU N N 120.571 0.068 1 390 122 122 TYR H H 8.809 0.036 1 391 122 122 TYR C C 176.674 0.000 1 392 122 122 TYR CA C 62.353 0.084 1 393 122 122 TYR CB C 37.337 0.225 1 394 122 122 TYR N N 121.767 0.150 1 395 123 123 ASP H H 8.855 0.023 1 396 123 123 ASP C C 178.543 0.123 1 397 123 123 ASP CA C 56.927 0.043 1 398 123 123 ASP CB C 38.971 0.069 1 399 123 123 ASP N N 118.969 0.072 1 400 124 124 ALA H H 7.680 0.026 1 401 124 124 ALA C C 180.657 0.048 1 402 124 124 ALA CA C 54.215 0.045 1 403 124 124 ALA CB C 17.136 0.089 1 404 124 124 ALA N N 120.809 0.084 1 405 125 125 ALA H H 7.944 0.044 1 406 125 125 ALA C C 180.899 0.040 1 407 125 125 ALA CA C 54.499 0.072 1 408 125 125 ALA CB C 17.515 0.016 1 409 125 125 ALA N N 119.680 0.054 1 410 126 126 TRP H H 9.525 0.044 1 411 126 126 TRP C C 175.971 0.030 1 412 126 126 TRP CA C 61.008 0.038 1 413 126 126 TRP CB C 27.721 0.000 1 414 126 126 TRP N N 122.056 0.133 1 415 127 127 ASN H H 7.031 0.024 1 416 127 127 ASN C C 174.492 0.007 1 417 127 127 ASN CA C 53.201 0.017 1 418 127 127 ASN CB C 39.694 0.048 1 419 127 127 ASN N N 110.524 0.020 1 420 128 128 SER H H 7.868 0.028 1 421 128 128 SER C C 175.188 0.042 1 422 128 128 SER CA C 58.910 0.109 1 423 128 128 SER CB C 65.059 0.055 1 424 128 128 SER N N 116.265 0.078 1 425 129 129 PHE H H 9.507 0.027 1 426 129 129 PHE C C 178.670 0.000 1 427 129 129 PHE CA C 61.623 0.042 1 428 129 129 PHE CB C 38.141 0.000 1 429 129 129 PHE N N 124.812 0.044 1 430 130 130 VAL H H 8.403 0.000 1 431 130 130 VAL C C 178.347 0.000 1 432 130 130 VAL CA C 65.538 0.014 1 433 130 130 VAL CB C 30.733 0.000 1 434 130 130 VAL N N 119.100 0.000 1 435 131 131 VAL H H 7.358 0.059 1 436 131 131 VAL C C 176.663 0.000 1 437 131 131 VAL CA C 66.529 0.023 1 438 131 131 VAL CB C 30.457 0.000 1 439 131 131 VAL N N 121.456 0.142 1 440 132 132 LYS H H 7.735 0.016 1 441 132 132 LYS C C 180.290 0.000 1 442 132 132 LYS CA C 59.566 0.099 1 443 132 132 LYS N N 120.824 0.000 1 444 133 133 SER H H 8.337 0.019 1 445 133 133 SER C C 177.119 0.030 1 446 133 133 SER CA C 60.532 0.037 1 447 133 133 SER CB C 61.748 0.020 1 448 133 133 SER N N 115.261 0.062 1 449 134 134 LEU H H 8.599 0.147 1 450 134 134 LEU C C 181.128 0.000 1 451 134 134 LEU CA C 57.108 0.000 1 452 134 134 LEU CB C 42.680 0.000 1 453 134 134 LEU N N 123.726 0.112 1 454 135 135 VAL C C 176.954 0.000 1 455 135 135 VAL CA C 68.403 0.000 1 456 136 136 ALA H H 7.430 0.027 1 457 136 136 ALA C C 180.731 0.015 1 458 136 136 ALA CA C 54.649 0.116 1 459 136 136 ALA CB C 16.667 0.015 1 460 136 136 ALA N N 120.874 0.014 1 461 137 137 GLN H H 8.763 0.173 1 462 137 137 GLN C C 179.254 0.000 1 463 137 137 GLN CA C 58.698 0.007 1 464 137 137 GLN CB C 28.665 0.000 1 465 137 137 GLN N N 118.682 0.039 1 466 138 138 GLN H H 7.844 0.013 1 467 138 138 GLN C C 179.490 0.339 1 468 138 138 GLN CA C 59.461 0.108 1 469 138 138 GLN CB C 29.980 0.080 1 470 138 138 GLN N N 119.532 0.269 1 471 139 139 GLN H H 8.185 0.033 1 472 139 139 GLN C C 179.562 0.028 1 473 139 139 GLN CA C 59.352 0.024 1 474 139 139 GLN CB C 28.892 0.057 1 475 139 139 GLN N N 121.055 0.110 1 476 140 140 LYS H H 8.749 0.031 1 477 140 140 LYS C C 177.493 0.000 1 478 140 140 LYS CA C 58.293 0.000 1 479 140 140 LYS CB C 27.780 0.000 1 480 140 140 LYS N N 122.013 0.082 1 481 141 141 ALA H H 8.021 0.118 1 482 141 141 ALA C C 180.197 0.702 1 483 141 141 ALA CA C 54.680 0.134 1 484 141 141 ALA CB C 17.548 0.027 1 485 141 141 ALA N N 119.463 0.204 1 486 142 142 ALA H H 7.288 0.039 1 487 142 142 ALA C C 178.714 0.052 1 488 142 142 ALA CA C 54.200 0.384 1 489 142 142 ALA CB C 16.976 0.059 1 490 142 142 ALA N N 117.004 0.213 1 491 143 143 ALA H H 7.705 0.033 1 492 143 143 ALA C C 182.418 0.008 1 493 143 143 ALA CA C 54.289 0.067 1 494 143 143 ALA CB C 17.060 0.047 1 495 143 143 ALA N N 120.779 0.050 1 496 144 144 ASP H H 9.226 0.025 1 497 144 144 ASP C C 178.109 0.051 1 498 144 144 ASP CA C 56.940 0.024 1 499 144 144 ASP CB C 39.618 0.039 1 500 144 144 ASP N N 120.585 0.038 1 501 145 145 VAL H H 7.004 0.046 1 502 145 145 VAL C C 173.988 0.002 1 503 145 145 VAL CA C 59.824 0.022 1 504 145 145 VAL CB C 29.611 0.000 1 505 145 145 VAL N N 108.528 0.111 1 506 146 146 GLN H H 7.737 0.087 1 507 146 146 GLN C C 175.220 0.148 1 508 146 146 GLN CA C 55.700 0.114 1 509 146 146 GLN CB C 25.161 0.184 1 510 146 146 GLN N N 118.058 0.280 1 511 147 147 LEU H H 7.684 0.050 1 512 147 147 LEU C C 178.389 0.036 1 513 147 147 LEU CA C 55.767 0.002 1 514 147 147 LEU CB C 41.913 0.000 1 515 147 147 LEU N N 117.698 0.166 1 516 148 148 ARG H H 9.249 0.161 1 517 148 148 ARG C C 175.621 0.057 1 518 148 148 ARG CA C 54.619 0.067 1 519 148 148 ARG CB C 31.811 0.000 1 520 148 148 ARG N N 123.299 0.073 1 521 149 149 GLY H H 7.079 0.019 1 522 149 149 GLY C C 170.959 0.011 1 523 149 149 GLY CA C 44.823 0.050 1 524 149 149 GLY N N 105.593 0.144 1 525 150 150 VAL H H 8.545 0.026 1 526 150 150 VAL C C 172.829 0.000 1 527 150 150 VAL CA C 57.514 0.020 1 528 150 150 VAL CB C 34.037 0.000 1 529 150 150 VAL N N 111.190 0.082 1 530 151 151 PRO C C 175.921 0.000 1 531 151 151 PRO CA C 61.996 0.000 1 532 151 151 PRO CB C 35.613 0.000 1 533 152 152 ALA H H 8.234 0.029 1 534 152 152 ALA C C 174.525 0.010 1 535 152 152 ALA CA C 51.595 0.046 1 536 152 152 ALA CB C 24.630 0.056 1 537 152 152 ALA N N 122.625 0.076 1 538 153 153 MET H H 8.692 0.030 1 539 153 153 MET C C 173.060 0.013 1 540 153 153 MET CA C 54.795 0.128 1 541 153 153 MET CB C 35.819 0.000 1 542 153 153 MET CG C 31.098 0.000 1 543 153 153 MET N N 121.071 0.038 1 544 154 154 PHE H H 9.740 0.049 1 545 154 154 PHE C C 176.188 0.032 1 546 154 154 PHE CA C 55.602 0.039 1 547 154 154 PHE CB C 42.840 0.000 1 548 154 154 PHE N N 124.268 0.447 1 549 155 155 VAL H H 9.528 0.038 1 550 155 155 VAL C C 175.987 0.127 1 551 155 155 VAL CA C 60.279 0.127 1 552 155 155 VAL N N 122.675 0.140 1 553 156 156 ASN H H 10.218 0.027 1 554 156 156 ASN C C 173.992 0.085 1 555 156 156 ASN CA C 54.369 0.065 1 556 156 156 ASN CB C 36.859 0.078 1 557 156 156 ASN N N 126.764 0.076 1 558 157 157 GLY H H 9.457 0.027 1 559 157 157 GLY C C 172.525 0.010 1 560 157 157 GLY CA C 46.065 0.029 1 561 157 157 GLY N N 105.515 0.058 1 562 158 158 LYS H H 8.019 0.023 1 563 158 158 LYS C C 175.226 0.138 1 564 158 158 LYS CA C 56.695 0.062 1 565 158 158 LYS CB C 36.380 0.070 1 566 158 158 LYS N N 114.525 0.085 1 567 159 159 TYR H H 7.810 0.040 1 568 159 159 TYR C C 174.120 0.045 1 569 159 159 TYR CA C 55.098 0.083 1 570 159 159 TYR CB C 42.775 0.026 1 571 159 159 TYR N N 117.537 0.111 1 572 160 160 GLN H H 9.613 0.056 1 573 160 160 GLN HE21 H 6.082 0.014 1 574 160 160 GLN C C 175.580 0.000 1 575 160 160 GLN CA C 53.005 0.059 1 576 160 160 GLN CB C 29.875 0.021 1 577 160 160 GLN CG C 31.773 0.050 1 578 160 160 GLN N N 124.737 0.156 1 579 161 161 LEU H H 8.448 0.029 1 580 161 161 LEU C C 177.475 0.009 1 581 161 161 LEU CA C 53.982 0.052 1 582 161 161 LEU CB C 39.443 0.056 1 583 161 161 LEU N N 130.494 0.056 1 584 162 162 ASN H H 8.484 0.018 1 585 162 162 ASN C C 172.132 0.000 1 586 162 162 ASN CA C 49.699 0.000 1 587 162 162 ASN CB C 37.803 0.000 1 588 162 162 ASN N N 118.370 0.022 1 589 163 163 PRO C C 177.380 0.000 1 590 164 164 GLN H H 8.317 0.046 1 591 164 164 GLN C C 177.031 0.003 1 592 164 164 GLN CA C 57.481 0.095 1 593 164 164 GLN CB C 27.178 0.000 1 594 164 164 GLN N N 114.830 0.161 1 595 165 165 GLY H H 8.053 0.022 1 596 165 165 GLY C C 173.816 0.011 1 597 165 165 GLY CA C 44.201 0.024 1 598 165 165 GLY N N 107.135 0.052 1 599 166 166 MET H H 7.438 0.018 1 600 166 166 MET C C 174.043 0.019 1 601 166 166 MET CA C 54.364 0.031 1 602 166 166 MET CB C 33.088 0.000 1 603 166 166 MET N N 119.567 0.047 1 604 167 167 ASP H H 8.741 0.051 1 605 167 167 ASP C C 176.030 0.000 1 606 167 167 ASP CA C 53.841 0.101 1 607 167 167 ASP CB C 40.046 0.000 1 608 167 167 ASP N N 120.578 0.093 1 609 168 168 THR H H 7.959 0.061 1 610 168 168 THR C C 175.359 0.000 1 611 168 168 THR CA C 60.141 0.071 1 612 168 168 THR CB C 67.796 0.000 1 613 168 168 THR CG2 C 20.982 0.000 1 614 168 168 THR N N 112.272 0.086 1 615 169 169 SER H H 8.760 0.020 1 616 169 169 SER CA C 60.324 0.000 1 617 169 169 SER CB C 62.815 0.000 1 618 169 169 SER N N 117.951 0.031 1 619 170 170 ASN H H 7.441 0.070 1 620 170 170 ASN C C 175.292 0.015 1 621 170 170 ASN CA C 52.231 0.045 1 622 170 170 ASN CB C 39.119 0.000 1 623 170 170 ASN N N 117.535 0.018 1 624 171 171 MET H H 9.387 0.014 1 625 171 171 MET C C 177.560 0.064 1 626 171 171 MET CA C 57.186 0.045 1 627 171 171 MET N N 123.345 0.131 1 628 172 172 ASP H H 8.272 0.033 1 629 172 172 ASP C C 178.999 0.000 1 630 172 172 ASP CA C 57.195 0.000 1 631 172 172 ASP CB C 39.290 0.000 1 632 172 172 ASP N N 119.965 0.026 1 633 173 173 VAL H H 7.412 0.000 1 634 173 173 VAL C C 177.714 0.000 1 635 173 173 VAL CA C 65.291 0.056 1 636 173 173 VAL N N 120.035 0.000 1 637 174 174 PHE H H 8.452 0.039 1 638 174 174 PHE C C 176.267 0.009 1 639 174 174 PHE CA C 61.297 0.048 1 640 174 174 PHE CB C 38.365 0.000 1 641 174 174 PHE N N 121.394 0.101 1 642 175 175 VAL H H 8.119 0.013 1 643 175 175 VAL C C 177.629 0.074 1 644 175 175 VAL CA C 66.361 0.011 1 645 175 175 VAL CB C 30.797 0.000 1 646 175 175 VAL N N 116.968 0.061 1 647 176 176 GLN H H 7.333 0.031 1 648 176 176 GLN C C 177.799 0.015 1 649 176 176 GLN CA C 57.949 0.089 1 650 176 176 GLN CB C 27.048 0.040 1 651 176 176 GLN N N 116.424 0.057 1 652 177 177 GLN H H 8.780 0.032 1 653 177 177 GLN C C 179.856 0.016 1 654 177 177 GLN CA C 58.806 0.087 1 655 177 177 GLN CB C 27.054 0.000 1 656 177 177 GLN N N 119.321 0.112 1 657 178 178 TYR H H 9.118 0.052 1 658 178 178 TYR C C 178.098 0.000 1 659 178 178 TYR CA C 61.307 0.025 1 660 178 178 TYR CB C 37.374 0.080 1 661 178 178 TYR N N 126.560 0.085 1 662 179 179 ALA H H 8.345 0.066 1 663 179 179 ALA C C 179.543 0.000 1 664 179 179 ALA CA C 55.181 0.225 1 665 179 179 ALA CB C 17.524 0.010 1 666 179 179 ALA N N 119.561 0.205 1 667 180 180 ASP H H 9.040 0.036 1 668 180 180 ASP C C 179.470 0.000 1 669 180 180 ASP CA C 57.072 0.109 1 670 180 180 ASP CB C 39.160 0.093 1 671 180 180 ASP N N 118.498 0.076 1 672 181 181 THR H H 8.359 0.031 1 673 181 181 THR C C 176.103 0.061 1 674 181 181 THR CA C 66.942 0.012 1 675 181 181 THR CG2 C 20.571 0.000 1 676 181 181 THR N N 120.239 0.107 1 677 182 182 VAL H H 7.821 0.036 1 678 182 182 VAL C C 177.661 0.047 1 679 182 182 VAL CA C 67.202 0.034 1 680 182 182 VAL CB C 29.881 0.124 1 681 182 182 VAL N N 121.224 0.031 1 682 183 183 LYS H H 7.857 0.067 1 683 183 183 LYS CA C 59.686 0.231 1 684 183 183 LYS CB C 31.097 0.000 1 685 183 183 LYS N N 120.246 0.165 1 686 184 184 TYR H H 7.945 0.021 1 687 184 184 TYR C C 177.864 0.000 1 688 184 184 TYR CA C 60.048 0.006 1 689 184 184 TYR CB C 37.043 0.028 1 690 184 184 TYR N N 119.886 0.111 1 691 185 185 LEU H H 8.252 0.026 1 692 185 185 LEU C C 179.312 0.029 1 693 185 185 LEU CA C 56.066 0.028 1 694 185 185 LEU CB C 41.050 0.024 1 695 185 185 LEU N N 117.968 0.061 1 696 186 186 SER H H 8.631 0.032 1 697 186 186 SER C C 175.462 0.040 1 698 186 186 SER CA C 61.365 0.070 1 699 186 186 SER CB C 61.683 0.005 1 700 186 186 SER N N 114.857 0.062 1 701 187 187 GLU H H 7.038 0.071 1 702 187 187 GLU C C 175.783 0.000 1 703 187 187 GLU CA C 55.508 0.000 1 704 187 187 GLU CB C 29.346 0.000 1 705 187 187 GLU N N 119.126 0.076 1 stop_ save_