data_16265 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete backbone 15N, 13C and 1H resonance assignments for the oxidized form of the N-terminal domain of AhpF ; _BMRB_accession_number 16265 _BMRB_flat_file_name bmr16265.str _Entry_type original _Submission_date 2009-04-27 _Accession_date 2009-04-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'backbone chemical shift assignments' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hall Andrea . . 2 Horita David . . 3 Barbar Elisar . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 "13C chemical shifts" 389 "15N chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-06-24 update BMRB 'complete entry citation' 2009-05-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15264 'Assignments for the reduced form of the N-terminal domain of AhpF' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Redox Dependent Dynamics of a Dual Thioredoxin-Fold Protein: Evolution of Specialized Folds' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19459661 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hall Andrea . . 2 Parsonage Derek . . 3 Horita David A. . 4 Karplus 'P. Andrew' . . 5 Poole Leslie B. . 6 Barbar Elisar J. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 48 _Journal_issue 25 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5984 _Page_last 5993 _Year 2009 _Details . loop_ _Keyword AhpF 'alkyl hydroperoxide reductase' 'N-terminal domain' 'oxidized disulfide' peroxiredoxin 'protein disulfide oxidoreductase' thioredoxin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain monomer' _Enzyme_commission_number 1.6.4.- loop_ _Mol_system_component_name _Mol_label 'N-terminal domain' $N-terminal_domain_of_AhpF stop_ _System_molecular_weight 44635.20 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_N-terminal_domain_of_AhpF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common N-terminal_domain_of_AhpF _Molecular_mass 44635.20 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Detoxification of hydroperoxides' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 202 _Mol_residue_sequence ; MLDTNMKTQLRAYLEKLTKP VELIATLDDSAKSAEIKELL AEIAELSDKVTFKEDNTLPV RKPSFLITNPGSQQGPRFAG SPLGHEFTSLVLALLWTGGH PSKEAQSLLEQIRDIDGDFE FETYYSLSCHNCPDVVQALN LMAVLNPRIKHTAIDGGTFQ NEITERNVMGVPAVFVNGKE FGQGRMTLTEIVAKVDTGAE KR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 ASP 4 THR 5 ASN 6 MET 7 LYS 8 THR 9 GLN 10 LEU 11 ARG 12 ALA 13 TYR 14 LEU 15 GLU 16 LYS 17 LEU 18 THR 19 LYS 20 PRO 21 VAL 22 GLU 23 LEU 24 ILE 25 ALA 26 THR 27 LEU 28 ASP 29 ASP 30 SER 31 ALA 32 LYS 33 SER 34 ALA 35 GLU 36 ILE 37 LYS 38 GLU 39 LEU 40 LEU 41 ALA 42 GLU 43 ILE 44 ALA 45 GLU 46 LEU 47 SER 48 ASP 49 LYS 50 VAL 51 THR 52 PHE 53 LYS 54 GLU 55 ASP 56 ASN 57 THR 58 LEU 59 PRO 60 VAL 61 ARG 62 LYS 63 PRO 64 SER 65 PHE 66 LEU 67 ILE 68 THR 69 ASN 70 PRO 71 GLY 72 SER 73 GLN 74 GLN 75 GLY 76 PRO 77 ARG 78 PHE 79 ALA 80 GLY 81 SER 82 PRO 83 LEU 84 GLY 85 HIS 86 GLU 87 PHE 88 THR 89 SER 90 LEU 91 VAL 92 LEU 93 ALA 94 LEU 95 LEU 96 TRP 97 THR 98 GLY 99 GLY 100 HIS 101 PRO 102 SER 103 LYS 104 GLU 105 ALA 106 GLN 107 SER 108 LEU 109 LEU 110 GLU 111 GLN 112 ILE 113 ARG 114 ASP 115 ILE 116 ASP 117 GLY 118 ASP 119 PHE 120 GLU 121 PHE 122 GLU 123 THR 124 TYR 125 TYR 126 SER 127 LEU 128 SER 129 CYS 130 HIS 131 ASN 132 CYS 133 PRO 134 ASP 135 VAL 136 VAL 137 GLN 138 ALA 139 LEU 140 ASN 141 LEU 142 MET 143 ALA 144 VAL 145 LEU 146 ASN 147 PRO 148 ARG 149 ILE 150 LYS 151 HIS 152 THR 153 ALA 154 ILE 155 ASP 156 GLY 157 GLY 158 THR 159 PHE 160 GLN 161 ASN 162 GLU 163 ILE 164 THR 165 GLU 166 ARG 167 ASN 168 VAL 169 MET 170 GLY 171 VAL 172 PRO 173 ALA 174 VAL 175 PHE 176 VAL 177 ASN 178 GLY 179 LYS 180 GLU 181 PHE 182 GLY 183 GLN 184 GLY 185 ARG 186 MET 187 THR 188 LEU 189 THR 190 GLU 191 ILE 192 VAL 193 ALA 194 LYS 195 VAL 196 ASP 197 THR 198 GLY 199 ALA 200 GLU 201 LYS 202 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 15264 ahpfn 100.00 202 100.00 100.00 2.19e-146 PDB 1HYU "Crystal Structure Of Intact Ahpf" 100.00 521 100.00 100.00 7.24e-143 PDB 1ZYN "Oxidized Structure Of The N-Terminal Domain Of Salmonella Typhimurium Ahpf" 100.00 202 100.00 100.00 2.19e-146 PDB 1ZYP "Synchrotron Reduced Form Of The N-Terminal Domain Of Salmonella Typhimurium Ahpf" 100.00 202 100.00 100.00 2.19e-146 DBJ BAA02486 "alkyl hydroperoxide reductase large subunit [Escherichia coli W3110]" 80.20 162 96.91 98.77 1.40e-111 DBJ BAH62352 "alkyl hydroperoxide reductase FAD/NAD(P)-binding subunit [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 521 97.52 99.01 4.08e-139 DBJ BAJ35614 "alkyl hydroperoxide reductase subunit F [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 100.00 521 100.00 100.00 7.24e-143 DBJ BAP06377 "alkyl hydroperoxide reductase F52A protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 100.00 521 100.00 100.00 7.24e-143 DBJ GAL49470 "alkyl hydroperoxide reductase subunit F [Citrobacter farmeri GTC 1319]" 100.00 521 97.03 99.01 1.49e-138 EMBL CAD05085 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 521 100.00 100.00 7.98e-143 EMBL CAR32166 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 100.00 521 100.00 100.00 7.16e-143 EMBL CAR36509 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 100.00 521 100.00 100.00 7.00e-143 EMBL CAR60178 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" 100.00 521 99.50 100.00 3.14e-142 EMBL CBG23683 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 100.00 521 100.00 100.00 7.24e-143 GB AAA16432 "alkyl hydroperoxide reductase [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 521 100.00 100.00 7.24e-143 GB AAL19560 "alkyl hydroperoxide reductase, F52a subunit [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 521 100.00 100.00 7.24e-143 GB AAO69861 "alkyl hydroperoxide reductase F52A protein subunit F [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 100.00 521 100.00 100.00 7.98e-143 GB AAV78017 "alkyl hydroperoxide reductase F52A protein (subunit F) [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]" 100.00 521 99.50 100.00 3.14e-142 GB AAX64546 "alkyl hydroperoxide reductase, F52a subunit; detoxification of hydroperoxides [Salmonella enterica subsp. enterica serovar Chol" 100.00 521 100.00 100.00 7.24e-143 PIR AC0577 "alkyl hydroperoxide reductase F52A protein (chain F) [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT1" 100.00 521 100.00 100.00 7.98e-143 REF NP_455185 "alkyl hydroperoxide reductase F52A protein subunit F [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 521 100.00 100.00 7.98e-143 REF NP_459601 "alkyl hydroperoxide reductase subunit F [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 521 100.00 100.00 7.24e-143 REF WP_000886405 "alkyl hydroperoxide reductase subunit F [Salmonella enterica]" 100.00 521 98.51 99.01 2.91e-140 REF WP_000887631 "alkyl hydroperoxide reductase subunit F [Salmonella enterica]" 100.00 521 99.50 100.00 2.24e-142 REF WP_000887632 "alkyl hydroperoxide reductase subunit F [Salmonella enterica]" 100.00 521 99.01 99.50 7.02e-141 SP P19480 "RecName: Full=Alkyl hydroperoxide reductase subunit F; AltName: Full=Alkyl hydroperoxide reductase F52A protein" 100.00 521 100.00 100.00 7.24e-143 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-terminal_domain_of_AhpF 'Salmonella enterica' 28901 Bacteria . Salmonella typhimurium 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 $N-terminal_domain_of_AhpF 'recombinant technology' . Escherichia coli . pOXO4 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $N-terminal_domain_of_AhpF 1 mM '[U-100% 13C; U-100% 15N]' DSS 1 mM 'natural abundance' 'maleic acid' 1 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' 'protease inhibitor' 1 mM 'natural abundance' 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Burrow_Owl _Saveframe_category software _Name Burrow_Owl _Version . loop_ _Vendor _Address _Electronic_address 'Greg Benison' . http://burrow-owl.sourceforge.net/ stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . 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_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 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 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 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_ _Software_label $Burrow_Owl $NMRPipe stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' 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 'N-terminal domain' _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 1 1 MET CA C 56.20 0.05 1 2 1 1 MET CB C 32.20 0.05 1 3 2 2 LEU H H 9.74 0.02 1 4 2 2 LEU CA C 54.68 0.05 1 5 2 2 LEU CB C 42.96 0.05 1 6 2 2 LEU N N 124.28 0.05 1 7 3 3 ASP H H 7.83 0.02 1 8 3 3 ASP CA C 53.03 0.05 1 9 3 3 ASP CB C 41.42 0.05 1 10 3 3 ASP N N 123.10 0.05 1 11 4 4 THR H H 8.36 0.02 1 12 4 4 THR CA C 66.94 0.05 1 13 4 4 THR CB C 68.65 0.05 1 14 4 4 THR N N 115.32 0.05 1 15 5 5 ASN H H 8.29 0.02 1 16 5 5 ASN CA C 56.48 0.05 1 17 5 5 ASN CB C 37.60 0.05 1 18 5 5 ASN N N 121.38 0.05 1 19 6 6 MET H H 8.46 0.02 1 20 6 6 MET CA C 59.01 0.05 1 21 6 6 MET CB C 33.10 0.05 1 22 6 6 MET N N 120.81 0.05 1 23 7 7 LYS H H 8.36 0.02 1 24 7 7 LYS CA C 61.28 0.05 1 25 7 7 LYS CB C 32.15 0.05 1 26 7 7 LYS N N 118.65 0.05 1 27 8 8 THR H H 8.11 0.02 1 28 8 8 THR CA C 66.94 0.05 1 29 8 8 THR CB C 68.96 0.05 1 30 8 8 THR N N 115.78 0.05 1 31 9 9 GLN H H 7.92 0.02 1 32 9 9 GLN CA C 58.90 0.05 1 33 9 9 GLN CB C 29.03 0.05 1 34 9 9 GLN N N 121.04 0.05 1 35 10 10 LEU H H 8.64 0.02 1 36 10 10 LEU CA C 58.47 0.05 1 37 10 10 LEU CB C 42.19 0.05 1 38 10 10 LEU N N 118.91 0.05 1 39 11 11 ARG H H 8.53 0.02 1 40 11 11 ARG CA C 60.66 0.05 1 41 11 11 ARG CB C 30.29 0.05 1 42 11 11 ARG N N 118.66 0.05 1 43 12 12 ALA H H 7.15 0.02 1 44 12 12 ALA CA C 54.81 0.05 1 45 12 12 ALA CB C 17.47 0.05 1 46 12 12 ALA N N 118.73 0.05 1 47 13 13 TYR H H 8.10 0.02 1 48 13 13 TYR CA C 60.99 0.05 1 49 13 13 TYR CB C 37.78 0.05 1 50 13 13 TYR N N 117.36 0.05 1 51 14 14 LEU H H 8.55 0.02 1 52 14 14 LEU CA C 56.87 0.05 1 53 14 14 LEU CB C 40.18 0.05 1 54 14 14 LEU N N 115.22 0.05 1 55 15 15 GLU H H 7.53 0.02 1 56 15 15 GLU CA C 58.84 0.05 1 57 15 15 GLU CB C 29.34 0.05 1 58 15 15 GLU N N 119.74 0.05 1 59 16 16 LYS H H 7.52 0.02 1 60 16 16 LYS CA C 56.21 0.05 1 61 16 16 LYS CB C 32.32 0.05 1 62 16 16 LYS N N 114.76 0.05 1 63 17 17 LEU H H 7.15 0.02 1 64 17 17 LEU CA C 56.66 0.05 1 65 17 17 LEU CB C 41.08 0.05 1 66 17 17 LEU N N 117.64 0.05 1 67 18 18 THR H H 8.57 0.02 1 68 18 18 THR CA C 62.03 0.05 1 69 18 18 THR CB C 69.96 0.05 1 70 18 18 THR N N 112.07 0.05 1 71 19 19 LYS H H 8.01 0.02 1 72 19 19 LYS CA C 53.03 0.05 1 73 19 19 LYS CB C 34.12 0.05 1 74 19 19 LYS N N 123.73 0.05 1 75 20 20 PRO CA C 62.65 0.05 1 76 20 20 PRO CB C 32.65 0.05 1 77 21 21 VAL H H 8.94 0.02 1 78 21 21 VAL CA C 61.14 0.05 1 79 21 21 VAL CB C 35.87 0.05 1 80 21 21 VAL N N 120.17 0.05 1 81 22 22 GLU H H 9.38 0.02 1 82 22 22 GLU CA C 54.74 0.05 1 83 22 22 GLU CB C 33.66 0.05 1 84 22 22 GLU N N 128.13 0.05 1 85 23 23 LEU H H 8.69 0.02 1 86 23 23 LEU CA C 52.26 0.05 1 87 23 23 LEU CB C 42.94 0.05 1 88 23 23 LEU N N 123.27 0.05 1 89 24 24 ILE H H 8.92 0.02 1 90 24 24 ILE CA C 60.19 0.05 1 91 24 24 ILE CB C 38.59 0.05 1 92 24 24 ILE N N 121.47 0.05 1 93 25 25 ALA H H 9.58 0.02 1 94 25 25 ALA CA C 50.82 0.05 1 95 25 25 ALA CB C 22.51 0.05 1 96 25 25 ALA N N 133.65 0.05 1 97 26 26 THR H H 9.34 0.02 1 98 26 26 THR CA C 63.38 0.05 1 99 26 26 THR CB C 71.34 0.05 1 100 26 26 THR N N 121.24 0.05 1 101 27 27 LEU H H 9.16 0.02 1 102 27 27 LEU CA C 53.96 0.05 1 103 27 27 LEU CB C 45.17 0.05 1 104 27 27 LEU N N 126.36 0.05 1 105 28 28 ASP H H 7.87 0.02 1 106 28 28 ASP CA C 52.08 0.05 1 107 28 28 ASP CB C 41.28 0.05 1 108 28 28 ASP N N 119.57 0.05 1 109 29 29 ASP H H 8.03 0.02 1 110 29 29 ASP CA C 53.78 0.05 1 111 29 29 ASP CB C 40.10 0.05 1 112 29 29 ASP N N 115.78 0.05 1 113 30 30 SER H H 8.14 0.02 1 114 30 30 SER CA C 58.78 0.05 1 115 30 30 SER CB C 65.70 0.05 1 116 30 30 SER N N 116.88 0.05 1 117 31 31 ALA H H 8.99 0.02 1 118 31 31 ALA CB C 18.02 0.05 1 119 31 31 ALA N N 125.37 0.05 1 120 32 32 LYS H H 8.20 0.02 1 121 32 32 LYS CA C 58.07 0.05 1 122 32 32 LYS CB C 30.68 0.05 1 123 32 32 LYS N N 117.77 0.05 1 124 33 33 SER H H 7.73 0.02 1 125 33 33 SER CA C 63.86 0.05 1 126 33 33 SER CB C 63.27 0.05 1 127 33 33 SER N N 116.70 0.05 1 128 34 34 ALA H H 7.73 0.02 1 129 34 34 ALA CA C 55.10 0.05 1 130 34 34 ALA CB C 17.38 0.05 1 131 34 34 ALA N N 124.66 0.05 1 132 35 35 GLU H H 7.79 0.02 1 133 35 35 GLU CA C 59.34 0.05 1 134 35 35 GLU CB C 29.60 0.05 1 135 35 35 GLU N N 118.63 0.05 1 136 36 36 ILE H H 7.63 0.02 1 137 36 36 ILE CA C 62.90 0.05 1 138 36 36 ILE CB C 37.67 0.05 1 139 36 36 ILE N N 119.95 0.05 1 140 37 37 LYS H H 8.55 0.02 1 141 37 37 LYS CA C 60.58 0.05 1 142 37 37 LYS CB C 34.76 0.05 1 143 37 37 LYS N N 121.18 0.05 1 144 38 38 GLU H H 7.56 0.02 1 145 38 38 GLU CA C 59.33 0.05 1 146 38 38 GLU CB C 29.38 0.05 1 147 38 38 GLU N N 116.51 0.05 1 148 39 39 LEU H H 7.66 0.02 1 149 39 39 LEU CA C 57.74 0.05 1 150 39 39 LEU CB C 40.48 0.05 1 151 39 39 LEU N N 119.29 0.05 1 152 40 40 LEU H H 8.15 0.02 1 153 40 40 LEU CA C 58.92 0.05 1 154 40 40 LEU CB C 39.96 0.05 1 155 40 40 LEU N N 116.85 0.05 1 156 41 41 ALA H H 7.55 0.02 1 157 41 41 ALA CA C 54.89 0.05 1 158 41 41 ALA CB C 17.06 0.05 1 159 41 41 ALA N N 119.60 0.05 1 160 42 42 GLU H H 7.68 0.02 1 161 42 42 GLU CA C 59.29 0.05 1 162 42 42 GLU CB C 29.47 0.05 1 163 42 42 GLU N N 119.08 0.05 1 164 43 43 ILE H H 7.93 0.02 1 165 43 43 ILE CA C 65.94 0.05 1 166 43 43 ILE CB C 37.34 0.05 1 167 43 43 ILE N N 118.55 0.05 1 168 44 44 ALA H H 7.98 0.02 1 169 44 44 ALA CA C 54.58 0.05 1 170 44 44 ALA CB C 18.27 0.05 1 171 44 44 ALA N N 119.07 0.05 1 172 45 45 GLU H H 7.34 0.02 1 173 45 45 GLU CA C 57.51 0.05 1 174 45 45 GLU CB C 29.76 0.05 1 175 45 45 GLU N N 114.52 0.05 1 176 46 46 LEU H H 7.60 0.02 1 177 46 46 LEU CA C 55.58 0.05 1 178 46 46 LEU CB C 42.71 0.05 1 179 46 46 LEU N N 115.96 0.05 1 180 47 47 SER H H 7.06 0.02 1 181 47 47 SER CA C 57.03 0.05 1 182 47 47 SER CB C 65.28 0.05 1 183 47 47 SER N N 108.97 0.05 1 184 48 48 ASP H H 9.14 0.02 1 185 48 48 ASP CA C 56.14 0.05 1 186 48 48 ASP CB C 39.90 0.05 1 187 48 48 ASP N N 130.38 0.05 1 188 49 49 LYS H H 8.51 0.02 1 189 49 49 LYS CA C 56.69 0.05 1 190 49 49 LYS CB C 32.52 0.05 1 191 49 49 LYS N N 118.75 0.05 1 192 50 50 VAL H H 7.19 0.02 1 193 50 50 VAL CA C 60.89 0.05 1 194 50 50 VAL CB C 33.11 0.05 1 195 50 50 VAL N N 118.13 0.05 1 196 51 51 THR H H 8.35 0.02 1 197 51 51 THR CA C 60.53 0.05 1 198 51 51 THR CB C 71.93 0.05 1 199 51 51 THR N N 118.70 0.05 1 200 52 52 PHE H H 8.81 0.02 1 201 52 52 PHE CA C 54.74 0.05 1 202 52 52 PHE CB C 41.49 0.05 1 203 52 52 PHE N N 124.59 0.05 1 204 53 53 LYS H H 8.95 0.02 1 205 53 53 LYS CA C 54.35 0.05 1 206 53 53 LYS CB C 36.57 0.05 1 207 53 53 LYS N N 128.69 0.05 1 208 54 54 GLU H H 8.27 0.02 1 209 54 54 GLU CA C 54.89 0.05 1 210 54 54 GLU CB C 32.62 0.05 1 211 54 54 GLU N N 119.92 0.05 1 212 55 55 ASP H H 9.02 0.02 1 213 55 55 ASP CA C 53.96 0.05 1 214 55 55 ASP CB C 40.64 0.05 1 215 55 55 ASP N N 121.57 0.05 1 216 56 56 ASN H H 9.28 0.02 1 217 56 56 ASN CA C 55.027 0.05 1 218 56 56 ASN CB C 37.83 0.05 1 219 56 56 ASN N N 123.72 0.05 1 220 57 57 THR H H 8.45 0.02 1 221 57 57 THR CA C 62.39 0.05 1 222 57 57 THR CB C 69.55 0.05 1 223 57 57 THR N N 109.96 0.05 1 224 58 58 LEU H H 6.43 0.02 1 225 58 58 LEU CA C 53.57 0.05 1 226 58 58 LEU CB C 41.55 0.05 1 227 58 58 LEU N N 122.23 0.05 1 228 59 59 PRO CA C 62.54 0.05 1 229 59 59 PRO CB C 27.61 0.05 1 230 60 60 VAL H H 7.76 0.02 1 231 60 60 VAL CA C 58.83 0.05 1 232 60 60 VAL CB C 35.45 0.05 1 233 60 60 VAL N N 114.70 0.05 1 234 61 61 ARG H H 7.76 0.02 1 235 61 61 ARG CA C 57.22 0.05 1 236 61 61 ARG CB C 32.46 0.05 1 237 61 61 ARG N N 118.59 0.05 1 238 62 62 LYS H H 8.35 0.02 1 239 62 62 LYS CA C 60.90 0.05 1 240 62 62 LYS CB C 35.26 0.05 1 241 62 62 LYS N N 118.09 0.05 1 242 63 63 PRO CA C 62.17 0.05 1 243 63 63 PRO CB C 34.95 0.05 1 244 64 64 SER H H 8.80 0.02 1 245 64 64 SER CA C 59.06 0.05 1 246 64 64 SER CB C 65.86 0.05 1 247 64 64 SER N N 110.62 0.05 1 248 65 65 PHE H H 8.79 0.02 1 249 65 65 PHE CA C 56.63 0.05 1 250 65 65 PHE CB C 42.38 0.05 1 251 65 65 PHE N N 111.93 0.05 1 252 66 66 LEU H H 8.60 0.02 1 253 66 66 LEU CA C 53.19 0.05 1 254 66 66 LEU CB C 46.59 0.05 1 255 66 66 LEU N N 124.97 0.05 1 256 67 67 ILE H H 8.00 0.02 1 257 67 67 ILE CA C 61.30 0.05 1 258 67 67 ILE CB C 38.96 0.05 1 259 67 67 ILE N N 125.73 0.05 1 260 68 68 THR H H 8.61 0.02 1 261 68 68 THR CA C 59.52 0.05 1 262 68 68 THR CB C 70.10 0.05 1 263 68 68 THR N N 119.79 0.05 1 264 69 69 ASN H H 8.90 0.02 1 265 69 69 ASN CA C 51.83 0.05 1 266 69 69 ASN CB C 40.90 0.05 1 267 69 69 ASN N N 119.81 0.05 1 268 70 70 PRO CA C 64.30 0.05 1 269 70 70 PRO CB C 31.31 0.05 1 270 71 71 GLY H H 8.79 0.02 1 271 71 71 GLY CA C 45.63 0.05 1 272 71 71 GLY N N 113.96 0.05 1 273 72 72 SER H H 8.07 0.02 1 274 72 72 SER CA C 56.67 0.05 1 275 72 72 SER CB C 64.82 0.05 1 276 72 72 SER N N 115.54 0.05 1 277 73 73 GLN H H 8.39 0.02 1 278 73 73 GLN CA C 55.09 0.05 1 279 73 73 GLN CB C 29.80 0.05 1 280 73 73 GLN N N 119.79 0.05 1 281 74 74 GLN H H 8.42 0.02 1 282 74 74 GLN CA C 55.33 0.05 1 283 74 74 GLN CB C 29.65 0.05 1 284 74 74 GLN N N 122.37 0.05 1 285 75 75 GLY H H 8.65 0.02 1 286 75 75 GLY CA C 55.40 0.05 1 287 75 75 GLY N N 115.50 0.05 1 288 76 76 PRO CA C 62.69 0.05 1 289 76 76 PRO CB C 33.27 0.05 1 290 77 77 ARG H H 8.01 0.02 1 291 77 77 ARG CA C 53.29 0.05 1 292 77 77 ARG CB C 33.79 0.05 1 293 77 77 ARG N N 119.79 0.05 1 294 78 78 PHE H H 7.96 0.02 1 295 78 78 PHE CA C 56.50 0.05 1 296 78 78 PHE CB C 42.32 0.05 1 297 78 78 PHE N N 121.32 0.05 1 298 79 79 ALA H H 9.69 0.02 1 299 79 79 ALA CA C 50.34 0.05 1 300 79 79 ALA CB C 20.85 0.05 1 301 79 79 ALA N N 128.08 0.05 1 302 80 80 GLY H H 8.18 0.02 1 303 80 80 GLY CA C 44.42 0.05 1 304 80 80 GLY N N 110.71 0.05 1 305 81 81 SER H H 8.76 0.02 1 306 81 81 SER CA C 56.08 0.05 1 307 81 81 SER CB C 63.53 0.05 1 308 81 81 SER N N 114.07 0.05 1 309 82 82 PRO CA C 62.21 0.05 1 310 82 82 PRO CB C 29.59 0.05 1 311 83 83 LEU H H 6.76 0.02 1 312 83 83 LEU CA C 52.89 0.05 1 313 83 83 LEU CB C 39.73 0.05 1 314 83 83 LEU N N 114.47 0.05 1 315 84 84 GLY H H 8.38 0.02 1 316 84 84 GLY CA C 47.09 0.05 1 317 84 84 GLY N N 108.36 0.05 1 318 85 85 HIS CA C 58.71 0.05 1 319 85 85 HIS CB C 29.99 0.05 1 320 86 86 GLU H H 8.18 0.02 1 321 86 86 GLU CA C 55.05 0.05 1 322 86 86 GLU CB C 26.18 0.05 1 323 86 86 GLU N N 112.71 0.05 1 324 87 87 PHE H H 7.43 0.02 1 325 87 87 PHE CA C 61.88 0.05 1 326 87 87 PHE CB C 38.70 0.05 1 327 87 87 PHE N N 123.80 0.05 1 328 88 88 THR H H 8.09 0.02 1 329 88 88 THR CA C 66.09 0.05 1 330 88 88 THR CB C 68.18 0.05 1 331 88 88 THR N N 111.97 0.05 1 332 89 89 SER H H 7.03 0.02 1 333 89 89 SER CA C 60.48 0.05 1 334 89 89 SER CB C 62.36 0.05 1 335 89 89 SER N N 115.31 0.05 1 336 90 90 LEU H H 8.20 0.02 1 337 90 90 LEU CA C 58.65 0.05 1 338 90 90 LEU CB C 39.43 0.05 1 339 90 90 LEU N N 126.60 0.05 1 340 91 91 VAL H H 7.80 0.02 1 341 91 91 VAL CA C 67.63 0.05 1 342 91 91 VAL CB C 30.38 0.05 1 343 91 91 VAL N N 118.35 0.05 1 344 92 92 LEU H H 7.85 0.02 1 345 92 92 LEU CA C 57.32 0.05 1 346 92 92 LEU CB C 40.49 0.05 1 347 92 92 LEU N N 116.47 0.05 1 348 93 93 ALA H H 7.22 0.02 1 349 93 93 ALA CA C 55.90 0.05 1 350 93 93 ALA CB C 17.72 0.05 1 351 93 93 ALA N N 116.92 0.05 1 352 94 94 LEU H H 7.82 0.02 1 353 94 94 LEU CA C 59.50 0.05 1 354 94 94 LEU CB C 41.93 0.05 1 355 94 94 LEU N N 119.83 0.05 1 356 95 95 LEU H H 7.97 0.02 1 357 95 95 LEU CA C 58.10 0.05 1 358 95 95 LEU CB C 40.77 0.05 1 359 95 95 LEU N N 118.22 0.05 1 360 96 96 TRP H H 9.13 0.02 1 361 96 96 TRP CA C 58.02 0.05 1 362 96 96 TRP CB C 29.26 0.05 1 363 96 96 TRP N N 119.22 0.05 1 364 97 97 THR H H 8.02 0.02 1 365 97 97 THR CA C 67.73 0.05 1 366 97 97 THR CB C 67.54 0.05 1 367 97 97 THR N N 118.95 0.05 1 368 98 98 GLY H H 8.11 0.02 1 369 98 98 GLY CA C 46.25 0.05 1 370 98 98 GLY N N 109.59 0.05 1 371 99 99 GLY H H 7.37 0.02 1 372 99 99 GLY CA C 45.33 0.05 1 373 99 99 GLY N N 106.14 0.05 1 374 100 100 HIS H H 8.78 0.02 1 375 100 100 HIS CA C 54.60 0.05 1 376 100 100 HIS CB C 32.24 0.05 1 377 100 100 HIS N N 125.89 0.05 1 378 101 101 PRO CA C 63.20 0.05 1 379 101 101 PRO CB C 31.99 0.05 1 380 102 102 SER H H 8.42 0.02 1 381 102 102 SER CA C 58.39 0.05 1 382 102 102 SER CB C 64.17 0.05 1 383 102 102 SER N N 116.29 0.05 1 384 103 103 LYS H H 8.52 0.02 1 385 103 103 LYS CA C 56.21 0.05 1 386 103 103 LYS CB C 31.90 0.05 1 387 103 103 LYS N N 121.15 0.05 1 388 104 104 GLU H H 7.44 0.02 1 389 104 104 GLU CA C 55.38 0.05 1 390 104 104 GLU CB C 29.43 0.05 1 391 104 104 GLU N N 119.01 0.05 1 392 105 105 ALA H H 8.78 0.02 1 393 105 105 ALA CA C 52.42 0.05 1 394 105 105 ALA CB C 18.78 0.05 1 395 105 105 ALA N N 122.41 0.05 1 396 106 106 GLN H H 8.67 0.02 1 397 106 106 GLN CA C 59.44 0.05 1 398 106 106 GLN CB C 28.10 0.05 1 399 106 106 GLN N N 123.28 0.05 1 400 107 107 SER H H 8.53 0.02 1 401 107 107 SER CA C 61.07 0.05 1 402 107 107 SER CB C 60.77 0.05 1 403 107 107 SER N N 111.63 0.05 1 404 108 108 LEU H H 6.90 0.02 1 405 108 108 LEU CA C 57.13 0.05 1 406 108 108 LEU CB C 41.69 0.05 1 407 108 108 LEU N N 125.21 0.05 1 408 109 109 LEU H H 7.69 0.02 1 409 109 109 LEU CA C 58.39 0.05 1 410 109 109 LEU CB C 38.76 0.05 1 411 109 109 LEU N N 118.43 0.05 1 412 110 110 GLU H H 8.24 0.02 1 413 110 110 GLU CA C 59.42 0.05 1 414 110 110 GLU CB C 28.94 0.05 1 415 110 110 GLU N N 117.85 0.05 1 416 111 111 GLN H H 7.48 0.02 1 417 111 111 GLN CA C 59.40 0.05 1 418 111 111 GLN CB C 28.09 0.05 1 419 111 111 GLN N N 118.92 0.05 1 420 112 112 ILE H H 8.07 0.02 1 421 112 112 ILE CA C 65.24 0.05 1 422 112 112 ILE CB C 37.42 0.05 1 423 112 112 ILE N N 118.01 0.05 1 424 113 113 ARG H H 7.97 0.02 1 425 113 113 ARG CA C 59.83 0.05 1 426 113 113 ARG CB C 30.29 0.05 1 427 113 113 ARG N N 120.08 0.05 1 428 114 114 ASP H H 7.43 0.02 1 429 114 114 ASP CA C 54.51 0.05 1 430 114 114 ASP CB C 41.03 0.05 1 431 114 114 ASP N N 115.80 0.05 1 432 115 115 ILE H H 7.06 0.02 1 433 115 115 ILE CA C 64.56 0.05 1 434 115 115 ILE CB C 37.38 0.05 1 435 115 115 ILE N N 122.18 0.05 1 436 116 116 ASP H H 8.69 0.02 1 437 116 116 ASP CA C 52.78 0.05 1 438 116 116 ASP CB C 41.42 0.05 1 439 116 116 ASP N N 129.94 0.05 1 440 117 117 GLY H H 7.10 0.02 1 441 117 117 GLY CA C 44.65 0.05 1 442 117 117 GLY N N 108.37 0.05 1 443 118 118 ASP H H 7.18 0.02 1 444 118 118 ASP CA C 53.70 0.05 1 445 118 118 ASP CB C 42.45 0.05 1 446 118 118 ASP N N 115.59 0.05 1 447 119 119 PHE H H 8.06 0.02 1 448 119 119 PHE CA C 57.14 0.05 1 449 119 119 PHE CB C 43.17 0.05 1 450 119 119 PHE N N 120.67 0.05 1 451 120 120 GLU H H 8.43 0.02 1 452 120 120 GLU CA C 54.84 0.05 1 453 120 120 GLU CB C 29.52 0.05 1 454 120 120 GLU N N 123.61 0.05 1 455 121 121 PHE H H 9.34 0.02 1 456 121 121 PHE CA C 58.28 0.05 1 457 121 121 PHE CB C 42.93 0.05 1 458 121 121 PHE N N 126.70 0.05 1 459 122 122 GLU H H 9.44 0.02 1 460 122 122 GLU CA C 55.24 0.05 1 461 122 122 GLU CB C 34.19 0.05 1 462 122 122 GLU N N 124.57 0.05 1 463 123 123 THR H H 8.38 0.02 1 464 123 123 THR CA C 61.77 0.05 1 465 123 123 THR CB C 69.25 0.05 1 466 123 123 THR N N 120.52 0.05 1 467 124 124 TYR H H 9.50 0.02 1 468 124 124 TYR CA C 58.68 0.05 1 469 124 124 TYR CB C 40.75 0.05 1 470 124 124 TYR N N 125.03 0.05 1 471 125 125 TYR H H 8.88 0.02 1 472 125 125 TYR CA C 55.17 0.05 1 473 125 125 TYR CB C 42.70 0.05 1 474 125 125 TYR N N 116.61 0.05 1 475 126 126 SER H H 7.11 0.02 1 476 126 126 SER CA C 56.38 0.05 1 477 126 126 SER CB C 65.00 0.05 1 478 126 126 SER N N 112.84 0.05 1 479 127 127 LEU H H 9.92 0.02 1 480 127 127 LEU CA C 59.53 0.05 1 481 127 127 LEU CB C 42.45 0.05 1 482 127 127 LEU N N 131.00 0.05 1 483 128 128 SER CA C 58.82 0.05 1 484 128 128 SER CB C 63.78 0.05 1 485 129 129 CYS H H 7.36 0.02 1 486 129 129 CYS CA C 54.80 0.05 1 487 129 129 CYS CB C 17.99 0.05 1 488 129 129 CYS N N 120.09 0.05 1 489 130 130 HIS H H 7.55 0.02 1 490 130 130 HIS CA C 59.43 0.05 1 491 130 130 HIS CB C 29.84 0.05 1 492 130 130 HIS N N 116.52 0.05 1 493 131 131 ASN H H 7.61 0.02 1 494 131 131 ASN CA C 53.85 0.05 1 495 131 131 ASN CB C 40.15 0.05 1 496 131 131 ASN N N 119.20 0.05 1 497 132 132 CYS H H 8.14 0.02 1 498 132 132 CYS CA C 58.29 0.05 1 499 132 132 CYS CB C 39.74 0.05 1 500 132 132 CYS N N 116.98 0.05 1 501 133 133 PRO CA C 63.31 0.05 1 502 133 133 PRO CB C 32.36 0.05 1 503 134 134 ASP CA C 57.96 0.05 1 504 134 134 ASP CB C 40.34 0.05 1 505 135 135 VAL H H 6.99 0.02 1 506 135 135 VAL CA C 66.30 0.05 1 507 135 135 VAL CB C 31.87 0.05 1 508 135 135 VAL N N 118.94 0.05 1 509 136 136 VAL H H 7.62 0.02 1 510 136 136 VAL CA C 67.05 0.05 1 511 136 136 VAL CB C 32.62 0.05 1 512 136 136 VAL N N 118.47 0.05 1 513 137 137 GLN H H 8.84 0.02 1 514 137 137 GLN CA C 59.36 0.05 1 515 137 137 GLN CB C 28.35 0.05 1 516 137 137 GLN N N 115.88 0.05 1 517 138 138 ALA H H 7.24 0.02 1 518 138 138 ALA CA C 55.60 0.05 1 519 138 138 ALA CB C 18.67 0.05 1 520 138 138 ALA N N 121.70 0.05 1 521 139 139 LEU H H 7.14 0.02 1 522 139 139 LEU CA C 56.87 0.05 1 523 139 139 LEU CB C 37.03 0.05 1 524 139 139 LEU N N 116.38 0.05 1 525 140 140 ASN H H 8.38 0.02 1 526 140 140 ASN CA C 55.64 0.05 1 527 140 140 ASN CB C 37.11 0.05 1 528 140 140 ASN N N 117.60 0.05 1 529 141 141 LEU H H 8.16 0.02 1 530 141 141 LEU CA C 57.97 0.05 1 531 141 141 LEU CB C 39.62 0.05 1 532 141 141 LEU N N 121.29 0.05 1 533 142 142 MET H H 7.33 0.02 1 534 142 142 MET CA C 60.87 0.05 1 535 142 142 MET CB C 33.66 0.05 1 536 142 142 MET N N 115.85 0.05 1 537 143 143 ALA H H 7.39 0.02 1 538 143 143 ALA CA C 53.73 0.05 1 539 143 143 ALA CB C 17.84 0.05 1 540 143 143 ALA N N 118.15 0.05 1 541 144 144 VAL H H 7.94 0.02 1 542 144 144 VAL CA C 65.51 0.05 1 543 144 144 VAL CB C 30.03 0.05 1 544 144 144 VAL N N 118.29 0.05 1 545 145 145 LEU H H 7.62 0.02 1 546 145 145 LEU CA C 54.09 0.05 1 547 145 145 LEU CB C 44.10 0.05 1 548 145 145 LEU N N 117.01 0.05 1 549 146 146 ASN H H 7.97 0.02 1 550 146 146 ASN CA C 49.64 0.05 1 551 146 146 ASN CB C 41.11 0.05 1 552 146 146 ASN N N 118.40 0.05 1 553 147 147 PRO CA C 63.87 0.05 1 554 147 147 PRO CB C 31.79 0.05 1 555 148 148 ARG H H 8.42 0.02 1 556 148 148 ARG CA C 57.22 0.05 1 557 148 148 ARG CB C 30.30 0.05 1 558 148 148 ARG N N 118.30 0.05 1 559 149 149 ILE H H 8.10 0.02 1 560 149 149 ILE CA C 59.96 0.05 1 561 149 149 ILE CB C 45.21 0.05 1 562 149 149 ILE N N 121.67 0.05 1 563 150 150 LYS H H 8.91 0.02 1 564 150 150 LYS CA C 54.59 0.05 1 565 150 150 LYS CB C 32.25 0.05 1 566 150 150 LYS N N 125.50 0.05 1 567 151 151 HIS H H 8.89 0.02 1 568 151 151 HIS CA C 55.57 0.05 1 569 151 151 HIS CB C 33.01 0.05 1 570 151 151 HIS N N 119.60 0.05 1 571 152 152 THR H H 7.77 0.02 1 572 152 152 THR CA C 60.81 0.05 1 573 152 152 THR CB C 69.60 0.05 1 574 152 152 THR N N 126.94 0.05 1 575 153 153 ALA H H 8.45 0.02 1 576 153 153 ALA CA C 49.69 0.05 1 577 153 153 ALA CB C 19.30 0.05 1 578 153 153 ALA N N 131.13 0.05 1 579 154 154 ILE H H 9.59 0.02 1 580 154 154 ILE CA C 61.50 0.05 1 581 154 154 ILE CB C 40.25 0.05 1 582 154 154 ILE N N 125.82 0.05 1 583 155 155 ASP H H 8.44 0.02 1 584 155 155 ASP CA C 52.59 0.05 1 585 155 155 ASP CB C 41.56 0.05 1 586 155 155 ASP N N 125.57 0.05 1 587 156 156 GLY H H 9.48 0.02 1 588 156 156 GLY CA C 46.58 0.05 1 589 156 156 GLY N N 119.62 0.05 1 590 157 157 GLY H H 8.49 0.02 1 591 157 157 GLY CA C 46.47 0.05 1 592 157 157 GLY N N 105.80 0.05 1 593 158 158 THR H H 7.31 0.02 1 594 158 158 THR CA C 64.98 0.05 1 595 158 158 THR CB C 69.09 0.05 1 596 158 158 THR N N 116.73 0.05 1 597 159 159 PHE H H 7.68 0.02 1 598 159 159 PHE CA C 57.25 0.05 1 599 159 159 PHE CB C 36.58 0.05 1 600 159 159 PHE N N 122.74 0.05 1 601 160 160 GLN H H 7.53 0.02 1 602 160 160 GLN CA C 59.21 0.05 1 603 160 160 GLN CB C 28.18 0.05 1 604 160 160 GLN N N 120.34 0.05 1 605 161 161 ASN H H 8.81 0.02 1 606 161 161 ASN CA C 56.10 0.05 1 607 161 161 ASN CB C 36.76 0.05 1 608 161 161 ASN N N 116.52 0.05 1 609 162 162 GLU H H 7.49 0.02 1 610 162 162 GLU CA C 59.39 0.05 1 611 162 162 GLU CB C 29.47 0.05 1 612 162 162 GLU N N 119.55 0.05 1 613 163 163 ILE H H 6.88 0.02 1 614 163 163 ILE CA C 62.18 0.05 1 615 163 163 ILE CB C 35.35 0.05 1 616 163 163 ILE N N 117.68 0.05 1 617 164 164 THR H H 7.40 0.02 1 618 164 164 THR CA C 65.76 0.05 1 619 164 164 THR CB C 68.44 0.05 1 620 164 164 THR N N 113.05 0.05 1 621 165 165 GLU H H 8.34 0.02 1 622 165 165 GLU CA C 59.76 0.05 1 623 165 165 GLU CB C 29.47 0.05 1 624 165 165 GLU N N 123.04 0.05 1 625 166 166 ARG H H 7.87 0.02 1 626 166 166 ARG CA C 56.09 0.05 1 627 166 166 ARG CB C 30.18 0.05 1 628 166 166 ARG N N 114.32 0.05 1 629 167 167 ASN H H 7.63 0.02 1 630 167 167 ASN CA C 54.20 0.05 1 631 167 167 ASN CB C 37.15 0.05 1 632 167 167 ASN N N 117.21 0.05 1 633 168 168 VAL H H 8.07 0.02 1 634 168 168 VAL CA C 63.79 0.05 1 635 168 168 VAL CB C 30.58 0.05 1 636 168 168 VAL N N 118.69 0.05 1 637 169 169 MET H H 8.84 0.02 1 638 169 169 MET CA C 55.39 0.05 1 639 169 169 MET CB C 32.13 0.05 1 640 169 169 MET N N 128.57 0.05 1 641 170 170 GLY H H 7.53 0.02 1 642 170 170 GLY CA C 45.02 0.05 1 643 170 170 GLY N N 108.31 0.05 1 644 171 171 VAL H H 8.03 0.02 1 645 171 171 VAL CA C 57.84 0.05 1 646 171 171 VAL CB C 33.14 0.05 1 647 171 171 VAL N N 109.68 0.05 1 648 172 172 PRO CA C 62.48 0.05 1 649 172 172 PRO CB C 34.30 0.05 1 650 173 173 ALA H H 7.89 0.02 1 651 173 173 ALA CA C 52.26 0.05 1 652 173 173 ALA CB C 22.67 0.05 1 653 173 173 ALA N N 124.65 0.05 1 654 174 174 VAL H H 8.93 0.02 1 655 174 174 VAL CA C 61.07 0.05 1 656 174 174 VAL CB C 34.32 0.05 1 657 174 174 VAL N N 122.32 0.05 1 658 175 175 PHE H H 10.21 0.02 1 659 175 175 PHE CA C 56.97 0.05 1 660 175 175 PHE CB C 42.71 0.05 1 661 175 175 PHE N N 130.99 0.05 1 662 176 176 VAL H H 9.90 0.02 1 663 176 176 VAL CA C 58.95 0.05 1 664 176 176 VAL CB C 34.39 0.05 1 665 176 176 VAL N N 120.45 0.05 1 666 177 177 ASN H H 9.20 0.02 1 667 177 177 ASN CA C 54.04 0.05 1 668 177 177 ASN CB C 36.89 0.05 1 669 177 177 ASN N N 128.30 0.05 1 670 178 178 GLY H H 9.07 0.02 1 671 178 178 GLY CA C 45.55 0.05 1 672 178 178 GLY N N 102.41 0.05 1 673 179 179 LYS H H 8.30 0.02 1 674 179 179 LYS CA C 54.75 0.05 1 675 179 179 LYS CB C 34.90 0.05 1 676 179 179 LYS N N 121.37 0.05 1 677 180 180 GLU H H 9.25 0.02 1 678 180 180 GLU CA C 59.85 0.05 1 679 180 180 GLU CB C 29.53 0.05 1 680 180 180 GLU N N 123.44 0.05 1 681 181 181 PHE H H 8.95 0.02 1 682 181 181 PHE CA C 58.52 0.05 1 683 181 181 PHE CB C 41.80 0.05 1 684 181 181 PHE N N 125.53 0.05 1 685 182 182 GLY H H 7.72 0.02 1 686 182 182 GLY CA C 45.68 0.05 1 687 182 182 GLY N N 104.61 0.05 1 688 183 183 GLN H H 8.33 0.02 1 689 183 183 GLN CA C 55.17 0.05 1 690 183 183 GLN CB C 31.97 0.05 1 691 183 183 GLN N N 119.44 0.05 1 692 184 184 GLY H H 8.05 0.02 1 693 184 184 GLY CA C 44.21 0.05 1 694 184 184 GLY N N 109.02 0.05 1 695 185 185 ARG H H 8.22 0.02 1 696 185 185 ARG CA C 58.23 0.05 1 697 185 185 ARG CB C 30.29 0.05 1 698 185 185 ARG N N 117.66 0.05 1 699 186 186 MET H H 6.92 0.02 1 700 186 186 MET CA C 54.88 0.05 1 701 186 186 MET CB C 20.98 0.05 1 702 186 186 MET N N 122.99 0.05 1 703 187 187 THR H H 8.17 0.02 1 704 187 187 THR CA C 59.66 0.05 1 705 187 187 THR CB C 71.55 0.05 1 706 187 187 THR N N 110.70 0.05 1 707 188 188 LEU H H 8.99 0.02 1 708 188 188 LEU CA C 58.75 0.05 1 709 188 188 LEU CB C 41.23 0.05 1 710 188 188 LEU N N 121.41 0.05 1 711 189 189 THR H H 8.03 0.02 1 712 189 189 THR CA C 67.05 0.05 1 713 189 189 THR CB C 68.57 0.05 1 714 189 189 THR N N 110.93 0.05 1 715 190 190 GLU H H 7.39 0.02 1 716 190 190 GLU CA C 58.92 0.05 1 717 190 190 GLU CB C 30.11 0.05 1 718 190 190 GLU N N 122.06 0.05 1 719 191 191 ILE H H 8.23 0.02 1 720 191 191 ILE CA C 66.46 0.05 1 721 191 191 ILE CB C 38.57 0.05 1 722 191 191 ILE N N 120.90 0.05 1 723 192 192 VAL H H 8.27 0.02 1 724 192 192 VAL CA C 67.45 0.05 1 725 192 192 VAL CB C 31.72 0.05 1 726 192 192 VAL N N 118.05 0.05 1 727 193 193 ALA H H 7.59 0.02 1 728 193 193 ALA CA C 54.59 0.05 1 729 193 193 ALA CB C 18.27 0.05 1 730 193 193 ALA N N 119.29 0.05 1 731 194 194 LYS H H 7.54 0.02 1 732 194 194 LYS CA C 58.34 0.05 1 733 194 194 LYS CB C 33.66 0.05 1 734 194 194 LYS N N 116.28 0.05 1 735 195 195 VAL H H 7.69 0.02 1 736 195 195 VAL CA C 63.74 0.05 1 737 195 195 VAL CB C 31.79 0.05 1 738 195 195 VAL N N 116.12 0.05 1 739 196 196 ASP H H 8.07 0.02 1 740 196 196 ASP CA C 54.46 0.05 1 741 196 196 ASP CB C 40.91 0.05 1 742 196 196 ASP N N 121.62 0.05 1 743 197 197 THR H H 7.95 0.02 1 744 197 197 THR CA C 62.61 0.05 1 745 197 197 THR CB C 69.61 0.05 1 746 197 197 THR N N 113.89 0.05 1 747 198 198 GLY H H 8.42 0.02 1 748 198 198 GLY CA C 45.63 0.05 1 749 198 198 GLY N N 111.22 0.05 1 750 199 199 ALA H H 7.98 0.02 1 751 199 199 ALA CA C 52.91 0.05 1 752 199 199 ALA CB C 19.43 0.05 1 753 199 199 ALA N N 123.67 0.05 1 754 200 200 GLU H H 8.36 0.02 1 755 200 200 GLU CA C 56.95 0.05 1 756 200 200 GLU CB C 30.29 0.05 1 757 200 200 GLU N N 119.68 0.05 1 758 201 201 LYS H H 8.21 0.02 1 759 201 201 LYS CA C 56.03 0.05 1 760 201 201 LYS CB C 32.75 0.05 1 761 201 201 LYS N N 123.17 0.05 1 762 202 202 ARG H H 7.92 0.02 1 763 202 202 ARG CA C 57.32 0.05 1 764 202 202 ARG CB C 31.59 0.05 1 765 202 202 ARG N N 128.19 0.05 1 stop_ save_