data_15264 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete backbone 15N, 13C, and 1H resonance assignments for the N-terminal domain of AhpF ; _BMRB_accession_number 15264 _BMRB_flat_file_name bmr15264.str _Entry_type original _Submission_date 2007-05-23 _Accession_date 2007-05-23 _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 Benison Gregory C. . 2 Barbar Elisar J. . 3 Horita David A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 191 "13C chemical shifts" 390 "15N chemical shifts" 191 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-06-22 update BMRB 'added time domain data' 2008-07-02 update BMRB 'complete entry citation' 2007-10-29 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protein assignments without peak lists using higher-order spectra' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17919953 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Benison Gregory C. . 2 Berkholz Donald S. . 3 Barbar Elisar J. . stop_ _Journal_abbreviation 'J. Magn. Reson.' _Journal_volume 189 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 173 _Page_last 181 _Year 2007 _Details . loop_ _Keyword AhpF assignments burrow-owl nmr peroxiredoxin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ahpfn _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ahpfn $ahpfn 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_ahpfn _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ahpfn _Molecular_mass . _Mol_thiol_state 'all free' _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 16265 N-terminal_domain_of_AhpF 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 $ahpfn 'Salmonella typhimurium' 602 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 $ahpfn '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 $ahpfn 1 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % . 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' DSS 1 mM '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_AutoAssign _Saveframe_category software _Name AutoAssign _Version . loop_ _Vendor _Address _Electronic_address 'Zimmerman, Moseley, Kulikowski and Montelione' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_burrow-owl _Saveframe_category software _Name Burrow-Owl _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Greg Benison; Barbar Lab' ; Biochemistry and Biophysics Oregon State University ; ; gbenison@gmail.com www.burrow-owl.org ; stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'chemical shift assignment; spectrum viewing and plotting' 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_NMR_spectrometer_expt_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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 'ionic strength' 0.25 . 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 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D 1H-15N NOESY' 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 ahpfn _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 55.78 0.05 1 2 1 1 MET CB C 32.50 0.05 1 3 2 2 LEU H H 9.78 0.02 1 4 2 2 LEU CA C 54.61 0.05 1 5 2 2 LEU CB C 43.23 0.05 1 6 2 2 LEU N N 124.36 0.05 1 7 3 3 ASP H H 7.79 0.02 1 8 3 3 ASP CA C 52.67 0.05 1 9 3 3 ASP CB C 41.42 0.05 1 10 3 3 ASP N N 123.03 0.05 1 11 4 4 THR H H 8.31 0.02 1 12 4 4 THR CA C 66.64 0.05 1 13 4 4 THR CB C 68.71 0.05 1 14 4 4 THR N N 114.99 0.05 1 15 5 5 ASN H H 8.26 0.02 1 16 5 5 ASN CA C 56.42 0.05 1 17 5 5 ASN CB C 37.93 0.05 1 18 5 5 ASN N N 121.39 0.05 1 19 6 6 MET H H 8.47 0.02 1 20 6 6 MET CA C 58.88 0.05 1 21 6 6 MET CB C 33.66 0.05 1 22 6 6 MET N N 120.86 0.05 1 23 7 7 LYS H H 8.34 0.02 1 24 7 7 LYS CA C 61.08 0.05 1 25 7 7 LYS CB C 32.50 0.05 1 26 7 7 LYS N N 118.64 0.05 1 27 8 8 THR H H 8.12 0.02 1 28 8 8 THR CA C 66.64 0.05 1 29 8 8 THR CB C 68.97 0.05 1 30 8 8 THR N N 115.80 0.05 1 31 9 9 GLN H H 7.91 0.02 1 32 9 9 GLN CA C 58.62 0.05 1 33 9 9 GLN CB C 29.00 0.05 1 34 9 9 GLN N N 121.00 0.05 1 35 10 10 LEU H H 8.64 0.02 1 36 10 10 LEU CA C 58.36 0.05 1 37 10 10 LEU CB C 42.20 0.05 1 38 10 10 LEU N N 119.00 0.05 1 39 11 11 ARG H H 8.52 0.02 1 40 11 11 ARG CA C 60.43 0.05 1 41 11 11 ARG CB C 30.30 0.05 1 42 11 11 ARG N N 118.58 0.05 1 43 12 12 ALA H H 7.14 0.02 1 44 12 12 ALA CA C 54.63 0.05 1 45 12 12 ALA CB C 17.85 0.05 1 46 12 12 ALA N N 118.58 0.05 1 47 13 13 TYR H H 8.11 0.02 1 48 13 13 TYR CA C 60.57 0.05 1 49 13 13 TYR CB C 38.06 0.05 1 50 13 13 TYR N N 117.37 0.05 1 51 14 14 LEU H H 8.53 0.02 1 52 14 14 LEU CA C 56.68 0.05 1 53 14 14 LEU CB C 40.00 0.05 1 54 14 14 LEU N N 115.18 0.05 1 55 15 15 GLU H H 7.53 0.02 1 56 15 15 GLU CA C 58.62 0.05 1 57 15 15 GLU CB C 29.91 0.05 1 58 15 15 GLU N N 119.96 0.05 1 59 16 16 LYS H H 7.53 0.02 1 60 16 16 LYS CA C 55.95 0.05 1 61 16 16 LYS CB C 32.40 0.05 1 62 16 16 LYS N N 114.70 0.05 1 63 17 17 LEU H H 7.17 0.02 1 64 17 17 LEU CA C 56.55 0.05 1 65 17 17 LEU CB C 41.40 0.05 1 66 17 17 LEU N N 117.80 0.05 1 67 18 18 THR H H 8.55 0.02 1 68 18 18 THR CA C 61.95 0.05 1 69 18 18 THR CB C 69.75 0.05 1 70 18 18 THR N N 112.27 0.05 1 71 19 19 LYS H H 7.98 0.02 1 72 19 19 LYS CA C 53.00 0.05 1 73 19 19 LYS CB C 34.13 0.05 1 74 19 19 LYS N N 123.60 0.05 1 75 20 20 PRO CA C 62.37 0.05 1 76 20 20 PRO CB C 32.63 0.05 1 77 21 21 VAL H H 8.83 0.02 1 78 21 21 VAL CA C 60.95 0.05 1 79 21 21 VAL CB C 36.25 0.05 1 80 21 21 VAL N N 120.02 0.05 1 81 22 22 GLU H H 9.33 0.02 1 82 22 22 GLU CA C 54.35 0.05 1 83 22 22 GLU CB C 33.66 0.05 1 84 22 22 GLU N N 127.98 0.05 1 85 23 23 LEU H H 8.73 0.02 1 86 23 23 LEU CA C 52.15 0.05 1 87 23 23 LEU CB C 42.58 0.05 1 88 23 23 LEU N N 123.61 0.05 1 89 24 24 ILE H H 8.90 0.02 1 90 24 24 ILE CA C 60.04 0.05 1 91 24 24 ILE CB C 38.83 0.05 1 92 24 24 ILE N N 121.46 0.05 1 93 25 25 ALA H H 9.60 0.02 1 94 25 25 ALA CA C 50.73 0.05 1 95 25 25 ALA CB C 22.41 0.05 1 96 25 25 ALA N N 133.74 0.05 1 97 26 26 THR H H 9.35 0.02 1 98 26 26 THR CA C 63.27 0.05 1 99 26 26 THR CB C 71.03 0.05 1 100 26 26 THR N N 121.22 0.05 1 101 27 27 LEU H H 9.14 0.02 1 102 27 27 LEU CA C 53.58 0.05 1 103 27 27 LEU CB C 45.17 0.05 1 104 27 27 LEU N N 126.43 0.05 1 105 28 28 ASP H H 7.87 0.02 1 106 28 28 ASP CA C 51.64 0.05 1 107 28 28 ASP CB C 41.81 0.05 1 108 28 28 ASP N N 119.56 0.05 1 109 29 29 ASP H H 8.03 0.02 1 110 29 29 ASP CA C 53.67 0.05 1 111 29 29 ASP CB C 40.00 0.05 1 112 29 29 ASP N N 115.75 0.05 1 113 30 30 SER H H 8.13 0.02 1 114 30 30 SER CA C 58.67 0.05 1 115 30 30 SER CB C 65.71 0.05 1 116 30 30 SER N N 116.98 0.05 1 117 31 31 ALA H H 8.93 0.02 1 118 31 31 ALA CA C 54.96 0.05 1 119 31 31 ALA CB C 17.86 0.05 1 120 31 31 ALA N N 125.13 0.05 1 121 32 32 LYS H H 8.17 0.02 1 122 32 32 LYS CA C 57.97 0.05 1 123 32 32 LYS CB C 30.95 0.05 1 124 32 32 LYS N N 117.55 0.05 1 125 33 33 SER H H 7.72 0.02 1 126 33 33 SER CA C 64.05 0.05 1 127 33 33 SER CB C 63.28 0.05 1 128 33 33 SER N N 116.49 0.05 1 129 34 34 ALA H H 7.74 0.02 1 130 34 34 ALA CA C 55.00 0.05 1 131 34 34 ALA CB C 17.76 0.05 1 132 34 34 ALA N N 124.75 0.05 1 133 35 35 GLU H H 7.81 0.02 1 134 35 35 GLU CA C 59.26 0.05 1 135 35 35 GLU CB C 30.17 0.05 1 136 35 35 GLU N N 118.69 0.05 1 137 36 36 ILE H H 7.60 0.02 1 138 36 36 ILE CA C 62.50 0.05 1 139 36 36 ILE CB C 35.99 0.05 1 140 36 36 ILE N N 119.93 0.05 1 141 37 37 LYS H H 8.55 0.02 1 142 37 37 LYS CA C 60.56 0.05 1 143 37 37 LYS CB C 32.37 0.05 1 144 37 37 LYS N N 121.24 0.05 1 145 38 38 GLU H H 7.55 0.02 1 146 38 38 GLU CA C 59.14 0.05 1 147 38 38 GLU CB C 29.91 0.05 1 148 38 38 GLU N N 116.55 0.05 1 149 39 39 LEU H H 7.67 0.02 1 150 39 39 LEU CA C 57.59 0.05 1 151 39 39 LEU CB C 41.81 0.05 1 152 39 39 LEU N N 119.42 0.05 1 153 40 40 LEU H H 8.13 0.02 1 154 40 40 LEU CA C 57.32 0.05 1 155 40 40 LEU CB C 40.00 0.05 1 156 40 40 LEU N N 116.97 0.05 1 157 41 41 ALA H H 7.51 0.02 1 158 41 41 ALA CA C 55.13 0.05 1 159 41 41 ALA CB C 17.63 0.05 1 160 41 41 ALA N N 119.67 0.05 1 161 42 42 GLU H H 7.66 0.02 1 162 42 42 GLU CA C 59.26 0.05 1 163 42 42 GLU CB C 30.04 0.05 1 164 42 42 GLU N N 118.91 0.05 1 165 43 43 ILE H H 7.92 0.02 1 166 43 43 ILE CA C 66.12 0.05 1 167 43 43 ILE CB C 37.67 0.05 1 168 43 43 ILE N N 118.76 0.05 1 169 44 44 ALA H H 7.90 0.02 1 170 44 44 ALA CA C 54.48 0.05 1 171 44 44 ALA CB C 18.28 0.05 1 172 44 44 ALA N N 119.06 0.05 1 173 45 45 GLU H H 7.29 0.02 1 174 45 45 GLU CA C 57.58 0.05 1 175 45 45 GLU CB C 30.17 0.05 1 176 45 45 GLU N N 113.79 0.05 1 177 46 46 LEU H H 7.58 0.02 1 178 46 46 LEU CA C 55.26 0.05 1 179 46 46 LEU CB C 42.71 0.05 1 180 46 46 LEU N N 115.71 0.05 1 181 47 47 SER H H 7.14 0.02 1 182 47 47 SER CA C 56.81 0.05 1 183 47 47 SER CB C 65.34 0.05 1 184 47 47 SER N N 109.90 0.05 1 185 48 48 ASP H H 8.85 0.02 1 186 48 48 ASP CA C 55.26 0.05 1 187 48 48 ASP CB C 40.00 0.05 1 188 48 48 ASP N N 127.57 0.05 1 189 49 49 LYS H H 8.47 0.02 1 190 49 49 LYS CA C 56.29 0.05 1 191 49 49 LYS CB C 34.18 0.05 1 192 49 49 LYS N N 118.52 0.05 1 193 50 50 VAL H H 7.14 0.02 1 194 50 50 VAL CA C 60.69 0.05 1 195 50 50 VAL CB C 34.05 0.05 1 196 50 50 VAL N N 118.40 0.05 1 197 51 51 THR H H 8.31 0.02 1 198 51 51 THR CA C 60.30 0.05 1 199 51 51 THR CB C 71.94 0.05 1 200 51 51 THR N N 118.04 0.05 1 201 52 52 PHE H H 8.77 0.02 1 202 52 52 PHE CA C 54.61 0.05 1 203 52 52 PHE CB C 41.29 0.05 1 204 52 52 PHE N N 124.35 0.05 1 205 53 53 LYS H H 8.97 0.02 1 206 53 53 LYS CA C 54.22 0.05 1 207 53 53 LYS CB C 36.77 0.05 1 208 53 53 LYS N N 128.34 0.05 1 209 54 54 GLU H H 8.29 0.02 1 210 54 54 GLU CA C 54.61 0.05 1 211 54 54 GLU CB C 32.63 0.05 1 212 54 54 GLU N N 119.96 0.05 1 213 55 55 ASP H H 9.03 0.02 1 214 55 55 ASP CA C 53.83 0.05 1 215 55 55 ASP CB C 40.65 0.05 1 216 55 55 ASP N N 121.76 0.05 1 217 56 56 ASN H H 9.25 0.02 1 218 56 56 ASN CA C 54.74 0.05 1 219 56 56 ASN CB C 37.67 0.05 1 220 56 56 ASN N N 123.61 0.05 1 221 57 57 THR H H 8.43 0.02 1 222 57 57 THR CA C 61.98 0.05 1 223 57 57 THR CB C 69.74 0.05 1 224 57 57 THR N N 109.96 0.05 1 225 58 58 LEU H H 6.40 0.02 1 226 58 58 LEU CA C 53.32 0.05 1 227 58 58 LEU CB C 41.55 0.05 1 228 58 58 LEU N N 122.36 0.05 1 229 59 59 PRO CA C 62.39 0.05 1 230 59 59 PRO CB C 27.61 0.05 1 231 60 60 VAL H H 7.75 0.02 1 232 60 60 VAL CA C 58.45 0.05 1 233 60 60 VAL CB C 35.50 0.05 1 234 60 60 VAL N N 114.73 0.05 1 235 61 61 ARG H H 7.75 0.02 1 236 61 61 ARG CA C 56.77 0.05 1 237 61 61 ARG CB C 32.15 0.05 1 238 61 61 ARG N N 118.50 0.05 1 239 62 62 LYS H H 8.33 0.02 1 240 62 62 LYS CA C 60.24 0.05 1 241 62 62 LYS CB C 35.26 0.05 1 242 62 62 LYS N N 117.94 0.05 1 243 63 63 PRO CA C 62.11 0.05 1 244 63 63 PRO CB C 34.95 0.05 1 245 64 64 SER H H 8.79 0.02 1 246 64 64 SER CA C 58.62 0.05 1 247 64 64 SER CB C 65.73 0.05 1 248 64 64 SER N N 110.36 0.05 1 249 65 65 PHE H H 8.76 0.02 1 250 65 65 PHE CA C 56.55 0.05 1 251 65 65 PHE CB C 42.07 0.05 1 252 65 65 PHE N N 111.86 0.05 1 253 66 66 LEU H H 8.57 0.02 1 254 66 66 LEU CA C 52.80 0.05 1 255 66 66 LEU CB C 46.59 0.05 1 256 66 66 LEU N N 125.07 0.05 1 257 67 67 ILE H H 8.00 0.02 1 258 67 67 ILE CA C 61.08 0.05 1 259 67 67 ILE CB C 38.96 0.05 1 260 67 67 ILE N N 125.72 0.05 1 261 68 68 THR H H 8.62 0.02 1 262 68 68 THR CA C 59.44 0.05 1 263 68 68 THR CB C 70.18 0.05 1 264 68 68 THR N N 119.96 0.05 1 265 69 69 ASN H H 8.89 0.02 1 266 69 69 ASN CA C 55.51 0.05 1 267 69 69 ASN CB C 40.90 0.05 1 268 69 69 ASN N N 119.60 0.05 1 269 70 70 PRO CA C 63.83 0.05 1 270 70 70 PRO CB C 31.31 0.05 1 271 71 71 GLY H H 8.77 0.02 1 272 71 71 GLY CA C 45.56 0.05 1 273 71 71 GLY N N 113.89 0.05 1 274 72 72 SER H H 8.07 0.02 1 275 72 72 SER CA C 55.51 0.05 1 276 72 72 SER CB C 64.82 0.05 1 277 72 72 SER N N 115.54 0.05 1 278 73 73 GLN H H 8.38 0.02 1 279 73 73 GLN CA C 54.87 0.05 1 280 73 73 GLN CB C 29.40 0.05 1 281 73 73 GLN N N 119.90 0.05 1 282 74 74 GLN H H 8.40 0.02 1 283 74 74 GLN CA C 55.13 0.05 1 284 74 74 GLN CB C 29.65 0.05 1 285 74 74 GLN N N 122.38 0.05 1 286 75 75 GLY H H 8.63 0.02 1 287 75 75 GLY CA C 44.75 0.05 1 288 75 75 GLY N N 115.53 0.05 1 289 76 76 PRO CA C 62.37 0.05 1 290 76 76 PRO CB C 33.27 0.05 1 291 77 77 ARG H H 8.01 0.02 1 292 77 77 ARG CA C 53.06 0.05 1 293 77 77 ARG CB C 33.79 0.05 1 294 77 77 ARG N N 119.74 0.05 1 295 78 78 PHE H H 7.96 0.02 1 296 78 78 PHE CA C 56.42 0.05 1 297 78 78 PHE CB C 42.33 0.05 1 298 78 78 PHE N N 121.44 0.05 1 299 79 79 ALA H H 9.70 0.02 1 300 79 79 ALA CA C 50.34 0.05 1 301 79 79 ALA CB C 21.25 0.05 1 302 79 79 ALA N N 128.00 0.05 1 303 80 80 GLY H H 8.18 0.02 1 304 80 80 GLY CA C 44.27 0.05 1 305 80 80 GLY N N 110.68 0.05 1 306 81 81 SER H H 8.78 0.02 1 307 81 81 SER CA C 56.16 0.05 1 308 81 81 SER CB C 63.53 0.05 1 309 81 81 SER N N 114.21 0.05 1 310 82 82 PRO CA C 62.24 0.05 1 311 82 82 PRO CB C 29.78 0.05 1 312 83 83 LEU H H 6.70 0.02 1 313 83 83 LEU CA C 52.41 0.05 1 314 83 83 LEU CB C 39.74 0.05 1 315 83 83 LEU N N 114.25 0.05 1 316 84 84 GLY H H 8.31 0.02 1 317 84 84 GLY CA C 47.11 0.05 1 318 84 84 GLY N N 108.22 0.05 1 319 85 85 HIS H H 8.83 0.02 1 320 85 85 HIS CA C 58.10 0.05 1 321 85 85 HIS CB C 29.53 0.05 1 322 85 85 HIS N N 124.47 0.05 1 323 86 86 GLU H H 8.28 0.02 1 324 86 86 GLU CA C 54.74 0.05 1 325 86 86 GLU CB C 26.94 0.05 1 326 86 86 GLU N N 113.11 0.05 1 327 87 87 PHE H H 7.36 0.02 1 328 87 87 PHE CA C 61.72 0.05 1 329 87 87 PHE CB C 38.71 0.05 1 330 87 87 PHE N N 124.15 0.05 1 331 88 88 THR H H 8.10 0.02 1 332 88 88 THR CA C 65.86 0.05 1 333 88 88 THR CB C 68.19 0.05 1 334 88 88 THR N N 112.36 0.05 1 335 89 89 SER H H 6.94 0.02 1 336 89 89 SER CA C 60.17 0.05 1 337 89 89 SER CB C 62.37 0.05 1 338 89 89 SER N N 114.98 0.05 1 339 90 90 LEU H H 8.21 0.02 1 340 90 90 LEU CA C 58.62 0.05 1 341 90 90 LEU CB C 40.00 0.05 1 342 90 90 LEU N N 126.65 0.05 1 343 91 91 VAL H H 7.82 0.02 1 344 91 91 VAL CA C 67.29 0.05 1 345 91 91 VAL CB C 30.94 0.05 1 346 91 91 VAL N N 118.26 0.05 1 347 92 92 LEU H H 7.81 0.02 1 348 92 92 LEU CA C 57.32 0.05 1 349 92 92 LEU CB C 40.26 0.05 1 350 92 92 LEU N N 116.41 0.05 1 351 93 93 ALA H H 7.20 0.02 1 352 93 93 ALA CA C 55.65 0.05 1 353 93 93 ALA CB C 18.66 0.05 1 354 93 93 ALA N N 116.85 0.05 1 355 94 94 LEU H H 7.83 0.02 1 356 94 94 LEU CA C 59.27 0.05 1 357 94 94 LEU CB C 41.94 0.05 1 358 94 94 LEU N N 119.71 0.05 1 359 95 95 LEU H H 7.98 0.02 1 360 95 95 LEU CA C 58.10 0.05 1 361 95 95 LEU CB C 40.77 0.05 1 362 95 95 LEU N N 118.26 0.05 1 363 96 96 TRP H H 9.13 0.02 1 364 96 96 TRP CA C 57.33 0.05 1 365 96 96 TRP CB C 29.26 0.05 1 366 96 96 TRP N N 119.36 0.05 1 367 97 97 THR H H 7.97 0.02 1 368 97 97 THR CA C 68.45 0.05 1 369 97 97 THR CB C 67.54 0.05 1 370 97 97 THR N N 118.94 0.05 1 371 98 98 GLY H H 8.13 0.02 1 372 98 98 GLY CA C 46.02 0.05 1 373 98 98 GLY N N 109.44 0.05 1 374 99 99 GLY H H 7.38 0.02 1 375 99 99 GLY CA C 45.17 0.05 1 376 99 99 GLY N N 106.08 0.05 1 377 100 100 HIS H H 8.78 0.02 1 378 100 100 HIS CA C 54.61 0.05 1 379 100 100 HIS CB C 32.24 0.05 1 380 100 100 HIS N N 125.77 0.05 1 381 101 101 PRO CA C 62.89 0.05 1 382 101 101 PRO CB C 32.37 0.05 1 383 102 102 SER H H 8.42 0.02 1 384 102 102 SER CA C 58.23 0.05 1 385 102 102 SER CB C 64.18 0.05 1 386 102 102 SER N N 116.24 0.05 1 387 103 103 LYS H H 8.52 0.02 1 388 103 103 LYS CA C 55.78 0.05 1 389 103 103 LYS CB C 31.98 0.05 1 390 103 103 LYS N N 121.34 0.05 1 391 104 104 GLU H H 7.45 0.02 1 392 104 104 GLU CA C 55.39 0.05 1 393 104 104 GLU CB C 29.39 0.05 1 394 104 104 GLU N N 119.15 0.05 1 395 105 105 ALA H H 8.77 0.02 1 396 105 105 ALA CA C 52.03 0.05 1 397 105 105 ALA CB C 18.79 0.05 1 398 105 105 ALA N N 122.31 0.05 1 399 106 106 GLN H H 8.63 0.02 1 400 106 106 GLN CA C 59.01 0.05 1 401 106 106 GLN CB C 28.10 0.05 1 402 106 106 GLN N N 122.96 0.05 1 403 107 107 SER H H 8.48 0.02 1 404 107 107 SER CA C 60.56 0.05 1 405 107 107 SER CB C 61.72 0.05 1 406 107 107 SER N N 111.56 0.05 1 407 108 108 LEU H H 6.90 0.02 1 408 108 108 LEU CA C 56.81 0.05 1 409 108 108 LEU CB C 42.07 0.05 1 410 108 108 LEU N N 125.14 0.05 1 411 109 109 LEU H H 7.69 0.02 1 412 109 109 LEU CA C 58.23 0.05 1 413 109 109 LEU CB C 40.26 0.05 1 414 109 109 LEU N N 118.47 0.05 1 415 110 110 GLU H H 8.23 0.02 1 416 110 110 GLU CA C 59.27 0.05 1 417 110 110 GLU CB C 29.13 0.05 1 418 110 110 GLU N N 117.86 0.05 1 419 111 111 GLN H H 7.49 0.02 1 420 111 111 GLN CA C 59.01 0.05 1 421 111 111 GLN CB C 28.10 0.05 1 422 111 111 GLN N N 118.82 0.05 1 423 112 112 ILE H H 8.06 0.02 1 424 112 112 ILE CA C 65.09 0.05 1 425 112 112 ILE CB C 37.80 0.05 1 426 112 112 ILE N N 117.94 0.05 1 427 113 113 ARG H H 7.95 0.02 1 428 113 113 ARG CA C 59.78 0.05 1 429 113 113 ARG CB C 30.30 0.05 1 430 113 113 ARG N N 120.16 0.05 1 431 114 114 ASP H H 7.44 0.02 1 432 114 114 ASP CA C 54.35 0.05 1 433 114 114 ASP CB C 41.03 0.05 1 434 114 114 ASP N N 115.60 0.05 1 435 115 115 ILE H H 7.06 0.02 1 436 115 115 ILE CA C 64.57 0.05 1 437 115 115 ILE CB C 38.32 0.05 1 438 115 115 ILE N N 122.15 0.05 1 439 116 116 ASP H H 8.69 0.02 1 440 116 116 ASP CA C 52.54 0.05 1 441 116 116 ASP CB C 41.42 0.05 1 442 116 116 ASP N N 129.95 0.05 1 443 117 117 GLY H H 7.09 0.02 1 444 117 117 GLY CA C 44.65 0.05 1 445 117 117 GLY N N 108.38 0.05 1 446 118 118 ASP H H 7.15 0.02 1 447 118 118 ASP CA C 53.70 0.05 1 448 118 118 ASP CB C 42.46 0.05 1 449 118 118 ASP N N 115.67 0.05 1 450 119 119 PHE H H 8.07 0.02 1 451 119 119 PHE CA C 57.07 0.05 1 452 119 119 PHE CB C 43.36 0.05 1 453 119 119 PHE N N 120.66 0.05 1 454 120 120 GLU H H 8.43 0.02 1 455 120 120 GLU CA C 54.74 0.05 1 456 120 120 GLU CB C 29.52 0.05 1 457 120 120 GLU N N 123.69 0.05 1 458 121 121 PHE H H 9.32 0.02 1 459 121 121 PHE CA C 57.85 0.05 1 460 121 121 PHE CB C 42.84 0.05 1 461 121 121 PHE N N 126.69 0.05 1 462 122 122 GLU H H 9.43 0.02 1 463 122 122 GLU CA C 55.00 0.05 1 464 122 122 GLU CB C 34.57 0.05 1 465 122 122 GLU N N 124.58 0.05 1 466 123 123 THR H H 8.39 0.02 1 467 123 123 THR CA C 61.80 0.05 1 468 123 123 THR CB C 69.21 0.05 1 469 123 123 THR N N 120.56 0.05 1 470 124 124 TYR H H 9.50 0.02 1 471 124 124 TYR CA C 58.49 0.05 1 472 124 124 TYR CB C 40.51 0.05 1 473 124 124 TYR N N 125.64 0.05 1 474 125 125 TYR H H 8.91 0.02 1 475 125 125 TYR CA C 54.48 0.05 1 476 125 125 TYR CB C 43.49 0.05 1 477 125 125 TYR N N 116.34 0.05 1 478 126 126 SER H H 7.35 0.02 1 479 126 126 SER CA C 55.13 0.05 1 480 126 126 SER CB C 65.99 0.05 1 481 126 126 SER N N 112.59 0.05 1 482 127 127 LEU H H 9.92 0.02 1 483 127 127 LEU CA C 59.53 0.05 1 484 127 127 LEU CB C 42.45 0.05 1 485 127 127 LEU N N 131.00 0.05 1 486 128 128 SER H H 7.93 0.02 1 487 128 128 SER CA C 58.36 0.05 1 488 128 128 SER CB C 63.79 0.05 1 489 128 128 SER N N 109.67 0.05 1 490 129 129 CYS H H 7.13 0.02 1 491 129 129 CYS CA C 60.69 0.05 1 492 129 129 CYS CB C 32.24 0.05 1 493 129 129 CYS N N 124.49 0.05 1 494 130 130 HIS H H 7.54 0.02 1 495 130 130 HIS CA C 59.16 0.05 1 496 130 130 HIS CB C 30.04 0.05 1 497 130 130 HIS N N 116.63 0.05 1 498 131 131 ASN H H 7.66 0.02 1 499 131 131 ASN CA C 57.84 0.05 1 500 131 131 ASN CB C 41.55 0.05 1 501 131 131 ASN N N 119.43 0.05 1 502 132 132 CYS H H 8.14 0.02 1 503 132 132 CYS CA C 58.62 0.05 1 504 132 132 CYS CB C 39.74 0.05 1 505 132 132 CYS N N 116.84 0.05 1 506 133 133 PRO CA C 67.16 0.05 1 507 133 133 PRO CB C 30.30 0.05 1 508 134 134 ASP H H 7.88 0.02 1 509 134 134 ASP CA C 57.85 0.05 1 510 134 134 ASP CB C 40.90 0.05 1 511 134 134 ASP N N 114.11 0.05 1 512 135 135 VAL H H 7.04 0.02 1 513 135 135 VAL CA C 66.38 0.05 1 514 135 135 VAL CB C 32.63 0.05 1 515 135 135 VAL N N 119.42 0.05 1 516 136 136 VAL H H 7.88 0.02 1 517 136 136 VAL CA C 66.64 0.05 1 518 136 136 VAL CB C 32.63 0.05 1 519 136 136 VAL N N 118.54 0.05 1 520 137 137 GLN H H 8.70 0.02 1 521 137 137 GLN CA C 58.75 0.05 1 522 137 137 GLN CB C 28.36 0.05 1 523 137 137 GLN N N 115.67 0.05 1 524 138 138 ALA H H 7.32 0.02 1 525 138 138 ALA CA C 55.00 0.05 1 526 138 138 ALA CB C 19.05 0.05 1 527 138 138 ALA N N 121.54 0.05 1 528 139 139 LEU H H 7.21 0.02 1 529 139 139 LEU CA C 57.07 0.05 1 530 139 139 LEU CB C 37.41 0.05 1 531 139 139 LEU N N 116.44 0.05 1 532 140 140 ASN H H 8.34 0.02 1 533 140 140 ASN CA C 55.39 0.05 1 534 140 140 ASN CB C 37.28 0.05 1 535 140 140 ASN N N 117.45 0.05 1 536 141 141 LEU H H 8.15 0.02 1 537 141 141 LEU CA C 57.97 0.05 1 538 141 141 LEU CB C 40.00 0.05 1 539 141 141 LEU N N 121.34 0.05 1 540 142 142 MET H H 7.35 0.02 1 541 142 142 MET CA C 60.56 0.05 1 542 142 142 MET CB C 33.66 0.05 1 543 142 142 MET N N 115.95 0.05 1 544 143 143 ALA H H 7.38 0.02 1 545 143 143 ALA CA C 53.58 0.05 1 546 143 143 ALA CB C 18.41 0.05 1 547 143 143 ALA N N 118.06 0.05 1 548 144 144 VAL H H 7.94 0.02 1 549 144 144 VAL CA C 65.60 0.05 1 550 144 144 VAL CB C 31.80 0.05 1 551 144 144 VAL N N 118.34 0.05 1 552 145 145 LEU H H 7.62 0.02 1 553 145 145 LEU CA C 56.18 0.05 1 554 145 145 LEU CB C 44.10 0.05 1 555 145 145 LEU N N 116.97 0.05 1 556 146 146 ASN H H 7.93 0.02 1 557 146 146 ASN CA C 49.24 0.05 1 558 146 146 ASN CB C 41.12 0.05 1 559 146 146 ASN N N 118.21 0.05 1 560 147 147 PRO CA C 63.79 0.05 1 561 147 147 PRO CB C 31.80 0.05 1 562 148 148 ARG H H 8.42 0.02 1 563 148 148 ARG CA C 57.07 0.05 1 564 148 148 ARG CB C 30.30 0.05 1 565 148 148 ARG N N 118.25 0.05 1 566 149 149 ILE H H 8.10 0.02 1 567 149 149 ILE CA C 60.04 0.05 1 568 149 149 ILE CB C 37.15 0.05 1 569 149 149 ILE N N 121.83 0.05 1 570 150 150 LYS H H 8.92 0.02 1 571 150 150 LYS CA C 54.22 0.05 1 572 150 150 LYS CB C 34.69 0.05 1 573 150 150 LYS N N 125.64 0.05 1 574 151 151 HIS H H 8.88 0.02 1 575 151 151 HIS CA C 55.26 0.05 1 576 151 151 HIS CB C 33.02 0.05 1 577 151 151 HIS N N 119.72 0.05 1 578 152 152 THR H H 7.80 0.02 1 579 152 152 THR CA C 60.82 0.05 1 580 152 152 THR CB C 69.61 0.05 1 581 152 152 THR N N 126.99 0.05 1 582 153 153 ALA H H 8.48 0.02 1 583 153 153 ALA CA C 49.70 0.05 1 584 153 153 ALA CB C 19.30 0.05 1 585 153 153 ALA N N 131.47 0.05 1 586 154 154 ILE H H 9.65 0.02 1 587 154 154 ILE CA C 60.95 0.05 1 588 154 154 ILE CB C 40.26 0.05 1 589 154 154 ILE N N 126.04 0.05 1 590 155 155 ASP H H 8.45 0.02 1 591 155 155 ASP CA C 52.67 0.05 1 592 155 155 ASP CB C 41.94 0.05 1 593 155 155 ASP N N 125.88 0.05 1 594 156 156 GLY H H 9.36 0.02 1 595 156 156 GLY CA C 46.98 0.05 1 596 156 156 GLY N N 119.79 0.05 1 597 157 157 GLY H H 8.49 0.02 1 598 157 157 GLY CA C 46.08 0.05 1 599 157 157 GLY N N 105.91 0.05 1 600 158 158 THR H H 7.27 0.02 1 601 158 158 THR CA C 64.83 0.05 1 602 158 158 THR CB C 69.10 0.05 1 603 158 158 THR N N 116.79 0.05 1 604 159 159 PHE H H 7.68 0.02 1 605 159 159 PHE CA C 57.07 0.05 1 606 159 159 PHE CB C 37.15 0.05 1 607 159 159 PHE N N 122.56 0.05 1 608 160 160 GLN H H 7.47 0.02 1 609 160 160 GLN CA C 59.14 0.05 1 610 160 160 GLN CB C 28.75 0.05 1 611 160 160 GLN N N 120.29 0.05 1 612 161 161 ASN H H 8.82 0.02 1 613 161 161 ASN CA C 56.42 0.05 1 614 161 161 ASN CB C 36.76 0.05 1 615 161 161 ASN N N 116.47 0.05 1 616 162 162 GLU H H 7.45 0.02 1 617 162 162 GLU CA C 59.40 0.05 1 618 162 162 GLU CB C 29.78 0.05 1 619 162 162 GLU N N 119.52 0.05 1 620 163 163 ILE H H 6.89 0.02 1 621 163 163 ILE CA C 62.11 0.05 1 622 163 163 ILE CB C 35.73 0.05 1 623 163 163 ILE N N 117.85 0.05 1 624 164 164 THR H H 7.44 0.02 1 625 164 164 THR CA C 65.60 0.05 1 626 164 164 THR CB C 68.44 0.05 1 627 164 164 THR N N 113.12 0.05 1 628 165 165 GLU H H 8.28 0.02 1 629 165 165 GLU CA C 59.52 0.05 1 630 165 165 GLU CB C 30.04 0.05 1 631 165 165 GLU N N 122.92 0.05 1 632 166 166 ARG H H 7.88 0.02 1 633 166 166 ARG CA C 55.78 0.05 1 634 166 166 ARG CB C 30.56 0.05 1 635 166 166 ARG N N 114.17 0.05 1 636 167 167 ASN H H 7.62 0.02 1 637 167 167 ASN CA C 53.97 0.05 1 638 167 167 ASN CB C 37.15 0.05 1 639 167 167 ASN N N 117.05 0.05 1 640 168 168 VAL H H 8.08 0.02 1 641 168 168 VAL CA C 63.79 0.05 1 642 168 168 VAL CB C 31.33 0.05 1 643 168 168 VAL N N 118.75 0.05 1 644 169 169 MET H H 8.85 0.02 1 645 169 169 MET CA C 55.00 0.05 1 646 169 169 MET CB C 32.88 0.05 1 647 169 169 MET N N 128.57 0.05 1 648 170 170 GLY H H 7.55 0.02 1 649 170 170 GLY CA C 44.78 0.05 1 650 170 170 GLY N N 108.62 0.05 1 651 171 171 VAL H H 8.11 0.02 1 652 171 171 VAL CA C 57.84 0.05 1 653 171 171 VAL CB C 33.15 0.05 1 654 171 171 VAL N N 109.96 0.05 1 655 172 172 PRO CA C 62.24 0.05 1 656 172 172 PRO CB C 34.31 0.05 1 657 173 173 ALA H H 8.07 0.02 1 658 173 173 ALA CA C 51.89 0.05 1 659 173 173 ALA CB C 22.67 0.05 1 660 173 173 ALA N N 125.56 0.05 1 661 174 174 VAL H H 8.87 0.02 1 662 174 174 VAL CA C 61.08 0.05 1 663 174 174 VAL CB C 34.69 0.05 1 664 174 174 VAL N N 122.40 0.05 1 665 175 175 PHE H H 10.25 0.02 1 666 175 175 PHE CA C 56.81 0.05 1 667 175 175 PHE CB C 42.71 0.05 1 668 175 175 PHE N N 131.14 0.05 1 669 176 176 VAL H H 9.90 0.02 1 670 176 176 VAL CA C 58.88 0.05 1 671 176 176 VAL CB C 34.96 0.05 1 672 176 176 VAL N N 120.53 0.05 1 673 177 177 ASN H H 9.20 0.02 1 674 177 177 ASN CA C 53.97 0.05 1 675 177 177 ASN CB C 36.89 0.05 1 676 177 177 ASN N N 128.25 0.05 1 677 178 178 GLY H H 9.05 0.02 1 678 178 178 GLY CA C 45.56 0.05 1 679 178 178 GLY N N 102.39 0.05 1 680 179 179 LYS H H 8.28 0.02 1 681 179 179 LYS CA C 54.35 0.05 1 682 179 179 LYS CB C 35.47 0.05 1 683 179 179 LYS N N 121.26 0.05 1 684 180 180 GLU H H 9.24 0.02 1 685 180 180 GLU CA C 60.17 0.05 1 686 180 180 GLU CB C 29.61 0.05 1 687 180 180 GLU N N 123.25 0.05 1 688 181 181 PHE H H 8.93 0.02 1 689 181 181 PHE CA C 58.36 0.05 1 690 181 181 PHE CB C 41.81 0.05 1 691 181 181 PHE N N 125.51 0.05 1 692 182 182 GLY H H 7.72 0.02 1 693 182 182 GLY CA C 45.69 0.05 1 694 182 182 GLY N N 104.51 0.05 1 695 183 183 GLN H H 8.31 0.02 1 696 183 183 GLN CA C 54.61 0.05 1 697 183 183 GLN CB C 31.98 0.05 1 698 183 183 GLN N N 119.46 0.05 1 699 184 184 GLY H H 8.24 0.02 1 700 184 184 GLY CA C 44.14 0.05 1 701 184 184 GLY N N 109.46 0.05 1 702 185 185 ARG H H 8.20 0.02 1 703 185 185 ARG CA C 58.23 0.05 1 704 185 185 ARG CB C 30.30 0.05 1 705 185 185 ARG N N 116.85 0.05 1 706 186 186 MET H H 6.85 0.02 1 707 186 186 MET CA C 50.09 0.05 1 708 186 186 MET CB C 38.07 0.05 1 709 186 186 MET N N 122.72 0.05 1 710 187 187 THR H H 8.209 0.02 1 711 187 187 THR CA C 59.27 0.05 1 712 187 187 THR CB C 71.55 0.05 1 713 187 187 THR N N 110.56 0.05 1 714 188 188 LEU H H 8.98 0.02 1 715 188 188 LEU CA C 58.62 0.05 1 716 188 188 LEU CB C 41.42 0.05 1 717 188 188 LEU N N 121.29 0.05 1 718 189 189 THR H H 8.02 0.02 1 719 189 189 THR CA C 66.90 0.05 1 720 189 189 THR CB C 68.58 0.05 1 721 189 189 THR N N 110.96 0.05 1 722 190 190 GLU H H 7.40 0.02 1 723 190 190 GLU CA C 58.88 0.05 1 724 190 190 GLU CB C 30.30 0.05 1 725 190 190 GLU N N 122.04 0.05 1 726 191 191 ILE H H 8.20 0.02 1 727 191 191 ILE CA C 66.38 0.05 1 728 191 191 ILE CB C 38.57 0.05 1 729 191 191 ILE N N 120.79 0.05 1 730 192 192 VAL H H 8.27 0.02 1 731 192 192 VAL CA C 66.89 0.05 1 732 192 192 VAL CB C 31.72 0.05 1 733 192 192 VAL N N 118.26 0.05 1 734 193 193 ALA H H 7.59 0.02 1 735 193 193 ALA CA C 54.35 0.05 1 736 193 193 ALA CB C 18.27 0.05 1 737 193 193 ALA N N 119.25 0.05 1 738 194 194 LYS H H 7.48 0.02 1 739 194 194 LYS CA C 58.23 0.05 1 740 194 194 LYS CB C 33.66 0.05 1 741 194 194 LYS N N 116.32 0.05 1 742 195 195 VAL H H 7.69 0.02 1 743 195 195 VAL CA C 63.54 0.05 1 744 195 195 VAL CB C 31.98 0.05 1 745 195 195 VAL N N 116.55 0.05 1 746 196 196 ASP H H 8.08 0.02 1 747 196 196 ASP CA C 54.22 0.05 1 748 196 196 ASP CB C 41.29 0.05 1 749 196 196 ASP N N 121.67 0.05 1 750 197 197 THR H H 7.97 0.02 1 751 197 197 THR CA C 62.37 0.05 1 752 197 197 THR CB C 69.61 0.05 1 753 197 197 THR N N 114.05 0.05 1 754 198 198 GLY H H 8.42 0.02 1 755 198 198 GLY CA C 45.56 0.05 1 756 198 198 GLY N N 111.21 0.05 1 757 199 199 ALA H H 7.95 0.02 1 758 199 199 ALA CA C 52.67 0.05 1 759 199 199 ALA CB C 19.43 0.05 1 760 199 199 ALA N N 123.63 0.05 1 761 200 200 GLU H H 8.33 0.02 1 762 200 200 GLU CA C 56.55 0.05 1 763 200 200 GLU CB C 30.30 0.05 1 764 200 200 GLU N N 119.47 0.05 1 765 201 201 LYS H H 8.19 0.02 1 766 201 201 LYS CA C 56.03 0.05 1 767 201 201 LYS CB C 32.75 0.05 1 768 201 201 LYS N N 123.10 0.05 1 769 202 202 ARG H H 7.90 0.02 1 770 202 202 ARG CA C 57.32 0.05 1 771 202 202 ARG CB C 31.59 0.05 1 772 202 202 ARG N N 128.23 0.05 1 stop_ save_