data_5062 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignment for Unfolded HIV-1 protease tethered dimer ; _BMRB_accession_number 5062 _BMRB_flat_file_name bmr5062.str _Entry_type original _Submission_date 2001-06-19 _Accession_date 2001-06-19 _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 Bhavesh Neel Sarovar . 2 Panchal Sanjay C. . 3 Mittal Rohit . . 4 Hosur Ramkrishna V. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 "13C chemical shifts" 569 "15N chemical shifts" 191 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-01-23 original author . stop_ _Original_release_date 2002-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Identification of local Structural Preferences in HIV-I Protease Tethered Heterodimer in 6 M Guanidine Hydrochloride ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21617172 _PubMed_ID 11741592 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhavesh Neel Sarovar . 2 Panchal Sanjay C. . 3 Mittal Rohit . . 4 Hosur Ramkrishna V. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 509 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 218 _Page_last 224 _Year 2001 _Details . loop_ _Keyword 'denatured/unfolded protein' 'Guanidine hydrochloride' 'HIV-1 protease' HN(C)N HNN 'residual structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_HIV-1_protease _Saveframe_category molecular_system _Mol_system_name 'HIV-1 protease tethered dimer' _Abbreviation_common 'HIV-1 protease' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HIV-1 protease' $HIV-1_protease stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HIV-1_protease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'HIV-1 protease' _Name_variant 'C95M, C195A' _Abbreviation_common Protease _Molecular_mass 21971 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 203 _Mol_residue_sequence ; PQVTLWQRPLVTIKIGGQLK EALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYD QILIEICAHKAIGTVLVGPT PVNIIGRNLLTQIGMTLNFG GSSGPQVTLWQRPLVTIKIG GQLKEALLDTGADDTVLEEM SLPGRWKPKMIGGIGGFIKV RQYDQILIEICAHKAIGTVL VGPTPVNIIGRNLLTQIGAT LNF ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 GLN 3 VAL 4 THR 5 LEU 6 TRP 7 GLN 8 ARG 9 PRO 10 LEU 11 VAL 12 THR 13 ILE 14 LYS 15 ILE 16 GLY 17 GLY 18 GLN 19 LEU 20 LYS 21 GLU 22 ALA 23 LEU 24 LEU 25 ASP 26 THR 27 GLY 28 ALA 29 ASP 30 ASP 31 THR 32 VAL 33 LEU 34 GLU 35 GLU 36 MET 37 SER 38 LEU 39 PRO 40 GLY 41 ARG 42 TRP 43 LYS 44 PRO 45 LYS 46 MET 47 ILE 48 GLY 49 GLY 50 ILE 51 GLY 52 GLY 53 PHE 54 ILE 55 LYS 56 VAL 57 ARG 58 GLN 59 TYR 60 ASP 61 GLN 62 ILE 63 LEU 64 ILE 65 GLU 66 ILE 67 CYS 68 ALA 69 HIS 70 LYS 71 ALA 72 ILE 73 GLY 74 THR 75 VAL 76 LEU 77 VAL 78 GLY 79 PRO 80 THR 81 PRO 82 VAL 83 ASN 84 ILE 85 ILE 86 GLY 87 ARG 88 ASN 89 LEU 90 LEU 91 THR 92 GLN 93 ILE 94 GLY 95 MET 96 THR 97 LEU 98 ASN 99 PHE 100 GLY 101 GLY 102 SER 103 SER 104 GLY 105 PRO 106 GLN 107 VAL 108 THR 109 LEU 110 TRP 111 GLN 112 ARG 113 PRO 114 LEU 115 VAL 116 THR 117 ILE 118 LYS 119 ILE 120 GLY 121 GLY 122 GLN 123 LEU 124 LYS 125 GLU 126 ALA 127 LEU 128 LEU 129 ASP 130 THR 131 GLY 132 ALA 133 ASP 134 ASP 135 THR 136 VAL 137 LEU 138 GLU 139 GLU 140 MET 141 SER 142 LEU 143 PRO 144 GLY 145 ARG 146 TRP 147 LYS 148 PRO 149 LYS 150 MET 151 ILE 152 GLY 153 GLY 154 ILE 155 GLY 156 GLY 157 PHE 158 ILE 159 LYS 160 VAL 161 ARG 162 GLN 163 TYR 164 ASP 165 GLN 166 ILE 167 LEU 168 ILE 169 GLU 170 ILE 171 CYS 172 ALA 173 HIS 174 LYS 175 ALA 176 ILE 177 GLY 178 THR 179 VAL 180 LEU 181 VAL 182 GLY 183 PRO 184 THR 185 PRO 186 VAL 187 ASN 188 ILE 189 ILE 190 GLY 191 ARG 192 ASN 193 LEU 194 LEU 195 THR 196 GLN 197 ILE 198 GLY 199 ALA 200 THR 201 LEU 202 ASN 203 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 4356 HIV-1_protease 100.00 203 98.03 98.03 5.12e-136 PDB 1G6L "1.9a Crystal Structure Of Tethered Hiv-1 Protease" 100.00 203 98.52 98.52 3.75e-137 PDB 1LV1 "Crystal Structure Analysis Of The Non-Active Site Mutant Of Tethered Hiv-1 Protease To 2.1a Resolution" 100.00 203 99.01 99.01 4.60e-138 PDB 2WHH "Hiv-1 Protease Tethered Dimer Q-Product Complex Along With Nucleophilic Water Molecule" 100.00 203 99.01 99.01 4.60e-138 PDB 3DOX "X-Ray Structure Of Hiv-1 Protease In Situ Product Complex" 100.00 203 99.01 99.01 4.60e-138 PDB 3KT2 "Crystal Structure Of N88d Mutant Hiv-1 Protease" 100.00 203 97.54 98.52 7.03e-136 PDB 3KT5 "Crystal Structure Of N88s Mutant Hiv-1 Protease" 100.00 203 97.54 98.52 1.02e-135 PDB 3N3I "Crystal Structure Of G48v/c95f Tethered Hiv-1 Protease/saquinavir Complex" 100.00 203 97.04 97.04 5.45e-134 PDB 4QLH "Crystal Structure Of Drug Resistant V82s/v1082s Hiv-1 Protease" 100.00 203 97.54 97.54 7.92e-136 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _ATCC_number _Gene_mnemonic $HIV-1_protease HIV-1 11676 Viruses . Lentivirus Lentivirus 11676 gag-pol stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _ATCC_number _Vector_type _Vector_name $HIV-1_protease 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) 37762 plasmid pET11a 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 $HIV-1_protease 1.2 mM '[U-95% 13C; U-90% 15N]' 'guanidine hydrochloride' 6 M . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Two_new_pulse_sequences_HNN,_HN(C)N_were_used_to_get_HN,_NH_assignments_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Two new pulse sequences HNN, HN(C)N were used to get HN, NH assignments' _Sample_label $sample_1 save_ save_in_this_poorly_amide_proton_dispersed_spectra_in_unfolded_condition._2 _Saveframe_category NMR_applied_experiment _Experiment_name 'in this poorly amide proton dispersed spectra in unfolded condition.' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 0.1 n/a temperature 305 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 external indirect cylindrical external parallel 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external parallel 0.10132905 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'HIV-1 protease' _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 PRO CB C 37.23 0.10 1 2 . 1 PRO C C 176.69 0.10 1 3 . 1 PRO CA C 56.20 0.10 1 4 . 2 GLN H H 8.72 0.02 1 5 . 2 GLN CB C 33.57 0.10 1 6 . 2 GLN C C 176.05 0.10 1 7 . 2 GLN CA C 53.15 0.10 1 8 . 2 GLN N N 120.53 0.05 1 9 . 3 VAL H H 8.34 0.02 1 10 . 3 VAL CB C 33.92 0.10 1 11 . 3 VAL C C 176.23 0.10 1 12 . 3 VAL CA C 60.63 0.10 1 13 . 3 VAL N N 120.58 0.05 1 14 . 4 THR H H 8.39 0.02 1 15 . 4 THR CB C 70.02 0.10 1 16 . 4 THR C C 177.02 0.10 1 17 . 4 THR CA C 61.38 0.10 1 18 . 4 THR N N 118.98 0.05 1 19 . 5 LEU H H 8.61 0.03 1 20 . 5 LEU CB C 43.63 0.10 1 21 . 5 LEU C C 175.34 0.10 1 22 . 5 LEU CA C 52.84 0.10 1 23 . 5 LEU N N 122.41 0.10 1 24 . 6 TRP H H 8.45 0.02 1 25 . 6 TRP CB C 31.92 0.10 1 26 . 6 TRP C C 177.27 0.10 1 27 . 6 TRP CA C 57.65 0.10 1 28 . 6 TRP N N 121.84 0.05 1 29 . 7 GLN H H 8.53 0.02 1 30 . 7 GLN CB C 31.27 0.10 1 31 . 7 GLN C C 176.37 0.10 1 32 . 7 GLN CA C 52.68 0.10 1 33 . 7 GLN N N 120.64 0.05 1 34 . 8 ARG H H 7.98 0.02 1 35 . 8 ARG CB C 31.27 0.10 1 36 . 8 ARG CA C 59.21 0.10 1 37 . 8 ARG N N 126.14 0.05 1 38 . 9 PRO CB C 32.28 0.10 1 39 . 9 PRO C C 177.60 0.10 1 40 . 9 PRO CA C 62.93 0.10 1 41 . 10 LEU H H 8.75 0.02 1 42 . 10 LEU CB C 43.48 0.10 1 43 . 10 LEU C C 177.40 0.10 1 44 . 10 LEU CA C 55.95 0.10 1 45 . 10 LEU N N 122.83 0.05 1 46 . 11 VAL H H 8.22 0.02 1 47 . 11 VAL CB C 32.98 0.10 1 48 . 11 VAL C C 176.63 0.10 1 49 . 11 VAL CA C 61.85 0.10 1 50 . 11 VAL N N 122.22 0.05 1 51 . 12 THR H H 8.36 0.02 1 52 . 12 THR CB C 69.67 0.10 1 53 . 12 THR C C 174.88 0.10 1 54 . 12 THR CA C 61.23 0.10 1 55 . 12 THR N N 118.76 0.05 1 56 . 13 ILE H H 8.31 0.02 1 57 . 13 ILE CB C 38.92 0.10 1 58 . 13 ILE C C 176.36 0.10 1 59 . 13 ILE CA C 60.76 0.10 1 60 . 13 ILE N N 124.63 0.05 1 61 . 14 LYS H H 8.56 0.02 1 62 . 14 LYS CB C 33.33 0.10 1 63 . 14 LYS C C 175.79 0.10 1 64 . 14 LYS CA C 55.95 0.10 1 65 . 14 LYS N N 126.72 0.05 1 66 . 15 ILE H H 8.45 0.02 1 67 . 15 ILE CB C 38.57 0.10 1 68 . 15 ILE C C 177.27 0.10 1 69 . 15 ILE CA C 61.07 0.10 1 70 . 15 ILE N N 124.11 0.05 1 71 . 16 GLY H H 8.67 0.02 1 72 . 16 GLY C C 175.07 0.10 1 73 . 16 GLY CA C 45.07 0.10 1 74 . 16 GLY N N 114.21 0.05 1 75 . 17 GLY H H 8.49 0.02 1 76 . 17 GLY C C 174.69 0.10 1 77 . 17 GLY CA C 45.07 0.10 1 78 . 17 GLY N N 109.95 0.05 1 79 . 18 GLN H H 8.56 0.02 1 80 . 18 GLN CB C 29.83 0.10 1 81 . 18 GLN C C 176.63 0.10 1 82 . 18 GLN CA C 55.79 0.10 1 83 . 18 GLN N N 120.97 0.05 1 84 . 19 LEU H H 8.50 0.02 1 85 . 19 LEU CB C 42.06 0.10 1 86 . 19 LEU C C 175.14 0.10 1 87 . 19 LEU CA C 55.01 0.10 1 88 . 19 LEU N N 124.37 0.05 1 89 . 20 LYS H H 8.56 0.02 1 90 . 20 LYS CB C 33.33 0.10 1 91 . 20 LYS C C 176.39 0.10 1 92 . 20 LYS CA C 56.05 0.10 1 93 . 20 LYS N N 123.41 0.05 1 94 . 21 GLU H H 8.61 0.02 1 95 . 21 GLU CB C 30.53 0.10 1 96 . 21 GLU C C 175.01 0.10 1 97 . 21 GLU CA C 55.25 0.10 1 98 . 21 GLU N N 122.84 0.05 1 99 . 22 ALA H H 8.46 0.02 1 100 . 22 ALA CB C 19.69 0.10 1 101 . 22 ALA C C 176.53 0.10 1 102 . 22 ALA CA C 52.06 0.10 1 103 . 22 ALA N N 125.33 0.05 1 104 . 23 LEU H H 8.34 0.02 1 105 . 23 LEU CB C 43.33 0.10 1 106 . 23 LEU C C 176.50 0.10 1 107 . 23 LEU CA C 54.86 0.10 1 108 . 23 LEU N N 122.60 0.05 1 109 . 24 LEU H H 8.43 0.02 1 110 . 24 LEU CB C 42.53 0.10 1 111 . 24 LEU C C 177.60 0.10 1 112 . 24 LEU CA C 57.07 0.10 1 113 . 24 LEU N N 123.30 0.05 1 114 . 25 ASP H H 8.58 0.02 1 115 . 25 ASP CB C 40.02 0.10 1 116 . 25 ASP C C 176.95 0.10 1 117 . 25 ASP CA C 52.84 0.10 1 118 . 25 ASP N N 122.21 0.05 1 119 . 26 THR H H 8.30 0.02 1 120 . 26 THR CB C 70.02 0.10 1 121 . 26 THR C C 175.91 0.10 1 122 . 26 THR CA C 61.54 0.10 1 123 . 26 THR N N 114.21 0.05 1 124 . 27 GLY H H 8.69 0.02 1 125 . 27 GLY C C 174.88 0.10 1 126 . 27 GLY CA C 45.23 0.10 1 127 . 27 GLY N N 111.89 0.05 1 128 . 28 ALA H H 8.32 0.02 1 129 . 28 ALA CB C 20.04 0.10 1 130 . 28 ALA C C 174.29 0.10 1 131 . 28 ALA CA C 52.37 0.10 1 132 . 28 ALA N N 124.37 0.05 1 133 . 29 ASP H H 8.55 0.02 1 134 . 29 ASP CB C 39.36 0.10 1 135 . 29 ASP C C 176.56 0.10 1 136 . 29 ASP CA C 54.06 0.10 1 137 . 29 ASP N N 119.20 0.05 1 138 . 30 ASP H H 8.54 0.02 1 139 . 30 ASP CB C 39.36 0.10 1 140 . 30 ASP C C 177.02 0.10 1 141 . 30 ASP CA C 54.48 0.10 1 142 . 30 ASP N N 121.54 0.05 1 143 . 31 THR H H 8.33 0.02 1 144 . 31 THR CB C 70.02 0.10 1 145 . 31 THR C C 177.47 0.10 1 146 . 31 THR CA C 62.00 0.10 1 147 . 31 THR N N 114.66 0.05 1 148 . 32 VAL H H 8.26 0.02 1 149 . 32 VAL CB C 33.73 0.10 1 150 . 32 VAL C C 175.89 0.10 1 151 . 32 VAL CA C 61.18 0.10 1 152 . 32 VAL N N 122.99 0.05 1 153 . 33 LEU H H 8.42 0.02 1 154 . 33 LEU CB C 43.38 0.10 1 155 . 33 LEU C C 177.18 0.10 1 156 . 33 LEU CA C 55.17 0.10 1 157 . 33 LEU N N 126.49 0.05 1 158 . 34 GLU H H 8.57 0.02 1 159 . 34 GLU CB C 30.36 0.10 1 160 . 34 GLU C C 175.86 0.10 1 161 . 34 GLU CA C 54.70 0.10 1 162 . 34 GLU N N 122.56 0.10 1 163 . 35 GLU H H 8.43 0.03 1 164 . 35 GLU CB C 29.83 0.10 1 165 . 35 GLU C C 175.83 0.10 1 166 . 35 GLU CA C 55.79 0.10 1 167 . 35 GLU N N 121.03 0.05 1 168 . 36 MET H H 8.37 0.02 1 169 . 36 MET CB C 34.41 0.10 1 170 . 36 MET C C 176.12 0.10 1 171 . 36 MET CA C 54.86 0.10 1 172 . 36 MET N N 122.75 0.05 1 173 . 37 SER H H 8.55 0.02 1 174 . 37 SER CB C 65.07 0.10 1 175 . 37 SER C C 174.22 0.10 1 176 . 37 SER CA C 56.93 0.10 1 177 . 37 SER N N 121.82 0.05 1 178 . 38 LEU H H 8.47 0.02 1 179 . 38 LEU CB C 42.06 0.10 1 180 . 38 LEU CA C 54.86 0.10 1 181 . 38 LEU N N 127.21 0.05 1 182 . 39 PRO CB C 32.27 0.10 1 183 . 39 PRO C C 177.92 0.10 1 184 . 39 PRO CA C 63.09 0.10 1 185 . 40 GLY H H 8.59 0.02 1 186 . 40 GLY C C 178.18 0.10 1 187 . 40 GLY CA C 45.23 0.10 1 188 . 40 GLY N N 110.17 0.05 1 189 . 41 ARG H H 8.33 0.02 1 190 . 41 ARG CB C 30.88 0.10 1 191 . 41 ARG C C 177.86 0.10 1 192 . 41 ARG CA C 55.94 0.10 1 193 . 41 ARG N N 121.53 0.05 1 194 . 42 TRP H H 8.47 0.02 1 195 . 42 TRP CB C 29.83 0.10 1 196 . 42 TRP C C 176.17 0.10 1 197 . 42 TRP CA C 57.34 0.10 1 198 . 42 TRP N N 123.24 0.05 1 199 . 43 LYS H H 8.08 0.02 1 200 . 43 LYS CB C 32.63 0.10 1 201 . 43 LYS CA C 53.61 0.10 1 202 . 43 LYS N N 125.48 0.05 1 203 . 44 PRO CB C 30.18 0.10 1 204 . 44 PRO C C 174.69 0.10 1 205 . 44 PRO CA C 56.25 0.10 1 206 . 45 LYS H H 8.42 0.02 1 207 . 45 LYS CB C 30.53 0.10 1 208 . 45 LYS C C 176.62 0.10 1 209 . 45 LYS CA C 51.91 0.10 1 210 . 45 LYS N N 125.76 0.05 1 211 . 46 MET H H 8.31 0.02 1 212 . 46 MET CB C 32.98 0.10 1 213 . 46 MET C C 175.60 0.10 1 214 . 46 MET CA C 54.86 0.10 1 215 . 46 MET N N 122.10 0.05 1 216 . 47 ILE H H 8.38 0.03 1 217 . 47 ILE CB C 38.57 0.10 1 218 . 47 ILE C C 177.27 0.10 1 219 . 47 ILE CA C 61.07 0.10 1 220 . 47 ILE N N 123.28 0.10 1 221 . 48 GLY H H 8.67 0.10 1 222 . 48 GLY C C 174.94 0.10 1 223 . 48 GLY CA C 44.92 0.10 1 224 . 48 GLY N N 114.03 0.05 1 225 . 49 GLY H H 8.44 0.02 1 226 . 49 GLY C C 174.75 0.10 1 227 . 49 GLY CA C 44.92 0.10 1 228 . 49 GLY N N 109.80 0.05 1 229 . 50 ILE H H 8.29 0.02 1 230 . 50 ILE CB C 38.57 0.10 1 231 . 50 ILE C C 177.27 0.10 1 232 . 50 ILE CA C 61.23 0.10 1 233 . 50 ILE N N 120.51 0.05 1 234 . 51 GLY H H 8.65 0.02 1 235 . 51 GLY C C 174.94 0.10 1 236 . 51 GLY CA C 45.07 0.10 1 237 . 51 GLY N N 113.40 0.05 1 238 . 52 GLY H H 8.37 0.02 1 239 . 52 GLY C C 178.18 0.10 1 240 . 52 GLY CA C 45.07 0.10 1 241 . 52 GLY N N 109.76 0.05 1 242 . 53 PHE H H 8.33 0.02 1 243 . 53 PHE CB C 39.96 0.10 1 244 . 53 PHE C C 176.17 0.10 1 245 . 53 PHE CA C 55.95 0.10 1 246 . 53 PHE N N 121.30 0.05 1 247 . 54 ILE H H 8.28 0.02 1 248 . 54 ILE CB C 37.62 0.10 1 249 . 54 ILE C C 174.62 0.10 1 250 . 54 ILE CA C 60.61 0.10 1 251 . 54 ILE N N 123.52 0.05 1 252 . 55 LYS H H 8.53 0.02 1 253 . 55 LYS CB C 34.41 0.10 1 254 . 55 LYS C C 175.40 0.10 1 255 . 55 LYS CA C 54.70 0.10 1 256 . 55 LYS N N 126.97 0.05 1 257 . 56 VAL H H 8.26 0.02 1 258 . 56 VAL CB C 32.98 0.10 1 259 . 56 VAL C C 176.50 0.10 1 260 . 56 VAL CA C 60.92 0.10 1 261 . 56 VAL N N 122.76 0.05 1 262 . 57 ARG H H 8.60 0.02 1 263 . 57 ARG CB C 30.88 0.10 1 264 . 57 ARG C C 176.62 0.10 1 265 . 57 ARG CA C 56.10 0.10 1 266 . 57 ARG N N 125.51 0.05 1 267 . 58 GLN H H 8.54 0.03 1 268 . 58 GLN CB C 29.83 0.10 1 269 . 58 GLN C C 176.24 0.10 1 270 . 58 GLN CA C 55.79 0.10 1 271 . 58 GLN N N 122.58 0.10 1 272 . 59 TYR H H 8.38 0.03 1 273 . 59 TYR CB C 37.18 0.10 1 274 . 59 TYR C C 177.11 0.10 1 275 . 59 TYR CA C 57.50 0.10 1 276 . 59 TYR N N 121.56 0.05 1 277 . 60 ASP H H 8.39 0.02 1 278 . 60 ASP CB C 38.92 0.10 1 279 . 60 ASP C C 176.17 0.10 1 280 . 60 ASP CA C 54.23 0.10 1 281 . 60 ASP N N 122.49 0.05 1 282 . 61 GLN H H 8.59 0.02 1 283 . 61 GLN CB C 32.98 0.10 1 284 . 61 GLN C C 177.62 0.10 1 285 . 61 GLN CA C 58.43 0.10 1 286 . 61 GLN N N 123.08 0.05 1 287 . 62 ILE H H 8.57 0.02 1 288 . 62 ILE CB C 39.83 0.10 1 289 . 62 ILE C C 177.53 0.10 1 290 . 62 ILE CA C 60.10 0.10 1 291 . 62 ILE N N 125.63 0.05 1 292 . 63 LEU H H 8.25 0.02 1 293 . 63 LEU CB C 42.98 0.10 1 294 . 63 LEU C C 176.69 0.10 1 295 . 63 LEU CA C 56.85 0.10 1 296 . 63 LEU N N 121.47 0.05 1 297 . 64 ILE H H 8.48 0.02 1 298 . 64 ILE CB C 38.56 0.10 1 299 . 64 ILE C C 174.43 0.10 1 300 . 64 ILE CA C 61.23 0.10 1 301 . 64 ILE N N 117.85 0.05 1 302 . 65 GLU H H 8.32 0.02 1 303 . 65 GLU CB C 29.92 0.10 1 304 . 65 GLU C C 174.69 0.10 1 305 . 65 GLU CA C 57.38 0.10 1 306 . 65 GLU N N 124.22 0.05 1 307 . 66 ILE H H 8.44 0.02 1 308 . 66 ILE CB C 38.92 0.10 1 309 . 66 ILE C C 176.89 0.10 1 310 . 66 ILE CA C 55.79 0.10 1 311 . 66 ILE N N 125.90 0.05 1 312 . 67 CYS H H 8.39 0.02 1 313 . 67 CYS CB C 30.18 0.10 1 314 . 67 CYS C C 176.37 0.10 1 315 . 67 CYS CA C 59.91 0.10 1 316 . 67 CYS N N 123.76 0.05 1 317 . 68 ALA H H 8.34 0.02 1 318 . 68 ALA CB C 18.64 0.10 1 319 . 68 ALA C C 176.69 0.10 1 320 . 68 ALA CA C 55.32 0.10 1 321 . 68 ALA N N 122.45 0.05 1 322 . 69 HIS H H 8.51 0.02 1 323 . 69 HIS CB C 32.97 0.10 1 324 . 69 HIS C C 177.86 0.10 1 325 . 69 HIS CA C 54.70 0.10 1 326 . 69 HIS N N 125.72 0.05 1 327 . 70 LYS H H 8.36 0.02 1 328 . 70 LYS CB C 33.33 0.10 1 329 . 70 LYS C C 176.76 0.10 1 330 . 70 LYS CA C 56.05 0.10 1 331 . 70 LYS N N 123.35 0.05 1 332 . 71 ALA H H 8.61 0.02 1 333 . 71 ALA CB C 19.34 0.10 1 334 . 71 ALA C C 174.69 0.10 1 335 . 71 ALA CA C 52.06 0.10 1 336 . 71 ALA N N 126.94 0.05 1 337 . 72 ILE H H 8.31 0.02 1 338 . 72 ILE CB C 38.92 0.10 1 339 . 72 ILE C C 177.27 0.10 1 340 . 72 ILE CA C 61.07 0.10 1 341 . 72 ILE N N 121.16 0.05 1 342 . 73 GLY H H 8.65 0.02 1 343 . 73 GLY C C 174.62 0.10 1 344 . 73 GLY CA C 45.07 0.10 1 345 . 73 GLY N N 113.66 0.05 1 346 . 74 THR H H 8.22 0.02 1 347 . 74 THR CB C 70.02 0.10 1 348 . 74 THR C C 175.07 0.10 1 349 . 74 THR CA C 60.86 0.10 1 350 . 74 THR N N 115.02 0.05 1 351 . 75 VAL H H 8.35 0.02 1 352 . 75 VAL CB C 32.98 0.10 1 353 . 75 VAL C C 176.37 0.10 1 354 . 75 VAL CA C 62.00 0.10 1 355 . 75 VAL N N 122.39 0.05 1 356 . 76 LEU H H 8.54 0.02 1 357 . 76 LEU CB C 42.16 0.10 1 358 . 76 LEU C C 177.53 0.10 1 359 . 76 LEU CA C 54.86 0.10 1 360 . 76 LEU N N 127.27 0.05 1 361 . 77 VAL H H 8.23 0.02 1 362 . 77 VAL CB C 32.62 0.10 1 363 . 77 VAL C C 175.76 0.10 1 364 . 77 VAL CA C 61.84 0.10 1 365 . 77 VAL N N 121.51 0.05 1 366 . 78 GLY H H 8.49 0.02 1 367 . 78 GLY CA C 44.45 0.10 1 368 . 78 GLY N N 113.35 0.05 1 369 . 79 PRO CB C 43.11 0.10 1 370 . 79 PRO C C 175.18 0.10 1 371 . 79 PRO CA C 60.91 0.10 1 372 . 80 THR H H 8.19 0.02 1 373 . 80 THR CA C 56.72 0.10 1 374 . 80 THR N N 132.55 0.05 1 375 . 81 PRO CB C 29.82 0.10 1 376 . 81 PRO C C 176.86 0.10 1 377 . 81 PRO CA C 55.33 0.10 1 378 . 82 VAL H H 8.51 0.02 1 379 . 82 VAL CB C 33.58 0.10 1 380 . 82 VAL C C 176.18 0.10 1 381 . 82 VAL CA C 61.25 0.10 1 382 . 82 VAL N N 123.37 0.05 1 383 . 83 ASN H H 8.60 0.03 1 384 . 83 ASN CB C 39.82 0.10 1 385 . 83 ASN C C 175.11 0.10 1 386 . 83 ASN CA C 50.94 0.10 1 387 . 83 ASN N N 122.45 0.10 1 388 . 84 ILE H H 8.59 0.10 1 389 . 84 ILE CB C 39.70 0.10 1 390 . 84 ILE C C 176.26 0.10 1 391 . 84 ILE CA C 59.79 0.10 1 392 . 84 ILE N N 123.54 0.05 1 393 . 85 ILE H H 8.26 0.02 1 394 . 85 ILE CB C 38.21 0.10 1 395 . 85 ILE C C 177.27 0.10 1 396 . 85 ILE CA C 61.23 0.10 1 397 . 85 ILE N N 121.36 0.05 1 398 . 86 GLY H H 8.62 0.02 1 399 . 86 GLY C C 176.24 0.10 1 400 . 86 GLY CA C 45.23 0.10 1 401 . 86 GLY N N 113.80 0.05 1 402 . 87 ARG H H 8.40 0.02 1 403 . 87 ARG CB C 30.53 0.10 1 404 . 87 ARG C C 176.76 0.10 1 405 . 87 ARG CA C 55.79 0.10 1 406 . 87 ARG N N 121.49 0.05 1 407 . 88 ASN H H 8.30 0.02 1 408 . 88 ASN CB C 38.57 0.10 1 409 . 88 ASN C C 174.69 0.10 1 410 . 88 ASN CA C 55.07 0.10 1 411 . 88 ASN N N 122.54 0.10 1 412 . 89 LEU H H 8.47 0.02 1 413 . 89 LEU CB C 41.71 0.10 1 414 . 89 LEU C C 175.53 0.10 1 415 . 89 LEU CA C 54.86 0.10 1 416 . 89 LEU N N 125.76 0.05 1 417 . 90 LEU H H 8.35 0.02 1 418 . 90 LEU CB C 42.06 0.10 1 419 . 90 LEU C C 178.18 0.10 1 420 . 90 LEU CA C 61.07 0.10 1 421 . 90 LEU N N 123.06 0.05 1 422 . 91 THR H H 8.18 0.02 1 423 . 91 THR CB C 69.67 0.10 1 424 . 91 THR C C 177.86 0.10 1 425 . 91 THR CA C 61.54 0.10 1 426 . 91 THR N N 114.80 0.05 1 427 . 92 GLN H H 8.24 0.02 1 428 . 92 GLN CB C 28.92 0.10 1 429 . 92 GLN C C 176.56 0.10 1 430 . 92 GLN CA C 57.27 0.10 1 431 . 92 GLN N N 122.08 0.05 1 432 . 93 ILE H H 8.33 0.02 1 433 . 93 ILE CB C 38.56 0.10 1 434 . 93 ILE C C 177.27 0.10 1 435 . 93 ILE CA C 61.23 0.10 1 436 . 93 ILE N N 125.18 0.05 1 437 . 94 GLY H H 8.61 0.02 1 438 . 94 GLY C C 174.56 0.10 1 439 . 94 GLY CA C 45.23 0.10 1 440 . 94 GLY N N 113.56 0.05 1 441 . 95 MET H H 8.38 0.10 1 442 . 95 MET CB C 33.33 0.10 1 443 . 95 MET C C 176.95 0.10 1 444 . 95 MET CA C 55.48 0.10 1 445 . 95 MET N N 121.01 0.05 1 446 . 96 THR H H 8.38 0.02 1 447 . 96 THR CB C 69.67 0.10 1 448 . 96 THR C C 175.01 0.10 1 449 . 96 THR CA C 61.38 0.10 1 450 . 96 THR N N 116.24 0.05 1 451 . 97 LEU H H 8.41 0.02 1 452 . 97 LEU CB C 42.06 0.10 1 453 . 97 LEU C C 177.14 0.10 1 454 . 97 LEU CA C 54.86 0.10 1 455 . 97 LEU N N 125.04 0.05 1 456 . 98 ASN H H 8.49 0.02 1 457 . 98 ASN CB C 39.27 0.10 1 458 . 98 ASN C C 176.24 0.10 1 459 . 98 ASN CA C 52.68 0.10 1 460 . 98 ASN N N 120.18 0.05 1 461 . 99 PHE H H 8.41 0.02 1 462 . 99 PHE CB C 39.27 0.10 1 463 . 99 PHE C C 176.62 0.10 1 464 . 99 PHE CA C 57.65 0.10 1 465 . 99 PHE N N 122.08 0.05 1 466 . 100 GLY H H 8.64 0.02 1 467 . 100 GLY C C 175.14 0.10 1 468 . 100 GLY CA C 45.23 0.10 1 469 . 100 GLY N N 111.31 0.05 1 470 . 101 GLY H H 8.29 0.02 1 471 . 101 GLY C C 174.81 0.10 1 472 . 101 GLY CA C 45.23 0.10 1 473 . 101 GLY N N 109.85 0.05 1 474 . 102 SER H H 8.49 0.02 1 475 . 102 SER CB C 63.38 0.10 1 476 . 102 SER C C 175.20 0.10 1 477 . 102 SER CA C 57.96 0.10 1 478 . 102 SER N N 116.80 0.05 1 479 . 103 SER H H 8.59 0.02 1 480 . 103 SER CB C 63.73 0.10 1 481 . 103 SER C C 175.14 0.10 1 482 . 103 SER CA C 58.12 0.10 1 483 . 103 SER N N 118.48 0.05 1 484 . 104 GLY H H 8.44 0.02 1 485 . 104 GLY CA C 44.60 0.10 1 486 . 104 GLY N N 111.26 0.05 1 487 . 105 PRO CB C 39.83 0.10 1 488 . 105 PRO C C 176.69 0.10 1 489 . 105 PRO CA C 56.91 0.10 1 490 . 106 GLN H H 8.57 0.03 1 491 . 106 GLN CB C 32.98 0.10 1 492 . 106 GLN C C 175.40 0.10 1 493 . 106 GLN CA C 53.43 0.10 1 494 . 106 GLN N N 123.54 0.05 1 495 . 107 VAL H H 8.57 0.02 1 496 . 107 VAL CB C 34.41 0.10 1 497 . 107 VAL C C 176.23 0.10 1 498 . 107 VAL CA C 60.94 0.10 1 499 . 107 VAL N N 120.36 0.05 1 500 . 108 THR H H 8.39 0.02 1 501 . 108 THR CB C 70.02 0.10 1 502 . 108 THR C C 177.02 0.10 1 503 . 108 THR CA C 61.38 0.10 1 504 . 108 THR N N 119.16 0.05 1 505 . 109 LEU H H 8.61 0.02 1 506 . 109 LEU CB C 43.63 0.10 1 507 . 109 LEU C C 175.34 0.10 1 508 . 109 LEU CA C 52.84 0.10 1 509 . 109 LEU N N 122.41 0.05 1 510 . 110 TRP H H 8.45 0.02 1 511 . 110 TRP CB C 31.92 0.10 1 512 . 110 TRP C C 177.27 0.10 1 513 . 110 TRP CA C 57.65 0.10 1 514 . 110 TRP N N 121.84 0.05 1 515 . 111 GLN H H 8.53 0.02 1 516 . 111 GLN CB C 31.27 0.10 1 517 . 111 GLN C C 176.37 0.10 1 518 . 111 GLN CA C 52.68 0.10 1 519 . 111 GLN N N 120.64 0.05 1 520 . 112 ARG H H 7.98 0.02 1 521 . 112 ARG CB C 31.27 0.10 1 522 . 112 ARG CA C 59.21 0.10 1 523 . 112 ARG N N 126.14 0.05 1 524 . 113 PRO CB C 32.28 0.10 1 525 . 113 PRO C C 177.60 0.10 1 526 . 113 PRO CA C 62.93 0.10 1 527 . 114 LEU H H 8.75 0.02 1 528 . 114 LEU CB C 43.48 0.10 1 529 . 114 LEU C C 177.40 0.10 1 530 . 114 LEU CA C 55.95 0.10 1 531 . 114 LEU N N 122.83 0.05 1 532 . 115 VAL H H 8.22 0.02 1 533 . 115 VAL CB C 32.98 0.10 1 534 . 115 VAL C C 176.63 0.10 1 535 . 115 VAL CA C 61.85 0.10 1 536 . 115 VAL N N 122.22 0.05 1 537 . 116 THR H H 8.36 0.02 1 538 . 116 THR CB C 69.67 0.10 1 539 . 116 THR C C 174.88 0.10 1 540 . 116 THR CA C 61.23 0.10 1 541 . 116 THR N N 118.76 0.05 1 542 . 117 ILE H H 8.31 0.02 1 543 . 117 ILE CB C 38.92 0.10 1 544 . 117 ILE C C 176.36 0.10 1 545 . 117 ILE CA C 60.76 0.10 1 546 . 117 ILE N N 124.63 0.05 1 547 . 118 LYS H H 8.56 0.02 1 548 . 118 LYS CB C 33.33 0.10 1 549 . 118 LYS C C 175.79 0.10 1 550 . 118 LYS CA C 55.95 0.10 1 551 . 118 LYS N N 126.72 0.05 1 552 . 119 ILE H H 8.45 0.02 1 553 . 119 ILE CB C 38.57 0.10 1 554 . 119 ILE C C 177.27 0.10 1 555 . 119 ILE CA C 61.07 0.10 1 556 . 119 ILE N N 124.11 0.05 1 557 . 120 GLY H H 8.67 0.02 1 558 . 120 GLY C C 175.07 0.10 1 559 . 120 GLY CA C 45.07 0.10 1 560 . 120 GLY N N 114.21 0.05 1 561 . 121 GLY H H 8.49 0.02 1 562 . 121 GLY C C 174.69 0.10 1 563 . 121 GLY CA C 45.07 0.10 1 564 . 121 GLY N N 109.95 0.05 1 565 . 122 GLN H H 8.56 0.02 1 566 . 122 GLN CB C 29.83 0.10 1 567 . 122 GLN C C 176.63 0.10 1 568 . 122 GLN CA C 55.79 0.10 1 569 . 122 GLN N N 120.97 0.05 1 570 . 123 LEU H H 8.50 0.02 1 571 . 123 LEU CB C 42.06 0.10 1 572 . 123 LEU C C 175.14 0.10 1 573 . 123 LEU CA C 55.01 0.10 1 574 . 123 LEU N N 124.37 0.05 1 575 . 124 LYS H H 8.56 0.02 1 576 . 124 LYS CB C 33.33 0.10 1 577 . 124 LYS C C 176.39 0.10 1 578 . 124 LYS CA C 56.05 0.10 1 579 . 124 LYS N N 123.41 0.05 1 580 . 125 GLU H H 8.61 0.02 1 581 . 125 GLU CB C 30.53 0.10 1 582 . 125 GLU C C 175.01 0.10 1 583 . 125 GLU CA C 55.25 0.10 1 584 . 125 GLU N N 122.84 0.05 1 585 . 126 ALA H H 8.46 0.02 1 586 . 126 ALA CB C 19.69 0.10 1 587 . 126 ALA C C 176.53 0.10 1 588 . 126 ALA CA C 52.06 0.10 1 589 . 126 ALA N N 125.33 0.05 1 590 . 127 LEU H H 8.34 0.02 1 591 . 127 LEU CB C 43.33 0.10 1 592 . 127 LEU C C 176.50 0.10 1 593 . 127 LEU CA C 54.86 0.10 1 594 . 127 LEU N N 122.60 0.05 1 595 . 128 LEU H H 8.43 0.02 1 596 . 128 LEU CB C 42.53 0.10 1 597 . 128 LEU C C 177.60 0.10 1 598 . 128 LEU CA C 57.07 0.10 1 599 . 128 LEU N N 123.30 0.05 1 600 . 129 ASP H H 8.58 0.02 1 601 . 129 ASP CB C 40.02 0.10 1 602 . 129 ASP C C 176.95 0.10 1 603 . 129 ASP CA C 52.84 0.10 1 604 . 129 ASP N N 122.21 0.05 1 605 . 130 THR H H 8.30 0.02 1 606 . 130 THR CB C 70.02 0.10 1 607 . 130 THR C C 175.91 0.10 1 608 . 130 THR CA C 61.54 0.10 1 609 . 130 THR N N 114.21 0.05 1 610 . 131 GLY H H 8.69 0.02 1 611 . 131 GLY C C 174.88 0.10 1 612 . 131 GLY CA C 45.23 0.10 1 613 . 131 GLY N N 111.89 0.05 1 614 . 132 ALA H H 8.32 0.02 1 615 . 132 ALA CB C 20.04 0.10 1 616 . 132 ALA C C 174.29 0.10 1 617 . 132 ALA CA C 52.37 0.10 1 618 . 132 ALA N N 124.37 0.05 1 619 . 133 ASP H H 8.55 0.02 1 620 . 133 ASP CB C 39.36 0.10 1 621 . 133 ASP C C 176.56 0.10 1 622 . 133 ASP CA C 54.06 0.10 1 623 . 133 ASP N N 119.20 0.05 1 624 . 134 ASP H H 8.54 0.02 1 625 . 134 ASP CB C 39.36 0.10 1 626 . 134 ASP C C 177.02 0.10 1 627 . 134 ASP CA C 54.48 0.10 1 628 . 134 ASP N N 121.54 0.05 1 629 . 135 THR H H 8.33 0.02 1 630 . 135 THR CB C 70.02 0.10 1 631 . 135 THR C C 177.47 0.10 1 632 . 135 THR CA C 62.00 0.10 1 633 . 135 THR N N 114.66 0.05 1 634 . 136 VAL H H 8.26 0.02 1 635 . 136 VAL CB C 33.73 0.10 1 636 . 136 VAL C C 175.89 0.10 1 637 . 136 VAL CA C 61.18 0.10 1 638 . 136 VAL N N 122.99 0.05 1 639 . 137 LEU H H 8.42 0.02 1 640 . 137 LEU CB C 43.38 0.10 1 641 . 137 LEU C C 177.18 0.10 1 642 . 137 LEU CA C 55.17 0.10 1 643 . 137 LEU N N 126.49 0.05 1 644 . 138 GLU H H 8.57 0.02 1 645 . 138 GLU CB C 30.36 0.10 1 646 . 138 GLU C C 175.86 0.10 1 647 . 138 GLU CA C 54.70 0.10 1 648 . 138 GLU N N 122.56 0.05 1 649 . 139 GLU H H 8.43 0.02 1 650 . 139 GLU CB C 29.83 0.10 1 651 . 139 GLU C C 175.83 0.10 1 652 . 139 GLU CA C 55.79 0.10 1 653 . 139 GLU N N 121.03 0.05 1 654 . 140 MET H H 8.37 0.02 1 655 . 140 MET CB C 34.41 0.10 1 656 . 140 MET C C 176.12 0.10 1 657 . 140 MET CA C 54.86 0.10 1 658 . 140 MET N N 122.75 0.05 1 659 . 141 SER H H 8.55 0.02 1 660 . 141 SER CB C 65.07 0.10 1 661 . 141 SER C C 174.22 0.10 1 662 . 141 SER CA C 56.93 0.10 1 663 . 141 SER N N 121.82 0.05 1 664 . 142 LEU H H 8.47 0.02 1 665 . 142 LEU CB C 42.06 0.10 1 666 . 142 LEU CA C 54.86 0.10 1 667 . 142 LEU N N 127.21 0.05 1 668 . 143 PRO CB C 32.27 0.10 1 669 . 143 PRO C C 177.92 0.10 1 670 . 143 PRO CA C 63.09 0.10 1 671 . 144 GLY H H 8.59 0.02 1 672 . 144 GLY C C 178.18 0.10 1 673 . 144 GLY CA C 45.23 0.10 1 674 . 144 GLY N N 110.17 0.05 1 675 . 145 ARG H H 8.33 0.02 1 676 . 145 ARG CB C 30.88 0.10 1 677 . 145 ARG C C 177.86 0.10 1 678 . 145 ARG CA C 55.94 0.10 1 679 . 145 ARG N N 121.53 0.05 1 680 . 146 TRP H H 8.47 0.02 1 681 . 146 TRP CB C 29.83 0.10 1 682 . 146 TRP C C 176.17 0.10 1 683 . 146 TRP CA C 57.34 0.10 1 684 . 146 TRP N N 123.24 0.05 1 685 . 147 LYS H H 8.08 0.02 1 686 . 147 LYS CB C 32.63 0.10 1 687 . 147 LYS CA C 53.61 0.10 1 688 . 147 LYS N N 125.48 0.05 1 689 . 148 PRO CB C 30.18 0.10 1 690 . 148 PRO C C 174.69 0.10 1 691 . 148 PRO CA C 56.25 0.10 1 692 . 149 LYS CB C 30.53 0.10 1 693 . 149 LYS C C 176.62 0.10 1 694 . 149 LYS CA C 51.91 0.10 1 695 . 149 LYS N N 125.76 0.05 1 696 . 150 MET H H 8.31 0.02 1 697 . 150 MET CB C 32.98 0.10 1 698 . 150 MET C C 175.60 0.10 1 699 . 150 MET CA C 54.86 0.10 1 700 . 150 MET N N 122.10 0.05 1 701 . 151 ILE H H 8.38 0.02 1 702 . 151 ILE CB C 38.57 0.10 1 703 . 151 ILE C C 177.27 0.10 1 704 . 151 ILE CA C 61.07 0.10 1 705 . 151 ILE N N 123.28 0.05 1 706 . 152 GLY H H 8.67 0.02 1 707 . 152 GLY C C 174.94 0.10 1 708 . 152 GLY CA C 44.92 0.10 1 709 . 152 GLY N N 114.03 0.05 1 710 . 153 GLY H H 8.44 0.02 1 711 . 153 GLY C C 174.75 0.10 1 712 . 153 GLY CA C 44.92 0.10 1 713 . 153 GLY N N 109.80 0.05 1 714 . 154 ILE H H 8.29 0.02 1 715 . 154 ILE CB C 38.57 0.10 1 716 . 154 ILE C C 177.27 0.10 1 717 . 154 ILE CA C 61.23 0.10 1 718 . 154 ILE N N 120.51 0.05 1 719 . 155 GLY H H 8.65 0.02 1 720 . 155 GLY C C 174.94 0.10 1 721 . 155 GLY CA C 45.07 0.10 1 722 . 155 GLY N N 113.40 0.05 1 723 . 156 GLY H H 8.37 0.02 1 724 . 156 GLY C C 178.18 0.10 1 725 . 156 GLY CA C 45.07 0.10 1 726 . 156 GLY N N 109.76 0.05 1 727 . 157 PHE H H 8.33 0.02 1 728 . 157 PHE CB C 39.96 0.10 1 729 . 157 PHE C C 176.17 0.10 1 730 . 157 PHE CA C 55.95 0.10 1 731 . 157 PHE N N 121.30 0.05 1 732 . 158 ILE H H 8.28 0.02 1 733 . 158 ILE CB C 37.62 0.10 1 734 . 158 ILE C C 174.62 0.10 1 735 . 158 ILE CA C 60.61 0.10 1 736 . 158 ILE N N 123.52 0.05 1 737 . 159 LYS H H 8.53 0.02 1 738 . 159 LYS CB C 34.41 0.10 1 739 . 159 LYS C C 175.40 0.10 1 740 . 159 LYS CA C 54.70 0.10 1 741 . 159 LYS N N 126.97 0.05 1 742 . 160 VAL H H 8.26 0.02 1 743 . 160 VAL CB C 32.98 0.10 1 744 . 160 VAL C C 176.50 0.10 1 745 . 160 VAL CA C 60.92 0.10 1 746 . 160 VAL N N 122.76 0.05 1 747 . 161 ARG H H 8.60 0.02 1 748 . 161 ARG CB C 30.88 0.10 1 749 . 161 ARG C C 176.62 0.10 1 750 . 161 ARG CA C 56.10 0.10 1 751 . 161 ARG N N 125.51 0.05 1 752 . 162 GLN H H 8.54 0.02 1 753 . 162 GLN CB C 29.83 0.10 1 754 . 162 GLN C C 176.24 0.10 1 755 . 162 GLN CA C 55.79 0.10 1 756 . 162 GLN N N 122.58 0.05 1 757 . 163 TYR H H 8.38 0.02 1 758 . 163 TYR CB C 37.18 0.10 1 759 . 163 TYR C C 177.11 0.10 1 760 . 163 TYR CA C 57.50 0.10 1 761 . 163 TYR N N 121.56 0.05 1 762 . 164 ASP H H 8.39 0.02 1 763 . 164 ASP CB C 38.92 0.10 1 764 . 164 ASP C C 176.17 0.10 1 765 . 164 ASP CA C 54.23 0.10 1 766 . 164 ASP N N 122.49 0.05 1 767 . 165 GLN H H 8.59 0.02 1 768 . 165 GLN CB C 32.98 0.10 1 769 . 165 GLN C C 177.62 0.10 1 770 . 165 GLN CA C 58.43 0.10 1 771 . 165 GLN N N 123.08 0.05 1 772 . 166 ILE H H 8.57 0.02 1 773 . 166 ILE CB C 39.83 0.10 1 774 . 166 ILE C C 177.53 0.10 1 775 . 166 ILE CA C 60.10 0.10 1 776 . 166 ILE N N 125.63 0.05 1 777 . 167 LEU H H 8.25 0.02 1 778 . 167 LEU CB C 42.98 0.10 1 779 . 167 LEU C C 176.69 0.10 1 780 . 167 LEU CA C 56.85 0.10 1 781 . 167 LEU N N 121.47 0.05 1 782 . 168 ILE H H 8.48 0.02 1 783 . 168 ILE CB C 38.56 0.10 1 784 . 168 ILE C C 174.43 0.10 1 785 . 168 ILE CA C 61.23 0.10 1 786 . 168 ILE N N 117.85 0.05 1 787 . 169 GLU H H 8.32 0.10 1 788 . 169 GLU CB C 29.92 0.10 1 789 . 169 GLU C C 174.69 0.10 1 790 . 169 GLU CA C 57.38 0.10 1 791 . 169 GLU N N 124.22 0.05 1 792 . 170 ILE H H 8.44 0.02 1 793 . 170 ILE CB C 38.92 0.10 1 794 . 170 ILE C C 176.89 0.10 1 795 . 170 ILE CA C 55.79 0.10 1 796 . 170 ILE N N 125.90 0.05 1 797 . 171 CYS H H 8.39 0.02 1 798 . 171 CYS CB C 30.18 0.10 1 799 . 171 CYS C C 176.37 0.10 1 800 . 171 CYS CA C 59.91 0.10 1 801 . 171 CYS N N 123.76 0.05 1 802 . 172 ALA H H 8.34 0.02 1 803 . 172 ALA CB C 18.64 0.10 1 804 . 172 ALA C C 176.69 0.10 1 805 . 172 ALA CA C 55.32 0.10 1 806 . 172 ALA N N 122.45 0.05 1 807 . 173 HIS H H 8.51 0.02 1 808 . 173 HIS CB C 32.97 0.10 1 809 . 173 HIS C C 177.86 0.10 1 810 . 173 HIS CA C 54.70 0.10 1 811 . 173 HIS N N 125.72 0.05 1 812 . 174 LYS H H 8.36 0.02 1 813 . 174 LYS CB C 33.33 0.10 1 814 . 174 LYS C C 176.76 0.10 1 815 . 174 LYS CA C 56.05 0.10 1 816 . 174 LYS N N 123.35 0.05 1 817 . 175 ALA H H 8.61 0.02 1 818 . 175 ALA CB C 19.34 0.10 1 819 . 175 ALA C C 174.69 0.10 1 820 . 175 ALA CA C 52.06 0.10 1 821 . 175 ALA N N 126.94 0.05 1 822 . 176 ILE H H 8.31 0.02 1 823 . 176 ILE CB C 38.92 0.10 1 824 . 176 ILE C C 177.27 0.10 1 825 . 176 ILE CA C 61.07 0.10 1 826 . 176 ILE N N 121.16 0.05 1 827 . 177 GLY H H 8.65 0.02 1 828 . 177 GLY C C 174.62 0.10 1 829 . 177 GLY CA C 45.07 0.10 1 830 . 177 GLY N N 113.66 0.05 1 831 . 178 THR H H 8.22 0.02 1 832 . 178 THR CB C 70.02 0.10 1 833 . 178 THR C C 175.07 0.10 1 834 . 178 THR CA C 60.86 0.10 1 835 . 178 THR N N 115.02 0.05 1 836 . 179 VAL H H 8.35 0.02 1 837 . 179 VAL CB C 32.98 0.10 1 838 . 179 VAL C C 176.37 0.10 1 839 . 179 VAL CA C 62.00 0.10 1 840 . 179 VAL N N 122.39 0.05 1 841 . 180 LEU H H 8.54 0.02 1 842 . 180 LEU CB C 42.16 0.10 1 843 . 180 LEU C C 177.53 0.10 1 844 . 180 LEU CA C 54.86 0.10 1 845 . 180 LEU N N 127.27 0.05 1 846 . 181 VAL H H 8.23 0.02 1 847 . 181 VAL CB C 32.62 0.10 1 848 . 181 VAL C C 175.76 0.10 1 849 . 181 VAL CA C 61.84 0.10 1 850 . 181 VAL N N 121.51 0.05 1 851 . 182 GLY H H 8.49 0.02 1 852 . 182 GLY CA C 44.45 0.10 1 853 . 182 GLY N N 113.35 0.05 1 854 . 183 PRO CB C 43.11 0.10 1 855 . 183 PRO C C 175.18 0.10 1 856 . 183 PRO CA C 60.91 0.10 1 857 . 184 THR H H 8.19 0.02 1 858 . 184 THR CA C 56.72 0.10 1 859 . 184 THR N N 132.55 0.05 1 860 . 185 PRO CB C 29.82 0.10 1 861 . 185 PRO C C 176.86 0.10 1 862 . 185 PRO CA C 55.33 0.10 1 863 . 186 VAL H H 8.51 0.02 1 864 . 186 VAL CB C 33.58 0.10 1 865 . 186 VAL C C 176.18 0.10 1 866 . 186 VAL CA C 61.25 0.10 1 867 . 186 VAL N N 123.37 0.05 1 868 . 187 ASN H H 8.60 0.02 1 869 . 187 ASN CB C 39.82 0.10 1 870 . 187 ASN C C 175.11 0.10 1 871 . 187 ASN CA C 50.94 0.10 1 872 . 187 ASN N N 122.45 0.05 1 873 . 188 ILE H H 8.59 0.02 1 874 . 188 ILE CB C 39.70 0.10 1 875 . 188 ILE C C 176.26 0.10 1 876 . 188 ILE CA C 59.79 0.10 1 877 . 188 ILE N N 123.54 0.05 1 878 . 189 ILE H H 8.26 0.02 1 879 . 189 ILE CB C 38.21 0.10 1 880 . 189 ILE C C 177.27 0.10 1 881 . 189 ILE CA C 61.23 0.10 1 882 . 189 ILE N N 121.36 0.05 1 883 . 190 GLY H H 8.62 0.02 1 884 . 190 GLY C C 176.24 0.10 1 885 . 190 GLY CA C 45.23 0.10 1 886 . 190 GLY N N 113.80 0.05 1 887 . 191 ARG H H 8.40 0.02 1 888 . 191 ARG CB C 30.53 0.10 1 889 . 191 ARG C C 176.76 0.10 1 890 . 191 ARG CA C 55.79 0.10 1 891 . 191 ARG N N 121.49 0.05 1 892 . 192 ASN H H 8.30 0.02 1 893 . 192 ASN CB C 38.57 0.10 1 894 . 192 ASN C C 174.69 0.10 1 895 . 192 ASN CA C 55.07 0.10 1 896 . 192 ASN N N 122.54 0.05 1 897 . 193 LEU H H 8.47 0.02 1 898 . 193 LEU CB C 41.71 0.10 1 899 . 193 LEU C C 175.53 0.10 1 900 . 193 LEU CA C 54.86 0.10 1 901 . 193 LEU N N 125.76 0.05 1 902 . 194 LEU H H 8.35 0.02 1 903 . 194 LEU CB C 42.06 0.10 1 904 . 194 LEU C C 178.18 0.10 1 905 . 194 LEU CA C 61.07 0.10 1 906 . 194 LEU N N 123.06 0.05 1 907 . 195 THR H H 8.18 0.02 1 908 . 195 THR CB C 69.67 0.10 1 909 . 195 THR C C 177.86 0.10 1 910 . 195 THR CA C 61.54 0.10 1 911 . 195 THR N N 114.80 0.05 1 912 . 196 GLN H H 8.24 0.02 1 913 . 196 GLN CB C 28.92 0.10 1 914 . 196 GLN C C 176.56 0.10 1 915 . 196 GLN CA C 57.27 0.10 1 916 . 196 GLN N N 122.08 0.05 1 917 . 197 ILE H H 8.33 0.02 1 918 . 197 ILE CB C 38.56 0.10 1 919 . 197 ILE C C 177.27 0.10 1 920 . 197 ILE CA C 61.23 0.10 1 921 . 197 ILE N N 125.18 0.05 1 922 . 198 GLY H H 8.57 0.02 1 923 . 198 GLY C C 177.15 0.10 1 924 . 198 GLY CA C 45.23 0.10 1 925 . 198 GLY N N 113.66 0.05 1 926 . 199 ALA H H 8.54 0.02 1 927 . 199 ALA CB C 19.69 0.10 1 928 . 199 ALA C C 178.50 0.10 1 929 . 199 ALA CA C 55.17 0.10 1 930 . 199 ALA N N 124.13 0.05 1 931 . 200 THR H H 8.32 0.02 1 932 . 200 THR CB C 69.67 0.10 1 933 . 200 THR C C 175.01 0.10 1 934 . 200 THR CA C 61.54 0.10 1 935 . 200 THR N N 114.07 0.05 1 936 . 201 LEU H H 8.41 0.02 1 937 . 201 LEU CB C 42.06 0.10 1 938 . 201 LEU C C 177.14 0.10 1 939 . 201 LEU CA C 54.86 0.10 1 940 . 201 LEU N N 125.04 0.05 1 941 . 202 ASN H H 8.49 0.02 1 942 . 202 ASN CB C 39.27 0.10 1 943 . 202 ASN C C 176.24 0.10 1 944 . 202 ASN CA C 52.68 0.10 1 945 . 202 ASN N N 120.18 0.05 1 946 . 203 PHE H H 8.41 0.02 1 947 . 203 PHE CB C 39.27 0.10 1 948 . 203 PHE C C 176.62 0.10 1 949 . 203 PHE CA C 57.65 0.10 1 950 . 203 PHE N N 122.08 0.05 1 stop_ save_