data_5918 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Multiple time-scale dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes ; _BMRB_accession_number 5918 _BMRB_flat_file_name bmr5918.str _Entry_type original _Submission_date 2003-08-21 _Accession_date 2003-08-25 _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 Butterwick Joel A. . 2 Patrick Loria J. . 3 Astrof Nathan S. . 4 Kroenke Christopher D. . 5 Cole Roger . . 6 Rance Mark . . 7 Palmer Arthur G. III stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 149 "13C chemical shifts" 439 "15N chemical shifts" 149 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-23 original author . stop_ _Original_release_date 2004-07-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Multiple time-scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15165855 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Butterwick Joel A. . 2 Patrick Loria J. . 3 Astrof Nathan S. . 4 Kroenke Christopher D. . 5 Cole Roger . . 6 Rance Mark . . 7 Palmer Arthur G. III stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 339 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 855 _Page_last 871 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_Ref._1 _Saveframe_category citation _Citation_full ; Hollien J, Marqusee S. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry. 1999 Mar 23;38(12):3831-6. ; _Citation_title 'A thermodynamic comparison of mesophilic and thermophilic ribonucleases H.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10090773 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hollien J . . 2 Marqusee S . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue 12 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 3831 _Page_last 3836 _Year 1999 _Details ; The mechanisms by which thermophilic proteins attain their increased thermostability remain unclear, as usually the sequence and structure of these proteins are very similar to those of their mesophilic homologues. To gain insight into the basis of thermostability, we have determined protein stability curves describing the temperature dependence of the free energy of unfolding for two ribonucleases H, one from the mesophile Escherichia coli and one from the thermophile Thermus thermophilus. The circular dichroism signal was monitored as a function of temperature and guanidinium chloride concentration, and the resulting free energies of unfolding were fit to the Gibbs-Helmholtz equation to obtain a set of thermodynamic parameters for these proteins. Although the maximal stabilities for these proteins occur at similar temperatures, the heat capacity of unfolding for T. thermophilus RNase H is lower, resulting in a smaller temperature dependence of the free energy of unfolding and therefore a higher thermal melting temperature. In addition, the stabilities of these proteins are similar at the optimal growth temperatures for their respective organisms, suggesting that a balance of thermodynamic stability and flexibility is important for function. ; save_ save_Ref._2 _Saveframe_category citation _Citation_full ; Hollien J, Marqusee S. Structural distribution of stability in a thermophilic enzyme. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13674-8. ; _Citation_title 'Structural distribution of stability in a thermophilic enzyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10570131 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hollien J . . 2 Marqusee S . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 96 _Journal_issue 24 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 13674 _Page_last 13678 _Year 1999 _Details ; Stability parameters for individual residues in Thermus thermophilus cysteine-free RNase H were determined by native state hydrogen exchange, thus providing a unique comparison of regional thermodynamics between thermophilic and mesophilic homologues. The general distribution of stability in the thermophilic protein is similar to that of its mesophilic homologue, with a proportional increase in stability for almost all residues. As a consequence, the residue-specific stabilities of the two proteins are remarkably similar under conditions where their global stabilities are the same. These results indicate that T. thermophilus RNase H is stabilized in a delocalized fashion, preserving a finely tuned balance of stabilizing interactions throughout the structure. Therefore, although protein stability can be altered by single amino acid substitution, evolution for optimal function may require more subtle and delocalized mechanisms. ; save_ ################################## # Molecular system description # ################################## save_system_ttRNH_RNase_H _Saveframe_category molecular_system _Mol_system_name 'Thermus thermophilus Ribonuclease HI' _Abbreviation_common 'ttRNH, RNase H' _Enzyme_commission_number 3.1.26.4 loop_ _Mol_system_component_name _Mol_label 'ttRNH monomer' $ttRNH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'RNA degradation in RNA-DNA hybrids' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ttRNH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ribonuclease HI' _Name_variant C17A/C45S/C67A/C154S _Abbreviation_common 'RNase H' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; MNPSPRKRVALFTDGAALGN PGPGGWAALLRFHAHEKLLS GGEASTTNNRMELKAAIEGL KALKEPAEVDLYTDSHYLKK AFTEGWLEGWRKRGWRTAEG KPVKNRDLWEALLLAMAPHR VRFHFVKGHTGHPENERVDR EARRQAQSQAKTPSPPRAPT LFHEEA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 PRO 4 SER 5 PRO 6 ARG 7 LYS 8 ARG 9 VAL 10 ALA 11 LEU 12 PHE 13 THR 14 ASP 15 GLY 16 ALA 17 ALA 18 LEU 19 GLY 20 ASN 21 PRO 22 GLY 23 PRO 24 GLY 25 GLY 26 TRP 27 ALA 28 ALA 29 LEU 30 LEU 31 ARG 32 PHE 33 HIS 34 ALA 35 HIS 36 GLU 37 LYS 38 LEU 39 LEU 40 SER 41 GLY 42 GLY 43 GLU 44 ALA 45 SER 46 THR 47 THR 48 ASN 49 ASN 50 ARG 51 MET 52 GLU 53 LEU 54 LYS 55 ALA 56 ALA 57 ILE 58 GLU 59 GLY 60 LEU 61 LYS 62 ALA 63 LEU 64 LYS 65 GLU 66 PRO 67 ALA 68 GLU 69 VAL 70 ASP 71 LEU 72 TYR 73 THR 74 ASP 75 SER 76 HIS 77 TYR 78 LEU 79 LYS 80 LYS 81 ALA 82 PHE 83 THR 84 GLU 85 GLY 86 TRP 87 LEU 88 GLU 89 GLY 90 TRP 91 ARG 92 LYS 93 ARG 94 GLY 95 TRP 96 ARG 97 THR 98 ALA 99 GLU 100 GLY 101 LYS 102 PRO 103 VAL 104 LYS 105 ASN 106 ARG 107 ASP 108 LEU 109 TRP 110 GLU 111 ALA 112 LEU 113 LEU 114 LEU 115 ALA 116 MET 117 ALA 118 PRO 119 HIS 120 ARG 121 VAL 122 ARG 123 PHE 124 HIS 125 PHE 126 VAL 127 LYS 128 GLY 129 HIS 130 THR 131 GLY 132 HIS 133 PRO 134 GLU 135 ASN 136 GLU 137 ARG 138 VAL 139 ASP 140 ARG 141 GLU 142 ALA 143 ARG 144 ARG 145 GLN 146 ALA 147 GLN 148 SER 149 GLN 150 ALA 151 LYS 152 THR 153 PRO 154 SER 155 PRO 156 PRO 157 ARG 158 ALA 159 PRO 160 THR 161 LEU 162 PHE 163 HIS 164 GLU 165 GLU 166 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-25 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 7277 dG85_ttRNH 100.00 165 99.40 99.40 6.10e-113 PDB 1RIL "Crystal Structure Of Ribonuclease H From Thermus Thermophilus Hb8 Refined At 2.8 Angstroms Resolution" 100.00 166 97.59 97.59 4.78e-114 DBJ BAD71379 "ribonuclease H (RNase H) [Thermus thermophilus HB8]" 100.00 166 97.59 97.59 4.78e-114 EMBL CAA43026 "ribonuclease h [Thermus thermophilus HB8]" 100.00 166 97.59 97.59 5.53e-113 PIR A42673 "ribonuclease H (EC 3.1.26.4) - Thermus aquaticus" 100.00 166 97.59 97.59 4.78e-114 REF WP_011228761 "ribonuclease HI [Thermus thermophilus]" 100.00 166 97.59 97.59 4.78e-114 REF YP_144822 "ribonuclease H [Thermus thermophilus HB8]" 100.00 166 97.59 97.59 4.78e-114 SP P29253 "RecName: Full=Ribonuclease H; Short=RNase H [Thermus thermophilus HB8]" 100.00 166 97.59 97.59 4.78e-114 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $ttRNH 'Thermus thermophilus' 274 Eubacteria . Thermus thermophilus HB8 rnhA 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 _Details $ttRNH 'recombinant technology' 'E. coli' Escherichia coli 'BL21-Gold (DE3)' . ; Plasmid used for overexpression was obtaind from Dr. Susan Marqusee: a pAED4 vector with synthesized rnhA gene that has codons optimized for expression in E. coli (see Ref. 1). ; 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 $ttRNH 0.3 mM '[U-90% 2H; U-96% 13C; U-96% 15N]' 'sodium acetate-d3' 100 mM . 'sodium azide' 0.02 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_[1H,15N]-TROSY_Triple-Resonance_1 _Saveframe_category NMR_applied_experiment _Experiment_name '[1H,15N]-TROSY Triple-Resonance' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '[1H,15N]-TROSY Triple-Resonance' _BMRB_pulse_sequence_accession_number . _Details 'All 1H and 15N resonances reported are for the TROSY peak at 14.1 T.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'All 1H and 15N resonances reported are for the TROSY peak at 14.1 T.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'All 1H and 15N resonances reported are for the TROSY peak at 14.1 T.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details 'All 1H and 15N resonances reported are for the TROSY peak at 14.1 T.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'All 1H and 15N resonances reported are for the TROSY peak at 14.1 T.' save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 na temperature 310 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '[1H,15N]-TROSY Triple-Resonance' HNCA HN(CO)CA HN(COCA)CB HNCO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ttRNH monomer' _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 . 5 PRO C C 177.100 0.200 1 2 . 5 PRO CA C 62.900 0.200 1 3 . 5 PRO CB C 31.700 0.200 1 4 . 6 ARG N N 122.700 0.050 1 5 . 6 ARG H H 8.210 0.010 1 6 . 6 ARG C C 176.500 0.200 1 7 . 6 ARG CA C 55.800 0.200 1 8 . 6 ARG CB C 31.400 0.200 1 9 . 7 LYS N N 124.800 0.050 1 10 . 7 LYS H H 8.340 0.010 1 11 . 7 LYS C C 175.300 0.200 1 12 . 7 LYS CA C 55.800 0.200 1 13 . 7 LYS CB C 32.800 0.200 1 14 . 8 ARG N N 124.200 0.050 1 15 . 8 ARG H H 8.140 0.010 1 16 . 8 ARG C C 176.200 0.200 1 17 . 8 ARG CA C 55.200 0.200 1 18 . 8 ARG CB C 30.800 0.200 1 19 . 9 VAL N N 125.500 0.050 1 20 . 9 VAL H H 8.620 0.010 1 21 . 9 VAL C C 173.500 0.200 1 22 . 9 VAL CA C 60.200 0.200 1 23 . 9 VAL CB C 35.500 0.200 1 24 . 10 ALA N N 130.400 0.050 1 25 . 10 ALA H H 8.130 0.010 1 26 . 10 ALA C C 174.300 0.200 1 27 . 10 ALA CA C 50.000 0.200 1 28 . 10 ALA CB C 20.900 0.200 1 29 . 11 LEU N N 126.500 0.050 1 30 . 11 LEU H H 8.730 0.010 1 31 . 11 LEU C C 173.300 0.200 1 32 . 11 LEU CA C 52.500 0.200 1 33 . 11 LEU CB C 45.400 0.200 1 34 . 12 PHE N N 127.900 0.050 1 35 . 12 PHE H H 9.190 0.010 1 36 . 12 PHE C C 176.400 0.200 1 37 . 12 PHE CA C 55.500 0.200 1 38 . 12 PHE CB C 40.300 0.200 1 39 . 13 THR N N 113.000 0.050 1 40 . 13 THR H H 7.900 0.010 1 41 . 13 THR C C 175.000 0.200 1 42 . 13 THR CA C 59.800 0.200 1 43 . 13 THR CB C 70.900 0.200 1 44 . 14 ASP N N 123.000 0.050 1 45 . 14 ASP H H 8.830 0.010 1 46 . 14 ASP C C 173.000 0.200 1 47 . 14 ASP CA C 53.800 0.200 1 48 . 14 ASP CB C 44.100 0.200 1 49 . 15 GLY N N 107.900 0.050 1 50 . 15 GLY H H 8.280 0.010 1 51 . 15 GLY C C 170.400 0.200 1 52 . 15 GLY CA C 44.900 0.200 1 53 . 16 ALA N N 123.700 0.050 1 54 . 16 ALA H H 8.920 0.010 1 55 . 16 ALA C C 175.400 0.200 1 56 . 16 ALA CA C 51.400 0.200 1 57 . 16 ALA CB C 22.700 0.200 1 58 . 17 ALA N N 121.700 0.050 1 59 . 17 ALA H H 8.380 0.010 1 60 . 17 ALA C C 177.300 0.200 1 61 . 17 ALA CA C 51.000 0.200 1 62 . 17 ALA CB C 22.000 0.200 1 63 . 18 LEU N N 122.400 0.050 1 64 . 18 LEU H H 8.870 0.010 1 65 . 18 LEU C C 176.600 0.200 1 66 . 18 LEU CA C 53.500 0.200 1 67 . 18 LEU CB C 40.300 0.200 1 68 . 19 GLY N N 106.600 0.050 1 69 . 19 GLY H H 7.030 0.010 1 70 . 19 GLY C C 171.000 0.200 1 71 . 19 GLY CA C 44.000 0.200 1 72 . 20 ASN N N 118.200 0.050 1 73 . 20 ASN H H 8.240 0.010 1 74 . 20 ASN CA C 50.400 0.200 1 75 . 20 ASN CB C 36.800 0.200 1 76 . 21 PRO C C 177.100 0.200 1 77 . 21 PRO CA C 62.700 0.200 1 78 . 21 PRO CB C 35.000 0.200 1 79 . 22 GLY N N 108.100 0.050 1 80 . 22 GLY H H 8.860 0.010 1 81 . 22 GLY CA C 45.300 0.200 1 82 . 23 PRO C C 176.400 0.010 1 83 . 23 PRO CA C 63.200 0.200 1 84 . 23 PRO CB C 31.700 0.200 1 85 . 24 GLY N N 110.300 0.050 1 86 . 24 GLY H H 8.820 0.010 1 87 . 24 GLY C C 171.500 0.200 1 88 . 24 GLY CA C 44.900 0.200 1 89 . 25 GLY N N 107.300 0.050 1 90 . 25 GLY H H 8.880 0.010 1 91 . 25 GLY C C 170.800 0.200 1 92 . 25 GLY CA C 45.100 0.200 1 93 . 26 TRP N N 119.100 0.050 1 94 . 26 TRP H H 8.430 0.010 1 95 . 26 TRP C C 174.000 0.200 1 96 . 26 TRP CA C 54.200 0.200 1 97 . 26 TRP CB C 32.700 0.200 1 98 . 27 ALA N N 120.500 0.050 1 99 . 27 ALA H H 8.870 0.010 1 100 . 27 ALA C C 174.200 0.200 1 101 . 27 ALA CA C 51.800 0.200 1 102 . 27 ALA CB C 22.800 0.200 1 103 . 28 ALA N N 125.200 0.050 1 104 . 28 ALA H H 9.450 0.010 1 105 . 28 ALA C C 174.000 0.200 1 106 . 28 ALA CA C 50.000 0.200 1 107 . 28 ALA CB C 22.000 0.200 1 108 . 29 LEU N N 126.700 0.050 1 109 . 29 LEU H H 9.300 0.010 1 110 . 29 LEU C C 174.800 0.200 1 111 . 29 LEU CA C 53.000 0.200 1 112 . 29 LEU CB C 45.500 0.200 1 113 . 30 LEU N N 130.400 0.050 1 114 . 30 LEU H H 9.150 0.010 1 115 . 30 LEU C C 175.600 0.200 1 116 . 30 LEU CA C 53.800 0.200 1 117 . 30 LEU CB C 44.100 0.200 1 118 . 31 ARG N N 125.000 0.050 1 119 . 31 ARG H H 9.340 0.010 1 120 . 31 ARG C C 175.400 0.200 1 121 . 31 ARG CA C 55.300 0.200 1 122 . 31 ARG CB C 32.400 0.200 1 123 . 32 PHE N N 127.600 0.050 1 124 . 32 PHE H H 8.390 0.010 1 125 . 32 PHE C C 175.000 0.200 1 126 . 32 PHE CA C 56.000 0.200 1 127 . 32 PHE CB C 39.800 0.200 1 128 . 33 HIS N N 123.000 0.050 1 129 . 33 HIS H H 9.050 0.010 1 130 . 33 HIS C C 175.600 0.200 1 131 . 33 HIS CA C 58.200 0.200 1 132 . 33 HIS CB C 28.600 0.200 1 133 . 34 ALA N N 121.700 0.050 1 134 . 34 ALA H H 8.480 0.010 1 135 . 34 ALA C C 176.500 0.200 1 136 . 34 ALA CA C 52.100 0.200 1 137 . 34 ALA CB C 18.700 0.200 1 138 . 35 HIS N N 117.500 0.050 1 139 . 35 HIS H H 7.530 0.010 1 140 . 35 HIS C C 172.800 0.200 1 141 . 35 HIS CA C 55.300 0.200 1 142 . 35 HIS CB C 31.100 0.200 1 143 . 36 GLU N N 121.800 0.050 1 144 . 36 GLU H H 8.420 0.010 1 145 . 36 GLU C C 175.300 0.200 1 146 . 36 GLU CA C 54.100 0.200 1 147 . 36 GLU CB C 33.300 0.200 1 148 . 37 LYS N N 123.700 0.050 1 149 . 37 LYS H H 8.830 0.010 1 150 . 37 LYS C C 173.000 0.200 1 151 . 37 LYS CA C 55.400 0.200 1 152 . 37 LYS CB C 36.100 0.200 1 153 . 38 LEU N N 130.500 0.050 1 154 . 38 LEU H H 8.620 0.010 1 155 . 38 LEU C C 175.200 0.200 1 156 . 38 LEU CA C 53.600 0.200 1 157 . 38 LEU CB C 43.200 0.200 1 158 . 39 LEU N N 131.300 0.050 1 159 . 39 LEU H H 9.510 0.010 1 160 . 39 LEU C C 175.100 0.200 1 161 . 39 LEU CA C 53.400 0.200 1 162 . 39 LEU CB C 44.000 0.200 1 163 . 40 SER N N 114.900 0.050 1 164 . 40 SER H H 7.850 0.010 1 165 . 40 SER C C 172.300 0.200 1 166 . 40 SER CA C 56.400 0.200 1 167 . 40 SER CB C 65.800 0.200 1 168 . 41 GLY N N 107.000 0.050 1 169 . 41 GLY H H 6.390 0.010 1 170 . 41 GLY C C 170.300 0.200 1 171 . 41 GLY CA C 45.000 0.200 1 172 . 42 GLY N N 105.900 0.050 1 173 . 42 GLY H H 7.960 0.010 1 174 . 42 GLY C C 172.400 0.200 1 175 . 42 GLY CA C 46.200 0.200 1 176 . 43 GLU N N 119.600 0.050 1 177 . 43 GLU H H 8.210 0.010 1 178 . 43 GLU C C 175.100 0.200 1 179 . 43 GLU CA C 55.200 0.200 1 180 . 43 GLU CB C 34.400 0.200 1 181 . 44 ALA N N 125.300 0.050 1 182 . 44 ALA H H 8.280 0.010 1 183 . 44 ALA C C 178.000 0.200 1 184 . 44 ALA CA C 54.700 0.200 1 185 . 44 ALA CB C 19.200 0.200 1 186 . 45 SER N N 111.700 0.050 1 187 . 45 SER H H 7.700 0.010 1 188 . 45 SER C C 172.900 0.200 1 189 . 45 SER CA C 56.700 0.200 1 190 . 45 SER CB C 62.000 0.200 1 191 . 46 THR N N 126.900 0.050 1 192 . 46 THR H H 9.290 0.010 1 193 . 46 THR C C 172.000 0.200 1 194 . 46 THR CA C 59.500 0.200 1 195 . 46 THR CB C 68.300 0.200 1 196 . 47 THR N N 108.700 0.050 1 197 . 47 THR H H 8.340 0.010 1 198 . 47 THR C C 175.300 0.200 1 199 . 47 THR CA C 57.700 0.200 1 200 . 47 THR CB C 72.700 0.200 1 201 . 48 ASN N N 123.200 0.050 1 202 . 48 ASN H H 9.140 0.010 1 203 . 48 ASN C C 177.000 0.200 1 204 . 48 ASN CA C 57.600 0.200 1 205 . 48 ASN CB C 38.700 0.200 1 206 . 49 ASN N N 117.500 0.050 1 207 . 49 ASN H H 8.270 0.010 1 208 . 49 ASN C C 177.000 0.200 1 209 . 49 ASN CA C 55.600 0.200 1 210 . 49 ASN CB C 36.800 0.200 1 211 . 50 ARG N N 118.200 0.050 1 212 . 50 ARG H H 7.250 0.010 1 213 . 50 ARG C C 178.200 0.200 1 214 . 50 ARG CA C 60.600 0.200 1 215 . 50 ARG CB C 29.100 0.200 1 216 . 51 MET N N 119.100 0.050 1 217 . 51 MET H H 7.650 0.010 1 218 . 51 MET C C 178.300 0.200 1 219 . 51 MET CA C 57.500 0.200 1 220 . 51 MET CB C 36.100 0.200 1 221 . 52 GLU N N 121.300 0.050 1 222 . 52 GLU H H 8.320 0.010 1 223 . 52 GLU CA C 59.400 0.200 1 224 . 52 GLU CB C 29.000 0.200 1 225 . 53 LEU N N 118.400 0.050 1 226 . 53 LEU H H 7.210 0.010 1 227 . 53 LEU CA C 57.500 0.200 1 228 . 53 LEU CB C 41.800 0.200 1 229 . 54 LYS N N 121.700 0.050 1 230 . 54 LYS H H 8.570 0.010 1 231 . 54 LYS CA C 58.700 0.200 1 232 . 54 LYS CB C 32.000 0.200 1 233 . 55 ALA N N 119.200 0.050 1 234 . 55 ALA H H 7.770 0.010 1 235 . 55 ALA CA C 55.300 0.200 1 236 . 55 ALA CB C 19.000 0.200 1 237 . 56 ALA N N 117.800 0.050 1 238 . 56 ALA H H 6.570 0.010 1 239 . 56 ALA CA C 55.200 0.200 1 240 . 56 ALA CB C 16.400 0.200 1 241 . 57 ILE N N 118.400 0.050 1 242 . 57 ILE H H 7.900 0.010 1 243 . 57 ILE CA C 66.200 0.200 1 244 . 57 ILE CB C 38.700 0.200 1 245 . 58 GLU N N 117.000 0.050 1 246 . 58 GLU H H 8.180 0.010 1 247 . 58 GLU CA C 58.900 0.200 1 248 . 58 GLU CB C 28.700 0.200 1 249 . 59 GLY N N 106.900 0.050 1 250 . 59 GLY H H 7.840 0.010 1 251 . 59 GLY CA C 47.600 0.200 1 252 . 60 LEU N N 119.200 0.050 1 253 . 60 LEU H H 7.440 0.010 1 254 . 60 LEU C C 175.900 0.200 1 255 . 60 LEU CA C 57.300 0.200 1 256 . 60 LEU CB C 42.600 0.200 1 257 . 61 LYS N N 121.000 0.050 1 258 . 61 LYS H H 8.630 0.010 1 259 . 61 LYS C C 177.600 0.200 1 260 . 61 LYS CA C 58.500 0.200 1 261 . 61 LYS CB C 32.000 0.200 1 262 . 62 ALA N N 120.000 0.050 1 263 . 62 ALA H H 6.980 0.010 1 264 . 62 ALA C C 177.800 0.200 1 265 . 62 ALA CA C 52.700 0.200 1 266 . 62 ALA CB C 18.700 0.200 1 267 . 63 LEU N N 121.200 0.050 1 268 . 63 LEU H H 7.060 0.010 1 269 . 63 LEU C C 176.300 0.200 1 270 . 63 LEU CA C 53.900 0.200 1 271 . 63 LEU CB C 40.800 0.200 1 272 . 64 LYS N N 124.100 0.050 1 273 . 64 LYS H H 8.240 0.010 1 274 . 64 LYS C C 176.700 0.200 1 275 . 64 LYS CA C 56.500 0.200 1 276 . 64 LYS CB C 32.200 0.200 1 277 . 65 GLU N N 119.600 0.050 1 278 . 65 GLU H H 7.510 0.010 1 279 . 65 GLU CA C 53.000 0.200 1 280 . 65 GLU CB C 30.100 0.200 1 281 . 66 PRO C C 177.100 0.200 1 282 . 67 ALA N N 132.900 0.050 1 283 . 67 ALA H H 11.250 0.010 1 284 . 67 ALA C C 177.100 0.200 1 285 . 67 ALA CB C 22.200 0.200 1 286 . 68 GLU N N 124.300 0.050 1 287 . 68 GLU H H 8.510 0.010 1 288 . 68 GLU C C 174.700 0.200 1 289 . 68 GLU CA C 55.400 0.200 1 290 . 68 GLU CB C 30.000 0.200 1 291 . 69 VAL N N 127.200 0.050 1 292 . 69 VAL H H 8.930 0.010 1 293 . 69 VAL C C 175.100 0.200 1 294 . 69 VAL CA C 59.900 0.200 1 295 . 69 VAL CB C 34.600 0.200 1 296 . 70 ASP N N 128.800 0.050 1 297 . 70 ASP H H 8.310 0.010 1 298 . 70 ASP C C 177.600 0.200 1 299 . 70 ASP CA C 53.600 0.200 1 300 . 70 ASP CB C 43.700 0.200 1 301 . 71 LEU N N 130.600 0.050 1 302 . 71 LEU H H 8.410 0.010 1 303 . 71 LEU C C 174.000 0.200 1 304 . 71 LEU CA C 53.700 0.200 1 305 . 71 LEU CB C 43.700 0.200 1 306 . 72 TYR N N 128.000 0.050 1 307 . 72 TYR H H 9.190 0.010 1 308 . 72 TYR C C 175.500 0.200 1 309 . 72 TYR CA C 55.800 0.200 1 310 . 72 TYR CB C 40.400 0.200 1 311 . 73 THR N N 118.500 0.050 1 312 . 73 THR H H 8.100 0.010 1 313 . 73 THR C C 171.800 0.200 1 314 . 73 THR CA C 59.900 0.200 1 315 . 73 THR CB C 69.000 0.200 1 316 . 74 ASP N N 129.100 0.050 1 317 . 74 ASP H H 8.650 0.010 1 318 . 74 ASP C C 175.400 0.200 1 319 . 74 ASP CA C 52.600 0.200 1 320 . 74 ASP CB C 40.400 0.200 1 321 . 75 SER N N 116.100 0.050 1 322 . 75 SER H H 7.840 0.010 1 323 . 75 SER C C 176.500 0.200 1 324 . 75 SER CA C 58.000 0.200 1 325 . 75 SER CB C 64.100 0.200 1 326 . 76 HIS N N 133.500 0.050 1 327 . 76 HIS H H 9.290 0.010 1 328 . 76 HIS C C 176.800 0.200 1 329 . 76 HIS CA C 58.600 0.200 1 330 . 76 HIS CB C 29.400 0.200 1 331 . 77 TYR N N 124.700 0.050 1 332 . 77 TYR H H 8.400 0.010 1 333 . 77 TYR C C 177.500 0.200 1 334 . 77 TYR CA C 59.700 0.200 1 335 . 77 TYR CB C 39.700 0.200 1 336 . 78 LEU N N 118.100 0.050 1 337 . 78 LEU H H 8.070 0.010 1 338 . 78 LEU C C 177.800 0.200 1 339 . 78 LEU CA C 57.700 0.200 1 340 . 78 LEU CB C 41.700 0.200 1 341 . 79 LYS N N 120.000 0.050 1 342 . 79 LYS H H 7.320 0.010 1 343 . 79 LYS C C 179.900 0.200 1 344 . 79 LYS CA C 59.100 0.200 1 345 . 79 LYS CB C 31.800 0.200 1 346 . 80 LYS N N 122.600 0.050 1 347 . 80 LYS H H 7.790 0.010 1 348 . 80 LYS C C 177.300 0.200 1 349 . 80 LYS CA C 59.000 0.200 1 350 . 80 LYS CB C 31.300 0.200 1 351 . 81 ALA N N 120.200 0.050 1 352 . 81 ALA H H 6.890 0.010 1 353 . 81 ALA C C 179.800 0.200 1 354 . 81 ALA CA C 54.300 0.200 1 355 . 81 ALA CB C 19.700 0.200 1 356 . 82 PHE N N 114.600 0.050 1 357 . 82 PHE H H 7.600 0.010 1 358 . 82 PHE C C 178.000 0.200 1 359 . 82 PHE CA C 60.900 0.200 1 360 . 82 PHE CB C 38.800 0.200 1 361 . 83 THR N N 114.100 0.050 1 362 . 83 THR H H 7.810 0.010 1 363 . 83 THR C C 176.600 0.200 1 364 . 83 THR CA C 64.200 0.200 1 365 . 83 THR CB C 70.000 0.200 1 366 . 84 GLU N N 121.100 0.050 1 367 . 84 GLU H H 7.620 0.010 1 368 . 84 GLU C C 177.400 0.200 1 369 . 84 GLU CA C 55.800 0.200 1 370 . 84 GLU CB C 28.600 0.200 1 371 . 85 GLY N N 108.200 0.050 1 372 . 85 GLY H H 7.190 0.010 1 373 . 85 GLY C C 176.100 0.200 1 374 . 85 GLY CA C 46.500 0.200 1 375 . 86 TRP N N 121.200 0.050 1 376 . 86 TRP H H 7.010 0.010 1 377 . 86 TRP C C 176.900 0.200 1 378 . 86 TRP CA C 57.800 0.200 1 379 . 86 TRP CB C 28.300 0.200 1 380 . 87 LEU N N 118.400 0.050 1 381 . 87 LEU H H 7.200 0.010 1 382 . 87 LEU C C 178.500 0.200 1 383 . 87 LEU CA C 57.700 0.200 1 384 . 87 LEU CB C 40.600 0.200 1 385 . 88 GLU N N 119.200 0.050 1 386 . 88 GLU H H 7.630 0.010 1 387 . 88 GLU C C 179.000 0.200 1 388 . 88 GLU CA C 58.400 0.200 1 389 . 88 GLU CB C 28.600 0.200 1 390 . 89 GLY N N 107.700 0.050 1 391 . 89 GLY H H 7.260 0.010 1 392 . 89 GLY C C 176.300 0.200 1 393 . 89 GLY CA C 47.000 0.200 1 394 . 90 TRP N N 123.500 0.050 1 395 . 90 TRP H H 7.800 0.010 1 396 . 90 TRP CA C 57.500 0.200 1 397 . 90 TRP CB C 28.600 0.200 1 398 . 91 ARG N N 120.400 0.050 1 399 . 91 ARG H H 7.580 0.010 1 400 . 91 ARG CA C 59.100 0.200 1 401 . 91 ARG CB C 29.400 0.200 1 402 . 92 LYS N N 120.400 0.050 1 403 . 92 LYS H H 7.560 0.010 1 404 . 92 LYS C C 177.900 0.200 1 405 . 92 LYS CA C 58.300 0.200 1 406 . 92 LYS CB C 32.100 0.200 1 407 . 93 ARG N N 118.300 0.050 1 408 . 93 ARG H H 7.310 0.010 1 409 . 93 ARG C C 176.800 0.200 1 410 . 93 ARG CA C 55.200 0.200 1 411 . 93 ARG CB C 30.700 0.200 1 412 . 94 GLY N N 110.700 0.050 1 413 . 94 GLY H H 7.560 0.010 1 414 . 94 GLY C C 174.900 0.200 1 415 . 94 GLY CA C 46.900 0.200 1 416 . 95 TRP N N 115.800 0.050 1 417 . 95 TRP H H 8.330 0.010 1 418 . 95 TRP C C 175.000 0.200 1 419 . 95 TRP CA C 57.800 0.200 1 420 . 95 TRP CB C 25.500 0.200 1 421 . 96 ARG N N 119.700 0.050 1 422 . 96 ARG H H 6.840 0.010 1 423 . 96 ARG C C 176.400 0.200 1 424 . 96 ARG CA C 53.600 0.200 1 425 . 96 ARG CB C 33.700 0.200 1 426 . 97 THR N N 113.100 0.050 1 427 . 97 THR H H 8.970 0.010 1 428 . 97 THR C C 177.000 0.200 1 429 . 97 THR CA C 60.300 0.200 1 430 . 97 THR CB C 71.700 0.200 1 431 . 98 ALA N N 125.900 0.050 1 432 . 98 ALA H H 8.970 0.010 1 433 . 98 ALA C C 178.700 0.200 1 434 . 98 ALA CA C 54.600 0.200 1 435 . 98 ALA CB C 17.700 0.200 1 436 . 99 GLU N N 115.400 0.050 1 437 . 99 GLU H H 7.630 0.010 1 438 . 99 GLU C C 176.700 0.200 1 439 . 99 GLU CA C 56.100 0.200 1 440 . 99 GLU CB C 29.300 0.200 1 441 . 100 GLY N N 109.800 0.050 1 442 . 100 GLY H H 7.950 0.010 1 443 . 100 GLY C C 173.800 0.200 1 444 . 100 GLY CA C 45.400 0.200 1 445 . 101 LYS N N 122.100 0.050 1 446 . 101 LYS H H 7.090 0.010 1 447 . 101 LYS CA C 53.400 0.200 1 448 . 101 LYS CB C 31.400 0.200 1 449 . 102 PRO C C 177.100 0.200 1 450 . 102 PRO CA C 62.800 0.200 1 451 . 102 PRO CB C 31.600 0.200 1 452 . 103 VAL N N 124.900 0.050 1 453 . 103 VAL H H 7.620 0.010 1 454 . 103 VAL C C 176.600 0.200 1 455 . 103 VAL CA C 62.200 0.200 1 456 . 103 VAL CB C 32.400 0.200 1 457 . 104 LYS N N 130.600 0.050 1 458 . 104 LYS H H 8.240 0.010 1 459 . 104 LYS C C 177.200 0.200 1 460 . 104 LYS CA C 56.700 0.200 1 461 . 104 LYS CB C 32.100 0.200 1 462 . 105 ASN N N 115.100 0.050 1 463 . 105 ASN H H 8.890 0.010 1 464 . 105 ASN C C 175.100 0.200 1 465 . 105 ASN CA C 54.300 0.200 1 466 . 105 ASN CB C 36.600 0.200 1 467 . 106 ARG N N 120.900 0.050 1 468 . 106 ARG H H 7.670 0.010 1 469 . 106 ARG C C 175.300 0.200 1 470 . 106 ARG CA C 59.700 0.200 1 471 . 106 ARG CB C 29.300 0.200 1 472 . 107 ASP N N 117.000 0.050 1 473 . 107 ASP H H 8.410 0.010 1 474 . 107 ASP C C 175.300 0.200 1 475 . 107 ASP CA C 56.000 0.200 1 476 . 107 ASP CB C 38.200 0.200 1 477 . 108 LEU N N 122.800 0.050 1 478 . 108 LEU H H 7.250 0.010 1 479 . 108 LEU C C 178.700 0.200 1 480 . 108 LEU CA C 55.300 0.200 1 481 . 108 LEU CB C 41.800 0.200 1 482 . 109 TRP N N 122.900 0.050 1 483 . 109 TRP H H 8.130 0.010 1 484 . 109 TRP C C 179.100 0.200 1 485 . 109 TRP CA C 60.700 0.200 1 486 . 109 TRP CB C 30.500 0.200 1 487 . 110 GLU N N 118.300 0.050 1 488 . 110 GLU H H 8.330 0.010 1 489 . 110 GLU C C 179.500 0.200 1 490 . 110 GLU CA C 59.900 0.200 1 491 . 110 GLU CB C 28.800 0.200 1 492 . 111 ALA N N 122.600 0.050 1 493 . 111 ALA H H 7.080 0.010 1 494 . 111 ALA CA C 54.600 0.200 1 495 . 111 ALA CB C 16.200 0.200 1 496 . 112 LEU N N 123.700 0.050 1 497 . 112 LEU H H 8.600 0.010 1 498 . 112 LEU C C 178.100 0.200 1 499 . 112 LEU CA C 58.300 0.200 1 500 . 112 LEU CB C 39.800 0.200 1 501 . 113 LEU N N 121.200 0.050 1 502 . 113 LEU H H 8.120 0.010 1 503 . 113 LEU C C 180.900 0.200 1 504 . 113 LEU CA C 58.400 0.200 1 505 . 113 LEU CB C 41.000 0.200 1 506 . 114 LEU N N 120.600 0.050 1 507 . 114 LEU H H 7.630 0.010 1 508 . 114 LEU C C 179.800 0.200 1 509 . 114 LEU CA C 57.500 0.200 1 510 . 114 LEU CB C 41.500 0.200 1 511 . 115 ALA N N 123.500 0.050 1 512 . 115 ALA H H 8.070 0.010 1 513 . 115 ALA C C 179.500 0.200 1 514 . 115 ALA CA C 53.600 0.200 1 515 . 115 ALA CB C 18.400 0.200 1 516 . 116 MET N N 115.000 0.050 1 517 . 116 MET H H 8.270 0.010 1 518 . 116 MET C C 177.100 0.200 1 519 . 116 MET CA C 57.700 0.200 1 520 . 116 MET CB C 34.800 0.200 1 521 . 117 ALA N N 123.100 0.050 1 522 . 117 ALA H H 7.020 0.010 1 523 . 117 ALA CA C 56.400 0.200 1 524 . 117 ALA CB C 16.200 0.200 1 525 . 118 PRO C C 176.600 0.200 1 526 . 118 PRO CA C 63.900 0.200 1 527 . 118 PRO CB C 31.200 0.200 1 528 . 119 HIS N N 117.400 0.050 1 529 . 119 HIS H H 7.570 0.010 1 530 . 119 HIS C C 175.200 0.200 1 531 . 119 HIS CA C 55.000 0.200 1 532 . 119 HIS CB C 34.900 0.200 1 533 . 120 ARG N N 122.600 0.050 1 534 . 120 ARG H H 8.160 0.010 1 535 . 120 ARG C C 175.200 0.200 1 536 . 120 ARG CA C 54.800 0.200 1 537 . 120 ARG CB C 30.500 0.200 1 538 . 121 VAL N N 127.800 0.050 1 539 . 121 VAL H H 8.680 0.010 1 540 . 121 VAL C C 175.000 0.200 1 541 . 121 VAL CA C 61.300 0.200 1 542 . 121 VAL CB C 32.700 0.200 1 543 . 122 ARG N N 130.500 0.050 1 544 . 122 ARG H H 8.780 0.010 1 545 . 122 ARG C C 174.300 0.200 1 546 . 122 ARG CA C 54.100 0.200 1 547 . 122 ARG CB C 31.100 0.200 1 548 . 123 PHE N N 125.900 0.050 1 549 . 123 PHE H H 8.390 0.010 1 550 . 123 PHE C C 176.000 0.200 1 551 . 123 PHE CA C 58.200 0.200 1 552 . 123 PHE CB C 40.700 0.200 1 553 . 124 HIS N N 125.000 0.050 1 554 . 124 HIS H H 8.520 0.010 1 555 . 124 HIS C C 172.500 0.200 1 556 . 124 HIS CA C 53.200 0.200 1 557 . 124 HIS CB C 29.800 0.200 1 558 . 125 PHE N N 125.800 0.050 1 559 . 125 PHE H H 8.450 0.010 1 560 . 125 PHE C C 176.400 0.200 1 561 . 125 PHE CA C 56.900 0.200 1 562 . 125 PHE CB C 38.300 0.200 1 563 . 126 VAL N N 126.000 0.050 1 564 . 126 VAL H H 7.790 0.010 1 565 . 126 VAL C C 174.400 0.200 1 566 . 126 VAL CA C 60.400 0.200 1 567 . 126 VAL CB C 33.000 0.200 1 568 . 127 LYS N N 124.600 0.050 1 569 . 127 LYS H H 8.080 0.010 1 570 . 127 LYS C C 177.000 0.200 1 571 . 127 LYS CA C 55.800 0.200 1 572 . 127 LYS CB C 32.900 0.200 1 573 . 128 GLY N N 113.000 0.050 1 574 . 128 GLY H H 8.200 0.010 1 575 . 128 GLY CA C 44.700 0.200 1 576 . 129 HIS C C 179.000 0.200 1 577 . 129 HIS CA C 55.500 0.200 1 578 . 129 HIS CB C 29.000 0.200 1 579 . 130 THR N N 115.900 0.050 1 580 . 130 THR H H 7.820 0.010 1 581 . 130 THR C C 175.400 0.200 1 582 . 130 THR CA C 62.500 0.200 1 583 . 130 THR CB C 69.300 0.200 1 584 . 131 GLY N N 114.000 0.050 1 585 . 131 GLY H H 8.560 0.010 1 586 . 131 GLY C C 174.400 0.200 1 587 . 131 GLY CA C 45.400 0.200 1 588 . 132 HIS N N 119.700 0.050 1 589 . 132 HIS H H 7.960 0.010 1 590 . 132 HIS CA C 52.900 0.200 1 591 . 132 HIS CB C 28.900 0.200 1 592 . 133 PRO C C 179.400 0.200 1 593 . 133 PRO CA C 65.600 0.200 1 594 . 133 PRO CB C 31.200 0.200 1 595 . 134 GLU N N 120.600 0.050 1 596 . 134 GLU H H 9.150 0.010 1 597 . 134 GLU C C 178.600 0.200 1 598 . 134 GLU CA C 60.200 0.200 1 599 . 134 GLU CB C 26.600 0.200 1 600 . 135 ASN N N 117.000 0.050 1 601 . 135 ASN H H 7.220 0.010 1 602 . 135 ASN C C 177.300 0.200 1 603 . 135 ASN CA C 57.500 0.200 1 604 . 135 ASN CB C 38.800 0.200 1 605 . 136 GLU N N 122.200 0.050 1 606 . 136 GLU H H 7.660 0.010 1 607 . 136 GLU C C 178.700 0.200 1 608 . 136 GLU CA C 59.200 0.200 1 609 . 136 GLU CB C 28.100 0.200 1 610 . 137 ARG N N 120.300 0.050 1 611 . 137 ARG H H 7.590 0.010 1 612 . 137 ARG C C 180.200 0.200 1 613 . 137 ARG CA C 59.200 0.200 1 614 . 137 ARG CB C 29.900 0.200 1 615 . 138 VAL N N 114.300 0.050 1 616 . 138 VAL H H 7.600 0.010 1 617 . 138 VAL C C 177.300 0.200 1 618 . 138 VAL CA C 65.300 0.200 1 619 . 138 VAL CB C 30.900 0.200 1 620 . 139 ASP N N 125.400 0.050 1 621 . 139 ASP H H 7.760 0.010 1 622 . 139 ASP C C 176.700 0.200 1 623 . 139 ASP CA C 57.000 0.200 1 624 . 139 ASP CB C 41.300 0.200 1 625 . 140 ARG N N 119.000 0.050 1 626 . 140 ARG H H 7.840 0.010 1 627 . 140 ARG C C 179.700 0.200 1 628 . 140 ARG CA C 59.200 0.200 1 629 . 140 ARG CB C 29.600 0.200 1 630 . 141 GLU N N 121.600 0.050 1 631 . 141 GLU H H 7.680 0.010 1 632 . 141 GLU C C 177.800 0.200 1 633 . 141 GLU CA C 57.500 0.200 1 634 . 141 GLU CB C 27.500 0.200 1 635 . 142 ALA N N 125.500 0.050 1 636 . 142 ALA H H 8.370 0.010 1 637 . 142 ALA C C 180.100 0.200 1 638 . 142 ALA CA C 55.700 0.200 1 639 . 142 ALA CB C 17.000 0.200 1 640 . 143 ARG N N 117.700 0.050 1 641 . 143 ARG H H 7.680 0.010 1 642 . 143 ARG C C 178.500 0.200 1 643 . 143 ARG CA C 59.400 0.200 1 644 . 143 ARG CB C 28.900 0.200 1 645 . 144 ARG N N 124.300 0.050 1 646 . 144 ARG H H 8.080 0.010 1 647 . 144 ARG C C 180.600 0.200 1 648 . 144 ARG CA C 59.200 0.200 1 649 . 144 ARG CB C 29.600 0.200 1 650 . 145 GLN N N 120.600 0.050 1 651 . 145 GLN H H 8.070 0.010 1 652 . 145 GLN C C 179.500 0.200 1 653 . 145 GLN CA C 58.000 0.200 1 654 . 145 GLN CB C 28.200 0.200 1 655 . 146 ALA N N 124.500 0.050 1 656 . 146 ALA H H 7.890 0.010 1 657 . 146 ALA C C 176.800 0.200 1 658 . 146 ALA CA C 55.400 0.200 1 659 . 146 ALA CB C 17.100 0.200 1 660 . 147 GLN N N 116.200 0.050 1 661 . 147 GLN H H 7.850 0.010 1 662 . 147 GLN C C 178.900 0.200 1 663 . 147 GLN CA C 57.800 0.200 1 664 . 147 GLN CB C 28.000 0.200 1 665 . 148 SER N N 116.800 0.050 1 666 . 148 SER H H 7.790 0.010 1 667 . 148 SER C C 176.500 0.200 1 668 . 148 SER CA C 60.500 0.200 1 669 . 148 SER CB C 62.900 0.200 1 670 . 149 GLN N N 121.300 0.050 1 671 . 149 GLN H H 7.490 0.010 1 672 . 149 GLN C C 177.000 0.200 1 673 . 149 GLN CA C 56.100 0.200 1 674 . 149 GLN CB C 28.300 0.200 1 675 . 150 ALA N N 123.600 0.050 1 676 . 150 ALA H H 7.560 0.010 1 677 . 150 ALA C C 177.700 0.200 1 678 . 150 ALA CA C 52.500 0.200 1 679 . 150 ALA CB C 18.500 0.200 1 680 . 151 LYS N N 120.200 0.050 1 681 . 151 LYS H H 7.620 0.010 1 682 . 151 LYS C C 177.900 0.200 1 683 . 151 LYS CA C 56.000 0.200 1 684 . 151 LYS CB C 32.400 0.200 1 685 . 152 THR N N 118.800 0.050 1 686 . 152 THR H H 7.830 0.010 1 687 . 152 THR CA C 59.300 0.200 1 688 . 152 THR CB C 69.700 0.200 1 689 . 156 PRO C C 177.000 0.200 1 690 . 156 PRO CA C 62.700 0.200 1 691 . 156 PRO CB C 31.500 0.200 1 692 . 157 ARG N N 122.900 0.050 1 693 . 157 ARG H H 8.130 0.010 1 694 . 157 ARG C C 175.900 0.200 1 695 . 157 ARG CA C 55.300 0.200 1 696 . 157 ARG CB C 30.600 0.200 1 697 . 158 ALA N N 128.400 0.050 1 698 . 158 ALA H H 8.110 0.010 1 699 . 158 ALA CA C 50.200 0.200 1 700 . 158 ALA CB C 17.600 0.200 1 701 . 159 PRO C C 177.100 0.200 1 702 . 159 PRO CA C 62.900 0.200 1 703 . 159 PRO CB C 31.600 0.200 1 704 . 160 THR N N 115.900 0.050 1 705 . 160 THR H H 7.920 0.010 1 706 . 160 THR C C 174.300 0.200 1 707 . 160 THR CA C 61.400 0.200 1 708 . 160 THR CB C 69.800 0.200 1 709 . 161 LEU N N 126.300 0.050 1 710 . 161 LEU H H 7.940 0.010 1 711 . 161 LEU C C 176.800 0.200 1 712 . 161 LEU CA C 54.800 0.200 1 713 . 161 LEU CB C 41.900 0.200 1 714 . 162 PHE N N 122.600 0.050 1 715 . 162 PHE H H 7.990 0.010 1 716 . 162 PHE C C 175.300 0.200 1 717 . 162 PHE CA C 57.300 0.200 1 718 . 162 PHE CB C 39.400 0.200 1 719 . 163 HIS N N 122.600 0.050 1 720 . 163 HIS H H 8.090 0.010 1 721 . 163 HIS C C 173.700 0.200 1 722 . 163 HIS CA C 54.900 0.200 1 723 . 163 HIS CB C 29.400 0.200 1 724 . 164 GLU N N 124.800 0.050 1 725 . 164 GLU H H 8.250 0.010 1 726 . 164 GLU C C 176.200 0.200 1 727 . 164 GLU CA C 56.200 0.200 1 728 . 164 GLU CB C 30.000 0.200 1 729 . 165 GLU N N 124.400 0.050 1 730 . 165 GLU H H 8.300 0.010 1 731 . 165 GLU C C 175.200 0.200 1 732 . 165 GLU CA C 56.000 0.200 1 733 . 165 GLU CB C 30.000 0.200 1 734 . 166 ALA N N 132.400 0.050 1 735 . 166 ALA H H 7.780 0.010 1 736 . 166 ALA CA C 53.400 0.200 1 737 . 166 ALA CB C 19.600 0.200 1 stop_ save_