data_5031 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N resonance assignments of the N-terminal, 135-residue domain of KaiA, a clock protein from Synechococcus elongatus ; _BMRB_accession_number 5031 _BMRB_flat_file_name bmr5031.str _Entry_type original _Submission_date 2001-05-24 _Accession_date 2001-05-24 _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 Vakonakis Ioannis . . 2 Risinger Aaron T. . 3 Latham Michael P. . 4 Williams Stanly B. . 5 Golden Susan S. . 6 LiWang Andy C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 773 "13C chemical shifts" 596 "15N chemical shifts" 147 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-13 update author 'update of chemical shifts' 2001-05-25 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the N-terminal, 135-residue domain of KaiA, a clock protein from Synechococcus elongatus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vakonakis Ioannis . . 2 Risinger Aaron T. . 3 Latham Michael P. . 4 Williams Stanly B. . 5 Golden Susan S. . 6 LiWang Andy C. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 179 _Page_last 180 _Year 2001 _Details . loop_ _Keyword assignment 'circadian clock' KaiA 'Synechococcus elongatus' stop_ save_ ################################## # Molecular system description # ################################## save_system_KaiA_N-terminus _Saveframe_category molecular_system _Mol_system_name 'KaiA N-terminus' _Abbreviation_common 'KaiA N-terminus' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiA N-terminus' $KaiA_N-terminus stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_KaiA_N-terminus _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common KaiA _Name_variant N-terminus _Abbreviation_common 'KaiA N-terminus' _Molecular_mass 15066 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; MLSQIAICIWVESTAILQDC QRALSADRYQLQVCESGEML LEYAQTHRDQIDCLILVAAN PSFRAVVQQLCFEGVVVPAI VVGDRDSEDPDEPAKEQLYH SAELHLGIHQLEQLPYQVDA ALAEFLRLAPVETMA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 SER 4 GLN 5 ILE 6 ALA 7 ILE 8 CYS 9 ILE 10 TRP 11 VAL 12 GLU 13 SER 14 THR 15 ALA 16 ILE 17 LEU 18 GLN 19 ASP 20 CYS 21 GLN 22 ARG 23 ALA 24 LEU 25 SER 26 ALA 27 ASP 28 ARG 29 TYR 30 GLN 31 LEU 32 GLN 33 VAL 34 CYS 35 GLU 36 SER 37 GLY 38 GLU 39 MET 40 LEU 41 LEU 42 GLU 43 TYR 44 ALA 45 GLN 46 THR 47 HIS 48 ARG 49 ASP 50 GLN 51 ILE 52 ASP 53 CYS 54 LEU 55 ILE 56 LEU 57 VAL 58 ALA 59 ALA 60 ASN 61 PRO 62 SER 63 PHE 64 ARG 65 ALA 66 VAL 67 VAL 68 GLN 69 GLN 70 LEU 71 CYS 72 PHE 73 GLU 74 GLY 75 VAL 76 VAL 77 VAL 78 PRO 79 ALA 80 ILE 81 VAL 82 VAL 83 GLY 84 ASP 85 ARG 86 ASP 87 SER 88 GLU 89 ASP 90 PRO 91 ASP 92 GLU 93 PRO 94 ALA 95 LYS 96 GLU 97 GLN 98 LEU 99 TYR 100 HIS 101 SER 102 ALA 103 GLU 104 LEU 105 HIS 106 LEU 107 GLY 108 ILE 109 HIS 110 GLN 111 LEU 112 GLU 113 GLN 114 LEU 115 PRO 116 TYR 117 GLN 118 VAL 119 ASP 120 ALA 121 ALA 122 LEU 123 ALA 124 GLU 125 PHE 126 LEU 127 ARG 128 LEU 129 ALA 130 PRO 131 VAL 132 GLU 133 THR 134 MET 135 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 PDB 1M2E "Solution Structure Of The N-Terminal Domain Of Synechococcus Elongatus Kaia (Kaia135n); Average Minimized Structure." 100.00 135 100.00 100.00 2.38e-91 PDB 1M2F "Solution Structure Of The N-Terminal Domain Of Synechococcus Elongatus Kaia (Kaia135n); Family Of 25 Structures" 100.00 135 100.00 100.00 2.38e-91 PDB 1R8J "Crystal Structure Of Circadian Clock Protein Kaia From Synechococcus Elongatus" 100.00 289 99.26 100.00 1.45e-89 PDB 4G86 "Crystal Structure Of The Redox-active Cofactor Dbmib Bound To The Full Length Circadian Clock Protein Kaia From Synechococcus E" 100.00 284 99.26 100.00 1.59e-89 DBJ BAA37101 "KaiA [Synechococcus elongatus PCC 7942]" 100.00 284 100.00 100.00 2.25e-90 DBJ BAD78522 "circadian clock protein KaiA [Synechococcus elongatus PCC 6301]" 100.00 284 99.26 99.26 1.51e-89 GB AAM82684 "KaiA [Synechococcus elongatus PCC 7942]" 100.00 284 100.00 100.00 2.25e-90 GB ABB57248 "circadian clock protein KaiA [Synechococcus elongatus PCC 7942]" 100.00 284 100.00 100.00 2.25e-90 GB AJD58238 "circadian clock protein KaiA [Synechococcus sp. UTEX 2973]" 100.00 284 100.00 100.00 2.25e-90 REF WP_011242646 "circadian clock protein KaiA [Synechococcus elongatus]" 100.00 284 99.26 99.26 1.51e-89 REF WP_011377921 "circadian clock protein KaiA [Synechococcus elongatus]" 100.00 284 100.00 100.00 2.25e-90 REF YP_171042 "circadian clock protein KaiA [Synechococcus elongatus PCC 6301]" 100.00 284 99.26 99.26 1.51e-89 REF YP_400235 "circadian clock protein KaiA [Synechococcus elongatus PCC 7942]" 100.00 284 100.00 100.00 2.25e-90 SP Q79PF6 "RecName: Full=Circadian clock protein KaiA [Synechococcus elongatus PCC 7942]" 100.00 284 100.00 100.00 2.25e-90 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $KaiA_N-terminus 'Synechococcus elongatus' 32046 Eubacteria . Synechococcus elongatus 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 $KaiA_N-terminus 'recombinant technology' Escherichia coli . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_KaiA-135 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $KaiA_N-terminus . mM 2.9 3.4 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version '1.8 rev 2001.030.21.27' loop_ _Task 'NMR data processing' stop_ _Details ; Delaglio, F., S. Grzesiek, Vuister, G.W., Zhu, G., Pfeifer, J. and A. Bax. (1995) J. Biomol. NMR. 6, 277-293. ; save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.2.6 loop_ _Task 'Spectra visualization' stop_ _Details ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M, (1991) J. Magn. Reson., 95, 214-220. ; save_ save_STAPP _Saveframe_category software _Name STAPP _Version 4.2.6 loop_ _Task 'Spin system creation' 'partial sequence specific assignments' stop_ _Details ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M, (1991) J. Magn. Reson., 95, 214-220. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details 'Triple resonance, XYZ-PGF probe was used.' save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_HBHACONH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label . save_ save_HCCH-COSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.05 n/a temperature 298 0.05 K 'ionic strength' 0.22 0.016 M 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_cs_KaiA-135 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' HNHA CBCA(CO)NH CBCANH C(CO)NH H(CCO)NH HBHACONH HCCH-COSY stop_ loop_ _Sample_label $sample_KaiA-135 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'KaiA N-terminus' _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 . 2 LEU CA C 55.24 0.50 1 2 . 2 LEU CB C 42.44 0.50 1 3 . 2 LEU HA H 4.43 0.05 1 4 . 2 LEU HB2 H 1.55 0.05 2 5 . 2 LEU HB3 H 1.65 0.05 2 6 . 2 LEU CG C 27.05 0.50 1 7 . 2 LEU HG H 1.62 0.05 1 8 . 2 LEU CD2 C 25.02 0.50 2 9 . 2 LEU CD1 C 23.49 0.50 2 10 . 2 LEU HD2 H 0.93 0.05 2 11 . 2 LEU HD1 H 0.90 0.05 2 12 . 2 LEU C C 176.99 0.50 1 13 . 3 SER H H 8.44 0.05 1 14 . 3 SER N N 117.57 0.30 1 15 . 3 SER CA C 58.70 0.50 1 16 . 3 SER CB C 63.59 0.50 1 17 . 3 SER HA H 4.36 0.05 1 18 . 3 SER HB2 H 3.86 0.05 1 19 . 3 SER HB3 H 3.86 0.05 1 20 . 3 SER C C 174.05 0.50 1 21 . 4 GLN H H 8.14 0.05 1 22 . 4 GLN N N 121.29 0.30 1 23 . 4 GLN CA C 55.50 0.50 1 24 . 4 GLN CB C 31.57 0.50 1 25 . 4 GLN HA H 4.72 0.05 1 26 . 4 GLN HB2 H 1.85 0.05 2 27 . 4 GLN HB3 H 1.92 0.05 2 28 . 4 GLN CG C 34.73 0.50 1 29 . 4 GLN CD C 177.70 0.50 1 30 . 4 GLN HG2 H 2.23 0.05 1 31 . 4 GLN HG3 H 2.23 0.05 1 32 . 4 GLN NE2 N 112.06 0.30 1 33 . 4 GLN HE22 H 6.80 0.05 1 34 . 4 GLN HE21 H 7.41 0.05 1 35 . 4 GLN C C 175.46 0.50 1 36 . 5 ILE H H 8.63 0.05 1 37 . 5 ILE N N 123.76 0.30 1 38 . 5 ILE CA C 60.94 0.50 1 39 . 5 ILE CB C 40.28 0.50 1 40 . 5 ILE HA H 4.28 0.05 1 41 . 5 ILE HB H 1.82 0.05 1 42 . 5 ILE CG1 C 27.66 0.50 1 43 . 5 ILE CG2 C 17.86 0.50 1 44 . 5 ILE CD1 C 12.84 0.50 1 45 . 5 ILE HG12 H 1.48 0.05 2 46 . 5 ILE HG13 H 0.99 0.05 2 47 . 5 ILE HD1 H 0.89 0.05 1 48 . 5 ILE HG2 H 0.90 0.05 1 49 . 5 ILE C C 174.17 0.50 1 50 . 6 ALA H H 10.24 0.05 1 51 . 6 ALA N N 133.66 0.30 1 52 . 6 ALA CA C 51.83 0.50 1 53 . 6 ALA CB C 19.29 0.50 1 54 . 6 ALA HA H 4.99 0.05 1 55 . 6 ALA HB H 1.47 0.05 1 56 . 6 ALA C C 176.32 0.50 1 57 . 7 ILE H H 8.91 0.05 1 58 . 7 ILE N N 126.51 0.30 1 59 . 7 ILE CA C 58.60 0.50 1 60 . 7 ILE CB C 39.88 0.50 1 61 . 7 ILE HA H 5.00 0.05 1 62 . 7 ILE HB H 1.84 0.05 1 63 . 7 ILE CG1 C 27.92 0.50 1 64 . 7 ILE CG2 C 17.49 0.50 1 65 . 7 ILE CD1 C 14.67 0.50 1 66 . 7 ILE HG12 H 1.18 0.05 2 67 . 7 ILE HG13 H 1.64 0.05 2 68 . 7 ILE HD1 H 0.81 0.05 1 69 . 7 ILE HG2 H 0.67 0.05 1 70 . 7 ILE C C 174.65 0.50 1 71 . 8 CYS H H 8.62 0.05 1 72 . 8 CYS N N 128.29 0.30 1 73 . 8 CYS CA C 56.78 0.50 1 74 . 8 CYS CB C 28.88 0.50 1 75 . 8 CYS HA H 5.44 0.05 1 76 . 8 CYS HB2 H 2.78 0.05 1 77 . 8 CYS HB3 H 2.78 0.05 1 78 . 8 CYS C C 172.43 0.50 1 79 . 9 ILE H H 9.22 0.05 1 80 . 9 ILE N N 127.88 0.30 1 81 . 9 ILE CA C 58.72 0.50 1 82 . 9 ILE CB C 41.79 0.50 1 83 . 9 ILE HA H 5.38 0.05 1 84 . 9 ILE HB H 1.62 0.05 1 85 . 9 ILE CG1 C 27.99 0.50 1 86 . 9 ILE HG12 H 1.60 0.05 2 87 . 9 ILE HG13 H 0.80 0.05 2 88 . 9 ILE CD1 C 16.57 0.50 1 89 . 9 ILE CG2 C 17.38 0.50 1 90 . 9 ILE HG2 H 0.89 0.05 1 91 . 9 ILE HD1 H 0.71 0.05 1 92 . 9 ILE C C 173.85 0.50 1 93 . 10 TRP H H 8.80 0.05 1 94 . 10 TRP N N 127.73 0.30 1 95 . 10 TRP CA C 53.78 0.50 1 96 . 10 TRP CB C 30.22 0.50 1 97 . 10 TRP HA H 6.06 0.05 1 98 . 10 TRP HB3 H 3.37 0.05 1 99 . 10 TRP HB2 H 2.84 0.05 1 100 . 10 TRP CD1 C 126.66 0.50 1 101 . 10 TRP HD1 H 7.22 0.05 1 102 . 10 TRP CE3 C 119.53 0.50 1 103 . 10 TRP HE3 H 7.40 0.05 1 104 . 10 TRP NE1 N 134.32 0.30 1 105 . 10 TRP HE1 H 11.56 0.05 1 106 . 10 TRP CZ2 C 116.40 0.50 1 107 . 10 TRP HZ2 H 7.68 0.05 1 108 . 10 TRP CH2 C 124.93 0.50 1 109 . 10 TRP HH2 H 7.13 0.05 1 110 . 10 TRP CZ3 C 121.51 0.50 1 111 . 10 TRP HZ3 H 6.90 0.05 1 112 . 10 TRP C C 173.94 0.50 1 113 . 11 VAL H H 8.36 0.05 1 114 . 11 VAL N N 125.66 0.30 1 115 . 11 VAL CA C 59.90 0.50 1 116 . 11 VAL CB C 34.44 0.50 1 117 . 11 VAL HA H 4.23 0.05 1 118 . 11 VAL HB H 1.87 0.05 1 119 . 11 VAL CG2 C 22.87 0.50 2 120 . 11 VAL CG1 C 20.94 0.50 2 121 . 11 VAL HG2 H 1.02 0.05 2 122 . 11 VAL HG1 H 0.92 0.05 2 123 . 11 VAL C C 171.97 0.50 1 124 . 12 GLU H H 8.27 0.05 1 125 . 12 GLU N N 125.08 0.30 1 126 . 12 GLU CA C 56.01 0.50 1 127 . 12 GLU CB C 29.51 0.50 1 128 . 12 GLU HA H 4.60 0.05 1 129 . 12 GLU HB3 H 2.38 0.05 1 130 . 12 GLU HB2 H 1.53 0.05 1 131 . 12 GLU CG C 36.49 0.50 1 132 . 12 GLU HG2 H 2.22 0.05 2 133 . 12 GLU HG3 H 1.80 0.05 2 134 . 12 GLU C C 175.30 0.50 1 135 . 13 SER H H 7.05 0.05 1 136 . 13 SER N N 114.13 0.30 1 137 . 13 SER CA C 55.85 0.50 1 138 . 13 SER CB C 64.59 0.50 1 139 . 13 SER HA H 4.85 0.05 1 140 . 13 SER HB2 H 4.04 0.05 1 141 . 13 SER HB3 H 3.53 0.05 1 142 . 13 SER C C 174.34 0.50 1 143 . 14 THR H H 8.96 0.05 1 144 . 14 THR N N 125.43 0.30 1 145 . 14 THR CA C 66.18 0.50 1 146 . 14 THR CB C 68.57 0.50 1 147 . 14 THR HB H 4.15 0.05 1 148 . 14 THR HA H 3.90 0.05 1 149 . 14 THR CG2 C 22.15 0.50 1 150 . 14 THR HG2 H 1.28 0.05 1 151 . 14 THR C C 175.77 0.50 1 152 . 15 ALA H H 8.23 0.05 1 153 . 15 ALA N N 124.34 0.30 1 154 . 15 ALA CA C 55.43 0.50 1 155 . 15 ALA CB C 18.41 0.50 1 156 . 15 ALA HA H 4.09 0.05 1 157 . 15 ALA HB H 1.38 0.05 1 158 . 15 ALA C C 180.00 0.50 1 159 . 16 ILE H H 7.24 0.05 1 160 . 16 ILE N N 116.73 0.30 1 161 . 16 ILE CA C 64.12 0.50 1 162 . 16 ILE CB C 38.11 0.50 1 163 . 16 ILE HA H 3.80 0.05 1 164 . 16 ILE HB H 1.62 0.05 1 165 . 16 ILE CG1 C 28.40 0.50 1 166 . 16 ILE CG2 C 17.45 0.50 1 167 . 16 ILE CD1 C 13.10 0.50 1 168 . 16 ILE HG12 H 1.08 0.05 2 169 . 16 ILE HG13 H 1.68 0.05 2 170 . 16 ILE HG2 H 0.79 0.05 1 171 . 16 ILE HD1 H 0.84 0.05 1 172 . 16 ILE C C 178.76 0.50 1 173 . 17 LEU H H 8.06 0.05 1 174 . 17 LEU N N 121.79 0.30 1 175 . 17 LEU CA C 59.13 0.50 1 176 . 17 LEU CB C 40.75 0.50 1 177 . 17 LEU HA H 3.83 0.05 1 178 . 17 LEU HB2 H 2.03 0.05 2 179 . 17 LEU HB3 H 1.51 0.05 2 180 . 17 LEU CG C 27.40 0.50 1 181 . 17 LEU HG H 1.49 0.05 1 182 . 17 LEU CD1 C 26.00 0.50 1 183 . 17 LEU CD2 C 23.21 0.50 1 184 . 17 LEU HD1 H 0.95 0.05 1 185 . 17 LEU HD2 H 0.88 0.05 1 186 . 17 LEU C C 178.24 0.50 1 187 . 18 GLN H H 8.35 0.05 1 188 . 18 GLN N N 116.97 0.30 1 189 . 18 GLN CA C 59.21 0.50 1 190 . 18 GLN CB C 28.14 0.50 1 191 . 18 GLN HA H 4.16 0.05 1 192 . 18 GLN HB2 H 2.21 0.05 1 193 . 18 GLN HB3 H 2.07 0.05 1 194 . 18 GLN CG C 34.61 0.50 1 195 . 18 GLN CD C 180.30 0.50 1 196 . 18 GLN HG2 H 2.60 0.05 2 197 . 18 GLN HG3 H 2.43 0.05 2 198 . 18 GLN NE2 N 111.10 0.30 1 199 . 18 GLN HE21 H 7.45 0.05 1 200 . 18 GLN HE22 H 6.81 0.05 1 201 . 18 GLN C C 179.08 0.50 1 202 . 19 ASP H H 7.58 0.05 1 203 . 19 ASP N N 120.35 0.30 1 204 . 19 ASP CA C 57.72 0.50 1 205 . 19 ASP CB C 41.08 0.50 1 206 . 19 ASP HA H 4.52 0.05 1 207 . 19 ASP HB2 H 2.87 0.05 1 208 . 19 ASP HB3 H 2.52 0.05 1 209 . 19 ASP C C 179.79 0.50 1 210 . 20 CYS H H 8.27 0.05 1 211 . 20 CYS N N 119.24 0.30 1 212 . 20 CYS CA C 64.08 0.50 1 213 . 20 CYS CB C 26.85 0.50 1 214 . 20 CYS HA H 3.93 0.05 1 215 . 20 CYS HB2 H 3.23 0.05 2 216 . 20 CYS HB3 H 2.21 0.05 2 217 . 20 CYS C C 176.20 0.50 1 218 . 21 GLN H H 8.65 0.05 1 219 . 21 GLN N N 117.31 0.30 1 220 . 21 GLN CA C 59.18 0.50 1 221 . 21 GLN CB C 28.65 0.50 1 222 . 21 GLN HA H 3.62 0.05 1 223 . 21 GLN HB2 H 2.18 0.05 1 224 . 21 GLN HB3 H 1.90 0.05 1 225 . 21 GLN CG C 34.77 0.50 1 226 . 21 GLN CD C 179.11 0.50 1 227 . 21 GLN HG2 H 2.37 0.05 2 228 . 21 GLN HG3 H 2.09 0.05 2 229 . 21 GLN NE2 N 110.02 0.30 1 230 . 21 GLN HE21 H 7.13 0.05 2 231 . 21 GLN HE22 H 6.75 0.05 2 232 . 21 GLN C C 178.53 0.50 1 233 . 22 ARG H H 7.89 0.05 1 234 . 22 ARG N N 117.47 0.30 1 235 . 22 ARG CA C 59.14 0.50 1 236 . 22 ARG CB C 30.55 0.50 1 237 . 22 ARG HA H 4.03 0.05 1 238 . 22 ARG HB2 H 1.93 0.05 1 239 . 22 ARG HB3 H 1.93 0.05 1 240 . 22 ARG CG C 27.92 0.50 1 241 . 22 ARG HG2 H 1.82 0.05 2 242 . 22 ARG HG3 H 1.67 0.05 2 243 . 22 ARG CD C 43.51 0.50 1 244 . 22 ARG HD2 H 3.28 0.05 1 245 . 22 ARG HD3 H 3.28 0.05 1 246 . 22 ARG NE N 84.38 0.30 1 247 . 22 ARG HE H 7.29 0.05 1 248 . 22 ARG C C 178.67 0.50 1 249 . 23 ALA H H 7.46 0.05 1 250 . 23 ALA N N 119.77 0.30 1 251 . 23 ALA CA C 54.13 0.50 1 252 . 23 ALA CB C 20.65 0.50 1 253 . 23 ALA HA H 4.28 0.05 1 254 . 23 ALA HB H 1.52 0.05 1 255 . 23 ALA C C 178.97 0.50 1 256 . 24 LEU H H 7.44 0.05 1 257 . 24 LEU N N 117.90 0.30 1 258 . 24 LEU CA C 52.56 0.50 1 259 . 24 LEU CB C 40.25 0.50 1 260 . 24 LEU HA H 4.32 0.05 1 261 . 24 LEU HB2 H 1.56 0.05 1 262 . 24 LEU HB3 H 1.19 0.05 1 263 . 24 LEU CG C 25.80 0.50 1 264 . 24 LEU CD1 C 26.58 0.50 1 265 . 24 LEU HG H 1.33 0.05 1 266 . 24 LEU CD2 C 20.87 0.50 1 267 . 24 LEU HD1 H 0.51 0.05 1 268 . 24 LEU HD2 H -0.22 0.05 1 269 . 24 LEU C C 174.67 0.50 1 270 . 25 SER H H 7.09 0.05 1 271 . 25 SER N N 112.79 0.30 1 272 . 25 SER CA C 59.41 0.50 1 273 . 25 SER CB C 63.87 0.50 1 274 . 25 SER HA H 4.35 0.05 1 275 . 25 SER HB2 H 4.14 0.05 1 276 . 25 SER HB3 H 4.14 0.05 1 277 . 25 SER C C 175.78 0.50 1 278 . 26 ALA H H 8.41 0.05 1 279 . 26 ALA N N 125.84 0.30 1 280 . 26 ALA CA C 53.12 0.50 1 281 . 26 ALA CB C 19.34 0.50 1 282 . 26 ALA HA H 4.48 0.05 1 283 . 26 ALA HB H 1.63 0.05 1 284 . 26 ALA C C 177.83 0.50 1 285 . 27 ASP H H 8.44 0.05 1 286 . 27 ASP N N 118.38 0.30 1 287 . 27 ASP CA C 56.15 0.50 1 288 . 27 ASP CB C 40.28 0.50 1 289 . 27 ASP HA H 4.40 0.05 1 290 . 27 ASP HB2 H 2.71 0.05 1 291 . 27 ASP HB3 H 2.71 0.05 1 292 . 27 ASP C C 176.52 0.50 1 293 . 28 ARG H H 7.12 0.05 1 294 . 28 ARG N N 115.67 0.30 1 295 . 28 ARG CA C 56.51 0.50 1 296 . 28 ARG CB C 30.71 0.50 1 297 . 28 ARG HA H 4.15 0.05 1 298 . 28 ARG HB2 H 1.60 0.05 2 299 . 28 ARG HB3 H 1.09 0.05 2 300 . 28 ARG CG C 26.19 0.50 1 301 . 28 ARG CD C 43.32 0.50 1 302 . 28 ARG HG2 H 1.01 0.05 2 303 . 28 ARG HG3 H 0.82 0.05 2 304 . 28 ARG HD2 H 2.94 0.05 2 305 . 28 ARG HD3 H 2.90 0.05 2 306 . 28 ARG NE N 83.65 0.30 1 307 . 28 ARG HE H 6.87 0.05 1 308 . 28 ARG C C 174.23 0.50 1 309 . 29 TYR H H 7.62 0.05 1 310 . 29 TYR N N 117.03 0.30 1 311 . 29 TYR CA C 56.92 0.50 1 312 . 29 TYR CB C 39.69 0.50 1 313 . 29 TYR HA H 5.18 0.05 1 314 . 29 TYR HB2 H 2.98 0.05 1 315 . 29 TYR HB3 H 2.78 0.05 1 316 . 29 TYR CD1 C 133.51 0.50 1 317 . 29 TYR HD1 H 7.12 0.05 1 318 . 29 TYR CD2 C 133.51 0.50 1 319 . 29 TYR HD2 H 7.12 0.05 1 320 . 29 TYR CE1 C 117.53 0.50 1 321 . 29 TYR HE1 H 6.88 0.05 1 322 . 29 TYR CE2 C 117.53 0.50 1 323 . 29 TYR HE2 H 6.88 0.05 1 324 . 29 TYR C C 175.03 0.50 1 325 . 30 GLN H H 8.78 0.05 1 326 . 30 GLN N N 123.54 0.30 1 327 . 30 GLN CA C 54.54 0.50 1 328 . 30 GLN CB C 30.32 0.50 1 329 . 30 GLN HA H 4.68 0.05 1 330 . 30 GLN HB2 H 2.06 0.05 2 331 . 30 GLN HB3 H 1.93 0.05 2 332 . 30 GLN CG C 33.89 0.50 1 333 . 30 GLN CD C 180.27 0.50 1 334 . 30 GLN HG2 H 2.31 0.05 2 335 . 30 GLN HG3 H 2.23 0.05 2 336 . 30 GLN NE2 N 112.12 0.30 1 337 . 30 GLN HE21 H 7.41 0.05 1 338 . 30 GLN HE22 H 6.80 0.05 1 339 . 30 GLN C C 174.84 0.50 1 340 . 31 LEU H H 8.98 0.05 1 341 . 31 LEU N N 127.67 0.30 1 342 . 31 LEU CA C 54.69 0.50 1 343 . 31 LEU CB C 43.59 0.50 1 344 . 31 LEU HA H 5.04 0.05 1 345 . 31 LEU HB2 H 1.65 0.05 1 346 . 31 LEU HB3 H 1.32 0.05 1 347 . 31 LEU CG C 28.21 0.50 1 348 . 31 LEU HG H 1.58 0.05 1 349 . 31 LEU CD1 C 24.80 0.50 1 350 . 31 LEU HD1 H 0.76 0.05 1 351 . 31 LEU CD2 C 24.80 0.50 1 352 . 31 LEU HD2 H 0.76 0.05 1 353 . 31 LEU C C 175.99 0.50 1 354 . 32 GLN H H 8.92 0.05 1 355 . 32 GLN N N 126.09 0.30 1 356 . 32 GLN CA C 54.39 0.50 1 357 . 32 GLN CB C 29.20 0.50 1 358 . 32 GLN HA H 4.47 0.05 1 359 . 32 GLN HB2 H 1.92 0.05 2 360 . 32 GLN HB3 H 1.54 0.05 2 361 . 32 GLN CG C 32.42 0.50 1 362 . 32 GLN CD C 178.79 0.50 1 363 . 32 GLN HG2 H 1.42 0.05 2 364 . 32 GLN HG3 H 0.91 0.05 2 365 . 32 GLN NE2 N 110.99 0.30 1 366 . 32 GLN HE21 H 6.74 0.05 2 367 . 32 GLN HE22 H 6.41 0.05 2 368 . 32 GLN C C 174.06 0.50 1 369 . 33 VAL H H 8.83 0.05 1 370 . 33 VAL N N 128.50 0.30 1 371 . 33 VAL CA C 62.37 0.50 1 372 . 33 VAL CB C 32.84 0.50 1 373 . 33 VAL HA H 4.37 0.05 1 374 . 33 VAL HB H 2.00 0.05 1 375 . 33 VAL CG1 C 21.58 0.50 1 376 . 33 VAL HG1 H 0.86 0.05 1 377 . 33 VAL CG2 C 21.58 0.50 1 378 . 33 VAL HG2 H 0.86 0.05 1 379 . 33 VAL C C 176.16 0.50 1 380 . 34 CYS H H 9.31 0.05 1 381 . 34 CYS N N 126.02 0.30 1 382 . 34 CYS CA C 58.03 0.50 1 383 . 34 CYS CB C 29.99 0.50 1 384 . 34 CYS HA H 4.83 0.05 1 385 . 34 CYS HB2 H 2.80 0.05 1 386 . 34 CYS HB3 H 2.54 0.05 1 387 . 34 CYS C C 178.94 0.50 1 388 . 35 GLU H H 8.73 0.05 1 389 . 35 GLU N N 123.75 0.30 1 390 . 35 GLU CA C 56.81 0.50 1 391 . 35 GLU CB C 30.26 0.50 1 392 . 35 GLU HA H 4.82 0.05 1 393 . 35 GLU HB3 H 2.35 0.05 1 394 . 35 GLU HB2 H 2.07 0.05 1 395 . 35 GLU CG C 36.90 0.50 1 396 . 35 GLU HG2 H 2.33 0.05 2 397 . 35 GLU HG3 H 2.22 0.05 2 398 . 35 GLU C C 173.95 0.50 1 399 . 36 SER H H 7.36 0.05 1 400 . 36 SER N N 109.89 0.30 1 401 . 36 SER CA C 56.46 0.50 1 402 . 36 SER CB C 66.64 0.50 1 403 . 36 SER HA H 5.33 0.05 1 404 . 36 SER HB2 H 4.32 0.05 2 405 . 36 SER HB3 H 4.05 0.05 2 406 . 36 SER C C 174.46 0.50 1 407 . 37 GLY H H 9.58 0.05 1 408 . 37 GLY N N 111.65 0.30 1 409 . 37 GLY CA C 47.40 0.50 1 410 . 37 GLY HA2 H 3.42 0.05 2 411 . 37 GLY HA3 H 2.26 0.05 2 412 . 37 GLY C C 174.99 0.50 1 413 . 38 GLU H H 8.54 0.05 1 414 . 38 GLU N N 120.07 0.30 1 415 . 38 GLU CA C 59.98 0.50 1 416 . 38 GLU CB C 29.15 0.50 1 417 . 38 GLU HA H 3.87 0.05 1 418 . 38 GLU HB2 H 1.99 0.05 1 419 . 38 GLU HB3 H 1.92 0.05 1 420 . 38 GLU CG C 36.74 0.50 1 421 . 38 GLU HG2 H 2.29 0.05 1 422 . 38 GLU HG3 H 2.29 0.05 1 423 . 38 GLU C C 179.27 0.50 1 424 . 39 MET H H 7.85 0.05 1 425 . 39 MET N N 119.27 0.30 1 426 . 39 MET CA C 58.76 0.50 1 427 . 39 MET CB C 32.96 0.50 1 428 . 39 MET HA H 4.24 0.05 1 429 . 39 MET HG2 H 2.83 0.05 2 430 . 39 MET HG3 H 2.55 0.05 2 431 . 39 MET HB2 H 2.17 0.05 1 432 . 39 MET HB3 H 1.93 0.05 1 433 . 39 MET CG C 32.86 0.50 1 434 . 39 MET C C 178.64 0.50 1 435 . 40 LEU H H 7.75 0.05 1 436 . 40 LEU N N 121.00 0.30 1 437 . 40 LEU CA C 57.82 0.50 1 438 . 40 LEU CB C 40.18 0.50 1 439 . 40 LEU HA H 4.47 0.05 1 440 . 40 LEU HB2 H 1.50 0.05 2 441 . 40 LEU HB3 H 0.85 0.05 2 442 . 40 LEU CG C 27.84 0.50 1 443 . 40 LEU CD2 C 26.20 0.50 1 444 . 40 LEU HD2 H 0.70 0.05 1 445 . 40 LEU CD1 C 24.26 0.50 1 446 . 40 LEU HG H 1.32 0.05 1 447 . 40 LEU HD1 H 0.86 0.05 1 448 . 40 LEU C C 177.75 0.50 1 449 . 41 LEU H H 8.10 0.05 1 450 . 41 LEU N N 118.72 0.30 1 451 . 41 LEU CA C 58.16 0.50 1 452 . 41 LEU CB C 41.16 0.50 1 453 . 41 LEU HA H 3.76 0.05 1 454 . 41 LEU HB2 H 1.73 0.05 1 455 . 41 LEU HB3 H 1.41 0.05 1 456 . 41 LEU CG C 27.06 0.50 1 457 . 41 LEU HG H 1.58 0.05 1 458 . 41 LEU CD1 C 24.96 0.50 1 459 . 41 LEU CD2 C 22.47 0.50 1 460 . 41 LEU HD2 H 0.77 0.05 1 461 . 41 LEU HD1 H 0.77 0.05 1 462 . 41 LEU C C 178.44 0.50 1 463 . 42 GLU H H 7.86 0.05 1 464 . 42 GLU N N 118.72 0.30 1 465 . 42 GLU CA C 59.51 0.50 1 466 . 42 GLU CB C 29.76 0.50 1 467 . 42 GLU HA H 4.06 0.05 1 468 . 42 GLU HB2 H 2.08 0.05 1 469 . 42 GLU HB3 H 2.08 0.05 1 470 . 42 GLU CG C 36.11 0.50 1 471 . 42 GLU HG2 H 2.36 0.05 2 472 . 42 GLU HG3 H 2.24 0.05 2 473 . 42 GLU C C 179.08 0.50 1 474 . 43 TYR H H 8.55 0.05 1 475 . 43 TYR N N 120.99 0.30 1 476 . 43 TYR CA C 62.49 0.50 1 477 . 43 TYR CB C 38.93 0.50 1 478 . 43 TYR HA H 4.03 0.05 1 479 . 43 TYR HB2 H 3.13 0.05 1 480 . 43 TYR HB3 H 2.95 0.05 1 481 . 43 TYR CD1 C 133.10 0.50 1 482 . 43 TYR HD1 H 6.81 0.05 1 483 . 43 TYR CD2 C 133.10 0.50 1 484 . 43 TYR HD2 H 6.81 0.05 1 485 . 43 TYR CE1 C 117.06 0.50 1 486 . 43 TYR HE1 H 6.21 0.05 1 487 . 43 TYR CE2 C 117.06 0.50 1 488 . 43 TYR HE2 H 6.21 0.05 1 489 . 43 TYR C C 178.53 0.50 1 490 . 44 ALA H H 9.40 0.05 1 491 . 44 ALA N N 121.42 0.30 1 492 . 44 ALA CA C 55.32 0.50 1 493 . 44 ALA CB C 17.91 0.50 1 494 . 44 ALA HA H 3.77 0.05 1 495 . 44 ALA HB H 1.36 0.05 1 496 . 44 ALA C C 178.36 0.50 1 497 . 45 GLN H H 7.92 0.05 1 498 . 45 GLN N N 112.02 0.30 1 499 . 45 GLN CA C 58.76 0.50 1 500 . 45 GLN CB C 29.30 0.50 1 501 . 45 GLN HA H 3.97 0.05 1 502 . 45 GLN HB2 H 2.29 0.05 1 503 . 45 GLN HB3 H 2.13 0.05 1 504 . 45 GLN CG C 34.71 0.50 1 505 . 45 GLN CD C 179.66 0.50 1 506 . 45 GLN HG2 H 2.53 0.05 2 507 . 45 GLN HG3 H 2.37 0.05 2 508 . 45 GLN NE2 N 110.02 0.30 1 509 . 45 GLN HE21 H 7.32 0.05 1 510 . 45 GLN HE22 H 6.75 0.05 1 511 . 45 GLN C C 178.37 0.50 1 512 . 46 THR H H 7.38 0.05 1 513 . 46 THR N N 106.32 0.30 1 514 . 46 THR CA C 62.29 0.50 1 515 . 46 THR CB C 70.45 0.50 1 516 . 46 THR HA H 4.29 0.05 1 517 . 46 THR HB H 4.13 0.05 1 518 . 46 THR CG2 C 21.98 0.50 1 519 . 46 THR HG2 H 1.18 0.05 1 520 . 46 THR C C 175.14 0.50 1 521 . 47 HIS H H 7.75 0.05 1 522 . 47 HIS N N 119.94 0.30 1 523 . 47 HIS CA C 55.21 0.50 1 524 . 47 HIS CB C 27.04 0.50 1 525 . 47 HIS HA H 4.73 0.05 1 526 . 47 HIS HB2 H 3.01 0.05 2 527 . 47 HIS HB3 H 1.90 0.05 2 528 . 47 HIS C C 175.26 0.50 1 529 . 48 ARG H H 7.60 0.05 1 530 . 48 ARG N N 120.90 0.30 1 531 . 48 ARG CA C 59.68 0.50 1 532 . 48 ARG CB C 29.83 0.50 1 533 . 48 ARG HA H 3.96 0.05 1 534 . 48 ARG HB2 H 2.00 0.05 1 535 . 48 ARG HB3 H 1.92 0.05 1 536 . 48 ARG CG C 26.55 0.50 1 537 . 48 ARG HG2 H 1.67 0.05 1 538 . 48 ARG HG3 H 1.67 0.05 1 539 . 48 ARG CD C 43.54 0.50 1 540 . 48 ARG HD2 H 3.25 0.05 1 541 . 48 ARG HD3 H 3.25 0.05 1 542 . 48 ARG NE N 84.82 0.30 1 543 . 48 ARG HE H 7.16 0.05 1 544 . 48 ARG C C 176.71 0.50 1 545 . 49 ASP H H 8.55 0.05 1 546 . 49 ASP N N 116.08 0.30 1 547 . 49 ASP CA C 54.70 0.50 1 548 . 49 ASP CB C 40.18 0.50 1 549 . 49 ASP HA H 4.68 0.05 1 550 . 49 ASP HB2 H 2.79 0.05 1 551 . 49 ASP HB3 H 2.79 0.05 1 552 . 49 ASP C C 176.39 0.50 1 553 . 50 GLN H H 7.82 0.05 1 554 . 50 GLN N N 117.36 0.30 1 555 . 50 GLN CA C 55.13 0.50 1 556 . 50 GLN CB C 30.48 0.50 1 557 . 50 GLN HA H 4.61 0.05 1 558 . 50 GLN HB3 H 2.53 0.05 1 559 . 50 GLN HB2 H 1.78 0.05 1 560 . 50 GLN CG C 34.31 0.50 1 561 . 50 GLN CD C 180.77 0.50 1 562 . 50 GLN HG2 H 2.36 0.05 2 563 . 50 GLN HG3 H 2.25 0.05 2 564 . 50 GLN NE2 N 112.18 0.30 1 565 . 50 GLN HE22 H 6.84 0.05 1 566 . 50 GLN HE21 H 7.61 0.05 1 567 . 50 GLN C C 174.83 0.50 1 568 . 51 ILE H H 7.45 0.05 1 569 . 51 ILE N N 119.25 0.30 1 570 . 51 ILE CA C 61.81 0.50 1 571 . 51 ILE CB C 40.98 0.50 1 572 . 51 ILE HA H 3.97 0.05 1 573 . 51 ILE HB H 1.74 0.05 1 574 . 51 ILE CG1 C 26.58 0.50 1 575 . 51 ILE CG2 C 18.79 0.50 1 576 . 51 ILE CD1 C 13.76 0.50 1 577 . 51 ILE HG12 H 1.93 0.05 2 578 . 51 ILE HG13 H 1.02 0.05 2 579 . 51 ILE HG2 H 0.81 0.05 1 580 . 51 ILE HD1 H 0.84 0.05 1 581 . 51 ILE C C 174.23 0.50 1 582 . 52 ASP H H 9.00 0.05 1 583 . 52 ASP N N 125.68 0.30 1 584 . 52 ASP CA C 56.39 0.50 1 585 . 52 ASP CB C 41.98 0.50 1 586 . 52 ASP HA H 4.80 0.05 1 587 . 52 ASP HB2 H 2.88 0.05 1 588 . 52 ASP HB3 H 2.50 0.05 1 589 . 52 ASP C C 175.78 0.50 1 590 . 53 CYS H H 7.49 0.05 1 591 . 53 CYS N N 114.44 0.30 1 592 . 53 CYS CA C 57.90 0.50 1 593 . 53 CYS CB C 29.33 0.50 1 594 . 53 CYS HA H 4.67 0.05 1 595 . 53 CYS HB2 H 2.49 0.05 1 596 . 53 CYS HB3 H 2.49 0.05 1 597 . 53 CYS C C 171.61 0.50 1 598 . 54 LEU H H 9.38 0.05 1 599 . 54 LEU N N 130.97 0.30 1 600 . 54 LEU CA C 53.34 0.50 1 601 . 54 LEU CB C 46.17 0.50 1 602 . 54 LEU HA H 5.49 0.05 1 603 . 54 LEU HB2 H 1.66 0.05 1 604 . 54 LEU HB3 H 1.66 0.05 1 605 . 54 LEU CG C 27.45 0.50 1 606 . 54 LEU HG H 1.64 0.05 1 607 . 54 LEU CD1 C 25.83 0.50 1 608 . 54 LEU HD1 H 0.96 0.05 1 609 . 54 LEU CD2 C 25.83 0.50 1 610 . 54 LEU HD2 H 0.96 0.05 1 611 . 54 LEU C C 175.89 0.50 1 612 . 55 ILE H H 9.06 0.05 1 613 . 55 ILE N N 122.95 0.30 1 614 . 55 ILE CA C 60.75 0.50 1 615 . 55 ILE CB C 39.16 0.50 1 616 . 55 ILE HA H 5.03 0.05 1 617 . 55 ILE HB H 1.60 0.05 1 618 . 55 ILE CG1 C 27.42 0.50 1 619 . 55 ILE HG12 H 1.61 0.05 1 620 . 55 ILE HG13 H 1.61 0.05 1 621 . 55 ILE CG2 C 16.20 0.50 1 622 . 55 ILE CD1 C 14.33 0.50 1 623 . 55 ILE HG2 H 0.67 0.05 1 624 . 55 ILE HD1 H 0.66 0.05 1 625 . 55 ILE C C 174.25 0.50 1 626 . 56 LEU H H 9.00 0.05 1 627 . 56 LEU N N 125.23 0.30 1 628 . 56 LEU CA C 53.14 0.50 1 629 . 56 LEU CB C 46.10 0.50 1 630 . 56 LEU HA H 5.03 0.05 1 631 . 56 LEU HB2 H 2.05 0.05 2 632 . 56 LEU HB3 H 1.75 0.05 2 633 . 56 LEU CD1 C 26.03 0.50 1 634 . 56 LEU CG C 26.70 0.50 1 635 . 56 LEU HG H 1.74 0.05 1 636 . 56 LEU CD2 C 24.82 0.50 1 637 . 56 LEU HD2 H 1.13 0.05 1 638 . 56 LEU HD1 H 0.75 0.05 1 639 . 56 LEU C C 174.87 0.50 1 640 . 57 VAL H H 6.60 0.05 1 641 . 57 VAL N N 122.62 0.30 1 642 . 57 VAL CA C 62.65 0.50 1 643 . 57 VAL CB C 31.92 0.50 1 644 . 57 VAL HA H 4.25 0.05 1 645 . 57 VAL HB H 1.90 0.05 1 646 . 57 VAL CG1 C 21.53 0.50 1 647 . 57 VAL HG1 H 0.83 0.05 1 648 . 57 VAL CG2 C 21.53 0.50 1 649 . 57 VAL HG2 H 0.83 0.05 1 650 . 57 VAL C C 174.52 0.50 1 651 . 58 ALA H H 7.83 0.05 1 652 . 58 ALA N N 130.21 0.30 1 653 . 58 ALA CA C 53.68 0.50 1 654 . 58 ALA CB C 17.54 0.50 1 655 . 58 ALA HA H 2.37 0.05 1 656 . 58 ALA HB H 0.62 0.05 1 657 . 58 ALA C C 176.23 0.50 1 658 . 59 ALA H H 7.44 0.05 1 659 . 59 ALA N N 115.85 0.30 1 660 . 59 ALA CA C 51.91 0.50 1 661 . 59 ALA CB C 18.54 0.50 1 662 . 59 ALA HA H 4.10 0.05 1 663 . 59 ALA HB H 1.25 0.05 1 664 . 59 ALA C C 177.33 0.50 1 665 . 60 ASN H H 7.38 0.05 1 666 . 60 ASN N N 119.86 0.30 1 667 . 60 ASN CA C 51.46 0.50 1 668 . 60 ASN CB C 37.09 0.50 1 669 . 60 ASN HA H 4.39 0.05 1 670 . 60 ASN HB3 H 2.13 0.05 1 671 . 60 ASN HB2 H 1.66 0.05 1 672 . 61 PRO CA C 64.26 0.50 1 673 . 61 PRO CB C 31.94 0.50 1 674 . 61 PRO HA H 4.47 0.05 1 675 . 61 PRO HB2 H 2.46 0.05 1 676 . 61 PRO HB3 H 2.17 0.05 1 677 . 61 PRO CG C 28.07 0.50 1 678 . 61 PRO HG3 H 2.40 0.05 1 679 . 61 PRO HG2 H 2.17 0.05 1 680 . 61 PRO CD C 50.83 0.50 1 681 . 61 PRO HD3 H 3.84 0.05 1 682 . 61 PRO HD2 H 3.69 0.05 1 683 . 61 PRO C C 177.55 0.50 1 684 . 62 SER H H 9.05 0.05 1 685 . 62 SER N N 113.30 0.30 1 686 . 62 SER CA C 58.96 0.50 1 687 . 62 SER CB C 62.40 0.50 1 688 . 62 SER HA H 4.44 0.05 1 689 . 62 SER HB2 H 4.27 0.05 1 690 . 62 SER HB3 H 4.27 0.05 1 691 . 62 SER C C 174.16 0.50 1 692 . 63 PHE H H 7.76 0.05 1 693 . 63 PHE N N 118.72 0.30 1 694 . 63 PHE CA C 63.36 0.50 1 695 . 63 PHE CB C 40.64 0.50 1 696 . 63 PHE HA H 4.22 0.05 1 697 . 63 PHE HB2 H 3.47 0.05 1 698 . 63 PHE HB3 H 3.05 0.05 1 699 . 63 PHE CD1 C 132.94 0.50 1 700 . 63 PHE HD1 H 7.03 0.05 1 701 . 63 PHE CD2 C 132.94 0.50 1 702 . 63 PHE HD2 H 7.03 0.05 1 703 . 63 PHE CE1 C 130.50 0.50 1 704 . 63 PHE HE1 H 7.04 0.05 1 705 . 63 PHE CE2 C 130.50 0.50 1 706 . 63 PHE HE2 H 7.04 0.05 1 707 . 63 PHE HZ H 6.91 0.05 1 708 . 63 PHE CZ C 128.04 0.50 1 709 . 63 PHE C C 176.29 0.50 1 710 . 64 ARG H H 8.85 0.05 1 711 . 64 ARG N N 115.89 0.30 1 712 . 64 ARG CA C 59.71 0.50 1 713 . 64 ARG CB C 29.57 0.50 1 714 . 64 ARG HA H 3.84 0.05 1 715 . 64 ARG HB2 H 1.95 0.05 1 716 . 64 ARG HB3 H 1.95 0.05 1 717 . 64 ARG CG C 28.28 0.50 1 718 . 64 ARG HG2 H 1.77 0.05 2 719 . 64 ARG HG3 H 1.94 0.05 2 720 . 64 ARG CD C 43.33 0.50 1 721 . 64 ARG HD2 H 3.32 0.05 1 722 . 64 ARG HD3 H 3.32 0.05 1 723 . 64 ARG NE N 84.68 0.30 1 724 . 64 ARG HE H 7.50 0.05 1 725 . 64 ARG C C 178.33 0.50 1 726 . 65 ALA H H 7.94 0.05 1 727 . 65 ALA N N 121.55 0.30 1 728 . 65 ALA CA C 54.98 0.50 1 729 . 65 ALA CB C 18.32 0.50 1 730 . 65 ALA HA H 4.17 0.05 1 731 . 65 ALA HB H 1.51 0.05 1 732 . 65 ALA C C 181.10 0.50 1 733 . 66 VAL H H 8.25 0.05 1 734 . 66 VAL N N 120.68 0.30 1 735 . 66 VAL CA C 66.57 0.50 1 736 . 66 VAL CB C 31.47 0.50 1 737 . 66 VAL HA H 3.54 0.05 1 738 . 66 VAL HB H 2.03 0.05 1 739 . 66 VAL CG2 C 23.02 0.50 1 740 . 66 VAL CG1 C 21.08 0.50 1 741 . 66 VAL HG2 H 0.80 0.05 1 742 . 66 VAL HG1 H 0.21 0.05 1 743 . 66 VAL C C 177.85 0.50 1 744 . 67 VAL H H 8.26 0.05 1 745 . 67 VAL N N 118.05 0.30 1 746 . 67 VAL CA C 66.81 0.50 1 747 . 67 VAL CB C 31.25 0.50 1 748 . 67 VAL HA H 3.37 0.05 1 749 . 67 VAL HB H 1.80 0.05 1 750 . 67 VAL CG2 C 22.10 0.50 1 751 . 67 VAL CG1 C 22.02 0.50 1 752 . 67 VAL HG1 H 0.71 0.05 1 753 . 67 VAL HG2 H 0.39 0.05 1 754 . 67 VAL C C 178.50 0.50 1 755 . 68 GLN H H 8.26 0.05 1 756 . 68 GLN N N 119.80 0.30 1 757 . 68 GLN CA C 60.00 0.50 1 758 . 68 GLN CB C 28.39 0.50 1 759 . 68 GLN HA H 3.92 0.05 1 760 . 68 GLN HB2 H 2.21 0.05 2 761 . 68 GLN HB3 H 2.09 0.05 2 762 . 68 GLN CG C 34.60 0.50 1 763 . 68 GLN CD C 180.34 0.50 1 764 . 68 GLN HG2 H 2.49 0.05 2 765 . 68 GLN HG3 H 2.18 0.05 2 766 . 68 GLN NE2 N 111.63 0.30 1 767 . 68 GLN HE21 H 7.68 0.05 1 768 . 68 GLN HE22 H 6.81 0.05 1 769 . 68 GLN C C 178.42 0.50 1 770 . 69 GLN H H 7.71 0.05 1 771 . 69 GLN N N 120.03 0.30 1 772 . 69 GLN CA C 59.22 0.50 1 773 . 69 GLN CB C 28.15 0.50 1 774 . 69 GLN HA H 4.10 0.05 1 775 . 69 GLN HB2 H 2.14 0.05 1 776 . 69 GLN HB3 H 2.14 0.05 1 777 . 69 GLN CG C 34.10 0.50 1 778 . 69 GLN CD C 179.44 0.50 1 779 . 69 GLN HG2 H 2.50 0.05 1 780 . 69 GLN HG3 H 2.50 0.05 1 781 . 69 GLN NE2 N 112.37 0.30 1 782 . 69 GLN HE21 H 7.79 0.05 1 783 . 69 GLN HE22 H 6.79 0.05 1 784 . 69 GLN C C 178.38 0.50 1 785 . 70 LEU H H 8.43 0.05 1 786 . 70 LEU N N 120.28 0.30 1 787 . 70 LEU CA C 58.90 0.50 1 788 . 70 LEU CB C 41.19 0.50 1 789 . 70 LEU HA H 3.85 0.05 1 790 . 70 LEU HB2 H 2.09 0.05 1 791 . 70 LEU HB3 H 1.82 0.05 1 792 . 70 LEU CG C 25.83 0.50 1 793 . 70 LEU CD1 C 25.19 0.50 1 794 . 70 LEU HG H 1.76 0.05 1 795 . 70 LEU CD2 C 22.82 0.50 1 796 . 70 LEU HD2 H 0.63 0.05 1 797 . 70 LEU HD1 H 0.49 0.05 1 798 . 70 LEU C C 179.20 0.50 1 799 . 71 CYS H H 8.01 0.05 1 800 . 71 CYS N N 115.60 0.30 1 801 . 71 CYS CA C 64.57 0.50 1 802 . 71 CYS CB C 26.84 0.50 1 803 . 71 CYS HA H 4.08 0.05 1 804 . 71 CYS HB2 H 3.31 0.05 1 805 . 71 CYS HB3 H 2.93 0.05 1 806 . 71 CYS C C 174.45 0.50 1 807 . 72 PHE H H 8.72 0.05 1 808 . 72 PHE N N 123.53 0.30 1 809 . 72 PHE CA C 60.45 0.50 1 810 . 72 PHE CB C 38.77 0.50 1 811 . 72 PHE HA H 4.39 0.05 1 812 . 72 PHE HB2 H 3.38 0.05 2 813 . 72 PHE HB3 H 3.32 0.05 2 814 . 72 PHE CD1 C 131.45 0.50 1 815 . 72 PHE HD1 H 7.29 0.05 1 816 . 72 PHE CD2 C 131.45 0.50 1 817 . 72 PHE HD2 H 7.29 0.05 1 818 . 72 PHE C C 178.17 0.50 1 819 . 73 GLU H H 8.25 0.05 1 820 . 73 GLU N N 116.16 0.30 1 821 . 73 GLU CA C 56.22 0.50 1 822 . 73 GLU CB C 29.58 0.50 1 823 . 73 GLU HA H 4.32 0.05 1 824 . 73 GLU HB2 H 2.36 0.05 2 825 . 73 GLU HB3 H 2.02 0.05 2 826 . 73 GLU CG C 35.75 0.50 1 827 . 73 GLU HG2 H 2.61 0.05 2 828 . 73 GLU HG3 H 2.46 0.05 2 829 . 73 GLU C C 176.68 0.50 1 830 . 74 GLY H H 7.96 0.05 1 831 . 74 GLY N N 107.99 0.30 1 832 . 74 GLY CA C 46.03 0.50 1 833 . 74 GLY HA2 H 4.16 0.05 2 834 . 74 GLY HA3 H 3.77 0.05 2 835 . 74 GLY C C 174.81 0.50 1 836 . 75 VAL H H 8.57 0.05 1 837 . 75 VAL N N 123.00 0.30 1 838 . 75 VAL CA C 62.19 0.50 1 839 . 75 VAL CB C 30.06 0.50 1 840 . 75 VAL HA H 4.08 0.05 1 841 . 75 VAL HB H 2.24 0.05 1 842 . 75 VAL CG1 C 20.90 0.50 1 843 . 75 VAL CG2 C 19.73 0.50 1 844 . 75 VAL HG1 H 0.87 0.05 1 845 . 75 VAL HG2 H 0.79 0.05 1 846 . 75 VAL C C 174.25 0.50 1 847 . 76 VAL H H 8.34 0.05 1 848 . 76 VAL N N 131.53 0.30 1 849 . 76 VAL CA C 63.17 0.50 1 850 . 76 VAL CB C 33.12 0.50 1 851 . 76 VAL HA H 4.16 0.05 1 852 . 76 VAL HB H 2.09 0.05 1 853 . 76 VAL CG1 C 21.85 0.50 1 854 . 76 VAL CG2 C 20.63 0.50 1 855 . 76 VAL HG2 H 0.88 0.05 1 856 . 76 VAL HG1 H 0.58 0.05 1 857 . 76 VAL C C 173.35 0.50 1 858 . 77 VAL H H 7.45 0.05 1 859 . 77 VAL N N 118.69 0.30 1 860 . 77 VAL CA C 57.65 0.50 1 861 . 77 VAL CB C 33.32 0.50 1 862 . 77 VAL HA H 4.39 0.05 1 863 . 77 VAL HB H 2.11 0.05 1 864 . 77 VAL CG1 C 21.65 0.50 1 865 . 77 VAL CG2 C 18.97 0.50 1 866 . 77 VAL HG1 H 0.93 0.05 1 867 . 77 VAL HG2 H 0.93 0.05 1 868 . 78 PRO CA C 64.15 0.50 1 869 . 78 PRO CB C 31.48 0.50 1 870 . 78 PRO HA H 4.36 0.05 1 871 . 78 PRO HB2 H 2.06 0.05 1 872 . 78 PRO HB3 H 2.06 0.05 1 873 . 78 PRO CG C 27.83 0.50 1 874 . 78 PRO HG3 H 2.24 0.05 1 875 . 78 PRO HG2 H 1.36 0.05 1 876 . 78 PRO CD C 50.01 0.50 1 877 . 78 PRO HD3 H 3.28 0.05 1 878 . 78 PRO HD2 H 2.36 0.05 1 879 . 78 PRO C C 174.05 0.50 1 880 . 79 ALA H H 8.46 0.05 1 881 . 79 ALA N N 121.07 0.30 1 882 . 79 ALA CA C 51.21 0.50 1 883 . 79 ALA CB C 24.19 0.50 1 884 . 79 ALA HA H 5.92 0.05 1 885 . 79 ALA HB H 1.54 0.05 1 886 . 79 ALA C C 175.02 0.50 1 887 . 80 ILE H H 8.52 0.05 1 888 . 80 ILE N N 119.46 0.30 1 889 . 80 ILE CA C 59.30 0.50 1 890 . 80 ILE CB C 41.78 0.50 1 891 . 80 ILE HA H 4.72 0.05 1 892 . 80 ILE HB H 1.50 0.05 1 893 . 80 ILE CG1 C 28.27 0.50 1 894 . 80 ILE CG2 C 17.79 0.50 1 895 . 80 ILE CD1 C 15.13 0.50 1 896 . 80 ILE HG12 H 1.46 0.05 2 897 . 80 ILE HG13 H 0.84 0.05 2 898 . 80 ILE HD1 H 0.62 0.05 1 899 . 80 ILE HG2 H 0.62 0.05 1 900 . 80 ILE C C 174.57 0.50 1 901 . 81 VAL H H 9.27 0.05 1 902 . 81 VAL N N 127.13 0.30 1 903 . 81 VAL CA C 60.98 0.50 1 904 . 81 VAL CB C 32.96 0.50 1 905 . 81 VAL HA H 4.79 0.05 1 906 . 81 VAL HB H 1.74 0.05 1 907 . 81 VAL CG1 C 22.19 0.50 1 908 . 81 VAL CG2 C 20.43 0.50 1 909 . 81 VAL HG2 H 1.01 0.05 1 910 . 81 VAL HG1 H 0.76 0.05 1 911 . 81 VAL C C 175.90 0.50 1 912 . 82 VAL H H 9.10 0.05 1 913 . 82 VAL N N 129.51 0.30 1 914 . 82 VAL CA C 60.93 0.50 1 915 . 82 VAL CB C 33.10 0.50 1 916 . 82 VAL HA H 4.98 0.05 1 917 . 82 VAL HB H 1.87 0.05 1 918 . 82 VAL CG2 C 21.30 0.50 1 919 . 82 VAL HG2 H 0.70 0.05 1 920 . 82 VAL CG1 C 21.53 0.50 1 921 . 82 VAL HG1 H 0.78 0.05 1 922 . 82 VAL C C 176.80 0.50 1 923 . 83 GLY H H 8.87 0.05 1 924 . 83 GLY N N 116.37 0.30 1 925 . 83 GLY CA C 44.89 0.50 1 926 . 83 GLY HA2 H 4.12 0.05 2 927 . 83 GLY HA3 H 3.97 0.05 2 928 . 83 GLY C C 171.81 0.50 1 929 . 84 ASP H H 8.36 0.05 1 930 . 84 ASP N N 119.05 0.30 1 931 . 84 ASP CA C 53.74 0.50 1 932 . 84 ASP CB C 42.43 0.50 1 933 . 84 ASP HA H 4.70 0.05 1 934 . 84 ASP HB2 H 2.65 0.05 2 935 . 84 ASP HB3 H 2.52 0.05 2 936 . 84 ASP C C 176.29 0.50 1 937 . 85 ARG H H 8.47 0.05 1 938 . 85 ARG N N 119.86 0.30 1 939 . 85 ARG CA C 55.88 0.50 1 940 . 85 ARG CB C 31.09 0.50 1 941 . 85 ARG HA H 4.24 0.05 1 942 . 85 ARG HB2 H 1.79 0.05 2 943 . 85 ARG HB3 H 1.68 0.05 2 944 . 85 ARG CG C 26.95 0.50 1 945 . 85 ARG HG2 H 1.54 0.05 1 946 . 85 ARG HG3 H 1.54 0.05 1 947 . 85 ARG CD C 43.31 0.50 1 948 . 85 ARG HD2 H 3.11 0.05 1 949 . 85 ARG HD3 H 3.11 0.05 1 950 . 85 ARG NE N 84.66 0.30 1 951 . 85 ARG HE H 7.37 0.05 1 952 . 85 ARG C C 175.85 0.50 1 953 . 86 ASP H H 8.49 0.05 1 954 . 86 ASP N N 121.32 0.30 1 955 . 86 ASP CA C 54.72 0.50 1 956 . 86 ASP CB C 41.44 0.50 1 957 . 86 ASP HA H 4.53 0.05 1 958 . 86 ASP HB2 H 2.65 0.05 2 959 . 86 ASP HB3 H 2.74 0.05 2 960 . 86 ASP C C 176.47 0.50 1 961 . 87 SER H H 8.23 0.05 1 962 . 87 SER N N 115.58 0.30 1 963 . 87 SER CA C 58.66 0.50 1 964 . 87 SER CB C 63.94 0.50 1 965 . 87 SER HA H 4.37 0.05 1 966 . 87 SER HB2 H 3.93 0.05 2 967 . 87 SER HB3 H 3.81 0.05 2 968 . 87 SER C C 174.66 0.50 1 969 . 88 GLU H H 8.48 0.05 1 970 . 88 GLU N N 122.07 0.30 1 971 . 88 GLU CA C 56.49 0.50 1 972 . 88 GLU CB C 30.16 0.50 1 973 . 88 GLU HA H 4.31 0.05 1 974 . 88 GLU HB3 H 2.12 0.05 1 975 . 88 GLU HB2 H 1.92 0.05 1 976 . 88 GLU CG C 36.48 0.50 1 977 . 88 GLU HG2 H 2.26 0.05 1 978 . 88 GLU HG3 H 2.26 0.05 1 979 . 88 GLU C C 175.97 0.50 1 980 . 89 ASP H H 8.21 0.05 1 981 . 89 ASP N N 122.04 0.30 1 982 . 89 ASP CA C 51.95 0.50 1 983 . 89 ASP CB C 41.85 0.50 1 984 . 89 ASP HA H 4.90 0.05 1 985 . 89 ASP HB2 H 2.79 0.05 2 986 . 89 ASP HB3 H 2.58 0.05 2 987 . 90 PRO CA C 64.13 0.50 1 988 . 90 PRO CB C 32.26 0.50 1 989 . 90 PRO HA H 4.39 0.05 1 990 . 90 PRO HB3 H 2.29 0.05 1 991 . 90 PRO HB2 H 1.99 0.05 1 992 . 90 PRO CG C 27.01 0.50 1 993 . 90 PRO HG2 H 2.01 0.05 1 994 . 90 PRO HG3 H 2.01 0.05 1 995 . 90 PRO CD C 50.98 0.50 1 996 . 90 PRO HD2 H 3.86 0.05 1 997 . 90 PRO HD3 H 3.86 0.05 1 998 . 90 PRO C C 177.02 0.50 1 999 . 91 ASP H H 8.39 0.05 1 1000 . 91 ASP N N 118.14 0.30 1 1001 . 91 ASP CA C 54.68 0.50 1 1002 . 91 ASP CB C 41.24 0.50 1 1003 . 91 ASP HA H 4.64 0.05 1 1004 . 91 ASP HB3 H 2.72 0.05 1 1005 . 91 ASP HB2 H 2.66 0.05 1 1006 . 91 ASP C C 176.03 0.50 1 1007 . 92 GLU H H 7.71 0.05 1 1008 . 92 GLU N N 121.60 0.30 1 1009 . 92 GLU CA C 54.57 0.50 1 1010 . 92 GLU CB C 30.19 0.50 1 1011 . 92 GLU HA H 4.57 0.05 1 1012 . 92 GLU HB3 H 2.05 0.05 1 1013 . 92 GLU HB2 H 1.97 0.05 1 1014 . 92 GLU CG C 36.11 0.50 1 1015 . 92 GLU HG2 H 2.27 0.05 1 1016 . 92 GLU HG3 H 2.27 0.05 1 1017 . 93 PRO CA C 63.20 0.50 1 1018 . 93 PRO CB C 32.04 0.50 1 1019 . 93 PRO HA H 4.37 0.05 1 1020 . 93 PRO HB3 H 2.25 0.05 1 1021 . 93 PRO HB2 H 1.91 0.05 1 1022 . 93 PRO CG C 27.45 0.50 1 1023 . 93 PRO HG2 H 2.02 0.05 1 1024 . 93 PRO HG3 H 2.02 0.05 1 1025 . 93 PRO CD C 50.61 0.50 1 1026 . 93 PRO HD2 H 3.73 0.05 1 1027 . 93 PRO HD3 H 3.73 0.05 1 1028 . 93 PRO C C 176.79 0.50 1 1029 . 94 ALA H H 8.38 0.05 1 1030 . 94 ALA N N 123.99 0.30 1 1031 . 94 ALA CA C 52.44 0.50 1 1032 . 94 ALA CB C 18.87 0.50 1 1033 . 94 ALA HA H 4.26 0.05 1 1034 . 94 ALA HB H 1.31 0.05 1 1035 . 94 ALA C C 173.73 0.50 1 1036 . 95 LYS H H 8.28 0.05 1 1037 . 95 LYS N N 120.88 0.30 1 1038 . 95 LYS CA C 56.26 0.50 1 1039 . 95 LYS CB C 33.40 0.50 1 1040 . 95 LYS HA H 4.32 0.05 1 1041 . 95 LYS HB2 H 1.87 0.05 2 1042 . 95 LYS HB3 H 1.73 0.05 2 1043 . 95 LYS CG C 24.90 0.50 1 1044 . 95 LYS CD C 29.17 0.50 1 1045 . 95 LYS HD2 H 1.69 0.05 1 1046 . 95 LYS HD3 H 1.69 0.05 1 1047 . 95 LYS HG2 H 1.45 0.05 1 1048 . 95 LYS HG3 H 1.45 0.05 1 1049 . 95 LYS CE C 42.33 0.50 1 1050 . 95 LYS HE2 H 3.03 0.05 1 1051 . 95 LYS HE3 H 3.03 0.05 1 1052 . 95 LYS C C 176.29 0.50 1 1053 . 96 GLU H H 8.26 0.05 1 1054 . 96 GLU N N 121.24 0.30 1 1055 . 96 GLU CA C 56.54 0.50 1 1056 . 96 GLU CB C 30.87 0.50 1 1057 . 96 GLU HA H 4.26 0.05 1 1058 . 96 GLU HB2 H 1.94 0.05 1 1059 . 96 GLU HB3 H 1.94 0.05 1 1060 . 96 GLU CG C 36.34 0.50 1 1061 . 96 GLU HG2 H 2.23 0.05 1 1062 . 96 GLU HG3 H 2.23 0.05 1 1063 . 96 GLU C C 175.81 0.50 1 1064 . 97 GLN H H 8.11 0.05 1 1065 . 97 GLN N N 120.19 0.30 1 1066 . 97 GLN CA C 55.51 0.50 1 1067 . 97 GLN CB C 29.67 0.50 1 1068 . 97 GLN HA H 4.71 0.05 1 1069 . 97 GLN HB2 H 2.01 0.05 2 1070 . 97 GLN HB3 H 1.76 0.05 2 1071 . 97 GLN CG C 34.83 0.50 1 1072 . 97 GLN HG2 H 2.29 0.05 1 1073 . 97 GLN HG3 H 2.29 0.05 1 1074 . 97 GLN C C 175.40 0.50 1 1075 . 98 LEU H H 10.46 0.05 1 1076 . 98 LEU N N 124.85 0.30 1 1077 . 98 LEU CA C 56.06 0.50 1 1078 . 98 LEU CB C 44.57 0.50 1 1079 . 98 LEU HA H 4.47 0.05 1 1080 . 98 LEU HB2 H 1.87 0.05 1 1081 . 98 LEU HB3 H 1.77 0.05 1 1082 . 98 LEU CG C 27.89 0.50 1 1083 . 98 LEU HG H 1.80 0.05 1 1084 . 98 LEU CD1 C 25.91 0.50 1 1085 . 98 LEU CD2 C 23.52 0.50 1 1086 . 98 LEU HD1 H 0.89 0.05 1 1087 . 98 LEU HD2 H 0.89 0.05 1 1088 . 98 LEU C C 175.80 0.50 1 1089 . 99 TYR H H 11.07 0.05 1 1090 . 99 TYR N N 122.89 0.30 1 1091 . 99 TYR CA C 56.29 0.50 1 1092 . 99 TYR CB C 39.23 0.50 1 1093 . 99 TYR HA H 4.97 0.05 1 1094 . 99 TYR HB3 H 3.37 0.05 1 1095 . 99 TYR HB2 H 2.62 0.05 1 1096 . 99 TYR CD1 C 131.81 0.50 1 1097 . 99 TYR HD1 H 6.78 0.05 1 1098 . 99 TYR CD2 C 131.81 0.50 1 1099 . 99 TYR HD2 H 6.78 0.05 1 1100 . 99 TYR CE1 C 117.92 0.50 1 1101 . 99 TYR HE1 H 7.02 0.05 1 1102 . 99 TYR CE2 C 117.92 0.50 1 1103 . 99 TYR HE2 H 7.02 0.05 1 1104 . 99 TYR C C 175.07 0.50 1 1105 . 100 HIS H H 8.67 0.05 1 1106 . 100 HIS N N 112.63 0.30 1 1107 . 100 HIS CA C 56.15 0.50 1 1108 . 100 HIS CB C 32.91 0.50 1 1109 . 100 HIS HA H 5.09 0.05 1 1110 . 100 HIS HB3 H 2.73 0.05 1 1111 . 100 HIS HB2 H 2.78 0.05 1 1112 . 100 HIS NE2 N 165.35 0.30 1 1113 . 100 HIS HE2 H 11.71 0.05 1 1114 . 100 HIS CD2 C 118.91 0.50 1 1115 . 100 HIS HD2 H 5.05 0.05 1 1116 . 100 HIS CE1 C 136.60 0.50 1 1117 . 100 HIS HE1 H 7.49 0.05 1 1118 . 100 HIS C C 175.97 0.50 1 1119 . 101 SER H H 8.62 0.05 1 1120 . 101 SER N N 110.58 0.30 1 1121 . 101 SER CA C 60.30 0.50 1 1122 . 101 SER CB C 63.37 0.50 1 1123 . 101 SER HA H 4.22 0.05 1 1124 . 101 SER HB2 H 3.95 0.05 2 1125 . 101 SER HB3 H 4.24 0.05 2 1126 . 101 SER C C 174.87 0.50 1 1127 . 102 ALA H H 9.94 0.05 1 1128 . 102 ALA N N 126.19 0.30 1 1129 . 102 ALA CA C 50.54 0.50 1 1130 . 102 ALA CB C 21.53 0.50 1 1131 . 102 ALA HA H 4.90 0.05 1 1132 . 102 ALA HB H 1.49 0.05 1 1133 . 102 ALA C C 176.59 0.50 1 1134 . 103 GLU H H 7.45 0.05 1 1135 . 103 GLU N N 121.88 0.30 1 1136 . 103 GLU CA C 55.82 0.50 1 1137 . 103 GLU CB C 29.06 0.50 1 1138 . 103 GLU HA H 4.49 0.05 1 1139 . 103 GLU HB2 H 1.78 0.05 1 1140 . 103 GLU HB3 H 1.78 0.05 1 1141 . 103 GLU CG C 34.60 0.50 1 1142 . 103 GLU HG2 H 2.69 0.05 2 1143 . 103 GLU HG3 H 1.80 0.05 2 1144 . 103 GLU C C 177.87 0.50 1 1145 . 104 LEU H H 8.52 0.05 1 1146 . 104 LEU N N 121.50 0.30 1 1147 . 104 LEU CA C 53.24 0.50 1 1148 . 104 LEU CB C 44.55 0.50 1 1149 . 104 LEU HA H 4.90 0.05 1 1150 . 104 LEU HB2 H 1.69 0.05 1 1151 . 104 LEU HB3 H 1.69 0.05 1 1152 . 104 LEU CG C 28.47 0.50 1 1153 . 104 LEU HG H 1.84 0.05 1 1154 . 104 LEU CD2 C 26.33 0.50 1 1155 . 104 LEU CD1 C 23.81 0.50 1 1156 . 104 LEU HD2 H 0.99 0.05 1 1157 . 104 LEU HD1 H 0.99 0.05 1 1158 . 104 LEU C C 176.48 0.50 1 1159 . 105 HIS H H 9.09 0.05 1 1160 . 105 HIS N N 120.92 0.30 1 1161 . 105 HIS CA C 53.37 0.50 1 1162 . 105 HIS CB C 31.55 0.50 1 1163 . 105 HIS HA H 5.70 0.05 1 1164 . 105 HIS HB2 H 3.20 0.05 1 1165 . 105 HIS HB3 H 3.20 0.05 1 1166 . 105 HIS CD2 C 117.59 0.50 1 1167 . 105 HIS HD2 H 7.01 0.05 1 1168 . 105 HIS C C 174.03 0.50 1 1169 . 106 LEU H H 8.24 0.05 1 1170 . 106 LEU N N 123.45 0.30 1 1171 . 106 LEU CA C 53.60 0.50 1 1172 . 106 LEU CB C 47.89 0.50 1 1173 . 106 LEU HA H 4.64 0.05 1 1174 . 106 LEU HB3 H 1.50 0.05 1 1175 . 106 LEU HB2 H 1.09 0.05 1 1176 . 106 LEU CG C 26.50 0.50 1 1177 . 106 LEU HG H 1.70 0.05 1 1178 . 106 LEU CD2 C 26.03 0.50 1 1179 . 106 LEU CD1 C 24.62 0.50 1 1180 . 106 LEU HD1 H 0.84 0.05 1 1181 . 106 LEU HD2 H 0.77 0.05 1 1182 . 106 LEU C C 174.99 0.50 1 1183 . 107 GLY H H 8.85 0.05 1 1184 . 107 GLY N N 111.66 0.30 1 1185 . 107 GLY CA C 44.78 0.50 1 1186 . 107 GLY HA2 H 4.45 0.05 2 1187 . 107 GLY HA3 H 3.74 0.05 2 1188 . 107 GLY C C 177.02 0.50 1 1189 . 108 ILE H H 8.40 0.05 1 1190 . 108 ILE N N 118.34 0.30 1 1191 . 108 ILE CA C 63.71 0.50 1 1192 . 108 ILE CB C 38.35 0.50 1 1193 . 108 ILE HA H 3.66 0.05 1 1194 . 108 ILE HB H 1.78 0.05 1 1195 . 108 ILE CG1 C 28.03 0.50 1 1196 . 108 ILE CG2 C 17.90 0.50 1 1197 . 108 ILE HG12 H 1.13 0.05 2 1198 . 108 ILE HG13 H 1.26 0.05 2 1199 . 108 ILE CD1 C 13.29 0.50 1 1200 . 108 ILE HD1 H 0.81 0.05 1 1201 . 108 ILE HG2 H 0.81 0.05 1 1202 . 108 ILE C C 176.33 0.50 1 1203 . 109 HIS H H 8.78 0.05 1 1204 . 109 HIS N N 116.81 0.30 1 1205 . 109 HIS CA C 56.18 0.50 1 1206 . 109 HIS CB C 29.18 0.50 1 1207 . 109 HIS HA H 4.90 0.05 1 1208 . 109 HIS HB2 H 3.24 0.05 1 1209 . 109 HIS HB3 H 3.24 0.05 1 1210 . 109 HIS CD2 C 119.58 0.50 1 1211 . 109 HIS HD2 H 7.17 0.05 1 1212 . 109 HIS C C 176.07 0.50 1 1213 . 110 GLN H H 7.56 0.05 1 1214 . 110 GLN N N 119.47 0.30 1 1215 . 110 GLN CA C 55.11 0.50 1 1216 . 110 GLN CB C 30.07 0.50 1 1217 . 110 GLN HA H 4.77 0.05 1 1218 . 110 GLN HB2 H 2.33 0.05 2 1219 . 110 GLN HB3 H 1.90 0.05 2 1220 . 110 GLN CG C 34.20 0.50 1 1221 . 110 GLN CD C 175.80 0.50 1 1222 . 110 GLN HG2 H 2.02 0.05 2 1223 . 110 GLN HG3 H 1.53 0.05 2 1224 . 110 GLN NE2 N 113.14 0.30 1 1225 . 110 GLN HE21 H 7.60 0.05 1 1226 . 110 GLN HE22 H 7.03 0.05 1 1227 . 110 GLN C C 176.51 0.50 1 1228 . 111 LEU H H 7.72 0.05 1 1229 . 111 LEU N N 118.80 0.30 1 1230 . 111 LEU CA C 58.02 0.50 1 1231 . 111 LEU CB C 40.00 0.50 1 1232 . 111 LEU HA H 3.85 0.05 1 1233 . 111 LEU HB2 H 1.87 0.05 1 1234 . 111 LEU HB3 H 1.32 0.05 1 1235 . 111 LEU CD1 C 27.14 0.50 1 1236 . 111 LEU CG C 26.34 0.50 1 1237 . 111 LEU HG H 1.97 0.05 1 1238 . 111 LEU CD2 C 22.39 0.50 1 1239 . 111 LEU HD1 H 1.06 0.05 1 1240 . 111 LEU HD2 H 0.72 0.05 1 1241 . 111 LEU C C 177.84 0.50 1 1242 . 112 GLU H H 8.87 0.05 1 1243 . 112 GLU N N 117.91 0.30 1 1244 . 112 GLU CA C 58.71 0.50 1 1245 . 112 GLU CB C 28.70 0.50 1 1246 . 112 GLU HA H 4.18 0.05 1 1247 . 112 GLU HB2 H 2.09 0.05 1 1248 . 112 GLU HB3 H 2.09 0.05 1 1249 . 112 GLU CG C 36.23 0.50 1 1250 . 112 GLU HG2 H 2.33 0.05 1 1251 . 112 GLU HG3 H 2.33 0.05 1 1252 . 112 GLU C C 177.87 0.50 1 1253 . 113 GLN H H 7.99 0.05 1 1254 . 113 GLN N N 115.26 0.30 1 1255 . 113 GLN CA C 55.51 0.50 1 1256 . 113 GLN CB C 28.72 0.50 1 1257 . 113 GLN HA H 4.51 0.05 1 1258 . 113 GLN HB3 H 2.60 0.05 1 1259 . 113 GLN HB2 H 2.14 0.05 1 1260 . 113 GLN CG C 33.90 0.50 1 1261 . 113 GLN CD C 179.92 0.50 1 1262 . 113 GLN HG2 H 2.51 0.05 1 1263 . 113 GLN HG3 H 2.51 0.05 1 1264 . 113 GLN NE2 N 110.51 0.30 1 1265 . 113 GLN HE21 H 7.65 0.05 1 1266 . 113 GLN HE22 H 6.72 0.05 1 1267 . 113 GLN C C 177.01 0.50 1 1268 . 114 LEU H H 7.97 0.05 1 1269 . 114 LEU N N 120.16 0.30 1 1270 . 114 LEU CA C 60.31 0.50 1 1271 . 114 LEU CB C 40.71 0.50 1 1272 . 114 LEU HA H 3.87 0.05 1 1273 . 114 LEU HB2 H 1.93 0.05 2 1274 . 114 LEU HB3 H 1.06 0.05 2 1275 . 114 LEU CG C 28.41 0.50 1 1276 . 114 LEU HG H 1.80 0.05 1 1277 . 114 LEU CD2 C 24.49 0.50 1 1278 . 114 LEU CD1 C 26.53 0.50 1 1279 . 114 LEU HD2 H 0.73 0.05 1 1280 . 114 LEU HD1 H 0.95 0.05 1 1281 . 115 PRO CA C 67.40 0.50 1 1282 . 115 PRO CB C 31.03 0.50 1 1283 . 115 PRO HA H 3.81 0.05 1 1284 . 115 PRO HB3 H 2.46 0.05 1 1285 . 115 PRO HB2 H 1.77 0.05 1 1286 . 115 PRO CG C 28.93 0.50 1 1287 . 115 PRO HG2 H 2.13 0.05 1 1288 . 115 PRO HG3 H 1.99 0.05 1 1289 . 115 PRO CD C 49.33 0.50 1 1290 . 115 PRO HD3 H 3.21 0.05 1 1291 . 115 PRO HD2 H 3.76 0.05 1 1292 . 115 PRO C C 178.76 0.50 1 1293 . 116 TYR H H 7.05 0.05 1 1294 . 116 TYR N N 116.30 0.30 1 1295 . 116 TYR CA C 59.84 0.50 1 1296 . 116 TYR CB C 38.21 0.50 1 1297 . 116 TYR HA H 4.51 0.05 1 1298 . 116 TYR HB2 H 3.23 0.05 1 1299 . 116 TYR HB3 H 3.23 0.05 1 1300 . 116 TYR CD1 C 133.40 0.50 1 1301 . 116 TYR HD1 H 7.21 0.05 1 1302 . 116 TYR CD2 C 133.40 0.50 1 1303 . 116 TYR HD2 H 7.21 0.05 1 1304 . 116 TYR CE1 C 118.37 0.50 1 1305 . 116 TYR HE1 H 6.90 0.05 1 1306 . 116 TYR CE2 C 118.37 0.50 1 1307 . 116 TYR HE2 H 6.90 0.05 1 1308 . 116 TYR C C 178.81 0.50 1 1309 . 117 GLN H H 8.28 0.05 1 1310 . 117 GLN N N 120.37 0.30 1 1311 . 117 GLN CA C 57.36 0.50 1 1312 . 117 GLN CB C 27.93 0.50 1 1313 . 117 GLN HA H 4.51 0.05 1 1314 . 117 GLN HB3 H 2.17 0.05 1 1315 . 117 GLN HB2 H 1.83 0.05 1 1316 . 117 GLN CG C 32.82 0.50 1 1317 . 117 GLN CD C 177.34 0.50 1 1318 . 117 GLN HG2 H 2.43 0.05 2 1319 . 117 GLN HG3 H 2.34 0.05 2 1320 . 117 GLN NE2 N 109.05 0.30 1 1321 . 117 GLN HE21 H 6.91 0.05 2 1322 . 117 GLN HE22 H 6.81 0.05 2 1323 . 117 GLN C C 178.04 0.50 1 1324 . 118 VAL H H 8.90 0.05 1 1325 . 118 VAL N N 121.66 0.30 1 1326 . 118 VAL CA C 66.95 0.50 1 1327 . 118 VAL CB C 31.51 0.50 1 1328 . 118 VAL HA H 3.66 0.05 1 1329 . 118 VAL HB H 2.24 0.05 1 1330 . 118 VAL CG2 C 22.87 0.50 1 1331 . 118 VAL CG1 C 21.64 0.50 1 1332 . 118 VAL HG1 H 0.98 0.05 1 1333 . 118 VAL HG2 H 0.84 0.05 1 1334 . 118 VAL C C 177.35 0.50 1 1335 . 119 ASP H H 6.92 0.05 1 1336 . 119 ASP N N 118.21 0.30 1 1337 . 119 ASP CA C 57.93 0.50 1 1338 . 119 ASP CB C 40.14 0.50 1 1339 . 119 ASP HA H 4.44 0.05 1 1340 . 119 ASP HB2 H 2.79 0.05 1 1341 . 119 ASP HB3 H 2.67 0.05 1 1342 . 119 ASP C C 179.80 0.50 1 1343 . 120 ALA H H 8.03 0.05 1 1344 . 120 ALA N N 123.03 0.30 1 1345 . 120 ALA CA C 55.07 0.50 1 1346 . 120 ALA CB C 17.92 0.50 1 1347 . 120 ALA HA H 4.25 0.05 1 1348 . 120 ALA HB H 1.47 0.05 1 1349 . 120 ALA C C 179.61 0.50 1 1350 . 121 ALA H H 9.11 0.05 1 1351 . 121 ALA N N 125.45 0.30 1 1352 . 121 ALA CA C 55.61 0.50 1 1353 . 121 ALA CB C 17.74 0.50 1 1354 . 121 ALA HA H 4.14 0.05 1 1355 . 121 ALA HB H 1.62 0.05 1 1356 . 121 ALA C C 181.85 0.50 1 1357 . 122 LEU H H 8.18 0.05 1 1358 . 122 LEU N N 121.30 0.30 1 1359 . 122 LEU CA C 59.15 0.50 1 1360 . 122 LEU CB C 41.58 0.50 1 1361 . 122 LEU HA H 4.04 0.05 1 1362 . 122 LEU HB2 H 1.97 0.05 2 1363 . 122 LEU HB3 H 1.77 0.05 2 1364 . 122 LEU CG C 28.69 0.50 1 1365 . 122 LEU HG H 2.02 0.05 1 1366 . 122 LEU CD1 C 24.84 0.50 1 1367 . 122 LEU HD1 H 0.95 0.05 1 1368 . 122 LEU CD2 C 24.84 0.50 1 1369 . 122 LEU HD2 H 0.95 0.05 1 1370 . 122 LEU C C 179.17 0.50 1 1371 . 123 ALA H H 7.75 0.05 1 1372 . 123 ALA N N 120.86 0.30 1 1373 . 123 ALA CA C 55.20 0.50 1 1374 . 123 ALA CB C 18.37 0.50 1 1375 . 123 ALA HA H 4.23 0.05 1 1376 . 123 ALA HB H 1.60 0.05 1 1377 . 123 ALA C C 181.31 0.50 1 1378 . 124 GLU H H 9.08 0.05 1 1379 . 124 GLU N N 121.47 0.30 1 1380 . 124 GLU CA C 58.49 0.50 1 1381 . 124 GLU CB C 30.07 0.50 1 1382 . 124 GLU HA H 4.49 0.05 1 1383 . 124 GLU HB2 H 2.29 0.05 1 1384 . 124 GLU HB3 H 2.13 0.05 1 1385 . 124 GLU CG C 35.09 0.50 1 1386 . 124 GLU HG2 H 2.57 0.05 2 1387 . 124 GLU HG3 H 2.37 0.05 2 1388 . 124 GLU C C 177.67 0.50 1 1389 . 125 PHE H H 7.68 0.05 1 1390 . 125 PHE N N 118.66 0.30 1 1391 . 125 PHE CA C 61.76 0.50 1 1392 . 125 PHE CB C 40.54 0.50 1 1393 . 125 PHE HA H 3.67 0.05 1 1394 . 125 PHE HB2 H 3.28 0.05 1 1395 . 125 PHE HB3 H 3.28 0.05 1 1396 . 125 PHE CD1 C 132.22 0.50 1 1397 . 125 PHE HD1 H 6.94 0.05 1 1398 . 125 PHE CD2 C 132.22 0.50 1 1399 . 125 PHE HD2 H 6.94 0.05 1 1400 . 125 PHE CE1 C 131.33 0.50 1 1401 . 125 PHE HE1 H 6.70 0.05 1 1402 . 125 PHE CE2 C 131.33 0.50 1 1403 . 125 PHE HE2 H 6.70 0.05 1 1404 . 125 PHE CZ C 129.81 0.50 1 1405 . 125 PHE HZ H 7.10 0.05 1 1406 . 125 PHE C C 176.16 0.50 1 1407 . 126 LEU H H 7.43 0.05 1 1408 . 126 LEU N N 114.46 0.30 1 1409 . 126 LEU CA C 57.25 0.50 1 1410 . 126 LEU CB C 42.25 0.50 1 1411 . 126 LEU HA H 4.16 0.05 1 1412 . 126 LEU HB3 H 1.67 0.05 1 1413 . 126 LEU HB2 H 1.92 0.05 1 1414 . 126 LEU CG C 27.10 0.50 1 1415 . 126 LEU HG H 1.96 0.05 1 1416 . 126 LEU CD1 C 24.95 0.50 1 1417 . 126 LEU CD2 C 23.35 0.50 1 1418 . 126 LEU HD1 H 1.02 0.05 1 1419 . 126 LEU HD2 H 1.02 0.05 1 1420 . 126 LEU C C 179.88 0.50 1 1421 . 127 ARG H H 8.14 0.05 1 1422 . 127 ARG N N 119.82 0.30 1 1423 . 127 ARG CA C 59.25 0.50 1 1424 . 127 ARG CB C 31.40 0.50 1 1425 . 127 ARG HA H 4.04 0.05 1 1426 . 127 ARG HB2 H 1.95 0.05 1 1427 . 127 ARG HB3 H 1.95 0.05 1 1428 . 127 ARG CG C 28.27 0.50 1 1429 . 127 ARG HG2 H 1.60 0.05 1 1430 . 127 ARG HG3 H 1.60 0.05 1 1431 . 127 ARG CD C 43.32 0.50 1 1432 . 127 ARG HD2 H 3.41 0.05 2 1433 . 127 ARG HD3 H 3.08 0.05 2 1434 . 127 ARG NE N 83.34 0.30 1 1435 . 127 ARG HE H 8.15 0.05 1 1436 . 127 ARG C C 178.17 0.50 1 1437 . 128 LEU H H 7.60 0.05 1 1438 . 128 LEU N N 116.98 0.30 1 1439 . 128 LEU CA C 54.10 0.50 1 1440 . 128 LEU CB C 42.42 0.50 1 1441 . 128 LEU HA H 4.28 0.05 1 1442 . 128 LEU HB2 H 1.53 0.05 1 1443 . 128 LEU HB3 H 1.53 0.05 1 1444 . 128 LEU CG C 27.26 0.50 1 1445 . 128 LEU HG H 1.59 0.05 1 1446 . 128 LEU CD2 C 25.80 0.50 1 1447 . 128 LEU CD1 C 22.42 0.50 1 1448 . 128 LEU HD2 H 0.87 0.05 1 1449 . 128 LEU HD1 H 0.87 0.05 1 1450 . 128 LEU C C 175.48 0.50 1 1451 . 129 ALA H H 7.04 0.05 1 1452 . 129 ALA N N 122.33 0.30 1 1453 . 129 ALA CA C 51.38 0.50 1 1454 . 129 ALA CB C 17.45 0.50 1 1455 . 129 ALA HA H 3.99 0.05 1 1456 . 129 ALA HB H 1.23 0.05 1 1457 . 130 PRO CA C 61.75 0.50 1 1458 . 130 PRO CB C 33.36 0.50 1 1459 . 130 PRO HA H 4.46 0.05 1 1460 . 130 PRO HB3 H 2.26 0.05 1 1461 . 130 PRO HB2 H 2.04 0.05 1 1462 . 130 PRO CG C 25.02 0.50 1 1463 . 130 PRO HG2 H 2.11 0.05 1 1464 . 130 PRO HG3 H 1.89 0.05 1 1465 . 130 PRO CD C 50.12 0.50 1 1466 . 130 PRO HD2 H 3.48 0.05 1 1467 . 130 PRO HD3 H 3.57 0.05 1 1468 . 130 PRO C C 173.46 0.50 1 1469 . 131 VAL H H 7.91 0.05 1 1470 . 131 VAL N N 121.44 0.30 1 1471 . 131 VAL CA C 61.90 0.50 1 1472 . 131 VAL CB C 31.92 0.50 1 1473 . 131 VAL HA H 3.66 0.05 1 1474 . 131 VAL HB H 1.77 0.05 1 1475 . 131 VAL CG1 C 21.99 0.50 2 1476 . 131 VAL CG2 C 19.65 0.50 2 1477 . 131 VAL HG1 H 0.25 0.05 2 1478 . 131 VAL HG2 H 0.10 0.05 2 1479 . 131 VAL C C 175.35 0.50 1 1480 . 132 GLU H H 8.08 0.05 1 1481 . 132 GLU N N 123.39 0.30 1 1482 . 132 GLU CA C 54.74 0.50 1 1483 . 132 GLU CB C 31.86 0.50 1 1484 . 132 GLU HA H 4.68 0.05 1 1485 . 132 GLU HB2 H 2.04 0.05 2 1486 . 132 GLU HB3 H 1.89 0.05 2 1487 . 132 GLU CG C 36.11 0.50 1 1488 . 132 GLU HG2 H 2.31 0.05 1 1489 . 132 GLU HG3 H 2.31 0.05 1 1490 . 132 GLU C C 176.93 0.50 1 1491 . 133 THR H H 8.61 0.05 1 1492 . 133 THR N N 114.73 0.30 1 1493 . 133 THR CA C 61.33 0.50 1 1494 . 133 THR CB C 70.18 0.50 1 1495 . 133 THR HA H 4.69 0.05 1 1496 . 133 THR HB H 4.83 0.05 1 1497 . 133 THR CG2 C 23.44 0.50 1 1498 . 133 THR HG2 H 1.36 0.05 1 1499 . 133 THR C C 175.66 0.50 1 1500 . 134 MET H H 8.26 0.05 1 1501 . 134 MET N N 119.20 0.30 1 1502 . 134 MET CA C 54.16 0.50 1 1503 . 134 MET CB C 32.52 0.50 1 1504 . 134 MET HA H 4.78 0.05 1 1505 . 134 MET HG2 H 2.56 0.05 2 1506 . 134 MET HG3 H 2.08 0.05 2 1507 . 134 MET HB3 H 2.07 0.05 1 1508 . 134 MET HB2 H 1.54 0.05 1 1509 . 134 MET CG C 32.49 0.50 1 1510 . 134 MET C C 175.19 0.50 1 1511 . 135 ALA H H 7.45 0.05 1 1512 . 135 ALA N N 128.79 0.30 1 1513 . 135 ALA CA C 53.67 0.50 1 1514 . 135 ALA CB C 21.44 0.50 1 1515 . 135 ALA HA H 4.29 0.05 1 1516 . 135 ALA HB H 1.50 0.05 1 stop_ save_