data_5595 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: 1H, 13C, 15N backbone resonance assignments of apo-NosL, a novel 18.5 kDa copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes ; _BMRB_accession_number 5595 _BMRB_flat_file_name bmr5595.str _Entry_type original _Submission_date 2002-11-21 _Accession_date 2002-11-21 _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 Taubner Lara M . 2 McGuirl Michele A . 3 Dooley David M . 4 Copie Valerie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 696 "13C chemical shifts" 596 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-15 original author . stop_ _Original_release_date 2004-03-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15014237 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Taubner Lara M . 2 McGuirl Michele A . 3 Dooley David M . 4 Copie Valerie V . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 211 _Page_last 212 _Year 2004 _Details . loop_ _Keyword NosL 'nitrous oxide reductase' 'copper chaperone' 'NMR resonance' assignments stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; McGuirl MA, Bollinger JA, Cosper N, Scott RA, Dooley DM. Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster. J Biol Inorg Chem. 2001 Feb;6(2):189-95. ; _Citation_title 'Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11293413 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McGuirl 'M A' A. . 2 Bollinger 'J A' A. . 3 Cosper N . . 4 Scott 'R A' A. . 5 Dooley 'D M' M. . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_name_full 'Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry' _Journal_volume 6 _Journal_issue 2 _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 189 _Page_last 195 _Year 2001 _Details ; NosL, one of the accessory proteins of the nos (nitrous oxide reductase) gene cluster, has been heterologously expressed, purified, and characterized. NosL is a monomeric protein of 18,540 MW that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. While it is possible to oxidize Cu(I)-NosL with ferricyanide, the Cu(II) ion thus formed appears to dissociate from the protein. The function of Cu(I)NosL is not yet known, but the data indicate that NosL does not act as an electron transfer partner to nitrous oxide reductase. NosL is encoded on the same transcript as three other gene products (NosD, NosF, and NosY). These have been shown to be required for assembly of the active site in nitrous oxide reductase, which is thought to be a copper cluster. Accordingly, it is possible that NosL is a copper chaperone involved in metallocenter assembly. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; McGuirl MA, Nelson LK, Bollinger JA, Chan YK, Dooley DM. The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression. J Inorg Biochem. 1998 Jul;70(3-4):155-69. ; _Citation_title 'The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9720302 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McGuirl 'M A' A. . 2 Nelson 'L K' K. . 3 Bollinger 'J A' A. . 4 Chan 'Y K' K. . 5 Dooley 'D M' M. . stop_ _Journal_abbreviation 'J. Inorg. Biochem.' _Journal_name_full 'Journal of inorganic biochemistry' _Journal_volume 70 _Journal_issue 3-4 _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 155 _Page_last 169 _Year 1998 _Details ; The nitrous oxide (N2O) reductase (nos) gene cluster from Achromobacter cycloclastes has been cloned and sequenced. Seven protein coding regions corresponding to nosR, nosZ (structural N2O reductase gene), nosD, nosF, nosY, nosL, and nosX are detected, indicating a genetic organization similar to that of Rhizobium meliloti. To aid homology studies, nosR from R. meliloti has also been sequenced. Comparison of the deduced amino acid sequences with corresponding sequences from other organisms has also allowed structural and functional inferences to be made. The heterologous expression of NosD, NosZ (N2O reductase), and NosL is also reported. A model of the CuA site in N2O reductase, based on the crystal structure of this site in bovine heart cytochrome c oxidase, is presented. The model suggests that a His residue of the CuA domain may be a ligand to the catalytic CuZ site. In addition, the origin of the spectroscopically-observed Cys coordination to CuZ is discussed in terms of the sequence alignment of seven N2O reductases. ; save_ ################################## # Molecular system description # ################################## save_system_NosL _Saveframe_category molecular_system _Mol_system_name NosL _Abbreviation_common NosL _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NosL monomer' $NosL stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'copper(I) binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NosL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NosL _Abbreviation_common NosL _Molecular_mass 18538 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 175 _Mol_residue_sequence ; MDKEDVAQSIVPQDMTPETL GHYCQMNLLEHPGPKAQIFL EGSPAPLFFSQVRDAIAYAR GPEQIAPILVIYVNDMGAAG ATWDQPGDGNWIAADKAFYV VGSARRGGMGAPEAVPFSSR DEAAAFVLAEGGQVLALADI TDAMVLTPVETGSEPRADDE DYLGRLRALPHPAGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 LYS 4 GLU 5 ASP 6 VAL 7 ALA 8 GLN 9 SER 10 ILE 11 VAL 12 PRO 13 GLN 14 ASP 15 MET 16 THR 17 PRO 18 GLU 19 THR 20 LEU 21 GLY 22 HIS 23 TYR 24 CYS 25 GLN 26 MET 27 ASN 28 LEU 29 LEU 30 GLU 31 HIS 32 PRO 33 GLY 34 PRO 35 LYS 36 ALA 37 GLN 38 ILE 39 PHE 40 LEU 41 GLU 42 GLY 43 SER 44 PRO 45 ALA 46 PRO 47 LEU 48 PHE 49 PHE 50 SER 51 GLN 52 VAL 53 ARG 54 ASP 55 ALA 56 ILE 57 ALA 58 TYR 59 ALA 60 ARG 61 GLY 62 PRO 63 GLU 64 GLN 65 ILE 66 ALA 67 PRO 68 ILE 69 LEU 70 VAL 71 ILE 72 TYR 73 VAL 74 ASN 75 ASP 76 MET 77 GLY 78 ALA 79 ALA 80 GLY 81 ALA 82 THR 83 TRP 84 ASP 85 GLN 86 PRO 87 GLY 88 ASP 89 GLY 90 ASN 91 TRP 92 ILE 93 ALA 94 ALA 95 ASP 96 LYS 97 ALA 98 PHE 99 TYR 100 VAL 101 VAL 102 GLY 103 SER 104 ALA 105 ARG 106 ARG 107 GLY 108 GLY 109 MET 110 GLY 111 ALA 112 PRO 113 GLU 114 ALA 115 VAL 116 PRO 117 PHE 118 SER 119 SER 120 ARG 121 ASP 122 GLU 123 ALA 124 ALA 125 ALA 126 PHE 127 VAL 128 LEU 129 ALA 130 GLU 131 GLY 132 GLY 133 GLN 134 VAL 135 LEU 136 ALA 137 LEU 138 ALA 139 ASP 140 ILE 141 THR 142 ASP 143 ALA 144 MET 145 VAL 146 LEU 147 THR 148 PRO 149 VAL 150 GLU 151 THR 152 GLY 153 SER 154 GLU 155 PRO 156 ARG 157 ALA 158 ASP 159 ASP 160 GLU 161 ASP 162 TYR 163 LEU 164 GLY 165 ARG 166 LEU 167 ARG 168 ALA 169 LEU 170 PRO 171 HIS 172 PRO 173 ALA 174 GLY 175 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 2HPU "Solution Nmr Structure Of The Apo-Nosl Protein From Achromobacter Cycloclastes" 100.00 175 100.00 100.00 3.23e-122 PDB 2HQ3 "Solution Nmr Structure Of The Apo-Nosl Protein From Achromobacter Cycloclastes" 100.00 175 100.00 100.00 3.23e-122 EMBL CAA75429 "nosL [Achromobacter cycloclastes]" 98.86 193 100.00 100.00 4.71e-121 GB AAD09161 "NosL precursor [Achromobacter cycloclastes]" 98.86 193 100.00 100.00 4.71e-121 GB KDP72987 "copper chaperone [Ensifer adhaerens]" 98.86 193 100.00 100.00 5.99e-121 REF WP_029742711 "copper chaperone [Ensifer sp. JGI 0001011-A08]" 98.86 193 100.00 100.00 4.71e-121 REF WP_034799000 "copper chaperone [Ensifer adhaerens]" 98.86 193 100.00 100.00 5.99e-121 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $NosL 'Denitrifying bacteria' 223 Eubacteria . Achromobacter cycloclastes nosl stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $NosL 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET-20b+ stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_13C_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NosL 1.0 mM '[U-15N; U-13C]' DTT 1.0 mM [U-2D] EDTA 1.0 mM . D2O 10 % . 'sodium phosphate' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing 'peak picking' 'peak tables' stop_ _Details 'Delaglio, F., Grzesiek S., Vuister G.' save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task processing 'peak picking' 'peak tables' stop_ _Details 'Garret, D.S., Powers, R., Gronenborn, A.' save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 loop_ _Task processing stop_ _Details 'Bruker Inc.' 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_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CCONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _Sample_label . save_ save_HCCONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _Sample_label . save_ save_HBHACONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label . save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_15N-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSY _Sample_label . save_ save_15N-NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY _Sample_label . save_ save_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_15N_13C_NosL_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.5 0.1 n/a temperature 303 1 K 'ionic strength' 0.1 0.02 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_15N-13C_NosL_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $15N_13C_sample stop_ _Sample_conditions_label $15N_13C_NosL_cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'NosL 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 . 2 ASP HA H 4.65 0.02 1 2 . 2 ASP HB2 H 2.71 0.02 2 3 . 2 ASP HB3 H 2.60 0.02 2 4 . 2 ASP C C 175.90 0.50 1 5 . 2 ASP CA C 54.64 0.50 1 6 . 2 ASP CB C 41.40 0.50 1 7 . 3 LYS H H 8.38 0.02 1 8 . 3 LYS HA H 4.23 0.02 1 9 . 3 LYS HB2 H 1.79 0.02 2 10 . 3 LYS HG2 H 1.41 0.02 2 11 . 3 LYS HD2 H 1.67 0.02 2 12 . 3 LYS HE2 H 2.99 0.02 2 13 . 3 LYS C C 176.59 0.50 1 14 . 3 LYS CA C 56.81 0.50 1 15 . 3 LYS CB C 33.12 0.50 1 16 . 3 LYS CG C 24.51 0.50 1 17 . 3 LYS CD C 29.12 0.50 1 18 . 3 LYS CE C 42.17 0.50 1 19 . 3 LYS N N 121.50 0.30 1 20 . 4 GLU H H 8.48 0.02 1 21 . 4 GLU HA H 4.22 0.02 1 22 . 4 GLU HB2 H 1.97 0.02 2 23 . 4 GLU HG2 H 2.23 0.02 2 24 . 4 GLU C C 176.33 0.50 1 25 . 4 GLU CA C 56.90 0.50 1 26 . 4 GLU CB C 30.12 0.50 1 27 . 4 GLU CG C 36.39 0.50 1 28 . 4 GLU N N 121.42 0.30 1 29 . 5 ASP H H 8.24 0.02 1 30 . 5 ASP HA H 4.56 0.02 1 31 . 5 ASP HB2 H 2.62 0.02 2 32 . 5 ASP CA C 54.46 0.50 1 33 . 5 ASP CB C 41.08 0.50 1 34 . 5 ASP N N 121.48 0.30 1 35 . 6 VAL H H 7.95 0.02 1 36 . 6 VAL HA H 4.03 0.02 1 37 . 6 VAL HB H 2.08 0.02 1 38 . 6 VAL HG1 H 0.90 0.02 2 39 . 6 VAL C C 176.31 0.50 1 40 . 6 VAL CA C 62.84 0.50 1 41 . 6 VAL CB C 32.57 0.50 1 42 . 6 VAL CG1 C 23.77 0.50 2 43 . 6 VAL CG2 C 20.85 0.50 2 44 . 6 VAL N N 120.48 0.30 1 45 . 7 ALA H H 8.24 0.02 1 46 . 7 ALA HA H 4.19 0.02 1 47 . 7 ALA HB H 1.35 0.02 1 48 . 7 ALA C C 177.90 0.50 1 49 . 7 ALA CA C 53.03 0.50 1 50 . 7 ALA CB C 18.95 0.50 1 51 . 7 ALA N N 126.15 0.30 1 52 . 8 GLN H H 8.05 0.02 1 53 . 8 GLN HA H 4.22 0.02 1 54 . 8 GLN HB2 H 2.00 0.02 2 55 . 8 GLN HG2 H 2.32 0.02 2 56 . 8 GLN C C 175.97 0.50 1 57 . 8 GLN CA C 56.10 0.50 1 58 . 8 GLN CB C 29.27 0.50 1 59 . 8 GLN CG C 33.84 0.50 1 60 . 8 GLN N N 118.26 0.30 1 61 . 9 SER H H 8.12 0.02 1 62 . 9 SER HA H 4.35 0.02 1 63 . 9 SER HB2 H 3.79 0.02 2 64 . 9 SER C C 174.44 0.50 1 65 . 9 SER CA C 58.42 0.50 1 66 . 9 SER CB C 63.76 0.50 1 67 . 9 SER N N 116.43 0.30 1 68 . 10 ILE H H 7.88 0.02 1 69 . 10 ILE HA H 3.65 0.02 1 70 . 10 ILE HB H 1.43 0.02 1 71 . 10 ILE HG12 H 0.82 0.02 2 72 . 10 ILE HG2 H 0.55 0.02 1 73 . 10 ILE HD1 H -0.06 0.02 1 74 . 10 ILE C C 175.03 0.50 1 75 . 10 ILE CA C 60.57 0.50 1 76 . 10 ILE CB C 37.49 0.50 1 77 . 10 ILE CG1 C 27.06 0.50 1 78 . 10 ILE CG2 C 16.61 0.50 1 79 . 10 ILE CD1 C 13.37 0.50 1 80 . 10 ILE N N 122.57 0.30 1 81 . 11 VAL H H 7.47 0.02 1 82 . 11 VAL HA H 4.11 0.02 1 83 . 11 VAL HB H 1.89 0.02 1 84 . 11 VAL HG1 H 0.89 0.02 2 85 . 11 VAL CA C 59.58 0.50 1 86 . 11 VAL CB C 32.63 0.50 1 87 . 11 VAL N N 126.28 0.30 1 88 . 12 PRO HA H 3.78 0.02 1 89 . 12 PRO HB2 H 0.92 0.02 2 90 . 12 PRO HB3 H 0.62 0.02 2 91 . 12 PRO HG2 H 0.54 0.02 2 92 . 12 PRO HG3 H 1.56 0.02 2 93 . 12 PRO HD2 H 3.41 0.02 2 94 . 12 PRO HD3 H 3.12 0.02 2 95 . 12 PRO C C 176.80 0.50 1 96 . 12 PRO CA C 62.62 0.50 1 97 . 12 PRO CB C 31.32 0.50 1 98 . 12 PRO CG C 26.48 0.50 1 99 . 12 PRO CD C 50.02 0.50 1 100 . 13 GLN H H 9.22 0.02 1 101 . 13 GLN HA H 4.37 0.02 1 102 . 13 GLN HB2 H 2.18 0.02 2 103 . 13 GLN HB3 H 1.68 0.02 2 104 . 13 GLN HG2 H 2.49 0.02 2 105 . 13 GLN C C 175.10 0.50 1 106 . 13 GLN CA C 54.15 0.50 1 107 . 13 GLN CB C 31.02 0.50 1 108 . 13 GLN CG C 34.19 0.50 1 109 . 13 GLN N N 122.88 0.3 1 110 . 14 ASP H H 8.32 0.02 1 111 . 14 ASP HA H 5.33 0.02 1 112 . 14 ASP HB2 H 2.85 0.02 2 113 . 14 ASP C C 175.38 0.50 1 114 . 14 ASP CA C 54.13 0.50 1 115 . 14 ASP CB C 43.05 0.50 1 116 . 14 ASP N N 117.82 0.30 1 117 . 15 MET H H 8.41 0.02 1 118 . 15 MET CA C 56.37 0.50 1 119 . 15 MET CB C 33.95 0.50 1 120 . 15 MET N N 118.64 0.30 1 121 . 17 PRO HA H 4.72 0.02 1 122 . 17 PRO HB2 H 2.08 0.02 2 123 . 17 PRO HB3 H 2.34 0.02 2 124 . 17 PRO HG2 H 1.86 0.02 2 125 . 17 PRO HD2 H 3.51 0.02 1 126 . 17 PRO C C 176.18 0.50 1 127 . 17 PRO CA C 62.39 0.50 1 128 . 17 PRO CB C 34.40 0.50 1 129 . 17 PRO CG C 24.76 0.50 1 130 . 17 PRO CD C 50.24 0.50 1 131 . 18 GLU H H 8.57 0.02 1 132 . 18 GLU HA H 4.19 0.02 1 133 . 18 GLU HB2 H 2.07 0.02 2 134 . 18 GLU HG2 H 2.17 0.02 2 135 . 18 GLU C C 176.66 0.50 1 136 . 18 GLU CA C 56.45 0.50 1 137 . 18 GLU CB C 30.09 0.50 1 138 . 18 GLU CG C 36.86 0.50 1 139 . 18 GLU N N 122.42 0.30 1 140 . 19 THR H H 7.61 0.02 1 141 . 19 THR CA C 64.66 0.50 1 142 . 19 THR CB C 68.84 0.50 1 143 . 19 THR N N 117.36 0.30 1 144 . 20 LEU C C 177.53 0.50 1 145 . 21 GLY H H 8.22 0.02 1 146 . 21 GLY HA2 H 3.87 0.02 2 147 . 21 GLY C C 174.77 0.50 1 148 . 21 GLY CA C 45.79 0.50 1 149 . 21 GLY N N 106.67 0.30 1 150 . 22 HIS H H 7.80 0.02 1 151 . 22 HIS HA H 5.20 0.02 1 152 . 22 HIS CA C 56.43 0.50 1 153 . 22 HIS CB C 30.70 0.50 1 154 . 22 HIS N N 119.64 0.30 1 155 . 29 LEU HA H 4.08 0.02 1 156 . 29 LEU HB2 H 1.55 0.02 2 157 . 29 LEU HD1 H 0.74 0.02 2 158 . 29 LEU C C 176.63 0.50 1 159 . 29 LEU CA C 56.92 0.50 1 160 . 29 LEU CB C 41.67 0.50 1 161 . 29 LEU CG C 27.06 0.50 1 162 . 29 LEU CD1 C 24.38 0.50 2 163 . 29 LEU CD2 C 24.85 0.50 2 164 . 30 GLU H H 7.65 0.02 1 165 . 30 GLU HA H 4.21 0.02 1 166 . 30 GLU HB2 H 2.04 0.02 2 167 . 30 GLU HB3 H 1.81 0.02 2 168 . 30 GLU HG2 H 2.13 0.02 2 169 . 30 GLU C C 175.73 0.50 1 170 . 30 GLU CA C 55.97 0.50 1 171 . 30 GLU CB C 29.96 0.50 1 172 . 30 GLU CG C 36.46 0.50 1 173 . 30 GLU N N 114.88 0.30 1 174 . 31 HIS H H 7.71 0.02 1 175 . 31 HIS HA H 5.06 0.02 1 176 . 31 HIS HB2 H 3.18 0.02 2 177 . 31 HIS HB3 H 4.18 0.02 2 178 . 31 HIS CA C 53.54 0.50 1 179 . 31 HIS CB C 30.71 0.50 1 180 . 31 HIS N N 119.38 0.30 1 181 . 32 PRO HA H 4.71 0.02 1 182 . 32 PRO HB2 H 2.50 0.02 2 183 . 32 PRO HB3 H 2.04 0.02 2 184 . 32 PRO HG2 H 2.23 0.02 2 185 . 32 PRO HG3 H 2.06 0.02 2 186 . 32 PRO HD2 H 3.95 0.02 2 187 . 32 PRO HD3 H 3.81 0.02 2 188 . 32 PRO C C 175.55 0.50 1 189 . 32 PRO CA C 63.02 0.50 1 190 . 32 PRO CB C 33.89 0.50 1 191 . 32 PRO CG C 27.05 0.50 1 192 . 32 PRO CD C 50.47 0.50 1 193 . 33 GLY H H 7.85 0.02 1 194 . 33 GLY HA2 H 4.02 0.02 2 195 . 33 GLY CA C 43.45 0.50 1 196 . 33 GLY N N 105.94 0.30 1 197 . 34 PRO HA H 4.30 0.02 1 198 . 34 PRO HB2 H 1.81 0.02 2 199 . 34 PRO HG2 H 2.49 0.02 2 200 . 34 PRO HG3 H 2.02 0.02 2 201 . 34 PRO HD2 H 3.36 0.02 2 202 . 34 PRO C C 174.35 0.50 1 203 . 34 PRO CA C 62.75 0.50 1 204 . 34 PRO CB C 31.73 0.50 1 205 . 34 PRO CG C 26.99 0.50 1 206 . 35 LYS H H 8.58 0.02 1 207 . 35 LYS HA H 4.74 0.02 1 208 . 35 LYS HB2 H 2.43 0.02 2 209 . 35 LYS HB3 H 1.90 0.02 2 210 . 35 LYS HG2 H 1.55 0.02 2 211 . 35 LYS HG3 H 2.34 0.02 2 212 . 35 LYS HE2 H 3.11 0.02 2 213 . 35 LYS C C 174.80 0.50 1 214 . 35 LYS CA C 53.37 0.50 1 215 . 35 LYS CB C 35.94 0.50 1 216 . 35 LYS CG C 29.19 0.50 1 217 . 35 LYS N N 117.42 0.30 1 218 . 36 ALA H H 7.74 0.02 1 219 . 36 ALA HA H 5.90 0.02 1 220 . 36 ALA HB H 1.38 0.02 1 221 . 36 ALA C C 175.21 0.50 1 222 . 36 ALA CA C 50.05 0.50 1 223 . 36 ALA CB C 26.49 0.50 1 224 . 36 ALA N N 115.89 0.30 1 225 . 37 GLN H H 9.33 0.02 1 226 . 37 GLN HA H 5.52 0.02 1 227 . 37 GLN HB2 H 0.96 0.02 2 228 . 37 GLN HB3 H 0.84 0.02 2 229 . 37 GLN HG2 H 1.60 0.02 2 230 . 37 GLN HG3 H 1.30 0.02 2 231 . 37 GLN C C 173.16 0.50 1 232 . 37 GLN CA C 53.39 0.50 1 233 . 37 GLN CB C 33.30 0.50 1 234 . 37 GLN CG C 34.91 0.50 1 235 . 37 GLN N N 116.98 0.30 1 236 . 38 ILE H H 9.07 0.02 1 237 . 38 ILE HA H 4.69 0.02 1 238 . 38 ILE HB H 1.53 0.02 4 239 . 38 ILE HG12 H 1.48 0.02 4 240 . 38 ILE HG2 H 0.81 0.02 1 241 . 38 ILE HD1 H 0.61 0.02 1 242 . 38 ILE C C 174.52 0.50 1 243 . 38 ILE CA C 60.97 0.50 1 244 . 38 ILE CB C 41.81 0.50 1 245 . 38 ILE CG1 C 18.27 0.50 1 246 . 38 ILE CG2 C 14.71 0.50 1 247 . 38 ILE CD1 C 12.73 0.50 1 248 . 38 ILE N N 121.70 0.30 1 249 . 39 PHE H H 8.36 0.02 1 250 . 39 PHE HA H 4.77 0.02 1 251 . 39 PHE HB2 H 2.81 0.02 2 252 . 39 PHE C C 175.06 0.50 1 253 . 39 PHE CA C 57.41 0.50 1 254 . 39 PHE CB C 40.98 0.50 1 255 . 39 PHE N N 124.12 0.30 1 256 . 40 LEU H H 9.54 0.02 1 257 . 40 LEU HA H 4.95 0.02 1 258 . 40 LEU HB2 H 1.62 0.02 2 259 . 40 LEU HB3 H 1.31 0.02 2 260 . 40 LEU HG H 1.56 0.02 1 261 . 40 LEU HD1 H 0.97 0.02 2 262 . 40 LEU HD2 H 0.87 0.02 2 263 . 40 LEU C C 177.64 0.50 1 264 . 40 LEU CA C 52.67 0.50 1 265 . 40 LEU CB C 43.99 0.50 1 266 . 40 LEU CG C 27.10 0.50 1 267 . 40 LEU CD1 C 24.97 0.50 2 268 . 40 LEU CD2 C 25.53 0.50 2 269 . 40 LEU N N 124.64 0.30 1 270 . 41 GLU H H 8.71 0.02 1 271 . 41 GLU HA H 3.99 0.02 1 272 . 41 GLU HB2 H 1.94 0.02 2 273 . 41 GLU HB3 H 1.86 0.02 2 274 . 41 GLU HG2 H 2.20 0.02 2 275 . 41 GLU HG3 H 2.10 0.02 2 276 . 41 GLU C C 177.53 0.50 1 277 . 41 GLU CA C 58.34 0.50 1 278 . 41 GLU CB C 30.59 0.50 1 279 . 41 GLU CG C 36.42 0.50 1 280 . 41 GLU N N 123.56 0.30 1 281 . 42 GLY H H 8.98 0.02 1 282 . 42 GLY HA2 H 4.22 0.02 2 283 . 42 GLY HA3 H 3.69 0.02 2 284 . 42 GLY C C 174.17 0.50 1 285 . 42 GLY CA C 45.43 0.50 1 286 . 42 GLY N N 114.82 0.30 1 287 . 43 SER H H 7.46 0.02 1 288 . 43 SER HA H 5.11 0.02 1 289 . 43 SER HB2 H 4.25 0.02 2 290 . 43 SER HB3 H 3.83 0.02 2 291 . 43 SER CA C 55.29 0.50 1 292 . 43 SER CB C 64.74 0.50 1 293 . 43 SER N N 115.26 0.30 1 294 . 44 PRO HA H 4.49 0.02 1 295 . 44 PRO HB2 H 2.30 0.02 2 296 . 44 PRO HB3 H 2.04 0.02 2 297 . 44 PRO HD2 H 3.97 0.02 2 298 . 44 PRO HD3 H 3.81 0.02 2 299 . 44 PRO C C 175.81 0.50 1 300 . 44 PRO CA C 64.16 0.50 1 301 . 44 PRO CB C 32.33 0.50 1 302 . 44 PRO CG C 26.88 0.50 1 303 . 44 PRO CD C 51.13 0.50 1 304 . 45 ALA H H 7.47 0.02 1 305 . 45 ALA HA H 4.00 0.02 1 306 . 45 ALA HB H 1.25 0.02 1 307 . 45 ALA CA C 48.78 0.50 1 308 . 45 ALA CB C 19.27 0.50 1 309 . 45 ALA N N 120.92 0.30 1 310 . 46 PRO HA H 4.10 0.02 1 311 . 46 PRO HB2 H 0.41 0.02 2 312 . 46 PRO HG2 H 1.14 0.02 2 313 . 46 PRO HG3 H 2.42 0.02 2 314 . 46 PRO HD2 H 3.44 0.02 2 315 . 46 PRO C C 175.41 0.50 1 316 . 46 PRO CA C 61.59 0.50 1 317 . 46 PRO CB C 31.06 0.50 1 318 . 46 PRO CG C 25.76 0.50 1 319 . 46 PRO CD C 49.83 0.50 1 320 . 47 LEU H H 8.41 0.02 1 321 . 47 LEU HA H 4.15 0.02 1 322 . 47 LEU HB2 H 1.27 0.02 2 323 . 47 LEU HD1 H 0.31 0.02 2 324 . 47 LEU C C 176.12 0.50 1 325 . 47 LEU CA C 53.71 0.50 1 326 . 47 LEU CB C 44.09 0.50 1 327 . 47 LEU CD1 C 24.44 0.50 2 328 . 47 LEU N N 118.60 0.30 1 329 . 48 PHE H H 8.67 0.02 1 330 . 48 PHE HA H 5.19 0.02 1 331 . 48 PHE HB2 H 2.74 0.02 2 332 . 48 PHE HB3 H 2.57 0.02 2 333 . 48 PHE C C 175.02 0.50 1 334 . 48 PHE CA C 57.57 0.50 1 335 . 48 PHE CB C 42.98 0.50 1 336 . 48 PHE N N 120.90 0.30 1 337 . 49 PHE H H 8.92 0.02 1 338 . 49 PHE HA H 5.09 0.02 1 339 . 49 PHE HB2 H 2.62 0.02 2 340 . 49 PHE CA C 57.32 0.50 1 341 . 49 PHE CB C 43.24 0.50 1 342 . 49 PHE N N 117.10 0.30 1 343 . 50 SER HA H 4.39 0.02 1 344 . 50 SER HB2 H 3.05 0.02 2 345 . 50 SER HB3 H 3.81 0.02 2 346 . 50 SER C C 173.33 0.50 1 347 . 50 SER CA C 59.59 0.50 1 348 . 50 SER CB C 64.18 0.50 1 349 . 51 GLN H H 8.06 0.02 1 350 . 51 GLN HA H 5.32 0.02 1 351 . 51 GLN HB2 H 2.53 0.02 2 352 . 51 GLN HG2 H 2.73 0.02 2 353 . 51 GLN C C 177.06 0.50 1 354 . 51 GLN CA C 54.80 0.50 1 355 . 51 GLN CB C 32.18 0.50 1 356 . 51 GLN CG C 36.44 0.50 1 357 . 51 GLN N N 121.15 0.30 1 358 . 52 VAL H H 10.46 0.02 1 359 . 52 VAL HA H 3.37 0.02 1 360 . 52 VAL HB H 2.61 0.02 1 361 . 52 VAL HG1 H 1.02 0.02 2 362 . 52 VAL C C 180.22 0.50 1 363 . 52 VAL CA C 67.21 0.50 1 364 . 52 VAL CB C 31.00 0.50 1 365 . 52 VAL CG1 C 23.84 0.50 2 366 . 52 VAL CG2 C 22.27 0.50 2 367 . 52 VAL N N 130.78 0.30 1 368 . 53 ARG H H 10.54 0.02 1 369 . 53 ARG HA H 3.71 0.02 1 370 . 53 ARG HB2 H 2.09 0.02 2 371 . 53 ARG HB3 H 1.84 0.02 4 372 . 53 ARG HG2 H 1.84 0.02 4 373 . 53 ARG HG3 H 1.61 0.02 2 374 . 53 ARG HD2 H 3.20 0.02 2 375 . 53 ARG HD3 H 3.13 0.02 2 376 . 53 ARG C C 176.81 0.50 1 377 . 53 ARG CA C 59.49 0.50 1 378 . 53 ARG CB C 29.88 0.50 1 379 . 53 ARG CG C 26.42 0.50 1 380 . 53 ARG CD C 43.66 0.50 1 381 . 53 ARG N N 119.10 0.30 1 382 . 54 ASP H H 6.81 0.02 1 383 . 54 ASP HA H 4.59 0.02 1 384 . 54 ASP HB2 H 3.23 0.02 2 385 . 54 ASP HB3 H 3.00 0.02 2 386 . 54 ASP C C 177.93 0.50 1 387 . 54 ASP CA C 56.78 0.50 1 388 . 54 ASP CB C 41.07 0.50 1 389 . 54 ASP N N 116.62 0.30 1 390 . 55 ALA H H 7.11 0.02 1 391 . 55 ALA HA H 2.57 0.02 1 392 . 55 ALA HB H 0.90 0.02 1 393 . 55 ALA C C 178.17 0.50 1 394 . 55 ALA CA C 53.87 0.50 1 395 . 55 ALA CB C 19.10 0.50 1 396 . 55 ALA N N 123.98 0.30 1 397 . 56 ILE H H 7.63 0.02 1 398 . 56 ILE HA H 3.25 0.02 1 399 . 56 ILE HB H 1.58 0.02 1 400 . 56 ILE HG2 H 0.57 0.02 1 401 . 56 ILE HD1 H 0.23 0.02 1 402 . 56 ILE C C 176.61 0.50 1 403 . 56 ILE CA C 65.16 0.50 1 404 . 56 ILE CB C 37.12 0.50 1 405 . 56 ILE CG2 C 17.58 0.50 1 406 . 56 ILE CD1 C 12.46 0.50 1 407 . 56 ILE N N 116.27 0.30 1 408 . 57 ALA H H 7.99 0.02 1 409 . 57 ALA HA H 3.70 0.02 1 410 . 57 ALA HB H 1.48 0.02 1 411 . 57 ALA C C 180.70 0.50 1 412 . 57 ALA CA C 55.64 0.50 1 413 . 57 ALA CB C 18.49 0.50 1 414 . 57 ALA N N 120.62 0.30 1 415 . 58 TYR H H 8.24 0.02 1 416 . 58 TYR HA H 3.86 0.02 1 417 . 58 TYR HB2 H 3.11 0.02 2 418 . 58 TYR HB3 H 2.86 0.02 2 419 . 58 TYR C C 178.58 0.50 1 420 . 58 TYR CA C 61.92 0.50 1 421 . 58 TYR CB C 38.27 0.50 1 422 . 58 TYR N N 120.49 0.30 1 423 . 59 ALA H H 7.86 0.02 1 424 . 59 ALA HA H 3.88 0.02 1 425 . 59 ALA HB H 1.37 0.02 1 426 . 59 ALA C C 177.98 0.50 1 427 . 59 ALA CA C 54.10 0.50 1 428 . 59 ALA CB C 18.62 0.50 1 429 . 59 ALA N N 120.55 0.30 1 430 . 60 ARG H H 7.57 0.02 1 431 . 60 ARG HA H 4.31 0.02 1 432 . 60 ARG HB2 H 1.94 0.02 2 433 . 60 ARG HB3 H 1.59 0.02 4 434 . 60 ARG HG2 H 1.58 0.02 4 435 . 60 ARG HD2 H 3.08 0.02 2 436 . 60 ARG HD3 H 2.91 0.02 2 437 . 60 ARG C C 176.79 0.50 1 438 . 60 ARG CA C 55.13 0.50 1 439 . 60 ARG CB C 30.69 0.50 1 440 . 60 ARG CG C 26.81 0.50 1 441 . 60 ARG CD C 43.00 0.50 1 442 . 60 ARG N N 114.88 0.30 1 443 . 61 GLY H H 7.35 0.02 1 444 . 61 GLY HA2 H 4.17 0.02 2 445 . 61 GLY HA3 H 3.82 0.02 2 446 . 61 GLY CA C 44.88 0.50 1 447 . 61 GLY N N 108.32 0.30 1 448 . 62 PRO HA H 4.38 0.02 1 449 . 62 PRO HB2 H 2.19 0.02 2 450 . 62 PRO HB3 H 1.96 0.02 4 451 . 62 PRO HG2 H 1.97 0.02 4 452 . 62 PRO HD2 H 3.63 0.02 2 453 . 62 PRO CA C 63.83 0.50 1 454 . 62 PRO CB C 32.23 0.50 1 455 . 62 PRO CG C 26.96 0.50 1 456 . 62 PRO CD C 49.94 0.50 1 457 . 63 GLU H H 8.09 0.02 1 458 . 63 GLU HA H 4.29 0.02 1 459 . 63 GLU HB2 H 1.91 0.02 2 460 . 63 GLU HG2 H 2.12 0.02 2 461 . 63 GLU C C 175.58 0.50 1 462 . 63 GLU CA C 56.04 0.50 1 463 . 63 GLU CB C 29.60 0.50 1 464 . 63 GLU CG C 36.36 0.50 1 465 . 63 GLU N N 119.72 0.30 1 466 . 64 GLN H H 8.01 0.02 1 467 . 64 GLN HA H 4.26 0.02 1 468 . 64 GLN HB2 H 2.01 0.02 2 469 . 64 GLN HB3 H 1.75 0.02 2 470 . 64 GLN HG2 H 2.16 0.02 2 471 . 64 GLN C C 176.53 0.50 1 472 . 64 GLN CA C 54.75 0.50 1 473 . 64 GLN CB C 29.42 0.50 1 474 . 64 GLN CG C 33.15 0.50 1 475 . 64 GLN N N 122.56 0.30 1 476 . 65 ILE H H 8.22 0.02 1 477 . 65 ILE HA H 4.03 0.02 1 478 . 65 ILE HB H 1.89 0.02 1 479 . 65 ILE HG12 H 1.22 0.02 2 480 . 65 ILE HG2 H 0.92 0.02 1 481 . 65 ILE HD1 H 0.70 0.02 1 482 . 65 ILE C C 175.28 0.50 1 483 . 65 ILE CA C 62.80 0.50 1 484 . 65 ILE CB C 39.06 0.50 1 485 . 65 ILE CG1 C 27.57 0.50 1 486 . 65 ILE CG2 C 17.69 0.50 1 487 . 65 ILE CD1 C 13.47 0.50 1 488 . 65 ILE N N 121.80 0.30 1 489 . 66 ALA H H 7.61 0.02 1 490 . 66 ALA HA H 4.22 0.02 1 491 . 66 ALA HB H 1.41 0.02 1 492 . 66 ALA CA C 50.37 0.50 1 493 . 66 ALA CB C 20.58 0.50 1 494 . 66 ALA N N 122.34 0.30 1 495 . 67 PRO HA H 4.33 0.02 1 496 . 67 PRO HB2 H 2.26 0.02 2 497 . 67 PRO HB3 H 1.74 0.02 2 498 . 67 PRO HG2 H 1.89 0.02 2 499 . 67 PRO HG3 H 2.08 0.02 2 500 . 67 PRO HD2 H 3.80 0.02 2 501 . 67 PRO HD3 H 3.53 0.02 2 502 . 67 PRO C C 175.87 0.50 1 503 . 67 PRO CA C 63.15 0.50 1 504 . 67 PRO CB C 32.31 0.50 1 505 . 67 PRO CG C 27.83 0.50 1 506 . 67 PRO CD C 50.88 0.50 1 507 . 68 ILE H H 8.29 0.02 1 508 . 68 ILE HA H 4.03 0.02 1 509 . 68 ILE HB H 1.74 0.02 1 510 . 68 ILE HG2 H 1.01 0.02 1 511 . 68 ILE HD1 H 0.74 0.02 1 512 . 68 ILE C C 177.22 0.50 1 513 . 68 ILE CA C 62.27 0.50 1 514 . 68 ILE CB C 39.15 0.50 1 515 . 68 ILE CG2 C 17.59 0.50 1 516 . 68 ILE CD1 C 14.31 0.50 1 517 . 68 ILE N N 122.75 0.30 1 518 . 69 LEU H H 9.27 0.02 1 519 . 69 LEU HA H 4.36 0.02 1 520 . 69 LEU HB2 H 1.34 0.02 2 521 . 69 LEU HB3 H 1.46 0.02 2 522 . 69 LEU HG H 1.50 0.02 1 523 . 69 LEU HD1 H 0.79 0.02 2 524 . 69 LEU C C 176.76 0.50 1 525 . 69 LEU CA C 56.29 0.50 1 526 . 69 LEU CB C 43.59 0.50 1 527 . 69 LEU CG C 26.61 0.50 1 528 . 69 LEU CD1 C 26.07 0.50 2 529 . 69 LEU CD2 C 22.78 0.50 2 530 . 69 LEU N N 128.40 0.30 1 531 . 70 VAL H H 7.21 0.02 1 532 . 70 VAL HA H 4.22 0.02 1 533 . 70 VAL HB H 2.11 0.02 1 534 . 70 VAL HG1 H 0.59 0.02 2 535 . 70 VAL HG2 H 0.45 0.02 2 536 . 70 VAL C C 171.06 0.50 1 537 . 70 VAL CA C 61.12 0.50 1 538 . 70 VAL CB C 33.09 0.50 1 539 . 70 VAL CG1 C 20.29 0.50 2 540 . 70 VAL N N 114.57 0.30 1 541 . 71 ILE H H 7.66 0.02 1 542 . 71 ILE HA H 4.83 0.02 1 543 . 71 ILE HB H 1.58 0.02 1 544 . 71 ILE HG12 H 1.57 0.02 2 545 . 71 ILE HG2 H 0.83 0.02 1 546 . 71 ILE HD1 H 0.62 0.02 1 547 . 71 ILE C C 175.17 0.50 1 548 . 71 ILE CA C 59.96 0.50 1 549 . 71 ILE CB C 40.19 0.50 1 550 . 71 ILE CG1 C 19.14 0.50 1 551 . 71 ILE CG2 C 15.50 0.50 1 552 . 71 ILE CD1 C 13.21 0.50 1 553 . 71 ILE N N 124.59 0.30 1 554 . 72 TYR H H 9.37 0.02 1 555 . 72 TYR HA H 5.71 0.02 1 556 . 72 TYR HB2 H 3.19 0.02 2 557 . 72 TYR HB3 H 2.54 0.02 2 558 . 72 TYR C C 175.45 0.50 1 559 . 72 TYR CA C 56.45 0.50 1 560 . 72 TYR CB C 42.77 0.50 1 561 . 72 TYR N N 124.25 0.30 1 562 . 73 VAL H H 9.68 0.02 1 563 . 73 VAL HA H 5.75 0.02 1 564 . 73 VAL HB H 2.33 0.02 1 565 . 73 VAL HG1 H 1.06 0.02 2 566 . 73 VAL HG2 H 0.62 0.02 2 567 . 73 VAL C C 175.50 0.50 1 568 . 73 VAL CA C 58.36 0.50 1 569 . 73 VAL CB C 36.50 0.50 1 570 . 73 VAL CG1 C 23.00 0.50 2 571 . 73 VAL CG2 C 18.94 0.50 2 572 . 73 VAL N N 111.74 0.30 1 573 . 74 ASN H H 7.31 0.02 1 574 . 74 ASN HA H 4.62 0.02 1 575 . 74 ASN HB2 H 2.23 0.02 2 576 . 74 ASN HB3 H 1.92 0.02 2 577 . 74 ASN C C 172.36 0.50 1 578 . 74 ASN CA C 53.89 0.50 1 579 . 74 ASN CB C 42.62 0.50 1 580 . 74 ASN N N 118.74 0.30 1 581 . 75 ASP H H 6.61 0.02 1 582 . 75 ASP HA H 4.16 0.02 1 583 . 75 ASP HB2 H 3.51 0.02 2 584 . 75 ASP HB3 H 2.30 0.02 2 585 . 75 ASP C C 178.17 0.50 1 586 . 75 ASP CA C 52.00 0.50 1 587 . 75 ASP CB C 41.11 0.50 1 588 . 75 ASP N N 112.49 0.30 1 589 . 76 MET H H 8.43 0.02 1 590 . 76 MET HA H 4.47 0.02 1 591 . 76 MET HB2 H 1.82 0.02 2 592 . 76 MET HB3 H 0.91 0.02 2 593 . 76 MET HG2 H 2.26 0.02 2 594 . 76 MET HG3 H 2.15 0.02 2 595 . 76 MET HE H 2.10 0.02 1 596 . 76 MET C C 176.39 0.50 1 597 . 76 MET CA C 54.03 0.50 1 598 . 76 MET CB C 25.95 0.50 1 599 . 76 MET CG C 33.21 0.50 1 600 . 76 MET CE C 19.87 0.50 1 601 . 76 MET N N 124.06 0.30 1 602 . 77 GLY H H 8.35 0.02 1 603 . 77 GLY HA2 H 4.69 0.02 2 604 . 77 GLY HA3 H 4.00 0.02 2 605 . 77 GLY C C 174.13 0.50 1 606 . 77 GLY CA C 44.36 0.50 1 607 . 77 GLY N N 107.73 0.30 1 608 . 78 ALA H H 6.94 0.02 1 609 . 78 ALA HA H 4.14 0.02 1 610 . 78 ALA HB H 1.33 0.02 1 611 . 78 ALA C C 178.11 0.50 1 612 . 78 ALA CA C 52.18 0.50 1 613 . 78 ALA CB C 18.75 0.50 1 614 . 78 ALA N N 124.45 0.30 1 615 . 79 ALA H H 8.59 0.02 1 616 . 79 ALA HA H 4.13 0.02 1 617 . 79 ALA HB H 1.35 0.02 1 618 . 79 ALA C C 179.24 0.50 1 619 . 79 ALA CA C 53.97 0.50 1 620 . 79 ALA CB C 17.87 0.50 1 621 . 79 ALA N N 125.35 0.30 1 622 . 80 GLY H H 8.72 0.02 1 623 . 80 GLY HA2 H 4.11 0.02 2 624 . 80 GLY HA3 H 3.69 0.02 2 625 . 80 GLY C C 173.94 0.50 1 626 . 80 GLY CA C 45.25 0.50 1 627 . 80 GLY N N 111.02 0.30 1 628 . 81 ALA H H 7.71 0.02 1 629 . 81 ALA HA H 4.25 0.02 1 630 . 81 ALA HB H 1.25 0.02 1 631 . 81 ALA C C 177.85 0.50 1 632 . 81 ALA CA C 53.00 0.50 1 633 . 81 ALA CB C 20.30 0.50 1 634 . 81 ALA N N 123.07 0.30 1 635 . 82 THR H H 7.61 0.02 1 636 . 82 THR HA H 4.70 0.02 1 637 . 82 THR HB H 4.60 0.02 1 638 . 82 THR HG2 H 1.19 0.02 1 639 . 82 THR C C 173.60 0.50 1 640 . 82 THR CA C 59.31 0.50 1 641 . 82 THR CB C 72.38 0.50 1 642 . 82 THR CG2 C 21.83 0.50 1 643 . 82 THR N N 113.96 0.30 1 644 . 83 TRP H H 8.75 0.02 1 645 . 83 TRP HA H 3.85 0.02 1 646 . 83 TRP HB2 H 3.36 0.02 2 647 . 83 TRP HB3 H 3.17 0.02 2 648 . 83 TRP C C 176.54 0.50 1 649 . 83 TRP CA C 60.99 0.50 1 650 . 83 TRP CB C 29.52 0.50 1 651 . 83 TRP N N 119.92 0.30 1 652 . 84 ASP H H 7.92 0.02 1 653 . 84 ASP HA H 4.35 0.02 1 654 . 84 ASP HB2 H 2.65 0.02 2 655 . 84 ASP HB3 H 2.52 0.02 2 656 . 84 ASP C C 176.40 0.50 1 657 . 84 ASP CA C 55.91 0.50 1 658 . 84 ASP CB C 41.37 0.50 1 659 . 84 ASP N N 110.86 0.30 1 660 . 85 GLN H H 7.53 0.02 1 661 . 85 GLN HA H 4.55 0.02 1 662 . 85 GLN HB2 H 1.82 0.02 2 663 . 85 GLN HG2 H 2.12 0.02 2 664 . 85 GLN CA C 53.15 0.50 1 665 . 85 GLN CB C 30.01 0.50 1 666 . 85 GLN N N 117.00 0.30 1 667 . 86 PRO HA H 4.07 0.02 1 668 . 86 PRO HB2 H 1.75 0.02 2 669 . 86 PRO HB3 H 1.48 0.02 2 670 . 86 PRO HG2 H 1.43 0.02 4 671 . 86 PRO HD2 H 3.49 0.02 2 672 . 86 PRO HD3 H 3.28 0.02 2 673 . 86 PRO C C 177.44 0.50 1 674 . 86 PRO CA C 65.23 0.50 1 675 . 86 PRO CB C 32.03 0.50 1 676 . 86 PRO CG C 27.96 0.50 1 677 . 86 PRO CD C 49.68 0.50 1 678 . 87 GLY H H 8.02 0.02 1 679 . 87 GLY HA2 H 4.28 0.02 2 680 . 87 GLY HA3 H 3.42 0.02 2 681 . 87 GLY C C 174.64 0.50 1 682 . 87 GLY CA C 43.99 0.50 1 683 . 87 GLY N N 102.95 0.30 1 684 . 88 ASP H H 8.49 0.02 1 685 . 88 ASP HA H 4.40 0.02 1 686 . 88 ASP HB2 H 2.59 0.02 2 687 . 88 ASP HB3 H 2.39 0.02 2 688 . 88 ASP C C 177.94 0.50 1 689 . 88 ASP CA C 55.73 0.50 1 690 . 88 ASP CB C 39.93 0.50 1 691 . 88 ASP N N 126.58 0.30 1 692 . 89 GLY H H 10.51 0.02 1 693 . 89 GLY HA2 H 4.01 0.02 2 694 . 89 GLY HA3 H 4.13 0.02 2 695 . 89 GLY C C 173.96 0.50 1 696 . 89 GLY CA C 45.79 0.50 1 697 . 89 GLY N N 112.97 0.30 1 698 . 90 ASN H H 6.74 0.02 1 699 . 90 ASN HA H 4.53 0.02 1 700 . 90 ASN HB2 H 2.53 0.02 2 701 . 90 ASN HB3 H 2.33 0.02 2 702 . 90 ASN C C 172.95 0.50 1 703 . 90 ASN CA C 51.06 0.50 1 704 . 90 ASN CB C 36.41 0.50 1 705 . 90 ASN N N 118.83 0.30 1 706 . 91 TRP H H 7.27 0.02 1 707 . 91 TRP HA H 5.24 0.02 1 708 . 91 TRP HB2 H 2.71 0.02 2 709 . 91 TRP HB3 H 2.57 0.02 2 710 . 91 TRP C C 175.54 0.50 1 711 . 91 TRP CA C 54.60 0.50 1 712 . 91 TRP CB C 33.98 0.50 1 713 . 91 TRP N N 121.57 0.30 1 714 . 92 ILE H H 9.72 0.02 1 715 . 92 ILE HA H 4.99 0.02 1 716 . 92 ILE HB H 1.99 0.02 1 717 . 92 ILE HG2 H 1.00 0.02 1 718 . 92 ILE HD1 H 0.54 0.02 1 719 . 92 ILE C C 175.15 0.50 1 720 . 92 ILE CA C 59.05 0.50 1 721 . 92 ILE CB C 42.29 0.50 1 722 . 92 ILE CG2 C 18.63 0.50 1 723 . 92 ILE CD1 C 13.84 0.50 1 724 . 92 ILE N N 118.10 0.30 1 725 . 93 ALA H H 9.05 0.02 1 726 . 93 ALA HA H 4.48 0.02 1 727 . 93 ALA HB H 1.43 0.02 1 728 . 93 ALA C C 179.96 0.50 1 729 . 93 ALA CA C 52.83 0.50 1 730 . 93 ALA CB C 18.58 0.50 1 731 . 93 ALA N N 127.12 0.30 1 732 . 94 ALA H H 8.84 0.02 1 733 . 94 ALA HA H 3.98 0.02 1 734 . 94 ALA HB H 1.31 0.02 1 735 . 94 ALA C C 180.59 0.50 1 736 . 94 ALA CA C 54.17 0.50 1 737 . 94 ALA CB C 18.85 0.50 1 738 . 94 ALA N N 123.63 0.30 1 739 . 95 ASP H H 8.85 0.02 1 740 . 95 ASP HA H 4.37 0.02 1 741 . 95 ASP HB2 H 2.79 0.02 2 742 . 95 ASP HB3 H 2.57 0.02 2 743 . 95 ASP C C 176.55 0.50 1 744 . 95 ASP CA C 55.20 0.50 1 745 . 95 ASP CB C 39.24 0.50 1 746 . 95 ASP N N 113.14 0.30 1 747 . 96 LYS H H 7.46 0.02 1 748 . 96 LYS HA H 4.43 0.02 1 749 . 96 LYS HB2 H 2.01 0.02 2 750 . 96 LYS HB3 H 1.77 0.02 2 751 . 96 LYS HG2 H 1.41 0.02 2 752 . 96 LYS HD2 H 1.68 0.02 2 753 . 96 LYS HE2 H 3.02 0.02 2 754 . 96 LYS C C 175.41 0.50 1 755 . 96 LYS CA C 54.76 0.50 1 756 . 96 LYS CB C 32.82 0.50 1 757 . 96 LYS CG C 24.73 0.50 1 758 . 96 LYS CD C 28.59 0.50 1 759 . 96 LYS CE C 42.27 0.50 1 760 . 96 LYS N N 118.32 0.30 1 761 . 97 ALA H H 6.65 0.02 1 762 . 97 ALA HA H 4.27 0.02 1 763 . 97 ALA HB H 0.84 0.02 1 764 . 97 ALA C C 175.06 0.50 1 765 . 97 ALA CA C 51.13 0.50 1 766 . 97 ALA CB C 19.73 0.50 1 767 . 97 ALA N N 121.19 0.30 1 768 . 98 PHE H H 8.82 0.02 1 769 . 98 PHE HA H 4.53 0.02 1 770 . 98 PHE HB2 H 2.69 0.02 2 771 . 98 PHE HB3 H 2.46 0.02 2 772 . 98 PHE C C 174.26 0.50 1 773 . 98 PHE CA C 57.34 0.50 1 774 . 98 PHE CB C 41.41 0.50 1 775 . 98 PHE N N 117.63 0.30 1 776 . 99 TYR H H 9.39 0.02 1 777 . 99 TYR HA H 5.34 0.02 1 778 . 99 TYR HB2 H 2.75 0.02 2 779 . 99 TYR HB3 H 2.24 0.02 2 780 . 99 TYR C C 176.02 0.50 1 781 . 99 TYR CA C 56.38 0.50 1 782 . 99 TYR CB C 41.77 0.50 1 783 . 99 TYR N N 118.70 0.30 1 784 . 100 VAL H H 9.67 0.02 1 785 . 100 VAL HA H 5.19 0.02 1 786 . 100 VAL HB H 2.19 0.02 1 787 . 100 VAL HG1 H 1.18 0.02 2 788 . 100 VAL C C 177.73 0.50 1 789 . 100 VAL CA C 62.06 0.50 1 790 . 100 VAL CB C 32.68 0.50 1 791 . 100 VAL CG1 C 23.27 0.50 2 792 . 100 VAL N N 121.04 0.30 1 793 . 101 VAL H H 8.96 0.02 1 794 . 101 VAL HA H 4.97 0.02 1 795 . 101 VAL HB H 2.05 0.02 1 796 . 101 VAL HG1 H 1.00 0.02 2 797 . 101 VAL C C 176.21 0.50 1 798 . 101 VAL CA C 60.82 0.50 1 799 . 101 VAL CB C 34.71 0.50 1 800 . 101 VAL CG1 C 20.99 0.50 2 801 . 101 VAL N N 128.83 0.30 1 802 . 102 GLY H H 9.93 0.02 1 803 . 102 GLY HA2 H 4.31 0.02 2 804 . 102 GLY HA3 H 3.93 0.02 2 805 . 102 GLY C C 175.51 0.50 1 806 . 102 GLY CA C 45.43 0.50 1 807 . 102 GLY N N 113.62 0.30 1 808 . 103 SER H H 8.79 0.02 1 809 . 103 SER HA H 4.27 0.02 1 810 . 103 SER HB2 H 3.89 0.02 2 811 . 103 SER C C 174.41 0.50 1 812 . 103 SER CA C 58.92 0.50 1 813 . 103 SER CB C 65.65 0.50 1 814 . 103 SER N N 117.85 0.30 1 815 . 104 ALA H H 8.66 0.02 1 816 . 104 ALA HA H 4.23 0.02 1 817 . 104 ALA HB H 1.52 0.02 1 818 . 104 ALA C C 178.31 0.50 1 819 . 104 ALA CA C 53.30 0.50 1 820 . 104 ALA CB C 19.22 0.50 1 821 . 104 ALA N N 119.66 0.30 1 822 . 105 ARG H H 7.76 0.02 1 823 . 105 ARG HA H 4.12 0.02 1 824 . 105 ARG HB2 H 1.48 0.02 2 825 . 105 ARG HG2 H 1.82 0.02 2 826 . 105 ARG HG3 H 1.12 0.02 2 827 . 105 ARG HD3 H 2.27 0.02 2 828 . 105 ARG C C 175.80 0.50 1 829 . 105 ARG CA C 55.34 0.50 1 830 . 105 ARG CB C 30.48 0.50 1 831 . 105 ARG CG C 26.52 0.50 1 832 . 105 ARG CD C 41.57 0.50 1 833 . 105 ARG N N 117.34 0.30 1 834 . 106 ARG H H 8.51 0.02 1 835 . 106 ARG HA H 4.56 0.02 1 836 . 106 ARG HB2 H 1.83 0.02 2 837 . 106 ARG HB3 H 1.54 0.02 2 838 . 106 ARG HG2 H 1.64 0.02 2 839 . 106 ARG HG3 H 1.50 0.02 2 840 . 106 ARG HD2 H 3.04 0.02 2 841 . 106 ARG C C 176.90 0.50 1 842 . 106 ARG CA C 54.20 0.50 1 843 . 106 ARG CB C 31.74 0.50 1 844 . 106 ARG CG C 27.61 0.50 1 845 . 106 ARG CD C 42.67 0.50 1 846 . 106 ARG N N 123.84 0.30 1 847 . 107 GLY H H 8.98 0.02 1 848 . 107 GLY HA2 H 4.64 0.02 2 849 . 107 GLY HA3 H 3.95 0.02 2 850 . 107 GLY C C 176.77 0.50 1 851 . 107 GLY CA C 44.31 0.50 1 852 . 107 GLY N N 105.08 0.30 1 853 . 108 GLY H H 9.71 0.02 1 854 . 108 GLY HA2 H 4.22 0.02 2 855 . 108 GLY HA3 H 4.03 0.02 2 856 . 108 GLY C C 175.00 0.50 1 857 . 108 GLY CA C 48.48 0.50 1 858 . 108 GLY N N 108.50 0.30 1 859 . 109 MET H H 8.32 0.02 1 860 . 109 MET HA H 4.88 0.02 1 861 . 109 MET HB2 H 1.85 0.02 2 862 . 109 MET HG2 H 2.31 0.02 2 863 . 109 MET HG3 H 2.72 0.02 2 864 . 109 MET C C 177.48 0.50 1 865 . 109 MET CA C 53.64 0.50 1 866 . 109 MET CB C 32.12 0.50 1 867 . 109 MET CG C 32.70 0.50 1 868 . 109 MET N N 115.96 0.30 1 869 . 110 GLY H H 8.45 0.02 1 870 . 110 GLY HA2 H 4.35 0.02 2 871 . 110 GLY HA3 H 3.71 0.02 2 872 . 110 GLY C C 173.67 0.50 1 873 . 110 GLY CA C 45.62 0.50 1 874 . 110 GLY N N 108.10 0.30 1 875 . 111 ALA H H 7.88 0.02 1 876 . 111 ALA HA H 4.92 0.02 1 877 . 111 ALA HB H 1.40 0.02 1 878 . 111 ALA CA C 50.34 0.50 1 879 . 111 ALA CB C 16.43 0.50 1 880 . 111 ALA N N 123.84 0.30 1 881 . 112 PRO HA H 4.42 0.02 1 882 . 112 PRO HB2 H 2.52 0.02 2 883 . 112 PRO HB3 H 1.88 0.02 2 884 . 112 PRO HG2 H 2.18 0.02 2 885 . 112 PRO HD2 H 3.90 0.02 2 886 . 112 PRO C C 175.31 0.50 1 887 . 112 PRO CA C 64.76 0.50 1 888 . 112 PRO CB C 31.80 0.50 1 889 . 112 PRO CG C 28.32 0.50 1 890 . 112 PRO CD C 50.84 0.50 1 891 . 113 GLU H H 8.77 0.02 1 892 . 113 GLU HA H 5.66 0.02 1 893 . 113 GLU HB2 H 2.06 0.02 2 894 . 113 GLU HB3 H 1.82 0.02 2 895 . 113 GLU HG2 H 2.27 0.02 2 896 . 113 GLU C C 174.93 0.50 1 897 . 113 GLU CA C 52.74 0.50 1 898 . 113 GLU CB C 34.77 0.50 1 899 . 113 GLU CG C 37.06 0.50 1 900 . 113 GLU N N 125.30 0.30 1 901 . 114 ALA H H 10.08 0.02 1 902 . 114 ALA HA H 4.95 0.02 1 903 . 114 ALA HB H 1.01 0.02 1 904 . 114 ALA C C 174.50 0.50 1 905 . 114 ALA CA C 49.67 0.50 1 906 . 114 ALA CB C 18.63 0.50 1 907 . 114 ALA N N 132.32 0.30 1 908 . 115 VAL H H 8.71 0.02 1 909 . 115 VAL HA H 3.99 0.02 1 910 . 115 VAL HB H 2.20 0.02 1 911 . 115 VAL HG1 H 0.90 0.02 2 912 . 115 VAL CA C 61.06 0.50 1 913 . 115 VAL CB C 33.23 0.50 1 914 . 115 VAL N N 123.57 0.30 1 915 . 116 PRO HA H 4.79 0.02 1 916 . 116 PRO HB2 H 1.87 0.02 2 917 . 116 PRO HB3 H 1.63 0.02 2 918 . 116 PRO HG2 H 2.43 0.02 2 919 . 116 PRO HG3 H 1.83 0.02 2 920 . 116 PRO HD2 H 3.28 0.02 2 921 . 116 PRO C C 175.80 0.50 1 922 . 116 PRO CA C 61.58 0.50 1 923 . 116 PRO CB C 33.20 0.50 1 924 . 116 PRO CG C 28.99 0.50 1 925 . 116 PRO CD C 51.05 0.50 1 926 . 117 PHE H H 8.84 0.02 1 927 . 117 PHE HA H 4.84 0.02 1 928 . 117 PHE HB2 H 3.35 0.02 2 929 . 117 PHE HB3 H 2.49 0.02 2 930 . 117 PHE C C 175.91 0.50 1 931 . 117 PHE CA C 57.29 0.50 1 932 . 117 PHE CB C 44.53 0.50 1 933 . 117 PHE N N 115.89 0.30 1 934 . 118 SER H H 8.28 0.02 1 935 . 118 SER HA H 4.40 0.02 1 936 . 118 SER HB2 H 3.80 0.02 2 937 . 118 SER C C 175.26 0.50 1 938 . 118 SER CA C 59.88 0.50 1 939 . 118 SER CB C 63.64 0.50 1 940 . 118 SER N N 116.04 0.30 1 941 . 119 SER H H 8.17 0.02 1 942 . 119 SER HA H 4.97 0.02 1 943 . 119 SER HB2 H 4.07 0.02 2 944 . 119 SER HB3 H 3.85 0.02 2 945 . 119 SER C C 175.21 0.50 1 946 . 119 SER CA C 55.35 0.50 1 947 . 119 SER CB C 64.47 0.50 1 948 . 119 SER N N 115.82 0.30 1 949 . 120 ARG H H 8.84 0.02 1 950 . 120 ARG HA H 3.05 0.02 1 951 . 120 ARG HB2 H 1.19 0.02 2 952 . 120 ARG HB3 H 0.86 0.02 2 953 . 120 ARG HG2 H 1.61 0.02 2 954 . 120 ARG HG3 H 1.45 0.02 2 955 . 120 ARG HD2 H 2.81 0.02 2 956 . 120 ARG C C 177.72 0.50 1 957 . 120 ARG CA C 59.02 0.50 1 958 . 120 ARG CB C 29.18 0.50 1 959 . 120 ARG CG C 27.53 0.50 1 960 . 120 ARG CD C 42.89 0.50 1 961 . 120 ARG N N 129.59 0.30 1 962 . 121 ASP H H 7.89 0.02 1 963 . 121 ASP HA H 4.25 0.02 1 964 . 121 ASP HB2 H 2.57 0.02 2 965 . 121 ASP HB3 H 2.38 0.02 2 966 . 121 ASP C C 179.27 0.50 1 967 . 121 ASP CA C 57.11 0.50 1 968 . 121 ASP CB C 40.20 0.50 1 969 . 121 ASP N N 117.93 0.30 1 970 . 122 GLU H H 7.43 0.02 1 971 . 122 GLU HA H 4.06 0.02 1 972 . 122 GLU HB2 H 2.14 0.02 2 973 . 122 GLU HG2 H 2.53 0.02 2 974 . 122 GLU HG3 H 2.35 0.02 2 975 . 122 GLU C C 178.79 0.50 1 976 . 122 GLU CA C 58.29 0.50 1 977 . 122 GLU CB C 29.10 0.50 1 978 . 122 GLU CG C 35.83 0.50 1 979 . 122 GLU N N 121.02 0.30 1 980 . 123 ALA H H 7.34 0.02 1 981 . 123 ALA HA H 4.01 0.02 1 982 . 123 ALA HB H 1.03 0.02 1 983 . 123 ALA C C 178.35 0.50 1 984 . 123 ALA CA C 54.18 0.50 1 985 . 123 ALA CB C 18.16 0.50 1 986 . 123 ALA N N 123.76 0.30 1 987 . 124 ALA H H 8.11 0.02 1 988 . 124 ALA HA H 3.77 0.02 1 989 . 124 ALA HB H 1.38 0.02 1 990 . 124 ALA C C 180.53 0.50 1 991 . 124 ALA CA C 54.90 0.50 1 992 . 124 ALA CB C 17.84 0.50 1 993 . 124 ALA N N 118.95 0.30 1 994 . 125 ALA H H 7.51 0.02 1 995 . 125 ALA HA H 4.03 0.02 1 996 . 125 ALA HB H 1.46 0.02 1 997 . 125 ALA C C 180.11 0.50 1 998 . 125 ALA CA C 55.05 0.50 1 999 . 125 ALA CB C 17.73 0.50 1 1000 . 125 ALA N N 121.44 0.30 1 1001 . 126 PHE H H 7.62 0.02 1 1002 . 126 PHE HA H 4.72 0.02 1 1003 . 126 PHE HB2 H 3.08 0.02 2 1004 . 126 PHE CA C 61.57 0.50 1 1005 . 126 PHE CB C 39.97 0.50 1 1006 . 126 PHE N N 122.79 0.30 1 1007 . 127 VAL H H 8.80 0.02 1 1008 . 127 VAL HA H 3.88 0.02 1 1009 . 127 VAL HB H 2.06 0.02 1 1010 . 127 VAL HG1 H 0.92 0.02 2 1011 . 127 VAL HG2 H 0.70 0.02 2 1012 . 127 VAL C C 179.92 0.50 1 1013 . 127 VAL CA C 64.71 0.50 1 1014 . 127 VAL CB C 31.65 0.50 1 1015 . 127 VAL CG1 C 24.70 0.50 2 1016 . 127 VAL CG2 C 21.74 0.50 2 1017 . 127 VAL N N 120.56 0.30 1 1018 . 128 LEU H H 7.59 0.02 1 1019 . 128 LEU HA H 3.94 0.02 1 1020 . 128 LEU HB2 H 1.80 0.02 2 1021 . 128 LEU HB3 H 1.57 0.02 2 1022 . 128 LEU HG H 1.76 0.02 1 1023 . 128 LEU HD1 H 0.86 0.02 1 1024 . 128 LEU C C 177.98 0.50 1 1025 . 128 LEU CA C 57.88 0.50 1 1026 . 128 LEU CB C 41.54 0.50 1 1027 . 128 LEU CG C 26.59 0.50 1 1028 . 128 LEU CD1 C 24.82 0.50 2 1029 . 128 LEU CD2 C 23.37 0.50 2 1030 . 128 LEU N N 120.62 0.30 1 1031 . 129 ALA H H 7.03 0.02 1 1032 . 129 ALA HA H 4.26 0.02 1 1033 . 129 ALA HB H 1.36 0.02 1 1034 . 129 ALA C C 179.45 0.50 1 1035 . 129 ALA CA C 54.10 0.50 1 1036 . 129 ALA CB C 20.28 0.50 1 1037 . 129 ALA N N 118.35 0.30 1 1038 . 130 GLU H H 8.42 0.02 1 1039 . 130 GLU HA H 4.56 0.02 1 1040 . 130 GLU HB2 H 1.96 0.02 2 1041 . 130 GLU HB3 H 0.89 0.02 2 1042 . 130 GLU HG2 H 1.50 0.02 2 1043 . 130 GLU HG3 H 1.08 0.02 2 1044 . 130 GLU C C 177.80 0.50 1 1045 . 130 GLU CA C 55.68 0.50 1 1046 . 130 GLU CB C 31.44 0.50 1 1047 . 130 GLU CG C 33.55 0.50 1 1048 . 130 GLU N N 114.08 0.30 1 1049 . 131 GLY H H 8.67 0.02 1 1050 . 131 GLY HA2 H 4.28 0.02 2 1051 . 131 GLY HA3 H 3.71 0.02 2 1052 . 131 GLY C C 171.16 0.50 1 1053 . 131 GLY CA C 44.10 0.50 1 1054 . 131 GLY N N 112.25 0.30 1 1055 . 132 GLY H H 7.57 0.02 1 1056 . 132 GLY HA2 H 4.25 0.02 2 1057 . 132 GLY HA3 H 3.53 0.02 2 1058 . 132 GLY C C 173.42 0.50 1 1059 . 132 GLY CA C 43.71 0.50 1 1060 . 132 GLY N N 99.92 0.30 1 1061 . 133 GLN H H 8.59 0.02 1 1062 . 133 GLN HA H 4.76 0.02 1 1063 . 133 GLN HB2 H 1.97 0.02 2 1064 . 133 GLN HG2 H 2.15 0.02 2 1065 . 133 GLN HG3 H 2.33 0.02 2 1066 . 133 GLN C C 173.56 0.50 1 1067 . 133 GLN CA C 54.17 0.50 1 1068 . 133 GLN CB C 32.84 0.50 1 1069 . 133 GLN CG C 33.59 0.50 1 1070 . 133 GLN N N 115.56 0.30 1 1071 . 134 VAL H H 8.49 0.02 1 1072 . 134 VAL HA H 4.81 0.02 1 1073 . 134 VAL HB H 1.97 0.02 1 1074 . 134 VAL HG1 H 0.84 0.02 2 1075 . 134 VAL C C 175.98 0.50 1 1076 . 134 VAL CA C 62.46 0.50 1 1077 . 134 VAL CB C 32.22 0.50 1 1078 . 134 VAL CG1 C 25.82 0.50 2 1079 . 134 VAL CG2 C 22.35 0.50 2 1080 . 134 VAL N N 121.79 0.30 1 1081 . 135 LEU H H 9.89 0.02 1 1082 . 135 LEU HA H 4.98 0.02 1 1083 . 135 LEU HB2 H 1.78 0.02 2 1084 . 135 LEU HG H 1.53 0.02 1 1085 . 135 LEU HD1 H 0.94 0.02 2 1086 . 135 LEU HD2 H 0.83 0.02 2 1087 . 135 LEU C C 176.00 0.50 1 1088 . 135 LEU CA C 54.08 0.50 1 1089 . 135 LEU CB C 46.91 0.50 1 1090 . 135 LEU CG C 27.41 0.50 1 1091 . 135 LEU CD1 C 27.07 0.50 2 1092 . 135 LEU CD2 C 23.75 0.50 2 1093 . 135 LEU N N 130.26 0.30 1 1094 . 136 ALA H H 8.82 0.02 1 1095 . 136 ALA HA H 4.77 0.02 1 1096 . 136 ALA HB H 1.51 0.02 1 1097 . 136 ALA C C 178.41 0.50 1 1098 . 136 ALA CA C 51.11 0.50 1 1099 . 136 ALA CB C 19.77 0.50 1 1100 . 136 ALA N N 123.46 0.30 1 1101 . 137 LEU H H 9.01 0.02 1 1102 . 137 LEU HA H 3.64 0.02 1 1103 . 137 LEU HB2 H 1.72 0.02 2 1104 . 137 LEU HG H 1.41 0.02 1 1105 . 137 LEU HD1 H 0.67 0.02 2 1106 . 137 LEU HD2 H 0.50 0.02 2 1107 . 137 LEU C C 178.97 0.50 1 1108 . 137 LEU CA C 58.58 0.50 1 1109 . 137 LEU CB C 41.60 0.50 1 1110 . 137 LEU CG C 26.56 0.50 1 1111 . 137 LEU CD1 C 25.92 0.50 2 1112 . 137 LEU CD2 C 22.38 0.50 2 1113 . 137 LEU N N 121.67 0.30 1 1114 . 138 ALA H H 8.15 0.02 1 1115 . 138 ALA HA H 3.94 0.02 1 1116 . 138 ALA HB H 1.31 0.02 1 1117 . 138 ALA C C 178.28 0.50 1 1118 . 138 ALA CA C 53.67 0.50 1 1119 . 138 ALA CB C 18.72 0.50 1 1120 . 138 ALA N N 115.07 0.30 1 1121 . 139 ASP H H 7.53 0.02 1 1122 . 139 ASP HA H 4.61 0.02 1 1123 . 139 ASP HB2 H 2.92 0.02 2 1124 . 139 ASP HB3 H 2.81 0.02 2 1125 . 139 ASP C C 175.55 0.50 1 1126 . 139 ASP CA C 54.36 0.50 1 1127 . 139 ASP CB C 43.17 0.50 1 1128 . 139 ASP N N 114.33 0.30 1 1129 . 140 ILE H H 7.36 0.02 1 1130 . 140 ILE HA H 4.07 0.02 1 1131 . 140 ILE HB H 1.77 0.02 1 1132 . 140 ILE HG2 H 0.68 0.02 1 1133 . 140 ILE HD1 H 0.18 0.02 1 1134 . 140 ILE C C 177.05 0.50 1 1135 . 140 ILE CA C 62.19 0.50 1 1136 . 140 ILE CB C 37.55 0.50 1 1137 . 140 ILE CG1 C 28.08 0.50 1 1138 . 140 ILE CG2 C 18.00 0.50 1 1139 . 140 ILE CD1 C 12.78 0.50 1 1140 . 140 ILE N N 120.79 0.30 1 1141 . 141 THR H H 8.12 0.02 1 1142 . 141 THR HA H 4.39 0.02 1 1143 . 141 THR HB H 4.40 0.02 1 1144 . 141 THR HG2 H 1.26 0.02 1 1145 . 141 THR C C 175.53 0.50 1 1146 . 141 THR CA C 60.65 0.50 1 1147 . 141 THR CB C 70.44 0.50 1 1148 . 141 THR CG2 C 22.10 0.50 1 1149 . 141 THR N N 122.07 0.30 1 1150 . 142 ASP H H 8.64 0.02 1 1151 . 142 ASP HA H 4.12 0.02 1 1152 . 142 ASP HB2 H 2.64 0.02 2 1153 . 142 ASP HB3 H 2.57 0.02 2 1154 . 142 ASP C C 178.12 0.50 1 1155 . 142 ASP CA C 57.38 0.50 1 1156 . 142 ASP CB C 39.50 0.50 1 1157 . 142 ASP N N 120.95 0.30 1 1158 . 143 ALA H H 8.11 0.02 1 1159 . 143 ALA HA H 4.06 0.02 1 1160 . 143 ALA HB H 1.35 0.02 1 1161 . 143 ALA C C 177.98 0.50 1 1162 . 143 ALA CA C 54.32 0.50 1 1163 . 143 ALA CB C 18.57 0.50 1 1164 . 143 ALA N N 119.66 0.30 1 1165 . 144 MET H H 7.55 0.02 1 1166 . 144 MET HA H 4.08 0.02 1 1167 . 144 MET HB2 H 2.24 0.02 2 1168 . 144 MET HB3 H 1.89 0.02 2 1169 . 144 MET HG2 H 2.77 0.02 2 1170 . 144 MET HG3 H 2.55 0.02 2 1171 . 144 MET C C 177.26 0.50 1 1172 . 144 MET CA C 58.12 0.50 1 1173 . 144 MET CB C 33.22 0.50 1 1174 . 144 MET CG C 33.40 0.50 1 1175 . 144 MET N N 114.92 0.30 1 1176 . 145 VAL H H 7.23 0.02 1 1177 . 145 VAL HA H 4.35 0.02 1 1178 . 145 VAL HB H 2.32 0.02 1 1179 . 145 VAL HG1 H 0.70 0.02 2 1180 . 145 VAL CA C 61.49 0.50 1 1181 . 145 VAL CB C 32.84 0.50 1 1182 . 145 VAL CG1 C 21.34 0.50 2 1183 . 145 VAL CG2 C 18.65 0.50 2 1184 . 145 VAL N N 108.66 0.30 1 1185 . 146 LEU H H 7.95 0.02 1 1186 . 146 LEU HA H 4.41 0.02 1 1187 . 146 LEU HB2 H 1.61 0.02 2 1188 . 146 LEU HB3 H 1.47 0.02 2 1189 . 146 LEU HG H 1.83 0.02 1 1190 . 146 LEU HD1 H 0.80 0.02 2 1191 . 146 LEU C C 177.25 0.50 1 1192 . 146 LEU CA C 54.82 0.50 1 1193 . 146 LEU CB C 42.71 0.50 1 1194 . 146 LEU CG C 26.91 0.50 1 1195 . 146 LEU CD1 C 25.22 0.50 2 1196 . 146 LEU CD2 C 23.33 0.50 2 1197 . 146 LEU N N 120.48 0.30 1 1198 . 147 THR H H 7.91 0.02 1 1199 . 147 THR HA H 4.45 0.02 1 1200 . 147 THR HB H 4.01 0.02 1 1201 . 147 THR HG2 H 1.21 0.02 1 1202 . 147 THR CA C 60.57 0.50 1 1203 . 147 THR CB C 69.97 0.50 1 1204 . 147 THR N N 117.67 0.30 1 1205 . 148 PRO HA H 4.42 0.02 1 1206 . 148 PRO HB2 H 2.27 0.02 2 1207 . 148 PRO HB3 H 1.87 0.02 2 1208 . 148 PRO HG2 H 2.01 0.02 2 1209 . 148 PRO HG3 H 1.95 0.02 2 1210 . 148 PRO HD2 H 3.67 0.02 2 1211 . 148 PRO HD3 H 3.84 0.02 2 1212 . 148 PRO C C 176.77 0.50 1 1213 . 148 PRO CA C 63.10 0.50 1 1214 . 148 PRO CB C 32.20 0.50 1 1215 . 148 PRO CG C 27.44 0.50 1 1216 . 148 PRO CD C 51.08 0.50 1 1217 . 149 VAL H H 8.17 0.02 1 1218 . 149 VAL HA H 4.04 0.02 1 1219 . 149 VAL HB H 2.02 0.02 1 1220 . 149 VAL HG1 H 0.92 0.02 2 1221 . 149 VAL C C 176.22 0.50 1 1222 . 149 VAL CA C 62.50 0.50 1 1223 . 149 VAL CB C 32.87 0.50 1 1224 . 149 VAL CG1 C 23.95 0.50 2 1225 . 149 VAL CG2 C 21.06 0.50 2 1226 . 149 VAL N N 120.32 0.30 1 1227 . 150 GLU H H 8.47 0.02 1 1228 . 150 GLU HA H 4.38 0.02 1 1229 . 150 GLU HB2 H 2.05 0.02 2 1230 . 150 GLU HB3 H 1.92 0.02 2 1231 . 150 GLU HG2 H 2.23 0.02 2 1232 . 150 GLU C C 176.67 0.50 1 1233 . 150 GLU CA C 56.34 0.50 1 1234 . 150 GLU CB C 30.31 0.50 1 1235 . 150 GLU CG C 36.29 0.50 1 1236 . 150 GLU N N 124.72 0.30 1 1237 . 151 THR H H 8.28 0.02 1 1238 . 151 THR HA H 4.36 0.02 1 1239 . 151 THR HB H 4.22 0.02 1 1240 . 151 THR HG2 H 1.19 0.02 1 1241 . 151 THR C C 175.31 0.50 1 1242 . 151 THR CA C 62.09 0.50 1 1243 . 151 THR CB C 69.61 0.50 1 1244 . 151 THR CG2 C 21.60 0.50 1 1245 . 151 THR N N 115.55 0.30 1 1246 . 152 GLY H H 8.51 0.02 1 1247 . 152 GLY HA2 H 4.02 0.02 2 1248 . 152 GLY C C 174.18 0.50 1 1249 . 152 GLY CA C 45.41 0.50 1 1250 . 152 GLY N N 111.66 0.30 1 1251 . 153 SER H H 8.15 0.02 1 1252 . 153 SER HA H 4.47 0.02 1 1253 . 153 SER HB2 H 3.82 0.02 2 1254 . 153 SER C C 174.44 0.50 1 1255 . 153 SER CA C 58.13 0.50 1 1256 . 153 SER CB C 64.08 0.50 1 1257 . 153 SER N N 115.42 0.30 1 1258 . 154 GLU H H 8.37 0.02 1 1259 . 154 GLU HA H 4.82 0.02 1 1260 . 154 GLU HB2 H 1.90 0.02 2 1261 . 154 GLU HG2 H 2.28 0.02 2 1262 . 154 GLU CA C 54.77 0.50 1 1263 . 154 GLU CB C 29.60 0.50 1 1264 . 154 GLU N N 123.72 0.30 1 1265 . 155 PRO HA H 4.38 0.02 1 1266 . 155 PRO HB2 H 2.23 0.02 2 1267 . 155 PRO HB3 H 1.84 0.02 2 1268 . 155 PRO HG2 H 1.98 0.02 2 1269 . 155 PRO HD2 H 3.78 0.02 2 1270 . 155 PRO HD3 H 3.65 0.02 2 1271 . 155 PRO C C 176.70 0.50 1 1272 . 155 PRO CA C 63.16 0.50 1 1273 . 155 PRO CB C 32.08 0.50 1 1274 . 155 PRO CG C 27.47 0.50 1 1275 . 155 PRO CD C 50.59 0.50 1 1276 . 156 ARG H H 8.41 0.02 1 1277 . 156 ARG HA H 4.32 0.02 1 1278 . 156 ARG HB2 H 1.82 0.02 2 1279 . 156 ARG HB3 H 1.74 0.02 2 1280 . 156 ARG HG2 H 1.64 0.02 2 1281 . 156 ARG HG3 H 1.80 0.02 2 1282 . 156 ARG HD2 H 3.17 0.02 2 1283 . 156 ARG C C 176.20 0.50 1 1284 . 156 ARG CA C 55.68 0.50 1 1285 . 156 ARG CB C 31.38 0.50 1 1286 . 156 ARG CG C 27.10 0.50 1 1287 . 156 ARG CD C 43.34 0.50 1 1288 . 156 ARG N N 121.75 0.30 1 1289 . 157 ALA H H 8.41 0.02 1 1290 . 157 ALA HA H 4.24 0.02 1 1291 . 157 ALA HB H 1.36 0.02 1 1292 . 157 ALA C C 177.49 0.50 1 1293 . 157 ALA CA C 52.75 0.50 1 1294 . 157 ALA CB C 19.31 0.50 1 1295 . 157 ALA N N 125.69 0.30 1 1296 . 158 ASP H H 8.26 0.02 1 1297 . 158 ASP HA H 4.55 0.02 1 1298 . 158 ASP HB2 H 2.65 0.02 2 1299 . 158 ASP CA C 54.30 0.50 1 1300 . 158 ASP CB C 40.92 0.50 1 1301 . 158 ASP N N 118.58 0.30 1 1302 . 159 ASP H H 8.07 0.02 1 1303 . 159 ASP HA H 4.57 0.02 1 1304 . 159 ASP HB2 H 2.68 0.02 2 1305 . 159 ASP C C 176.65 0.50 1 1306 . 159 ASP CA C 54.55 0.50 1 1307 . 159 ASP CB C 41.15 0.50 1 1308 . 159 ASP N N 120.05 0.30 1 1309 . 160 GLU H H 8.31 0.02 1 1310 . 160 GLU HA H 4.16 0.02 1 1311 . 160 GLU HB2 H 1.96 0.02 2 1312 . 160 GLU HG2 H 2.23 0.02 2 1313 . 160 GLU C C 177.10 0.50 1 1314 . 160 GLU CA C 57.37 0.50 1 1315 . 160 GLU CB C 30.11 0.50 1 1316 . 160 GLU CG C 36.36 0.50 1 1317 . 160 GLU N N 120.98 0.30 1 1318 . 161 ASP H H 8.31 0.02 1 1319 . 161 ASP HA H 4.55 0.02 1 1320 . 161 ASP HB2 H 2.65 0.02 2 1321 . 161 ASP C C 176.98 0.50 1 1322 . 161 ASP CA C 54.74 0.50 1 1323 . 161 ASP CB C 40.95 0.50 1 1324 . 161 ASP N N 120.82 0.30 1 1325 . 162 TYR H H 8.01 0.02 1 1326 . 162 TYR HA H 4.29 0.02 1 1327 . 162 TYR HB2 H 3.08 0.02 2 1328 . 162 TYR CA C 59.50 0.50 1 1329 . 162 TYR CB C 38.38 0.50 1 1330 . 162 TYR N N 121.08 0.30 1 1331 . 163 LEU H H 8.06 0.02 1 1332 . 163 LEU HA H 4.12 0.02 1 1333 . 163 LEU HB2 H 1.64 0.02 2 1334 . 163 LEU HB3 H 1.49 0.02 2 1335 . 163 LEU HG H 1.46 0.02 1 1336 . 163 LEU HD1 H 0.84 0.02 2 1337 . 163 LEU C C 178.49 0.50 1 1338 . 163 LEU CA C 56.34 0.50 1 1339 . 163 LEU CB C 41.70 0.50 1 1340 . 163 LEU CG C 26.83 0.50 1 1341 . 163 LEU CD1 C 24.97 0.50 2 1342 . 163 LEU CD2 C 23.27 0.50 2 1343 . 163 LEU N N 120.56 0.30 1 1344 . 164 GLY H H 8.02 0.02 1 1345 . 164 GLY HA2 H 3.85 0.02 2 1346 . 164 GLY C C 175.47 0.50 1 1347 . 164 GLY CA C 46.28 0.50 1 1348 . 164 GLY N N 107.92 0.30 1 1349 . 165 ARG H H 7.84 0.02 1 1350 . 165 ARG HA H 4.20 0.02 1 1351 . 165 ARG HB2 H 1.80 0.02 2 1352 . 165 ARG HG2 H 1.60 0.02 2 1353 . 165 ARG HD2 H 3.15 0.02 2 1354 . 165 ARG CA C 57.20 0.50 1 1355 . 165 ARG CB C 30.56 0.50 1 1356 . 165 ARG CG C 27.47 0.50 1 1357 . 165 ARG CD C 43.49 0.50 1 1358 . 165 ARG N N 120.24 0.30 1 1359 . 166 LEU H H 7.95 0.02 1 1360 . 166 LEU HA H 4.21 0.02 1 1361 . 166 LEU HB2 H 1.60 0.02 2 1362 . 166 LEU HD1 H 0.82 0.02 2 1363 . 166 LEU C C 177.89 0.50 1 1364 . 166 LEU CA C 55.81 0.50 1 1365 . 166 LEU CB C 42.09 0.50 1 1366 . 166 LEU CG C 26.92 0.50 1 1367 . 166 LEU CD1 C 24.93 0.50 2 1368 . 166 LEU CD2 C 23.34 0.50 2 1369 . 166 LEU N N 120.99 0.30 1 1370 . 167 ARG H H 7.92 0.02 1 1371 . 167 ARG HA H 4.24 0.02 1 1372 . 167 ARG HB2 H 1.79 0.02 2 1373 . 167 ARG HG2 H 1.61 0.02 2 1374 . 167 ARG HD2 H 3.14 0.02 2 1375 . 167 ARG C C 175.85 0.50 1 1376 . 167 ARG CA C 56.35 0.50 1 1377 . 167 ARG CB C 30.75 0.50 1 1378 . 167 ARG CG C 27.41 0.50 1 1379 . 167 ARG CD C 43.42 0.50 1 1380 . 167 ARG N N 119.92 0.30 1 1381 . 168 ALA H H 7.88 0.02 1 1382 . 168 ALA HA H 4.30 0.02 1 1383 . 168 ALA HB H 1.34 0.02 1 1384 . 168 ALA C C 177.21 0.50 1 1385 . 168 ALA CA C 52.12 0.50 1 1386 . 168 ALA CB C 19.35 0.50 1 1387 . 168 ALA N N 123.59 0.30 1 1388 . 169 LEU H H 7.95 0.02 1 1389 . 169 LEU HA H 4.52 0.02 1 1390 . 169 LEU HB2 H 1.80 0.02 2 1391 . 169 LEU HB3 H 1.55 0.02 2 1392 . 169 LEU CA C 53.29 0.50 1 1393 . 169 LEU CB C 41.81 0.50 1 1394 . 169 LEU N N 122.56 0.30 1 1395 . 170 PRO HA H 4.36 0.02 1 1396 . 170 PRO HB2 H 2.20 0.02 2 1397 . 170 PRO HB3 H 1.77 0.02 2 1398 . 170 PRO HG2 H 1.97 0.02 2 1399 . 170 PRO HD2 H 3.79 0.02 2 1400 . 170 PRO HD3 H 3.58 0.02 2 1401 . 170 PRO C C 176.38 0.50 1 1402 . 170 PRO CA C 63.06 0.50 1 1403 . 170 PRO CB C 32.02 0.50 1 1404 . 170 PRO CG C 27.41 0.50 1 1405 . 170 PRO CD C 50.46 0.50 1 1406 . 171 HIS H H 8.32 0.02 1 1407 . 171 HIS HA H 4.91 0.02 1 1408 . 171 HIS HB2 H 4.48 0.02 2 1409 . 171 HIS HB3 H 3.12 0.02 2 1410 . 171 HIS CA C 53.69 0.50 1 1411 . 171 HIS CB C 29.49 0.50 1 1412 . 171 HIS N N 119.77 0.30 1 1413 . 172 PRO HA H 4.39 0.02 1 1414 . 172 PRO HB2 H 2.26 0.02 2 1415 . 172 PRO HB3 H 1.91 0.02 2 1416 . 172 PRO HG2 H 1.73 0.02 2 1417 . 172 PRO HG3 H 1.94 0.02 2 1418 . 172 PRO HD2 H 3.45 0.02 2 1419 . 172 PRO HD3 H 3.71 0.02 2 1420 . 172 PRO C C 176.82 0.50 1 1421 . 172 PRO CA C 63.24 0.50 1 1422 . 172 PRO CB C 32.13 0.50 1 1423 . 172 PRO CG C 27.43 0.50 1 1424 . 172 PRO CD C 50.57 0.50 1 1425 . 173 ALA H H 8.56 0.02 1 1426 . 173 ALA HA H 4.33 0.02 1 1427 . 173 ALA HB H 1.40 0.02 1 1428 . 173 ALA C C 178.34 0.50 1 1429 . 173 ALA CA C 52.90 0.50 1 1430 . 173 ALA CB C 19.18 0.50 1 1431 . 173 ALA N N 124.90 0.30 1 1432 . 174 GLY H H 8.34 0.02 1 1433 . 174 GLY HA2 H 3.95 0.02 2 1434 . 174 GLY C C 173.73 0.50 1 1435 . 174 GLY CA C 45.34 0.50 1 1436 . 174 GLY N N 108.84 0.30 1 1437 . 175 GLY H H 7.86 0.02 1 1438 . 175 GLY HA2 H 3.75 0.02 2 1439 . 175 GLY CA C 45.94 0.50 1 1440 . 175 GLY N N 115.10 0.30 1 stop_ save_