data_4376 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments, 3JHNHA coupling constants, secondary structure and 15N{1H} Heteronuclear NOE values of the N-domain of VAT (VCP like ATPase of Thermoplasma). A group II AAA ATPase. ; _BMRB_accession_number 4376 _BMRB_flat_file_name bmr4376.str _Entry_type original _Submission_date 1999-08-13 _Accession_date 1999-08-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data presented are for VAT-N, the N-domain of VAT (VCP like ATPase of Thermoplasma),a member of the AAA family of ATPases. VAT is assigned to the group II sub-branch of the family as it contains two AAA ATPase domains. These are preceeded by the N-domain, which is responsible for substrate binding. In general, the AAA proteins are responsible for the disassembly and/or disassociation of protein complexes. VAT is able to assist both unfolding an refolding of proteins, while the N-domain alone is able to assist refolding of permissive substrates. This is the first structure of a domain of a AAA protein solved by NMR methods. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Coles Murray . . 2 Diercks Tammo . . 3 Liermann Jens . . 4 Groeger Adriane . . 5 Rockel Beate . . 6 Baumeister Wolfgang . . 7 Koretke Kirstin K . 8 Lupas Andrei . . 9 Peters Juergen . . 10 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1077 "13C chemical shifts" 785 "15N chemical shifts" 183 "coupling constants" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-13 original author . stop_ _Original_release_date 1999-10-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Coles, M., Diercks, T., Liermann, J., Groeger, A., Rockel, B., Baumeister, W., Koretke, K.K., Lupas, A., Peters, J., Kessler, H., "The Solution Structure of VAT-N Reveals a 'Missing Link' in the Evolution of Complex Enzymes from a Simple babb Element." Current Biology 1999, 9:1158-1168. ; _Citation_title ; The Solution Strucutre of VAT-N Reveals a Missing Link in the Evolution of Complex Enzymes from a Simple bbab Element. ; _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 Coles Murray . . 2 Diercks Tammo . . 3 Liermann Jens . . 4 Groeger Adriane . . 5 Rockel Beate . . 6 Baumeister Wolfgang . . 7 Koretke Kirstin K . 8 Lupas Andrei . . 9 Peters Juergen . . 10 Kessler Horst . . stop_ _Journal_abbreviation 'Current Biology' _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1158 _Page_last 1168 _Year 1999 _Details . loop_ _Keyword 'AAA ATPaseN-domain' 'coupling constants' NMR protein 'resonance assignment' 'secondary structure' VAT-N stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Golbik, R., Lupas, A., Koretke, K.K., Peters, J., Baumeister, W. The Janus Face of the Archaeal Cdc48/p97 Homologue VAT: Protein Folding versus Unfolding. Biological Chemistry 1999, 380:1049-1062. ; _Citation_title 'The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10543442 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Golbik R . . 2 Lupas 'A N' N. . 3 Koretke 'K K' K. . 4 Baumeister W . . 5 Peters J . . stop_ _Journal_abbreviation 'Biol. Chem.' _Journal_name_full 'Biological chemistry' _Journal_volume 380 _Journal_issue 9 _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 1049 _Page_last 1062 _Year 1999 _Details ; Members of the AAA family of ATPases have been implicated in chaperone-like activities. We used the archaeal Cdc48/p97 homologue VAT as a model system to investigate the effect of an AAA protein on the folding and unfolding of two well-studied, heterologous substrates, cyclophilin and penicillinase. We found that, depending on the Mg2+ concentration, VAT assumes two states with maximum rates of ATP hydrolysis that differ by an order of magnitude. In the low-activity state, VAT accelerated the refolding of penicillinase, whereas in the high-activity state, it accelerated its unfolding. Both reactions were ATP-dependent. In its interaction with cyclophilin, VAT was ATP-independent and only promoted refolding. The N-terminal domain of VAT, which lacks ATPase activity, also accelerated the refolding of cyclophilin but showed no effect on penicillinase. VAT appears to be structurally equivalent over its entire length to Sec18/NSF, suggesting that these results apply more broadly to group II AAA proteins. ; save_ save_citation_2 _Saveframe_category citation _Citation_full ; Pamnani, V., Tamura T., Lupas, A., Peters, J.,Cejka, Z., Ashraf, W. & Baumeister, W. FEBS Lett. 404 263-268 (1997) ; _Citation_title 'Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9119075 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pamnani V . . 2 Tamura T . . 3 Lupas A . . 4 Peters J . . 5 Cejka Z . . 6 Ashraf W . . 7 Baumeister W . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 404 _Journal_issue 2-3 _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 263 _Page_last 268 _Year 1997 _Details ; A member of the AAA family of Mg2(+)-ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (Mr 83,000), which has an optimal Mg2(+)-ATPase activity at 70 degrees C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings. Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL. ; save_ save_citation_3 _Saveframe_category citation _Citation_full 'Wishart, D.S. & Sykes, B.D. J. Biomol. NMR 4 171-180 (1994)' _Citation_title 'The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8019132 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 4 _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 171 _Page_last 180 _Year 1994 _Details ; A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements. ; save_ ################################## # Molecular system description # ################################## save_system_VATN _Saveframe_category molecular_system _Mol_system_name 'VATN VCP-like ATPase of Thermoplasma N-domain' _Abbreviation_common VAT-N _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label VATN $VATN stop_ _System_molecular_weight 21702 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'Fully reduced' loop_ _Biological_function 'peptide binding' 'protein folding and unfolding' 'protein recognition' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_VATN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'VCP-like ATPase of Thermoplasma N-domain' _Abbreviation_common VAT-N _Molecular_mass 21702 _Mol_thiol_state . _Details ; The construct contains the mature protein sequence (1-183), followed by a diglycyl spacer.Cysteine 77 is unpaired. ; ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MESNNGIILRVAEANSTDPG MSRVRLDESSRRLLDAEIGD VVEIEKVRKTVGRVYRARPE DENKGIVRIDSVMRNNCGAS IGDKVKVRKVRTEIAKKVTL APIIRKDQRLKFGEGIEEYV QRALIRRPMLEQDNISVPGL TLAGQTGLLFKVVKTLPSKV PVEIGEETKIEIREEPASEV LEEGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 SER 4 ASN 5 ASN 6 GLY 7 ILE 8 ILE 9 LEU 10 ARG 11 VAL 12 ALA 13 GLU 14 ALA 15 ASN 16 SER 17 THR 18 ASP 19 PRO 20 GLY 21 MET 22 SER 23 ARG 24 VAL 25 ARG 26 LEU 27 ASP 28 GLU 29 SER 30 SER 31 ARG 32 ARG 33 LEU 34 LEU 35 ASP 36 ALA 37 GLU 38 ILE 39 GLY 40 ASP 41 VAL 42 VAL 43 GLU 44 ILE 45 GLU 46 LYS 47 VAL 48 ARG 49 LYS 50 THR 51 VAL 52 GLY 53 ARG 54 VAL 55 TYR 56 ARG 57 ALA 58 ARG 59 PRO 60 GLU 61 ASP 62 GLU 63 ASN 64 LYS 65 GLY 66 ILE 67 VAL 68 ARG 69 ILE 70 ASP 71 SER 72 VAL 73 MET 74 ARG 75 ASN 76 ASN 77 CYS 78 GLY 79 ALA 80 SER 81 ILE 82 GLY 83 ASP 84 LYS 85 VAL 86 LYS 87 VAL 88 ARG 89 LYS 90 VAL 91 ARG 92 THR 93 GLU 94 ILE 95 ALA 96 LYS 97 LYS 98 VAL 99 THR 100 LEU 101 ALA 102 PRO 103 ILE 104 ILE 105 ARG 106 LYS 107 ASP 108 GLN 109 ARG 110 LEU 111 LYS 112 PHE 113 GLY 114 GLU 115 GLY 116 ILE 117 GLU 118 GLU 119 TYR 120 VAL 121 GLN 122 ARG 123 ALA 124 LEU 125 ILE 126 ARG 127 ARG 128 PRO 129 MET 130 LEU 131 GLU 132 GLN 133 ASP 134 ASN 135 ILE 136 SER 137 VAL 138 PRO 139 GLY 140 LEU 141 THR 142 LEU 143 ALA 144 GLY 145 GLN 146 THR 147 GLY 148 LEU 149 LEU 150 PHE 151 LYS 152 VAL 153 VAL 154 LYS 155 THR 156 LEU 157 PRO 158 SER 159 LYS 160 VAL 161 PRO 162 VAL 163 GLU 164 ILE 165 GLY 166 GLU 167 GLU 168 THR 169 LYS 170 ILE 171 GLU 172 ILE 173 ARG 174 GLU 175 GLU 176 PRO 177 ALA 178 SER 179 GLU 180 VAL 181 LEU 182 GLU 183 GLU 184 GLY 185 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 1CZ4 "Nmr Structure Of Vat-N: The N-Terminal Domain Of Vat (Vcp-Like Atpase Of Thermoplasma)" 100.00 185 100.00 100.00 1.87e-124 PDB 1CZ5 "Nmr Structure Of Vat-N: The N-Terminal Domain Of Vat (Vcp- Like Atpase Of Thermoplasma)" 100.00 185 100.00 100.00 1.87e-124 EMBL CAC11969 "VAT ATPase (VCP-like ATPase) [Thermoplasma acidophilum]" 98.92 745 100.00 100.00 1.31e-115 GB AAC45089 "VCP-like ATPase [Thermoplasma acidophilum]" 98.92 745 100.00 100.00 1.31e-115 REF WP_010901251 "ATPase AAA [Thermoplasma acidophilum]" 98.92 745 100.00 100.00 1.31e-115 SP O05209 "RecName: Full=VCP-like ATPase" 98.92 745 100.00 100.00 1.31e-115 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $VATN 'Thermoplasma acidophilum' 2302 Archaea Euryarchaeota Thermoplasma acididophilum 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 _Details $VATN 'recombinant technology' 'E. coli' BL21[DE3] Escherichia coli plasmid pET28 ; The gene coding for the protein plus a diglycyl linker and hexahistidine tag was synthesised to optimise codon usage for expression in E. coli. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_VATN_sample_N15 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $VATN 1.40 mM [U-15N] 'phosphate buffer' 40 mM . 'sodium chloride' 80 mM . 'sodium azide' 10 mM . D2O 10.0 % . H2O 90.0 % . stop_ save_ save_VATN_sample_dl _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $VATN 1.20 mM '[U-15N; U-13C]' 'phosphate buffer' 100 mM . 'sodium chloride' 200 mM . 'sodium azide' 10 mM . D2O 10.0 % . H2O 90.0 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_label_750 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details 'four channel, three gradient, triple resonance' save_ save_NMR_spectrometer_label_600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details 'four channel, three gradient, triple resonance' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_all _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.9 . n/a temperature 320 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details 'Internal TMS referencing for proton, 15N and 13C by frequency ratio' 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 TMS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.25144953 TMS H 1 'methyl protons' ppm 0.0 internal direct . . . . TMS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.10132912 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; Many methylene and valine/luecine methyl groups have been stereospecifically assigned. those not stereo-assigned are given ambiguity code 1 even where HB2,HB3 etc. are stated as having different shifts. Many glycine HA pairs are steroassigned. ; loop_ _Sample_label $VATN_sample_N15 stop_ _Sample_conditions_label $sample_conditions_all _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name VATN _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 GLU HA H 4.64 . 1 2 . 2 GLU HB2 H 2.37 . 2 3 . 2 GLU HB3 H 2.20 . 2 4 . 2 GLU C C 176.09 . 1 5 . 2 GLU CA C 56.87 . 1 6 . 2 GLU CB C 30.68 . 1 7 . 3 SER H H 8.56 . 1 8 . 3 SER HA H 4.68 . 1 9 . 3 SER HB2 H 4.08 . 1 10 . 3 SER HB3 H 4.08 . 1 11 . 3 SER C C 173.63 . 1 12 . 3 SER CA C 58.38 . 1 13 . 3 SER CB C 64.53 . 1 14 . 3 SER N N 116.97 . 1 15 . 4 ASN H H 8.29 . 1 16 . 4 ASN HA H 4.74 . 1 17 . 4 ASN HB2 H 3.00 . 1 18 . 4 ASN HB3 H 2.92 . 1 19 . 4 ASN HD21 H 7.77 . 1 20 . 4 ASN HD22 H 7.12 . 1 21 . 4 ASN C C 175.74 . 1 22 . 4 ASN CA C 55.17 . 1 23 . 4 ASN CB C 41.30 . 1 24 . 4 ASN CG C 177.42 . 1 25 . 4 ASN N N 125.91 . 1 26 . 4 ASN ND2 N 112.49 . 1 27 . 5 ASN H H 8.51 . 1 28 . 5 ASN HA H 4.94 . 1 29 . 5 ASN HB2 H 3.05 . 1 30 . 5 ASN HB3 H 3.05 . 1 31 . 5 ASN HD21 H 7.12 . 2 32 . 5 ASN HD22 H 7.75 . 2 33 . 5 ASN C C 175.53 . 1 34 . 5 ASN CA C 53.55 . 1 35 . 5 ASN CB C 39.37 . 1 36 . 5 ASN CG C 177.69 . 1 37 . 5 ASN N N 123.47 . 1 38 . 5 ASN ND2 N 112.47 . 1 39 . 6 GLY H H 8.47 . 1 40 . 6 GLY HA2 H 4.18 . 1 41 . 6 GLY HA3 H 4.47 . 1 42 . 6 GLY C C 173.37 . 1 43 . 6 GLY CA C 45.15 . 1 44 . 6 GLY N N 108.03 . 1 45 . 7 ILE H H 8.87 . 1 46 . 7 ILE HA H 5.05 . 1 47 . 7 ILE HB H 2.16 . 1 48 . 7 ILE HG12 H 1.50 . 2 49 . 7 ILE HG13 H 1.36 . 2 50 . 7 ILE HG2 H 1.12 . 1 51 . 7 ILE HD1 H 1.11 . 1 52 . 7 ILE C C 173.59 . 1 53 . 7 ILE CA C 59.80 . 1 54 . 7 ILE CB C 41.41 . 1 55 . 7 ILE CG1 C 25.50 . 1 56 . 7 ILE CG2 C 17.58 . 1 57 . 7 ILE CD1 C 14.41 . 1 58 . 7 ILE N N 114.53 . 1 59 . 8 ILE H H 8.30 . 1 60 . 8 ILE HA H 5.41 . 1 61 . 8 ILE HB H 1.98 . 1 62 . 8 ILE HG12 H 1.70 . 2 63 . 8 ILE HG13 H 1.39 . 2 64 . 8 ILE HG2 H 1.05 . 1 65 . 8 ILE HD1 H 1.00 . 1 66 . 8 ILE C C 176.65 . 1 67 . 8 ILE CA C 59.45 . 1 68 . 8 ILE CB C 38.46 . 1 69 . 8 ILE CG1 C 27.33 . 1 70 . 8 ILE CG2 C 17.89 . 1 71 . 8 ILE CD1 C 11.82 . 1 72 . 8 ILE N N 122.25 . 1 73 . 9 LEU H H 8.73 . 1 74 . 9 LEU HA H 4.88 . 1 75 . 9 LEU HB2 H 1.30 . 1 76 . 9 LEU HB3 H 1.34 . 1 77 . 9 LEU HG H 1.54 . 1 78 . 9 LEU HD1 H 1.01 . 2 79 . 9 LEU HD2 H 0.93 . 2 80 . 9 LEU C C 174.75 . 1 81 . 9 LEU CA C 52.96 . 1 82 . 9 LEU CB C 48.47 . 1 83 . 9 LEU CG C 26.62 . 1 84 . 9 LEU CD1 C 22.63 . 1 85 . 9 LEU CD2 C 27.39 . 1 86 . 9 LEU N N 127.13 . 1 87 . 10 ARG H H 8.48 . 1 88 . 10 ARG HA H 5.27 . 1 89 . 10 ARG HB2 H 1.86 . 1 90 . 10 ARG HB3 H 1.86 . 1 91 . 10 ARG HG2 H 1.82 . 2 92 . 10 ARG HG3 H 1.67 . 2 93 . 10 ARG HD2 H 3.44 . 1 94 . 10 ARG HD3 H 3.44 . 1 95 . 10 ARG C C 175.91 . 1 96 . 10 ARG CA C 55.11 . 1 97 . 10 ARG CB C 32.47 . 1 98 . 10 ARG CG C 27.93 . 1 99 . 10 ARG CD C 43.56 . 1 100 . 10 ARG N N 119.00 . 1 101 . 11 VAL H H 9.05 . 1 102 . 11 VAL HA H 4.36 . 1 103 . 11 VAL HB H 2.35 . 1 104 . 11 VAL HG1 H 1.10 . 1 105 . 11 VAL HG2 H 0.92 . 1 106 . 11 VAL C C 175.96 . 1 107 . 11 VAL CA C 64.15 . 1 108 . 11 VAL CB C 32.27 . 1 109 . 11 VAL CG1 C 24.89 . 1 110 . 11 VAL CG2 C 22.92 . 1 111 . 11 VAL N N 124.28 . 1 112 . 12 ALA H H 9.30 . 1 113 . 12 ALA HA H 4.93 . 1 114 . 12 ALA HB H 1.55 . 1 115 . 12 ALA C C 174.27 . 1 116 . 12 ALA CA C 50.49 . 1 117 . 12 ALA CB C 23.52 . 1 118 . 12 ALA N N 108.02 . 1 119 . 13 GLU H H 8.61 . 1 120 . 13 GLU HA H 4.46 . 1 121 . 13 GLU HB2 H 2.15 . 1 122 . 13 GLU HB3 H 2.15 . 1 123 . 13 GLU HG2 H 2.50 . 1 124 . 13 GLU HG3 H 2.50 . 1 125 . 13 GLU C C 176.13 . 1 126 . 13 GLU CA C 56.55 . 1 127 . 13 GLU CB C 30.68 . 1 128 . 13 GLU CG C 36.16 . 1 129 . 13 GLU N N 118.29 . 1 130 . 14 ALA H H 8.80 . 1 131 . 14 ALA HA H 4.21 . 1 132 . 14 ALA HB H 1.47 . 1 133 . 14 ALA C C 176.65 . 1 134 . 14 ALA CA C 54.01 . 1 135 . 14 ALA CB C 20.16 . 1 136 . 14 ALA N N 124.89 . 1 137 . 15 ASN H H 7.86 . 1 138 . 15 ASN HA H 4.64 . 1 139 . 15 ASN HB2 H 2.96 . 2 140 . 15 ASN HB3 H 2.88 . 2 141 . 15 ASN C C 175.82 . 1 142 . 15 ASN CA C 54.93 . 1 143 . 15 ASN CB C 42.00 . 1 144 . 15 ASN N N 119.82 . 1 145 . 17 THR HA H 4.62 . 1 146 . 17 THR HB H 4.58 . 1 147 . 17 THR HG2 H 1.45 . 1 148 . 17 THR C C 175.10 . 1 149 . 17 THR CA C 62.07 . 1 150 . 17 THR CB C 69.36 . 1 151 . 17 THR CG2 C 21.84 . 1 152 . 18 ASP H H 8.07 . 1 153 . 18 ASP HA H 4.92 . 1 154 . 18 ASP HB2 H 2.87 . 1 155 . 18 ASP HB3 H 3.10 . 1 156 . 18 ASP C C 176.79 . 1 157 . 18 ASP CA C 55.15 . 1 158 . 18 ASP CB C 41.77 . 1 159 . 18 ASP N N 122.66 . 1 160 . 19 PRO HA H 4.73 . 1 161 . 19 PRO HB2 H 2.53 . 1 162 . 19 PRO HB3 H 2.09 . 1 163 . 19 PRO HG2 H 2.34 . 2 164 . 19 PRO HG3 H 2.21 . 2 165 . 19 PRO HD2 H 4.24 . 2 166 . 19 PRO HD3 H 3.89 . 2 167 . 19 PRO CA C 66.06 . 1 168 . 19 PRO CB C 31.54 . 1 169 . 19 PRO CG C 27.94 . 1 170 . 19 PRO CD C 50.71 . 1 171 . 20 GLY H H 9.23 . 1 172 . 20 GLY HA2 H 4.00 . 1 173 . 20 GLY HA3 H 4.38 . 1 174 . 20 GLY C C 174.02 . 1 175 . 20 GLY CA C 46.13 . 1 176 . 20 GLY N N 110.46 . 1 177 . 21 MET H H 7.93 . 1 178 . 21 MET HA H 4.87 . 1 179 . 21 MET HB2 H 2.42 . 1 180 . 21 MET HB3 H 2.08 . 1 181 . 21 MET HE H 2.26 . 1 182 . 21 MET C C 175.79 . 1 183 . 21 MET CA C 54.91 . 1 184 . 21 MET CB C 33.27 . 1 185 . 21 MET CE C 17.67 . 1 186 . 21 MET N N 116.97 . 1 187 . 22 SER H H 9.29 . 1 188 . 22 SER HA H 4.60 . 1 189 . 22 SER HB2 H 3.77 . 1 190 . 22 SER HB3 H 3.77 . 1 191 . 22 SER C C 173.84 . 1 192 . 22 SER CA C 59.60 . 1 193 . 22 SER CB C 61.37 . 1 194 . 22 SER N N 114.94 . 1 195 . 23 ARG H H 8.69 . 1 196 . 23 ARG HA H 4.83 . 1 197 . 23 ARG HB2 H 1.93 . 1 198 . 23 ARG HB3 H 1.93 . 1 199 . 23 ARG C C 175.83 . 1 200 . 23 ARG CA C 56.25 . 1 201 . 23 ARG CB C 32.06 . 1 202 . 23 ARG N N 118.65 . 1 203 . 24 VAL H H 9.01 . 1 204 . 24 VAL HA H 4.55 . 1 205 . 24 VAL HB H 1.98 . 1 206 . 24 VAL HG1 H 0.80 . 1 207 . 24 VAL HG2 H 0.85 . 1 208 . 24 VAL C C 175.87 . 1 209 . 24 VAL CA C 61.14 . 1 210 . 24 VAL CB C 32.29 . 1 211 . 24 VAL CG1 C 21.41 . 1 212 . 24 VAL CG2 C 20.69 . 1 213 . 24 VAL N N 122.74 . 1 214 . 25 ARG H H 8.14 . 1 215 . 25 ARG HA H 5.12 . 1 216 . 25 ARG HB2 H 1.60 . 1 217 . 25 ARG HB3 H 1.99 . 1 218 . 25 ARG HG2 H 1.84 . 2 219 . 25 ARG HG3 H 1.59 . 2 220 . 25 ARG C C 175.65 . 1 221 . 25 ARG CA C 56.18 . 1 222 . 25 ARG CB C 30.98 . 1 223 . 25 ARG CG C 27.47 . 1 224 . 25 ARG N N 124.69 . 1 225 . 26 LEU H H 8.14 . 1 226 . 26 LEU HA H 5.24 . 1 227 . 26 LEU HB2 H 1.72 . 2 228 . 26 LEU HB3 H 1.69 . 2 229 . 26 LEU HG H 1.52 . 1 230 . 26 LEU HD1 H 0.90 . 2 231 . 26 LEU HD2 H 1.04 . 2 232 . 26 LEU C C 176.43 . 1 233 . 26 LEU CA C 52.86 . 1 234 . 26 LEU CB C 48.03 . 1 235 . 26 LEU CG C 25.96 . 1 236 . 26 LEU CD1 C 26.45 . 1 237 . 26 LEU CD2 C 24.20 . 1 238 . 26 LEU N N 122.05 . 1 239 . 27 ASP H H 9.59 . 1 240 . 27 ASP HA H 4.84 . 1 241 . 27 ASP HB2 H 3.96 . 1 242 . 27 ASP HB3 H 2.64 . 1 243 . 27 ASP C C 175.35 . 1 244 . 27 ASP CA C 53.06 . 1 245 . 27 ASP CB C 40.84 . 1 246 . 27 ASP N N 125.91 . 1 247 . 28 GLU H H 9.89 . 1 248 . 28 GLU HA H 3.94 . 1 249 . 28 GLU HB2 H 2.44 . 1 250 . 28 GLU HB3 H 2.33 . 1 251 . 28 GLU HG2 H 2.84 . 2 252 . 28 GLU HG3 H 2.70 . 2 253 . 28 GLU C C 179.67 . 1 254 . 28 GLU CA C 61.26 . 1 255 . 28 GLU CB C 29.75 . 1 256 . 28 GLU CG C 36.47 . 1 257 . 28 GLU N N 121.64 . 1 258 . 29 SER H H 9.29 . 1 259 . 29 SER HA H 4.33 . 1 260 . 29 SER HB2 H 4.20 . 1 261 . 29 SER HB3 H 4.20 . 1 262 . 29 SER C C 177.55 . 1 263 . 29 SER CA C 62.10 . 1 264 . 29 SER CB C 62.79 . 1 265 . 29 SER N N 115.95 . 1 266 . 30 SER H H 9.16 . 1 267 . 30 SER HA H 4.33 . 1 268 . 30 SER HB2 H 3.75 . 1 269 . 30 SER HB3 H 3.75 . 1 270 . 30 SER C C 175.96 . 1 271 . 30 SER CA C 63.12 . 1 272 . 30 SER CB C 63.34 . 1 273 . 30 SER N N 118.49 . 1 274 . 31 ARG H H 8.52 . 1 275 . 31 ARG HA H 3.96 . 1 276 . 31 ARG HB2 H 2.38 . 2 277 . 31 ARG HB3 H 2.21 . 2 278 . 31 ARG HG2 H 2.40 . 2 279 . 31 ARG HG3 H 2.24 . 2 280 . 31 ARG HD2 H 3.12 . 1 281 . 31 ARG HD3 H 3.12 . 1 282 . 31 ARG C C 179.19 . 1 283 . 31 ARG CA C 62.04 . 1 284 . 31 ARG CB C 29.06 . 1 285 . 31 ARG CG C 29.16 . 1 286 . 31 ARG CD C 43.47 . 1 287 . 31 ARG N N 120.02 . 1 288 . 32 ARG H H 8.55 . 1 289 . 32 ARG HA H 4.44 . 1 290 . 32 ARG HB2 H 2.26 . 2 291 . 32 ARG HB3 H 2.22 . 2 292 . 32 ARG HG2 H 2.05 . 2 293 . 32 ARG HG3 H 1.91 . 2 294 . 32 ARG HD2 H 3.48 . 1 295 . 32 ARG HD3 H 3.48 . 1 296 . 32 ARG C C 180.66 . 1 297 . 32 ARG CA C 59.60 . 1 298 . 32 ARG CB C 29.75 . 1 299 . 32 ARG CG C 27.33 . 1 300 . 32 ARG CD C 43.47 . 1 301 . 32 ARG N N 118.80 . 1 302 . 33 LEU H H 8.25 . 1 303 . 33 LEU HA H 4.32 . 1 304 . 33 LEU HB2 H 1.70 . 1 305 . 33 LEU HB3 H 2.23 . 1 306 . 33 LEU HG H 2.15 . 1 307 . 33 LEU HD1 H 1.17 . 2 308 . 33 LEU HD2 H 1.18 . 2 309 . 33 LEU C C 179.32 . 1 310 . 33 LEU CA C 58.14 . 1 311 . 33 LEU CB C 42.69 . 1 312 . 33 LEU CG C 26.97 . 1 313 . 33 LEU CD1 C 22.91 . 1 314 . 33 LEU CD2 C 25.27 . 1 315 . 33 LEU N N 120.77 . 1 316 . 34 LEU H H 7.75 . 1 317 . 34 LEU HA H 4.45 . 1 318 . 34 LEU HB2 H 1.96 . 1 319 . 34 LEU HB3 H 1.67 . 1 320 . 34 LEU HG H 2.01 . 1 321 . 34 LEU HD1 H 0.82 . 2 322 . 34 LEU HD2 H 1.22 . 2 323 . 34 LEU C C 176.58 . 1 324 . 34 LEU CA C 54.82 . 1 325 . 34 LEU CB C 44.54 . 1 326 . 34 LEU CG C 26.41 . 1 327 . 34 LEU CD1 C 26.26 . 1 328 . 34 LEU CD2 C 23.98 . 1 329 . 34 LEU N N 116.16 . 1 330 . 35 ASP H H 8.22 . 1 331 . 35 ASP HA H 4.46 . 1 332 . 35 ASP HB2 H 3.35 . 2 333 . 35 ASP HB3 H 2.67 . 2 334 . 35 ASP C C 174.79 . 1 335 . 35 ASP CA C 55.10 . 1 336 . 35 ASP CB C 40.29 . 1 337 . 35 ASP N N 119.82 . 1 338 . 36 ALA H H 8.58 . 1 339 . 36 ALA HA H 5.09 . 1 340 . 36 ALA HB H 1.31 . 1 341 . 36 ALA C C 176.17 . 1 342 . 36 ALA CA C 50.42 . 1 343 . 36 ALA CB C 21.44 . 1 344 . 36 ALA N N 119.21 . 1 345 . 37 GLU H H 9.31 . 1 346 . 37 GLU HA H 4.59 . 1 347 . 37 GLU HB2 H 2.21 . 1 348 . 37 GLU HB3 H 1.90 . 1 349 . 37 GLU HG2 H 2.64 . 2 350 . 37 GLU HG3 H 2.47 . 2 351 . 37 GLU C C 177.08 . 1 352 . 37 GLU CA C 53.94 . 1 353 . 37 GLU CB C 31.60 . 1 354 . 37 GLU CG C 36.86 . 1 355 . 37 GLU N N 123.47 . 1 356 . 38 ILE H H 8.76 . 1 357 . 38 ILE HA H 3.59 . 1 358 . 38 ILE HB H 2.03 . 1 359 . 38 ILE HG12 H 1.72 . 2 360 . 38 ILE HG13 H 1.42 . 2 361 . 38 ILE HG2 H 1.13 . 1 362 . 38 ILE HD1 H 0.97 . 1 363 . 38 ILE C C 177.94 . 1 364 . 38 ILE CA C 63.31 . 1 365 . 38 ILE CB C 36.22 . 1 366 . 38 ILE CG1 C 27.94 . 1 367 . 38 ILE CG2 C 17.70 . 1 368 . 38 ILE CD1 C 11.80 . 1 369 . 38 ILE N N 121.23 . 1 370 . 39 GLY H H 9.22 . 1 371 . 39 GLY HA2 H 4.70 . 1 372 . 39 GLY HA3 H 3.67 . 1 373 . 39 GLY C C 174.92 . 1 374 . 39 GLY CA C 45.25 . 1 375 . 39 GLY N N 117.17 . 1 376 . 40 ASP H H 8.23 . 1 377 . 40 ASP HA H 5.03 . 1 378 . 40 ASP HB2 H 3.09 . 1 379 . 40 ASP HB3 H 2.94 . 1 380 . 40 ASP C C 174.53 . 1 381 . 40 ASP CA C 55.18 . 1 382 . 40 ASP CB C 41.30 . 1 383 . 40 ASP N N 121.64 . 1 384 . 41 VAL H H 9.19 . 1 385 . 41 VAL HA H 4.92 . 1 386 . 41 VAL HB H 2.22 . 1 387 . 41 VAL HG1 H 0.95 . 1 388 . 41 VAL HG2 H 1.17 . 1 389 . 41 VAL C C 175.79 . 1 390 . 41 VAL CA C 62.53 . 1 391 . 41 VAL CB C 32.29 . 1 392 . 41 VAL CG1 C 21.54 . 1 393 . 41 VAL CG2 C 22.22 . 1 394 . 41 VAL N N 120.22 . 1 395 . 42 VAL H H 8.69 . 1 396 . 42 VAL HA H 5.47 . 1 397 . 42 VAL HB H 2.21 . 1 398 . 42 VAL HG1 H 0.76 . 1 399 . 42 VAL HG2 H 0.80 . 1 400 . 42 VAL C C 174.15 . 1 401 . 42 VAL CA C 57.65 . 1 402 . 42 VAL CB C 34.84 . 1 403 . 42 VAL CG1 C 21.11 . 1 404 . 42 VAL CG2 C 18.24 . 1 405 . 42 VAL N N 115.14 . 1 406 . 43 GLU H H 9.52 . 1 407 . 43 GLU HA H 5.57 . 1 408 . 43 GLU HB2 H 2.13 . 2 409 . 43 GLU HB3 H 2.09 . 2 410 . 43 GLU HG2 H 2.34 . 2 411 . 43 GLU HG3 H 2.18 . 2 412 . 43 GLU C C 175.14 . 1 413 . 43 GLU CA C 53.71 . 1 414 . 43 GLU CB C 34.60 . 1 415 . 43 GLU CG C 37.24 . 1 416 . 43 GLU N N 120.83 . 1 417 . 44 ILE H H 8.82 . 1 418 . 44 ILE HA H 5.19 . 1 419 . 44 ILE HB H 1.68 . 1 420 . 44 ILE HG12 H 1.62 . 2 421 . 44 ILE HG13 H 1.20 . 2 422 . 44 ILE HG2 H 0.98 . 1 423 . 44 ILE HD1 H 0.95 . 1 424 . 44 ILE C C 175.18 . 1 425 . 44 ILE CA C 59.88 . 1 426 . 44 ILE CB C 40.38 . 1 427 . 44 ILE CG1 C 27.94 . 1 428 . 44 ILE CG2 C 19.11 . 1 429 . 44 ILE CD1 C 15.45 . 1 430 . 44 ILE N N 124.59 . 1 431 . 45 GLU H H 9.34 . 1 432 . 45 GLU HA H 5.46 . 1 433 . 45 GLU HB2 H 1.95 . 1 434 . 45 GLU HB3 H 2.20 . 1 435 . 45 GLU HG2 H 2.26 . 2 436 . 45 GLU HG3 H 2.05 . 2 437 . 45 GLU C C 176.48 . 1 438 . 45 GLU CA C 54.82 . 1 439 . 45 GLU CB C 35.07 . 1 440 . 45 GLU CG C 36.05 . 1 441 . 45 GLU N N 125.91 . 1 442 . 46 LYS H H 8.02 . 1 443 . 46 LYS HA H 4.73 . 1 444 . 46 LYS HB2 H 2.02 . 2 445 . 46 LYS HB3 H 1.77 . 2 446 . 46 LYS HG2 H 1.55 . 1 447 . 46 LYS HG3 H 1.55 . 1 448 . 46 LYS HD2 H 1.88 . 1 449 . 46 LYS HD3 H 1.88 . 1 450 . 46 LYS HE2 H 3.20 . 1 451 . 46 LYS HE3 H 3.20 . 1 452 . 46 LYS C C 177.34 . 1 453 . 46 LYS CA C 59.02 . 1 454 . 46 LYS CB C 33.22 . 1 455 . 46 LYS CG C 26.10 . 1 456 . 46 LYS CD C 29.24 . 1 457 . 46 LYS CE C 42.15 . 1 458 . 46 LYS N N 126.52 . 1 459 . 47 VAL H H 8.44 . 1 460 . 47 VAL HA H 4.29 . 1 461 . 47 VAL HB H 2.28 . 1 462 . 47 VAL HG1 H 1.29 . 1 463 . 47 VAL HG2 H 1.40 . 1 464 . 47 VAL C C 176.09 . 1 465 . 47 VAL CA C 64.91 . 1 466 . 47 VAL CB C 33.08 . 1 467 . 47 VAL CG1 C 21.42 . 1 468 . 47 VAL CG2 C 21.93 . 1 469 . 47 VAL N N 122.05 . 1 470 . 48 ARG H H 7.89 . 1 471 . 48 ARG HA H 4.90 . 1 472 . 48 ARG HB2 H 2.22 . 2 473 . 48 ARG HB3 H 2.13 . 2 474 . 48 ARG HG2 H 1.85 . 2 475 . 48 ARG HG3 H 1.77 . 2 476 . 48 ARG HD2 H 3.64 . 2 477 . 48 ARG HD3 H 3.45 . 2 478 . 48 ARG C C 174.75 . 1 479 . 48 ARG CA C 54.23 . 1 480 . 48 ARG CB C 33.68 . 1 481 . 48 ARG CG C 27.68 . 1 482 . 48 ARG CD C 43.17 . 1 483 . 48 ARG N N 117.58 . 1 484 . 49 LYS H H 8.25 . 1 485 . 49 LYS HA H 5.49 . 1 486 . 49 LYS HB2 H 1.74 . 1 487 . 49 LYS HB3 H 1.74 . 1 488 . 49 LYS HG2 H 1.37 . 1 489 . 49 LYS HG3 H 1.37 . 1 490 . 49 LYS HD2 H 1.79 . 1 491 . 49 LYS HD3 H 1.79 . 1 492 . 49 LYS HE2 H 3.12 . 1 493 . 49 LYS HE3 H 3.12 . 1 494 . 49 LYS C C 174.88 . 1 495 . 49 LYS CA C 55.70 . 1 496 . 49 LYS CB C 35.84 . 1 497 . 49 LYS CG C 25.26 . 1 498 . 49 LYS CD C 29.51 . 1 499 . 49 LYS CE C 42.16 . 1 500 . 49 LYS N N 119.41 . 1 501 . 50 THR H H 8.70 . 1 502 . 50 THR HA H 4.98 . 1 503 . 50 THR HB H 4.10 . 1 504 . 50 THR HG2 H 1.33 . 1 505 . 50 THR C C 172.81 . 1 506 . 50 THR CA C 61.26 . 1 507 . 50 THR CB C 69.49 . 1 508 . 50 THR CG2 C 18.35 . 1 509 . 50 THR N N 113.01 . 1 510 . 51 VAL H H 7.90 . 1 511 . 51 VAL HA H 6.13 . 1 512 . 51 VAL HB H 2.09 . 1 513 . 51 VAL HG1 H 1.02 . 1 514 . 51 VAL HG2 H 0.92 . 1 515 . 51 VAL C C 174.75 . 1 516 . 51 VAL CA C 58.33 . 1 517 . 51 VAL CB C 36.92 . 1 518 . 51 VAL CG1 C 22.02 . 1 519 . 51 VAL CG2 C 17.89 . 1 520 . 51 VAL N N 111.98 . 1 521 . 52 GLY H H 8.56 . 1 522 . 52 GLY HA2 H 3.90 . 1 523 . 52 GLY HA3 H 4.49 . 1 524 . 52 GLY C C 171.08 . 1 525 . 52 GLY CA C 45.93 . 1 526 . 52 GLY N N 129.16 . 1 527 . 53 ARG H H 8.77 . 1 528 . 53 ARG HA H 5.54 . 1 529 . 53 ARG HB2 H 2.09 . 2 530 . 53 ARG HB3 H 1.92 . 2 531 . 53 ARG HG2 H 1.91 . 2 532 . 53 ARG HG3 H 1.77 . 2 533 . 53 ARG HD2 H 3.61 . 2 534 . 53 ARG HD3 H 3.52 . 2 535 . 53 ARG C C 176.04 . 1 536 . 53 ARG CA C 55.73 . 1 537 . 53 ARG CB C 32.81 . 1 538 . 53 ARG CG C 29.16 . 1 539 . 53 ARG CD C 42.86 . 1 540 . 53 ARG N N 118.60 . 1 541 . 54 VAL H H 9.35 . 1 542 . 54 VAL HA H 4.42 . 1 543 . 54 VAL HB H 2.32 . 1 544 . 54 VAL HG1 H 1.13 . 1 545 . 54 VAL HG2 H 0.94 . 1 546 . 54 VAL C C 175.53 . 1 547 . 54 VAL CA C 64.54 . 1 548 . 54 VAL CB C 32.58 . 1 549 . 54 VAL CG1 C 24.74 . 1 550 . 54 VAL CG2 C 22.48 . 1 551 . 54 VAL N N 123.46 . 1 552 . 55 TYR H H 9.47 . 1 553 . 55 TYR HA H 4.81 . 1 554 . 55 TYR HB2 H 2.71 . 1 555 . 55 TYR HB3 H 3.17 . 1 556 . 55 TYR HD1 H 7.51 . 1 557 . 55 TYR HD2 H 7.51 . 1 558 . 55 TYR HE1 H 7.06 . 1 559 . 55 TYR HE2 H 7.06 . 1 560 . 55 TYR C C 173.97 . 1 561 . 55 TYR CA C 57.06 . 1 562 . 55 TYR CB C 42.69 . 1 563 . 55 TYR N N 130.59 . 1 564 . 56 ARG H H 8.40 . 1 565 . 56 ARG HA H 4.39 . 1 566 . 56 ARG HB2 H 2.00 . 2 567 . 56 ARG HB3 H 1.84 . 2 568 . 56 ARG HD2 H 3.44 . 1 569 . 56 ARG HD3 H 3.44 . 1 570 . 56 ARG C C 176.65 . 1 571 . 56 ARG CA C 57.44 . 1 572 . 56 ARG CB C 31.37 . 1 573 . 56 ARG N N 121.24 . 1 574 . 57 ALA H H 7.72 . 1 575 . 57 ALA HA H 4.66 . 1 576 . 57 ALA HB H 1.52 . 1 577 . 57 ALA C C 177.85 . 1 578 . 57 ALA CA C 51.89 . 1 579 . 57 ALA CB C 18.71 . 1 580 . 57 ALA N N 126.32 . 1 581 . 58 ARG H H 9.30 . 1 582 . 58 ARG HA H 4.66 . 1 583 . 58 ARG HB2 H 1.89 . 1 584 . 58 ARG HB3 H 2.34 . 1 585 . 58 ARG C C 176.24 . 1 586 . 58 ARG CA C 55.40 . 1 587 . 58 ARG CB C 28.90 . 1 588 . 58 ARG N N 121.85 . 1 589 . 59 PRO HA H 4.65 . 1 590 . 59 PRO HB2 H 2.18 . 1 591 . 59 PRO HB3 H 2.65 . 1 592 . 59 PRO HG2 H 2.46 . 2 593 . 59 PRO HG3 H 2.37 . 2 594 . 59 PRO HD2 H 4.11 . 2 595 . 59 PRO HD3 H 4.07 . 2 596 . 59 PRO CA C 65.99 . 1 597 . 59 PRO CB C 31.89 . 1 598 . 59 PRO CG C 27.72 . 1 599 . 59 PRO CD C 50.10 . 1 600 . 60 GLU H H 9.80 . 1 601 . 60 GLU HA H 4.40 . 1 602 . 60 GLU HB2 H 2.25 . 2 603 . 60 GLU HB3 H 2.19 . 2 604 . 60 GLU HG2 H 2.50 . 1 605 . 60 GLU HG3 H 2.50 . 1 606 . 60 GLU C C 176.91 . 1 607 . 60 GLU CA C 58.82 . 1 608 . 60 GLU CB C 28.37 . 1 609 . 60 GLU CG C 36.10 . 1 610 . 60 GLU N N 116.36 . 1 611 . 61 ASP H H 8.16 . 1 612 . 61 ASP HA H 4.87 . 1 613 . 61 ASP HB2 H 3.04 . 1 614 . 61 ASP HB3 H 3.04 . 1 615 . 61 ASP C C 176.99 . 1 616 . 61 ASP CA C 54.56 . 1 617 . 61 ASP CB C 42.00 . 1 618 . 61 ASP N N 118.80 . 1 619 . 62 GLU H H 7.69 . 1 620 . 62 GLU HA H 4.39 . 1 621 . 62 GLU HB2 H 2.31 . 2 622 . 62 GLU HB3 H 2.28 . 2 623 . 62 GLU HG2 H 2.70 . 1 624 . 62 GLU HG3 H 2.70 . 1 625 . 62 GLU C C 177.73 . 1 626 . 62 GLU CA C 58.78 . 1 627 . 62 GLU CB C 29.98 . 1 628 . 62 GLU CG C 35.77 . 1 629 . 62 GLU N N 121.85 . 1 630 . 63 ASN H H 9.92 . 1 631 . 63 ASN HA H 4.77 . 1 632 . 63 ASN HB2 H 3.35 . 1 633 . 63 ASN HB3 H 3.35 . 1 634 . 63 ASN HD21 H 7.23 . 2 635 . 63 ASN HD22 H 7.85 . 2 636 . 63 ASN C C 176.04 . 1 637 . 63 ASN CA C 55.70 . 1 638 . 63 ASN CB C 37.15 . 1 639 . 63 ASN CG C 178.97 . 1 640 . 63 ASN N N 117.78 . 1 641 . 63 ASN ND2 N 114.94 . 1 642 . 64 LYS H H 7.91 . 1 643 . 64 LYS HA H 4.66 . 1 644 . 64 LYS HB2 H 2.17 . 2 645 . 64 LYS HB3 H 1.96 . 2 646 . 64 LYS HG2 H 1.57 . 1 647 . 64 LYS HG3 H 1.57 . 1 648 . 64 LYS HD2 H 1.94 . 1 649 . 64 LYS HD3 H 1.94 . 1 650 . 64 LYS HE2 H 3.22 . 1 651 . 64 LYS HE3 H 3.22 . 1 652 . 64 LYS C C 177.29 . 1 653 . 64 LYS CA C 56.48 . 1 654 . 64 LYS CB C 33.68 . 1 655 . 64 LYS CG C 24.44 . 1 656 . 64 LYS CD C 28.73 . 1 657 . 64 LYS CE C 42.14 . 1 658 . 64 LYS N N 115.96 . 1 659 . 65 GLY H H 9.03 . 1 660 . 65 GLY HA2 H 4.15 . 1 661 . 65 GLY HA3 H 3.91 . 1 662 . 65 GLY C C 175.53 . 1 663 . 65 GLY CA C 47.41 . 1 664 . 65 GLY N N 111.07 . 1 665 . 66 ILE H H 8.40 . 1 666 . 66 ILE HA H 5.76 . 1 667 . 66 ILE HB H 1.91 . 1 668 . 66 ILE HG12 H 1.62 . 2 669 . 66 ILE HG13 H 1.19 . 2 670 . 66 ILE HG2 H 0.97 . 1 671 . 66 ILE HD1 H 0.89 . 1 672 . 66 ILE C C 174.88 . 1 673 . 66 ILE CA C 59.11 . 1 674 . 66 ILE CB C 42.69 . 1 675 . 66 ILE CG1 C 25.81 . 1 676 . 66 ILE CG2 C 17.89 . 1 677 . 66 ILE CD1 C 13.63 . 1 678 . 66 ILE N N 114.53 . 1 679 . 67 VAL H H 8.89 . 1 680 . 67 VAL HA H 4.95 . 1 681 . 67 VAL HB H 1.98 . 1 682 . 67 VAL HG1 H 0.86 . 1 683 . 67 VAL HG2 H 0.96 . 1 684 . 67 VAL C C 173.50 . 1 685 . 67 VAL CA C 58.55 . 1 686 . 67 VAL CB C 33.91 . 1 687 . 67 VAL CG1 C 19.04 . 1 688 . 67 VAL CG2 C 23.17 . 1 689 . 67 VAL N N 120.63 . 1 690 . 68 ARG H H 7.62 . 1 691 . 68 ARG HA H 5.25 . 1 692 . 68 ARG HB2 H 1.73 . 1 693 . 68 ARG HB3 H 1.73 . 1 694 . 68 ARG HD2 H 2.92 . 2 695 . 68 ARG HD3 H 2.88 . 2 696 . 68 ARG C C 176.52 . 1 697 . 68 ARG CA C 55.89 . 1 698 . 68 ARG CB C 31.37 . 1 699 . 68 ARG CD C 43.16 . 1 700 . 68 ARG N N 125.30 . 1 701 . 69 ILE H H 8.04 . 1 702 . 69 ILE HA H 5.14 . 1 703 . 69 ILE HB H 2.25 . 1 704 . 69 ILE HG12 H 1.77 . 2 705 . 69 ILE HG13 H 1.28 . 2 706 . 69 ILE HG2 H 1.29 . 1 707 . 69 ILE HD1 H 0.81 . 1 708 . 69 ILE C C 174.49 . 1 709 . 69 ILE CA C 59.60 . 1 710 . 69 ILE CB C 42.92 . 1 711 . 69 ILE CG1 C 24.34 . 1 712 . 69 ILE CG2 C 21.54 . 1 713 . 69 ILE CD1 C 13.02 . 1 714 . 69 ILE N N 116.36 . 1 715 . 70 ASP H H 8.77 . 1 716 . 70 ASP HA H 4.81 . 1 717 . 70 ASP HB2 H 3.62 . 1 718 . 70 ASP HB3 H 3.62 . 1 719 . 70 ASP C C 176.48 . 1 720 . 70 ASP CA C 53.84 . 1 721 . 70 ASP CB C 42.23 . 1 722 . 70 ASP N N 121.24 . 1 723 . 71 SER H H 9.05 . 1 724 . 71 SER HA H 4.07 . 1 725 . 71 SER HB2 H 4.23 . 2 726 . 71 SER HB3 H 4.19 . 2 727 . 71 SER C C 176.82 . 1 728 . 71 SER CA C 62.14 . 1 729 . 71 SER CB C 63.04 . 1 730 . 71 SER N N 113.11 . 1 731 . 72 VAL H H 7.92 . 1 732 . 72 VAL HA H 3.95 . 1 733 . 72 VAL HB H 2.52 . 1 734 . 72 VAL HG1 H 1.18 . 1 735 . 72 VAL HG2 H 1.23 . 1 736 . 72 VAL C C 178.85 . 1 737 . 72 VAL CA C 66.44 . 1 738 . 72 VAL CB C 31.83 . 1 739 . 72 VAL CG1 C 21.84 . 1 740 . 72 VAL CG2 C 23.40 . 1 741 . 72 VAL N N 125.09 . 1 742 . 73 MET H H 8.74 . 1 743 . 73 MET HA H 4.41 . 1 744 . 73 MET HB2 H 2.48 . 1 745 . 73 MET HB3 H 2.48 . 1 746 . 73 MET HE H 2.09 . 1 747 . 73 MET C C 179.93 . 1 748 . 73 MET CA C 59.80 . 1 749 . 73 MET CB C 33.45 . 1 750 . 73 MET CE C 17.58 . 1 751 . 73 MET N N 120.83 . 1 752 . 74 ARG H H 9.05 . 1 753 . 74 ARG HA H 3.99 . 1 754 . 74 ARG HB2 H 2.16 . 1 755 . 74 ARG HB3 H 2.16 . 1 756 . 74 ARG HG2 H 2.43 . 1 757 . 74 ARG HG3 H 2.43 . 1 758 . 74 ARG C C 178.93 . 1 759 . 74 ARG CA C 61.55 . 1 760 . 74 ARG CB C 33.89 . 1 761 . 74 ARG N N 117.78 . 1 762 . 75 ASN H H 8.32 . 1 763 . 75 ASN HA H 4.80 . 1 764 . 75 ASN HB2 H 3.21 . 2 765 . 75 ASN HB3 H 3.14 . 2 766 . 75 ASN HD21 H 7.12 . 2 767 . 75 ASN HD22 H 7.83 . 2 768 . 75 ASN C C 178.24 . 1 769 . 75 ASN CA C 56.49 . 1 770 . 75 ASN CB C 38.47 . 1 771 . 75 ASN CG C 176.77 . 1 772 . 75 ASN N N 118.49 . 1 773 . 75 ASN ND2 N 112.50 . 1 774 . 76 ASN H H 8.61 . 1 775 . 76 ASN HA H 4.98 . 1 776 . 76 ASN HB2 H 3.24 . 1 777 . 76 ASN HB3 H 3.19 . 1 778 . 76 ASN HD21 H 6.85 . 2 779 . 76 ASN HD22 H 7.32 . 2 780 . 76 ASN C C 176.73 . 1 781 . 76 ASN CA C 55.56 . 1 782 . 76 ASN CB C 38.30 . 1 783 . 76 ASN N N 118.80 . 1 784 . 76 ASN ND2 N 109.45 . 1 785 . 77 CYS H H 7.84 . 1 786 . 77 CYS HA H 5.04 . 1 787 . 77 CYS HB2 H 3.40 . 1 788 . 77 CYS HB3 H 2.95 . 1 789 . 77 CYS C C 175.10 . 1 790 . 77 CYS CA C 57.45 . 1 791 . 77 CYS CB C 29.29 . 1 792 . 77 CYS N N 109.66 . 1 793 . 78 GLY H H 8.41 . 1 794 . 78 GLY HA2 H 4.22 . 1 795 . 78 GLY HA3 H 4.22 . 1 796 . 78 GLY C C 173.28 . 1 797 . 78 GLY CA C 47.23 . 1 798 . 78 GLY N N 114.94 . 1 799 . 79 ALA H H 8.36 . 1 800 . 79 ALA HA H 5.00 . 1 801 . 79 ALA HB H 1.43 . 1 802 . 79 ALA C C 176.65 . 1 803 . 79 ALA CA C 51.01 . 1 804 . 79 ALA CB C 23.75 . 1 805 . 79 ALA N N 121.84 . 1 806 . 80 SER H H 9.35 . 1 807 . 80 SER HA H 4.86 . 1 808 . 80 SER HB2 H 3.80 . 1 809 . 80 SER HB3 H 4.06 . 1 810 . 80 SER C C 174.79 . 1 811 . 80 SER CA C 57.16 . 1 812 . 80 SER CB C 64.87 . 1 813 . 80 SER N N 117.78 . 1 814 . 81 ILE H H 8.59 . 1 815 . 81 ILE HA H 3.51 . 1 816 . 81 ILE HB H 1.99 . 1 817 . 81 ILE HG12 H 1.80 . 2 818 . 81 ILE HG13 H 1.16 . 2 819 . 81 ILE HG2 H 1.20 . 1 820 . 81 ILE HD1 H 1.06 . 1 821 . 81 ILE C C 177.51 . 1 822 . 81 ILE CA C 64.39 . 1 823 . 81 ILE CB C 36.92 . 1 824 . 81 ILE CG1 C 28.55 . 1 825 . 81 ILE CG2 C 17.72 . 1 826 . 81 ILE CD1 C 12.61 . 1 827 . 81 ILE N N 122.86 . 1 828 . 82 GLY H H 9.14 . 1 829 . 82 GLY HA2 H 4.74 . 1 830 . 82 GLY HA3 H 3.74 . 1 831 . 82 GLY C C 174.40 . 1 832 . 82 GLY CA C 45.25 . 1 833 . 82 GLY N N 117.07 . 1 834 . 83 ASP H H 8.08 . 1 835 . 83 ASP HA H 4.86 . 1 836 . 83 ASP HB2 H 3.15 . 1 837 . 83 ASP HB3 H 2.67 . 1 838 . 83 ASP C C 176.35 . 1 839 . 83 ASP CA C 54.91 . 1 840 . 83 ASP CB C 42.23 . 1 841 . 83 ASP N N 120.43 . 1 842 . 84 LYS H H 8.61 . 1 843 . 84 LYS HA H 5.08 . 1 844 . 84 LYS HB2 H 1.76 . 1 845 . 84 LYS HB3 H 1.91 . 1 846 . 84 LYS HG2 H 1.46 . 1 847 . 84 LYS HG3 H 1.46 . 1 848 . 84 LYS HD2 H 1.85 . 1 849 . 84 LYS HD3 H 1.85 . 1 850 . 84 LYS HE2 H 3.20 . 1 851 . 84 LYS HE3 H 3.20 . 1 852 . 84 LYS C C 176.99 . 1 853 . 84 LYS CA C 56.38 . 1 854 . 84 LYS CB C 33.22 . 1 855 . 84 LYS CG C 24.33 . 1 856 . 84 LYS CD C 28.74 . 1 857 . 84 LYS CE C 42.09 . 1 858 . 84 LYS N N 118.80 . 1 859 . 85 VAL H H 9.22 . 1 860 . 85 VAL HA H 4.97 . 1 861 . 85 VAL HB H 2.19 . 1 862 . 85 VAL HG1 H 0.91 . 1 863 . 85 VAL HG2 H 0.77 . 1 864 . 85 VAL C C 173.71 . 1 865 . 85 VAL CA C 58.87 . 1 866 . 85 VAL CB C 35.50 . 1 867 . 85 VAL CG1 C 23.00 . 1 868 . 85 VAL CG2 C 18.34 . 1 869 . 85 VAL N N 114.94 . 1 870 . 86 LYS H H 8.13 . 1 871 . 86 LYS HA H 5.25 . 1 872 . 86 LYS HB2 H 1.96 . 2 873 . 86 LYS HB3 H 1.84 . 2 874 . 86 LYS HG2 H 1.58 . 1 875 . 86 LYS HG3 H 1.58 . 1 876 . 86 LYS HD2 H 1.86 . 1 877 . 86 LYS HD3 H 1.86 . 1 878 . 86 LYS HE2 H 3.10 . 1 879 . 86 LYS HE3 H 3.10 . 1 880 . 86 LYS C C 176.30 . 1 881 . 86 LYS CA C 55.40 . 1 882 . 86 LYS CB C 34.60 . 1 883 . 86 LYS CG C 24.89 . 1 884 . 86 LYS CD C 28.89 . 1 885 . 86 LYS CE C 42.02 . 1 886 . 86 LYS N N 120.22 . 1 887 . 87 VAL H H 9.26 . 1 888 . 87 VAL HA H 5.49 . 1 889 . 87 VAL HB H 2.02 . 1 890 . 87 VAL HG1 H 1.01 . 2 891 . 87 VAL HG2 H 1.03 . 2 892 . 87 VAL C C 174.71 . 1 893 . 87 VAL CA C 60.73 . 1 894 . 87 VAL CB C 34.50 . 1 895 . 87 VAL CG1 C 21.48 . 1 896 . 87 VAL CG2 C 21.78 . 1 897 . 87 VAL N N 124.89 . 1 898 . 88 ARG H H 8.80 . 1 899 . 88 ARG HA H 5.08 . 1 900 . 88 ARG HB2 H 1.97 . 2 901 . 88 ARG HB3 H 1.92 . 2 902 . 88 ARG HG2 H 1.84 . 2 903 . 88 ARG HG3 H 1.60 . 2 904 . 88 ARG HD2 H 3.44 . 2 905 . 88 ARG HD3 H 3.25 . 2 906 . 88 ARG HE H 7.39 . 1 907 . 88 ARG C C 174.66 . 1 908 . 88 ARG CA C 54.82 . 1 909 . 88 ARG CB C 34.37 . 1 910 . 88 ARG CG C 27.03 . 1 911 . 88 ARG CD C 43.47 . 1 912 . 88 ARG N N 122.05 . 1 913 . 89 LYS H H 9.19 . 1 914 . 89 LYS HA H 4.91 . 1 915 . 89 LYS HB2 H 2.14 . 1 916 . 89 LYS HB3 H 1.83 . 1 917 . 89 LYS HG2 H 1.55 . 1 918 . 89 LYS HG3 H 1.55 . 1 919 . 89 LYS HD2 H 1.88 . 1 920 . 89 LYS HD3 H 1.88 . 1 921 . 89 LYS HE2 H 3.20 . 1 922 . 89 LYS HE3 H 3.20 . 1 923 . 89 LYS C C 176.22 . 1 924 . 89 LYS CA C 58.14 . 1 925 . 89 LYS CB C 33.91 . 1 926 . 89 LYS CG C 24.79 . 1 927 . 89 LYS CD C 29.98 . 1 928 . 89 LYS CE C 42.03 . 1 929 . 89 LYS N N 125.09 . 1 930 . 90 VAL H H 8.36 . 1 931 . 90 VAL HA H 4.96 . 1 932 . 90 VAL HB H 2.35 . 1 933 . 90 VAL HG1 H 1.03 . 1 934 . 90 VAL HG2 H 0.83 . 1 935 . 90 VAL C C 173.46 . 1 936 . 90 VAL CA C 59.62 . 1 937 . 90 VAL CB C 35.85 . 1 938 . 90 VAL CG1 C 22.37 . 1 939 . 90 VAL CG2 C 18.74 . 1 940 . 90 VAL N N 118.60 . 1 941 . 91 ARG H H 8.15 . 1 942 . 91 ARG HA H 4.90 . 1 943 . 91 ARG HB2 H 2.05 . 1 944 . 91 ARG HB3 H 1.96 . 1 945 . 91 ARG HG2 H 1.87 . 1 946 . 91 ARG HG3 H 1.87 . 1 947 . 91 ARG HD2 H 3.45 . 1 948 . 91 ARG HD3 H 3.45 . 1 949 . 91 ARG C C 176.73 . 1 950 . 91 ARG CA C 55.00 . 1 951 . 91 ARG CB C 32.06 . 1 952 . 91 ARG CG C 27.04 . 1 953 . 91 ARG CD C 43.17 . 1 954 . 91 ARG N N 119.61 . 1 955 . 92 THR H H 8.30 . 1 956 . 92 THR HA H 4.62 . 1 957 . 92 THR HB H 4.19 . 1 958 . 92 THR HG2 H 1.16 . 1 959 . 92 THR C C 175.18 . 1 960 . 92 THR CA C 59.89 . 1 961 . 92 THR CB C 70.41 . 1 962 . 92 THR CG2 C 24.57 . 1 963 . 92 THR N N 111.48 . 1 964 . 93 GLU H H 7.87 . 1 965 . 93 GLU HA H 4.85 . 1 966 . 93 GLU HB2 H 2.20 . 1 967 . 93 GLU HB3 H 1.78 . 1 968 . 93 GLU HG2 H 2.49 . 1 969 . 93 GLU HG3 H 2.49 . 1 970 . 93 GLU C C 176.30 . 1 971 . 93 GLU CA C 54.43 . 1 972 . 93 GLU CB C 32.53 . 1 973 . 93 GLU CG C 35.58 . 1 974 . 93 GLU N N 118.39 . 1 975 . 94 ILE H H 8.89 . 1 976 . 94 ILE HA H 4.33 . 1 977 . 94 ILE HB H 2.03 . 1 978 . 94 ILE HG12 H 1.74 . 2 979 . 94 ILE HG13 H 1.51 . 2 980 . 94 ILE HG2 H 1.06 . 1 981 . 94 ILE HD1 H 0.98 . 1 982 . 94 ILE C C 177.16 . 1 983 . 94 ILE CA C 61.07 . 1 984 . 94 ILE CB C 36.45 . 1 985 . 94 ILE CG1 C 27.63 . 1 986 . 94 ILE CG2 C 17.28 . 1 987 . 94 ILE CD1 C 11.19 . 1 988 . 94 ILE N N 122.66 . 1 989 . 95 ALA H H 8.96 . 1 990 . 95 ALA HA H 4.56 . 1 991 . 95 ALA HB H 1.35 . 1 992 . 95 ALA C C 178.46 . 1 993 . 95 ALA CA C 52.67 . 1 994 . 95 ALA CB C 18.43 . 1 995 . 95 ALA N N 128.55 . 1 996 . 96 LYS H H 9.79 . 1 997 . 96 LYS HA H 4.63 . 1 998 . 96 LYS HB2 H 2.12 . 1 999 . 96 LYS HB3 H 1.90 . 1 1000 . 96 LYS HG2 H 1.74 . 1 1001 . 96 LYS HG3 H 1.74 . 1 1002 . 96 LYS HD2 H 2.15 . 1 1003 . 96 LYS HD3 H 2.15 . 1 1004 . 96 LYS HE2 H 3.23 . 1 1005 . 96 LYS HE3 H 3.23 . 1 1006 . 96 LYS C C 178.67 . 1 1007 . 96 LYS CA C 58.04 . 1 1008 . 96 LYS CB C 32.76 . 1 1009 . 96 LYS CG C 25.31 . 1 1010 . 96 LYS CD C 28.68 . 1 1011 . 96 LYS CE C 42.05 . 1 1012 . 96 LYS N N 125.30 . 1 1013 . 97 LYS H H 8.00 . 1 1014 . 97 LYS HA H 5.67 . 1 1015 . 97 LYS HB2 H 1.94 . 2 1016 . 97 LYS HB3 H 1.87 . 2 1017 . 97 LYS HG2 H 1.47 . 1 1018 . 97 LYS HG3 H 1.47 . 1 1019 . 97 LYS HD2 H 1.98 . 1 1020 . 97 LYS HD3 H 1.98 . 1 1021 . 97 LYS HE2 H 2.97 . 1 1022 . 97 LYS HE3 H 2.97 . 1 1023 . 97 LYS C C 174.75 . 1 1024 . 97 LYS CA C 55.70 . 1 1025 . 97 LYS CB C 36.45 . 1 1026 . 97 LYS CG C 24.97 . 1 1027 . 97 LYS CD C 28.68 . 1 1028 . 97 LYS CE C 42.05 . 1 1029 . 97 LYS N N 118.90 . 1 1030 . 98 VAL H H 8.76 . 1 1031 . 98 VAL HA H 4.68 . 1 1032 . 98 VAL HB H 1.95 . 1 1033 . 98 VAL HG1 H 1.05 . 1 1034 . 98 VAL HG2 H 0.95 . 1 1035 . 98 VAL C C 173.46 . 1 1036 . 98 VAL CA C 62.04 . 1 1037 . 98 VAL CB C 36.45 . 1 1038 . 98 VAL CG1 C 21.71 . 1 1039 . 98 VAL CG2 C 21.51 . 1 1040 . 98 VAL N N 123.67 . 1 1041 . 99 THR H H 9.01 . 1 1042 . 99 THR HA H 5.49 . 1 1043 . 99 THR HB H 4.05 . 1 1044 . 99 THR HG2 H 1.33 . 1 1045 . 99 THR C C 173.76 . 1 1046 . 99 THR CA C 62.06 . 1 1047 . 99 THR CB C 69.72 . 1 1048 . 99 THR CG2 C 21.84 . 1 1049 . 99 THR N N 123.27 . 1 1050 . 100 LEU H H 9.37 . 1 1051 . 100 LEU HA H 5.74 . 1 1052 . 100 LEU HB2 H 1.46 . 1 1053 . 100 LEU HB3 H 1.80 . 1 1054 . 100 LEU HG H 1.65 . 1 1055 . 100 LEU HD1 H 0.43 . 2 1056 . 100 LEU HD2 H 0.83 . 2 1057 . 100 LEU C C 175.74 . 1 1058 . 100 LEU CA C 52.86 . 1 1059 . 100 LEU CB C 46.16 . 1 1060 . 100 LEU CG C 27.02 . 1 1061 . 100 LEU CD1 C 25.11 . 1 1062 . 100 LEU CD2 C 24.66 . 1 1063 . 100 LEU N N 126.32 . 1 1064 . 101 ALA H H 9.24 . 1 1065 . 101 ALA HA H 5.66 . 1 1066 . 101 ALA HB H 1.63 . 1 1067 . 101 ALA C C 174.58 . 1 1068 . 101 ALA CA C 49.25 . 1 1069 . 101 ALA CB C 22.13 . 1 1070 . 101 ALA N N 122.05 . 1 1071 . 102 PRO HA H 4.35 . 1 1072 . 102 PRO HB2 H 2.91 . 1 1073 . 102 PRO HB3 H 2.25 . 1 1074 . 102 PRO HG2 H 2.23 . 2 1075 . 102 PRO HG3 H 1.92 . 2 1076 . 102 PRO HD2 H 4.29 . 2 1077 . 102 PRO HD3 H 4.09 . 2 1078 . 102 PRO CA C 62.87 . 1 1079 . 102 PRO CB C 32.34 . 1 1080 . 102 PRO CG C 27.1 . 1 1081 . 102 PRO CD C 51.40 . 1 1082 . 103 ILE H H 8.56 . 1 1083 . 103 ILE HA H 4.45 . 1 1084 . 103 ILE HB H 1.93 . 1 1085 . 103 ILE HG12 H 1.65 . 2 1086 . 103 ILE HG13 H 1.06 . 2 1087 . 103 ILE HG2 H 1.03 . 1 1088 . 103 ILE HD1 H 0.96 . 1 1089 . 103 ILE C C 174.84 . 1 1090 . 103 ILE CA C 61.44 . 1 1091 . 103 ILE CB C 35.83 . 1 1092 . 103 ILE CG1 C 27.33 . 1 1093 . 103 ILE CG2 C 17.28 . 1 1094 . 103 ILE CD1 C 12.92 . 1 1095 . 103 ILE N N 124.29 . 1 1096 . 104 ILE H H 7.36 . 1 1097 . 104 ILE HA H 4.77 . 1 1098 . 104 ILE HB H 2.20 . 1 1099 . 104 ILE HG12 H 1.62 . 2 1100 . 104 ILE HG13 H 1.06 . 2 1101 . 104 ILE HG2 H 0.98 . 1 1102 . 104 ILE HD1 H 0.94 . 1 1103 . 104 ILE C C 175.14 . 1 1104 . 104 ILE CA C 59.40 . 1 1105 . 104 ILE CB C 41.77 . 1 1106 . 104 ILE CG1 C 24.73 . 1 1107 . 104 ILE CG2 C 18.21 . 1 1108 . 104 ILE CD1 C 13.32 . 1 1109 . 104 ILE N N 120.22 . 1 1110 . 105 ARG H H 8.41 . 1 1111 . 105 ARG HA H 4.50 . 1 1112 . 105 ARG HB2 H 1.98 . 1 1113 . 105 ARG HB3 H 2.18 . 1 1114 . 105 ARG HG2 H 1.90 . 1 1115 . 105 ARG HG3 H 1.90 . 1 1116 . 105 ARG HD2 H 3.48 . 1 1117 . 105 ARG HD3 H 3.48 . 1 1118 . 105 ARG C C 177.47 . 1 1119 . 105 ARG CA C 56.70 . 1 1120 . 105 ARG CB C 32.06 . 1 1121 . 105 ARG CG C 27.63 . 1 1122 . 105 ARG CD C 43.47 . 1 1123 . 105 ARG N N 120.94 . 1 1124 . 106 LYS H H 8.54 . 1 1125 . 106 LYS HA H 4.20 . 1 1126 . 106 LYS HB2 H 2.05 . 1 1127 . 106 LYS HB3 H 2.05 . 1 1128 . 106 LYS HG2 H 1.72 . 1 1129 . 106 LYS HG3 H 1.72 . 1 1130 . 106 LYS HD2 H 2.09 . 1 1131 . 106 LYS HD3 H 2.09 . 1 1132 . 106 LYS HE2 H 3.25 . 1 1133 . 106 LYS HE3 H 3.25 . 1 1134 . 106 LYS C C 176.65 . 1 1135 . 106 LYS CA C 58.86 . 1 1136 . 106 LYS CB C 32.54 . 1 1137 . 106 LYS CG C 24.69 . 1 1138 . 106 LYS CD C 28.67 . 1 1139 . 106 LYS CE C 42.04 . 1 1140 . 106 LYS N N 119.00 . 1 1141 . 107 ASP H H 8.53 . 1 1142 . 107 ASP HA H 4.73 . 1 1143 . 107 ASP HB2 H 3.10 . 1 1144 . 107 ASP HB3 H 2.83 . 1 1145 . 107 ASP C C 175.91 . 1 1146 . 107 ASP CA C 54.23 . 1 1147 . 107 ASP CB C 40.15 . 1 1148 . 107 ASP N N 115.55 . 1 1149 . 108 GLN H H 7.89 . 1 1150 . 108 GLN HA H 4.66 . 1 1151 . 108 GLN HB2 H 2.28 . 2 1152 . 108 GLN HB3 H 2.18 . 2 1153 . 108 GLN HG2 H 2.50 . 1 1154 . 108 GLN HG3 H 2.50 . 1 1155 . 108 GLN HE21 H 6.93 . 2 1156 . 108 GLN HE22 H 7.67 . 2 1157 . 108 GLN C C 174.88 . 1 1158 . 108 GLN CA C 55.57 . 1 1159 . 108 GLN CB C 31.14 . 1 1160 . 108 GLN CG C 34.50 . 1 1161 . 108 GLN CD C 180.26 . 1 1162 . 108 GLN N N 120.02 . 1 1163 . 108 GLN NE2 N 111.55 . 1 1164 . 109 ARG H H 8.23 . 1 1165 . 109 ARG HA H 4.70 . 1 1166 . 109 ARG HB2 H 1.92 . 1 1167 . 109 ARG HB3 H 1.92 . 1 1168 . 109 ARG HG2 H 1.98 . 1 1169 . 109 ARG HG3 H 1.98 . 1 1170 . 109 ARG HD2 H 3.45 . 1 1171 . 109 ARG HD3 H 3.45 . 1 1172 . 109 ARG C C 175.61 . 1 1173 . 109 ARG CA C 55.30 . 1 1174 . 109 ARG CB C 32.29 . 1 1175 . 109 ARG CG C 27.33 . 1 1176 . 109 ARG CD C 43.47 . 1 1177 . 109 ARG N N 120.02 . 1 1178 . 110 LEU H H 8.60 . 1 1179 . 110 LEU HA H 4.65 . 1 1180 . 110 LEU HB2 H 1.42 . 1 1181 . 110 LEU HB3 H 1.55 . 1 1182 . 110 LEU HG H 1.64 . 1 1183 . 110 LEU HD1 H 0.97 . 2 1184 . 110 LEU HD2 H 1.02 . 2 1185 . 110 LEU C C 175.31 . 1 1186 . 110 LEU CA C 54.49 . 1 1187 . 110 LEU CB C 43.94 . 1 1188 . 110 LEU CG C 26.72 . 1 1189 . 110 LEU CD1 C 24.37 . 1 1190 . 110 LEU CD2 C 25.37 . 1 1191 . 110 LEU N N 124.29 . 1 1192 . 111 LYS H H 8.07 . 1 1193 . 111 LYS HA H 4.57 . 1 1194 . 111 LYS HB2 H 1.91 . 1 1195 . 111 LYS HB3 H 1.79 . 1 1196 . 111 LYS HG2 H 1.55 . 1 1197 . 111 LYS HG3 H 1.55 . 1 1198 . 111 LYS HD2 H 1.91 . 1 1199 . 111 LYS HD3 H 1.91 . 1 1200 . 111 LYS HE2 H 3.20 . 1 1201 . 111 LYS HE3 H 3.20 . 1 1202 . 111 LYS C C 175.83 . 1 1203 . 111 LYS CA C 55.17 . 1 1204 . 111 LYS CB C 33.57 . 1 1205 . 111 LYS CG C 24.26 . 1 1206 . 111 LYS CD C 28.66 . 1 1207 . 111 LYS CE C 42.10 . 1 1208 . 111 LYS N N 122.25 . 1 1209 . 112 PHE H H 8.76 . 1 1210 . 112 PHE HA H 4.94 . 1 1211 . 112 PHE HB2 H 3.19 . 1 1212 . 112 PHE HB3 H 3.35 . 1 1213 . 112 PHE HD1 H 7.51 . 1 1214 . 112 PHE HD2 H 7.51 . 1 1215 . 112 PHE HE1 H 7.48 . 1 1216 . 112 PHE HE2 H 7.48 . 1 1217 . 112 PHE HZ H 7.33 . 1 1218 . 112 PHE C C 176.39 . 1 1219 . 112 PHE CA C 57.55 . 1 1220 . 112 PHE CB C 40.61 . 1 1221 . 112 PHE N N 123.26 . 1 1222 . 113 GLY H H 8.62 . 1 1223 . 113 GLY HA2 H 4.43 . 1 1224 . 113 GLY HA3 H 4.17 . 1 1225 . 113 GLY C C 174.10 . 1 1226 . 113 GLY CA C 44.66 . 1 1227 . 113 GLY N N 108.84 . 1 1228 . 114 GLU H H 8.66 . 1 1229 . 114 GLU HA H 4.49 . 1 1230 . 114 GLU HB2 H 2.27 . 1 1231 . 114 GLU HB3 H 2.27 . 1 1232 . 114 GLU HG2 H 2.61 . 1 1233 . 114 GLU HG3 H 2.61 . 1 1234 . 114 GLU C C 178.33 . 1 1235 . 114 GLU CA C 58.22 . 1 1236 . 114 GLU CB C 30.00 . 1 1237 . 114 GLU CG C 36.16 . 1 1238 . 114 GLU N N 120.22 . 1 1239 . 115 GLY H H 9.23 . 1 1240 . 115 GLY HA2 H 4.44 . 1 1241 . 115 GLY HA3 H 4.29 . 1 1242 . 115 GLY C C 176.82 . 1 1243 . 115 GLY CA C 46.23 . 1 1244 . 115 GLY N N 111.28 . 1 1245 . 116 ILE H H 7.76 . 1 1246 . 116 ILE HA H 4.37 . 1 1247 . 116 ILE HB H 2.26 . 1 1248 . 116 ILE HG12 H 1.48 . 2 1249 . 116 ILE HG13 H 1.32 . 2 1250 . 116 ILE HG2 H 1.10 . 1 1251 . 116 ILE HD1 H 0.99 . 1 1252 . 116 ILE C C 176.48 . 1 1253 . 116 ILE CA C 62.14 . 1 1254 . 116 ILE CB C 37.61 . 1 1255 . 116 ILE CG1 C 28.47 . 1 1256 . 116 ILE CG2 C 18.02 . 1 1257 . 116 ILE CD1 C 13.01 . 1 1258 . 116 ILE N N 120.93 . 1 1259 . 117 GLU H H 9.32 . 1 1260 . 117 GLU HA H 3.79 . 1 1261 . 117 GLU HB2 H 2.32 . 2 1262 . 117 GLU HB3 H 2.18 . 2 1263 . 117 GLU HG2 H 2.69 . 2 1264 . 117 GLU HG3 H 2.44 . 2 1265 . 117 GLU C C 178.50 . 1 1266 . 117 GLU CA C 61.67 . 1 1267 . 117 GLU CB C 28.38 . 1 1268 . 117 GLU CG C 37.38 . 1 1269 . 117 GLU N N 122.46 . 1 1270 . 118 GLU H H 8.21 . 1 1271 . 118 GLU HA H 4.30 . 1 1272 . 118 GLU HB2 H 2.32 . 2 1273 . 118 GLU HB3 H 2.26 . 2 1274 . 118 GLU HG2 H 2.58 . 1 1275 . 118 GLU HG3 H 2.58 . 1 1276 . 118 GLU C C 178.67 . 1 1277 . 118 GLU CA C 59.74 . 1 1278 . 118 GLU CB C 29.60 . 1 1279 . 118 GLU CG C 36.81 . 1 1280 . 118 GLU N N 118.59 . 1 1281 . 119 TYR H H 7.91 . 1 1282 . 119 TYR HA H 4.23 . 1 1283 . 119 TYR HB2 H 3.37 . 1 1284 . 119 TYR HB3 H 3.37 . 1 1285 . 119 TYR HD1 H 7.18 . 1 1286 . 119 TYR HD2 H 7.18 . 1 1287 . 119 TYR HE1 H 6.93 . 1 1288 . 119 TYR HE2 H 6.93 . 1 1289 . 119 TYR C C 178.16 . 1 1290 . 119 TYR CA C 61.94 . 1 1291 . 119 TYR CB C 38.30 . 1 1292 . 119 TYR N N 119.92 . 1 1293 . 120 VAL H H 8.73 . 1 1294 . 120 VAL HA H 3.40 . 1 1295 . 120 VAL HB H 2.12 . 1 1296 . 120 VAL HG1 H 0.78 . 1 1297 . 120 VAL HG2 H 1.12 . 1 1298 . 120 VAL C C 176.60 . 1 1299 . 120 VAL CA C 67.19 . 1 1300 . 120 VAL CB C 31.14 . 1 1301 . 120 VAL CG1 C 22.28 . 1 1302 . 120 VAL CG2 C 23.82 . 1 1303 . 120 VAL N N 118.80 . 1 1304 . 121 GLN H H 8.22 . 1 1305 . 121 GLN HA H 3.63 . 1 1306 . 121 GLN HB2 H 2.43 . 1 1307 . 121 GLN HB3 H 2.25 . 1 1308 . 121 GLN HG2 H 2.58 . 2 1309 . 121 GLN HG3 H 2.29 . 2 1310 . 121 GLN HE21 H 6.63 . 2 1311 . 121 GLN HE22 H 7.33 . 2 1312 . 121 GLN C C 177.34 . 1 1313 . 121 GLN CA C 60.92 . 1 1314 . 121 GLN CB C 28.05 . 1 1315 . 121 GLN CG C 33.11 . 1 1316 . 121 GLN CD C 179.33 . 1 1317 . 121 GLN N N 118.59 . 1 1318 . 121 GLN NE2 N 110.78 . 1 1319 . 122 ARG H H 7.65 . 1 1320 . 122 ARG HA H 4.08 . 1 1321 . 122 ARG HB2 H 2.05 . 2 1322 . 122 ARG HB3 H 2.00 . 2 1323 . 122 ARG HG2 H 2.03 . 2 1324 . 122 ARG HG3 H 1.88 . 2 1325 . 122 ARG HD2 H 3.47 . 2 1326 . 122 ARG HD3 H 3.41 . 2 1327 . 122 ARG C C 179.45 . 1 1328 . 122 ARG CA C 58.83 . 1 1329 . 122 ARG CB C 29.98 . 1 1330 . 122 ARG CG C 27.33 . 1 1331 . 122 ARG CD C 43.17 . 1 1332 . 122 ARG N N 114.43 . 1 1333 . 123 ALA H H 8.25 . 1 1334 . 123 ALA HA H 4.24 . 1 1335 . 123 ALA HB H 1.38 . 1 1336 . 123 ALA C C 179.45 . 1 1337 . 123 ALA CA C 54.13 . 1 1338 . 123 ALA CB C 18.90 . 1 1339 . 123 ALA N N 120.63 . 1 1340 . 124 LEU H H 7.86 . 1 1341 . 124 LEU HA H 4.63 . 1 1342 . 124 LEU HB2 H 1.88 . 1 1343 . 124 LEU HB3 H 1.88 . 1 1344 . 124 LEU HG H 2.03 . 1 1345 . 124 LEU HD1 H 0.76 . 2 1346 . 124 LEU HD2 H 1.04 . 2 1347 . 124 LEU C C 176.04 . 1 1348 . 124 LEU CA C 53.84 . 1 1349 . 124 LEU CB C 43.85 . 1 1350 . 124 LEU CG C 25.81 . 1 1351 . 124 LEU CD1 C 26.12 . 1 1352 . 124 LEU CD2 C 22.82 . 1 1353 . 124 LEU N N 114.53 . 1 1354 . 125 ILE H H 7.14 . 1 1355 . 125 ILE HA H 3.73 . 1 1356 . 125 ILE HB H 2.13 . 1 1357 . 125 ILE HG12 H 1.72 . 2 1358 . 125 ILE HG13 H 1.65 . 2 1359 . 125 ILE HG2 H 1.20 . 1 1360 . 125 ILE HD1 H 0.99 . 1 1361 . 125 ILE C C 176.39 . 1 1362 . 125 ILE CA C 63.31 . 1 1363 . 125 ILE CB C 37.61 . 1 1364 . 125 ILE CG1 C 28.85 . 1 1365 . 125 ILE CG2 C 17.88 . 1 1366 . 125 ILE CD1 C 13.01 . 1 1367 . 125 ILE N N 121.84 . 1 1368 . 126 ARG H H 8.91 . 1 1369 . 126 ARG HA H 4.05 . 1 1370 . 126 ARG HB2 H 2.26 . 1 1371 . 126 ARG HB3 H 1.96 . 1 1372 . 126 ARG HG2 H 2.02 . 2 1373 . 126 ARG HG3 H 1.89 . 2 1374 . 126 ARG HD2 H 3.49 . 2 1375 . 126 ARG HD3 H 3.45 . 2 1376 . 126 ARG C C 176.52 . 1 1377 . 126 ARG CA C 59.04 . 1 1378 . 126 ARG CB C 28.77 . 1 1379 . 126 ARG CG C 27.33 . 1 1380 . 126 ARG CD C 43.17 . 1 1381 . 126 ARG N N 118.60 . 1 1382 . 127 ARG H H 9.06 . 1 1383 . 127 ARG HA H 4.85 . 1 1384 . 127 ARG HB2 H 2.09 . 2 1385 . 127 ARG HB3 H 1.98 . 2 1386 . 127 ARG HG2 H 1.88 . 1 1387 . 127 ARG HG3 H 1.88 . 1 1388 . 127 ARG HD2 H 3.46 . 1 1389 . 127 ARG HD3 H 3.46 . 1 1390 . 127 ARG C C 176.33 . 1 1391 . 127 ARG CA C 54.24 . 1 1392 . 127 ARG CB C 30.68 . 1 1393 . 127 ARG CG C 27.03 . 1 1394 . 127 ARG CD C 43.47 . 1 1395 . 127 ARG N N 124.08 . 1 1396 . 128 PRO HA H 6.05 . 1 1397 . 128 PRO HB2 H 2.06 . 2 1398 . 128 PRO HB3 H 1.89 . 2 1399 . 128 PRO HG2 H 2.28 . 2 1400 . 128 PRO HG3 H 2.13 . 2 1401 . 128 PRO HD2 H 4.45 . 2 1402 . 128 PRO HD3 H 4.11 . 2 1403 . 128 PRO CA C 60.65 . 1 1404 . 128 PRO CB C 32.71 . 1 1405 . 128 PRO CG C 26.87 . 1 1406 . 128 PRO CD C 50.00 . 1 1407 . 129 MET H H 9.41 . 1 1408 . 129 MET HA H 4.74 . 1 1409 . 129 MET HB2 H 2.56 . 1 1410 . 129 MET HB3 H 2.01 . 1 1411 . 129 MET HG2 H 2.21 . 1 1412 . 129 MET HG3 H 2.21 . 1 1413 . 129 MET HE H 1.98 . 1 1414 . 129 MET C C 172.64 . 1 1415 . 129 MET CA C 56.18 . 1 1416 . 129 MET CB C 34.60 . 1 1417 . 129 MET CG C 29.6 . 1 1418 . 129 MET CE C 17.37 . 1 1419 . 129 MET N N 115.14 . 1 1420 . 130 LEU H H 8.67 . 1 1421 . 130 LEU HA H 4.93 . 1 1422 . 130 LEU HB2 H 1.76 . 2 1423 . 130 LEU HB3 H 1.57 . 2 1424 . 130 LEU HG H 1.77 . 1 1425 . 130 LEU HD1 H 0.95 . 1 1426 . 130 LEU HD2 H 0.92 . 1 1427 . 130 LEU C C 176.60 . 1 1428 . 130 LEU CA C 52.78 . 1 1429 . 130 LEU CB C 46.62 . 1 1430 . 130 LEU CG C 27.33 . 1 1431 . 130 LEU CD1 C 24.61 . 1 1432 . 130 LEU CD2 C 24.84 . 1 1433 . 130 LEU N N 120.43 . 1 1434 . 131 GLU H H 8.77 . 1 1435 . 131 GLU HA H 3.86 . 1 1436 . 131 GLU HB2 H 2.18 . 1 1437 . 131 GLU HB3 H 2.36 . 1 1438 . 131 GLU HG2 H 2.57 . 2 1439 . 131 GLU HG3 H 2.38 . 2 1440 . 131 GLU C C 176.26 . 1 1441 . 131 GLU CA C 59.80 . 1 1442 . 131 GLU CB C 30.68 . 1 1443 . 131 GLU CG C 38.47 . 1 1444 . 131 GLU N N 121.84 . 1 1445 . 132 GLN H H 9.33 . 1 1446 . 132 GLN HA H 3.81 . 1 1447 . 132 GLN HB2 H 2.57 . 1 1448 . 132 GLN HB3 H 2.57 . 1 1449 . 132 GLN HG2 H 2.97 . 2 1450 . 132 GLN HG3 H 2.74 . 2 1451 . 132 GLN HE21 H 7.00 . 2 1452 . 132 GLN HE22 H 7.87 . 2 1453 . 132 GLN C C 176.48 . 1 1454 . 132 GLN CA C 59.69 . 1 1455 . 132 GLN CB C 26.29 . 1 1456 . 132 GLN CG C 34.47 . 1 1457 . 132 GLN CD C 180.65 . 1 1458 . 132 GLN N N 114.94 . 1 1459 . 132 GLN NE2 N 112.35 . 1 1460 . 133 ASP H H 8.70 . 1 1461 . 133 ASP HA H 4.51 . 1 1462 . 133 ASP HB2 H 2.66 . 1 1463 . 133 ASP HB3 H 3.17 . 1 1464 . 133 ASP C C 176.04 . 1 1465 . 133 ASP CA C 56.77 . 1 1466 . 133 ASP CB C 42.46 . 1 1467 . 133 ASP N N 121.64 . 1 1468 . 134 ASN H H 8.61 . 1 1469 . 134 ASN HA H 6.16 . 1 1470 . 134 ASN HB2 H 2.52 . 1 1471 . 134 ASN HB3 H 3.24 . 1 1472 . 134 ASN HD21 H 8.02 . 1 1473 . 134 ASN HD22 H 7.77 . 1 1474 . 134 ASN C C 176.17 . 1 1475 . 134 ASN CA C 52.08 . 1 1476 . 134 ASN CB C 39.23 . 1 1477 . 134 ASN N N 116.16 . 1 1478 . 134 ASN ND2 N 111.68 . 1 1479 . 135 ILE H H 9.81 . 1 1480 . 135 ILE HA H 4.91 . 1 1481 . 135 ILE HB H 1.99 . 1 1482 . 135 ILE HG12 H 1.67 . 2 1483 . 135 ILE HG13 H 1.24 . 2 1484 . 135 ILE HG2 H 1.07 . 1 1485 . 135 ILE HD1 H 0.93 . 1 1486 . 135 ILE C C 173.76 . 1 1487 . 135 ILE CA C 59.80 . 1 1488 . 135 ILE CB C 43.38 . 1 1489 . 135 ILE CG1 C 26.18 . 1 1490 . 135 ILE CG2 C 17.89 . 1 1491 . 135 ILE CD1 C 14.84 . 1 1492 . 135 ILE N N 116.77 . 1 1493 . 136 SER H H 8.70 . 1 1494 . 136 SER HA H 5.28 . 1 1495 . 136 SER HB2 H 4.05 . 1 1496 . 136 SER HB3 H 4.05 . 1 1497 . 136 SER C C 174.02 . 1 1498 . 136 SER CA C 56.67 . 1 1499 . 136 SER CB C 65.56 . 1 1500 . 136 SER N N 117.58 . 1 1501 . 137 VAL H H 9.31 . 1 1502 . 137 VAL HA H 4.71 . 1 1503 . 137 VAL HB H 2.44 . 1 1504 . 137 VAL HG1 H 1.13 . 1 1505 . 137 VAL HG2 H 0.95 . 1 1506 . 137 VAL C C 174.24 . 1 1507 . 137 VAL CA C 59.46 . 1 1508 . 137 VAL CB C 33.13 . 1 1509 . 137 VAL CG1 C 21.71 . 1 1510 . 137 VAL CG2 C 21.02 . 1 1511 . 137 VAL N N 125.09 . 1 1512 . 138 PRO HA H 4.63 . 1 1513 . 138 PRO HB2 H 2.51 . 1 1514 . 138 PRO HB3 H 2.17 . 1 1515 . 138 PRO HG2 H 2.21 . 1 1516 . 138 PRO HG3 H 2.21 . 1 1517 . 138 PRO HD2 H 3.92 . 2 1518 . 138 PRO HD3 H 3.83 . 2 1519 . 138 PRO CA C 63.84 . 1 1520 . 138 PRO CB C 32.25 . 1 1521 . 138 PRO CG C 27.33 . 1 1522 . 138 PRO CD C 50.53 . 1 1523 . 139 GLY H H 8.93 . 1 1524 . 139 GLY HA2 H 4.00 . 1 1525 . 139 GLY HA3 H 4.36 . 1 1526 . 139 GLY C C 175.44 . 1 1527 . 139 GLY CA C 46.16 . 1 1528 . 139 GLY N N 110.26 . 1 1529 . 140 LEU H H 7.77 . 1 1530 . 140 LEU HA H 4.75 . 1 1531 . 140 LEU HB2 H 2.00 . 1 1532 . 140 LEU HB3 H 1.72 . 1 1533 . 140 LEU HG H 1.77 . 1 1534 . 140 LEU HD1 H 1.03 . 1 1535 . 140 LEU HD2 H 1.03 . 1 1536 . 140 LEU C C 176.13 . 1 1537 . 140 LEU CA C 54.91 . 1 1538 . 140 LEU CB C 42.92 . 1 1539 . 140 LEU CG C 26.92 . 1 1540 . 140 LEU CD1 C 24.82 . 1 1541 . 140 LEU CD2 C 24.82 . 1 1542 . 140 LEU N N 121.24 . 1 1543 . 141 THR H H 8.49 . 1 1544 . 141 THR HA H 4.87 . 1 1545 . 141 THR HB H 4.31 . 1 1546 . 141 THR HG2 H 1.32 . 1 1547 . 141 THR C C 173.76 . 1 1548 . 141 THR CA C 61.16 . 1 1549 . 141 THR CB C 71.41 . 1 1550 . 141 THR CG2 C 21.11 . 1 1551 . 141 THR N N 119.00 . 1 1552 . 142 LEU H H 8.44 . 1 1553 . 142 LEU HA H 4.74 . 1 1554 . 142 LEU HB2 H 1.79 . 2 1555 . 142 LEU HB3 H 1.71 . 2 1556 . 142 LEU HG H 1.80 . 1 1557 . 142 LEU HD1 H 1.08 . 2 1558 . 142 LEU HD2 H 1.11 . 2 1559 . 142 LEU C C 176.39 . 1 1560 . 142 LEU CA C 54.62 . 1 1561 . 142 LEU CB C 44.08 . 1 1562 . 142 LEU CG C 27.03 . 1 1563 . 142 LEU CD1 C 24.44 . 1 1564 . 142 LEU CD2 C 25.20 . 1 1565 . 142 LEU N N 124.08 . 1 1566 . 143 ALA H H 8.83 . 1 1567 . 143 ALA HA H 4.35 . 1 1568 . 143 ALA HB H 1.61 . 1 1569 . 143 ALA C C 177.98 . 1 1570 . 143 ALA CA C 53.26 . 1 1571 . 143 ALA CB C 18.20 . 1 1572 . 143 ALA N N 125.71 . 1 1573 . 144 GLY H H 8.60 . 1 1574 . 144 GLY HA2 H 4.33 . 1 1575 . 144 GLY HA3 H 3.92 . 1 1576 . 144 GLY C C 174.49 . 1 1577 . 144 GLY CA C 45.93 . 1 1578 . 144 GLY N N 107.22 . 1 1579 . 145 GLN H H 8.27 . 1 1580 . 145 GLN HA H 4.80 . 1 1581 . 145 GLN HB2 H 2.41 . 1 1582 . 145 GLN HB3 H 2.27 . 1 1583 . 145 GLN HG2 H 2.56 . 1 1584 . 145 GLN HG3 H 2.56 . 1 1585 . 145 GLN HE21 H 6.95 . 2 1586 . 145 GLN HE22 H 7.67 . 2 1587 . 145 GLN C C 175.83 . 1 1588 . 145 GLN CA C 55.40 . 1 1589 . 145 GLN CB C 30.22 . 1 1590 . 145 GLN CG C 33.67 . 1 1591 . 145 GLN CD C 180.26 . 1 1592 . 145 GLN N N 119.20 . 1 1593 . 145 GLN NE2 N 111.64 . 1 1594 . 146 THR H H 8.42 . 1 1595 . 146 THR HA H 4.69 . 1 1596 . 146 THR HB H 4.42 . 1 1597 . 146 THR HG2 H 1.46 . 1 1598 . 146 THR C C 175.05 . 1 1599 . 146 THR CA C 62.21 . 1 1600 . 146 THR CB C 69.95 . 1 1601 . 146 THR CG2 C 21.35 . 1 1602 . 146 THR N N 115.55 . 1 1603 . 147 GLY H H 8.62 . 1 1604 . 147 GLY HA2 H 4.14 . 1 1605 . 147 GLY HA3 H 4.18 . 1 1606 . 147 GLY C C 173.59 . 1 1607 . 147 GLY CA C 46.03 . 1 1608 . 147 GLY N N 111.89 . 1 1609 . 148 LEU H H 8.05 . 1 1610 . 148 LEU HA H 4.53 . 1 1611 . 148 LEU HB2 H 1.72 . 2 1612 . 148 LEU HB3 H 1.59 . 2 1613 . 148 LEU HG H 1.43 . 1 1614 . 148 LEU HD1 H 0.89 . 2 1615 . 148 LEU HD2 H 0.90 . 2 1616 . 148 LEU C C 175.44 . 1 1617 . 148 LEU CA C 55.34 . 1 1618 . 148 LEU CB C 43.89 . 1 1619 . 148 LEU CG C 26.72 . 1 1620 . 148 LEU CD1 C 23.79 . 1 1621 . 148 LEU CD2 C 23.98 . 1 1622 . 148 LEU N N 122.35 . 1 1623 . 149 LEU H H 8.80 . 1 1624 . 149 LEU HA H 5.22 . 1 1625 . 149 LEU HB2 H 1.51 . 1 1626 . 149 LEU HB3 H 1.85 . 1 1627 . 149 LEU HG H 1.87 . 1 1628 . 149 LEU HD1 H 1.02 . 2 1629 . 149 LEU HD2 H 1.10 . 2 1630 . 149 LEU C C 175.35 . 1 1631 . 149 LEU CA C 53.55 . 1 1632 . 149 LEU CB C 45.92 . 1 1633 . 149 LEU CG C 27.03 . 1 1634 . 149 LEU CD1 C 24.12 . 1 1635 . 149 LEU CD2 C 25.69 . 1 1636 . 149 LEU N N 126.52 . 1 1637 . 150 PHE H H 9.28 . 1 1638 . 150 PHE HA H 5.23 . 1 1639 . 150 PHE HB2 H 2.88 . 1 1640 . 150 PHE HB3 H 2.88 . 1 1641 . 150 PHE HD1 H 7.13 . 1 1642 . 150 PHE HD2 H 7.13 . 1 1643 . 150 PHE HE1 H 7.30 . 1 1644 . 150 PHE HE2 H 7.30 . 1 1645 . 150 PHE HZ H 7.33 . 1 1646 . 150 PHE C C 174.40 . 1 1647 . 150 PHE CA C 56.38 . 1 1648 . 150 PHE CB C 43.38 . 1 1649 . 150 PHE N N 116.97 . 1 1650 . 151 LYS H H 9.80 . 1 1651 . 151 LYS HA H 5.33 . 1 1652 . 151 LYS HB2 H 1.88 . 1 1653 . 151 LYS HB3 H 1.88 . 1 1654 . 151 LYS HG2 H 1.57 . 1 1655 . 151 LYS HG3 H 1.57 . 1 1656 . 151 LYS HD2 H 1.87 . 1 1657 . 151 LYS HD3 H 1.87 . 1 1658 . 151 LYS HE2 H 3.09 . 1 1659 . 151 LYS HE3 H 3.09 . 1 1660 . 151 LYS C C 176.65 . 1 1661 . 151 LYS CA C 54.52 . 1 1662 . 151 LYS CB C 34.37 . 1 1663 . 151 LYS CG C 24.79 . 1 1664 . 151 LYS CD C 28.77 . 1 1665 . 151 LYS CE C 42.06 . 1 1666 . 151 LYS N N 122.05 . 1 1667 . 152 VAL H H 9.42 . 1 1668 . 152 VAL HA H 4.37 . 1 1669 . 152 VAL HB H 2.62 . 1 1670 . 152 VAL HG1 H 0.89 . 1 1671 . 152 VAL HG2 H 1.11 . 1 1672 . 152 VAL C C 176.00 . 1 1673 . 152 VAL CA C 62.24 . 1 1674 . 152 VAL CB C 29.98 . 1 1675 . 152 VAL CG1 C 22.86 . 1 1676 . 152 VAL CG2 C 21.34 . 1 1677 . 152 VAL N N 127.54 . 1 1678 . 153 VAL H H 8.62 . 1 1679 . 153 VAL HA H 4.13 . 1 1680 . 153 VAL HB H 2.16 . 1 1681 . 153 VAL HG1 H 1.17 . 1 1682 . 153 VAL HG2 H 1.11 . 1 1683 . 153 VAL C C 176.00 . 1 1684 . 153 VAL CA C 64.48 . 1 1685 . 153 VAL CB C 32.53 . 1 1686 . 153 VAL CG1 C 21.87 . 1 1687 . 153 VAL CG2 C 21.32 . 1 1688 . 153 VAL N N 127.33 . 1 1689 . 154 LYS H H 7.66 . 1 1690 . 154 LYS HA H 4.92 . 1 1691 . 154 LYS HB2 H 1.95 . 1 1692 . 154 LYS HB3 H 1.95 . 1 1693 . 154 LYS HG2 H 1.60 . 1 1694 . 154 LYS HG3 H 1.60 . 1 1695 . 154 LYS HD2 H 1.98 . 1 1696 . 154 LYS HD3 H 1.98 . 1 1697 . 154 LYS HE2 H 2.97 . 1 1698 . 154 LYS HE3 H 2.97 . 1 1699 . 154 LYS C C 175.10 . 1 1700 . 154 LYS CA C 55.85 . 1 1701 . 154 LYS CB C 36.45 . 1 1702 . 154 LYS CG C 24.88 . 1 1703 . 154 LYS CD C 28.77 . 1 1704 . 154 LYS CE C 42.06 . 1 1705 . 154 LYS N N 116.16 . 1 1706 . 155 THR H H 9.42 . 1 1707 . 155 THR HA H 5.13 . 1 1708 . 155 THR HB H 4.39 . 1 1709 . 155 THR HG2 H 1.24 . 1 1710 . 155 THR C C 172.16 . 1 1711 . 155 THR CA C 60.87 . 1 1712 . 155 THR CB C 72.03 . 1 1713 . 155 THR CG2 C 21.53 . 1 1714 . 155 THR N N 116.56 . 1 1715 . 156 LEU H H 8.52 . 1 1716 . 156 LEU HA H 4.79 . 1 1717 . 156 LEU HB2 H 1.71 . 1 1718 . 156 LEU HB3 H 1.90 . 1 1719 . 156 LEU HG H 1.73 . 1 1720 . 156 LEU HD1 H 1.18 . 1 1721 . 156 LEU HD2 H 1.18 . 1 1722 . 156 LEU CA C 52.46 . 1 1723 . 156 LEU CB C 45.46 . 1 1724 . 156 LEU CG C 27.33 . 1 1725 . 156 LEU CD1 C 24.48 . 1 1726 . 156 LEU CD2 C 24.56 . 1 1727 . 156 LEU N N 121.24 . 1 1728 . 157 PRO HA H 4.93 . 1 1729 . 157 PRO HB2 H 2.19 . 1 1730 . 157 PRO HB3 H 2.67 . 1 1731 . 157 PRO HG2 H 2.12 . 2 1732 . 157 PRO HG3 H 1.83 . 2 1733 . 157 PRO HD2 H 3.82 . 2 1734 . 157 PRO HD3 H 3.76 . 2 1735 . 157 PRO CA C 63.38 . 1 1736 . 157 PRO CB C 34.60 . 1 1737 . 157 PRO CG C 24.78 . 1 1738 . 157 PRO CD C 50.71 . 1 1739 . 158 SER H H 8.82 . 1 1740 . 158 SER HA H 4.75 . 1 1741 . 158 SER HB2 H 4.06 . 1 1742 . 158 SER HB3 H 4.33 . 1 1743 . 158 SER C C 175.65 . 1 1744 . 158 SER CA C 58.14 . 1 1745 . 158 SER CB C 65.10 . 1 1746 . 158 SER N N 116.57 . 1 1747 . 159 LYS H H 7.93 . 1 1748 . 159 LYS HA H 3.93 . 1 1749 . 159 LYS HB2 H 2.27 . 1 1750 . 159 LYS HB3 H 2.27 . 1 1751 . 159 LYS HG2 H 1.63 . 1 1752 . 159 LYS HG3 H 1.63 . 1 1753 . 159 LYS HD2 H 1.93 . 2 1754 . 159 LYS HD3 H 1.83 . 2 1755 . 159 LYS HE2 H 3.28 . 1 1756 . 159 LYS HE3 H 3.28 . 1 1757 . 159 LYS C C 174.96 . 1 1758 . 159 LYS CA C 59.99 . 1 1759 . 159 LYS CB C 30.45 . 1 1760 . 159 LYS CG C 25.49 . 1 1761 . 159 LYS CD C 29.17 . 1 1762 . 159 LYS CE C 42.13 . 1 1763 . 159 LYS N N 117.78 . 1 1764 . 160 VAL H H 7.51 . 1 1765 . 160 VAL HA H 4.94 . 1 1766 . 160 VAL HB H 2.45 . 1 1767 . 160 VAL HG1 H 1.16 . 1 1768 . 160 VAL HG2 H 0.81 . 1 1769 . 160 VAL C C 176.25 . 1 1770 . 160 VAL CA C 58.23 . 1 1771 . 160 VAL CB C 33.22 . 1 1772 . 160 VAL CG1 C 21.54 . 1 1773 . 160 VAL CG2 C 17.65 . 1 1774 . 160 VAL N N 112.10 . 1 1775 . 161 PRO HA H 4.67 . 1 1776 . 161 PRO HB2 H 2.54 . 1 1777 . 161 PRO HB3 H 2.09 . 1 1778 . 161 PRO HG2 H 2.27 . 1 1779 . 161 PRO HG3 H 2.27 . 1 1780 . 161 PRO HD2 H 4.11 . 2 1781 . 161 PRO HD3 H 4.06 . 2 1782 . 161 PRO CA C 64.00 . 1 1783 . 161 PRO CB C 31.80 . 1 1784 . 161 PRO CG C 27.03 . 1 1785 . 161 PRO CD C 50.65 . 1 1786 . 162 VAL H H 8.95 . 1 1787 . 162 VAL HA H 6.06 . 1 1788 . 162 VAL HB H 2.30 . 1 1789 . 162 VAL HG1 H 1.17 . 1 1790 . 162 VAL HG2 H 0.99 . 1 1791 . 162 VAL C C 174.92 . 1 1792 . 162 VAL CA C 58.14 . 1 1793 . 162 VAL CB C 36.68 . 1 1794 . 162 VAL CG1 C 21.70 . 1 1795 . 162 VAL CG2 C 18.23 . 1 1796 . 162 VAL N N 117.37 . 1 1797 . 163 GLU H H 8.51 . 1 1798 . 163 GLU HA H 5.69 . 1 1799 . 163 GLU HB2 H 1.79 . 2 1800 . 163 GLU HB3 H 1.71 . 2 1801 . 163 GLU HG2 H 2.04 . 2 1802 . 163 GLU HG3 H 1.97 . 2 1803 . 163 GLU C C 175.40 . 1 1804 . 163 GLU CA C 53.65 . 1 1805 . 163 GLU CB C 35.07 . 1 1806 . 163 GLU CG C 36.30 . 1 1807 . 163 GLU N N 114.33 . 1 1808 . 164 ILE H H 7.55 . 1 1809 . 164 ILE HA H 4.25 . 1 1810 . 164 ILE HB H 2.63 . 1 1811 . 164 ILE HG12 H 1.98 . 2 1812 . 164 ILE HG13 H 1.67 . 2 1813 . 164 ILE HG2 H 1.12 . 1 1814 . 164 ILE HD1 H 0.96 . 1 1815 . 164 ILE C C 177.16 . 1 1816 . 164 ILE CA C 60.58 . 1 1817 . 164 ILE CB C 35.11 . 1 1818 . 164 ILE CG1 C 27.94 . 1 1819 . 164 ILE CG2 C 17.58 . 1 1820 . 164 ILE CD1 C 11.38 . 1 1821 . 164 ILE N N 121.44 . 1 1822 . 165 GLY H H 9.61 . 1 1823 . 165 GLY HA2 H 4.92 . 1 1824 . 165 GLY HA3 H 4.02 . 1 1825 . 165 GLY C C 174.32 . 1 1826 . 165 GLY CA C 43.78 . 1 1827 . 165 GLY N N 119.00 . 1 1828 . 166 GLU H H 9.19 . 1 1829 . 166 GLU HA H 4.08 . 1 1830 . 166 GLU HB2 H 2.23 . 1 1831 . 166 GLU HB3 H 2.23 . 1 1832 . 166 GLU HG2 H 2.59 . 1 1833 . 166 GLU HG3 H 2.59 . 1 1834 . 166 GLU C C 177.98 . 1 1835 . 166 GLU CA C 60.09 . 1 1836 . 166 GLU CB C 29.75 . 1 1837 . 166 GLU CG C 36.77 . 1 1838 . 166 GLU N N 119.41 . 1 1839 . 167 GLU H H 9.24 . 1 1840 . 167 GLU HA H 4.63 . 1 1841 . 167 GLU HB2 H 2.38 . 2 1842 . 167 GLU HB3 H 2.18 . 2 1843 . 167 GLU HG2 H 2.42 . 1 1844 . 167 GLU HG3 H 2.42 . 1 1845 . 167 GLU C C 176.91 . 1 1846 . 167 GLU CA C 56.08 . 1 1847 . 167 GLU CB C 29.95 . 1 1848 . 167 GLU CG C 36.47 . 1 1849 . 167 GLU N N 114.74 . 1 1850 . 168 THR H H 7.64 . 1 1851 . 168 THR HA H 4.01 . 1 1852 . 168 THR HB H 4.20 . 1 1853 . 168 THR HG2 H 1.23 . 1 1854 . 168 THR C C 173.80 . 1 1855 . 168 THR CA C 64.59 . 1 1856 . 168 THR CB C 69.49 . 1 1857 . 168 THR CG2 C 23.93 . 1 1858 . 168 THR N N 119.41 . 1 1859 . 169 LYS H H 7.99 . 1 1860 . 169 LYS HA H 4.68 . 1 1861 . 169 LYS HB2 H 2.11 . 2 1862 . 169 LYS HB3 H 2.04 . 2 1863 . 169 LYS HG2 H 1.68 . 1 1864 . 169 LYS HG3 H 1.68 . 1 1865 . 169 LYS HD2 H 1.95 . 1 1866 . 169 LYS HD3 H 1.95 . 1 1867 . 169 LYS HE2 H 3.26 . 1 1868 . 169 LYS HE3 H 3.26 . 1 1869 . 169 LYS C C 174.84 . 1 1870 . 169 LYS CA C 55.40 . 1 1871 . 169 LYS CB C 32.99 . 1 1872 . 169 LYS CG C 24.75 . 1 1873 . 169 LYS CD C 28.73 . 1 1874 . 169 LYS CE C 42.16 . 1 1875 . 169 LYS N N 127.54 . 1 1876 . 170 ILE H H 8.83 . 1 1877 . 170 ILE HA H 4.98 . 1 1878 . 170 ILE HB H 2.04 . 1 1879 . 170 ILE HG12 H 1.44 . 2 1880 . 170 ILE HG13 H 1.37 . 2 1881 . 170 ILE HG2 H 0.80 . 1 1882 . 170 ILE HD1 H 0.82 . 1 1883 . 170 ILE C C 174.84 . 1 1884 . 170 ILE CA C 58.72 . 1 1885 . 170 ILE CB C 38.30 . 1 1886 . 170 ILE CG1 C 27.03 . 1 1887 . 170 ILE CG2 C 16.98 . 1 1888 . 170 ILE CD1 C 11.49 . 1 1889 . 170 ILE N N 126.22 . 1 1890 . 171 GLU H H 8.89 . 1 1891 . 171 GLU HA H 4.93 . 1 1892 . 171 GLU HB2 H 2.05 . 1 1893 . 171 GLU HB3 H 2.23 . 1 1894 . 171 GLU HG2 H 2.47 . 2 1895 . 171 GLU HG3 H 2.22 . 2 1896 . 171 GLU C C 174.79 . 1 1897 . 171 GLU CA C 54.23 . 1 1898 . 171 GLU CB C 32.99 . 1 1899 . 171 GLU CG C 36.16 . 1 1900 . 171 GLU N N 127.33 . 1 1901 . 172 ILE H H 9.30 . 1 1902 . 172 ILE HA H 4.94 . 1 1903 . 172 ILE HB H 1.89 . 1 1904 . 172 ILE HG12 H 1.51 . 2 1905 . 172 ILE HG13 H 0.98 . 2 1906 . 172 ILE HG2 H 0.88 . 1 1907 . 172 ILE HD1 H 0.64 . 1 1908 . 172 ILE C C 176.04 . 1 1909 . 172 ILE CA C 59.56 . 1 1910 . 172 ILE CB C 38.53 . 1 1911 . 172 ILE CG1 C 27.63 . 1 1912 . 172 ILE CG2 C 17.58 . 1 1913 . 172 ILE CD1 C 13.22 . 1 1914 . 172 ILE N N 126.15 . 1 1915 . 173 ARG H H 9.06 . 1 1916 . 173 ARG HA H 4.72 . 1 1917 . 173 ARG HB2 H 2.36 . 1 1918 . 173 ARG HB3 H 2.06 . 1 1919 . 173 ARG HG2 H 1.99 . 1 1920 . 173 ARG HG3 H 1.99 . 1 1921 . 173 ARG HD2 H 3.38 . 1 1922 . 173 ARG HD3 H 3.38 . 1 1923 . 173 ARG C C 175.14 . 1 1924 . 173 ARG CA C 55.11 . 1 1925 . 173 ARG CB C 31.60 . 1 1926 . 173 ARG CG C 26.72 . 1 1927 . 173 ARG CD C 43.17 . 1 1928 . 173 ARG N N 127.94 . 1 1929 . 174 GLU H H 8.62 . 1 1930 . 174 GLU HA H 4.50 . 1 1931 . 174 GLU HB2 H 2.39 . 2 1932 . 174 GLU HB3 H 2.22 . 2 1933 . 174 GLU HG2 H 2.55 . 2 1934 . 174 GLU HG3 H 2.48 . 2 1935 . 174 GLU C C 176.91 . 1 1936 . 174 GLU CA C 57.60 . 1 1937 . 174 GLU CB C 30.86 . 1 1938 . 174 GLU CG C 36.19 . 1 1939 . 174 GLU N N 119.31 . 1 1940 . 175 GLU H H 8.11 . 1 1941 . 175 GLU HA H 4.77 . 1 1942 . 175 GLU HB2 H 2.20 . 2 1943 . 175 GLU HB3 H 2.17 . 2 1944 . 175 GLU HG2 H 2.64 . 2 1945 . 175 GLU HG3 H 2.48 . 2 1946 . 175 GLU CA C 54.47 . 1 1947 . 175 GLU CB C 29.75 . 1 1948 . 175 GLU CG C 36.05 . 1 1949 . 175 GLU N N 118.80 . 1 1950 . 176 PRO HA H 4.73 . 1 1951 . 176 PRO HB2 H 2.14 . 1 1952 . 176 PRO HB3 H 2.54 . 1 1953 . 176 PRO HG2 H 2.31 . 2 1954 . 176 PRO HG3 H 2.22 . 2 1955 . 176 PRO HD2 H 4.24 . 2 1956 . 176 PRO HD3 H 3.89 . 2 1957 . 176 PRO CA C 62.71 . 1 1958 . 176 PRO CB C 32.99 . 1 1959 . 176 PRO CG C 27.94 . 1 1960 . 176 PRO CD C 50.78 . 1 1961 . 177 ALA H H 8.69 . 1 1962 . 177 ALA HA H 4.42 . 1 1963 . 177 ALA HB H 1.49 . 1 1964 . 177 ALA C C 177.81 . 1 1965 . 177 ALA CA C 53.06 . 1 1966 . 177 ALA CB C 19.36 . 1 1967 . 177 ALA N N 124.49 . 1 1968 . 178 SER H H 8.39 . 1 1969 . 178 SER HA H 4.52 . 1 1970 . 178 SER HB2 H 4.12 . 1 1971 . 178 SER HB3 H 4.12 . 1 1972 . 178 SER C C 175.22 . 1 1973 . 178 SER CA C 59.31 . 1 1974 . 178 SER CB C 63.71 . 1 1975 . 178 SER N N 113.31 . 1 1976 . 179 GLU H H 8.49 . 1 1977 . 179 GLU HA H 4.48 . 1 1978 . 179 GLU HB2 H 2.33 . 2 1979 . 179 GLU HB3 H 2.18 . 2 1980 . 179 GLU HG2 H 2.53 . 1 1981 . 179 GLU HG3 H 2.53 . 1 1982 . 179 GLU C C 177.04 . 1 1983 . 179 GLU CA C 57.32 . 1 1984 . 179 GLU CB C 30.53 . 1 1985 . 179 GLU CG C 36.20 . 1 1986 . 179 GLU N N 122.25 . 1 1987 . 180 VAL H H 8.09 . 1 1988 . 180 VAL HA H 4.20 . 1 1989 . 180 VAL HB H 2.26 . 1 1990 . 180 VAL HG1 H 1.15 . 1 1991 . 180 VAL HG2 H 1.15 . 1 1992 . 180 VAL C C 176.56 . 1 1993 . 180 VAL CA C 63.12 . 1 1994 . 180 VAL CB C 32.53 . 1 1995 . 180 VAL CG1 C 21.54 . 1 1996 . 180 VAL CG2 C 21.24 . 1 1997 . 180 VAL N N 120.02 . 1 1998 . 181 LEU H H 8.30 . 1 1999 . 181 LEU HA H 4.51 . 1 2000 . 181 LEU HB2 H 1.77 . 1 2001 . 181 LEU HB3 H 1.83 . 1 2002 . 181 LEU HG H 1.84 . 1 2003 . 181 LEU HD1 H 1.08 . 2 2004 . 181 LEU HD2 H 1.11 . 2 2005 . 181 LEU C C 177.21 . 1 2006 . 181 LEU CA C 55.60 . 1 2007 . 181 LEU CB C 42.46 . 1 2008 . 181 LEU CG C 27.03 . 1 2009 . 181 LEU CD1 C 23.54 . 1 2010 . 181 LEU CD2 C 24.89 . 1 2011 . 181 LEU N N 124.08 . 1 2012 . 182 GLU H H 8.31 . 1 2013 . 182 GLU HA H 4.50 . 1 2014 . 182 GLU HB2 H 2.28 . 2 2015 . 182 GLU HB3 H 2.16 . 2 2016 . 182 GLU HG2 H 2.51 . 1 2017 . 182 GLU HG3 H 2.51 . 1 2018 . 182 GLU C C 175.61 . 1 2019 . 182 GLU CA C 56.83 . 1 2020 . 182 GLU CB C 30.45 . 1 2021 . 182 GLU CG C 36.20 . 1 2022 . 182 GLU N N 121.44 . 1 2023 . 183 GLU H H 8.06 . 1 2024 . 183 GLU HA H 4.48 . 1 2025 . 183 GLU HB2 H 2.32 . 2 2026 . 183 GLU HB3 H 2.15 . 2 2027 . 183 GLU HG2 H 2.52 . 1 2028 . 183 GLU HG3 H 2.52 . 1 2029 . 183 GLU C C 177.34 . 1 2030 . 183 GLU CA C 57.24 . 1 2031 . 183 GLU CB C 30.45 . 1 2032 . 183 GLU CG C 36.20 . 1 2033 . 183 GLU N N 125.91 . 1 2034 . 184 GLY H H 8.58 . 1 2035 . 184 GLY HA2 H 4.21 . 2 2036 . 184 GLY HA3 H 4.17 . 2 2037 . 184 GLY C C 175.01 . 1 2038 . 184 GLY CA C 45.83 . 1 2039 . 184 GLY N N 109.66 . 1 2040 . 185 GLY H H 8.38 . 1 2041 . 185 GLY HA2 H 4.16 . 2 2042 . 185 GLY HA3 H 4.08 . 2 2043 . 185 GLY C C 174.30 . 1 2044 . 185 GLY CA C 45.48 . 1 2045 . 185 GLY N N 108.23 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details ; 3JHNHA couplings measured from ratio of cross to diagonal peaks in an HNHA experiment. ; loop_ _Sample_label $VATN_sample_N15 stop_ _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H . _Mol_system_component_name VATN _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 6 GLY H 6 GLY HA2 2.0 . . . 2 3JHNHA 6 GLY H 6 GLY HA3 8.0 . . . 3 3JHNHA 7 ILE H 7 ILE HA 9.3 . . . 4 3JHNHA 8 ILE H 8 ILE HA 8.6 . . . 5 3JHNHA 9 LEU H 9 LEU HA 8.6 . . . 6 3JHNHA 12 ALA H 12 ALA HA 9.1 . . . 7 3JHNHA 13 GLU H 13 GLU HA 4.0 . . . 8 3JHNHA 20 GLY H 20 GLY HA2 4.5 . . . 9 3JHNHA 20 GLY H 20 GLY HA3 8.0 . . . 10 3JHNHA 21 MET H 21 MET HA 8.4 . . . 11 3JHNHA 23 ARG H 23 ARG HA 8.0 . . . 12 3JHNHA 24 VAL H 24 VAL HA 8.9 . . . 13 3JHNHA 25 ARG H 25 ARG HA 6.9 . . . 14 3JHNHA 26 LEU H 26 LEU HA 8.1 . . . 15 3JHNHA 28 GLU H 28 GLU HA 4.0 . . . 16 3JHNHA 29 SER H 29 SER HA 3.1 . . . 17 3JHNHA 30 SER H 30 SER HA 3.5 . . . 18 3JHNHA 31 ARG H 31 ARG HA 4.0 . . . 19 3JHNHA 34 LEU H 34 LEU HA 9.0 . . . 20 3JHNHA 35 ASP H 35 ASP HA 6.5 . . . 21 3JHNHA 37 GLU H 37 GLU HA 8.2 . . . 22 3JHNHA 38 ILE H 38 ILE HA 4.1 . . . 23 3JHNHA 39 GLY H 39 GLY HA2 7.2 . . . 24 3JHNHA 39 GLY H 39 GLY HA3 4.5 . . . 25 3JHNHA 40 ASP H 40 ASP HA 8.4 . . . 26 3JHNHA 41 VAL H 41 VAL HA 8.5 . . . 27 3JHNHA 42 VAL H 42 VAL HA 8.1 . . . 28 3JHNHA 43 GLU H 43 GLU HA 8.6 . . . 29 3JHNHA 44 ILE H 44 ILE HA 9.0 . . . 30 3JHNHA 45 GLU H 45 GLU HA 9.6 . . . 31 3JHNHA 46 LYS H 46 LYS HA 8.3 . . . 32 3JHNHA 48 ARG H 48 ARG HA 8.4 . . . 33 3JHNHA 49 LYS H 49 LYS HA 8.6 . . . 34 3JHNHA 50 THR H 50 THR HA 8.9 . . . 35 3JHNHA 51 VAL H 51 VAL HA 8.7 . . . 36 3JHNHA 52 GLY H 52 GLY HA2 2.5 . . . 37 3JHNHA 52 GLY H 52 GLY HA3 4.0 . . . 38 3JHNHA 53 ARG H 53 ARG HA 8.3 . . . 39 3JHNHA 55 TYR H 55 TYR HA 9.5 . . . 40 3JHNHA 56 ARG H 56 ARG HA 8.9 . . . 41 3JHNHA 57 ALA H 57 ALA HA 4.8 . . . 42 3JHNHA 58 ARG H 58 ARG HA 4.2 . . . 43 3JHNHA 60 GLU H 60 GLU HA 5.9 . . . 44 3JHNHA 61 ASP H 61 ASP HA 8.5 . . . 45 3JHNHA 62 GLU H 62 GLU HA 8.00 . . . 46 3JHNHA 63 ASN H 63 ASN HA 4.1 . . . 47 3JHNHA 64 LYS H 64 LYS HA 8.2 . . . 48 3JHNHA 65 GLY H 65 GLY HA2 4.0 . . . 49 3JHNHA 65 GLY H 65 GLY HA3 4.5 . . . 50 3JHNHA 66 ILE H 66 ILE HA 9.1 . . . 51 3JHNHA 67 VAL H 67 VAL HA 8.9 . . . 52 3JHNHA 68 ARG H 68 ARG HA 8.3 . . . 53 3JHNHA 69 ILE H 69 ILE HA 8.1 . . . 54 3JHNHA 71 SER H 71 SER HA 3.8 . . . 55 3JHNHA 72 VAL H 72 VAL HA 5.2 . . . 56 3JHNHA 73 MET H 73 MET HA 2.7 . . . 57 3JHNHA 74 ARG H 74 ARG HA 3.4 . . . 58 3JHNHA 75 ASN H 75 ASN HA 4.5 . . . 59 3JHNHA 77 CYS H 77 CYS HA 8.6 . . . 60 3JHNHA 79 ALA H 79 ALA HA 8.2 . . . 61 3JHNHA 80 SER H 80 SER HA 9.5 . . . 62 3JHNHA 81 ILE H 81 ILE HA 5.0 . . . 63 3JHNHA 82 GLY H 82 GLY HA2 7.0 . . . 64 3JHNHA 82 GLY H 82 GLY HA3 4.5 . . . 65 3JHNHA 83 ASP H 83 ASP HA 3.3 . . . 66 3JHNHA 84 LYS H 84 LYS HA 8.4 . . . 67 3JHNHA 85 VAL H 85 VAL HA 8.6 . . . 68 3JHNHA 86 LYS H 86 LYS HA 8.8 . . . 69 3JHNHA 87 VAL H 87 VAL HA 8.6 . . . 70 3JHNHA 88 ARG H 88 ARG HA 8.4 . . . 71 3JHNHA 90 VAL H 90 VAL HA 8.5 . . . 72 3JHNHA 91 ARG H 91 ARG HA 8.6 . . . 73 3JHNHA 92 THR H 92 THR HA 8.1 . . . 74 3JHNHA 93 GLU H 93 GLU HA 9.4 . . . 75 3JHNHA 94 ILE H 94 ILE HA 8.9 . . . 76 3JHNHA 95 ALA H 95 ALA HA 3.3 . . . 77 3JHNHA 96 LYS H 96 LYS HA 8.6 . . . 78 3JHNHA 97 LYS H 97 LYS HA 8.2 . . . 79 3JHNHA 98 VAL H 98 VAL HA 8.3 . . . 80 3JHNHA 99 THR H 99 THR HA 9.2 . . . 81 3JHNHA 100 LEU H 100 LEU HA 10.0 . . . 82 3JHNHA 101 ALA H 101 ALA HA 8.5 . . . 83 3JHNHA 103 ILE H 103 ILE HA 8.6 . . . 84 3JHNHA 104 ILE H 104 ILE HA 9.0 . . . 85 3JHNHA 105 ARG H 105 ARG HA 8.3 . . . 86 3JHNHA 106 LYS H 106 LYS HA 4.0 . . . 87 3JHNHA 107 ASP H 107 ASP HA 9.0 . . . 88 3JHNHA 108 GLN H 108 GLN HA 9.0 . . . 89 3JHNHA 109 ARG H 109 ARG HA 8.5 . . . 90 3JHNHA 110 LEU H 110 LEU HA 9.0 . . . 91 3JHNHA 111 LYS H 111 LYS HA 9.0 . . . 92 3JHNHA 112 PHE H 112 PHE HA 8.8 . . . 93 3JHNHA 113 GLY H 113 GLY HA2 6.5 . . . 94 3JHNHA 113 GLY H 113 GLY HA3 6.5 . . . 95 3JHNHA 115 GLY H 115 GLY HA2 6.5 . . . 96 3JHNHA 115 GLY H 115 GLY HA3 6.5 . . . 97 3JHNHA 116 ILE H 116 ILE HA 4.0 . . . 98 3JHNHA 117 GLU H 117 GLU HA 3.6 . . . 99 3JHNHA 118 GLU H 118 GLU HA 4.2 . . . 100 3JHNHA 119 TYR H 119 TYR HA 3.0 . . . 101 3JHNHA 120 VAL H 120 VAL HA 3.8 . . . 102 3JHNHA 121 GLN H 121 GLN HA 3.8 . . . 103 3JHNHA 122 ARG H 122 ARG HA 5.2 . . . 104 3JHNHA 123 ALA H 123 ALA HA 5.1 . . . 105 3JHNHA 124 LEU H 124 LEU HA 8.4 . . . 106 3JHNHA 125 ILE H 125 ILE HA 1.9 . . . 107 3JHNHA 126 ARG H 126 ARG HA 5.0 . . . 108 3JHNHA 129 MET H 129 MET HA 5.4 . . . 109 3JHNHA 130 LEU H 130 LEU HA 8.3 . . . 110 3JHNHA 131 GLU H 131 GLU HA 2.0 . . . 111 3JHNHA 132 GLN H 132 GLN HA 5.0 . . . 112 3JHNHA 133 ASP H 133 ASP HA 3.7 . . . 113 3JHNHA 134 ASN H 134 ASN HA 8.3 . . . 114 3JHNHA 135 ILE H 135 ILE HA 9.2 . . . 115 3JHNHA 136 SER H 136 SER HA 9.0 . . . 116 3JHNHA 137 VAL H 137 VAL HA 9.1 . . . 117 3JHNHA 140 LEU H 140 LEU HA 8.6 . . . 118 3JHNHA 142 LEU H 142 LEU HA 8.6 . . . 119 3JHNHA 143 ALA H 143 ALA HA 4.4 . . . 120 3JHNHA 144 GLY H 144 GLY HA2 8.0 . . . 121 3JHNHA 144 GLY H 144 GLY HA3 5.5 . . . 122 3JHNHA 145 GLN H 145 GLN HA 9.0 . . . 123 3JHNHA 146 THR H 146 THR HA 9.2 . . . 124 3JHNHA 147 GLY H 147 GLY HA2 5.0 . . . 125 3JHNHA 147 GLY H 147 GLY HA3 3.0 . . . 126 3JHNHA 148 LEU H 148 LEU HA 8.6 . . . 127 3JHNHA 149 LEU H 149 LEU HA 9.3 . . . 128 3JHNHA 150 PHE H 150 PHE HA 8.8 . . . 129 3JHNHA 151 LYS H 151 LYS HA 8.3 . . . 130 3JHNHA 152 VAL H 152 VAL HA 5.8 . . . 131 3JHNHA 154 LYS H 154 LYS HA 8.3 . . . 132 3JHNHA 155 THR H 155 THR HA 8.2 . . . 133 3JHNHA 156 LEU H 156 LEU HA 8.8 . . . 134 3JHNHA 158 SER H 158 SER HA 6.0 . . . 135 3JHNHA 160 VAL H 160 VAL HA 8.3 . . . 136 3JHNHA 162 VAL H 162 VAL HA 9.1 . . . 137 3JHNHA 163 GLU H 163 GLU HA 9.0 . . . 138 3JHNHA 164 ILE H 164 ILE HA 5.7 . . . 139 3JHNHA 165 GLY H 165 GLY HA2 8.0 . . . 140 3JHNHA 165 GLY H 165 GLY HA3 2.0 . . . 141 3JHNHA 166 GLU H 166 GLU HA 3.5 . . . 142 3JHNHA 167 GLU H 167 GLU HA 8.5 . . . 143 3JHNHA 168 THR H 168 THR HA 3.6 . . . 144 3JHNHA 169 LYS H 169 LYS HA 8.1 . . . 145 3JHNHA 170 ILE H 170 ILE HA 9.2 . . . 146 3JHNHA 171 GLU H 171 GLU HA 9.7 . . . 147 3JHNHA 172 ILE H 172 ILE HA 8.4 . . . 148 3JHNHA 173 ARG H 173 ARG HA 8.1 . . . 149 3JHNHA 174 GLU H 174 GLU HA 8.6 . . . 150 3JHNHA 175 GLU H 175 GLU HA 8.5 . . . stop_ save_ save_heteronuclear_NOE_600 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Error assumed to be 0.05. ; loop_ _Sample_label $VATN_sample_N15 stop_ _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name ? _Atom_one_atom_name . _Atom_two_atom_name . _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 3 SER -1.10 0.05 4 ASN -0.61 0.05 5 ASN -0.17 0.05 6 GLY 0.25 0.05 7 ILE 0.77 0.05 8 ILE 0.77 0.05 9 LEU 0.87 0.05 10 ARG 0.84 0.05 11 VAL 0.82 0.05 12 ALA 0.85 0.05 13 GLU 0.83 0.05 14 ALA 0.00 0.05 15 ASN 0.00 0.05 16 SER 0.00 0.05 17 THR 0.00 0.05 18 ASP 0.73 0.05 19 PRO 0.70 0.05 20 GLY 0.65 0.05 21 MET 0.86 0.05 22 SER 0.79 0.05 23 ARG 0.79 0.05 24 VAL 0.89 0.05 25 ARG 0.87 0.05 26 LEU 0.81 0.05 27 ASP 0.88 0.05 28 GLU 0.87 0.05 29 SER 0.84 0.05 30 SER 0.83 0.05 31 ARG 0.89 0.05 32 ARG 0.86 0.05 33 LEU 0.83 0.05 34 LEU 0.82 0.05 35 ASP 0.81 0.05 36 ALA 0.78 0.05 37 GLU 0.79 0.05 38 ILE 0.77 0.05 39 GLY 0.86 0.05 40 ASP 0.84 0.05 41 VAL 0.78 0.05 42 VAL 0.85 0.05 43 GLU 0.89 0.05 44 ILE 0.88 0.05 45 GLU 0.83 0.05 46 LYS 0.88 0.05 47 VAL 0.73 0.05 48 ARG 0.74 0.05 49 LYS 0.73 0.05 50 THR 0.86 0.05 51 VAL 0.78 0.05 52 GLY 0.85 0.05 53 ARG 0.79 0.05 54 VAL 0.84 0.05 55 TYR 0.84 0.05 56 ARG 0.84 0.05 57 ALA 0.72 0.05 58 ARG 0.78 0.05 59 PRO 0.78 0.05 60 GLU 0.77 0.05 61 ASP 0.82 0.05 62 GLU 0.85 0.05 63 ASN 0.87 0.05 64 LYS 0.79 0.05 65 GLY 0.81 0.05 66 ILE 0.84 0.05 67 VAL 0.85 0.05 68 ARG 0.85 0.05 69 ILE 0.76 0.05 70 ASP 0.76 0.05 71 SER 0.76 0.05 72 VAL 0.83 0.05 73 MET 0.75 0.05 74 ARG 0.86 0.05 75 ASN 0.83 0.05 76 ASN 0.82 0.05 77 CYS 0.83 0.05 78 GLY 0.84 0.05 79 ALA 0.83 0.05 80 SER 0.79 0.05 81 ILE 0.79 0.05 82 GLY 0.82 0.05 83 ASP 0.83 0.05 84 LYS 0.82 0.05 85 VAL 0.81 0.05 86 LYS 0.83 0.05 87 VAL 0.81 0.05 88 ARG 0.81 0.05 89 LYS 0.80 0.05 90 VAL 0.76 0.05 91 ARG 0.77 0.05 92 THR 0.64 0.05 93 GLU 0.80 0.05 94 ILE 0.75 0.05 95 ALA 0.85 0.05 96 LYS 0.84 0.05 97 LYS 0.80 0.05 98 VAL 0.78 0.05 99 THR 0.80 0.05 100 LEU 0.83 0.05 101 ALA 0.84 0.05 102 PRO 0.80 0.05 103 ILE 0.80 0.05 104 ILE 0.72 0.05 105 ARG 0.63 0.05 106 LYS 0.68 0.05 107 ASP 0.54 0.05 108 GLN 0.50 0.05 109 ARG 0.48 0.05 110 LEU 0.53 0.05 111 LYS 0.48 0.05 112 PHE 0.41 0.05 113 GLY 0.23 0.05 114 GLU 0.52 0.05 115 GLY 0.50 0.05 116 ILE 0.71 0.05 117 GLU 0.77 0.05 118 GLU 0.78 0.05 119 TYR 0.82 0.05 120 VAL 0.86 0.05 121 GLN 0.82 0.05 122 ARG 0.80 0.05 123 ALA 0.81 0.05 124 LEU 0.82 0.05 125 ILE 0.82 0.05 126 ARG 0.76 0.05 127 ARG 0.80 0.05 128 PRO 0.81 0.05 129 MET 0.82 0.05 130 LEU 0.71 0.05 131 GLU 0.74 0.05 132 GLN 0.82 0.05 133 ASP 0.87 0.05 134 ASN 0.87 0.05 135 ILE 0.81 0.05 136 SER 0.76 0.05 137 VAL 0.82 0.05 138 PRO 0.77 0.05 139 GLY 0.71 0.05 140 LEU 0.69 0.05 141 THR 0.60 0.05 142 LEU 0.52 0.05 143 ALA 0.52 0.05 144 GLY 0.44 0.05 145 GLN 0.53 0.05 146 THR 0.38 0.05 147 GLY 0.42 0.05 148 LEU 0.45 0.05 149 LEU 0.64 0.05 150 PHE 0.90 0.05 151 LYS 0.79 0.05 152 VAL 0.90 0.05 153 VAL 0.84 0.05 154 LYS 0.81 0.05 155 THR 0.83 0.05 156 LEU 0.83 0.05 157 PRO 0.80 0.05 158 SER 0.76 0.05 159 LYS 0.65 0.05 160 VAL 0.61 0.05 161 PRO 0.77 0.05 162 VAL 0.83 0.05 163 GLU 0.80 0.05 164 ILE 0.86 0.05 165 GLY 0.82 0.05 166 GLU 0.76 0.05 167 GLU 0.77 0.05 168 THR 0.81 0.05 169 LYS 0.77 0.05 170 ILE 0.80 0.05 171 GLU 0.78 0.05 172 ILE 0.77 0.05 173 ARG 0.75 0.05 174 GLU 0.55 0.05 175 GLU 0.59 0.05 176 PRO 0.59 0.05 177 ALA 0.60 0.05 178 SER 0.47 0.05 179 GLU 0.39 0.05 180 VAL 0.26 0.05 181 LEU 0.18 0.05 182 GLU 0.06 0.05 183 GLU -0.18 0.05 184 GLY -0.33 0.05 185 GLY -0.38 0.05 stop_ save_