data_4242 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Motile Major Sperm Protein (MSP) of Ascaris suum ; _BMRB_accession_number 4242 _BMRB_flat_file_name bmr4242.str _Entry_type original _Submission_date 1998-10-09 _Accession_date 1998-10-10 _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 Haaf Andreas . . 2 LeClaire Lawrence . III 3 Roberts Gregory . . 4 Kent Helen M. . 5 Roberts Thomas M. . 6 Stewart Murray . . 7 Neuhaus David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 693 "13C chemical shifts" 410 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-01-25 original author . stop_ _Original_release_date 1999-01-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Haaf, A., LeClaire, L. III, Roberts, G., Kent, H. M., Roberts, T. M., Stewart, M., and Neuhaus, D., "Solution Structure of the Motile Major Sperm Protein (MSP) of Ascaris suum - Evidence for Two Manganese Binding Sites and the Possible Role of Divalent Cations in Filament Formation," J. Mol. Biol. 284, 1611-1623 (1998). ; _Citation_title ; Solution Structure of the Motile Major Sperm Protein (MSP) of Ascaris suum - Evidence for Two Manganese Binding Sites and the Possible Role of Divalent Cations in Filament Formation. ; _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 Haaf Andreas . . 2 LeClaire Lawrence . III 3 Roberts Gregory . . 4 Kent Helen M. . 5 Roberts Thomas M. . 6 Stewart Murray . . 7 Neuhaus David . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 284 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1611 _Page_last 1623 _Year 1998 _Details . loop_ _Keyword 'amoeboid motility' filaments 'major sperm protein' 'NMR structure' polymerization stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_MSP _Saveframe_category molecular_system _Mol_system_name 'Major Sperm Protein' _Abbreviation_common MSP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MSP subunit A' $MSP 'MSP subunit B' $MSP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'MSP subunit A' 1 'MSP subunit B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MSP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Major Sperm Protein' _Name_variant 'alpha isoform' _Abbreviation_common 'MSP subunit A' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; AQSVPPGDINTQPSQKIVFN APYDDKHTYHIKITNAGGRR IGWAIKTTNMRRLSVDPPCG VLDPKEKVLMAVSCDTFNAA TEDLNNDRITIEWTNTPDGA AKQFRREWFQGDGMVRRKNL PIEYNL ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 SER 4 VAL 5 PRO 6 PRO 7 GLY 8 ASP 9 ILE 10 ASN 11 THR 12 GLN 13 PRO 14 SER 15 GLN 16 LYS 17 ILE 18 VAL 19 PHE 20 ASN 21 ALA 22 PRO 23 TYR 24 ASP 25 ASP 26 LYS 27 HIS 28 THR 29 TYR 30 HIS 31 ILE 32 LYS 33 ILE 34 THR 35 ASN 36 ALA 37 GLY 38 GLY 39 ARG 40 ARG 41 ILE 42 GLY 43 TRP 44 ALA 45 ILE 46 LYS 47 THR 48 THR 49 ASN 50 MET 51 ARG 52 ARG 53 LEU 54 SER 55 VAL 56 ASP 57 PRO 58 PRO 59 CYS 60 GLY 61 VAL 62 LEU 63 ASP 64 PRO 65 LYS 66 GLU 67 LYS 68 VAL 69 LEU 70 MET 71 ALA 72 VAL 73 SER 74 CYS 75 ASP 76 THR 77 PHE 78 ASN 79 ALA 80 ALA 81 THR 82 GLU 83 ASP 84 LEU 85 ASN 86 ASN 87 ASP 88 ARG 89 ILE 90 THR 91 ILE 92 GLU 93 TRP 94 THR 95 ASN 96 THR 97 PRO 98 ASP 99 GLY 100 ALA 101 ALA 102 LYS 103 GLN 104 PHE 105 ARG 106 ARG 107 GLU 108 TRP 109 PHE 110 GLN 111 GLY 112 ASP 113 GLY 114 MET 115 VAL 116 ARG 117 ARG 118 LYS 119 ASN 120 LEU 121 PRO 122 ILE 123 GLU 124 TYR 125 ASN 126 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1MSP "Major Sperm Protein, Alpha Isoform (Recombinant), Ph 4.6" 100.00 126 100.00 100.00 2.09e-88 PDB 2BVU "D83r Mutant Of Asaris Suum Major Sperm Protein (Msp)" 100.00 126 99.21 99.21 2.33e-87 PDB 3MSP "Motile Major Sperm Protein (Msp) Of Ascaris Suum, Nmr, 20 Structures" 100.00 126 100.00 100.00 2.09e-88 EMBL CAA63933 "major sperm protein isoform alpha [Ascaris suum]" 100.00 127 100.00 100.00 1.85e-88 GB AAA29375 "major sperm protein [Ascaris lumbricoides]" 100.00 127 100.00 100.00 1.85e-88 GB AAB23264 "major sperm protein alpha isoform, alpha-MSP [Ascaris suum=nematodes, Peptide, 126 aa]" 100.00 126 99.21 99.21 2.81e-87 GB AAP76176 "major sperm protein alpha [Ascaris suum]" 100.00 127 100.00 100.00 1.85e-88 GB ERG81453 "major sperm protein isoform alpha [Ascaris suum]" 100.00 127 100.00 100.00 1.85e-88 SP P27439 "RecName: Full=Major sperm protein isoform alpha; AltName: Full=Alpha-MSP" 100.00 127 100.00 100.00 1.85e-88 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Cell_type $MSP 'Pig Roundworm' 6253 Eukaryota Metazoa Ascaris suum 'Sperm Cell' 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 $MSP recombinant_technology 'E. coli' Escherichia coli BL21(DE3) plasmid pET11d stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MSP . mM 2.5 3.5 . D2O 5 % . . . H2O 95 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MSP . mM 2.5 3.5 [U-98%15N] D2O 5 % . . . H2O 95 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MSP . mM 2.5 3.5 [U-98%13C;U-98%15N] D2O 5 % . . . H2O 95 % . . . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 2.30 loop_ _Task 'processing and analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_DQ-correlation_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQ-correlation _Sample_label . save_ save_DQF-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_3D_15N_HSQC-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HSQC-NOESY' _Sample_label . save_ save_3D_13C_HSQC-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C HSQC-NOESY' _Sample_label . save_ save_HCCH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 n/a pressure 1 . atm temperature 308 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'MSP subunit A' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 4.12 . 1 2 . 1 ALA HB H 1.53 . 1 3 . 1 ALA CA C 50.1 . 1 4 . 1 ALA CB C 17.7 . 1 5 . 2 GLN CG C 32.3 . 1 6 . 2 GLN H H 8.68 . 1 7 . 2 GLN HA H 4.40 . 1 8 . 2 GLN HB2 H 2.09 . 2 9 . 2 GLN HB3 H 2.00 . 2 10 . 2 GLN HG2 H 2.37 . 1 11 . 2 GLN HG3 H 2.37 . 1 12 . 2 GLN CA C 54.4 . 1 13 . 2 GLN CB C 28.2 . 1 14 . 2 GLN N N 127.0 . 1 15 . 3 SER H H 8.47 . 1 16 . 3 SER HA H 4.51 . 1 17 . 3 SER HB2 H 3.83 . 1 18 . 3 SER HB3 H 3.83 . 1 19 . 3 SER CA C 56.6 . 1 20 . 3 SER CB C 62.3 . 1 21 . 3 SER N N 125.5 . 1 22 . 4 VAL H H 8.13 . 1 23 . 4 VAL HA H 4.55 . 1 24 . 4 VAL HB H 2.07 . 1 25 . 4 VAL HG1 H 0.94 . 2 26 . 4 VAL HG2 H 0.86 . 2 27 . 4 VAL CA C 57.7 . 1 28 . 4 VAL CB C 31.5 . 1 29 . 4 VAL CG1 C 19.5 . 2 30 . 4 VAL CG2 C 18.2 . 2 31 . 4 VAL N N 128.6 . 1 32 . 5 PRO HA H 4.57 . 1 33 . 5 PRO HB2 H 2.32 . 2 34 . 5 PRO HB3 H 2.28 . 2 35 . 5 PRO HG2 H 2.04 . 2 36 . 5 PRO HG3 H 1.98 . 2 37 . 5 PRO HD2 H 3.86 . 2 38 . 5 PRO HD3 H 3.68 . 2 39 . 5 PRO CA C 60.1 . 1 40 . 5 PRO CB C 29.1 . 1 41 . 5 PRO CG C 25.6 . 1 42 . 5 PRO CD C 49.5 . 1 43 . 6 PRO HA H 4.67 . 2 44 . 6 PRO HB2 H 2.25 . 2 45 . 6 PRO HB3 H 2.04 . 2 46 . 6 PRO HG2 H 1.92 . 2 47 . 6 PRO HG3 H 1.64 . 2 48 . 6 PRO HD2 H 2.86 . 2 49 . 6 PRO HD3 H 3.30 . 2 50 . 6 PRO CA C 61.00 . 1 51 . 6 PRO CB C 31.2 . 1 52 . 6 PRO CG C 25.8 . 1 53 . 6 PRO CD C 48.7 . 1 54 . 7 GLY H H 8.92 . 1 55 . 7 GLY HA2 H 4.33 . 1 56 . 7 GLY HA3 H 3.85 . 1 57 . 7 GLY CA C 42.6 . 1 58 . 7 GLY N N 115.4 . 1 59 . 8 ASP H H 8.53 . 1 60 . 8 ASP HA H 4.78 . 1 61 . 8 ASP HB2 H 2.63 . 2 62 . 8 ASP HB3 H 2.46 . 2 63 . 8 ASP CA C 53.8 . 1 64 . 8 ASP CB C 40.8 . 1 65 . 8 ASP N N 126.00 . 1 66 . 9 ILE H H 7.2 . 1 67 . 9 ILE HA H 4.56 . 1 68 . 9 ILE HB H 0.88 . 1 69 . 9 ILE HG12 H 0.28 . 2 70 . 9 ILE HG13 H -0.64 . 2 71 . 9 ILE HG2 H -0.38 . 1 72 . 9 ILE HD1 H -0.18 . 1 73 . 9 ILE CA C 57.9 . 1 74 . 9 ILE CB C 38.8 . 1 75 . 9 ILE CG1 C 22.6 . 1 76 . 9 ILE CG2 C 14.6 . 1 77 . 9 ILE CD1 C 13.2 . 1 78 . 9 ILE N N 116.4 . 1 79 . 10 ASN H H 8.4 . 1 80 . 10 ASN HA H 5.05 . 1 81 . 10 ASN HB2 H 2.62 . 1 82 . 10 ASN HB3 H 2.38 . 1 83 . 10 ASN HD21 H 7.35 . 1 84 . 10 ASN HD22 H 6.92 . 1 85 . 10 ASN CA C 50.00 . 1 86 . 10 ASN CB C 40.4 . 1 87 . 10 ASN N N 126.1 . 1 88 . 10 ASN ND2 N 118.5 . 1 89 . 11 THR H H 8.77 . 1 90 . 11 THR HA H 5.34 . 1 91 . 11 THR HB H 3.91 . 1 92 . 11 THR HG2 H 0.71 . 1 93 . 11 THR CA C 57.8 . 1 94 . 11 THR CB C 70.00 . 1 95 . 11 THR CG2 C 19.8 . 1 96 . 11 THR N N 119.8 . 1 97 . 12 GLN H H 8.24 . 1 98 . 12 GLN HA H 4.25 . 1 99 . 12 GLN CA C 51.4 . 1 100 . 12 GLN N N 127.00 . 1 101 . 13 PRO HA H 4.75 . 1 102 . 13 PRO HB2 H 2.45 . 2 103 . 13 PRO HB3 H 2.42 . 2 104 . 13 PRO HG2 H 1.98 . 2 105 . 13 PRO HG3 H 1.77 . 2 106 . 13 PRO HD2 H 4.13 . 2 107 . 13 PRO HD3 H 3.15 . 2 108 . 13 PRO CA C 61.5 . 1 109 . 13 PRO CB C 33.2 . 1 110 . 13 PRO CG C 25.2 . 1 111 . 13 PRO CD C 48.7 . 1 112 . 14 SER H H 10.00 . 1 113 . 14 SER HA H 4.16 . 1 114 . 14 SER HB2 H 4.09 . 2 115 . 14 SER HB3 H 4.00 . 2 116 . 14 SER CA C 59.4 . 1 117 . 14 SER CB C 63.2 . 1 118 . 14 SER N N 123.00 . 1 119 . 15 GLN H H 8.56 . 1 120 . 15 GLN HA H 4.67 . 1 121 . 15 GLN HB2 H 2.16 . 2 122 . 15 GLN HB3 H 2.03 . 2 123 . 15 GLN CA C 55.1 . 1 124 . 15 GLN CB C 30.2 . 1 125 . 15 GLN N N 124.00 . 1 126 . 16 LYS H H 7.81 . 1 127 . 16 LYS HA H 4.68 . 1 128 . 16 LYS CA C 53.3 . 1 129 . 16 LYS N N 121.1 . 1 130 . 17 ILE H H 8.59 . 1 131 . 17 ILE HA H 4.06 . 1 132 . 17 ILE HB H 1.29 . 1 133 . 17 ILE HG12 H 1.29 . 2 134 . 17 ILE HG13 H 0.75 . 2 135 . 17 ILE HG2 H 0.46 . 1 136 . 17 ILE HD1 H 0.74 . 1 137 . 17 ILE CA C 59.00 . 1 138 . 17 ILE CB C 40.3 . 1 139 . 17 ILE CG1 C 26.9 . 1 140 . 17 ILE CG2 C 15.4 . 1 141 . 17 ILE CD1 C 13.2 . 1 142 . 17 ILE N N 126.4 . 1 143 . 18 VAL H H 7.96 . 1 144 . 18 VAL HA H 4.81 . 1 145 . 18 VAL HB H 1.91 . 1 146 . 18 VAL HG1 H 0.75 . 1 147 . 18 VAL HG2 H 0.75 . 1 148 . 18 VAL CA C 59.1 . 1 149 . 18 VAL CB C 31.3 . 1 150 . 18 VAL CG1 C 19.4 . 1 151 . 18 VAL CG2 C 19.4 . 1 152 . 18 VAL N N 133.00 . 1 153 . 19 PHE H H 8.79 . 1 154 . 19 PHE HA H 5.03 . 1 155 . 19 PHE HB2 H 3.32 . 1 156 . 19 PHE HB3 H 2.99 . 1 157 . 19 PHE HD1 H 6.65 . 1 158 . 19 PHE HD2 H 6.65 . 1 159 . 19 PHE HE1 H 6.61 . 1 160 . 19 PHE HE2 H 6.61 . 1 161 . 19 PHE HZ H 6.7 . 1 162 . 19 PHE CA C 53.4 . 1 163 . 19 PHE CB C 37.5 . 1 164 . 19 PHE CD1 C 129.00 . 1 165 . 19 PHE CD2 C 129.00 . 1 166 . 19 PHE CE1 C 129.00 . 1 167 . 19 PHE CE2 C 129.00 . 1 168 . 19 PHE CZ C 125.6 . 1 169 . 19 PHE N N 131.8 . 1 170 . 20 ASN HA H 5.53 . 1 171 . 20 ASN HB2 H 2.84 . 1 172 . 20 ASN HB3 H 2.77 . 1 173 . 20 ASN CA C 52.3 . 1 174 . 20 ASN CB C 42.00 . 1 175 . 21 ALA H H 7.85 . 1 176 . 21 ALA HA H 2.46 . 1 177 . 21 ALA HB H 1.29 . 1 178 . 21 ALA CA C 49.2 . 1 179 . 21 ALA CB C 17.8 . 1 180 . 21 ALA N N 132.4 . 1 181 . 22 PRO HA H 4.13 . 1 182 . 22 PRO HB2 H 2.28 . 2 183 . 22 PRO HB3 H 2.2 . 2 184 . 22 PRO HG2 H 1.93 . 2 185 . 22 PRO HG3 H 1.6 . 2 186 . 22 PRO HD2 H 3.61 . 2 187 . 22 PRO HD3 H 3.48 . 2 188 . 22 PRO CA C 59.2 . 1 189 . 22 PRO CB C 34.1 . 1 190 . 22 PRO CG C 23.5 . 1 191 . 22 PRO CD C 48.8 . 1 192 . 23 TYR H H 8.71 . 1 193 . 23 TYR HA H 5.05 . 1 194 . 23 TYR HB2 H 2.98 . 1 195 . 23 TYR HB3 H 2.18 . 1 196 . 23 TYR HD1 H 7.12 . 1 197 . 23 TYR HD2 H 7.12 . 1 198 . 23 TYR HE1 H 6.65 . 1 199 . 23 TYR HE2 H 6.65 . 1 200 . 23 TYR CA C 55.7 . 1 201 . 23 TYR CB C 35.2 . 1 202 . 23 TYR CD1 C 131.9 . 1 203 . 23 TYR CD2 C 131.9 . 1 204 . 23 TYR CE1 C 117.00 . 1 205 . 23 TYR CE2 C 117.00 . 1 206 . 23 TYR N N 128.5 . 1 207 . 24 ASP H H 7.6 . 1 208 . 24 ASP HA H 4.47 . 1 209 . 24 ASP HB2 H 2.67 . 1 210 . 24 ASP HB3 H 2.67 . 1 211 . 24 ASP CA C 52.6 . 1 212 . 24 ASP CB C 38.4 . 1 213 . 24 ASP N N 123.5 . 1 214 . 25 ASP H H 7.53 . 1 215 . 25 ASP HA H 4.7 . 1 216 . 25 ASP HB2 H 2.51 . 2 217 . 25 ASP HB3 H 2.34 . 2 218 . 25 ASP CA C 50.6 . 1 219 . 25 ASP CB C 42.4 . 1 220 . 25 ASP N N 124.5 . 1 221 . 26 LYS H H 8.46 . 1 222 . 26 LYS HA H 4.54 . 1 223 . 26 LYS HB2 H 1.76 . 1 224 . 26 LYS HB3 H 1.76 . 1 225 . 26 LYS HG2 H 1.32 . 1 226 . 26 LYS HG3 H 1.32 . 1 227 . 26 LYS HD2 H 1.62 . 1 228 . 26 LYS HD3 H 1.62 . 1 229 . 26 LYS CA C 55.2 . 1 230 . 26 LYS CB C 31.3 . 1 231 . 26 LYS CG C 23.4 . 1 232 . 26 LYS CD C 27.5 . 1 233 . 26 LYS N N 129.5 . 1 234 . 27 HIS H H 8.43 . 1 235 . 27 HIS HA H 4.91 . 1 236 . 27 HIS HB2 H 3.09 . 1 237 . 27 HIS HB3 H 3.09 . 1 238 . 27 HIS HD2 H 6.46 . 1 239 . 27 HIS CA C 53.1 . 1 240 . 27 HIS CB C 30.8 . 1 241 . 27 HIS CD2 C 119.3 . 1 242 . 27 HIS N N 128.8 . 1 243 . 28 THR H H 8.66 . 1 244 . 28 THR HA H 4.86 . 1 245 . 28 THR HB H 3.76 . 1 246 . 28 THR HG2 H 0.93 . 1 247 . 28 THR CA C 61.1 . 1 248 . 28 THR CB C 69.7 . 1 249 . 28 THR CG2 C 20.7 . 1 250 . 28 THR N N 128.00 . 1 251 . 29 TYR H H 9.21 . 1 252 . 29 TYR HA H 4.99 . 1 253 . 29 TYR HB2 H 3.17 . 2 254 . 29 TYR HB3 H 2.7 . 2 255 . 29 TYR HD2 H 6.93 . 1 256 . 29 TYR HE1 H 6.69 . 1 257 . 29 TYR HE2 H 6.69 . 1 258 . 29 TYR CA C 54.1 . 1 259 . 29 TYR CB C 39.1 . 1 260 . 29 TYR CD1 C 131.6 . 1 261 . 29 TYR CD2 C 131.6 . 1 262 . 29 TYR CE1 C 117.00 . 1 263 . 29 TYR CE2 C 117.00 . 1 264 . 29 TYR N N 135.00 . 1 265 . 30 HIS H H 8.62 . 1 266 . 30 HIS HA H 5.79 . 1 267 . 30 HIS HB2 H 3.09 . 2 268 . 30 HIS HB3 H 2.91 . 2 269 . 30 HIS HD2 H 6.99 . 1 270 . 30 HIS HE1 H 8.52 . 1 271 . 30 HIS CA C 54.1 . 1 272 . 30 HIS CB C 30.3 . 1 273 . 30 HIS CD2 C 117.3 . 1 274 . 30 HIS CE1 C 135.3 . 1 275 . 30 HIS N N 124.3 . 1 276 . 31 ILE H H 8.79 . 1 277 . 31 ILE HA H 4.87 . 1 278 . 31 ILE HB H 1.75 . 1 279 . 31 ILE HG12 H 1.39 . 2 280 . 31 ILE HG13 H 0.93 . 2 281 . 31 ILE HG2 H 0.64 . 1 282 . 31 ILE HD1 H 0.63 . 1 283 . 31 ILE CA C 58.3 . 1 284 . 31 ILE CB C 39.9 . 1 285 . 31 ILE CG1 C 26.00 . 1 286 . 31 ILE CG2 C 15.2 . 1 287 . 31 ILE CD1 C 12.6 . 1 288 . 31 ILE N N 125.5 . 1 289 . 32 LYS H H 9.06 . 1 290 . 32 LYS HA H 5.17 . 1 291 . 32 LYS CA C 53.3 . 1 292 . 32 LYS N N 133.6 . 1 293 . 33 ILE H H 8.77 . 1 294 . 33 ILE HA H 4.33 . 1 295 . 33 ILE HB H 1.06 . 1 296 . 33 ILE HG12 H 1.06 . 2 297 . 33 ILE HG13 H 0.24 . 2 298 . 33 ILE HG2 H 0.04 . 1 299 . 33 ILE HD1 H -0.27 . 1 300 . 33 ILE CA C 59.00 . 1 301 . 33 ILE CB C 38.3 . 1 302 . 33 ILE CG1 C 25.6 . 1 303 . 33 ILE CG2 C 15.2 . 1 304 . 33 ILE CD1 C 11.3 . 1 305 . 33 ILE N N 134.6 . 1 306 . 34 THR H H 8.47 . 1 307 . 34 THR HA H 4.85 . 1 308 . 34 THR HB H 3.63 . 1 309 . 34 THR HG2 H 0.82 . 1 310 . 34 THR CA C 59.5 . 1 311 . 34 THR CB C 69.6 . 1 312 . 34 THR CG2 C 18.9 . 1 313 . 34 THR N N 126.9 . 1 314 . 35 ASN H H 8.26 . 1 315 . 35 ASN HA H 4.45 . 1 316 . 35 ASN CA C 51.1 . 1 317 . 35 ASN N N 128.6 . 1 318 . 36 ALA H H 7.55 . 1 319 . 36 ALA HA H 4.53 . 1 320 . 36 ALA HB H 1.11 . 1 321 . 36 ALA CA C 49.9 . 1 322 . 36 ALA CB C 17.4 . 1 323 . 36 ALA N N 138.5 . 1 324 . 37 GLY H H 8.06 . 1 325 . 37 GLY HA2 H 4.57 . 2 326 . 37 GLY HA3 H 4.04 . 2 327 . 37 GLY CA C 42.6 . 1 328 . 37 GLY N N 115.3 . 1 329 . 38 GLY H H 8.44 . 1 330 . 38 GLY HA2 H 4.28 . 2 331 . 38 GLY HA3 H 3.74 . 2 332 . 38 GLY CA C 43.5 . 1 333 . 38 GLY N N 109.9 . 1 334 . 39 ARG H H 7.41 . 1 335 . 39 ARG HA H 4.69 . 1 336 . 39 ARG HB2 H 1.93 . 2 337 . 39 ARG HB3 H 1.65 . 2 338 . 39 ARG HG2 H 1.57 . 1 339 . 39 ARG HG3 H 1.57 . 1 340 . 39 ARG HD2 H 3.13 . 1 341 . 39 ARG HD3 H 3.13 . 1 342 . 39 ARG HE H 7.33 . 1 343 . 39 ARG CA C 51.9 . 1 344 . 39 ARG CB C 32.2 . 1 345 . 39 ARG CG C 25.1 . 1 346 . 39 ARG CD C 42.00 . 1 347 . 39 ARG N N 123.7 . 1 348 . 39 ARG NE N 91.7 . 1 349 . 40 ARG H H 8.56 . 1 350 . 40 ARG HA H 4.51 . 1 351 . 40 ARG HB2 H 2.07 . 2 352 . 40 ARG HB3 H 1.68 . 2 353 . 40 ARG HG2 H 1.32 . 1 354 . 40 ARG HG3 H 1.32 . 1 355 . 40 ARG HD2 H 2.97 . 1 356 . 40 ARG HD3 H 2.97 . 1 357 . 40 ARG HE H 8.18 . 1 358 . 40 ARG CA C 55.5 . 1 359 . 40 ARG CB C 30.2 . 1 360 . 40 ARG CG C 25.7 . 1 361 . 40 ARG CD C 42.5 . 1 362 . 40 ARG N N 129.3 . 1 363 . 40 ARG NE N 91.6 . 1 364 . 41 ILE H H 8.58 . 1 365 . 41 ILE HA H 5.62 . 1 366 . 41 ILE HB H 2.28 . 1 367 . 41 ILE HG2 H 1.23 . 1 368 . 41 ILE HD1 H 0.66 . 1 369 . 41 ILE CA C 57.9 . 1 370 . 41 ILE CB C 41.1 . 1 371 . 41 ILE CG2 C 15.9 . 1 372 . 41 ILE CD1 C 13.00 . 1 373 . 41 ILE N N 124.6 . 1 374 . 42 GLY H H 9.2 . 1 375 . 42 GLY HA2 H 5.78 . 2 376 . 42 GLY HA3 H 3.83 . 2 377 . 42 GLY CA C 43.1 . 1 378 . 42 GLY N N 114.8 . 1 379 . 43 TRP H H 9.17 . 1 380 . 43 TRP HA H 6.5 . 1 381 . 43 TRP HB2 H 3.44 . 2 382 . 43 TRP HB3 H 2.82 . 2 383 . 43 TRP HD1 H 6.5 . 1 384 . 43 TRP HE1 H 9.71 . 1 385 . 43 TRP HE3 H 6.98 . 1 386 . 43 TRP HZ2 H 6.88 . 1 387 . 43 TRP HZ3 H 6.7 . 1 388 . 43 TRP HH2 H 6.88 . 1 389 . 43 TRP CA C 52.9 . 1 390 . 43 TRP CB C 30.9 . 1 391 . 43 TRP CD1 C 123.8 . 1 392 . 43 TRP CE3 C 117.7 . 1 393 . 43 TRP CZ2 C 112.3 . 1 394 . 43 TRP CZ3 C 120.8 . 1 395 . 43 TRP CH2 C 123.5 . 1 396 . 43 TRP N N 128.8 . 1 397 . 43 TRP NE1 N 132.6 . 1 398 . 44 ALA H H 9.6 . 1 399 . 44 ALA HA H 4.52 . 1 400 . 44 ALA HB H 1.11 . 1 401 . 44 ALA CA C 50.00 . 1 402 . 44 ALA CB C 21.7 . 1 403 . 44 ALA N N 127.2 . 1 404 . 45 ILE H H 8.02 . 1 405 . 45 ILE HA H 5.54 . 1 406 . 45 ILE HB H 1.9 . 1 407 . 45 ILE HG12 H 1.8 . 2 408 . 45 ILE HG13 H 1.51 . 2 409 . 45 ILE HG2 H 0.99 . 1 410 . 45 ILE HD1 H 0.82 . 1 411 . 45 ILE CA C 56.6 . 1 412 . 45 ILE CB C 39.3 . 1 413 . 45 ILE CG1 C 26.7 . 1 414 . 45 ILE CG2 C 17.7 . 1 415 . 45 ILE CD1 C 12.2 . 1 416 . 45 ILE N N 125.8 . 1 417 . 46 LYS H H 8.9 . 1 418 . 46 LYS HA H 4.79 . 1 419 . 46 LYS HB2 H 1.92 . 2 420 . 46 LYS HB3 H 1.69 . 2 421 . 46 LYS HG2 H 1.38 . 1 422 . 46 LYS HG3 H 1.38 . 1 423 . 46 LYS HE2 H 2.91 . 1 424 . 46 LYS HE3 H 2.91 . 1 425 . 46 LYS CA C 53.3 . 1 426 . 46 LYS CB C 34.6 . 1 427 . 46 LYS CG C 22.8 . 1 428 . 46 LYS CE C 40.9 . 1 429 . 46 LYS N N 131.8 . 1 430 . 47 THR H H 8.53 . 1 431 . 47 THR HA H 5.37 . 1 432 . 47 THR HB H 4.19 . 1 433 . 47 THR HG2 H 1.08 . 1 434 . 47 THR CA C 58.3 . 1 435 . 47 THR CB C 69.6 . 1 436 . 47 THR CG2 C 19.1 . 1 437 . 47 THR N N 119.2 . 1 438 . 48 THR H H 7.63 . 1 439 . 48 THR HA H 4.38 . 1 440 . 48 THR HB H 4.68 . 1 441 . 48 THR HG2 H 1.36 . 1 442 . 48 THR CA C 60.4 . 1 443 . 48 THR CB C 67.9 . 1 444 . 48 THR CG2 C 21.6 . 1 445 . 48 THR N N 115.3 . 1 446 . 49 ASN H H 8.00 . 1 447 . 49 ASN HA H 4.75 . 1 448 . 49 ASN HB2 H 2.81 . 2 449 . 49 ASN HB3 H 2.61 . 2 450 . 49 ASN HD21 H 8.46 . 1 451 . 49 ASN HD22 H 6.54 . 1 452 . 49 ASN CA C 51.3 . 1 453 . 49 ASN CB C 36.8 . 1 454 . 49 ASN N N 125.8 . 1 455 . 49 ASN ND2 N 120.5 . 1 456 . 50 MET H H 8.64 . 1 457 . 50 MET HA H 4.49 . 1 458 . 50 MET HB2 H 2.21 . 1 459 . 50 MET HB3 H 2.05 . 1 460 . 50 MET HG2 H 2.63 . 1 461 . 50 MET HG3 H 2.63 . 1 462 . 50 MET HE H 2.18 . 1 463 . 50 MET CA C 55.6 . 1 464 . 50 MET CB C 30.8 . 1 465 . 50 MET CG C 30.6 . 1 466 . 50 MET CE C 15.2 . 1 467 . 50 MET N N 128.7 . 1 468 . 51 ARG H H 8.02 . 1 469 . 51 ARG HA H 4.24 . 1 470 . 51 ARG HB2 H 1.87 . 2 471 . 51 ARG HB3 H 1.85 . 2 472 . 51 ARG HG2 H 1.65 . 2 473 . 51 ARG HG3 H 1.57 . 2 474 . 51 ARG HD2 H 3.18 . 1 475 . 51 ARG HD3 H 3.18 . 1 476 . 51 ARG CA C 56.2 . 1 477 . 51 ARG CB C 28.7 . 1 478 . 51 ARG CG C 25.8 . 1 479 . 51 ARG CD C 41.4 . 1 480 . 51 ARG N N 124.9 . 1 481 . 52 ARG H H 7.48 . 1 482 . 52 ARG HA H 4.29 . 1 483 . 52 ARG HB2 H 1.64 . 2 484 . 52 ARG HB3 H 1.38 . 2 485 . 52 ARG HG2 H 1.59 . 2 486 . 52 ARG HG3 H 1.26 . 2 487 . 52 ARG HD2 H 2.55 . 2 488 . 52 ARG HD3 H 2.29 . 2 489 . 52 ARG HE H 6.53 . 1 490 . 52 ARG CA C 55.7 . 1 491 . 52 ARG CB C 32.00 . 1 492 . 52 ARG CG C 25.6 . 1 493 . 52 ARG CD C 42.4 . 1 494 . 52 ARG N N 124.2 . 1 495 . 52 ARG NE N 90.4 . 1 496 . 53 LEU H H 7.78 . 1 497 . 53 LEU HA H 5.5 . 1 498 . 53 LEU HB2 H 2.02 . 2 499 . 53 LEU HB3 H 1.06 . 2 500 . 53 LEU HG H 1.57 . 1 501 . 53 LEU HD1 H 0.78 . 2 502 . 53 LEU HD2 H 0.92 . 2 503 . 53 LEU CA C 51.7 . 1 504 . 53 LEU CB C 43.1 . 1 505 . 53 LEU CG C 25.9 . 1 506 . 53 LEU CD1 C 24.3 . 2 507 . 53 LEU CD2 C 22.3 . 2 508 . 53 LEU N N 125.3 . 1 509 . 54 SER H H 8.33 . 1 510 . 54 SER HA H 4.75 . 1 511 . 54 SER HB2 H 3.81 . 2 512 . 54 SER HB3 H 3.76 . 2 513 . 54 SER CA C 55.5 . 1 514 . 54 SER CB C 63.9 . 1 515 . 54 SER N N 121.8 . 1 516 . 55 VAL H H 8.34 . 1 517 . 55 VAL HA H 5.34 . 1 518 . 55 VAL HB H 2.05 . 1 519 . 55 VAL HG1 H 0.92 . 2 520 . 55 VAL HG2 H 0.85 . 2 521 . 55 VAL CA C 58.4 . 1 522 . 55 VAL CB C 33.5 . 1 523 . 55 VAL CG1 C 21.00 . 2 524 . 55 VAL CG2 C 20.00 . 2 525 . 55 VAL N N 125.9 . 1 526 . 56 ASP H H 8.66 . 1 527 . 56 ASP HA H 4.96 . 1 528 . 56 ASP HB2 H 2.73 . 2 529 . 56 ASP HB3 H 2.61 . 2 530 . 56 ASP CA C 50.1 . 1 531 . 56 ASP CB C 43.8 . 1 532 . 56 ASP N N 129.6 . 1 533 . 57 PRO HA H 5.57 . 1 534 . 57 PRO HB2 H 2.75 . 2 535 . 57 PRO HB3 H 2.36 . 2 536 . 57 PRO HG2 H 2.3 . 2 537 . 57 PRO HG3 H 2.28 . 2 538 . 57 PRO HD2 H 3.92 . 2 539 . 57 PRO HD3 H 3.84 . 2 540 . 57 PRO CA C 60.8 . 1 541 . 57 PRO CB C 32.1 . 1 542 . 57 PRO CG C 23.5 . 1 543 . 57 PRO CD C 48.7 . 1 544 . 58 PRO HA H 4.57 . 1 545 . 58 PRO HD2 H 3.88 . 1 546 . 58 PRO HD3 H 3.88 . 1 547 . 58 PRO CA C 61.4 . 1 548 . 58 PRO CD C 48.2 . 1 549 . 59 CYS H H 6.86 . 1 550 . 59 CYS HA H 3.5 . 1 551 . 59 CYS HB2 H 2.4 . 1 552 . 59 CYS HB3 H 2.4 . 1 553 . 59 CYS CA C 52.6 . 1 554 . 59 CYS CB C 26.9 . 1 555 . 59 CYS N N 120.2 . 1 556 . 60 GLY H H 7.09 . 1 557 . 60 GLY HA2 H 3.98 . 2 558 . 60 GLY HA3 H 3.73 . 2 559 . 60 GLY CA C 43.8 . 1 560 . 60 GLY N N 111.5 . 1 561 . 61 VAL H H 8.31 . 1 562 . 61 VAL HA H 5.55 . 1 563 . 61 VAL HB H 1.97 . 1 564 . 61 VAL HG1 H 1.08 . 2 565 . 61 VAL HG2 H 1.22 . 2 566 . 61 VAL CA C 59.00 . 1 567 . 61 VAL CB C 34.2 . 1 568 . 61 VAL CG1 C 21.4 . 2 569 . 61 VAL CG2 C 20.5 . 2 570 . 61 VAL N N 125.3 . 1 571 . 62 LEU H H 9.23 . 1 572 . 62 LEU HA H 5.14 . 1 573 . 62 LEU HB2 H 1.64 . 1 574 . 62 LEU HB3 H 1.64 . 1 575 . 62 LEU HG H 1.62 . 1 576 . 62 LEU HD1 H 0.48 . 2 577 . 62 LEU HD2 H 0.79 . 2 578 . 62 LEU CA C 51.5 . 1 579 . 62 LEU CB C 46.5 . 1 580 . 62 LEU CG C 25.1 . 1 581 . 62 LEU CD1 C 24.00 . 2 582 . 62 LEU CD2 C 22.1 . 2 583 . 62 LEU N N 131.7 . 1 584 . 63 ASP H H 9.97 . 1 585 . 63 ASP HA H 5.05 . 1 586 . 63 ASP CA C 53.1 . 1 587 . 63 ASP N N 134.5 . 1 588 . 64 PRO HA H 3.87 . 1 589 . 64 PRO HB2 H 2.46 . 2 590 . 64 PRO HB3 H 1.8 . 2 591 . 64 PRO HD2 H 3.58 . 2 592 . 64 PRO HD3 H 3.34 . 2 593 . 64 PRO CA C 64.3 . 1 594 . 64 PRO CB C 29.8 . 1 595 . 64 PRO CD C 49.3 . 1 596 . 65 LYS H H 8.49 . 1 597 . 65 LYS HA H 3.74 . 1 598 . 65 LYS HB2 H 2.27 . 2 599 . 65 LYS HB3 H 1.94 . 2 600 . 65 LYS HG2 H 1.37 . 1 601 . 65 LYS HG3 H 1.37 . 1 602 . 65 LYS HD2 H 1.63 . 1 603 . 65 LYS HD3 H 1.63 . 1 604 . 65 LYS HE2 H 2.92 . 1 605 . 65 LYS HE3 H 2.92 . 1 606 . 65 LYS CA C 57.4 . 1 607 . 65 LYS CB C 28.3 . 1 608 . 65 LYS CG C 23.7 . 1 609 . 65 LYS CD C 27.8 . 1 610 . 65 LYS CE C 40.2 . 1 611 . 65 LYS N N 124.8 . 1 612 . 66 GLU H H 8.25 . 1 613 . 66 GLU HA H 4.26 . 1 614 . 66 GLU HB2 H 2.22 . 2 615 . 66 GLU HB3 H 1.93 . 2 616 . 66 GLU HG2 H 2.51 . 1 617 . 66 GLU HG3 H 2.51 . 1 618 . 66 GLU CA C 55.3 . 1 619 . 66 GLU CB C 29.6 . 1 620 . 66 GLU CG C 35.6 . 1 621 . 66 GLU N N 129.7 . 1 622 . 67 LYS H H 8.07 . 1 623 . 67 LYS HA H 5.74 . 1 624 . 67 LYS HB2 H 1.64 . 2 625 . 67 LYS HB3 H 1.5 . 2 626 . 67 LYS HG2 H 1.48 . 2 627 . 67 LYS HG3 H 1.28 . 2 628 . 67 LYS HD2 H 1.48 . 1 629 . 67 LYS HD3 H 1.48 . 1 630 . 67 LYS HE2 H 2.94 . 1 631 . 67 LYS HE3 H 2.94 . 1 632 . 67 LYS CA C 51.7 . 1 633 . 67 LYS CB C 35.2 . 1 634 . 67 LYS CG C 22.1 . 1 635 . 67 LYS CD C 28.3 . 1 636 . 67 LYS CE C 40.6 . 1 637 . 67 LYS N N 127.6 . 1 638 . 68 VAL H H 8.78 . 1 639 . 68 VAL HA H 4.47 . 1 640 . 68 VAL HB H 2.13 . 1 641 . 68 VAL HG1 H 1.07 . 2 642 . 68 VAL HG2 H 0.59 . 2 643 . 68 VAL CA C 58.4 . 1 644 . 68 VAL CB C 33.8 . 1 645 . 68 VAL CG1 C 19.9 . 2 646 . 68 VAL CG2 C 18.00 . 2 647 . 68 VAL N N 126.5 . 1 648 . 69 LEU H H 8.23 . 1 649 . 69 LEU HA H 5.00 . 1 650 . 69 LEU HB2 H 1.55 . 2 651 . 69 LEU HB3 H 1.44 . 2 652 . 69 LEU HG H 1.4 . 1 653 . 69 LEU HD1 H 0.77 . 2 654 . 69 LEU HD2 H 0.67 . 2 655 . 69 LEU CA C 51.7 . 1 656 . 69 LEU CB C 41.9 . 1 657 . 69 LEU CG C 26.00 . 1 658 . 69 LEU CD1 C 23.00 . 1 659 . 69 LEU CD2 C 23.00 . 1 660 . 69 LEU N N 134.6 . 1 661 . 70 MET H H 9.17 . 1 662 . 70 MET HA H 4.94 . 1 663 . 70 MET HB2 H 1.93 . 2 664 . 70 MET HB3 H 1.86 . 2 665 . 70 MET HG2 H 2.43 . 2 666 . 70 MET HG3 H 2.35 . 2 667 . 70 MET HE H 1.6 . 1 668 . 70 MET CA C 53.00 . 1 669 . 70 MET CB C 33.5 . 1 670 . 70 MET CG C 29.5 . 1 671 . 70 MET CE C 16.00 . 1 672 . 70 MET N N 132.7 . 1 673 . 71 ALA H H 8.98 . 1 674 . 71 ALA HA H 4.81 . 1 675 . 71 ALA HB H 1.4 . 1 676 . 71 ALA CA C 49.5 . 1 677 . 71 ALA CB C 18.9 . 1 678 . 71 ALA N N 134.00 . 1 679 . 72 VAL H H 9.04 . 1 680 . 72 VAL HA H 4.96 . 1 681 . 72 VAL HB H 2.02 . 1 682 . 72 VAL HG1 H 0.91 . 2 683 . 72 VAL HG2 H 0.98 . 2 684 . 72 VAL CA C 58.9 . 1 685 . 72 VAL CB C 33.00 . 1 686 . 72 VAL CG1 C 20.5 . 2 687 . 72 VAL CG2 C 19.2 . 2 688 . 72 VAL N N 131.4 . 1 689 . 73 SER H H 9.33 . 1 690 . 73 SER HA H 5.51 . 1 691 . 73 SER HB2 H 3.68 . 2 692 . 73 SER HB3 H 3.61 . 2 693 . 73 SER CA C 55.7 . 1 694 . 73 SER CB C 63.4 . 1 695 . 73 SER N N 129.6 . 1 696 . 74 CYS H H 8.86 . 1 697 . 74 CYS HA H 5.11 . 1 698 . 74 CYS HB2 H 2.76 . 1 699 . 74 CYS HB3 H 1.71 . 1 700 . 74 CYS CA C 55.2 . 1 701 . 74 CYS CB C 26.7 . 1 702 . 74 CYS N N 131.6 . 1 703 . 75 ASP H H 8.73 . 1 704 . 75 ASP HA H 4.71 . 1 705 . 75 ASP HB2 H 2.89 . 2 706 . 75 ASP HB3 H 2.73 . 2 707 . 75 ASP CA C 51.9 . 1 708 . 75 ASP CB C 39.9 . 1 709 . 75 ASP N N 134.5 . 1 710 . 76 THR H H 8.6 . 1 711 . 76 THR HA H 4.3 . 1 712 . 76 THR HB H 3.94 . 1 713 . 76 THR HG2 H 1.06 . 1 714 . 76 THR CA C 60.3 . 1 715 . 76 THR CB C 68.2 . 1 716 . 76 THR CG2 C 19.00 . 1 717 . 76 THR N N 118.9 . 1 718 . 77 PHE H H 7.81 . 1 719 . 77 PHE HA H 4.66 . 1 720 . 77 PHE HB2 H 3.1 . 1 721 . 77 PHE HB3 H 2.87 . 1 722 . 77 PHE HD1 H 6.84 . 1 723 . 77 PHE HD2 H 6.84 . 1 724 . 77 PHE HE1 H 6.5 . 1 725 . 77 PHE HE2 H 6.5 . 1 726 . 77 PHE HZ H 5.67 . 1 727 . 77 PHE CA C 54.9 . 1 728 . 77 PHE CB C 37.6 . 1 729 . 77 PHE CD1 C 130.6 . 1 730 . 77 PHE CD2 C 130.6 . 1 731 . 77 PHE CE1 C 129.00 . 1 732 . 77 PHE CE2 C 129.00 . 1 733 . 77 PHE CZ C 128.3 . 1 734 . 77 PHE N N 125.7 . 1 735 . 78 ASN H H 8.54 . 1 736 . 78 ASN HA H 4.66 . 1 737 . 78 ASN HB2 H 3.24 . 1 738 . 78 ASN HB3 H 2.61 . 1 739 . 78 ASN HD21 H 7.54 . 1 740 . 78 ASN HD22 H 6.98 . 1 741 . 78 ASN CA C 49.9 . 1 742 . 78 ASN CB C 36.7 . 1 743 . 78 ASN N N 125.2 . 1 744 . 78 ASN ND2 N 118.9 . 1 745 . 79 ALA H H 8.2 . 1 746 . 79 ALA HA H 3.87 . 1 747 . 79 ALA HB H 1.27 . 1 748 . 79 ALA CA C 52.5 . 1 749 . 79 ALA CB C 17.2 . 1 750 . 79 ALA N N 134.3 . 1 751 . 80 ALA H H 8.05 . 1 752 . 80 ALA HA H 4.29 . 1 753 . 80 ALA HB H 1.47 . 1 754 . 80 ALA CA C 51.9 . 1 755 . 80 ALA CB C 17.5 . 1 756 . 80 ALA N N 123.4 . 1 757 . 81 THR H H 7.27 . 1 758 . 81 THR HA H 4.51 . 1 759 . 81 THR HB H 4.37 . 1 760 . 81 THR HG2 H 1.06 . 1 761 . 81 THR CA C 59.7 . 1 762 . 81 THR CB C 68.00 . 1 763 . 81 THR CG2 C 19.8 . 1 764 . 81 THR N N 112.00 . 1 765 . 82 GLU H H 7.27 . 1 766 . 82 GLU HA H 4.45 . 1 767 . 82 GLU HB2 H 1.8 . 2 768 . 82 GLU HB3 H 1.55 . 2 769 . 82 GLU HG2 H 2.28 . 1 770 . 82 GLU HG3 H 2.28 . 1 771 . 82 GLU CA C 53.8 . 1 772 . 82 GLU CB C 30.5 . 1 773 . 82 GLU CG C 34.5 . 1 774 . 82 GLU N N 127.8 . 1 775 . 83 ASP H H 8.36 . 1 776 . 83 ASP HA H 4.51 . 1 777 . 83 ASP HB2 H 2.77 . 1 778 . 83 ASP HB3 H 2.59 . 1 779 . 83 ASP CA C 52.7 . 1 780 . 83 ASP CB C 38.8 . 1 781 . 83 ASP N N 126.4 . 1 782 . 84 LEU H H 8.65 . 1 783 . 84 LEU HA H 4.29 . 1 784 . 84 LEU HB2 H 1.77 . 2 785 . 84 LEU HB3 H 1.6 . 2 786 . 84 LEU HG H 1.65 . 1 787 . 84 LEU HD1 H 0.91 . 1 788 . 84 LEU HD2 H 0.14 . 1 789 . 84 LEU CA C 52.7 . 1 790 . 84 LEU CB C 39.9 . 1 791 . 84 LEU CG C 24.6 . 1 792 . 84 LEU CD1 C 24.5 . 2 793 . 84 LEU CD2 C 20.2 . 2 794 . 84 LEU N N 133.00 . 1 795 . 85 ASN H H 8.46 . 1 796 . 85 ASN HA H 5.04 . 1 797 . 85 ASN HB2 H 2.93 . 1 798 . 85 ASN HB3 H 2.79 . 1 799 . 85 ASN HD21 H 7.72 . 1 800 . 85 ASN HD22 H 6.93 . 1 801 . 85 ASN CA C 53.1 . 1 802 . 85 ASN CB C 39.1 . 1 803 . 85 ASN N N 125.5 . 1 804 . 85 ASN ND2 N 120.6 . 1 805 . 86 ASN H H 8.68 . 1 806 . 86 ASN HA H 4.99 . 1 807 . 86 ASN HB2 H 2.98 . 1 808 . 86 ASN HB3 H 2.56 . 1 809 . 86 ASN HD21 H 8.32 . 1 810 . 86 ASN HD22 H 6.88 . 1 811 . 86 ASN CA C 52.1 . 1 812 . 86 ASN CB C 39.00 . 1 813 . 86 ASN N N 125.8 . 1 814 . 86 ASN ND2 N 123.7 . 1 815 . 87 ASP H H 9.26 . 1 816 . 87 ASP HA H 5.03 . 1 817 . 87 ASP HB2 H 2.85 . 1 818 . 87 ASP HB3 H 2.26 . 1 819 . 87 ASP CA C 52.7 . 1 820 . 87 ASP CB C 40.7 . 1 821 . 87 ASP N N 129.00 . 1 822 . 88 ARG H H 8.29 . 1 823 . 88 ARG HA H 4.72 . 1 824 . 88 ARG HB2 H 1.82 . 2 825 . 88 ARG HB3 H 1.45 . 2 826 . 88 ARG CA C 53.6 . 1 827 . 88 ARG CB C 31.8 . 1 828 . 88 ARG N N 126.00 . 1 829 . 89 ILE H H 8.38 . 1 830 . 89 ILE HA H 4.58 . 1 831 . 89 ILE HB H 1.84 . 1 832 . 89 ILE HG12 H 1.5 . 2 833 . 89 ILE HG13 H 1.08 . 2 834 . 89 ILE HG2 H 0.82 . 1 835 . 89 ILE HD1 H 0.73 . 1 836 . 89 ILE CA C 58.4 . 1 837 . 89 ILE CB C 39.00 . 1 838 . 89 ILE CG1 C 26.3 . 1 839 . 89 ILE CG2 C 15.8 . 1 840 . 89 ILE CD1 C 12.3 . 1 841 . 89 ILE N N 127.7 . 1 842 . 90 THR H H 9.15 . 1 843 . 90 THR HA H 5.16 . 1 844 . 90 THR HB H 3.78 . 1 845 . 90 THR HG2 H 1.18 . 1 846 . 90 THR CA C 60.6 . 1 847 . 90 THR CB C 70.3 . 1 848 . 90 THR CG2 C 20.1 . 1 849 . 90 THR N N 130.9 . 1 850 . 91 ILE H H 9.3 . 1 851 . 91 ILE HA H 4.85 . 1 852 . 91 ILE HB H 1.81 . 1 853 . 91 ILE HG12 H 1.55 . 2 854 . 91 ILE HG13 H 0.8 . 2 855 . 91 ILE HG2 H 0.93 . 1 856 . 91 ILE HD1 H 0.56 . 1 857 . 91 ILE CA C 59.2 . 1 858 . 91 ILE CB C 38.9 . 1 859 . 91 ILE CG1 C 26.3 . 1 860 . 91 ILE CG2 C 16.4 . 1 861 . 91 ILE CD1 C 13.5 . 1 862 . 91 ILE N N 134.3 . 1 863 . 92 GLU H H 9.46 . 1 864 . 92 GLU HA H 5.95 . 1 865 . 92 GLU HB2 H 2.1 . 1 866 . 92 GLU HB3 H 1.91 . 2 867 . 92 GLU HG2 H 2.26 . 2 868 . 92 GLU HG3 H 2.08 . 1 869 . 92 GLU CA C 52.7 . 1 870 . 92 GLU CB C 32.2 . 1 871 . 92 GLU CG C 36.1 . 1 872 . 92 GLU N N 133.3 . 1 873 . 93 TRP H H 9.35 . 1 874 . 93 TRP HA H 6.39 . 1 875 . 93 TRP HD1 H 6.76 . 1 876 . 93 TRP HE1 H 10.65 . 1 877 . 93 TRP HE3 H 7.26 . 1 878 . 93 TRP HZ2 H 7.39 . 1 879 . 93 TRP HZ3 H 6.86 . 1 880 . 93 TRP HH2 H 7.06 . 1 881 . 93 TRP CA C 56.6 . 1 882 . 93 TRP CD1 C 124.1 . 1 883 . 93 TRP CE3 C 121.7 . 1 884 . 93 TRP CZ2 C 112.9 . 1 885 . 93 TRP CZ3 C 119.9 . 1 886 . 93 TRP CH2 C 123.2 . 1 887 . 93 TRP N N 127.00 . 1 888 . 93 TRP NE1 N 135.3 . 1 889 . 94 THR H H 8.77 . 1 890 . 94 THR HA H 4.56 . 1 891 . 94 THR HB H 3.74 . 1 892 . 94 THR HG2 H 0.48 . 1 893 . 94 THR CA C 58.8 . 1 894 . 94 THR CB C 70.2 . 1 895 . 94 THR CG2 C 15.3 . 1 896 . 94 THR N N 119.5 . 1 897 . 95 ASN H H 8.22 . 1 898 . 95 ASN HA H 5.24 . 1 899 . 95 ASN HB2 H 2.7 . 1 900 . 95 ASN HB3 H 2.7 . 1 901 . 95 ASN HD21 H 7.13 . 1 902 . 95 ASN HD22 H 6.5 . 1 903 . 95 ASN CA C 51.8 . 1 904 . 95 ASN CB C 36.4 . 1 905 . 95 ASN N N 130.5 . 1 906 . 95 ASN ND2 N 116.00 . 1 907 . 96 THR H H 7.98 . 1 908 . 96 THR HA H 3.25 . 1 909 . 96 THR HB H 3.31 . 1 910 . 96 THR HG2 H 0.33 . 1 911 . 96 THR CA C 58.4 . 1 912 . 96 THR CB C 64.9 . 1 913 . 96 THR CG2 C 21.5 . 1 914 . 96 THR N N 120.6 . 1 915 . 97 PRO HA H 4.33 . 1 916 . 97 PRO HB2 H 2.25 . 2 917 . 97 PRO HB3 H 1.79 . 2 918 . 97 PRO HG2 H 1.89 . 1 919 . 97 PRO HG3 H 1.89 . 1 920 . 97 PRO HD2 H 2.28 . 2 921 . 97 PRO HD3 H 2.56 . 2 922 . 97 PRO CA C 60.9 . 1 923 . 97 PRO CB C 30.00 . 1 924 . 97 PRO CG C 26.3 . 1 925 . 97 PRO CD C 48.00 . 1 926 . 98 ASP H H 8.54 . 1 927 . 98 ASP HA H 4.34 . 1 928 . 98 ASP HB2 H 2.61 . 2 929 . 98 ASP HB3 H 2.54 . 2 930 . 98 ASP CA C 54.4 . 1 931 . 98 ASP CB C 39.3 . 1 932 . 98 ASP N N 129.9 . 1 933 . 99 GLY H H 8.78 . 1 934 . 99 GLY HA2 H 4.11 . 2 935 . 99 GLY HA3 H 3.74 . 2 936 . 99 GLY CA C 43.8 . 1 937 . 99 GLY N N 118.4 . 1 938 . 100 ALA H H 7.44 . 1 939 . 100 ALA HA H 4.37 . 1 940 . 100 ALA HB H 1.49 . 1 941 . 100 ALA CA C 50.9 . 1 942 . 100 ALA CB C 18.5 . 1 943 . 100 ALA N N 129.2 . 1 944 . 101 ALA H H 8.4 . 1 945 . 101 ALA HA H 4.46 . 1 946 . 101 ALA HB H 1.55 . 1 947 . 101 ALA CA C 50.00 . 1 948 . 101 ALA CB C 17.4 . 1 949 . 101 ALA N N 130.6 . 1 950 . 102 LYS H H 8.59 . 1 951 . 102 LYS HA H 4.29 . 1 952 . 102 LYS HB2 H 2.16 . 1 953 . 102 LYS HB3 H 2.16 . 1 954 . 102 LYS CA C 54.7 . 1 955 . 102 LYS CB C 29.9 . 1 956 . 102 LYS N N 128.4 . 1 957 . 103 GLN H H 7.82 . 1 958 . 103 GLN HA H 4.52 . 1 959 . 103 GLN HB2 H 1.9 . 1 960 . 103 GLN HB3 H 1.9 . 1 961 . 103 GLN HG2 H 2.26 . 1 962 . 103 GLN HG3 H 2.26 . 1 963 . 103 GLN CA C 53.4 . 1 964 . 103 GLN CB C 29.4 . 1 965 . 103 GLN CG C 32.00 . 1 966 . 103 GLN N N 128.00 . 1 967 . 104 PHE H H 8.89 . 1 968 . 104 PHE HA H 3.52 . 1 969 . 104 PHE HB2 H 2.72 . 1 970 . 104 PHE HB3 H 2.66 . 1 971 . 104 PHE HD1 H 7.01 . 1 972 . 104 PHE HD2 H 7.01 . 1 973 . 104 PHE HE1 H 6.98 . 1 974 . 104 PHE HE2 H 6.98 . 1 975 . 104 PHE HZ H 6.56 . 1 976 . 104 PHE CA C 59.00 . 1 977 . 104 PHE CB C 38.3 . 1 978 . 104 PHE CD1 C 130.6 . 1 979 . 104 PHE CD2 C 130.6 . 1 980 . 104 PHE CE1 C 130.1 . 1 981 . 104 PHE CE2 C 130.1 . 1 982 . 104 PHE CZ C 128.3 . 1 983 . 104 PHE N N 132.4 . 1 984 . 105 ARG H H 3.64 . 1 985 . 105 ARG HA H 3.94 . 1 986 . 105 ARG HB2 H 1.1 . 1 987 . 105 ARG HB3 H -0.74 . 1 988 . 105 ARG HG2 H 1.09 . 1 989 . 105 ARG HG3 H 1.00 . 1 990 . 105 ARG HD2 H 3.02 . 1 991 . 105 ARG HD3 H 2.91 . 1 992 . 105 ARG HE H 7.14 . 1 993 . 105 ARG CA C 51.2 . 1 994 . 105 ARG CB C 28.6 . 1 995 . 105 ARG CG C 24.4 . 1 996 . 105 ARG CD C 41.3 . 1 997 . 105 ARG N N 130.9 . 1 998 . 105 ARG NE N 92.00 . 1 999 . 106 ARG H H 8.33 . 1 1000 . 106 ARG HA H 3.6 . 1 1001 . 106 ARG HB2 H 1.8 . 1 1002 . 106 ARG HB3 H 1.74 . 1 1003 . 106 ARG HG2 H 1.72 . 1 1004 . 106 ARG HG3 H 1.66 . 1 1005 . 106 ARG HD2 H 3.18 . 1 1006 . 106 ARG HD3 H 3.18 . 1 1007 . 106 ARG CA C 56.2 . 1 1008 . 106 ARG CB C 27.7 . 1 1009 . 106 ARG CG C 25.1 . 1 1010 . 106 ARG CD C 41.3 . 1 1011 . 106 ARG N N 130.2 . 1 1012 . 107 GLU H H 9.4 . 1 1013 . 107 GLU HA H 3.95 . 1 1014 . 107 GLU HB2 H 1.96 . 1 1015 . 107 GLU HB3 H 1.84 . 1 1016 . 107 GLU HG2 H 2.23 . 1 1017 . 107 GLU HG3 H 2.23 . 1 1018 . 107 GLU CA C 58.1 . 1 1019 . 107 GLU CB C 26.5 . 1 1020 . 107 GLU CG C 35.1 . 1 1021 . 107 GLU N N 125.7 . 1 1022 . 108 TRP H H 7.18 . 1 1023 . 108 TRP HA H 4.66 . 2 1024 . 108 TRP HB2 H 2.88 . 2 1025 . 108 TRP HB3 H 2.88 . 1 1026 . 108 TRP HD1 H 7.06 . 1 1027 . 108 TRP HE1 H 10.47 . 1 1028 . 108 TRP HE3 H 6.94 . 1 1029 . 108 TRP HZ2 H 7.54 . 1 1030 . 108 TRP HZ3 H 6.94 . 1 1031 . 108 TRP HH2 H 7.17 . 1 1032 . 108 TRP CA C 55.00 . 1 1033 . 108 TRP CB C 26.5 . 1 1034 . 108 TRP CD1 C 122.8 . 1 1035 . 108 TRP CE3 C 118.1 . 1 1036 . 108 TRP CZ2 C 113.9 . 1 1037 . 108 TRP CZ3 C 118.5 . 1 1038 . 108 TRP CH2 C 125.3 . 1 1039 . 108 TRP N N 126.4 . 1 1040 . 108 TRP NE1 N 135.9 . 1 1041 . 109 PHE H H 7.97 . 1 1042 . 109 PHE HA H 4.36 . 1 1043 . 109 PHE HB2 H 3.45 . 2 1044 . 109 PHE HB3 H 3.11 . 2 1045 . 109 PHE HD1 H 7.29 . 1 1046 . 109 PHE HD2 H 7.29 . 1 1047 . 109 PHE HE1 H 7.29 . 1 1048 . 109 PHE HE2 H 7.29 . 1 1049 . 109 PHE HZ H 7.4 . 1 1050 . 109 PHE CA C 55.8 . 1 1051 . 109 PHE CB C 36.8 . 1 1052 . 109 PHE CD1 C 130.2 . 1 1053 . 109 PHE CD2 C 130.2 . 1 1054 . 109 PHE CE1 C 130.2 . 1 1055 . 109 PHE CE2 C 130.2 . 1 1056 . 109 PHE CZ C 127.7 . 1 1057 . 109 PHE N N 122.2 . 1 1058 . 110 GLN H H 7.53 . 1 1059 . 110 GLN HA H 4.57 . 1 1060 . 110 GLN HB2 H 2.29 . 2 1061 . 110 GLN HB3 H 2.01 . 2 1062 . 110 GLN HG2 H 2.38 . 1 1063 . 110 GLN HG3 H 2.38 . 1 1064 . 110 GLN CA C 53.7 . 1 1065 . 110 GLN CB C 28.5 . 1 1066 . 110 GLN CG C 32.2 . 1 1067 . 110 GLN N N 126.1 . 1 1068 . 111 GLY H H 8.23 . 1 1069 . 111 GLY HA2 H 4.1 . 2 1070 . 111 GLY HA3 H 3.98 . 2 1071 . 111 GLY CA C 44.00 . 1 1072 . 111 GLY N N 116.5 . 1 1073 . 112 ASP H H 8.41 . 1 1074 . 112 ASP HA H 4.61 . 1 1075 . 112 ASP HB2 H 2.69 . 1 1076 . 112 ASP HB3 H 2.69 . 1 1077 . 112 ASP CA C 52.9 . 1 1078 . 112 ASP CB C 39.5 . 1 1079 . 112 ASP N N 129.1 . 1 1080 . 113 GLY H H 8.22 . 1 1081 . 113 GLY HA2 H 3.98 . 2 1082 . 113 GLY HA3 H 3.81 . 2 1083 . 113 GLY CA C 43.7 . 1 1084 . 113 GLY N N 115.7 . 1 1085 . 114 MET H H 8.28 . 1 1086 . 114 MET HA H 4.44 . 1 1087 . 114 MET HB2 H 1.94 . 2 1088 . 114 MET HB3 H 1.87 . 2 1089 . 114 MET HG2 H 2.52 . 1 1090 . 114 MET HG3 H 2.32 . 1 1091 . 114 MET HE H 2.04 . 1 1092 . 114 MET CA C 53.8 . 1 1093 . 114 MET CB C 31.6 . 1 1094 . 114 MET CG C 31.00 . 1 1095 . 114 MET CE C 16.1 . 1 1096 . 114 MET N N 127.3 . 1 1097 . 115 VAL H H 8.27 . 1 1098 . 115 VAL HA H 4.35 . 1 1099 . 115 VAL HB H 1.9 . 1 1100 . 115 VAL HG1 H 0.83 . 2 1101 . 115 VAL HG2 H 0.78 . 2 1102 . 115 VAL CA C 59.6 . 1 1103 . 115 VAL CB C 31.8 . 1 1104 . 115 VAL CG1 C 20.00 . 2 1105 . 115 VAL CG2 C 19.1 . 2 1106 . 115 VAL N N 133.5 . 1 1107 . 116 ARG H H 8.31 . 1 1108 . 116 ARG HA H 4.2 . 1 1109 . 116 ARG HB2 H 0.73 . 2 1110 . 116 ARG HB3 H -0.46 . 2 1111 . 116 ARG HG2 H 1.3 . 2 1112 . 116 ARG HG3 H 1.24 . 2 1113 . 116 ARG HD2 H 3.2 . 2 1114 . 116 ARG HD3 H 2.78 . 2 1115 . 116 ARG HE H 7.2 . 1 1116 . 116 ARG CA C 53.2 . 1 1117 . 116 ARG CB C 30.6 . 1 1118 . 116 ARG CG C 25.7 . 1 1119 . 116 ARG CD C 42.3 . 1 1120 . 116 ARG N N 133.6 . 1 1121 . 116 ARG NE N 91.6 . 1 1122 . 117 ARG H H 7.85 . 1 1123 . 117 ARG HA H 5.8 . 1 1124 . 117 ARG HB2 H 1.63 . 2 1125 . 117 ARG HB3 H 1.53 . 2 1126 . 117 ARG HG2 H 1.48 . 1 1127 . 117 ARG HG3 H 1.48 . 1 1128 . 117 ARG HD2 H 3.17 . 2 1129 . 117 ARG HD3 H 3.06 . 2 1130 . 117 ARG HE H 7.66 . 1 1131 . 117 ARG CA C 53.1 . 1 1132 . 117 ARG CB C 33.2 . 1 1133 . 117 ARG CG C 26.5 . 1 1134 . 117 ARG CD C 41.8 . 1 1135 . 117 ARG N N 122.1 . 1 1136 . 117 ARG NE N 91.8 . 1 1137 . 118 LYS H H 9.44 . 1 1138 . 118 LYS HA H 4.74 . 1 1139 . 118 LYS HE2 H 3.00 . 1 1140 . 118 LYS HE3 H 3.00 . 1 1141 . 118 LYS CA C 54.1 . 1 1142 . 118 LYS CE C 41.4 . 1 1143 . 118 LYS N N 130.3 . 1 1144 . 119 ASN H H 9.1 . 1 1145 . 119 ASN HA H 5.53 . 1 1146 . 119 ASN HB2 H 2.8 . 2 1147 . 119 ASN HB3 H 2.29 . 2 1148 . 119 ASN HD21 H 7.67 . 1 1149 . 119 ASN HD22 H 6.87 . 1 1150 . 119 ASN CA C 50.6 . 1 1151 . 119 ASN CB C 39.7 . 1 1152 . 119 ASN N N 131.3 . 1 1153 . 119 ASN ND2 N 121.00 . 1 1154 . 120 LEU H H 9.43 . 1 1155 . 120 LEU HA H 4.93 . 1 1156 . 120 LEU HB2 H 1.5 . 2 1157 . 120 LEU HB3 H 1.14 . 2 1158 . 120 LEU HG H 1.26 . 1 1159 . 120 LEU HD1 H 0.59 . 2 1160 . 120 LEU HD2 H 0.51 . 2 1161 . 120 LEU CA C 50.3 . 1 1162 . 120 LEU CB C 42.7 . 1 1163 . 120 LEU CG C 25.8 . 1 1164 . 120 LEU CD1 C 23.9 . 2 1165 . 120 LEU CD2 C 23.00 . 2 1166 . 120 LEU N N 131.3 . 1 1167 . 121 PRO HA H 4.33 . 1 1168 . 121 PRO HB2 H 2.37 . 2 1169 . 121 PRO HB3 H 1.81 . 2 1170 . 121 PRO HG2 H 1.19 . 2 1171 . 121 PRO HG3 H 0.57 . 2 1172 . 121 PRO HD2 H 4.41 . 2 1173 . 121 PRO HD3 H 3.6 . 2 1174 . 121 PRO CA C 61.4 . 1 1175 . 121 PRO CB C 31.00 . 1 1176 . 121 PRO CG C 25.8 . 1 1177 . 121 PRO CD C 49.8 . 1 1178 . 122 ILE H H 7.47 . 1 1179 . 122 ILE HA H 4.48 . 1 1180 . 122 ILE HB H 1.17 . 1 1181 . 122 ILE HG12 H 1.19 . 2 1182 . 122 ILE HG13 H 0.57 . 2 1183 . 122 ILE HG2 H -0.24 . 1 1184 . 122 ILE HD1 H 0.54 . 1 1185 . 122 ILE CA C 57.2 . 1 1186 . 122 ILE CB C 37.00 . 1 1187 . 122 ILE CG1 C 25.8 . 1 1188 . 122 ILE CG2 C 15.2 . 1 1189 . 122 ILE CD1 C 12.4 . 1 1190 . 122 ILE N N 127.5 . 1 1191 . 123 GLU H H 8.46 . 1 1192 . 123 GLU HA H 4.68 . 1 1193 . 123 GLU HB2 H 1.85 . 2 1194 . 123 GLU HB3 H 1.75 . 2 1195 . 123 GLU CA C 51.9 . 1 1196 . 123 GLU CB C 31.8 . 1 1197 . 123 GLU N N 134.6 . 1 1198 . 124 TYR H H 8.83 . 1 1199 . 124 TYR HA H 4.83 . 1 1200 . 124 TYR HB2 H 3.12 . 1 1201 . 124 TYR HB3 H 2.79 . 1 1202 . 124 TYR HD1 H 7.22 . 1 1203 . 124 TYR HD2 H 7.22 . 1 1204 . 124 TYR HE1 H 6.64 . 1 1205 . 124 TYR HE2 H 6.64 . 1 1206 . 124 TYR CA C 56.7 . 1 1207 . 124 TYR CB C 36.7 . 1 1208 . 124 TYR CD1 C 132.1 . 1 1209 . 124 TYR CD2 C 132.1 . 1 1210 . 124 TYR CE1 C 116.8 . 1 1211 . 124 TYR CE2 C 116.8 . 1 1212 . 124 TYR N N 130.6 . 1 1213 . 125 ASN H H 8.43 . 1 1214 . 125 ASN HA H 4.97 . 1 1215 . 125 ASN HB2 H 2.89 . 2 1216 . 125 ASN HB3 H 2.45 . 2 1217 . 125 ASN HD21 H 8.96 . 1 1218 . 125 ASN HD22 H 7.36 . 1 1219 . 125 ASN CA C 51.8 . 1 1220 . 125 ASN CB C 38.3 . 1 1221 . 125 ASN N N 130.7 . 1 1222 . 125 ASN ND2 N 125.6 . 1 1223 . 126 LEU H H 8.2 . 1 1224 . 126 LEU HA H 4.41 . 1 1225 . 126 LEU HB2 H 1.78 . 1 1226 . 126 LEU HB3 H 1.78 . 1 1227 . 126 LEU HG H 1.9 . 1 1228 . 126 LEU HD1 H 1.04 . 1 1229 . 126 LEU HD2 H 1.04 . 1 1230 . 126 LEU CA C 56.7 . 1 1231 . 126 LEU CB C 42.6 . 1 1232 . 126 LEU CG C 26.8 . 1 1233 . 126 LEU CD1 C 24.1 . 2 1234 . 126 LEU CD2 C 23.5 . 2 1235 . 126 LEU N N 141.1 . 1 stop_ save_