data_5960 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N- Chemical Shift Assignments for Myristoylated HIV-1 Matrix Protein ; _BMRB_accession_number 5960 _BMRB_flat_file_name bmr5960.str _Entry_type original _Submission_date 2003-10-01 _Accession_date 2003-10-01 _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 Tang Chun . . 2 Loeliger Erin . . 3 Luncsford Paz . . 4 Kinde Isaac . . 5 Beckett Dorothy . . 6 Summers Michael F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 594 "13C chemical shifts" 500 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-11 update BMRB 'Updating non-standard residue' 2008-07-17 update BMRB 'Updating non-standard residue' 2007-03-23 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5316 'HIV-1 gag, p55' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'From the Cover: Entropic switch regulates myristate exposure in the HIV-1 matrix protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14699046 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tang Chun . . 2 Loeliger Erin . . 3 Luncsford Paz . . 4 Kinde Isaac . . 5 Beckett Dorothy . . 6 Summers Michael F. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 101 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 517 _Page_last 522 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_MA _Saveframe_category molecular_system _Mol_system_name 'myristoylated HIV-1 matrix' _Abbreviation_common MA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'matrix monomer' $MA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p17 _Abbreviation_common MA _Molecular_mass . _Mol_thiol_state 'all free' _Details 'Residue Glycine 1 is myristoylated' ############################## # Polymer residue sequence # ############################## _Residue_count 132 _Mol_residue_sequence ; XGARASVLSGGELDKWEKIR LRPGGKKQYKLKHIVWASRE LERFAVNPGLLETSEGCRQI LGQLQPSLQTGSEELRSLYN TIAVLYCVHQRIDVKDTKEA LDKIEEEQNKSKKKAQQAAA DTGNNSQVSQNY ; loop_ _Residue_seq_code _Residue_label 1 MYR 2 GLY 3 ALA 4 ARG 5 ALA 6 SER 7 VAL 8 LEU 9 SER 10 GLY 11 GLY 12 GLU 13 LEU 14 ASP 15 LYS 16 TRP 17 GLU 18 LYS 19 ILE 20 ARG 21 LEU 22 ARG 23 PRO 24 GLY 25 GLY 26 LYS 27 LYS 28 GLN 29 TYR 30 LYS 31 LEU 32 LYS 33 HIS 34 ILE 35 VAL 36 TRP 37 ALA 38 SER 39 ARG 40 GLU 41 LEU 42 GLU 43 ARG 44 PHE 45 ALA 46 VAL 47 ASN 48 PRO 49 GLY 50 LEU 51 LEU 52 GLU 53 THR 54 SER 55 GLU 56 GLY 57 CYS 58 ARG 59 GLN 60 ILE 61 LEU 62 GLY 63 GLN 64 LEU 65 GLN 66 PRO 67 SER 68 LEU 69 GLN 70 THR 71 GLY 72 SER 73 GLU 74 GLU 75 LEU 76 ARG 77 SER 78 LEU 79 TYR 80 ASN 81 THR 82 ILE 83 ALA 84 VAL 85 LEU 86 TYR 87 CYS 88 VAL 89 HIS 90 GLN 91 ARG 92 ILE 93 ASP 94 VAL 95 LYS 96 ASP 97 THR 98 LYS 99 GLU 100 ALA 101 LEU 102 ASP 103 LYS 104 ILE 105 GLU 106 GLU 107 GLU 108 GLN 109 ASN 110 LYS 111 SER 112 LYS 113 LYS 114 LYS 115 ALA 116 GLN 117 GLN 118 ALA 119 ALA 120 ALA 121 ASP 122 THR 123 GLY 124 ASN 125 ASN 126 SER 127 GLN 128 VAL 129 SER 130 GLN 131 ASN 132 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15114 Gag_polyprotein 99.24 131 99.24 99.24 1.30e-88 BMRB 15116 Gag_polyprotein 99.24 131 99.24 99.24 2.13e-88 BMRB 18715 MA 99.24 131 100.00 100.00 1.74e-89 BMRB 18716 MA 99.24 131 100.00 100.00 1.74e-89 BMRB 5316 Gag283 99.24 288 100.00 100.00 6.35e-88 BMRB 7250 HIV-1_MA 99.24 131 100.00 100.00 1.74e-89 BMRB 7267 HIV-1_MA 99.24 131 100.00 100.00 1.74e-89 BMRB 7275 HIV-1_MA 99.24 131 100.00 100.00 1.74e-89 BMRB 7309 HIV-1_myrMA 99.24 132 100.00 100.00 1.80e-89 PDB 1HIW "Trimeric Hiv-1 Matrix Protein" 99.24 133 100.00 100.00 1.40e-89 PDB 1L6N "Structure Of The N-Terminal 283-Residue Fragment Of The Hiv- 1 Gag Polyprotein" 99.24 289 100.00 100.00 6.14e-88 PDB 1UPH "Hiv-1 Myristoylated Matrix" 98.48 132 100.00 100.00 2.13e-88 PDB 2GOL "Xray Structure Of Gag278" 99.24 133 100.00 100.00 1.40e-89 PDB 2H3F "Solution Structure Of The Hiv-1 Ma Protein" 98.48 131 100.00 100.00 2.06e-88 PDB 2H3I "Solution Structure Of The Hiv-1 Myristoylated Matrix Protein" 97.73 131 100.00 100.00 1.45e-87 PDB 2H3Q "Solution Structure Of Hiv-1 Myrma Bound To Di-c4-phosphatidylinositol- (4,5)-bisphosphate" 97.73 131 100.00 100.00 1.45e-87 PDB 2H3V "Structure Of The Hiv-1 Matrix Protein Bound To Di-C8- Phosphatidylinositol-(4,5)-Bisphosphate" 98.48 131 100.00 100.00 2.06e-88 PDB 2H3Z "Structure Of The Hiv-1 Matrix Protein Bound To Di-c4- Phosphatidylinositol-(4,5)-bisphosphate" 98.48 131 100.00 100.00 2.06e-88 PDB 2HMX "Human Immunodeficiency Virus Type 1 Matrix Protein" 98.48 133 100.00 100.00 1.62e-88 PDB 2JMG "Solution Structure Of V7r Mutant Of Hiv-1 Myristoylated Matrix Protein" 97.73 131 99.22 99.22 1.83e-86 PDB 2LYA "Structure Of Hiv-1 Myr(-) Matrix Protein In Complex With 1,2- Dioctanoyl-sn-phosphatidylcholine" 99.24 137 100.00 100.00 1.62e-89 PDB 2LYB "Structure Of Hiv-1 Myr(-) Matrix Protein In Complex With 1,2- Dioctanoyl-sn-phosphatidyl-l-serine" 99.24 137 100.00 100.00 1.62e-89 PDB 2NV3 "Solution Structure Of L8a Mutant Of Hiv-1 Myristoylated Matrix Protein" 97.73 131 99.22 99.22 1.04e-86 PDB 4JMU "Crystal Structure Of Hiv Matrix Residues 1-111 In Complex With Inhibitor" 83.33 112 100.00 100.00 2.18e-73 DBJ BAF34641 "gag polyprotein [HIV-1 vector pNL-DT5R]" 99.24 498 100.00 100.00 7.35e-85 DBJ BAG48474 "gag protein [Human immunodeficiency virus 1]" 99.24 147 100.00 100.00 1.23e-89 EMBL CBI61180 "gag polyprotein [HIV-1 M:B 2003_KC005]" 99.24 497 99.24 99.24 1.50e-83 EMBL CBI61181 "gag polyprotein [HIV-1 M:B 2003_KC005]" 99.24 497 99.24 99.24 2.99e-84 EMBL CBI61182 "gag polyprotein [HIV-1 M:B 2003_KC005]" 99.24 497 99.24 100.00 2.10e-84 EMBL CBI61183 "gag polyprotein [HIV-1 M:B 2003_KC005]" 99.24 497 99.24 99.24 3.83e-84 EMBL CBI61184 "gag polyprotein [HIV-1 M:B 2003_KC005]" 99.24 497 100.00 100.00 5.54e-85 GB AAA44987 "gag polyprotein [Human immunodeficiency virus 1]" 99.24 500 100.00 100.00 7.49e-85 GB AAB00898 "p17 protein, partial [Human immunodeficiency virus 1]" 78.03 117 97.09 99.03 6.95e-64 GB AAB60571 "Gag polyprotein precursor [Human immunodeficiency virus 1]" 99.24 500 100.00 100.00 7.49e-85 GB AAC28445 "gag protein [Human immunodeficiency virus 1]" 99.24 500 97.71 98.47 7.73e-83 GB AAC29216 "Gag [Human immunodeficiency virus 1]" 62.88 83 98.80 100.00 2.07e-52 SP P12493 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 99.24 500 100.00 100.00 7.49e-85 SP P12497 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 99.24 1435 100.00 100.00 7.29e-80 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_MYR _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'MYRISTIC ACID' _BMRB_code . _PDB_code MYR _Standard_residue_derivative . _Molecular_mass 228.371 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 09:28:18 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? HO2 HO2 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H121 H121 H . 0 . ? H122 H122 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H143 H143 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 C7 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING C8 C9 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C9 C10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C11 C12 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C12 C13 ? ? SING C12 H121 ? ? SING C12 H122 ? ? SING C13 C14 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C14 H143 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $MA HIV-1 11676 Viruses . Lentivirus 'Human immunodeficiency virus 1' 'pnl4-3, subclone 4.20' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $MA 'recombinant technology' . . . . . ; yeast N-terminal myristyl transferase and HIV-1 matrix protein were subcloned into a co-expression vector ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1x protease inhibitor cocktail set I (Calbiochem)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MA 0.2 mM 0.02 0.8 '[U-13C; U-15N]' 'sodium phosophate buffer' 50 mM . . . NaCl 50 mM . . . DTT 5 mM . . . DTT 5 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task processing stop_ _Details . save_ save_NMRVIEW _Saveframe_category software _Name NMRVIEW _Version 5.0.4 loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_13C-edited_HMQC-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-edited HMQC-NOESY' _Sample_label $sample_1 save_ save_2D_13C-edited_HMQC-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-edited HMQC-NOESY' _Sample_label $sample_1 save_ save_4D_13C,_13C-edited_HMQC-NOESY-HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C, 13C-edited HMQC-NOESY-HMQC' _Sample_label $sample_1 save_ save_3D_15N-_edited_NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N- edited NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 n/a temperature 308 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label water H 1 proton ppm 4.677408 internal direct spherical internal parallel 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'matrix monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MYR C14 C 15.978 0.05 1 2 . 1 MYR H141 H 0.552 0.02 1 3 . 1 MYR H142 H 0.552 0.02 1 4 . 1 MYR H143 H 0.552 0.02 1 5 . 1 MYR C13 C 24.302 0.05 1 6 . 1 MYR H131 H 0.941 0.02 1 7 . 1 MYR H132 H 0.941 0.02 1 8 . 1 MYR C12 C 33.665 0.05 1 9 . 1 MYR H121 H 0.980 0.02 2 10 . 1 MYR H122 H 0.944 0.02 2 11 . 1 MYR C11 C 31.432 0.05 1 12 . 1 MYR H111 H 1.019 0.02 1 13 . 1 MYR H112 H 1.019 0.02 1 14 . 1 MYR C10 C 31.432 0.05 1 15 . 1 MYR H101 H 1.019 0.02 1 16 . 1 MYR H102 H 1.019 0.02 1 17 . 1 MYR C9 C 31.432 0.05 1 18 . 1 MYR H91 H 1.019 0.02 1 19 . 1 MYR H92 H 1.019 0.02 1 20 . 1 MYR C8 C 31.432 0.05 1 21 . 1 MYR H81 H 1.019 0.02 1 22 . 1 MYR H82 H 1.019 0.02 1 23 . 1 MYR C7 C 31.432 0.05 1 24 . 1 MYR H71 H 1.019 0.02 1 25 . 1 MYR H72 H 1.019 0.02 1 26 . 1 MYR C6 C 31.432 0.05 1 27 . 1 MYR H61 H 1.019 0.02 1 28 . 1 MYR H62 H 1.019 0.02 1 29 . 1 MYR C5 C 31.432 0.05 1 30 . 1 MYR H51 H 1.019 0.02 1 31 . 1 MYR H52 H 1.019 0.02 1 32 . 1 MYR C4 C 31.100 0.05 1 33 . 1 MYR H41 H 1.091 0.02 1 34 . 1 MYR H42 H 1.091 0.02 1 35 . 1 MYR C3 C 27.350 0.05 1 36 . 1 MYR H31 H 1.401 0.02 1 37 . 1 MYR H32 H 1.401 0.02 1 38 . 1 MYR C2 C 37.355 0.05 1 39 . 1 MYR H21 H 2.146 0.02 1 40 . 1 MYR H22 H 2.146 0.02 1 41 . 2 GLY N N 113.306 0.05 1 42 . 2 GLY H H 8.258 0.02 1 43 . 2 GLY CA C 45.613 0.05 1 44 . 2 GLY HA3 H 3.695 0.02 2 45 . 2 GLY HA2 H 3.835 0.02 2 46 . 2 GLY C C 174.964 0.05 1 47 . 3 ALA N N 124.766 0.05 1 48 . 3 ALA H H 8.437 0.02 1 49 . 3 ALA CA C 53.268 0.05 1 50 . 3 ALA HA H 4.162 0.02 1 51 . 3 ALA CB C 18.506 0.05 1 52 . 3 ALA HB H 1.297 0.02 1 53 . 3 ALA C C 178.247 0.05 1 54 . 4 ARG N N 117.772 0.05 1 55 . 4 ARG H H 8.089 0.02 1 56 . 4 ARG CA C 56.262 0.05 1 57 . 4 ARG HA H 4.142 0.02 1 58 . 4 ARG CB C 29.930 0.05 1 59 . 4 ARG HB2 H 1.753 0.02 1 60 . 4 ARG CG C 26.997 0.05 1 61 . 4 ARG HG2 H 1.549 0.02 1 62 . 4 ARG C C 176.092 0.05 1 63 . 5 ALA N N 121.728 0.05 1 64 . 5 ALA H H 7.936 0.02 1 65 . 5 ALA CA C 53.160 0.05 1 66 . 5 ALA HA H 4.052 0.02 1 67 . 5 ALA CB C 18.593 0.05 1 68 . 5 ALA HB H 1.281 0.02 1 69 . 5 ALA C C 177.426 0.05 1 70 . 6 SER N N 112.168 0.05 1 71 . 6 SER H H 7.927 0.02 1 72 . 6 SER CA C 59.100 0.05 1 73 . 6 SER HA H 4.256 0.02 1 74 . 6 SER CB C 63.350 0.05 1 75 . 6 SER HB2 H 3.795 0.02 1 76 . 6 SER C C 174.758 0.05 1 77 . 7 VAL N N 118.711 0.05 1 78 . 7 VAL H H 7.629 0.02 1 79 . 7 VAL CA C 63.753 0.05 1 80 . 7 VAL HA H 3.870 0.02 1 81 . 7 VAL CB C 31.790 0.05 1 82 . 7 VAL HB H 2.069 0.02 1 83 . 7 VAL CG2 C 20.738 0.05 1 84 . 7 VAL HG1 H 0.833 0.02 1 85 . 7 VAL C C 174.964 0.05 1 86 . 8 LEU N N 118.746 0.05 1 87 . 8 LEU H H 7.384 0.02 1 88 . 8 LEU CA C 54.392 0.05 1 89 . 8 LEU HA H 4.459 0.02 1 90 . 8 LEU CB C 42.937 0.05 1 91 . 8 LEU HB3 H 1.390 0.02 2 92 . 8 LEU HB2 H 1.527 0.02 2 93 . 8 LEU CG C 26.600 0.05 1 94 . 8 LEU HG H 1.442 0.02 1 95 . 8 LEU CD1 C 23.056 0.05 1 96 . 8 LEU HD1 H 0.564 0.02 2 97 . 8 LEU C C 176.400 0.05 1 98 . 9 SER N N 116.209 0.05 1 99 . 9 SER H H 8.536 0.02 1 100 . 9 SER CA C 57.625 0.05 1 101 . 9 SER HA H 4.474 0.02 1 102 . 9 SER CB C 64.368 0.05 1 103 . 9 SER HB2 H 3.934 0.02 1 104 . 9 SER HB3 H 3.954 0.02 2 105 . 9 SER C C 174.964 0.05 1 106 . 10 GLY N N 110.272 0.05 1 107 . 10 GLY H H 8.747 0.02 1 108 . 10 GLY CA C 46.614 0.05 1 109 . 10 GLY C C 175.716 0.05 1 110 . 10 GLY HA2 H 3.854 0.02 1 111 . 11 GLY N N 109.552 0.05 1 112 . 11 GLY H H 8.562 0.02 1 113 . 11 GLY CA C 46.269 0.05 1 114 . 11 GLY HA3 H 3.983 0.02 2 115 . 11 GLY HA2 H 3.847 0.02 2 116 . 11 GLY C C 176.024 0.05 1 117 . 12 GLU N N 120.748 0.05 1 118 . 12 GLU H H 8.079 0.02 1 119 . 12 GLU CA C 60.050 0.05 1 120 . 12 GLU HA H 3.951 0.02 1 121 . 12 GLU CB C 33.320 0.05 1 122 . 12 GLU HB2 H 2.190 0.02 1 123 . 12 GLU C C 178.110 0.05 1 124 . 13 LEU N N 120.790 0.05 1 125 . 13 LEU H H 8.130 0.02 1 126 . 13 LEU CA C 57.511 0.05 1 127 . 13 LEU HA H 4.013 0.02 1 128 . 13 LEU CG C 27.005 0.05 1 129 . 13 LEU HG H 1.654 0.02 1 130 . 13 LEU CD1 C 23.995 0.05 1 131 . 13 LEU HD1 H 0.907 0.02 2 132 . 13 LEU CD2 C 25.332 0.05 1 133 . 13 LEU HD2 H 0.898 0.02 2 134 . 13 LEU C C 177.529 0.05 1 135 . 14 ASP N N 116.882 0.05 1 136 . 14 ASP H H 7.699 0.02 1 137 . 14 ASP CA C 56.870 0.05 1 138 . 14 ASP HA H 4.315 0.02 1 139 . 14 ASP CB C 40.611 0.05 1 140 . 14 ASP HB2 H 2.632 0.02 1 141 . 14 ASP C C 178.349 0.05 1 142 . 15 LYS N N 116.216 0.05 1 143 . 15 LYS H H 7.242 0.02 1 144 . 15 LYS CA C 58.189 0.05 1 145 . 15 LYS HA H 3.948 0.02 1 146 . 15 LYS CB C 32.189 0.05 1 147 . 15 LYS HB3 H 1.785 0.02 2 148 . 15 LYS HB2 H 1.972 0.02 2 149 . 15 LYS CG C 24.814 0.05 1 150 . 15 LYS HG2 H 1.504 0.02 1 151 . 15 LYS CD C 28.843 0.05 1 152 . 15 LYS HD2 H 1.611 0.02 1 153 . 15 LYS HE2 H 2.634 0.02 1 154 . 15 LYS C C 178.965 0.05 1 155 . 16 TRP N N 121.542 0.05 1 156 . 16 TRP H H 8.368 0.02 1 157 . 16 TRP CA C 59.978 0.05 1 158 . 16 TRP HA H 4.028 0.02 1 159 . 16 TRP CB C 30.676 0.05 1 160 . 16 TRP HB3 H 3.478 0.02 2 161 . 16 TRP HB2 H 3.101 0.02 2 162 . 16 TRP CD1 C 123.657 0.05 3 163 . 16 TRP HD1 H 6.503 0.02 1 164 . 16 TRP NE1 N 126.696 0.05 1 165 . 16 TRP HE1 H 9.307 0.02 2 166 . 16 TRP CZ2 C 113.662 0.05 3 167 . 16 TRP HZ2 H 7.009 0.02 3 168 . 16 TRP CH2 C 123.753 0.05 1 169 . 16 TRP HH2 H 6.933 0.02 1 170 . 16 TRP CZ3 C 121.960 0.05 3 171 . 16 TRP HZ3 H 6.335 0.02 3 172 . 16 TRP CE3 C 118.834 0.05 3 173 . 16 TRP HE3 H 7.044 0.02 3 174 . 16 TRP C C 175.271 0.05 1 175 . 17 GLU N N 108.138 0.05 1 176 . 17 GLU H H 7.548 0.02 1 177 . 17 GLU CA C 56.282 0.05 1 178 . 17 GLU HA H 4.652 0.02 1 179 . 17 GLU CB C 29.600 0.05 1 180 . 17 GLU HB2 H 2.257 0.02 1 181 . 17 GLU CG C 33.636 0.05 1 182 . 17 GLU HG2 H 1.746 0.02 1 183 . 17 GLU C C 177.016 0.05 1 184 . 18 LYS N N 115.795 0.05 1 185 . 18 LYS H H 7.374 0.02 1 186 . 18 LYS CA C 55.429 0.05 1 187 . 18 LYS HA H 4.382 0.02 1 188 . 18 LYS CB C 33.558 0.05 1 189 . 18 LYS HB3 H 1.745 0.02 2 190 . 18 LYS HB2 H 1.961 0.02 2 191 . 18 LYS CD C 28.702 0.05 1 192 . 18 LYS HD2 H 1.595 0.02 1 193 . 18 LYS C C 177.118 0.05 1 194 . 19 ILE N N 124.234 0.05 1 195 . 19 ILE H H 7.592 0.02 1 196 . 19 ILE CA C 62.985 0.05 1 197 . 19 ILE HA H 3.474 0.02 1 198 . 19 ILE CD1 C 14.366 0.05 1 199 . 19 ILE HD1 H 0.408 0.02 1 200 . 19 ILE CG2 C 16.267 0.05 2 201 . 19 ILE HG2 H 0.498 0.02 1 202 . 19 ILE C C 175.271 0.05 1 203 . 20 ARG N N 126.065 0.05 1 204 . 20 ARG H H 8.022 0.02 1 205 . 20 ARG CA C 56.116 0.05 1 206 . 20 ARG HA H 4.325 0.02 1 207 . 20 ARG CG C 28.154 0.05 1 208 . 20 ARG HG3 H 1.593 0.02 2 209 . 20 ARG HG2 H 1.794 0.02 2 210 . 20 ARG C C 176.126 0.05 1 211 . 21 LEU N N 120.670 0.05 1 212 . 21 LEU H H 7.780 0.02 1 213 . 21 LEU CA C 57.968 0.05 1 214 . 21 LEU HA H 3.332 0.02 1 215 . 21 LEU CB C 41.227 0.05 1 216 . 21 LEU HB3 H 1.153 0.02 2 217 . 21 LEU HB2 H 1.346 0.02 2 218 . 21 LEU CG C 27.766 0.05 1 219 . 21 LEU HG H 0.653 0.02 1 220 . 21 LEU CD1 C 24.737 0.05 2 221 . 21 LEU HD1 H 0.190 0.02 2 222 . 21 LEU CD2 C 21.358 0.05 2 223 . 21 LEU HD2 H -0.446 0.02 2 224 . 21 LEU C C 179.512 0.05 1 225 . 22 ARG N N 119.632 0.05 1 226 . 22 ARG H H 8.948 0.02 1 227 . 22 ARG CA C 52.471 0.05 1 228 . 22 ARG HA H 4.791 0.02 1 229 . 22 ARG CB C 31.371 0.05 1 230 . 22 ARG HB3 H 1.563 0.02 2 231 . 22 ARG HB2 H 1.675 0.02 2 232 . 22 ARG CG C 26.222 0.05 1 233 . 22 ARG HG3 H 1.362 0.02 2 234 . 22 ARG HG2 H 1.491 0.02 2 235 . 22 ARG CD C 43.082 0.05 1 236 . 22 ARG HD2 H 3.052 0.02 1 237 . 23 PRO CA C 63.162 0.05 1 238 . 23 PRO HA H 4.290 0.02 1 239 . 23 PRO CD C 50.050 0.05 1 240 . 23 PRO HD3 H 3.443 0.02 2 241 . 23 PRO HD2 H 3.706 0.02 2 242 . 23 PRO C C 178.281 0.05 1 243 . 24 GLY N N 112.890 0.05 1 244 . 24 GLY H H 9.104 0.02 1 245 . 24 GLY CA C 45.569 0.05 1 246 . 24 GLY HA3 H 3.684 0.02 2 247 . 24 GLY HA2 H 3.977 0.02 2 248 . 24 GLY C C 174.314 0.05 1 249 . 25 GLY N N 108.082 0.05 1 250 . 25 GLY H H 8.106 0.02 1 251 . 25 GLY CA C 44.319 0.05 1 252 . 25 GLY C C 173.493 0.05 1 253 . 25 GLY HA2 H 4.099 0.02 1 254 . 26 LYS N N 117.797 0.05 1 255 . 26 LYS H H 8.494 0.02 1 256 . 26 LYS CA C 56.780 0.05 1 257 . 26 LYS HA H 4.301 0.02 1 258 . 26 LYS HB2 H 1.733 0.02 1 259 . 26 LYS HG2 H 1.413 0.02 1 260 . 26 LYS C C 177.529 0.05 1 261 . 27 LYS N N 117.939 0.05 1 262 . 27 LYS H H 7.696 0.02 1 263 . 27 LYS CA C 56.926 0.05 1 264 . 27 LYS HA H 4.301 0.02 1 265 . 27 LYS HB2 H 1.632 0.02 1 266 . 27 LYS HG2 H 1.416 0.02 1 267 . 27 LYS HD2 H 1.817 0.02 1 268 . 27 LYS C C 177.050 0.05 1 269 . 28 GLN N N 123.137 0.05 1 270 . 28 GLN H H 8.415 0.02 1 271 . 28 GLN CA C 54.410 0.05 1 272 . 28 GLN HA H 4.771 0.02 1 273 . 28 GLN CB C 28.704 0.05 1 274 . 28 GLN HB2 H 1.619 0.02 1 275 . 28 GLN CG C 34.931 0.05 1 276 . 28 GLN HG2 H 1.775 0.02 1 277 . 28 GLN C C 174.827 0.05 1 278 . 29 TYR N N 119.854 0.05 1 279 . 29 TYR H H 7.868 0.02 1 280 . 29 TYR CA C 61.010 0.05 1 281 . 29 TYR HA H 3.681 0.02 1 282 . 29 TYR CE1 C 116.356 0.05 3 283 . 29 TYR HE1 H 6.407 0.02 3 284 . 29 TYR CE2 C 116.323 0.05 3 285 . 29 TYR HE2 H 6.399 0.02 3 286 . 29 TYR CD2 C 132.555 0.05 3 287 . 29 TYR HD2 H 6.267 0.02 3 288 . 29 TYR C C 174.964 0.05 1 289 . 30 LYS N N 118.202 0.05 1 290 . 30 LYS H H 10.556 0.02 1 291 . 30 LYS CA C 53.767 0.05 1 292 . 30 LYS HA H 5.186 0.02 1 293 . 30 LYS HB3 H 1.742 0.02 2 294 . 30 LYS HB2 H 2.323 0.02 2 295 . 30 LYS C C 180.538 0.05 1 296 . 31 LEU N N 128.835 0.05 1 297 . 31 LEU H H 9.946 0.02 1 298 . 31 LEU CA C 58.833 0.05 1 299 . 31 LEU HA H 4.117 0.02 1 300 . 31 LEU CB C 40.817 0.05 1 301 . 31 LEU HB2 H 1.733 0.02 1 302 . 31 LEU CG C 26.725 0.05 1 303 . 31 LEU HG H 1.648 0.02 1 304 . 31 LEU CD1 C 23.572 0.05 1 305 . 31 LEU HD1 H 0.902 0.02 2 306 . 31 LEU CD2 C 25.253 0.05 1 307 . 31 LEU HD2 H 0.882 0.02 2 308 . 31 LEU C C 179.512 0.05 1 309 . 32 LYS N N 115.539 0.05 1 310 . 32 LYS H H 8.459 0.02 1 311 . 32 LYS CA C 59.011 0.05 1 312 . 32 LYS HA H 4.077 0.02 1 313 . 32 LYS C C 177.871 0.05 1 314 . 33 HIS N N 119.360 0.05 1 315 . 33 HIS H H 8.198 0.02 1 316 . 33 HIS CA C 62.825 0.05 1 317 . 33 HIS HA H 4.649 0.02 1 318 . 33 HIS C C 178.520 0.05 1 319 . 34 ILE N N 119.550 0.05 1 320 . 34 ILE H H 7.881 0.02 1 321 . 34 ILE CA C 64.274 0.05 1 322 . 34 ILE HA H 3.631 0.02 1 323 . 34 ILE CB C 37.165 0.05 1 324 . 34 ILE HB H 1.983 0.02 1 325 . 34 ILE CG1 C 29.121 0.05 2 326 . 34 ILE HG13 H 0.399 0.02 1 327 . 34 ILE HG12 H 1.334 0.02 1 328 . 34 ILE CD1 C 11.646 0.05 1 329 . 34 ILE HD1 H -0.297 0.02 1 330 . 34 ILE CG2 C 17.502 0.05 2 331 . 34 ILE HG2 H 0.649 0.02 1 332 . 34 ILE C C 177.529 0.05 1 333 . 35 VAL N N 121.364 0.05 1 334 . 35 VAL H H 7.711 0.02 1 335 . 35 VAL CA C 66.821 0.05 1 336 . 35 VAL HA H 3.413 0.02 1 337 . 35 VAL CB C 31.574 0.05 1 338 . 35 VAL HB H 2.082 0.02 1 339 . 35 VAL CG2 C 21.908 0.05 1 340 . 35 VAL HG2 H 0.926 0.02 2 341 . 35 VAL CG1 C 20.589 0.05 1 342 . 35 VAL HG1 H 0.908 0.02 2 343 . 35 VAL C C 178.623 0.05 1 344 . 36 TRP N N 120.567 0.05 1 345 . 36 TRP H H 8.543 0.02 1 346 . 36 TRP CA C 61.830 0.05 1 347 . 36 TRP HA H 4.177 0.02 1 348 . 36 TRP CB C 28.134 0.05 1 349 . 36 TRP HB2 H 3.446 0.02 1 350 . 36 TRP CD1 C 127.482 0.05 2 351 . 36 TRP HD1 H 7.282 0.02 1 352 . 36 TRP NE1 N 131.427 0.05 1 353 . 36 TRP HE1 H 10.259 0.02 2 354 . 36 TRP CZ2 C 114.571 0.05 2 355 . 36 TRP HZ2 H 7.397 0.02 2 356 . 36 TRP C C 177.084 0.05 1 357 . 37 ALA N N 120.526 0.05 1 358 . 37 ALA H H 8.289 0.02 1 359 . 37 ALA CA C 54.908 0.05 1 360 . 37 ALA HA H 3.289 0.02 1 361 . 37 ALA CB C 16.857 0.05 1 362 . 37 ALA HB H 1.459 0.02 1 363 . 37 ALA C C 178.452 0.05 1 364 . 38 SER N N 111.702 0.05 1 365 . 38 SER H H 8.210 0.02 1 366 . 38 SER CA C 62.613 0.05 1 367 . 38 SER HA H 3.826 0.02 1 368 . 38 SER C C 175.306 0.05 1 369 . 39 ARG N N 120.720 0.05 1 370 . 39 ARG H H 7.553 0.02 1 371 . 39 ARG CA C 58.215 0.05 1 372 . 39 ARG HA H 4.051 0.02 1 373 . 39 ARG CB C 29.857 0.05 1 374 . 39 ARG HB2 H 1.839 0.02 1 375 . 39 ARG CG C 26.815 0.05 1 376 . 39 ARG HG2 H 1.649 0.02 1 377 . 39 ARG CD C 43.150 0.05 1 378 . 39 ARG HD2 H 3.088 0.02 1 379 . 39 ARG C C 179.546 0.05 1 380 . 40 GLU N N 120.858 0.05 1 381 . 40 GLU H H 8.220 0.02 1 382 . 40 GLU CA C 58.002 0.05 1 383 . 40 GLU HA H 3.750 0.02 1 384 . 40 GLU CB C 29.324 0.05 1 385 . 40 GLU HB3 H 1.367 0.02 2 386 . 40 GLU HB2 H 1.596 0.02 2 387 . 40 GLU C C 178.418 0.05 1 388 . 41 LEU N N 117.109 0.05 1 389 . 41 LEU H H 7.987 0.02 1 390 . 41 LEU CA C 58.136 0.05 1 391 . 41 LEU HA H 3.812 0.02 1 392 . 41 LEU CB C 39.981 0.05 1 393 . 41 LEU HB3 H 1.305 0.02 2 394 . 41 LEU HB2 H 1.735 0.02 2 395 . 41 LEU CG C 26.177 0.05 1 396 . 41 LEU HG H 1.970 0.02 1 397 . 41 LEU CD1 C 26.149 0.05 2 398 . 41 LEU HD1 H 0.753 0.02 2 399 . 41 LEU CD2 C 22.529 0.05 2 400 . 41 LEU HD2 H 0.699 0.02 2 401 . 41 LEU C C 178.965 0.05 1 402 . 42 GLU N N 117.580 0.05 1 403 . 42 GLU H H 7.539 0.02 1 404 . 42 GLU CA C 59.399 0.05 1 405 . 42 GLU HA H 4.066 0.02 1 406 . 42 GLU CB C 28.703 0.05 1 407 . 42 GLU HB2 H 2.063 0.02 1 408 . 42 GLU HB3 H 1.633 0.02 2 409 . 42 GLU CG C 36.617 0.05 1 410 . 42 GLU HG3 H 2.105 0.02 2 411 . 42 GLU HG2 H 2.484 0.02 2 412 . 42 GLU C C 180.265 0.05 1 413 . 43 ARG N N 119.832 0.05 1 414 . 43 ARG H H 7.637 0.02 1 415 . 43 ARG CA C 58.281 0.05 1 416 . 43 ARG HA H 3.967 0.02 1 417 . 43 ARG CB C 29.326 0.05 1 418 . 43 ARG HB2 H 1.623 0.02 1 419 . 43 ARG CG C 27.134 0.05 1 420 . 43 ARG HG2 H 1.399 0.02 1 421 . 43 ARG CD C 43.145 0.05 1 422 . 43 ARG HD2 H 2.980 0.02 1 423 . 43 ARG C C 177.016 0.05 1 424 . 44 PHE N N 117.779 0.05 1 425 . 44 PHE H H 7.520 0.02 1 426 . 44 PHE CA C 57.013 0.05 1 427 . 44 PHE HA H 4.522 0.02 1 428 . 44 PHE CB C 38.754 0.05 1 429 . 44 PHE HB3 H 2.704 0.02 2 430 . 44 PHE HB2 H 3.380 0.02 2 431 . 44 PHE C C 173.698 0.05 1 432 . 45 ALA N N 119.032 0.05 1 433 . 45 ALA H H 7.917 0.02 1 434 . 45 ALA CA C 53.048 0.05 1 435 . 45 ALA HA H 3.954 0.02 1 436 . 45 ALA CB C 16.037 0.05 1 437 . 45 ALA HB H 1.407 0.02 1 438 . 45 ALA C C 175.716 0.05 1 439 . 46 VAL N N 119.568 0.05 1 440 . 46 VAL H H 7.768 0.02 1 441 . 46 VAL CA C 60.633 0.05 1 442 . 46 VAL HA H 4.029 0.02 1 443 . 46 VAL CB C 33.147 0.05 1 444 . 46 VAL HB H 1.706 0.02 1 445 . 46 VAL CG2 C 21.171 0.05 2 446 . 46 VAL HG2 H 0.790 0.02 2 447 . 46 VAL CG1 C 22.465 0.05 2 448 . 46 VAL HG1 H 0.761 0.02 2 449 . 46 VAL C C 174.724 0.05 1 450 . 47 ASN N N 125.792 0.05 1 451 . 47 ASN H H 8.352 0.02 1 452 . 47 ASN CA C 50.675 0.05 1 453 . 47 ASN HA H 4.607 0.02 1 454 . 47 ASN CB C 38.954 0.05 1 455 . 47 ASN HB2 H 2.812 0.02 1 456 . 48 PRO CA C 64.149 0.05 1 457 . 48 PRO HA H 4.147 0.02 1 458 . 48 PRO CB C 31.660 0.05 1 459 . 48 PRO HB3 H 1.861 0.02 2 460 . 48 PRO HB2 H 2.308 0.02 2 461 . 48 PRO CG C 27.428 0.05 1 462 . 48 PRO HG3 H 1.687 0.02 2 463 . 48 PRO HG2 H 1.943 0.02 2 464 . 48 PRO CD C 50.602 0.05 1 465 . 48 PRO HD3 H 4.170 0.02 2 466 . 48 PRO HD2 H 3.827 0.02 2 467 . 48 PRO C C 177.905 0.05 1 468 . 49 GLY N N 106.837 0.05 1 469 . 49 GLY H H 8.513 0.02 1 470 . 49 GLY CA C 46.289 0.05 1 471 . 49 GLY HA3 H 3.797 0.02 2 472 . 49 GLY HA2 H 3.688 0.02 2 473 . 49 GLY C C 176.503 0.05 1 474 . 50 LEU N N 122.144 0.05 1 475 . 50 LEU H H 7.772 0.02 1 476 . 50 LEU CA C 56.946 0.05 1 477 . 50 LEU HA H 4.091 0.02 1 478 . 50 LEU CB C 40.622 0.05 1 479 . 50 LEU HB2 H 1.750 0.02 1 480 . 50 LEU CG C 27.434 0.05 1 481 . 50 LEU HG H 1.594 0.02 1 482 . 50 LEU CD1 C 25.293 0.05 1 483 . 50 LEU HD1 H 0.915 0.02 2 484 . 50 LEU CD2 C 22.480 0.05 2 485 . 50 LEU HD2 H 0.805 0.02 2 486 . 50 LEU C C 176.981 0.05 1 487 . 51 LEU N N 112.434 0.05 1 488 . 51 LEU H H 7.484 0.02 1 489 . 51 LEU CA C 55.726 0.05 1 490 . 51 LEU HA H 4.105 0.02 1 491 . 51 LEU CG C 26.798 0.05 1 492 . 51 LEU HG H 1.561 0.02 1 493 . 51 LEU CD1 C 23.747 0.05 2 494 . 51 LEU HD1 H 0.699 0.02 2 495 . 51 LEU CD2 C 25.279 0.05 2 496 . 51 LEU HD2 H 0.681 0.02 2 497 . 51 LEU C C 177.871 0.05 1 498 . 52 GLU N N 114.581 0.05 1 499 . 52 GLU H H 7.467 0.02 1 500 . 52 GLU CA C 58.138 0.05 1 501 . 52 GLU HA H 3.846 0.02 1 502 . 52 GLU CB C 30.886 0.05 1 503 . 52 GLU HB2 H 2.056 0.02 1 504 . 52 GLU CG C 37.341 0.05 1 505 . 52 GLU HG3 H 2.119 0.02 2 506 . 52 GLU HG2 H 2.295 0.02 2 507 . 52 GLU C C 175.203 0.05 1 508 . 53 THR N N 103.302 0.05 1 509 . 53 THR H H 7.217 0.02 1 510 . 53 THR CA C 58.027 0.05 1 511 . 53 THR HA H 4.262 0.02 1 512 . 53 THR CB C 62.879 0.05 1 513 . 53 THR HB H 4.439 0.02 1 514 . 53 THR CG2 C 21.158 0.05 1 515 . 53 THR HG2 H 1.026 0.02 1 516 . 53 THR C C 174.758 0.05 1 517 . 54 SER N N 119.338 0.05 1 518 . 54 SER H H 9.250 0.02 1 519 . 54 SER CA C 62.409 0.05 1 520 . 54 SER HA H 3.931 0.02 1 521 . 54 SER CB C 62.582 0.05 1 522 . 54 SER HB2 H 3.708 0.02 1 523 . 54 SER C C 175.853 0.05 1 524 . 55 GLU N N 121.639 0.05 1 525 . 55 GLU H H 8.876 0.02 1 526 . 55 GLU CA C 59.334 0.05 1 527 . 55 GLU HA H 4.003 0.02 1 528 . 55 GLU CB C 28.646 0.05 1 529 . 55 GLU HB2 H 1.903 0.02 1 530 . 55 GLU CG C 35.952 0.05 1 531 . 55 GLU HG2 H 2.264 0.02 1 532 . 55 GLU C C 179.170 0.05 1 533 . 56 GLY N N 110.896 0.05 1 534 . 56 GLY H H 8.490 0.02 1 535 . 56 GLY CA C 47.514 0.05 1 536 . 56 GLY HA3 H 3.671 0.02 2 537 . 56 GLY HA2 H 4.518 0.02 2 538 . 56 GLY C C 176.981 0.05 1 539 . 57 CYS N N 118.682 0.05 1 540 . 57 CYS H H 8.127 0.02 1 541 . 57 CYS CA C 64.727 0.05 1 542 . 57 CYS HA H 3.946 0.02 1 543 . 57 CYS CB C 27.423 0.05 1 544 . 57 CYS HB3 H 3.475 0.02 2 545 . 57 CYS HB2 H 2.475 0.02 2 546 . 57 CYS C C 176.229 0.05 1 547 . 58 ARG N N 119.868 0.05 1 548 . 58 ARG H H 8.482 0.02 1 549 . 58 ARG CA C 59.430 0.05 1 550 . 58 ARG HA H 3.460 0.02 1 551 . 58 ARG CB C 29.834 0.05 1 552 . 58 ARG HB2 H 1.874 0.02 1 553 . 58 ARG CG C 27.363 0.05 1 554 . 58 ARG HG2 H 1.415 0.02 1 555 . 58 ARG CD C 42.924 0.05 1 556 . 58 ARG HD2 H 3.083 0.02 1 557 . 58 ARG C C 178.999 0.05 1 558 . 59 GLN N N 120.142 0.05 1 559 . 59 GLN H H 8.004 0.02 1 560 . 59 GLN CA C 58.863 0.05 1 561 . 59 GLN HA H 3.978 0.02 1 562 . 59 GLN CB C 28.487 0.05 1 563 . 59 GLN HB2 H 2.172 0.02 1 564 . 59 GLN CG C 34.339 0.05 1 565 . 59 GLN HG2 H 2.261 0.02 1 566 . 59 GLN HG3 H 2.277 0.02 2 567 . 59 GLN C C 179.239 0.05 1 568 . 60 ILE N N 120.530 0.05 1 569 . 60 ILE H H 8.137 0.02 1 570 . 60 ILE CA C 65.618 0.05 1 571 . 60 ILE HA H 3.488 0.02 1 572 . 60 ILE CD1 C 14.241 0.05 1 573 . 60 ILE HD1 H 0.682 0.02 1 574 . 60 ILE CG2 C 19.264 0.05 2 575 . 60 ILE HG2 H 0.775 0.02 1 576 . 60 ILE C C 177.905 0.05 1 577 . 61 LEU N N 119.029 0.05 1 578 . 61 LEU H H 8.347 0.02 1 579 . 61 LEU CA C 58.244 0.05 1 580 . 61 LEU HA H 3.774 0.02 1 581 . 61 LEU CG C 25.892 0.05 1 582 . 61 LEU HG H 1.607 0.02 1 583 . 61 LEU CD1 C 25.040 0.05 2 584 . 61 LEU HD1 H 0.306 0.02 2 585 . 61 LEU CD2 C 21.640 0.05 2 586 . 61 LEU HD2 H -0.051 0.02 2 587 . 61 LEU C C 179.478 0.05 1 588 . 62 GLY N N 103.696 0.05 1 589 . 62 GLY H H 7.876 0.02 1 590 . 62 GLY CA C 46.711 0.05 1 591 . 62 GLY C C 175.921 0.05 1 592 . 62 GLY HA2 H 3.841 0.02 1 593 . 63 GLN N N 119.879 0.05 1 594 . 63 GLN H H 7.784 0.02 1 595 . 63 GLN CA C 57.805 0.05 1 596 . 63 GLN HA H 4.135 0.02 1 597 . 63 GLN CB C 28.694 0.05 1 598 . 63 GLN HB2 H 2.094 0.02 1 599 . 63 GLN CG C 33.889 0.05 1 600 . 63 GLN HG2 H 2.389 0.02 1 601 . 63 GLN C C 178.076 0.05 1 602 . 64 LEU N N 117.106 0.05 1 603 . 64 LEU H H 8.213 0.02 1 604 . 64 LEU CA C 55.725 0.05 1 605 . 64 LEU HA H 4.168 0.02 1 606 . 64 LEU CB C 43.752 0.05 1 607 . 64 LEU HB3 H 1.390 0.02 2 608 . 64 LEU HB2 H 1.980 0.02 2 609 . 64 LEU CG C 26.264 0.05 1 610 . 64 LEU HG H 1.850 0.02 1 611 . 64 LEU CD1 C 25.548 0.05 2 612 . 64 LEU HD1 H 0.661 0.02 2 613 . 64 LEU CD2 C 21.176 0.05 2 614 . 64 LEU HD2 H 0.481 0.02 2 615 . 64 LEU C C 177.836 0.05 1 616 . 65 GLN N N 119.047 0.05 1 617 . 65 GLN H H 8.082 0.02 1 618 . 65 GLN CA C 61.246 0.05 1 619 . 65 GLN HA H 3.707 0.02 1 620 . 65 GLN CB C 25.587 0.05 1 621 . 65 GLN HB3 H 2.223 0.02 2 622 . 65 GLN HB2 H 2.477 0.02 2 623 . 65 GLN CG C 33.677 0.05 1 624 . 65 GLN HG3 H 2.266 0.02 2 625 . 65 GLN HG2 H 2.419 0.02 2 626 . 66 PRO CA C 65.388 0.05 1 627 . 66 PRO HA H 4.282 0.02 1 628 . 66 PRO CB C 30.799 0.05 1 629 . 66 PRO HB3 H 1.799 0.02 2 630 . 66 PRO HB2 H 2.326 0.02 2 631 . 66 PRO CG C 27.992 0.05 1 632 . 66 PRO HG2 H 2.000 0.02 1 633 . 66 PRO CD C 50.553 0.05 1 634 . 66 PRO HD3 H 3.448 0.02 2 635 . 66 PRO HD2 H 3.717 0.02 2 636 . 66 PRO C C 177.973 0.05 1 637 . 67 SER N N 111.672 0.05 1 638 . 67 SER H H 7.810 0.02 1 639 . 67 SER CA C 59.478 0.05 1 640 . 67 SER HA H 4.388 0.02 1 641 . 67 SER CB C 63.804 0.05 1 642 . 67 SER HB2 H 3.888 0.02 1 643 . 67 SER C C 174.964 0.05 1 644 . 68 LEU N N 121.278 0.05 1 645 . 68 LEU H H 7.650 0.02 1 646 . 68 LEU CA C 57.579 0.05 1 647 . 68 LEU HA H 3.764 0.02 1 648 . 68 LEU CB C 41.341 0.05 1 649 . 68 LEU HB3 H 1.257 0.02 2 650 . 68 LEU HB2 H 1.524 0.02 2 651 . 68 LEU CG C 25.701 0.05 1 652 . 68 LEU HG H 1.383 0.02 1 653 . 68 LEU CD1 C 23.715 0.05 2 654 . 68 LEU HD1 H 0.080 0.02 2 655 . 68 LEU CD2 C 21.717 0.05 2 656 . 68 LEU HD2 H 0.266 0.02 2 657 . 68 LEU C C 179.170 0.05 1 658 . 69 GLN N N 116.538 0.05 1 659 . 69 GLN H H 8.014 0.02 1 660 . 69 GLN CA C 58.139 0.05 1 661 . 69 GLN HA H 4.016 0.02 1 662 . 69 GLN CB C 28.096 0.05 1 663 . 69 GLN HB2 H 2.073 0.02 1 664 . 69 GLN CG C 33.379 0.05 1 665 . 69 GLN HG2 H 2.330 0.02 1 666 . 69 GLN C C 176.947 0.05 1 667 . 70 THR N N 107.155 0.05 1 668 . 70 THR H H 7.503 0.02 1 669 . 70 THR CA C 61.207 0.05 1 670 . 70 THR HA H 4.410 0.02 1 671 . 70 THR CG2 C 21.192 0.05 1 672 . 70 THR HG2 H 1.144 0.02 1 673 . 70 THR C C 175.237 0.05 1 674 . 71 GLY N N 109.819 0.05 1 675 . 71 GLY H H 7.694 0.02 1 676 . 71 GLY CA C 44.992 0.05 1 677 . 71 GLY HA3 H 3.801 0.02 2 678 . 71 GLY HA2 H 4.171 0.02 2 679 . 71 GLY C C 173.322 0.05 1 680 . 72 SER N N 114.652 0.05 1 681 . 72 SER H H 7.961 0.02 1 682 . 72 SER CA C 56.998 0.05 1 683 . 72 SER HA H 4.541 0.02 1 684 . 72 SER CB C 64.699 0.05 1 685 . 72 SER HB3 H 3.967 0.02 2 686 . 72 SER HB2 H 4.339 0.02 2 687 . 72 SER C C 175.511 0.05 1 688 . 73 GLU N N 124.640 0.05 1 689 . 73 GLU H H 9.065 0.02 1 690 . 73 GLU CA C 58.988 0.05 1 691 . 73 GLU HA H 4.059 0.02 1 692 . 73 GLU CB C 29.182 0.05 1 693 . 73 GLU HB2 H 2.027 0.02 1 694 . 73 GLU CG C 35.893 0.05 1 695 . 73 GLU HG2 H 2.311 0.02 1 696 . 73 GLU C C 178.794 0.05 1 697 . 74 GLU N N 120.483 0.05 1 698 . 74 GLU H H 8.590 0.02 1 699 . 74 GLU CA C 60.049 0.05 1 700 . 74 GLU HA H 4.201 0.02 1 701 . 74 GLU CB C 28.893 0.05 1 702 . 74 GLU HB2 H 2.070 0.02 1 703 . 74 GLU HB3 H 1.928 0.02 2 704 . 74 GLU CG C 36.830 0.05 1 705 . 74 GLU HG2 H 2.470 0.02 1 706 . 74 GLU C C 178.178 0.05 1 707 . 75 LEU N N 121.203 0.05 1 708 . 75 LEU H H 7.698 0.02 1 709 . 75 LEU CA C 57.514 0.05 1 710 . 75 LEU HA H 4.122 0.02 1 711 . 75 LEU CB C 40.921 0.05 1 712 . 75 LEU HB2 H 1.741 0.02 1 713 . 75 LEU CD2 C 24.739 0.05 1 714 . 75 LEU HD1 H 0.786 0.02 1 715 . 75 LEU C C 178.589 0.05 1 716 . 76 ARG N N 119.471 0.05 1 717 . 76 ARG H H 7.880 0.02 1 718 . 76 ARG CA C 59.456 0.05 1 719 . 76 ARG HA H 3.810 0.02 1 720 . 76 ARG CB C 29.025 0.05 1 721 . 76 ARG HB2 H 1.931 0.02 1 722 . 76 ARG CG C 27.272 0.05 1 723 . 76 ARG HG2 H 1.605 0.02 1 724 . 76 ARG C C 177.939 0.05 1 725 . 77 SER N N 114.414 0.05 1 726 . 77 SER H H 8.559 0.02 1 727 . 77 SER CA C 61.812 0.05 1 728 . 77 SER HA H 4.270 0.02 1 729 . 77 SER CB C 62.541 0.05 1 730 . 77 SER HB3 H 3.942 0.02 2 731 . 77 SER HB2 H 4.181 0.02 2 732 . 77 SER C C 177.255 0.05 1 733 . 78 LEU N N 126.153 0.05 1 734 . 78 LEU H H 8.455 0.02 1 735 . 78 LEU CA C 58.845 0.05 1 736 . 78 LEU HA H 4.347 0.02 1 737 . 78 LEU CD1 C 25.765 0.05 2 738 . 78 LEU HD1 H 0.716 0.02 2 739 . 78 LEU CD2 C 24.168 0.05 2 740 . 78 LEU HD2 H 0.769 0.02 2 741 . 78 LEU C C 176.708 0.05 1 742 . 79 TYR N N 120.358 0.05 1 743 . 79 TYR H H 8.694 0.02 1 744 . 79 TYR CA C 62.553 0.05 1 745 . 79 TYR HA H 3.547 0.02 1 746 . 79 TYR CB C 39.376 0.05 1 747 . 79 TYR HB3 H 2.668 0.02 2 748 . 79 TYR HB2 H 3.232 0.02 2 749 . 79 TYR CE2 C 118.202 0.05 3 750 . 79 TYR HE2 H 6.788 0.02 3 751 . 79 TYR CD2 C 133.266 0.05 3 752 . 79 TYR HD2 H 6.988 0.02 3 753 . 79 TYR C C 176.297 0.05 1 754 . 80 ASN N N 117.136 0.05 1 755 . 80 ASN H H 8.838 0.02 1 756 . 80 ASN CA C 55.585 0.05 1 757 . 80 ASN HA H 4.244 0.02 1 758 . 80 ASN CB C 37.486 0.05 1 759 . 80 ASN HB3 H 2.724 0.02 2 760 . 80 ASN HB2 H 3.146 0.02 2 761 . 80 ASN C C 176.708 0.05 1 762 . 81 THR N N 115.775 0.05 1 763 . 81 THR H H 8.092 0.02 1 764 . 81 THR CA C 67.545 0.05 1 765 . 81 THR HA H 3.858 0.02 1 766 . 81 THR CB C 68.887 0.05 1 767 . 81 THR HB H 4.656 0.02 1 768 . 81 THR CG2 C 20.618 0.05 1 769 . 81 THR HG2 H 1.480 0.02 1 770 . 81 THR C C 175.750 0.05 1 771 . 82 ILE N N 121.318 0.05 1 772 . 82 ILE H H 8.084 0.02 1 773 . 82 ILE CA C 63.787 0.05 1 774 . 82 ILE HA H 3.579 0.02 1 775 . 82 ILE CD1 C 13.528 0.05 1 776 . 82 ILE HD1 H 0.715 0.02 1 777 . 82 ILE CG2 C 17.701 0.05 2 778 . 82 ILE HG2 H 0.774 0.02 1 779 . 82 ILE C C 176.708 0.05 1 780 . 83 ALA N N 125.311 0.05 1 781 . 83 ALA H H 8.759 0.02 1 782 . 83 ALA CA C 55.547 0.05 1 783 . 83 ALA HA H 3.805 0.02 1 784 . 83 ALA CB C 17.438 0.05 1 785 . 83 ALA HB H 1.266 0.02 1 786 . 83 ALA C C 179.546 0.05 1 787 . 84 VAL N N 117.721 0.05 1 788 . 84 VAL H H 7.780 0.02 1 789 . 84 VAL CA C 66.885 0.05 1 790 . 84 VAL HA H 3.276 0.02 1 791 . 84 VAL CB C 30.543 0.05 1 792 . 84 VAL HB H 1.901 0.02 1 793 . 84 VAL CG2 C 23.098 0.05 2 794 . 84 VAL HG2 H 0.889 0.02 2 795 . 84 VAL CG1 C 24.423 0.05 2 796 . 84 VAL HG1 H 0.328 0.02 2 797 . 84 VAL C C 177.768 0.05 1 798 . 85 LEU N N 122.241 0.05 1 799 . 85 LEU H H 8.154 0.02 1 800 . 85 LEU CA C 58.025 0.05 1 801 . 85 LEU HA H 3.791 0.02 1 802 . 85 LEU CB C 41.788 0.05 1 803 . 85 LEU HB3 H 1.482 0.02 2 804 . 85 LEU HB2 H 1.802 0.02 2 805 . 85 LEU CG C 26.241 0.05 1 806 . 85 LEU HG H 1.352 0.02 1 807 . 85 LEU CD1 C 26.498 0.05 2 808 . 85 LEU HD1 H 0.488 0.02 2 809 . 85 LEU CD2 C 23.098 0.05 2 810 . 85 LEU HD2 H 0.154 0.02 2 811 . 85 LEU C C 177.460 0.05 1 812 . 86 TYR N N 119.196 0.05 1 813 . 86 TYR H H 9.057 0.02 1 814 . 86 TYR CA C 62.570 0.05 1 815 . 86 TYR HA H 3.847 0.02 1 816 . 86 TYR CB C 38.081 0.05 1 817 . 86 TYR HB3 H 2.781 0.02 2 818 . 86 TYR HB2 H 3.429 0.02 2 819 . 86 TYR CD1 C 133.192 0.05 3 820 . 86 TYR HD1 H 7.132 0.02 3 821 . 86 TYR CE1 C 117.732 0.05 3 822 . 86 TYR HE1 H 6.594 0.02 3 823 . 86 TYR C C 176.503 0.05 1 824 . 87 CYS N N 116.251 0.05 1 825 . 87 CYS H H 7.509 0.02 1 826 . 87 CYS CA C 65.080 0.05 1 827 . 87 CYS HA H 3.699 0.02 1 828 . 87 CYS CB C 26.150 0.05 1 829 . 87 CYS HB3 H 2.800 0.02 2 830 . 87 CYS HB2 H 3.307 0.02 2 831 . 87 CYS C C 176.366 0.05 1 832 . 88 VAL N N 120.959 0.05 1 833 . 88 VAL H H 8.364 0.02 1 834 . 88 VAL CA C 66.297 0.05 1 835 . 88 VAL HA H 3.791 0.02 1 836 . 88 VAL CB C 31.172 0.05 1 837 . 88 VAL HB H 2.079 0.02 1 838 . 88 VAL CG2 C 23.268 0.05 2 839 . 88 VAL HG2 H 1.056 0.02 2 840 . 88 VAL CG1 C 21.182 0.05 2 841 . 88 VAL HG1 H 0.845 0.02 2 842 . 88 VAL C C 180.880 0.05 1 843 . 89 HIS N N 119.566 0.05 1 844 . 89 HIS H H 8.774 0.02 1 845 . 89 HIS CA C 57.625 0.05 1 846 . 89 HIS HA H 4.664 0.02 1 847 . 89 HIS CB C 29.365 0.05 1 848 . 89 HIS HB3 H 3.097 0.02 2 849 . 89 HIS HB2 H 3.180 0.02 2 850 . 89 HIS CD2 C 118.685 0.05 1 851 . 89 HIS HD2 H 6.763 0.02 3 852 . 89 HIS C C 177.084 0.05 1 853 . 90 GLN N N 116.416 0.05 1 854 . 90 GLN H H 7.890 0.02 1 855 . 90 GLN CA C 55.007 0.05 1 856 . 90 GLN HA H 4.298 0.02 1 857 . 90 GLN CB C 30.624 0.05 1 858 . 90 GLN HB3 H 1.590 0.02 2 859 . 90 GLN HB2 H 1.935 0.02 2 860 . 90 GLN CG C 33.109 0.05 1 861 . 90 GLN HG2 H 1.752 0.02 1 862 . 90 GLN C C 174.553 0.05 1 863 . 91 ARG N N 115.683 0.05 1 864 . 91 ARG H H 7.898 0.02 1 865 . 91 ARG CA C 56.864 0.05 1 866 . 91 ARG HA H 3.892 0.02 1 867 . 91 ARG CB C 27.441 0.05 1 868 . 91 ARG HB2 H 1.542 0.02 1 869 . 91 ARG CD C 43.409 0.05 1 870 . 91 ARG HD2 H 3.149 0.02 1 871 . 91 ARG C C 175.374 0.05 1 872 . 92 ILE N N 120.718 0.05 1 873 . 92 ILE H H 8.297 0.02 1 874 . 92 ILE CA C 60.607 0.05 1 875 . 92 ILE HA H 3.931 0.02 1 876 . 92 ILE CB C 38.737 0.05 1 877 . 92 ILE HB H 1.455 0.02 1 878 . 92 ILE CG1 C 26.819 0.05 2 879 . 92 ILE HG13 H 0.885 0.02 9 880 . 92 ILE HG12 H 1.389 0.02 9 881 . 92 ILE CD1 C 13.036 0.05 1 882 . 92 ILE HD1 H 0.784 0.02 1 883 . 92 ILE CG2 C 17.381 0.05 2 884 . 92 ILE HG2 H 0.757 0.02 1 885 . 92 ILE C C 175.990 0.05 1 886 . 93 ASP N N 129.318 0.05 1 887 . 93 ASP H H 8.583 0.02 1 888 . 93 ASP CA C 54.503 0.05 1 889 . 93 ASP HA H 4.397 0.02 1 890 . 93 ASP CB C 40.008 0.05 1 891 . 93 ASP HB3 H 2.442 0.02 2 892 . 93 ASP HB2 H 2.602 0.02 2 893 . 93 ASP C C 175.511 0.05 1 894 . 94 VAL N N 116.186 0.05 1 895 . 94 VAL H H 7.727 0.02 1 896 . 94 VAL CA C 58.774 0.05 1 897 . 94 VAL HA H 4.587 0.02 1 898 . 94 VAL CB C 34.955 0.05 1 899 . 94 VAL HB H 2.080 0.02 1 900 . 94 VAL CG2 C 23.011 0.05 2 901 . 94 VAL HG1 H 0.841 0.02 1 902 . 94 VAL C C 175.887 0.05 1 903 . 95 LYS N N 119.137 0.05 1 904 . 95 LYS H H 9.214 0.02 1 905 . 95 LYS CA C 56.314 0.05 1 906 . 95 LYS HA H 4.317 0.02 1 907 . 95 LYS CB C 33.661 0.05 1 908 . 95 LYS HB2 H 1.692 0.02 1 909 . 95 LYS CG C 24.371 0.05 1 910 . 95 LYS HG2 H 1.483 0.02 1 911 . 95 LYS CD C 29.881 0.05 1 912 . 95 LYS HD2 H 2.053 0.02 1 913 . 95 LYS C C 177.563 0.05 1 914 . 96 ASP N N 112.324 0.05 1 915 . 96 ASP H H 7.419 0.02 1 916 . 96 ASP CA C 52.577 0.05 1 917 . 96 ASP HA H 5.496 0.02 1 918 . 96 ASP HB3 H 2.796 0.02 2 919 . 96 ASP HB2 H 2.006 0.02 2 920 . 96 ASP C C 176.297 0.05 1 921 . 97 THR N N 109.616 0.05 1 922 . 97 THR H H 7.229 0.02 1 923 . 97 THR CA C 65.722 0.05 1 924 . 97 THR HA H 3.593 0.02 1 925 . 97 THR CG2 C 22.455 0.05 1 926 . 97 THR HG2 H 1.269 0.02 1 927 . 97 THR C C 174.827 0.05 1 928 . 98 LYS N N 121.364 0.05 1 929 . 98 LYS H H 7.870 0.02 1 930 . 98 LYS CA C 59.374 0.05 1 931 . 98 LYS HA H 3.891 0.02 1 932 . 98 LYS CB C 31.591 0.05 1 933 . 98 LYS HB3 H 1.684 0.02 2 934 . 98 LYS HB2 H 2.027 0.02 2 935 . 98 LYS CG C 24.903 0.05 1 936 . 98 LYS HG2 H 1.396 0.02 1 937 . 98 LYS CD C 27.897 0.05 1 938 . 98 LYS HD2 H 2.041 0.02 1 939 . 98 LYS C C 177.973 0.05 1 940 . 99 GLU N N 119.526 0.05 1 941 . 99 GLU H H 8.379 0.02 1 942 . 99 GLU CA C 59.703 0.05 1 943 . 99 GLU HA H 4.040 0.02 1 944 . 99 GLU CB C 29.874 0.05 1 945 . 99 GLU HB2 H 2.053 0.02 1 946 . 99 GLU CG C 36.872 0.05 1 947 . 99 GLU HG3 H 2.217 0.02 2 948 . 99 GLU HG2 H 2.682 0.02 2 949 . 99 GLU C C 178.931 0.05 1 950 . 100 ALA N N 119.222 0.05 1 951 . 100 ALA H H 7.383 0.02 1 952 . 100 ALA CA C 55.032 0.05 1 953 . 100 ALA HA H 4.333 0.02 1 954 . 100 ALA CB C 19.336 0.05 1 955 . 100 ALA HB H 1.445 0.02 1 956 . 100 ALA C C 178.486 0.05 1 957 . 101 LEU N N 118.204 0.05 1 958 . 101 LEU H H 8.110 0.02 1 959 . 101 LEU CA C 57.655 0.05 1 960 . 101 LEU HA H 3.944 0.02 1 961 . 101 LEU CG C 26.583 0.05 1 962 . 101 LEU HG H 1.835 0.02 1 963 . 101 LEU CD1 C 25.348 0.05 2 964 . 101 LEU HD1 H 0.865 0.02 2 965 . 101 LEU CD2 C 21.770 0.05 2 966 . 101 LEU HD2 H 0.965 0.02 2 967 . 101 LEU C C 180.333 0.05 1 968 . 102 ASP N N 120.690 0.05 1 969 . 102 ASP H H 8.654 0.02 1 970 . 102 ASP CA C 56.974 0.05 1 971 . 102 ASP HA H 4.334 0.02 1 972 . 102 ASP CB C 39.333 0.05 1 973 . 102 ASP HB3 H 2.620 0.02 2 974 . 102 ASP HB2 H 2.861 0.02 2 975 . 102 ASP C C 179.444 0.05 1 976 . 103 LYS N N 120.730 0.05 1 977 . 103 LYS H H 8.183 0.02 1 978 . 103 LYS CA C 57.917 0.05 1 979 . 103 LYS HA H 4.168 0.02 1 980 . 103 LYS CB C 30.823 0.05 1 981 . 103 LYS HB3 H 1.837 0.02 2 982 . 103 LYS HB2 H 2.178 0.02 2 983 . 103 LYS CG C 24.557 0.05 1 984 . 103 LYS HG3 H 1.411 0.02 2 985 . 103 LYS HG2 H 1.696 0.02 2 986 . 103 LYS C C 179.752 0.05 1 987 . 104 ILE N N 120.114 0.05 1 988 . 104 ILE H H 8.142 0.02 1 989 . 104 ILE CA C 64.396 0.05 1 990 . 104 ILE HA H 3.724 0.02 1 991 . 104 ILE CB C 37.341 0.05 1 992 . 104 ILE HB H 1.900 0.02 1 993 . 104 ILE CG1 C 28.652 0.05 2 994 . 104 ILE HG13 H 1.280 0.02 9 995 . 104 ILE HG12 H 1.539 0.02 9 996 . 104 ILE CD1 C 13.598 0.05 1 997 . 104 ILE HD1 H 0.732 0.02 1 998 . 104 ILE CG2 C 17.458 0.05 2 999 . 104 ILE HG2 H 0.800 0.02 1 1000 . 104 ILE C C 178.178 0.05 1 1001 . 105 GLU N N 121.696 0.05 1 1002 . 105 GLU H H 8.000 0.02 1 1003 . 105 GLU CA C 59.305 0.05 1 1004 . 105 GLU HA H 3.996 0.02 1 1005 . 105 GLU CB C 32.319 0.05 1 1006 . 105 GLU HB2 H 2.191 0.02 1 1007 . 105 GLU C C 178.589 0.05 1 1008 . 106 GLU N N 119.486 0.05 1 1009 . 106 GLU H H 8.009 0.02 1 1010 . 106 GLU CA C 58.866 0.05 1 1011 . 106 GLU HA H 4.008 0.02 1 1012 . 106 GLU CB C 29.340 0.05 1 1013 . 106 GLU HB2 H 2.145 0.02 1 1014 . 106 GLU CG C 36.151 0.05 1 1015 . 106 GLU HG3 H 2.187 0.02 2 1016 . 106 GLU HG2 H 2.384 0.02 2 1017 . 106 GLU C C 178.794 0.05 1 1018 . 107 GLU N N 119.158 0.05 1 1019 . 107 GLU H H 7.980 0.02 1 1020 . 107 GLU CA C 59.039 0.05 1 1021 . 107 GLU HA H 4.003 0.02 1 1022 . 107 GLU CB C 29.322 0.05 1 1023 . 107 GLU HB2 H 2.125 0.02 1 1024 . 107 GLU CG C 35.912 0.05 1 1025 . 107 GLU HG3 H 2.198 0.02 2 1026 . 107 GLU HG2 H 2.371 0.02 2 1027 . 107 GLU C C 178.965 0.05 1 1028 . 108 GLN N N 118.640 0.05 1 1029 . 108 GLN H H 8.223 0.02 1 1030 . 108 GLN CA C 57.784 0.05 1 1031 . 108 GLN HA H 4.054 0.02 1 1032 . 108 GLN CB C 28.246 0.05 1 1033 . 108 GLN HB2 H 2.105 0.02 1 1034 . 108 GLN CG C 33.707 0.05 1 1035 . 108 GLN HG3 H 2.348 0.02 2 1036 . 108 GLN HG2 H 2.468 0.02 2 1037 . 108 GLN C C 177.802 0.05 1 1038 . 109 ASN N N 118.176 0.05 1 1039 . 109 ASN H H 8.218 0.02 1 1040 . 109 ASN CA C 54.599 0.05 1 1041 . 109 ASN HA H 4.531 0.02 1 1042 . 109 ASN CB C 38.078 0.05 1 1043 . 109 ASN HB2 H 2.823 0.02 1 1044 . 109 ASN C C 176.639 0.05 1 1045 . 110 LYS N N 120.472 0.05 1 1046 . 110 LYS H H 8.009 0.02 1 1047 . 110 LYS CA C 58.111 0.05 1 1048 . 110 LYS HA H 4.108 0.02 1 1049 . 110 LYS CB C 32.257 0.05 1 1050 . 110 LYS HB2 H 1.858 0.02 1 1051 . 110 LYS CG C 24.858 0.05 1 1052 . 110 LYS HG3 H 1.399 0.02 2 1053 . 110 LYS HG2 H 1.553 0.02 2 1054 . 110 LYS CD C 29.161 0.05 1 1055 . 110 LYS HD3 H 1.634 0.02 2 1056 . 110 LYS HD2 H 2.146 0.02 2 1057 . 110 LYS C C 177.768 0.05 1 1058 . 111 SER N N 114.651 0.05 1 1059 . 111 SER H H 7.987 0.02 1 1060 . 111 SER CA C 59.428 0.05 1 1061 . 111 SER HA H 4.292 0.02 1 1062 . 111 SER CB C 63.165 0.05 1 1063 . 111 SER HB2 H 3.901 0.02 1 1064 . 111 SER C C 175.032 0.05 1 1065 . 112 LYS N N 122.376 0.05 1 1066 . 112 LYS H H 7.917 0.02 1 1067 . 112 LYS CA C 56.956 0.05 1 1068 . 112 LYS HA H 4.165 0.02 1 1069 . 112 LYS CB C 32.413 0.05 1 1070 . 112 LYS HB2 H 1.791 0.02 1 1071 . 112 LYS CG C 24.858 0.05 1 1072 . 112 LYS HG2 H 1.451 0.02 1 1073 . 112 LYS CD C 28.778 0.05 1 1074 . 112 LYS HD2 H 1.630 0.02 1 1075 . 112 LYS C C 176.913 0.05 1 1076 . 113 LYS N N 121.030 0.05 1 1077 . 113 LYS H H 7.990 0.02 1 1078 . 113 LYS CA C 56.832 0.05 1 1079 . 113 LYS HA H 4.179 0.02 1 1080 . 113 LYS CB C 32.405 0.05 1 1081 . 113 LYS HB2 H 1.762 0.02 1 1082 . 113 LYS CG C 24.526 0.05 1 1083 . 113 LYS HG2 H 1.401 0.02 1 1084 . 113 LYS CD C 28.708 0.05 1 1085 . 113 LYS HD2 H 1.627 0.02 1 1086 . 113 LYS C C 176.879 0.05 1 1087 . 114 LYS N N 121.862 0.05 1 1088 . 114 LYS H H 8.100 0.02 1 1089 . 114 LYS CA C 56.829 0.05 1 1090 . 114 LYS HA H 4.171 0.02 1 1091 . 114 LYS CB C 32.409 0.05 1 1092 . 114 LYS HB2 H 1.752 0.02 1 1093 . 114 LYS CG C 24.348 0.05 1 1094 . 114 LYS HG2 H 1.422 0.02 1 1095 . 114 LYS CD C 28.729 0.05 1 1096 . 114 LYS HD2 H 1.639 0.02 1 1097 . 114 LYS C C 176.605 0.05 1 1098 . 115 ALA N N 124.430 0.05 1 1099 . 115 ALA H H 8.149 0.02 1 1100 . 115 ALA CA C 52.684 0.05 1 1101 . 115 ALA HA H 4.200 0.02 1 1102 . 115 ALA CB C 18.715 0.05 1 1103 . 115 ALA HB H 1.349 0.02 1 1104 . 115 ALA C C 177.905 0.05 1 1105 . 116 GLN N N 119.254 0.05 1 1106 . 116 GLN H H 8.198 0.02 1 1107 . 116 GLN CA C 56.210 0.05 1 1108 . 116 GLN HA H 4.209 0.02 1 1109 . 116 GLN CB C 28.955 0.05 1 1110 . 116 GLN HB2 H 1.974 0.02 1 1111 . 116 GLN CG C 33.636 0.05 1 1112 . 116 GLN HG2 H 2.321 0.02 1 1113 . 116 GLN C C 176.024 0.05 1 1114 . 117 GLN N N 121.270 0.05 1 1115 . 117 GLN H H 8.241 0.02 1 1116 . 117 GLN CA C 56.184 0.05 1 1117 . 117 GLN HA H 4.204 0.02 1 1118 . 117 GLN CB C 29.212 0.05 1 1119 . 117 GLN HB2 H 1.985 0.02 1 1120 . 117 GLN CG C 33.745 0.05 1 1121 . 117 GLN HG2 H 2.316 0.02 1 1122 . 117 GLN C C 175.579 0.05 1 1123 . 118 ALA N N 125.144 0.05 1 1124 . 118 ALA H H 8.240 0.02 1 1125 . 118 ALA CA C 52.539 0.05 1 1126 . 118 ALA HA H 4.219 0.02 1 1127 . 118 ALA CB C 18.740 0.05 1 1128 . 118 ALA HB H 1.339 0.02 1 1129 . 118 ALA C C 177.323 0.05 1 1130 . 119 ALA N N 123.174 0.05 1 1131 . 119 ALA H H 8.136 0.02 1 1132 . 119 ALA CA C 52.386 0.05 1 1133 . 119 ALA HA H 4.209 0.02 1 1134 . 119 ALA CB C 18.799 0.05 1 1135 . 119 ALA HB H 1.339 0.02 1 1136 . 119 ALA C C 177.323 0.05 1 1137 . 120 ALA N N 122.798 0.05 1 1138 . 120 ALA H H 8.134 0.02 1 1139 . 120 ALA CA C 52.466 0.05 1 1140 . 120 ALA HA H 4.233 0.02 1 1141 . 120 ALA CB C 18.661 0.05 1 1142 . 120 ALA HB H 1.321 0.02 1 1143 . 120 ALA C C 177.358 0.05 1 1144 . 121 ASP N N 119.464 0.05 1 1145 . 121 ASP H H 8.226 0.02 1 1146 . 121 ASP CA C 54.013 0.05 1 1147 . 121 ASP HA H 4.572 0.02 1 1148 . 121 ASP CB C 41.027 0.05 1 1149 . 121 ASP HB3 H 2.392 0.02 2 1150 . 121 ASP HB2 H 2.625 0.02 2 1151 . 121 ASP C C 176.434 0.05 1 1152 . 122 THR N N 113.628 0.05 1 1153 . 122 THR H H 8.047 0.02 1 1154 . 122 THR CA C 61.865 0.05 1 1155 . 122 THR HA H 4.280 0.02 1 1156 . 122 THR CG2 C 21.223 0.05 1 1157 . 122 THR HG2 H 1.140 0.02 1 1158 . 122 THR C C 175.237 0.05 1 1159 . 123 GLY N N 110.702 0.05 1 1160 . 123 GLY H H 8.399 0.02 1 1161 . 123 GLY CA C 45.283 0.05 1 1162 . 123 GLY C C 173.869 0.05 1 1163 . 123 GLY HA2 H 3.895 0.02 1 1164 . 124 ASN N N 118.608 0.05 1 1165 . 124 ASN H H 8.237 0.02 1 1166 . 124 ASN CA C 53.160 0.05 1 1167 . 124 ASN HA H 4.709 0.02 1 1168 . 124 ASN HB2 H 2.859 0.02 1 1169 . 124 ASN C C 174.964 0.05 1 1170 . 125 ASN N N 119.308 0.05 1 1171 . 125 ASN H H 8.413 0.02 1 1172 . 125 ASN CA C 53.300 0.05 1 1173 . 125 ASN HA H 4.697 0.02 1 1174 . 125 ASN HB2 H 2.751 0.02 1 1175 . 125 ASN C C 175.271 0.05 1 1176 . 126 SER N N 115.914 0.05 1 1177 . 126 SER H H 8.234 0.02 1 1178 . 126 SER CA C 58.669 0.05 1 1179 . 126 SER HA H 4.322 0.02 1 1180 . 126 SER HB2 H 3.859 0.02 1 1181 . 126 SER C C 174.485 0.05 1 1182 . 127 GLN N N 121.802 0.05 1 1183 . 127 GLN H H 8.321 0.02 1 1184 . 127 GLN CA C 55.661 0.05 1 1185 . 127 GLN HA H 4.265 0.02 1 1186 . 127 GLN CB C 28.843 0.05 1 1187 . 127 GLN HB2 H 1.878 0.02 1 1188 . 127 GLN HG3 H 2.330 0.02 2 1189 . 127 GLN HG2 H 2.106 0.02 2 1190 . 127 GLN C C 176.024 0.05 1 1191 . 128 VAL N N 119.836 0.05 1 1192 . 128 VAL H H 7.957 0.02 1 1193 . 128 VAL CA C 62.645 0.05 1 1194 . 128 VAL HA H 4.055 0.02 1 1195 . 128 VAL CB C 32.361 0.05 1 1196 . 128 VAL HB H 1.999 0.02 1 1197 . 128 VAL CG2 C 20.129 0.05 2 1198 . 128 VAL HG1 H 0.843 0.02 1 1199 . 128 VAL C C 176.126 0.05 1 1200 . 129 SER N N 118.408 0.05 1 1201 . 129 SER H H 8.195 0.02 1 1202 . 129 SER CA C 58.330 0.05 1 1203 . 129 SER HA H 4.395 0.02 1 1204 . 129 SER CB C 63.228 0.05 1 1205 . 129 SER HB2 H 3.816 0.02 1 1206 . 129 SER C C 174.553 0.05 1 1207 . 130 GLN N N 121.686 0.05 1 1208 . 130 GLN H H 8.298 0.02 1 1209 . 130 GLN CA C 56.010 0.05 1 1210 . 130 GLN HA H 4.698 0.02 1 1211 . 130 GLN HB2 H 1.848 0.02 1 1212 . 130 GLN HG3 H 1.989 0.02 2 1213 . 130 GLN HG2 H 2.235 0.02 2 1214 . 130 GLN C C 175.408 0.05 1 1215 . 131 ASN N N 118.824 0.05 1 1216 . 131 ASN H H 8.229 0.02 1 1217 . 131 ASN CA C 53.026 0.05 1 1218 . 131 ASN HA H 4.541 0.02 1 1219 . 131 ASN HB3 H 2.602 0.02 2 1220 . 131 ASN HB2 H 2.729 0.02 2 1221 . 131 ASN C C 174.621 0.05 1 1222 . 132 TYR N N 120.424 0.05 1 1223 . 132 TYR H H 7.920 0.02 1 1224 . 132 TYR CA C 57.960 0.05 1 stop_ save_