data_4661 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of APAF-1 CARD ; _BMRB_accession_number 4661 _BMRB_flat_file_name bmr4661.str _Entry_type original _Submission_date 2000-02-02 _Accession_date 2000-02-02 _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 Zhou Pei . . 2 Chou James . . 3 Sanchez-Olea Roberto . . 4 Yuan Junying . . 5 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 511 "13C chemical shifts" 141 "15N chemical shifts" 90 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-07 original author . stop_ _Original_release_date 2000-03-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: A structural basis for specific adaptor/caspase interaction ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99432221 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Pei . . 2 Chou James . . 3 Sanchez-Olea Roberto . . 4 Yuan Junying . . 5 Wagner Gerhard . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 96 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11265 _Page_last 11270 _Year 1999 _Details . loop_ _Keyword Apoptosis 'Programmed cell death' APAF CARD DED DD 'Caspase recruitment domain' 'homophilic interaction' stop_ save_ ################################## # Molecular system description # ################################## save_system_Apaf-1_CARD _Saveframe_category molecular_system _Mol_system_name 'Apoptotic protease activating factor 1' _Abbreviation_common 'Apaf-1 CARD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Apaf-1 CARD' $Apaf-1_CARD 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_Apaf-1_CARD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'APOPTOTIC PROTEASE ACTIVATING FACTOR 1' _Abbreviation_common 'Apaf-1 CARD' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; MDAKARNCLLQHREALEKDI KTSYIMDHMISDGFLTISEE EKVRNEPTQQQRAAMLIKMI LKKDNDSYVSFYNALLHEGY KDLAALLHDGIPVVSSS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ALA 4 LYS 5 ALA 6 ARG 7 ASN 8 CYS 9 LEU 10 LEU 11 GLN 12 HIS 13 ARG 14 GLU 15 ALA 16 LEU 17 GLU 18 LYS 19 ASP 20 ILE 21 LYS 22 THR 23 SER 24 TYR 25 ILE 26 MET 27 ASP 28 HIS 29 MET 30 ILE 31 SER 32 ASP 33 GLY 34 PHE 35 LEU 36 THR 37 ILE 38 SER 39 GLU 40 GLU 41 GLU 42 LYS 43 VAL 44 ARG 45 ASN 46 GLU 47 PRO 48 THR 49 GLN 50 GLN 51 GLN 52 ARG 53 ALA 54 ALA 55 MET 56 LEU 57 ILE 58 LYS 59 MET 60 ILE 61 LEU 62 LYS 63 LYS 64 ASP 65 ASN 66 ASP 67 SER 68 TYR 69 VAL 70 SER 71 PHE 72 TYR 73 ASN 74 ALA 75 LEU 76 LEU 77 HIS 78 GLU 79 GLY 80 TYR 81 LYS 82 ASP 83 LEU 84 ALA 85 ALA 86 LEU 87 LEU 88 HIS 89 ASP 90 GLY 91 ILE 92 PRO 93 VAL 94 VAL 95 SER 96 SER 97 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1C15 "Solution Structure Of Apaf-1 Card" 100.00 97 100.00 100.00 3.36e-64 PDB 1CWW "Solution Structure Of The Caspase Recruitment Domain (Card) From Apaf-1" 100.00 102 100.00 100.00 5.54e-64 PDB 1CY5 "Crystal Structure Of The Apaf-1 Card" 100.00 97 100.00 100.00 3.36e-64 PDB 1Z6T "Structure Of The Apoptotic Protease-activating Factor 1 Bound To Adp" 100.00 591 100.00 100.00 8.69e-59 PDB 2P1H "Rapid Folding And Unfolding Of Apaf-1 Card" 94.85 94 100.00 100.00 1.02e-60 PDB 2YGS "Card Domain From Apaf-1" 94.85 92 100.00 100.00 9.85e-61 PDB 3J2T "An Improved Model Of The Human Apoptosome" 100.00 1263 100.00 100.00 3.18e-57 PDB 3YGS "Apaf-1 Card In Complex With Prodomain Of Procaspase-9" 97.94 95 100.00 100.00 7.23e-63 PDB 4RHW "Crystal Structure Of Apaf-1 Card And Caspase-9 Card Complex" 100.00 97 100.00 100.00 3.36e-64 DBJ BAA24843 "KIAA0413 [Homo sapiens]" 100.00 1237 100.00 100.00 2.57e-57 DBJ BAC77343 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 338 100.00 100.00 1.41e-61 DBJ BAJ20211 "apoptotic peptidase activating factor 1 [synthetic construct]" 100.00 1237 100.00 100.00 2.57e-57 EMBL CAB55579 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1205 100.00 100.00 1.90e-57 EMBL CAB55580 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1205 100.00 100.00 1.70e-57 EMBL CAB55581 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1205 100.00 100.00 1.75e-57 EMBL CAB55582 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1205 100.00 100.00 1.86e-57 EMBL CAB55583 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1205 100.00 100.00 2.01e-57 GB AAC51678 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1194 100.00 100.00 2.05e-57 GB AAD34016 "apoptotic protease activating factor 1 [Homo sapiens]" 100.00 1248 100.00 100.00 2.60e-57 GB AAD38344 "apoptotic protease activating factor-1 long isoform APAF-1L [Homo sapiens]" 100.00 1237 100.00 100.00 2.57e-57 GB AAI36532 "Apoptotic peptidase activating factor 1 [Homo sapiens]" 100.00 1248 100.00 100.00 2.60e-57 GB AAI36533 "Apoptotic peptidase activating factor 1 [Homo sapiens]" 100.00 1248 100.00 100.00 2.60e-57 REF NP_001151 "apoptotic protease-activating factor 1 isoform b [Homo sapiens]" 100.00 1194 100.00 100.00 2.05e-57 REF NP_037361 "apoptotic protease-activating factor 1 isoform a [Homo sapiens]" 100.00 1237 100.00 100.00 2.57e-57 REF NP_863651 "apoptotic protease-activating factor 1 isoform c [Homo sapiens]" 100.00 1248 100.00 100.00 2.60e-57 REF NP_863658 "apoptotic protease-activating factor 1 isoform d [Homo sapiens]" 100.00 1205 100.00 100.00 1.90e-57 REF NP_863659 "apoptotic protease-activating factor 1 isoform e [Homo sapiens]" 100.00 338 100.00 100.00 1.41e-61 SP O14727 "RecName: Full=Apoptotic protease-activating factor 1; Short=APAF-1" 100.00 1248 100.00 100.00 2.60e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Apaf-1_CARD Human 9606 Eukaryota metazoa Homo sapiens 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 $Apaf-1_CARD 'recombinant technology' Bacteria Escherichia coli . pGEX-2T stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Apaf-1_CARD . mM 0.5 1 [U-15N] 'phosphate buffer' 20 mM . . . NaCl 50 mM . . . DTT 5 mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Apaf-1_CARD 1 mM [U-13C] 'phosphate buffer' 20 mM . NaCl 50 mM . DTT 5 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Apaf-1_CARD 1 mM . 'phosphate buffer' 20 mM . NaCl 50 mM . DTT 5 mM . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Apaf-1_CARD 1 mM '[U-13C; U-15N; U-80% 2H]' 'phosphate buffer' 20 mM . NaCl 50 mM . DTT 5 mM . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'Structure solution' stop_ _Details 'GUNTERT ET AL' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details BRUNGER save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_13C-separated_NOESY _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_HMQC-J_4 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 pH temperature 300 1 K pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 $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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Apaf-1 CARD' _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 MET N N 123.5 . 1 2 . 1 MET H H 8.11 . 1 3 . 1 MET CA C 55.3 . 1 4 . 1 MET HA H 4.09 . 1 5 . 1 MET HB2 H 1.71 . 2 6 . 1 MET HB3 H 2.05 . 2 7 . 1 MET HG2 H 2.24 . 2 8 . 1 MET HG3 H 2.52 . 2 9 . 2 ASP N N 127.0 . 1 10 . 2 ASP H H 9.39 . 1 11 . 2 ASP CA C 54.7 . 1 12 . 2 ASP HA H 4.28 . 1 13 . 2 ASP HB2 H 2.56 . 2 14 . 2 ASP HB3 H 2.64 . 2 15 . 3 ALA N N 125.9 . 1 16 . 3 ALA H H 8.69 . 1 17 . 3 ALA CA C 55.2 . 1 18 . 3 ALA HA H 3.83 . 1 19 . 3 ALA HB H 1.33 . 1 20 . 3 ALA CB C 18.0 . 1 21 . 4 LYS N N 116.3 . 1 22 . 4 LYS H H 8.54 . 1 23 . 4 LYS CA C 59.2 . 1 24 . 4 LYS HA H 3.87 . 1 25 . 4 LYS HB2 H 1.66 . 2 26 . 4 LYS HB3 H 1.73 . 2 27 . 4 LYS HG2 H 1.21 . 2 28 . 4 LYS HG3 H 1.38 . 2 29 . 4 LYS HD2 H 1.53 . 1 30 . 4 LYS HD3 H 1.53 . 1 31 . 5 ALA N N 122.8 . 1 32 . 5 ALA H H 6.74 . 1 33 . 5 ALA CA C 54.5 . 1 34 . 5 ALA HA H 3.67 . 1 35 . 5 ALA HB H 0.62 . 1 36 . 5 ALA CB C 16.4 . 1 37 . 6 ARG N N 118.3 . 1 38 . 6 ARG H H 7.90 . 1 39 . 6 ARG CA C 59.7 . 1 40 . 6 ARG HA H 3.72 . 1 41 . 6 ARG HB2 H 1.59 . 1 42 . 6 ARG HB3 H 1.59 . 1 43 . 6 ARG HG2 H 1.42 . 1 44 . 6 ARG HG3 H 1.42 . 1 45 . 6 ARG HD2 H 3.17 . 1 46 . 6 ARG HD3 H 3.17 . 1 47 . 7 ASN N N 114.1 . 1 48 . 7 ASN H H 8.61 . 1 49 . 7 ASN CA C 55.5 . 1 50 . 7 ASN HA H 4.33 . 1 51 . 7 ASN HB2 H 2.67 . 2 52 . 7 ASN HB3 H 2.76 . 2 53 . 8 CYS N N 121.3 . 1 54 . 8 CYS H H 7.71 . 1 55 . 8 CYS CA C 63.7 . 1 56 . 8 CYS HA H 4.14 . 1 57 . 8 CYS HB2 H 3.18 . 2 58 . 8 CYS HB3 H 3.29 . 2 59 . 9 LEU N N 118.0 . 1 60 . 9 LEU H H 7.86 . 1 61 . 9 LEU CA C 57.9 . 1 62 . 9 LEU HA H 3.94 . 1 63 . 9 LEU HB2 H 1.76 . 2 64 . 9 LEU HB3 H 1.97 . 2 65 . 9 LEU HG H 1.48 . 1 66 . 9 LEU HD1 H 0.73 . 2 67 . 9 LEU HD2 H 0.74 . 2 68 . 9 LEU CD1 C 24.5 . 1 69 . 9 LEU CD2 C 25.7 . 1 70 . 10 LEU N N 114.6 . 1 71 . 10 LEU H H 8.16 . 1 72 . 10 LEU CA C 57.5 . 1 73 . 10 LEU HA H 3.87 . 1 74 . 10 LEU HB2 H 1.76 . 2 75 . 10 LEU HB3 H 1.82 . 2 76 . 10 LEU HG H 1.35 . 1 77 . 10 LEU CD1 C 23.0 . 1 78 . 10 LEU HD1 H 0.78 . 1 79 . 10 LEU HD2 H 0.78 . 1 80 . 11 GLN N N 119.1 . 1 81 . 11 GLN H H 8.30 . 1 82 . 11 GLN CA C 58.0 . 1 83 . 11 GLN HA H 3.81 . 1 84 . 11 GLN HB2 H 1.57 . 2 85 . 11 GLN HB3 H 1.73 . 2 86 . 11 GLN HG2 H 1.94 . 1 87 . 11 GLN HG3 H 1.94 . 1 88 . 12 HIS N N 114.1 . 1 89 . 12 HIS H H 7.29 . 1 90 . 12 HIS CA C 55.2 . 1 91 . 12 HIS HA H 5.08 . 1 92 . 12 HIS HB2 H 2.65 . 2 93 . 12 HIS HB3 H 3.27 . 2 94 . 12 HIS HD2 H 7.27 . 1 95 . 12 HIS HE1 H 7.80 . 1 96 . 13 ARG N N 120.9 . 1 97 . 13 ARG H H 7.37 . 1 98 . 13 ARG CA C 60.7 . 1 99 . 13 ARG HA H 3.86 . 1 100 . 13 ARG HB2 H 1.90 . 2 101 . 13 ARG HB3 H 2.11 . 2 102 . 13 ARG HG2 H 1.53 . 2 103 . 13 ARG HG3 H 1.69 . 2 104 . 14 GLU N N 118.0 . 1 105 . 14 GLU H H 8.68 . 1 106 . 14 GLU CA C 59.5 . 1 107 . 14 GLU HA H 3.86 . 1 108 . 14 GLU HB2 H 1.93 . 1 109 . 14 GLU HB3 H 1.93 . 1 110 . 14 GLU HG2 H 2.14 . 2 111 . 14 GLU HG3 H 2.24 . 2 112 . 15 ALA N N 121.7 . 1 113 . 15 ALA H H 7.73 . 1 114 . 15 ALA CA C 54.5 . 1 115 . 15 ALA HA H 2.68 . 1 116 . 15 ALA HB H 1.37 . 1 117 . 15 ALA CB C 17.3 . 1 118 . 16 LEU N N 116.3 . 1 119 . 16 LEU H H 7.91 . 1 120 . 16 LEU CA C 57.7 . 1 121 . 16 LEU HA H 3.88 . 1 122 . 16 LEU HB2 H 1.81 . 2 123 . 16 LEU HB3 H 2.05 . 2 124 . 16 LEU HG H 1.20 . 1 125 . 16 LEU HD1 H 0.92 . 2 126 . 16 LEU HD2 H 0.75 . 2 127 . 16 LEU CD1 C 26.5 . 1 128 . 16 LEU CD2 C 22.5 . 1 129 . 17 GLU N N 115.4 . 1 130 . 17 GLU H H 8.50 . 1 131 . 17 GLU CA C 58.3 . 1 132 . 17 GLU HA H 3.64 . 1 133 . 17 GLU HB2 H 1.86 . 2 134 . 17 GLU HB3 H 1.96 . 2 135 . 17 GLU HG2 H 2.51 . 1 136 . 17 GLU HG3 H 2.51 . 1 137 . 18 LYS N N 114.1 . 1 138 . 18 LYS H H 7.28 . 1 139 . 18 LYS CA C 58.4 . 1 140 . 18 LYS HA H 3.95 . 1 141 . 18 LYS HB2 H 1.76 . 1 142 . 18 LYS HB3 H 1.76 . 1 143 . 18 LYS HG2 H 1.45 . 1 144 . 18 LYS HG3 H 1.45 . 1 145 . 18 LYS HD2 H 1.64 . 1 146 . 18 LYS HD3 H 1.64 . 1 147 . 19 ASP N N 113.7 . 1 148 . 19 ASP H H 6.95 . 1 149 . 19 ASP CA C 55.0 . 1 150 . 19 ASP HA H 4.96 . 1 151 . 19 ASP HB2 H 2.38 . 2 152 . 19 ASP HB3 H 2.61 . 2 153 . 20 ILE N N 112.6 . 1 154 . 20 ILE H H 7.52 . 1 155 . 20 ILE CA C 63.2 . 1 156 . 20 ILE HA H 3.65 . 1 157 . 20 ILE HB H 1.29 . 1 158 . 20 ILE HG2 H 0.31 . 1 159 . 20 ILE CG2 C 16.9 . 1 160 . 20 ILE HG12 H 0.95 . 1 161 . 20 ILE HG13 H 0.95 . 1 162 . 20 ILE HD1 H 0.63 . 1 163 . 20 ILE CD1 C 14.0 . 1 164 . 21 LYS N N 122.8 . 1 165 . 21 LYS H H 7.37 . 1 166 . 21 LYS CA C 55.0 . 1 167 . 21 LYS HA H 4.50 . 1 168 . 21 LYS HB2 H 1.81 . 2 169 . 21 LYS HB3 H 1.95 . 2 170 . 21 LYS HG2 H 1.34 . 2 171 . 21 LYS HG3 H 1.53 . 2 172 . 21 LYS HD2 H 1.56 . 2 173 . 21 LYS HD3 H 1.65 . 2 174 . 22 THR CA C 66.2 . 1 175 . 22 THR HA H 3.64 . 1 176 . 22 THR CB C 69.2 . 1 177 . 22 THR HB H 4.04 . 1 178 . 22 THR HG2 H 1.10 . 1 179 . 22 THR CG2 C 21.2 . 1 180 . 23 SER HA H 4.42 . 1 181 . 24 TYR N N 118.7 . 1 182 . 24 TYR H H 7.46 . 1 183 . 24 TYR CA C 59.0 . 1 184 . 24 TYR HA H 4.39 . 1 185 . 24 TYR HB2 H 2.93 . 2 186 . 24 TYR HB3 H 3.14 . 2 187 . 24 TYR HD1 H 7.16 . 1 188 . 24 TYR HD2 H 7.16 . 1 189 . 24 TYR HE1 H 6.77 . 1 190 . 24 TYR HE2 H 6.77 . 1 191 . 25 ILE N N 116.5 . 1 192 . 25 ILE H H 7.27 . 1 193 . 25 ILE CA C 62.7 . 1 194 . 25 ILE HA H 3.80 . 1 195 . 25 ILE HB H 1.81 . 1 196 . 25 ILE HG2 H 0.89 . 1 197 . 25 ILE CG2 C 17.5 . 1 198 . 25 ILE HG12 H 1.39 . 1 199 . 25 ILE HG13 H 1.39 . 1 200 . 25 ILE HD1 H 0.70 . 1 201 . 25 ILE CD1 C 12.1 . 1 202 . 26 MET N N 117.0 . 1 203 . 26 MET H H 8.44 . 1 204 . 26 MET CA C 61.0 . 1 205 . 26 MET HA H 3.74 . 1 206 . 26 MET HB2 H 2.47 . 1 207 . 26 MET HB3 H 2.47 . 1 208 . 26 MET HG2 H 1.88 . 2 209 . 26 MET HG3 H 2.95 . 2 210 . 26 MET HE H 1.66 . 1 211 . 26 MET CE C 16.0 . 1 212 . 27 ASP N N 117.8 . 1 213 . 27 ASP H H 7.79 . 1 214 . 27 ASP CA C 57.7 . 1 215 . 27 ASP HA H 4.19 . 1 216 . 27 ASP HB2 H 2.42 . 2 217 . 27 ASP HB3 H 2.48 . 2 218 . 28 HIS N N 116.3 . 1 219 . 28 HIS H H 7.21 . 1 220 . 28 HIS CA C 58.5 . 1 221 . 28 HIS HA H 4.29 . 1 222 . 28 HIS HB2 H 3.18 . 2 223 . 28 HIS HB3 H 3.50 . 2 224 . 29 MET N N 117.0 . 1 225 . 29 MET H H 7.65 . 1 226 . 29 MET CA C 59.2 . 1 227 . 29 MET HA H 4.21 . 1 228 . 29 MET HB2 H 1.94 . 2 229 . 29 MET HB3 H 2.06 . 2 230 . 29 MET HG2 H 2.71 . 1 231 . 29 MET HG3 H 2.71 . 1 232 . 30 ILE N N 121.3 . 1 233 . 30 ILE H H 8.95 . 1 234 . 30 ILE CA C 64.2 . 1 235 . 30 ILE HA H 4.04 . 1 236 . 30 ILE HB H 1.77 . 1 237 . 30 ILE HG2 H 0.76 . 1 238 . 30 ILE CG2 C 16.5 . 1 239 . 30 ILE HG12 H 1.46 . 2 240 . 30 ILE HG13 H 1.63 . 2 241 . 30 ILE HD1 H 0.60 . 1 242 . 30 ILE CD1 C 13.3 . 1 243 . 31 SER N N 117.4 . 1 244 . 31 SER H H 7.80 . 1 245 . 31 SER CA C 61.4 . 1 246 . 31 SER HA H 4.05 . 1 247 . 31 SER HB2 H 3.96 . 1 248 . 31 SER HB3 H 3.96 . 1 249 . 32 ASP N N 117.8 . 1 250 . 32 ASP H H 7.93 . 1 251 . 32 ASP CA C 55.2 . 1 252 . 32 ASP HA H 4.36 . 1 253 . 32 ASP HB2 H 2.89 . 2 254 . 32 ASP HB3 H 2.98 . 2 255 . 33 GLY N N 104.3 . 1 256 . 33 GLY H H 7.54 . 1 257 . 33 GLY CA C 44.4 . 1 258 . 33 GLY HA2 H 3.61 . 2 259 . 33 GLY HA3 H 3.81 . 2 260 . 34 PHE N N 117.0 . 1 261 . 34 PHE H H 7.69 . 1 262 . 34 PHE CA C 58.6 . 1 263 . 34 PHE HA H 4.71 . 1 264 . 34 PHE HB2 H 2.37 . 2 265 . 34 PHE HB3 H 3.76 . 2 266 . 34 PHE HD1 H 7.24 . 1 267 . 34 PHE HD2 H 7.24 . 1 268 . 34 PHE HE1 H 7.24 . 1 269 . 34 PHE HE2 H 7.24 . 1 270 . 34 PHE HZ H 7.23 . 1 271 . 35 LEU N N 119.1 . 1 272 . 35 LEU H H 7.05 . 1 273 . 35 LEU CA C 53.2 . 1 274 . 35 LEU HA H 4.64 . 1 275 . 35 LEU HB2 H 1.47 . 2 276 . 35 LEU HB3 H 1.75 . 2 277 . 35 LEU HG H 1.10 . 1 278 . 35 LEU CD1 C 25.7 . 1 279 . 35 LEU HD1 H 0.77 . 1 280 . 35 LEU HD2 H 0.77 . 1 281 . 36 THR N N 115.7 . 1 282 . 36 THR H H 8.96 . 1 283 . 36 THR HA H 4.63 . 1 284 . 36 THR CB C 71.2 . 1 285 . 36 THR HB H 4.59 . 1 286 . 36 THR HG2 H 1.11 . 1 287 . 36 THR CG2 C 21.2 . 1 288 . 37 ILE N N 119.4 . 1 289 . 37 ILE H H 8.58 . 1 290 . 37 ILE CA C 63.7 . 1 291 . 37 ILE HA H 3.95 . 1 292 . 37 ILE HB H 1.85 . 1 293 . 37 ILE HG2 H 0.90 . 1 294 . 37 ILE CG2 C 17.2 . 1 295 . 37 ILE HG12 H 1.27 . 2 296 . 37 ILE HG13 H 1.48 . 2 297 . 37 ILE HD1 H 0.80 . 1 298 . 37 ILE CD1 C 12.4 . 1 299 . 38 SER N N 115.0 . 1 300 . 38 SER H H 7.98 . 1 301 . 38 SER CA C 61.2 . 1 302 . 38 SER HA H 4.19 . 1 303 . 38 SER HB2 H 3.75 . 1 304 . 38 SER HB3 H 3.75 . 1 305 . 39 GLU N N 123.3 . 1 306 . 39 GLU H H 7.57 . 1 307 . 39 GLU CA C 59.3 . 1 308 . 39 GLU HA H 3.73 . 1 309 . 39 GLU HB2 H 1.83 . 2 310 . 39 GLU HB3 H 2.17 . 2 311 . 39 GLU HG2 H 2.33 . 1 312 . 39 GLU HG3 H 2.33 . 1 313 . 40 GLU N N 120.2 . 1 314 . 40 GLU H H 8.23 . 1 315 . 40 GLU CA C 59.2 . 1 316 . 40 GLU HA H 3.93 . 1 317 . 40 GLU HB2 H 2.42 . 1 318 . 40 GLU HB3 H 2.42 . 1 319 . 41 GLU N N 117.6 . 1 320 . 41 GLU H H 8.03 . 1 321 . 41 GLU HA H 3.94 . 1 322 . 41 GLU HB2 H 1.91 . 2 323 . 41 GLU HB3 H 2.04 . 2 324 . 42 LYS N N 118.3 . 1 325 . 42 LYS H H 7.33 . 1 326 . 42 LYS CA C 58.7 . 1 327 . 42 LYS HA H 3.89 . 1 328 . 42 LYS HB2 H 1.56 . 2 329 . 42 LYS HB3 H 1.86 . 2 330 . 42 LYS HG2 H 1.34 . 1 331 . 42 LYS HG3 H 1.34 . 1 332 . 42 LYS HD2 H 1.48 . 1 333 . 42 LYS HD3 H 1.48 . 1 334 . 43 VAL N N 118.9 . 1 335 . 43 VAL H H 7.78 . 1 336 . 43 VAL CA C 66.9 . 1 337 . 43 VAL HA H 3.43 . 1 338 . 43 VAL CB C 31.7 . 1 339 . 43 VAL HB H 1.95 . 1 340 . 43 VAL HG1 H 0.96 . 2 341 . 43 VAL HG2 H 0.84 . 2 342 . 43 VAL CG1 C 21.5 . 1 343 . 43 VAL CG2 C 22.5 . 1 344 . 44 ARG N N 115.9 . 1 345 . 44 ARG H H 8.35 . 1 346 . 44 ARG CA C 58.7 . 1 347 . 44 ARG HA H 3.64 . 1 348 . 44 ARG HB2 H 1.69 . 1 349 . 44 ARG HB3 H 1.69 . 1 350 . 44 ARG HG2 H 1.54 . 1 351 . 44 ARG HG3 H 1.54 . 1 352 . 45 ASN N N 113.3 . 1 353 . 45 ASN H H 7.37 . 1 354 . 45 ASN CA C 53.6 . 1 355 . 45 ASN HA H 4.43 . 1 356 . 45 ASN HB2 H 2.69 . 2 357 . 45 ASN HB3 H 2.80 . 2 358 . 46 GLU N N 120.9 . 1 359 . 46 GLU H H 7.74 . 1 360 . 46 GLU CA C 54.0 . 1 361 . 46 GLU HA H 4.52 . 1 362 . 46 GLU HB2 H 1.82 . 2 363 . 46 GLU HB3 H 2.19 . 2 364 . 46 GLU HG2 H 2.42 . 1 365 . 46 GLU HG3 H 2.42 . 1 366 . 48 THR N N 104.6 . 1 367 . 48 THR H H 6.77 . 1 368 . 48 THR CA C 58.4 . 1 369 . 48 THR HA H 4.81 . 1 370 . 48 THR CB C 73.1 . 1 371 . 48 THR HB H 4.54 . 1 372 . 48 THR HG2 H 1.18 . 1 373 . 50 GLN HA H 4.29 . 1 374 . 51 GLN N N 117.0 . 1 375 . 51 GLN H H 7.60 . 1 376 . 51 GLN HA H 4.07 . 1 377 . 51 GLN HB2 H 1.86 . 2 378 . 51 GLN HB3 H 2.22 . 2 379 . 51 GLN HG2 H 2.47 . 1 380 . 51 GLN HG3 H 2.47 . 1 381 . 52 ARG N N 122.3 . 1 382 . 52 ARG H H 8.44 . 1 383 . 52 ARG CA C 57.3 . 1 384 . 52 ARG HA H 3.94 . 1 385 . 52 ARG HB2 H 2.02 . 1 386 . 52 ARG HB3 H 2.02 . 1 387 . 52 ARG HG2 H 1.66 . 1 388 . 52 ARG HG3 H 1.66 . 1 389 . 53 ALA N N 121.3 . 1 390 . 53 ALA H H 8.13 . 1 391 . 53 ALA CA C 55.3 . 1 392 . 53 ALA HA H 3.63 . 1 393 . 53 ALA HB H 1.49 . 1 394 . 53 ALA CB C 18.7 . 1 395 . 54 ALA N N 118.0 . 1 396 . 54 ALA H H 8.42 . 1 397 . 54 ALA CA C 54.7 . 1 398 . 54 ALA HA H 3.98 . 1 399 . 54 ALA HB H 1.34 . 1 400 . 54 ALA CB C 18.4 . 1 401 . 55 MET N N 117.6 . 1 402 . 55 MET H H 7.82 . 1 403 . 55 MET CA C 56.8 . 1 404 . 55 MET HA H 4.24 . 1 405 . 55 MET HB2 H 2.24 . 2 406 . 55 MET HB3 H 2.40 . 2 407 . 55 MET HE H 1.97 . 1 408 . 55 MET CE C 16.7 . 1 409 . 56 LEU N N 120.2 . 1 410 . 56 LEU H H 8.20 . 1 411 . 56 LEU CA C 57.7 . 1 412 . 56 LEU HA H 3.92 . 1 413 . 56 LEU HB2 H 1.95 . 1 414 . 56 LEU HB3 H 1.95 . 1 415 . 56 LEU HG H 1.40 . 1 416 . 56 LEU HD1 H 0.81 . 1 417 . 56 LEU HD2 H 0.81 . 1 418 . 57 ILE N N 117.6 . 1 419 . 57 ILE H H 8.11 . 1 420 . 57 ILE CA C 65.0 . 1 421 . 57 ILE HA H 3.14 . 1 422 . 57 ILE HB H 1.90 . 1 423 . 57 ILE HG2 H 0.68 . 1 424 . 57 ILE CG2 C 16.9 . 1 425 . 57 ILE HG12 H 0.97 . 2 426 . 57 ILE HG13 H 1.52 . 2 427 . 57 ILE HD1 H 0.74 . 1 428 . 57 ILE CD1 C 14.0 . 1 429 . 58 LYS N N 118.7 . 1 430 . 58 LYS H H 7.80 . 1 431 . 58 LYS CA C 60.0 . 1 432 . 58 LYS HA H 3.73 . 1 433 . 58 LYS HB2 H 1.90 . 1 434 . 58 LYS HB3 H 1.90 . 1 435 . 58 LYS HG2 H 1.26 . 1 436 . 58 LYS HG3 H 1.26 . 1 437 . 59 MET N N 116.3 . 1 438 . 59 MET H H 7.95 . 1 439 . 59 MET CA C 58.5 . 1 440 . 59 MET HA H 3.95 . 1 441 . 59 MET HB2 H 1.66 . 2 442 . 59 MET HB3 H 2.20 . 2 443 . 59 MET HG2 H 2.49 . 2 444 . 59 MET HG3 H 2.60 . 2 445 . 59 MET HE H 1.93 . 1 446 . 59 MET CE C 15.7 . 1 447 . 60 ILE N N 120.4 . 1 448 . 60 ILE H H 8.18 . 1 449 . 60 ILE CA C 65.0 . 1 450 . 60 ILE HA H 3.23 . 1 451 . 60 ILE HB H 1.48 . 1 452 . 60 ILE HG2 H 0.44 . 1 453 . 60 ILE CG2 C 16.8 . 1 454 . 60 ILE HG12 H 0.57 . 2 455 . 60 ILE HG13 H 0.56 . 2 456 . 60 ILE HD1 H -0.11 . 1 457 . 60 ILE CD1 C 12.7 . 1 458 . 61 LEU N N 117.6 . 1 459 . 61 LEU H H 8.02 . 1 460 . 61 LEU CA C 57.2 . 1 461 . 61 LEU HA H 3.77 . 1 462 . 61 LEU HB2 H 1.60 . 2 463 . 61 LEU HB3 H 1.87 . 2 464 . 61 LEU HG H 1.38 . 1 465 . 61 LEU HD1 H 0.41 . 2 466 . 61 LEU HD2 H 0.86 . 2 467 . 61 LEU CD1 C 17.5 . 1 468 . 61 LEU CD2 C 24.7 . 1 469 . 62 LYS N N 115.9 . 1 470 . 62 LYS H H 7.02 . 1 471 . 62 LYS CA C 55.7 . 1 472 . 62 LYS HA H 4.41 . 1 473 . 62 LYS HB2 H 1.77 . 2 474 . 62 LYS HB3 H 2.04 . 2 475 . 62 LYS HG2 H 1.40 . 2 476 . 62 LYS HG3 H 1.57 . 2 477 . 62 LYS HD2 H 1.60 . 1 478 . 62 LYS HD3 H 1.60 . 1 479 . 63 LYS N N 121.5 . 1 480 . 63 LYS H H 7.83 . 1 481 . 63 LYS CA C 55.7 . 1 482 . 63 LYS HA H 4.57 . 1 483 . 63 LYS HB2 H 1.97 . 2 484 . 63 LYS HB3 H 2.15 . 2 485 . 63 LYS HG2 H 1.39 . 1 486 . 63 LYS HG3 H 1.39 . 1 487 . 63 LYS HD2 H 1.73 . 2 488 . 63 LYS HD3 H 1.72 . 2 489 . 64 ASP N N 117.4 . 1 490 . 64 ASP H H 7.54 . 1 491 . 64 ASP CA C 52.2 . 1 492 . 64 ASP HA H 4.52 . 1 493 . 64 ASP HB2 H 2.69 . 2 494 . 64 ASP HB3 H 3.08 . 2 495 . 65 ASN N N 118.5 . 1 496 . 65 ASN H H 8.53 . 1 497 . 65 ASN CA C 55.7 . 1 498 . 65 ASN HA H 4.24 . 1 499 . 65 ASN HB2 H 2.55 . 2 500 . 65 ASN HB3 H 2.75 . 2 501 . 66 ASP N N 118.0 . 1 502 . 66 ASP H H 8.11 . 1 503 . 66 ASP CA C 57.0 . 1 504 . 66 ASP HA H 4.04 . 1 505 . 66 ASP HB2 H 2.14 . 2 506 . 66 ASP HB3 H 2.29 . 2 507 . 67 SER N N 117.6 . 1 508 . 67 SER H H 7.88 . 1 509 . 67 SER CA C 62.4 . 1 510 . 67 SER HA H 4.00 . 1 511 . 67 SER HB2 H 3.45 . 2 512 . 67 SER HB3 H 3.56 . 2 513 . 68 TYR N N 123.7 . 1 514 . 68 TYR H H 7.55 . 1 515 . 68 TYR CA C 61.9 . 1 516 . 68 TYR HA H 3.76 . 1 517 . 68 TYR HB2 H 2.78 . 2 518 . 68 TYR HB3 H 3.44 . 2 519 . 68 TYR HD1 H 6.70 . 1 520 . 68 TYR HD2 H 6.70 . 1 521 . 68 TYR HE1 H 6.57 . 1 522 . 68 TYR HE2 H 6.57 . 1 523 . 69 VAL N N 118.3 . 1 524 . 69 VAL H H 7.95 . 1 525 . 69 VAL CA C 67.0 . 1 526 . 69 VAL HA H 3.41 . 1 527 . 69 VAL HB H 2.08 . 1 528 . 69 VAL HG1 H 0.95 . 2 529 . 69 VAL HG2 H 1.06 . 2 530 . 69 VAL CG1 C 21.2 . 1 531 . 69 VAL CG2 C 23.4 . 1 532 . 70 SER N N 113.7 . 1 533 . 70 SER H H 7.66 . 1 534 . 70 SER CA C 61.5 . 1 535 . 70 SER HA H 4.27 . 1 536 . 70 SER HB2 H 3.83 . 2 537 . 70 SER HB3 H 4.02 . 2 538 . 71 PHE N N 120.9 . 1 539 . 71 PHE H H 8.17 . 1 540 . 71 PHE CA C 60.2 . 1 541 . 71 PHE HA H 4.38 . 1 542 . 71 PHE HB2 H 3.10 . 2 543 . 71 PHE HB3 H 3.09 . 2 544 . 71 PHE HD1 H 6.92 . 1 545 . 71 PHE HD2 H 6.92 . 1 546 . 71 PHE HE1 H 6.82 . 1 547 . 71 PHE HE2 H 6.82 . 1 548 . 71 PHE HZ H 6.73 . 1 549 . 72 TYR N N 119.8 . 1 550 . 72 TYR H H 8.43 . 1 551 . 72 TYR CA C 61.9 . 1 552 . 72 TYR HA H 3.46 . 1 553 . 72 TYR HB2 H 2.56 . 2 554 . 72 TYR HB3 H 3.17 . 2 555 . 72 TYR HD1 H 6.91 . 1 556 . 72 TYR HD2 H 6.91 . 1 557 . 72 TYR HE1 H 6.79 . 1 558 . 72 TYR HE2 H 6.79 . 1 559 . 73 ASN N N 116.7 . 1 560 . 73 ASN H H 8.85 . 1 561 . 73 ASN CA C 55.2 . 1 562 . 73 ASN HA H 4.00 . 1 563 . 73 ASN HB2 H 2.55 . 2 564 . 73 ASN HB3 H 2.95 . 2 565 . 74 ALA N N 124.8 . 1 566 . 74 ALA H H 8.39 . 1 567 . 74 ALA CA C 55.2 . 1 568 . 74 ALA HA H 3.56 . 1 569 . 74 ALA HB H 1.60 . 1 570 . 74 ALA CB C 19.5 . 1 571 . 75 LEU N N 117.2 . 1 572 . 75 LEU H H 7.96 . 1 573 . 75 LEU CA C 57.7 . 1 574 . 75 LEU HA H 3.69 . 1 575 . 75 LEU HB2 H 1.62 . 2 576 . 75 LEU HB3 H 1.72 . 2 577 . 75 LEU HG H 1.01 . 1 578 . 75 LEU HD1 H -0.06 . 2 579 . 75 LEU HD2 H 0.18 . 2 580 . 75 LEU CD1 C 26.0 . 1 581 . 75 LEU CD2 C 23.2 . 1 582 . 76 LEU N N 117.8 . 1 583 . 76 LEU H H 7.57 . 1 584 . 76 LEU CA C 57.6 . 1 585 . 76 LEU HA H 3.43 . 1 586 . 76 LEU HB2 H 1.24 . 1 587 . 76 LEU HB3 H 1.24 . 1 588 . 76 LEU HG H 1.15 . 1 589 . 76 LEU HD1 H 0.67 . 2 590 . 76 LEU HD2 H 0.51 . 2 591 . 76 LEU CD1 C 24.7 . 1 592 . 76 LEU CD2 C 24.0 . 1 593 . 77 HIS N N 118.9 . 1 594 . 77 HIS H H 8.39 . 1 595 . 77 HIS CA C 58.7 . 1 596 . 77 HIS HA H 4.06 . 1 597 . 77 HIS HB2 H 2.85 . 2 598 . 77 HIS HB3 H 2.93 . 2 599 . 77 HIS HD2 H 6.90 . 1 600 . 78 GLU N N 113.9 . 1 601 . 78 GLU H H 7.60 . 1 602 . 78 GLU CA C 54.7 . 1 603 . 78 GLU HA H 4.29 . 1 604 . 78 GLU HB2 H 2.41 . 2 605 . 78 GLU HB3 H 1.84 . 2 606 . 78 GLU HG2 H 2.40 . 2 607 . 78 GLU HG3 H 2.56 . 2 608 . 79 GLY N N 105.0 . 1 609 . 79 GLY H H 7.45 . 1 610 . 79 GLY CA C 45.5 . 1 611 . 79 GLY HA2 H 3.51 . 2 612 . 79 GLY HA3 H 3.88 . 2 613 . 80 TYR N N 122.8 . 1 614 . 80 TYR H H 8.32 . 1 615 . 80 TYR CA C 55.7 . 1 616 . 80 TYR HA H 4.73 . 1 617 . 80 TYR HB2 H 2.66 . 2 618 . 80 TYR HB3 H 2.94 . 2 619 . 80 TYR HD1 H 7.10 . 1 620 . 80 TYR HD2 H 7.10 . 1 621 . 80 TYR HE1 H 6.83 . 1 622 . 80 TYR HE2 H 6.83 . 1 623 . 81 LYS N N 120.7 . 1 624 . 81 LYS H H 7.70 . 1 625 . 81 LYS CA C 59.9 . 1 626 . 81 LYS HA H 3.56 . 1 627 . 81 LYS HB2 H 1.68 . 1 628 . 81 LYS HB3 H 1.68 . 1 629 . 81 LYS HG2 H 1.22 . 2 630 . 81 LYS HG3 H 1.26 . 2 631 . 81 LYS HD2 H 1.53 . 1 632 . 81 LYS HD3 H 1.53 . 1 633 . 82 ASP N N 118.9 . 1 634 . 82 ASP H H 8.41 . 1 635 . 82 ASP CA C 56.7 . 1 636 . 82 ASP HA H 4.29 . 1 637 . 82 ASP HB2 H 2.59 . 1 638 . 82 ASP HB3 H 2.59 . 1 639 . 83 LEU N N 119.6 . 1 640 . 83 LEU H H 7.68 . 1 641 . 83 LEU CA C 56.7 . 1 642 . 83 LEU HA H 3.95 . 1 643 . 83 LEU HB2 H 1.63 . 2 644 . 83 LEU HB3 H 1.74 . 2 645 . 83 LEU HG H 1.12 . 1 646 . 83 LEU HD1 H 0.76 . 2 647 . 83 LEU HD2 H 0.66 . 2 648 . 83 LEU CD1 C 26.5 . 1 649 . 83 LEU CD2 C 21.7 . 1 650 . 84 ALA N N 119.6 . 1 651 . 84 ALA H H 8.18 . 1 652 . 84 ALA CA C 55.1 . 1 653 . 84 ALA HA H 3.67 . 1 654 . 84 ALA HB H 0.98 . 1 655 . 84 ALA CB C 17.0 . 1 656 . 85 ALA N N 117.8 . 1 657 . 85 ALA H H 7.57 . 1 658 . 85 ALA CA C 54.7 . 1 659 . 85 ALA HA H 4.11 . 1 660 . 85 ALA HB H 1.40 . 1 661 . 85 ALA CB C 17.5 . 1 662 . 86 LEU N N 116.7 . 1 663 . 86 LEU H H 7.17 . 1 664 . 86 LEU CA C 56.7 . 1 665 . 86 LEU HA H 3.79 . 1 666 . 86 LEU HB2 H 1.68 . 2 667 . 86 LEU HB3 H 1.76 . 2 668 . 86 LEU HG H 0.12 . 1 669 . 86 LEU HD1 H 0.59 . 2 670 . 86 LEU HD2 H 0.48 . 2 671 . 86 LEU CD1 C 24.7 . 1 672 . 86 LEU CD2 C 20.7 . 1 673 . 87 LEU N N 114.1 . 1 674 . 87 LEU H H 7.29 . 1 675 . 87 LEU CA C 54.7 . 1 676 . 87 LEU HA H 4.63 . 1 677 . 87 LEU HB2 H 1.86 . 1 678 . 87 LEU HB3 H 1.86 . 1 679 . 87 LEU HG H 1.60 . 1 680 . 87 LEU HD1 H 0.63 . 2 681 . 87 LEU HD2 H 0.79 . 2 682 . 87 LEU CD1 C 25.7 . 1 683 . 87 LEU CD2 C 22.5 . 1 684 . 88 HIS N N 122.4 . 1 685 . 88 HIS H H 8.12 . 1 686 . 88 HIS CA C 60.0 . 1 687 . 88 HIS HA H 3.69 . 1 688 . 88 HIS HB2 H 3.17 . 2 689 . 88 HIS HB3 H 3.42 . 2 690 . 88 HIS HD2 H 6.99 . 1 691 . 89 ASP N N 116.7 . 1 692 . 89 ASP H H 8.28 . 1 693 . 89 ASP CA C 56.5 . 1 694 . 89 ASP HA H 4.28 . 1 695 . 89 ASP HB2 H 2.59 . 1 696 . 89 ASP HB3 H 2.59 . 1 697 . 90 GLY N N 104.6 . 1 698 . 90 GLY H H 7.47 . 1 699 . 90 GLY CA C 44.2 . 1 700 . 90 GLY HA2 H 3.42 . 2 701 . 90 GLY HA3 H 3.78 . 2 702 . 91 ILE N N 120.0 . 1 703 . 91 ILE H H 6.89 . 1 704 . 91 ILE CA C 59.0 . 1 705 . 91 ILE HA H 3.72 . 1 706 . 91 ILE HB H 1.43 . 1 707 . 91 ILE HG2 H 0.60 . 1 708 . 91 ILE CG2 C 15.3 . 1 709 . 91 ILE CG1 C 28.2 . 1 710 . 91 ILE HG12 H 0.74 . 2 711 . 91 ILE HG13 H 1.16 . 2 712 . 91 ILE HD1 H 0.04 . 1 713 . 91 ILE CD1 C 12.0 . 1 714 . 92 PRO HG2 H 2.53 . 1 715 . 92 PRO HG3 H 2.53 . 1 716 . 92 PRO HD2 H 3.25 . 1 717 . 92 PRO HD3 H 3.25 . 1 718 . 93 VAL N N 120.9 . 1 719 . 93 VAL H H 8.07 . 1 720 . 93 VAL CA C 62.0 . 1 721 . 93 VAL HA H 3.94 . 1 722 . 93 VAL HB H 1.91 . 1 723 . 93 VAL HG1 H 0.80 . 1 724 . 93 VAL HG2 H 0.80 . 1 725 . 94 VAL N N 124.1 . 1 726 . 94 VAL H H 8.16 . 1 727 . 94 VAL CA C 61.7 . 1 728 . 94 VAL HA H 4.09 . 1 729 . 94 VAL HB H 2.00 . 1 730 . 94 VAL HG1 H 0.82 . 1 731 . 94 VAL HG2 H 0.82 . 1 732 . 95 SER N N 119.8 . 1 733 . 95 SER H H 8.42 . 1 734 . 95 SER CA C 57.5 . 1 735 . 95 SER HA H 4.44 . 1 736 . 95 SER HB2 H 3.78 . 1 737 . 95 SER HB3 H 3.78 . 1 738 . 96 SER N N 122.8 . 1 739 . 96 SER H H 7.97 . 1 740 . 96 SER HA H 4.19 . 1 741 . 96 SER HB2 H 3.79 . 1 742 . 96 SER HB3 H 3.79 . 1 stop_ save_