data_5011 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Anabaena apoflavodoxin hydrogen exchange: on the stable exchange core of the alfa/beta(21345) flavodoxin-like family ; _BMRB_accession_number 5011 _BMRB_flat_file_name bmr5011.str _Entry_type original _Submission_date 2001-05-11 _Accession_date 2001-05-11 _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 Langdon Grant M. . 2 Jimenez 'M. Angeles' . . 3 Genzor Carlos G. . 4 Maldonado Susana . . 5 Sancho Javier . . 6 Rico Manuel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 715 "13C chemical shifts" 23 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-06-14 original author . stop_ _Original_release_date 2001-06-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Anabaena apoflavodoxin hydrogen exchange: on the stable exchange core of the alfa/beta(21345) flavodoxin-like family ; _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 Langdon Grant M. . 2 Jimenez 'M. Angeles' . . 3 Genzor Carlos G. . 4 Maldonado Susana . . 5 Sancho Javier . . 6 Rico Manuel . . stop_ _Journal_abbreviation 'Proteins: Struct. Funct. Genet.' _Journal_volume 43 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 476 _Page_last 488 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_apofld _Saveframe_category molecular_system _Mol_system_name 'Anabaena PCC 7119 apoflavodoxin' _Abbreviation_common apofld _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'apofld monomer' $apofld stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_apofld _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Anabaena apoflavodoxin' _Abbreviation_common apofld _Molecular_mass 18886 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 169 _Mol_residue_sequence ; AKKIGLFYGTQTGKTESVAE IIRDEFGNDVVTLHDVSQAE VTDLNDYQYLIIGCPTWNIG ELQSDWEGLYSELDDVDFNG KLVAYFGTGDQIGYADNFQD AIGILEEKISQRGGKTVGYW STDGYDFNDSKALRNGKFVG LALDEDNQSDLTDDRIKSWV AQLKSEFGL ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LYS 3 LYS 4 ILE 5 GLY 6 LEU 7 PHE 8 TYR 9 GLY 10 THR 11 GLN 12 THR 13 GLY 14 LYS 15 THR 16 GLU 17 SER 18 VAL 19 ALA 20 GLU 21 ILE 22 ILE 23 ARG 24 ASP 25 GLU 26 PHE 27 GLY 28 ASN 29 ASP 30 VAL 31 VAL 32 THR 33 LEU 34 HIS 35 ASP 36 VAL 37 SER 38 GLN 39 ALA 40 GLU 41 VAL 42 THR 43 ASP 44 LEU 45 ASN 46 ASP 47 TYR 48 GLN 49 TYR 50 LEU 51 ILE 52 ILE 53 GLY 54 CYS 55 PRO 56 THR 57 TRP 58 ASN 59 ILE 60 GLY 61 GLU 62 LEU 63 GLN 64 SER 65 ASP 66 TRP 67 GLU 68 GLY 69 LEU 70 TYR 71 SER 72 GLU 73 LEU 74 ASP 75 ASP 76 VAL 77 ASP 78 PHE 79 ASN 80 GLY 81 LYS 82 LEU 83 VAL 84 ALA 85 TYR 86 PHE 87 GLY 88 THR 89 GLY 90 ASP 91 GLN 92 ILE 93 GLY 94 TYR 95 ALA 96 ASP 97 ASN 98 PHE 99 GLN 100 ASP 101 ALA 102 ILE 103 GLY 104 ILE 105 LEU 106 GLU 107 GLU 108 LYS 109 ILE 110 SER 111 GLN 112 ARG 113 GLY 114 GLY 115 LYS 116 THR 117 VAL 118 GLY 119 TYR 120 TRP 121 SER 122 THR 123 ASP 124 GLY 125 TYR 126 ASP 127 PHE 128 ASN 129 ASP 130 SER 131 LYS 132 ALA 133 LEU 134 ARG 135 ASN 136 GLY 137 LYS 138 PHE 139 VAL 140 GLY 141 LEU 142 ALA 143 LEU 144 ASP 145 GLU 146 ASP 147 ASN 148 GLN 149 SER 150 ASP 151 LEU 152 THR 153 ASP 154 ASP 155 ARG 156 ILE 157 LYS 158 SER 159 TRP 160 VAL 161 ALA 162 GLN 163 LEU 164 LYS 165 SER 166 GLU 167 PHE 168 GLY 169 LEU 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 1580 flavodoxin 100.00 169 99.41 100.00 1.07e-115 BMRB 16593 F98N-fdx 100.00 169 100.00 100.00 3.24e-116 PDB 1DX9 "W57a Apoflavodoxin From Anabaena" 100.00 169 98.82 99.41 1.81e-114 PDB 1FLV "Structure Of The Oxidized Long Chain Flavodoxin From Anabaena 7120 At 2 Angstroms Resolution" 100.00 169 99.41 100.00 1.07e-115 PDB 1FTG "Structure Of Apoflavodoxin: Closure Of A TyrosineTRYPTOPHAN AROMATIC Gate Leads To A Compact Fold" 99.41 168 100.00 100.00 1.68e-115 PDB 1OBO "W57l Flavodoxin From Anabaena" 100.00 169 99.41 99.41 4.92e-115 PDB 1OBV "Y94f Flavodoxin From Anabaena" 100.00 169 99.41 100.00 8.75e-116 PDB 1QHE "Energetics Of A Hydrogen Bond (Charged And Neutral) And Of A Cation-Pi Interaction In Apoflavodoxin" 99.41 168 100.00 100.00 1.68e-115 PDB 1RCF "Structure Of The Trigonal Form Of Recombinant Oxidized Flavodoxin From Anabaena 7120 At 1.40 Angstroms Resolution" 100.00 169 99.41 100.00 1.07e-115 PDB 2KQU "F98n Apoflavodoxin From Anabaena Pcc 7119" 100.00 169 99.41 99.41 5.80e-115 PDB 2V5U "I92a Flavodoxin From Anabaena" 100.00 169 99.41 99.41 1.74e-115 PDB 2V5V "W57e Flavodoxin From Anabaena" 100.00 169 99.41 99.41 9.69e-115 PDB 3ESX "E16ke61kd126kd150k Flavodoxin From Anabaena" 100.00 169 97.04 98.82 4.96e-113 PDB 3ESY "E16ke61k Flavodoxin From Anabaena" 100.00 169 98.22 100.00 1.25e-114 PDB 3ESZ "K2ak3a Flavodoxin From Anabaena" 100.00 169 98.22 98.82 3.72e-114 DBJ BAB74104 "flavodoxin [Nostoc sp. PCC 7120]" 100.00 170 99.41 100.00 4.55e-116 EMBL CAA32720 "flavodoxin ORF [Nostoc sp. PCC 7120]" 100.00 170 99.41 100.00 4.55e-116 GB AAB20462 "flavodoxin [Anabaena]" 100.00 170 99.41 100.00 4.55e-116 PIR S04600 "flavodoxin - Anabaena variabilis" 100.00 170 99.41 100.00 4.55e-116 PIR S18374 "flavodoxin - Anabaena sp. (PCC 7119) (fragment)" 99.41 168 100.00 100.00 1.68e-115 REF NP_486445 "flavodoxin FldA [Nostoc sp. PCC 7120]" 100.00 170 99.41 100.00 4.55e-116 REF WP_010996561 "flavodoxin [Nostoc sp. PCC 7120]" 100.00 170 99.41 100.00 4.55e-116 SP P0A3D9 "RecName: Full=Flavodoxin [Nostoc sp. PCC 7120]" 100.00 170 99.41 100.00 4.55e-116 SP P0A3E0 "RecName: Full=Flavodoxin [Nostoc sp. PCC 7119]" 100.00 170 99.41 100.00 4.55e-116 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $apofld 'Anabaena PCC7119' 1168 Eubacteria . Anabaena PCC7119 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 $apofld 'recombinant technology' 'E. coli' Escherichia coli TG1 plasmid ptrc99a 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 _Isotopic_labeling $apofld 2.0 mM . 'sodium phosphate' 50 mM . dithiothreitol 2 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apofld 2.0 mM [U-15N] 'sodium phosphate' 50 mM . dithiothreitol 2 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apofld 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label . save_ save_2D_1H-1H_CLEAN-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H CLEAN-TOCSY' _Sample_label . save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H CLEAN-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 298 0.1 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 TSP H 1 'methyl protons' ppm 0.00 internal direct . internal . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H COSY' '2D 1H-1H CLEAN-TOCSY' '2D 1H-1H NOESY' '2D 1H-15N HSQC' '3D 1H-1H-15N TOCSY' '3D 1H-1H-15N NOESY' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'apofld monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 LYS HA H 4.41 . 1 2 . 3 LYS N N 119.8 . 1 3 . 3 LYS H H 8.00 . 1 4 . 3 LYS HA H 4.80 . 1 5 . 3 LYS HB2 H 1.92 . 1 6 . 3 LYS HB3 H 1.92 . 1 7 . 3 LYS HG3 H 1.56 . 2 8 . 4 ILE N N 120.7 . 1 9 . 4 ILE H H 8.51 . 1 10 . 4 ILE HA H 4.57 . 1 11 . 4 ILE HB H 1.21 . 1 12 . 4 ILE HG2 H 0.29 . 1 13 . 4 ILE HG12 H 1.02 . 2 14 . 4 ILE HG13 H 0.18 . 2 15 . 4 ILE HD1 H -0.19 . 1 16 . 5 GLY N N 117.6 . 1 17 . 5 GLY H H 8.11 . 1 18 . 5 GLY HA2 H 3.98 . 2 19 . 5 GLY HA3 H 1.84 . 2 20 . 6 LEU N N 130.8 . 1 21 . 6 LEU H H 8.80 . 1 22 . 6 LEU HA H 5.83 . 1 23 . 6 LEU HB2 H 1.88 . 1 24 . 6 LEU HB3 H 1.88 . 1 25 . 6 LEU HD1 H 1.12 . 2 26 . 6 LEU HD2 H 0.89 . 2 27 . 7 PHE N N 128.4 . 1 28 . 7 PHE H H 9.49 . 1 29 . 7 PHE HA H 5.52 . 1 30 . 7 PHE HB2 H 3.14 . 2 31 . 7 PHE HB3 H 2.69 . 2 32 . 7 PHE CD1 C 130.9 . 1 33 . 7 PHE HD1 H 6.85 . 1 34 . 7 PHE CD2 C 130.9 . 1 35 . 7 PHE HD2 H 6.85 . 1 36 . 8 TYR N N 121.0 . 1 37 . 8 TYR H H 8.78 . 1 38 . 8 TYR HA H 6.69 . 1 39 . 17 SER HA H 4.22 . 1 40 . 17 SER HB2 H 3.98 . 1 41 . 17 SER HB3 H 3.98 . 1 42 . 18 VAL N N 121.1 . 1 43 . 18 VAL H H 7.92 . 1 44 . 18 VAL HA H 3.42 . 1 45 . 18 VAL HB H 2.03 . 1 46 . 18 VAL HG1 H 0.87 . 2 47 . 18 VAL HG2 H 0.38 . 2 48 . 19 ALA N N 122.1 . 1 49 . 19 ALA H H 8.16 . 1 50 . 19 ALA HA H 3.62 . 1 51 . 19 ALA HB H 1.07 . 1 52 . 20 GLU N N 116.3 . 1 53 . 20 GLU H H 7.71 . 1 54 . 20 GLU HA H 3.65 . 1 55 . 20 GLU HB2 H 2.18 . 2 56 . 20 GLU HB3 H 1.97 . 2 57 . 20 GLU HG2 H 2.43 . 2 58 . 20 GLU HG3 H 2.38 . 2 59 . 21 ILE N N 120.7 . 1 60 . 21 ILE H H 7.50 . 1 61 . 21 ILE HA H 3.77 . 1 62 . 21 ILE HB H 1.90 . 1 63 . 21 ILE HG2 H 0.93 . 1 64 . 21 ILE HG12 H 1.82 . 2 65 . 21 ILE HG13 H 1.04 . 2 66 . 21 ILE HD1 H 0.76 . 1 67 . 22 ILE N N 120.3 . 1 68 . 22 ILE H H 8.30 . 1 69 . 22 ILE HA H 3.25 . 1 70 . 22 ILE HB H 1.73 . 1 71 . 22 ILE HG2 H 0.90 . 1 72 . 22 ILE HG12 H 0.90 . 2 73 . 22 ILE HG13 H 0.54 . 2 74 . 22 ILE HD1 H -0.01 . 1 75 . 23 ARG N N 119.2 . 1 76 . 23 ARG H H 8.31 . 1 77 . 23 ARG HA H 3.71 . 1 78 . 23 ARG HB2 H 2.37 . 2 79 . 24 ASP N N 120.3 . 1 80 . 24 ASP H H 8.25 . 1 81 . 24 ASP HA H 4.43 . 1 82 . 24 ASP HB2 H 2.86 . 2 83 . 24 ASP HB3 H 2.71 . 2 84 . 25 GLU N N 121.0 . 1 85 . 25 GLU H H 8.51 . 1 86 . 25 GLU HA H 4.01 . 1 87 . 25 GLU HB2 H 2.01 . 2 88 . 25 GLU HB3 H 1.91 . 2 89 . 25 GLU HG2 H 2.24 . 1 90 . 25 GLU HG3 H 2.24 . 1 91 . 26 PHE N N 117.4 . 1 92 . 26 PHE H H 8.01 . 1 93 . 26 PHE HA H 4.00 . 1 94 . 26 PHE HB2 H 2.98 . 1 95 . 26 PHE HB3 H 2.98 . 1 96 . 26 PHE CD1 C 132.2 . 1 97 . 26 PHE HD1 H 7.20 . 1 98 . 26 PHE CD2 C 132.2 . 1 99 . 26 PHE HD2 H 7.20 . 1 100 . 26 PHE HE1 H 6.79 . 1 101 . 26 PHE HE2 H 6.79 . 1 102 . 27 GLY N N 105.8 . 1 103 . 27 GLY H H 7.97 . 1 104 . 27 GLY HA2 H 4.37 . 2 105 . 27 GLY HA3 H 3.84 . 2 106 . 28 ASN N N 118.7 . 1 107 . 28 ASN H H 8.91 . 1 108 . 28 ASN HA H 4.36 . 1 109 . 28 ASN HB2 H 2.86 . 1 110 . 28 ASN HB3 H 2.86 . 1 111 . 28 ASN ND2 N 113.5 . 1 112 . 28 ASN HD21 H 7.68 . 2 113 . 28 ASN HD22 H 6.98 . 2 114 . 29 ASP N N 116.0 . 1 115 . 29 ASP H H 8.87 . 1 116 . 29 ASP HA H 4.51 . 1 117 . 29 ASP HB2 H 2.86 . 2 118 . 29 ASP HB3 H 2.68 . 2 119 . 30 VAL N N 118.2 . 1 120 . 30 VAL H H 7.64 . 1 121 . 30 VAL HA H 4.03 . 1 122 . 30 VAL HB H 2.04 . 1 123 . 30 VAL HG1 H 1.02 . 2 124 . 30 VAL HG2 H 0.84 . 2 125 . 31 VAL N N 119.4 . 1 126 . 31 VAL H H 7.88 . 1 127 . 31 VAL HA H 4.74 . 1 128 . 31 VAL HB H 1.81 . 1 129 . 31 VAL HG1 H 0.66 . 2 130 . 31 VAL HG2 H 0.53 . 2 131 . 32 THR N N 123.7 . 1 132 . 32 THR H H 8.50 . 1 133 . 32 THR HA H 4.38 . 1 134 . 32 THR HB H 4.08 . 1 135 . 32 THR HG2 H 0.93 . 1 136 . 33 LEU N N 127.0 . 1 137 . 33 LEU H H 8.63 . 1 138 . 33 LEU HA H 4.73 . 1 139 . 33 LEU HB2 H 1.84 . 2 140 . 33 LEU HB3 H 1.63 . 2 141 . 33 LEU HG H 1.61 . 1 142 . 33 LEU HD1 H 0.87 . 2 143 . 33 LEU HD2 H 0.81 . 2 144 . 34 HIS N N 120.9 . 1 145 . 34 HIS H H 9.21 . 1 146 . 34 HIS HA H 4.26 . 1 147 . 34 HIS HD2 H 7.82 . 1 148 . 34 HIS CD2 C 136.6 . 1 149 . 34 HIS HE1 H 5.81 . 1 150 . 34 HIS CE1 C 125.3 . 1 151 . 35 ASP N N 125.2 . 1 152 . 35 ASP H H 8.24 . 1 153 . 35 ASP HA H 3.61 . 1 154 . 35 ASP HB2 H 2.57 . 2 155 . 35 ASP HB3 H 2.42 . 2 156 . 36 VAL N N 124.6 . 1 157 . 36 VAL H H 8.27 . 1 158 . 36 VAL HA H 4.26 . 1 159 . 36 VAL HB H 2.12 . 1 160 . 36 VAL HG1 H 0.73 . 1 161 . 36 VAL HG2 H 0.73 . 1 162 . 37 SER N N 117.6 . 1 163 . 37 SER H H 8.86 . 1 164 . 37 SER HA H 4.13 . 1 165 . 37 SER HB2 H 3.93 . 2 166 . 37 SER HB3 H 3.84 . 2 167 . 38 GLN N N 119.2 . 1 168 . 38 GLN H H 7.71 . 1 169 . 38 GLN HA H 4.56 . 1 170 . 38 GLN HB2 H 1.86 . 1 171 . 38 GLN HB3 H 1.86 . 1 172 . 38 GLN HG2 H 2.31 . 1 173 . 38 GLN HG3 H 2.31 . 1 174 . 38 GLN NE2 N 112.7 . 1 175 . 38 GLN HE21 H 7.43 . 2 176 . 38 GLN HE22 H 6.78 . 2 177 . 39 ALA N N 121.8 . 1 178 . 39 ALA H H 7.20 . 1 179 . 39 ALA HA H 4.59 . 1 180 . 39 ALA HB H 1.36 . 1 181 . 40 GLU N N 118.3 . 1 182 . 40 GLU H H 8.26 . 1 183 . 40 GLU HA H 4.59 . 1 184 . 40 GLU HB2 H 2.06 . 2 185 . 40 GLU HB3 H 1.74 . 2 186 . 40 GLU HG2 H 2.25 . 1 187 . 40 GLU HG3 H 2.25 . 1 188 . 41 VAL N N 122.4 . 1 189 . 41 VAL H H 9.35 . 1 190 . 41 VAL HA H 3.63 . 1 191 . 41 VAL HB H 2.08 . 1 192 . 41 VAL HG1 H 0.94 . 1 193 . 41 VAL HG2 H 0.94 . 1 194 . 42 THR N N 106.8 . 1 195 . 42 THR H H 7.10 . 1 196 . 42 THR HA H 3.83 . 1 197 . 42 THR HG2 H 1.20 . 1 198 . 43 ASP N N 124.3 . 1 199 . 43 ASP H H 8.21 . 1 200 . 43 ASP HA H 4.45 . 1 201 . 43 ASP HB2 H 2.98 . 2 202 . 43 ASP HB3 H 2.74 . 2 203 . 44 LEU N N 124.3 . 1 204 . 44 LEU H H 8.21 . 1 205 . 44 LEU HA H 4.33 . 1 206 . 45 ASN N N 111.5 . 1 207 . 45 ASN H H 7.26 . 1 208 . 45 ASN HA H 4.15 . 1 209 . 45 ASN HB2 H 2.79 . 2 210 . 45 ASN HB3 H 1.20 . 2 211 . 45 ASN ND2 N 112.9 . 1 212 . 45 ASN HD21 H 7.64 . 2 213 . 45 ASN HD22 H 7.11 . 2 214 . 46 ASP N N 116.6 . 1 215 . 46 ASP H H 7.31 . 1 216 . 46 ASP HA H 4.31 . 1 217 . 46 ASP HB2 H 2.36 . 2 218 . 46 ASP HB3 H 2.26 . 2 219 . 47 TYR N N 115.3 . 1 220 . 47 TYR H H 6.85 . 1 221 . 47 TYR HA H 4.68 . 1 222 . 47 TYR HB2 H 3.31 . 2 223 . 47 TYR HB3 H 2.56 . 2 224 . 47 TYR HD1 H 7.00 . 1 225 . 47 TYR HD2 H 7.00 . 1 226 . 48 GLN N N 120.5 . 1 227 . 48 GLN H H 9.51 . 1 228 . 48 GLN HA H 4.22 . 1 229 . 48 GLN HB2 H 1.70 . 2 230 . 48 GLN HB3 H 1.64 . 2 231 . 48 GLN HG2 H 2.14 . 1 232 . 48 GLN HG3 H 2.14 . 1 233 . 48 GLN NE2 N 111.4 . 1 234 . 48 GLN HE21 H 7.26 . 2 235 . 48 GLN HE22 H 6.84 . 2 236 . 49 TYR N N 117.4 . 1 237 . 49 TYR H H 6.92 . 1 238 . 49 TYR HA H 5.30 . 1 239 . 49 TYR HB2 H 2.71 . 2 240 . 50 LEU N N 123.8 . 1 241 . 50 LEU H H 9.00 . 1 242 . 50 LEU HA H 5.57 . 1 243 . 50 LEU HB2 H 1.89 . 2 244 . 50 LEU HB3 H 1.31 . 2 245 . 50 LEU HG H 1.57 . 1 246 . 50 LEU HD1 H 1.08 . 2 247 . 50 LEU HD2 H 0.97 . 2 248 . 51 ILE N N 118.7 . 1 249 . 51 ILE H H 8.94 . 1 250 . 51 ILE HA H 4.88 . 1 251 . 51 ILE HB H 1.48 . 1 252 . 51 ILE HG2 H 0.72 . 1 253 . 51 ILE HD1 H 0.27 . 1 254 . 52 ILE N N 131.1 . 1 255 . 52 ILE H H 9.60 . 1 256 . 52 ILE HA H 4.99 . 1 257 . 52 ILE HB H 1.84 . 1 258 . 53 GLY N N 111.8 . 1 259 . 53 GLY H H 9.27 . 1 260 . 57 TRP HE3 H 7.67 . 1 261 . 57 TRP CE3 C 121.2 . 1 262 . 57 TRP HZ3 H 7.25 . 1 263 . 57 TRP CZ3 C 124.7 . 1 264 . 57 TRP HZ2 H 7.57 . 1 265 . 57 TRP CZ2 C 115.0 . 1 266 . 57 TRP HH2 H 7.17 . 1 267 . 57 TRP CH2 C 122.0 . 1 268 . 66 TRP HE3 H 7.82 . 1 269 . 66 TRP HZ3 H 6.93 . 1 270 . 66 TRP CZ3 C 123.3 . 1 271 . 66 TRP HZ2 H 7.49 . 1 272 . 66 TRP CZ2 C 115.8 . 1 273 . 66 TRP HH2 H 6.84 . 1 274 . 66 TRP CH2 C 120.8 . 1 275 . 70 TYR H H 8.69 . 1 276 . 70 TYR HB2 H 3.26 . 2 277 . 70 TYR HB3 H 3.18 . 2 278 . 70 TYR HD1 H 7.00 . 1 279 . 70 TYR HD2 H 7.00 . 1 280 . 71 SER N N 112.2 . 1 281 . 71 SER H H 8.04 . 1 282 . 71 SER HA H 4.21 . 1 283 . 71 SER HB2 H 4.08 . 1 284 . 71 SER HB3 H 4.08 . 1 285 . 72 GLU N N 120.2 . 1 286 . 72 GLU H H 7.83 . 1 287 . 72 GLU HA H 4.48 . 1 288 . 72 GLU HB2 H 2.24 . 2 289 . 72 GLU HB3 H 1.99 . 2 290 . 72 GLU HG2 H 2.39 . 1 291 . 72 GLU HG3 H 2.39 . 1 292 . 73 LEU N N 117.9 . 1 293 . 73 LEU H H 7.44 . 1 294 . 73 LEU HA H 3.99 . 1 295 . 73 LEU HB2 H 1.71 . 2 296 . 73 LEU HB3 H 1.34 . 2 297 . 73 LEU HG H 2.22 . 1 298 . 73 LEU HD1 H 0.87 . 1 299 . 73 LEU HD2 H 0.87 . 1 300 . 74 ASP N N 115.1 . 1 301 . 74 ASP H H 7.71 . 1 302 . 74 ASP HA H 4.33 . 1 303 . 74 ASP HB2 H 2.66 . 2 304 . 74 ASP HB3 H 2.54 . 2 305 . 75 ASP N N 116.3 . 1 306 . 75 ASP H H 7.75 . 1 307 . 75 ASP HA H 4.70 . 1 308 . 75 ASP HB2 H 2.79 . 2 309 . 75 ASP HB3 H 2.68 . 2 310 . 76 VAL N N 120.5 . 1 311 . 76 VAL H H 7.55 . 1 312 . 76 VAL HA H 4.00 . 1 313 . 76 VAL HB H 1.83 . 1 314 . 76 VAL HG1 H 0.68 . 2 315 . 76 VAL HG2 H -0.04 . 2 316 . 77 ASP N N 126.1 . 1 317 . 77 ASP H H 8.64 . 1 318 . 77 ASP HA H 4.90 . 1 319 . 77 ASP HB2 H 2.86 . 2 320 . 77 ASP HB3 H 2.56 . 2 321 . 78 PHE N N 123.1 . 1 322 . 78 PHE H H 8.32 . 1 323 . 78 PHE HA H 4.20 . 1 324 . 78 PHE HB2 H 3.01 . 2 325 . 78 PHE HB3 H 2.54 . 2 326 . 78 PHE HD1 H 7.02 . 1 327 . 78 PHE HD2 H 7.02 . 1 328 . 79 ASN N N 119.6 . 1 329 . 79 ASN H H 8.64 . 1 330 . 79 ASN HA H 4.46 . 1 331 . 79 ASN HB2 H 3.06 . 2 332 . 79 ASN HB3 H 2.64 . 2 333 . 79 ASN ND2 N 116.5 . 1 334 . 79 ASN HD21 H 8.52 . 2 335 . 79 ASN HD22 H 7.02 . 2 336 . 80 GLY N N 113.3 . 1 337 . 80 GLY H H 8.64 . 1 338 . 80 GLY HA2 H 4.28 . 2 339 . 80 GLY HA3 H 3.71 . 2 340 . 81 LYS N N 119.1 . 1 341 . 81 LYS H H 8.11 . 1 342 . 81 LYS HA H 4.90 . 1 343 . 81 LYS HB2 H 1.97 . 2 344 . 81 LYS HB3 H 1.47 . 2 345 . 81 LYS HG2 H 1.28 . 1 346 . 81 LYS HG3 H 1.28 . 1 347 . 82 LEU N N 124.4 . 1 348 . 82 LEU H H 8.08 . 1 349 . 82 LEU HA H 5.55 . 1 350 . 82 LEU HB2 H 2.18 . 2 351 . 82 LEU HB3 H 1.75 . 2 352 . 82 LEU HG H 2.05 . 1 353 . 82 LEU HD1 H 1.30 . 2 354 . 82 LEU HD2 H 1.10 . 2 355 . 83 VAL N N 123.5 . 1 356 . 83 VAL H H 8.92 . 1 357 . 83 VAL HA H 5.01 . 1 358 . 83 VAL HB H 1.88 . 1 359 . 83 VAL HG1 H 0.71 . 2 360 . 83 VAL HG2 H 0.54 . 2 361 . 84 ALA N N 129.3 . 1 362 . 84 ALA H H 8.76 . 1 363 . 84 ALA HA H 5.58 . 1 364 . 84 ALA HB H 1.45 . 1 365 . 85 TYR N N 118.7 . 1 366 . 85 TYR H H 10.72 . 1 367 . 85 TYR HA H 5.70 . 1 368 . 85 TYR HB2 H 2.51 . 2 369 . 85 TYR HB3 H 2.28 . 2 370 . 86 PHE N N 114.0 . 1 371 . 86 PHE H H 9.16 . 1 372 . 86 PHE HA H 5.12 . 1 373 . 86 PHE HB2 H 2.51 . 2 374 . 86 PHE HB3 H 2.28 . 2 375 . 86 PHE HD1 H 6.73 . 1 376 . 86 PHE HD2 H 6.73 . 1 377 . 87 GLY N N 104.3 . 1 378 . 87 GLY H H 7.92 . 1 379 . 87 GLY HA2 H 4.29 . 2 380 . 87 GLY HA3 H 3.64 . 2 381 . 88 THR N N 119.6 . 1 382 . 88 THR H H 8.16 . 1 383 . 88 THR HA H 5.20 . 1 384 . 88 THR HB H 3.68 . 1 385 . 88 THR HG2 H 1.16 . 1 386 . 89 GLY N N 109.8 . 1 387 . 89 GLY H H 8.24 . 1 388 . 89 GLY HA2 H 4.30 . 2 389 . 89 GLY HA3 H 3.77 . 2 390 . 90 ASP N N 119.4 . 1 391 . 90 ASP H H 8.18 . 1 392 . 90 ASP HA H 5.17 . 1 393 . 90 ASP HB2 H 3.13 . 2 394 . 90 ASP HB3 H 3.02 . 2 395 . 91 GLN N N 123.3 . 1 396 . 91 GLN H H 8.71 . 1 397 . 91 GLN HA H 3.59 . 1 398 . 91 GLN HB2 H 2.31 . 2 399 . 91 GLN HB3 H 2.15 . 2 400 . 91 GLN HG2 H 2.88 . 1 401 . 91 GLN HG3 H 2.88 . 1 402 . 91 GLN NE2 N 109.4 . 1 403 . 91 GLN HE21 H 9.24 . 2 404 . 91 GLN HE22 H 6.34 . 2 405 . 92 ILE N N 117.3 . 1 406 . 92 ILE H H 7.48 . 1 407 . 92 ILE HA H 4.10 . 1 408 . 92 ILE HB H 1.97 . 1 409 . 92 ILE HG2 H 0.87 . 1 410 . 92 ILE HG12 H 1.46 . 2 411 . 92 ILE HG13 H 1.26 . 2 412 . 92 ILE HD1 H 0.79 . 1 413 . 93 GLY N N 109.2 . 1 414 . 93 GLY H H 8.87 . 1 415 . 93 GLY HA2 H 3.77 . 2 416 . 93 GLY HA3 H 3.56 . 2 417 . 94 TYR N N 119.9 . 1 418 . 94 TYR H H 7.56 . 1 419 . 94 TYR HA H 5.05 . 1 420 . 94 TYR HB2 H 3.16 . 2 421 . 94 TYR HB3 H 2.99 . 2 422 . 95 ALA N N 121.0 . 1 423 . 95 ALA H H 7.34 . 1 424 . 95 ALA HA H 4.33 . 1 425 . 95 ALA HB H 1.55 . 1 426 . 96 ASP N N 115.7 . 1 427 . 96 ASP H H 8.69 . 1 428 . 96 ASP HA H 4.87 . 1 429 . 96 ASP HB2 H 2.90 . 2 430 . 96 ASP HB3 H 2.59 . 2 431 . 97 ASN N N 119.8 . 1 432 . 97 ASN H H 7.82 . 1 433 . 97 ASN HA H 5.21 . 1 434 . 97 ASN HB2 H 3.17 . 2 435 . 97 ASN HB3 H 1.97 . 2 436 . 97 ASN ND2 N 111.8 . 1 437 . 97 ASN HD21 H 8.61 . 2 438 . 97 ASN HD22 H 6.63 . 2 439 . 98 PHE N N 122.0 . 1 440 . 98 PHE H H 7.66 . 1 441 . 98 PHE HA H 4.64 . 1 442 . 98 PHE HB2 H 3.31 . 2 443 . 98 PHE HB3 H 2.79 . 2 444 . 100 ASP N N 117.2 . 1 445 . 100 ASP H H 7.20 . 1 446 . 100 ASP HA H 4.12 . 1 447 . 100 ASP HB2 H 2.44 . 1 448 . 100 ASP HB3 H 2.44 . 1 449 . 101 ALA N N 117.7 . 1 450 . 101 ALA H H 8.46 . 1 451 . 101 ALA HA H 3.72 . 1 452 . 101 ALA HB H 1.28 . 1 453 . 102 ILE N N 117.2 . 1 454 . 102 ILE H H 7.20 . 1 455 . 102 ILE HA H 3.89 . 1 456 . 102 ILE HB H 1.50 . 1 457 . 102 ILE HG12 H 1.37 . 2 458 . 102 ILE HG13 H 1.13 . 2 459 . 103 GLY N N 107.8 . 1 460 . 103 GLY H H 7.14 . 1 461 . 103 GLY HA2 H 3.50 . 2 462 . 103 GLY HA3 H 3.26 . 2 463 . 104 ILE N N 123.9 . 1 464 . 104 ILE H H 8.11 . 1 465 . 104 ILE HA H 3.71 . 1 466 . 104 ILE HB H 1.70 . 1 467 . 104 ILE HG2 H 0.65 . 1 468 . 104 ILE HG12 H 1.53 . 2 469 . 104 ILE HD1 H 0.95 . 1 470 . 105 LEU N N 120.2 . 1 471 . 105 LEU H H 7.88 . 1 472 . 105 LEU HA H 3.82 . 1 473 . 105 LEU HB2 H 1.51 . 2 474 . 105 LEU HB3 H 1.01 . 2 475 . 105 LEU HG H 1.41 . 1 476 . 105 LEU HD1 H 0.52 . 2 477 . 105 LEU HD2 H -0.16 . 2 478 . 106 GLU N N 119.4 . 1 479 . 106 GLU H H 7.88 . 1 480 . 106 GLU HA H 3.90 . 1 481 . 106 GLU HB2 H 1.52 . 2 482 . 106 GLU HB3 H 0.29 . 2 483 . 107 GLU N N 118.8 . 1 484 . 107 GLU H H 7.59 . 1 485 . 107 GLU HA H 3.77 . 1 486 . 107 GLU HB2 H 2.04 . 1 487 . 107 GLU HB3 H 2.04 . 1 488 . 108 LYS N N 118.1 . 1 489 . 108 LYS H H 7.03 . 1 490 . 108 LYS HA H 4.13 . 1 491 . 108 LYS HB2 H 2.02 . 2 492 . 108 LYS HB3 H 1.85 . 2 493 . 108 LYS HG2 H 1.47 . 2 494 . 108 LYS HG3 H 1.11 . 2 495 . 109 ILE N N 120.5 . 1 496 . 109 ILE H H 8.48 . 1 497 . 109 ILE HA H 2.91 . 1 498 . 109 ILE HB H 1.93 . 1 499 . 109 ILE HG2 H -0.06 . 1 500 . 109 ILE HG12 H 1.47 . 2 501 . 109 ILE HG13 H -0.04 . 2 502 . 109 ILE HD1 H 0.54 . 1 503 . 110 SER N N 117.4 . 1 504 . 110 SER H H 8.94 . 1 505 . 110 SER HA H 4.80 . 1 506 . 110 SER HB2 H 3.99 . 2 507 . 110 SER HB3 H 3.89 . 2 508 . 111 GLN N N 124.9 . 1 509 . 111 GLN H H 7.65 . 1 510 . 111 GLN HA H 4.15 . 1 511 . 111 GLN HB2 H 2.44 . 2 512 . 111 GLN HB3 H 2.31 . 2 513 . 111 GLN HG2 H 2.67 . 2 514 . 111 GLN HG3 H 2.45 . 2 515 . 111 GLN NE2 N 111.6 . 1 516 . 111 GLN HE21 H 7.53 . 2 517 . 111 GLN HE22 H 6.87 . 2 518 . 112 ARG N N 116.1 . 1 519 . 112 ARG H H 7.50 . 1 520 . 112 ARG HA H 4.42 . 1 521 . 112 ARG HB2 H 1.98 . 1 522 . 112 ARG HB3 H 1.98 . 1 523 . 113 GLY N N 106.9 . 1 524 . 113 GLY H H 7.69 . 1 525 . 113 GLY HA2 H 4.48 . 2 526 . 113 GLY HA3 H 3.72 . 2 527 . 114 GLY N N 110.5 . 1 528 . 114 GLY H H 8.47 . 1 529 . 114 GLY HA2 H 4.08 . 2 530 . 114 GLY HA3 H 3.02 . 2 531 . 115 LYS N N 126.1 . 1 532 . 115 LYS H H 8.18 . 1 533 . 115 LYS HA H 4.77 . 1 534 . 115 LYS HB2 H 2.14 . 2 535 . 115 LYS HB3 H 1.89 . 2 536 . 115 LYS HG2 H 1.56 . 1 537 . 115 LYS HG3 H 1.56 . 1 538 . 116 THR N N 126.7 . 1 539 . 116 THR H H 8.58 . 1 540 . 116 THR HA H 5.33 . 1 541 . 116 THR HB H 4.16 . 1 542 . 116 THR HG2 H 0.93 . 1 543 . 117 VAL N N 121.7 . 1 544 . 117 VAL H H 8.90 . 1 545 . 117 VAL HA H 4.55 . 1 546 . 117 VAL HB H 2.18 . 1 547 . 117 VAL HG1 H 1.00 . 2 548 . 117 VAL HG2 H 0.40 . 2 549 . 118 GLY N N 107.5 . 1 550 . 118 GLY H H 9.23 . 1 551 . 118 GLY HA2 H 4.30 . 2 552 . 118 GLY HA3 H 3.70 . 2 553 . 119 TYR N N 115.6 . 1 554 . 119 TYR H H 7.52 . 1 555 . 119 TYR HA H 4.45 . 1 556 . 119 TYR HB2 H 2.88 . 1 557 . 119 TYR HB3 H 2.88 . 1 558 . 120 TRP N N 123.6 . 1 559 . 120 TRP H H 8.62 . 1 560 . 120 TRP HA H 5.39 . 1 561 . 120 TRP HB2 H 3.33 . 2 562 . 120 TRP HB3 H 2.96 . 2 563 . 120 TRP NE1 N 128.8 . 1 564 . 120 TRP CD1 C 126.4 . 1 565 . 120 TRP HD1 H 7.29 . 1 566 . 120 TRP CE3 C 122.4 . 1 567 . 120 TRP HE3 H 8.12 . 1 568 . 120 TRP HE1 H 10.38 . 1 569 . 120 TRP CZ3 C 121.3 . 1 570 . 120 TRP HZ3 H 7.34 . 1 571 . 120 TRP CZ2 C 114.2 . 1 572 . 120 TRP HZ2 H 7.58 . 1 573 . 120 TRP CH2 C 125.4 . 1 574 . 120 TRP HH2 H 7.48 . 1 575 . 121 SER N N 119.9 . 1 576 . 121 SER H H 7.55 . 1 577 . 121 SER HA H 4.39 . 1 578 . 121 SER HB2 H 3.84 . 2 579 . 121 SER HB3 H 3.50 . 2 580 . 122 THR N N 112.7 . 1 581 . 122 THR H H 8.36 . 1 582 . 122 THR HA H 4.40 . 1 583 . 122 THR HB H 4.55 . 1 584 . 122 THR HG2 H 0.33 . 1 585 . 123 ASP N N 125.2 . 1 586 . 123 ASP H H 8.45 . 1 587 . 123 ASP HA H 4.51 . 1 588 . 123 ASP HB2 H 2.59 . 2 589 . 123 ASP HB3 H 2.55 . 2 590 . 124 GLY N N 111.1 . 1 591 . 124 GLY H H 9.01 . 1 592 . 124 GLY HA2 H 4.05 . 2 593 . 124 GLY HA3 H 3.61 . 2 594 . 125 TYR N N 116.8 . 1 595 . 125 TYR H H 7.63 . 1 596 . 125 TYR HA H 5.08 . 1 597 . 125 TYR HB2 H 3.24 . 2 598 . 125 TYR HB3 H 2.89 . 2 599 . 126 ASP N N 124.3 . 1 600 . 126 ASP H H 9.45 . 1 601 . 126 ASP HA H 4.97 . 1 602 . 126 ASP HB2 H 2.70 . 2 603 . 126 ASP HB3 H 2.42 . 2 604 . 127 PHE N N 117.0 . 1 605 . 127 PHE H H 7.68 . 1 606 . 127 PHE HA H 4.85 . 1 607 . 127 PHE HB2 H 3.27 . 2 608 . 127 PHE HB3 H 3.02 . 2 609 . 127 PHE HD1 H 7.17 . 1 610 . 127 PHE HD2 H 7.17 . 1 611 . 128 ASN N N 118.0 . 1 612 . 128 ASN H H 9.13 . 1 613 . 128 ASN HA H 4.86 . 1 614 . 128 ASN HB2 H 3.02 . 2 615 . 128 ASN HB3 H 2.86 . 2 616 . 128 ASN ND2 N 115.0 . 1 617 . 128 ASN HD21 H 8.00 . 2 618 . 128 ASN HD22 H 6.87 . 2 619 . 129 ASP N N 118.7 . 1 620 . 129 ASP H H 9.00 . 1 621 . 129 ASP HA H 4.97 . 1 622 . 129 ASP HB2 H 2.88 . 2 623 . 129 ASP HB3 H 2.62 . 2 624 . 130 SER N N 111.1 . 1 625 . 130 SER H H 8.55 . 1 626 . 130 SER HA H 4.67 . 1 627 . 130 SER HB3 H 3.41 . 2 628 . 130 SER HG H 6.18 . 1 629 . 131 LYS N N 127.6 . 1 630 . 131 LYS H H 9.18 . 1 631 . 131 LYS HA H 4.46 . 1 632 . 131 LYS HB2 H 2.03 . 1 633 . 131 LYS HB3 H 2.03 . 1 634 . 131 LYS HG2 H 1.46 . 1 635 . 131 LYS HG3 H 1.46 . 1 636 . 131 LYS HD2 H 1.57 . 1 637 . 131 LYS HD3 H 1.57 . 1 638 . 132 ALA N N 121.8 . 1 639 . 132 ALA H H 9.22 . 1 640 . 132 ALA HA H 4.11 . 1 641 . 132 ALA HB H 1.37 . 1 642 . 133 LEU N N 119.0 . 1 643 . 133 LEU H H 7.04 . 1 644 . 133 LEU HA H 4.68 . 1 645 . 133 LEU HB2 H 1.84 . 2 646 . 133 LEU HB3 H 1.59 . 2 647 . 133 LEU HG H 1.52 . 1 648 . 133 LEU HD1 H 1.08 . 2 649 . 133 LEU HD2 H 0.50 . 2 650 . 134 ARG N N 124.9 . 1 651 . 134 ARG H H 9.66 . 1 652 . 134 ARG HA H 4.59 . 1 653 . 134 ARG HB2 H 1.73 . 2 654 . 134 ARG HB3 H 1.49 . 2 655 . 134 ARG HG2 H 1.47 . 1 656 . 134 ARG HG3 H 1.47 . 1 657 . 134 ARG HD2 H 3.42 . 2 658 . 134 ARG HD3 H 3.16 . 2 659 . 134 ARG NE N 86.7 . 1 660 . 134 ARG HE H 6.74 . 1 661 . 135 ASN N N 118.5 . 1 662 . 135 ASN H H 7.50 . 1 663 . 135 ASN HA H 4.27 . 1 664 . 135 ASN HB2 H 2.93 . 2 665 . 135 ASN HB3 H 2.55 . 2 666 . 135 ASN ND2 N 112.9 . 1 667 . 135 ASN HD21 H 7.47 . 2 668 . 135 ASN HD22 H 6.85 . 2 669 . 136 GLY N N 102.9 . 1 670 . 136 GLY H H 8.54 . 1 671 . 136 GLY HA2 H 4.12 . 2 672 . 136 GLY HA3 H 3.54 . 2 673 . 137 LYS N N 118.5 . 1 674 . 137 LYS H H 7.50 . 1 675 . 137 LYS HA H 4.64 . 1 676 . 137 LYS HB2 H 1.99 . 2 677 . 137 LYS HB3 H 1.60 . 2 678 . 138 PHE N N 118.3 . 1 679 . 138 PHE H H 9.40 . 1 680 . 138 PHE HA H 5.14 . 1 681 . 138 PHE HB2 H 3.44 . 2 682 . 138 PHE HB3 H 3.15 . 2 683 . 139 VAL N N 113.7 . 1 684 . 139 VAL H H 8.40 . 1 685 . 139 VAL HA H 3.84 . 1 686 . 139 VAL HB H 1.85 . 1 687 . 139 VAL HG1 H 0.68 . 2 688 . 139 VAL HG2 H 0.51 . 2 689 . 140 GLY N N 101.6 . 1 690 . 140 GLY H H 6.42 . 1 691 . 140 GLY HA2 H 4.55 . 1 692 . 140 GLY HA3 H 4.55 . 1 693 . 141 LEU N N 117.4 . 1 694 . 141 LEU H H 6.84 . 1 695 . 141 LEU HA H 2.43 . 1 696 . 141 LEU HB2 H -0.15 . 2 697 . 141 LEU HB3 H -1.79 . 2 698 . 141 LEU HG H 0.38 . 1 699 . 141 LEU HD1 H -0.03 . 2 700 . 141 LEU HD2 H -0.90 . 2 701 . 142 ALA H H 5.20 . 1 702 . 142 ALA HA H 4.02 . 1 703 . 142 ALA HB H 0.18 . 1 704 . 143 LEU N N 125.1 . 1 705 . 143 LEU H H 8.54 . 1 706 . 143 LEU HA H 4.39 . 1 707 . 143 LEU HB2 H 1.95 . 2 708 . 143 LEU HB3 H 1.31 . 2 709 . 143 LEU HG H 1.14 . 1 710 . 143 LEU HD1 H 0.83 . 2 711 . 143 LEU HD2 H 0.69 . 2 712 . 144 ASP N N 119.3 . 1 713 . 144 ASP H H 8.35 . 1 714 . 144 ASP HA H 5.39 . 1 715 . 144 ASP HB2 H 2.84 . 2 716 . 144 ASP HB3 H 2.35 . 2 717 . 145 GLU N N 125.0 . 1 718 . 145 GLU H H 8.85 . 1 719 . 145 GLU HA H 4.21 . 1 720 . 145 GLU HB2 H 2.05 . 2 721 . 145 GLU HB3 H 1.94 . 2 722 . 145 GLU HG2 H 2.23 . 1 723 . 145 GLU HG3 H 2.23 . 1 724 . 146 ASP N N 121.1 . 1 725 . 146 ASP H H 8.61 . 1 726 . 146 ASP HA H 4.58 . 1 727 . 146 ASP HB2 H 2.77 . 2 728 . 146 ASP HB3 H 2.61 . 2 729 . 147 ASN N N 113.5 . 1 730 . 147 ASN H H 8.93 . 1 731 . 147 ASN HA H 4.97 . 1 732 . 147 ASN HB2 H 2.88 . 2 733 . 147 ASN HB3 H 2.43 . 2 734 . 147 ASN ND2 N 124.4 . 1 735 . 147 ASN HD21 H 10.10 . 2 736 . 147 ASN HD22 H 7.80 . 2 737 . 148 GLN N N 117.1 . 1 738 . 148 GLN H H 7.58 . 1 739 . 148 GLN HA H 5.07 . 1 740 . 148 GLN HB2 H 2.33 . 2 741 . 148 GLN HB3 H 2.17 . 2 742 . 148 GLN HG2 H 2.55 . 2 743 . 148 GLN HG3 H 1.94 . 2 744 . 148 GLN NE2 N 115.9 . 1 745 . 148 GLN HE21 H 7.03 . 2 746 . 148 GLN HE22 H 7.87 . 2 747 . 149 SER N N 119.0 . 1 748 . 149 SER H H 8.73 . 1 749 . 149 SER HA H 4.33 . 1 750 . 149 SER HB2 H 4.15 . 1 751 . 149 SER HB3 H 4.15 . 1 752 . 150 ASP N N 119.0 . 1 753 . 150 ASP H H 9.21 . 1 754 . 150 ASP HA H 4.46 . 1 755 . 150 ASP HB2 H 2.71 . 1 756 . 150 ASP HB3 H 2.71 . 1 757 . 151 LEU N N 117.6 . 1 758 . 151 LEU H H 7.59 . 1 759 . 151 LEU HA H 4.63 . 1 760 . 151 LEU HB2 H 1.69 . 2 761 . 151 LEU HB3 H 1.60 . 2 762 . 151 LEU HG H 1.60 . 1 763 . 151 LEU HD1 H 0.81 . 1 764 . 151 LEU HD2 H 0.81 . 1 765 . 152 THR N N 118.3 . 1 766 . 152 THR H H 7.35 . 1 767 . 152 THR HA H 4.31 . 1 768 . 152 THR HB H 3.60 . 1 769 . 152 THR HG2 H 1.16 . 1 770 . 153 ASP N N 121.5 . 1 771 . 153 ASP H H 8.84 . 1 772 . 153 ASP HA H 4.19 . 1 773 . 153 ASP HB2 H 2.64 . 2 774 . 153 ASP HB3 H 2.58 . 2 775 . 154 ASP N N 118.7 . 1 776 . 154 ASP H H 8.63 . 1 777 . 154 ASP HA H 4.42 . 1 778 . 154 ASP HB2 H 2.72 . 1 779 . 154 ASP HB3 H 2.72 . 1 780 . 155 ARG N N 120.7 . 1 781 . 155 ARG H H 8.24 . 1 782 . 155 ARG HA H 4.28 . 1 783 . 155 ARG HB2 H 2.37 . 2 784 . 155 ARG HB3 H 1.70 . 2 785 . 155 ARG HG2 H 1.95 . 1 786 . 155 ARG HG3 H 1.95 . 1 787 . 155 ARG NE N 85.5 . 1 788 . 155 ARG HE H 7.63 . 1 789 . 156 ILE N N 117.3 . 1 790 . 156 ILE H H 8.51 . 1 791 . 156 ILE HA H 3.37 . 1 792 . 156 ILE HB H 1.88 . 1 793 . 156 ILE HG2 H 0.65 . 1 794 . 156 ILE HG12 H 0.73 . 2 795 . 156 ILE HG13 H 0.41 . 2 796 . 157 LYS N N 117.8 . 1 797 . 157 LYS H H 8.09 . 1 798 . 157 LYS HA H 3.62 . 1 799 . 157 LYS HB2 H 1.88 . 1 800 . 157 LYS HB3 H 1.88 . 1 801 . 157 LYS HG2 H 1.33 . 1 802 . 157 LYS HG3 H 1.33 . 1 803 . 157 LYS HD2 H 1.59 . 1 804 . 157 LYS HD3 H 1.59 . 1 805 . 158 SER N N 115.4 . 1 806 . 158 SER H H 8.33 . 1 807 . 158 SER HA H 4.41 . 1 808 . 159 TRP N N 126.4 . 1 809 . 159 TRP H H 8.98 . 1 810 . 159 TRP HA H 4.54 . 1 811 . 159 TRP HB2 H 3.02 . 2 812 . 159 TRP HB3 H 2.71 . 2 813 . 159 TRP NE1 N 132.2 . 1 814 . 159 TRP CD1 C 127.2 . 1 815 . 159 TRP HD1 H 7.47 . 1 816 . 159 TRP CE3 C 119.3 . 1 817 . 159 TRP HE3 H 6.92 . 1 818 . 159 TRP HE1 H 11.22 . 1 819 . 159 TRP CZ3 C 120.0 . 1 820 . 159 TRP HZ3 H 6.56 . 1 821 . 159 TRP CZ2 C 117.3 . 1 822 . 159 TRP HZ2 H 8.28 . 1 823 . 159 TRP CH2 C 124.2 . 1 824 . 159 TRP HH2 H 6.79 . 1 825 . 160 VAL N N 117.6 . 1 826 . 160 VAL H H 9.02 . 1 827 . 160 VAL HA H 2.95 . 1 828 . 160 VAL HB H 1.87 . 1 829 . 160 VAL HG1 H 0.88 . 2 830 . 160 VAL HG2 H -0.19 . 2 831 . 161 ALA N N 120.5 . 1 832 . 161 ALA H H 7.34 . 1 833 . 161 ALA HA H 3.91 . 1 834 . 161 ALA HB H 1.52 . 1 835 . 162 GLN N N 120.5 . 1 836 . 162 GLN H H 7.66 . 1 837 . 162 GLN HA H 4.13 . 1 838 . 162 GLN HB2 H 2.35 . 1 839 . 162 GLN HB3 H 2.35 . 1 840 . 162 GLN HG2 H 2.49 . 1 841 . 162 GLN HG3 H 2.49 . 1 842 . 162 GLN NE2 N 109.7 . 1 843 . 162 GLN HE21 H 7.83 . 2 844 . 162 GLN HE22 H 7.58 . 2 845 . 163 LEU N N 120.5 . 1 846 . 163 LEU H H 8.78 . 1 847 . 163 LEU HA H 3.44 . 1 848 . 163 LEU HB2 H 1.62 . 2 849 . 163 LEU HB3 H 0.87 . 2 850 . 163 LEU HG H 0.61 . 1 851 . 163 LEU HD1 H -0.16 . 2 852 . 163 LEU HD2 H -0.54 . 2 853 . 164 LYS N N 119.0 . 1 854 . 164 LYS H H 8.71 . 1 855 . 164 LYS HA H 3.90 . 1 856 . 164 LYS HB2 H 1.95 . 2 857 . 164 LYS HB3 H 1.84 . 2 858 . 164 LYS HG2 H 1.56 . 2 859 . 164 LYS HG3 H 1.27 . 2 860 . 164 LYS HD2 H 1.63 . 1 861 . 164 LYS HD3 H 1.63 . 1 862 . 165 SER N N 111.4 . 1 863 . 165 SER H H 7.07 . 1 864 . 165 SER HA H 4.42 . 1 865 . 165 SER HB2 H 4.11 . 2 866 . 165 SER HB3 H 4.06 . 2 867 . 166 GLU N N 122.0 . 1 868 . 166 GLU H H 8.35 . 1 869 . 166 GLU HA H 4.17 . 1 870 . 166 GLU HB2 H 2.02 . 2 871 . 166 GLU HB3 H 1.64 . 2 872 . 166 GLU HG2 H 2.54 . 2 873 . 166 GLU HG3 H 2.26 . 2 874 . 167 PHE N N 116.2 . 1 875 . 167 PHE H H 9.21 . 1 876 . 167 PHE HA H 4.70 . 1 877 . 167 PHE HB2 H 2.87 . 2 878 . 167 PHE HB3 H 2.73 . 2 879 . 167 PHE HD1 H 6.87 . 1 880 . 167 PHE HD2 H 6.87 . 1 881 . 167 PHE HE1 H 7.06 . 1 882 . 167 PHE HE2 H 7.06 . 1 883 . 168 GLY N N 107.5 . 1 884 . 168 GLY H H 7.52 . 1 885 . 168 GLY HA2 H 3.94 . 1 886 . 168 GLY HA3 H 3.94 . 1 887 . 169 LEU N N 125.6 . 1 888 . 169 LEU H H 8.01 . 1 889 . 169 LEU HA H 4.14 . 1 890 . 169 LEU HB2 H 1.74 . 2 891 . 169 LEU HB3 H 1.61 . 2 892 . 169 LEU HG H 1.57 . 1 893 . 169 LEU HD1 H 0.88 . 2 894 . 169 LEU HD2 H 0.69 . 2 stop_ save_