data_4721 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the Central Core Domain of TFIIEbeta with a Novel Double-stranded DNA-binding Surface ; _BMRB_accession_number 4721 _BMRB_flat_file_name bmr4721.str _Entry_type original _Submission_date 2000-04-14 _Accession_date 2000-04-17 _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 Okuda M. . . 2 Watanabe Y. . . 3 Okamura H. . . 4 Hanaoka F. . . 5 Ohkuma Y. . . 6 Nishimura Y. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 507 "13C chemical shifts" 256 "15N chemical shifts" 87 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Okuda, M., Watanabe, Y., Okamura, H., Hanaoka, F., Ohkuma, Y., and Nishimura, Y., "Structure of the Central Core Domain of TFIIEbeta with a Novel Double-stranded DNA-binding Surface," EMBO J. 19, 1346-1356 (2000). ; _Citation_title ; Structure of the Central Core Domain of TFIIEbeta with a Novel Double-stranded DNA-binding Surface ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20183615 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Okuda M. . . 2 Watanabe Y. . . 3 Okamura H. . . 4 Hanaoka F. . . 5 Ohkuma Y. . . 6 Nishimura Y. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'EMBO Journal' _Journal_volume 19 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1346 _Page_last 1356 _Year 2000 _Details . loop_ _Keyword 'WINGED HELIX-TURN-HELIX' stop_ save_ ################################## # Molecular system description # ################################## save_system_TFIIE-BETA _Saveframe_category molecular_system _Mol_system_name 'general transcription factor TFIIE-BETA' _Abbreviation_common TFIIE-BETA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TFIIE-BETA $TFIIE-BETA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TFIIE-BETA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'general transcription factor TFIIE-BETA' _Abbreviation_common TFIIE-BETA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; ALSGSSGYKFGVLAKIVNYM KTRHQRGDTHPLTLDEILDE TQHLDIGLKQKQWLMTEALV NNPKIEVIDGKYAFKPKYNV R ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LEU 3 SER 4 GLY 5 SER 6 SER 7 GLY 8 TYR 9 LYS 10 PHE 11 GLY 12 VAL 13 LEU 14 ALA 15 LYS 16 ILE 17 VAL 18 ASN 19 TYR 20 MET 21 LYS 22 THR 23 ARG 24 HIS 25 GLN 26 ARG 27 GLY 28 ASP 29 THR 30 HIS 31 PRO 32 LEU 33 THR 34 LEU 35 ASP 36 GLU 37 ILE 38 LEU 39 ASP 40 GLU 41 THR 42 GLN 43 HIS 44 LEU 45 ASP 46 ILE 47 GLY 48 LEU 49 LYS 50 GLN 51 LYS 52 GLN 53 TRP 54 LEU 55 MET 56 THR 57 GLU 58 ALA 59 LEU 60 VAL 61 ASN 62 ASN 63 PRO 64 LYS 65 ILE 66 GLU 67 VAL 68 ILE 69 ASP 70 GLY 71 LYS 72 TYR 73 ALA 74 PHE 75 LYS 76 PRO 77 LYS 78 TYR 79 ASN 80 VAL 81 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 1D8J "Solution Structure Of The Central Core Domain Of Tfiie Beta" 100.00 81 100.00 100.00 2.51e-52 PDB 1D8K "Solution Structure Of The Central Core Domain Of Tfiie Beta" 100.00 81 100.00 100.00 2.51e-52 DBJ BAE91442 "unnamed protein product [Macaca fascicularis]" 100.00 196 100.00 100.00 2.37e-52 DBJ BAG73195 "general transcription factor IIE, polypeptide 2, beta 34kDa [synthetic construct]" 100.00 291 100.00 100.00 3.09e-51 EMBL CAA45069 "transcription factor TFIIE beta [Homo sapiens]" 100.00 291 100.00 100.00 3.09e-51 GB AAB20414 "general transcription factor IIE 34 kda subunit [Homo sapiens]" 100.00 291 100.00 100.00 3.09e-51 GB AAG39077 "general transcription factor [Homo sapiens]" 100.00 291 97.53 97.53 4.45e-49 GB AAH30572 "General transcription factor IIE, polypeptide 2, beta 34kDa [Homo sapiens]" 100.00 291 100.00 100.00 3.09e-51 GB AAV38582 "general transcription factor IIE, polypeptide 2, beta 34kDa [synthetic construct]" 100.00 292 100.00 100.00 3.03e-51 GB AAX36090 "general transcription factor IIE polypeptide 2, partial [synthetic construct]" 100.00 292 100.00 100.00 3.03e-51 PRF 1802389A "transcription factor IIE:SUBUNIT=beta" 100.00 291 98.77 98.77 3.54e-50 REF NP_001247856 "general transcription factor IIE, polypeptide 2, beta 34kDa [Macaca mulatta]" 100.00 291 100.00 100.00 3.74e-51 REF NP_002086 "transcription initiation factor IIE subunit beta [Homo sapiens]" 100.00 291 100.00 100.00 3.09e-51 REF XP_001168104 "PREDICTED: transcription initiation factor IIE subunit beta [Pan troglodytes]" 100.00 291 100.00 100.00 3.09e-51 REF XP_002756966 "PREDICTED: transcription initiation factor IIE subunit beta [Callithrix jacchus]" 100.00 291 100.00 100.00 3.83e-51 REF XP_003269588 "PREDICTED: transcription initiation factor IIE subunit beta [Nomascus leucogenys]" 100.00 291 100.00 100.00 3.78e-51 SP P29084 "RecName: Full=Transcription initiation factor IIE subunit beta; Short=TFIIE-beta; AltName: Full=General transcription factor II" 100.00 291 100.00 100.00 3.09e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TFIIE-BETA 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 $TFIIE-BETA 'recombinant technology' bacteria Escherichia coli . PET3A 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 $TFIIE-BETA . mM 1 2 '[U-15N; U-13C]' 'phosphate buffer' 20 mM . . . NaCl 500 mM . . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TFIIE-BETA . mM 1 2 . 'phosphate buffer' 20 mM . . . NaCl 500 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version 1.6 loop_ _Task PROCESSING stop_ _Details 'DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER, BAX' save_ save_PIPP_CAPP_STAPP _Saveframe_category software _Name 'PIPP, CAPP, STAPP' _Version 3.9 loop_ _Task 'DATA ANALYSIS' stop_ _Details 'GARRETT, POWERS, GRONENBORN, CLORE' save_ save_EMBOSS _Saveframe_category software _Name EMBOSS _Version 5 loop_ _Task 'STRUCTURE CALCULATION' stop_ _Details 'NAKAI, KIDERA, NAKAMURA' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 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_3D_15N-SEPARATED_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-SEPARATED_NOESY _Sample_label . save_ save_4D_13C-SEPARATED_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 4D_13C-SEPARATED_NOESY _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HMQC-J_6 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_13C-SEPARATED_NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-SEPARATED_NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 4D_13C-SEPARATED_NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_label _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_label _Mol_system_component_name TFIIE-BETA _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 4.19 . 1 2 . 1 ALA HB H 1.60 . 1 3 . 1 ALA CA C 51.9 . 1 4 . 1 ALA CB C 19.5 . 1 5 . 2 LEU H H 8.68 . 1 6 . 2 LEU HA H 4.51 . 1 7 . 2 LEU HB2 H 1.67 . 1 8 . 2 LEU HB3 H 1.67 . 1 9 . 2 LEU HG H 1.74 . 1 10 . 2 LEU HD1 H 0.95 . 1 11 . 2 LEU HD2 H 0.99 . 1 12 . 2 LEU CA C 55.4 . 1 13 . 2 LEU CB C 42.3 . 1 14 . 2 LEU CG C 26.9 . 1 15 . 2 LEU CD1 C 23.9 . 1 16 . 3 SER H H 8.50 . 1 17 . 3 SER HA H 4.41 . 1 18 . 3 SER HB2 H 3.93 . 1 19 . 3 SER HB3 H 3.93 . 1 20 . 3 SER CA C 58.5 . 1 21 . 3 SER CB C 63.9 . 1 22 . 3 SER N N 117.4 . 1 23 . 4 GLY H H 8.47 . 1 24 . 4 GLY HA2 H 4.10 . 1 25 . 4 GLY HA3 H 4.10 . 1 26 . 4 GLY CA C 45.6 . 1 27 . 4 GLY N N 111.2 . 1 28 . 5 SER H H 8.26 . 1 29 . 5 SER HA H 4.47 . 1 30 . 5 SER HB2 H 3.93 . 1 31 . 5 SER HB3 H 3.93 . 1 32 . 5 SER CA C 58.5 . 1 33 . 5 SER CB C 63.9 . 1 34 . 5 SER N N 116.0 . 1 35 . 6 SER H H 8.45 . 1 36 . 6 SER HA H 4.44 . 1 37 . 6 SER HB2 H 3.93 . 1 38 . 6 SER HB3 H 3.93 . 1 39 . 6 SER CA C 59.3 . 1 40 . 6 SER CB C 63.7 . 1 41 . 6 SER N N 118.1 . 1 42 . 7 GLY H H 8.42 . 1 43 . 7 GLY HA2 H 4.04 . 1 44 . 7 GLY HA3 H 4.04 . 1 45 . 7 GLY CA C 45.7 . 1 46 . 7 GLY N N 110.2 . 1 47 . 8 TYR H H 8.06 . 1 48 . 8 TYR HA H 4.38 . 1 49 . 8 TYR HB2 H 2.73 . 2 50 . 8 TYR HB3 H 2.96 . 2 51 . 8 TYR HD1 H 7.00 . 1 52 . 8 TYR HD2 H 7.00 . 1 53 . 8 TYR HE1 H 6.77 . 1 54 . 8 TYR HE2 H 6.77 . 1 55 . 8 TYR CA C 59.5 . 1 56 . 8 TYR CB C 38.3 . 1 57 . 8 TYR N N 122.3 . 1 58 . 9 LYS H H 8.29 . 1 59 . 9 LYS HA H 3.93 . 1 60 . 9 LYS HB2 H 1.45 . 1 61 . 9 LYS HB3 H 1.45 . 1 62 . 9 LYS HG2 H 0.48 . 2 63 . 9 LYS HG3 H 0.87 . 2 64 . 9 LYS HD2 H 0.68 . 2 65 . 9 LYS HD3 H 1.14 . 2 66 . 9 LYS HE2 H 2.08 . 2 67 . 9 LYS HE3 H 2.34 . 2 68 . 9 LYS CA C 58.2 . 1 69 . 9 LYS CB C 31.3 . 1 70 . 9 LYS CG C 24.1 . 1 71 . 9 LYS CD C 28.9 . 1 72 . 9 LYS CE C 41.9 . 1 73 . 9 LYS N N 121.0 . 1 74 . 10 PHE H H 7.70 . 1 75 . 10 PHE HA H 4.50 . 1 76 . 10 PHE HB2 H 3.09 . 1 77 . 10 PHE HB3 H 3.33 . 1 78 . 10 PHE HD1 H 7.41 . 1 79 . 10 PHE HD2 H 7.41 . 1 80 . 10 PHE HE1 H 7.51 . 1 81 . 10 PHE HE2 H 7.51 . 1 82 . 10 PHE HZ H 7.46 . 1 83 . 10 PHE CA C 60.8 . 1 84 . 10 PHE CB C 38.6 . 1 85 . 10 PHE N N 120.0 . 1 86 . 11 GLY H H 8.28 . 1 87 . 11 GLY HA2 H 4.09 . 1 88 . 11 GLY HA3 H 4.09 . 1 89 . 11 GLY CA C 46.9 . 1 90 . 11 GLY N N 111.0 . 1 91 . 12 VAL H H 7.68 . 1 92 . 12 VAL HA H 3.53 . 1 93 . 12 VAL HB H 2.16 . 1 94 . 12 VAL HG1 H 0.68 . 1 95 . 12 VAL HG2 H 0.68 . 1 96 . 12 VAL CA C 66.1 . 1 97 . 12 VAL CB C 31.3 . 1 98 . 12 VAL CG1 C 21.2 . 1 99 . 12 VAL CG2 C 21.2 . 1 100 . 12 VAL N N 122.9 . 1 101 . 13 LEU H H 7.93 . 1 102 . 13 LEU HA H 3.94 . 1 103 . 13 LEU HB2 H 1.60 . 1 104 . 13 LEU HB3 H 2.27 . 1 105 . 13 LEU HG H 1.74 . 1 106 . 13 LEU HD1 H 0.70 . 1 107 . 13 LEU HD2 H 1.08 . 1 108 . 13 LEU CA C 58.3 . 1 109 . 13 LEU CB C 41.8 . 1 110 . 13 LEU CG C 26.9 . 1 111 . 13 LEU CD1 C 22.9 . 1 112 . 13 LEU CD2 C 26.0 . 1 113 . 13 LEU N N 120.0 . 1 114 . 14 ALA H H 8.10 . 1 115 . 14 ALA HA H 4.15 . 1 116 . 14 ALA HB H 1.57 . 1 117 . 14 ALA CA C 55.3 . 1 118 . 14 ALA CB C 17.6 . 1 119 . 14 ALA N N 119.8 . 1 120 . 15 LYS H H 7.81 . 1 121 . 15 LYS HA H 4.22 . 1 122 . 15 LYS HB2 H 2.06 . 2 123 . 15 LYS HB3 H 2.15 . 2 124 . 15 LYS HE2 H 3.08 . 1 125 . 15 LYS HE3 H 3.08 . 1 126 . 15 LYS CA C 59.6 . 1 127 . 15 LYS CB C 32.6 . 1 128 . 15 LYS CE C 42.4 . 1 129 . 15 LYS N N 118.2 . 1 130 . 16 ILE H H 8.33 . 1 131 . 16 ILE HA H 3.69 . 1 132 . 16 ILE HB H 2.17 . 1 133 . 16 ILE HG12 H 0.92 . 2 134 . 16 ILE HG13 H 1.92 . 2 135 . 16 ILE HG2 H 0.83 . 1 136 . 16 ILE HD1 H 0.69 . 1 137 . 16 ILE CA C 66.5 . 1 138 . 16 ILE CB C 37.7 . 1 139 . 16 ILE CG1 C 28.4 . 1 140 . 16 ILE CG2 C 16.1 . 1 141 . 16 ILE CD1 C 14.9 . 1 142 . 16 ILE N N 121.3 . 1 143 . 17 VAL H H 8.74 . 1 144 . 17 VAL HA H 3.47 . 1 145 . 17 VAL HB H 2.19 . 1 146 . 17 VAL HG1 H 1.11 . 1 147 . 17 VAL HG2 H 1.04 . 1 148 . 17 VAL CA C 68.1 . 1 149 . 17 VAL CB C 31.6 . 1 150 . 17 VAL CG1 C 21.9 . 1 151 . 17 VAL CG2 C 22.6 . 1 152 . 17 VAL N N 120.6 . 1 153 . 18 ASN H H 8.24 . 1 154 . 18 ASN HA H 4.48 . 1 155 . 18 ASN HB2 H 2.89 . 2 156 . 18 ASN HB3 H 2.95 . 2 157 . 18 ASN HD21 H 6.97 . 2 158 . 18 ASN HD22 H 7.70 . 2 159 . 18 ASN CA C 56.8 . 1 160 . 18 ASN CB C 38.8 . 1 161 . 18 ASN N N 116.7 . 1 162 . 18 ASN ND2 N 113.8 . 1 163 . 19 TYR H H 8.40 . 1 164 . 19 TYR HA H 4.32 . 1 165 . 19 TYR HB2 H 3.15 . 2 166 . 19 TYR HB3 H 3.29 . 2 167 . 19 TYR HD1 H 7.05 . 1 168 . 19 TYR HD2 H 7.05 . 1 169 . 19 TYR HE1 H 6.76 . 1 170 . 19 TYR HE2 H 6.76 . 1 171 . 19 TYR CA C 61.6 . 1 172 . 19 TYR CB C 38.6 . 1 173 . 19 TYR N N 123.3 . 1 174 . 20 MET H H 8.47 . 1 175 . 20 MET HA H 4.21 . 1 176 . 20 MET HB2 H 2.30 . 1 177 . 20 MET HB3 H 2.18 . 1 178 . 20 MET HG2 H 2.43 . 2 179 . 20 MET HG3 H 3.22 . 2 180 . 20 MET CA C 56.7 . 1 181 . 20 MET CB C 29.9 . 1 182 . 20 MET CG C 33.1 . 1 183 . 20 MET N N 117.3 . 1 184 . 21 LYS H H 8.39 . 1 185 . 21 LYS HA H 2.35 . 1 186 . 21 LYS HB2 H 1.33 . 1 187 . 21 LYS HB3 H 1.79 . 1 188 . 21 LYS HG2 H 1.62 . 2 189 . 21 LYS HG3 H 1.70 . 2 190 . 21 LYS HD2 H 0.90 . 1 191 . 21 LYS HD3 H 0.90 . 1 192 . 21 LYS HE2 H 2.99 . 1 193 . 21 LYS HE3 H 2.99 . 1 194 . 21 LYS CA C 59.4 . 1 195 . 21 LYS CB C 32.5 . 1 196 . 21 LYS CG C 29.4 . 1 197 . 21 LYS CD C 23.9 . 1 198 . 21 LYS CE C 42.3 . 1 199 . 21 LYS N N 123.7 . 1 200 . 22 THR H H 8.09 . 1 201 . 22 THR HA H 3.82 . 1 202 . 22 THR HB H 4.27 . 1 203 . 22 THR HG2 H 1.25 . 1 204 . 22 THR CA C 66.6 . 1 205 . 22 THR CB C 68.7 . 1 206 . 22 THR CG2 C 21.2 . 1 207 . 22 THR N N 116.3 . 1 208 . 23 ARG H H 8.04 . 1 209 . 23 ARG HA H 3.98 . 1 210 . 23 ARG HB2 H 1.73 . 2 211 . 23 ARG HB3 H 1.89 . 2 212 . 23 ARG HG2 H 1.62 . 2 213 . 23 ARG HG3 H 1.77 . 2 214 . 23 ARG HD2 H 2.86 . 2 215 . 23 ARG HD3 H 3.19 . 2 216 . 23 ARG HE H 7.46 . 1 217 . 23 ARG CA C 59.5 . 1 218 . 23 ARG CB C 29.6 . 1 219 . 23 ARG CG C 27.6 . 1 220 . 23 ARG CD C 44.2 . 1 221 . 23 ARG N N 121.2 . 1 222 . 23 ARG NE N 84.9 . 1 223 . 24 HIS H H 7.51 . 1 224 . 24 HIS HA H 3.83 . 1 225 . 24 HIS HB2 H 3.22 . 1 226 . 24 HIS HB3 H 3.22 . 1 227 . 24 HIS HD2 H 7.09 . 1 228 . 24 HIS HE1 H 7.94 . 1 229 . 24 HIS CA C 60.6 . 1 230 . 24 HIS CB C 31.7 . 1 231 . 24 HIS N N 121.4 . 1 232 . 25 GLN H H 8.32 . 1 233 . 25 GLN HA H 4.09 . 1 234 . 25 GLN HB2 H 2.20 . 2 235 . 25 GLN HB3 H 2.28 . 2 236 . 25 GLN HG2 H 2.55 . 2 237 . 25 GLN HG3 H 2.68 . 2 238 . 25 GLN HE21 H 6.85 . 2 239 . 25 GLN HE22 H 7.47 . 2 240 . 25 GLN CA C 58.5 . 1 241 . 25 GLN CB C 28.3 . 1 242 . 25 GLN CG C 34.5 . 1 243 . 25 GLN N N 118.5 . 1 244 . 25 GLN NE2 N 111.6 . 1 245 . 26 ARG H H 7.51 . 1 246 . 26 ARG HA H 4.50 . 1 247 . 26 ARG HB2 H 1.99 . 2 248 . 26 ARG HB3 H 2.07 . 2 249 . 26 ARG HG2 H 1.77 . 2 250 . 26 ARG HG3 H 1.96 . 2 251 . 26 ARG HD2 H 3.21 . 1 252 . 26 ARG HD3 H 3.21 . 1 253 . 26 ARG HE H 7.42 . 1 254 . 26 ARG CA C 56.3 . 1 255 . 26 ARG CB C 30.1 . 1 256 . 26 ARG CG C 27.2 . 1 257 . 26 ARG CD C 44.0 . 1 258 . 26 ARG N N 116.4 . 1 259 . 26 ARG NE N 85.6 . 1 260 . 27 GLY H H 7.75 . 1 261 . 27 GLY HA2 H 3.58 . 2 262 . 27 GLY HA3 H 4.42 . 2 263 . 27 GLY CA C 45.2 . 1 264 . 27 GLY N N 107.5 . 1 265 . 28 ASP H H 8.04 . 1 266 . 28 ASP HA H 5.07 . 1 267 . 28 ASP HB2 H 2.56 . 2 268 . 28 ASP HB3 H 2.66 . 2 269 . 28 ASP CA C 53.3 . 1 270 . 28 ASP CB C 40.3 . 1 271 . 28 ASP N N 124.3 . 1 272 . 29 THR H H 7.67 . 1 273 . 29 THR HA H 4.34 . 1 274 . 29 THR HB H 4.46 . 1 275 . 29 THR HG2 H 0.81 . 1 276 . 29 THR CA C 61.3 . 1 277 . 29 THR CB C 70.2 . 1 278 . 29 THR CG2 C 21.0 . 1 279 . 29 THR N N 108.6 . 1 280 . 30 HIS H H 8.31 . 1 281 . 30 HIS HA H 4.87 . 1 282 . 30 HIS HB2 H 3.31 . 2 283 . 30 HIS HB3 H 3.41 . 2 284 . 30 HIS HD2 H 7.27 . 1 285 . 30 HIS HE1 H 8.31 . 1 286 . 30 HIS CA C 54.9 . 1 287 . 30 HIS CB C 28.0 . 1 288 . 30 HIS N N 123.0 . 1 289 . 31 PRO HA H 4.83 . 1 290 . 31 PRO HB2 H 1.84 . 2 291 . 31 PRO HB3 H 1.99 . 2 292 . 31 PRO HG2 H 1.97 . 2 293 . 31 PRO HG3 H 2.07 . 2 294 . 31 PRO HD2 H 3.72 . 2 295 . 31 PRO HD3 H 4.08 . 2 296 . 31 PRO CA C 63.0 . 1 297 . 31 PRO CB C 33.5 . 1 298 . 31 PRO CG C 27.7 . 1 299 . 31 PRO CD C 50.8 . 1 300 . 32 LEU H H 8.93 . 1 301 . 32 LEU HA H 5.14 . 1 302 . 32 LEU HB2 H 1.81 . 1 303 . 32 LEU HB3 H 1.94 . 1 304 . 32 LEU HG H 1.80 . 1 305 . 32 LEU HD1 H 0.99 . 1 306 . 32 LEU HD2 H 0.97 . 1 307 . 32 LEU CA C 53.5 . 1 308 . 32 LEU CB C 47.7 . 1 309 . 32 LEU CG C 27.0 . 1 310 . 32 LEU CD1 C 26.6 . 1 311 . 32 LEU CD2 C 23.6 . 1 312 . 32 LEU N N 120.7 . 1 313 . 33 THR H H 9.42 . 1 314 . 33 THR HA H 4.84 . 1 315 . 33 THR HB H 4.92 . 1 316 . 33 THR HG2 H 1.50 . 1 317 . 33 THR CA C 61.2 . 1 318 . 33 THR CB C 71.0 . 1 319 . 33 THR CG2 C 21.9 . 1 320 . 33 THR N N 112.3 . 1 321 . 34 LEU H H 9.35 . 1 322 . 34 LEU HA H 4.18 . 1 323 . 34 LEU HB2 H 1.70 . 1 324 . 34 LEU HB3 H 2.10 . 1 325 . 34 LEU HG H 0.99 . 1 326 . 34 LEU HD1 H 0.75 . 1 327 . 34 LEU HD2 H 0.75 . 1 328 . 34 LEU CA C 58.2 . 1 329 . 34 LEU CB C 41.2 . 1 330 . 34 LEU CG C 27.0 . 1 331 . 34 LEU CD1 C 22.7 . 1 332 . 34 LEU CD2 C 22.7 . 1 333 . 34 LEU N N 121.1 . 1 334 . 35 ASP H H 8.41 . 1 335 . 35 ASP HA H 4.35 . 1 336 . 35 ASP HB2 H 2.59 . 1 337 . 35 ASP HB3 H 2.73 . 1 338 . 35 ASP CA C 58.1 . 1 339 . 35 ASP CB C 40.2 . 1 340 . 35 ASP N N 117.0 . 1 341 . 36 GLU H H 7.88 . 1 342 . 36 GLU HA H 4.20 . 1 343 . 36 GLU HB2 H 2.16 . 1 344 . 36 GLU HB3 H 2.60 . 1 345 . 36 GLU HG2 H 2.42 . 2 346 . 36 GLU HG3 H 2.49 . 2 347 . 36 GLU CA C 59.6 . 1 348 . 36 GLU CB C 30.6 . 1 349 . 36 GLU CG C 38.0 . 1 350 . 36 GLU N N 120.3 . 1 351 . 37 ILE H H 8.14 . 1 352 . 37 ILE HA H 3.48 . 1 353 . 37 ILE HB H 2.12 . 1 354 . 37 ILE HG12 H 1.25 . 2 355 . 37 ILE HG13 H 2.18 . 2 356 . 37 ILE HG2 H 0.87 . 1 357 . 37 ILE HD1 H 0.90 . 1 358 . 37 ILE CA C 66.2 . 1 359 . 37 ILE CB C 38.7 . 1 360 . 37 ILE CG1 C 30.0 . 1 361 . 37 ILE CG2 C 18.6 . 1 362 . 37 ILE CD1 C 14.1 . 1 363 . 37 ILE N N 120.1 . 1 364 . 38 LEU H H 8.92 . 1 365 . 38 LEU HA H 3.90 . 1 366 . 38 LEU HB2 H 2.01 . 1 367 . 38 LEU HB3 H 1.31 . 1 368 . 38 LEU HG H 1.97 . 1 369 . 38 LEU HD1 H 0.93 . 1 370 . 38 LEU HD2 H 0.72 . 1 371 . 38 LEU CA C 57.8 . 1 372 . 38 LEU CB C 40.1 . 1 373 . 38 LEU CG C 25.9 . 1 374 . 38 LEU CD1 C 26.0 . 1 375 . 38 LEU CD2 C 21.4 . 1 376 . 38 LEU N N 120.3 . 1 377 . 39 ASP H H 8.09 . 1 378 . 39 ASP HA H 4.43 . 1 379 . 39 ASP HB2 H 2.92 . 1 380 . 39 ASP HB3 H 2.92 . 1 381 . 39 ASP CA C 57.3 . 1 382 . 39 ASP CB C 41.8 . 1 383 . 39 ASP N N 119.5 . 1 384 . 40 GLU H H 8.05 . 1 385 . 40 GLU HA H 4.11 . 1 386 . 40 GLU HB2 H 1.77 . 1 387 . 40 GLU HB3 H 2.01 . 1 388 . 40 GLU HG2 H 2.44 . 2 389 . 40 GLU HG3 H 2.59 . 2 390 . 40 GLU CA C 58.8 . 1 391 . 40 GLU CB C 29.8 . 1 392 . 40 GLU CG C 34.4 . 1 393 . 40 GLU N N 117.2 . 1 394 . 41 THR H H 7.58 . 1 395 . 41 THR HA H 4.16 . 1 396 . 41 THR HB H 4.25 . 1 397 . 41 THR HG2 H 0.82 . 1 398 . 41 THR CA C 61.5 . 1 399 . 41 THR CB C 69.9 . 1 400 . 41 THR CG2 C 21.5 . 1 401 . 41 THR N N 106.3 . 1 402 . 42 GLN H H 7.76 . 1 403 . 42 GLN HA H 4.08 . 1 404 . 42 GLN HB2 H 2.14 . 1 405 . 42 GLN HB3 H 2.14 . 1 406 . 42 GLN HG2 H 2.26 . 2 407 . 42 GLN HG3 H 2.33 . 2 408 . 42 GLN HE21 H 6.70 . 2 409 . 42 GLN HE22 H 7.53 . 2 410 . 42 GLN CA C 56.8 . 1 411 . 42 GLN CB C 26.4 . 1 412 . 42 GLN N N 117.2 . 1 413 . 42 GLN NE2 N 113.0 . 1 414 . 43 HIS H H 8.82 . 1 415 . 43 HIS HA H 4.97 . 1 416 . 43 HIS HB2 H 2.79 . 2 417 . 43 HIS HB3 H 3.56 . 2 418 . 43 HIS HD2 H 7.05 . 1 419 . 43 HIS HE1 H 8.04 . 1 420 . 43 HIS CA C 56.0 . 1 421 . 43 HIS CB C 29.7 . 1 422 . 43 HIS N N 117.7 . 1 423 . 44 LEU H H 8.16 . 1 424 . 44 LEU HA H 4.22 . 1 425 . 44 LEU HB2 H 1.60 . 2 426 . 44 LEU HB3 H 1.72 . 2 427 . 44 LEU HG H 1.59 . 1 428 . 44 LEU HD1 H 0.92 . 2 429 . 44 LEU HD2 H 0.97 . 2 430 . 44 LEU CA C 56.4 . 1 431 . 44 LEU CB C 42.3 . 1 432 . 44 LEU CG C 27.1 . 1 433 . 44 LEU CD1 C 23.7 . 2 434 . 44 LEU CD2 C 24.3 . 2 435 . 44 LEU N N 119.8 . 1 436 . 45 ASP H H 8.52 . 1 437 . 45 ASP HA H 4.68 . 1 438 . 45 ASP HB2 H 2.73 . 2 439 . 45 ASP HB3 H 2.77 . 2 440 . 45 ASP CA C 53.7 . 1 441 . 45 ASP CB C 40.3 . 1 442 . 45 ASP N N 117.9 . 1 443 . 46 ILE H H 7.49 . 1 444 . 46 ILE HA H 4.32 . 1 445 . 46 ILE HB H 2.16 . 1 446 . 46 ILE HG12 H 1.57 . 2 447 . 46 ILE HG13 H 1.65 . 2 448 . 46 ILE HG2 H 1.10 . 1 449 . 46 ILE HD1 H 0.85 . 1 450 . 46 ILE CA C 62.1 . 1 451 . 46 ILE CB C 38.8 . 1 452 . 46 ILE CG1 C 25.7 . 1 453 . 46 ILE CG2 C 17.2 . 1 454 . 46 ILE N N 117.7 . 1 455 . 47 GLY H H 8.47 . 1 456 . 47 GLY HA2 H 4.16 . 2 457 . 47 GLY HA3 H 4.27 . 2 458 . 47 GLY CA C 45.0 . 1 459 . 47 GLY N N 111.6 . 1 460 . 48 LEU H H 8.45 . 1 461 . 48 LEU HA H 4.10 . 1 462 . 48 LEU HB2 H 1.76 . 2 463 . 48 LEU HB3 H 1.83 . 2 464 . 48 LEU HG H 1.75 . 1 465 . 48 LEU HD1 H 1.00 . 2 466 . 48 LEU HD2 H 1.06 . 2 467 . 48 LEU CA C 58.6 . 1 468 . 48 LEU CB C 42.1 . 1 469 . 48 LEU CG C 26.9 . 1 470 . 48 LEU CD1 C 24.0 . 1 471 . 48 LEU CD2 C 24.0 . 1 472 . 48 LEU N N 122.2 . 1 473 . 49 LYS H H 8.66 . 1 474 . 49 LYS HA H 4.20 . 1 475 . 49 LYS HB2 H 1.90 . 2 476 . 49 LYS HB3 H 1.99 . 2 477 . 49 LYS HG2 H 1.52 . 2 478 . 49 LYS HG3 H 1.66 . 2 479 . 49 LYS HD2 H 1.79 . 1 480 . 49 LYS HD3 H 1.79 . 1 481 . 49 LYS HE2 H 3.08 . 1 482 . 49 LYS HE3 H 3.08 . 1 483 . 49 LYS CA C 59.7 . 1 484 . 49 LYS CB C 31.8 . 1 485 . 49 LYS CG C 25.4 . 1 486 . 49 LYS CD C 29.1 . 1 487 . 49 LYS CE C 42.2 . 1 488 . 49 LYS N N 118.3 . 1 489 . 50 GLN H H 8.03 . 1 490 . 50 GLN HA H 4.38 . 1 491 . 50 GLN HB2 H 2.29 . 1 492 . 50 GLN HB3 H 2.07 . 1 493 . 50 GLN HG2 H 2.45 . 1 494 . 50 GLN HG3 H 2.45 . 1 495 . 50 GLN HE21 H 6.65 . 2 496 . 50 GLN HE22 H 7.24 . 2 497 . 50 GLN CA C 59.4 . 1 498 . 50 GLN CB C 28.0 . 1 499 . 50 GLN CG C 35.0 . 1 500 . 50 GLN N N 119.9 . 1 501 . 50 GLN NE2 N 110.3 . 1 502 . 51 LYS H H 8.42 . 1 503 . 51 LYS HA H 3.91 . 1 504 . 51 LYS HB2 H 2.00 . 1 505 . 51 LYS HB3 H 2.00 . 1 506 . 51 LYS HG2 H 1.34 . 2 507 . 51 LYS HG3 H 1.54 . 2 508 . 51 LYS HD2 H 1.74 . 1 509 . 51 LYS HD3 H 1.74 . 1 510 . 51 LYS HE2 H 2.85 . 2 511 . 51 LYS HE3 H 2.90 . 2 512 . 51 LYS CA C 61.4 . 1 513 . 51 LYS CB C 32.6 . 1 514 . 51 LYS CG C 26.7 . 1 515 . 51 LYS CD C 29.9 . 1 516 . 51 LYS CE C 42.1 . 1 517 . 51 LYS N N 121.1 . 1 518 . 52 GLN H H 8.64 . 1 519 . 52 GLN HA H 4.14 . 1 520 . 52 GLN HB2 H 2.35 . 1 521 . 52 GLN HB3 H 2.25 . 1 522 . 52 GLN HG2 H 2.49 . 2 523 . 52 GLN HG3 H 2.63 . 2 524 . 52 GLN HE21 H 6.80 . 2 525 . 52 GLN HE22 H 7.45 . 2 526 . 52 GLN CA C 59.4 . 1 527 . 52 GLN CB C 28.0 . 1 528 . 52 GLN CG C 34.0 . 1 529 . 52 GLN N N 117.8 . 1 530 . 52 GLN NE2 N 111.4 . 1 531 . 53 TRP H H 8.22 . 1 532 . 53 TRP HA H 4.40 . 1 533 . 53 TRP HB2 H 3.46 . 2 534 . 53 TRP HB3 H 3.66 . 2 535 . 53 TRP HD1 H 7.37 . 1 536 . 53 TRP HE1 H 10.23 . 1 537 . 53 TRP HE3 H 7.64 . 1 538 . 53 TRP HZ2 H 7.37 . 1 539 . 53 TRP HZ3 H 6.81 . 1 540 . 53 TRP HH2 H 6.77 . 1 541 . 53 TRP CA C 61.7 . 1 542 . 53 TRP CB C 27.6 . 1 543 . 53 TRP N N 124.0 . 1 544 . 53 TRP NE1 N 131.1 . 1 545 . 54 LEU H H 8.51 . 1 546 . 54 LEU HA H 3.46 . 1 547 . 54 LEU HB2 H 2.32 . 1 548 . 54 LEU HB3 H 1.06 . 1 549 . 54 LEU HG H 2.15 . 1 550 . 54 LEU HD1 H 0.83 . 1 551 . 54 LEU HD2 H 0.63 . 1 552 . 54 LEU CA C 58.5 . 1 553 . 54 LEU CB C 42.3 . 1 554 . 54 LEU CG C 26.9 . 1 555 . 54 LEU CD1 C 23.9 . 1 556 . 54 LEU CD2 C 26.8 . 1 557 . 54 LEU N N 121.5 . 1 558 . 55 MET H H 7.95 . 1 559 . 55 MET HA H 4.02 . 1 560 . 55 MET HB2 H 2.21 . 1 561 . 55 MET HB3 H 2.21 . 1 562 . 55 MET HG2 H 2.65 . 2 563 . 55 MET HG3 H 2.75 . 2 564 . 55 MET CA C 59.0 . 1 565 . 55 MET CB C 34.9 . 1 566 . 55 MET CG C 32.1 . 1 567 . 55 MET N N 113.1 . 1 568 . 56 THR H H 8.28 . 1 569 . 56 THR HA H 4.44 . 1 570 . 56 THR HB H 4.34 . 1 571 . 56 THR HG2 H 1.38 . 1 572 . 56 THR CA C 63.2 . 1 573 . 56 THR CB C 70.8 . 1 574 . 56 THR CG2 C 21.6 . 1 575 . 56 THR N N 106.8 . 1 576 . 57 GLU H H 7.68 . 1 577 . 57 GLU HA H 4.51 . 1 578 . 57 GLU HB2 H 1.79 . 2 579 . 57 GLU HB3 H 1.89 . 2 580 . 57 GLU HG2 H 2.18 . 2 581 . 57 GLU HG3 H 2.26 . 2 582 . 57 GLU CA C 57.7 . 1 583 . 57 GLU CB C 32.1 . 1 584 . 57 GLU CG C 36.2 . 1 585 . 57 GLU N N 120.1 . 1 586 . 58 ALA H H 7.39 . 1 587 . 58 ALA HA H 3.89 . 1 588 . 58 ALA HB H 0.36 . 1 589 . 58 ALA CA C 55.4 . 1 590 . 58 ALA CB C 19.6 . 1 591 . 58 ALA N N 121.0 . 1 592 . 59 LEU H H 8.42 . 1 593 . 59 LEU HA H 3.99 . 1 594 . 59 LEU HB2 H 1.65 . 1 595 . 59 LEU HB3 H 1.32 . 1 596 . 59 LEU HG H 1.24 . 1 597 . 59 LEU HD1 H 0.07 . 1 598 . 59 LEU HD2 H 0.46 . 1 599 . 59 LEU CA C 56.2 . 1 600 . 59 LEU CB C 41.0 . 1 601 . 59 LEU CG C 26.9 . 1 602 . 59 LEU CD1 C 24.7 . 1 603 . 59 LEU CD2 C 22.1 . 1 604 . 59 LEU N N 113.6 . 1 605 . 60 VAL H H 6.42 . 1 606 . 60 VAL HA H 3.96 . 1 607 . 60 VAL HB H 1.99 . 1 608 . 60 VAL HG1 H 0.97 . 1 609 . 60 VAL HG2 H 0.82 . 1 610 . 60 VAL CA C 62.6 . 1 611 . 60 VAL CB C 32.2 . 1 612 . 60 VAL CG1 C 20.6 . 1 613 . 60 VAL CG2 C 21.4 . 1 614 . 60 VAL N N 112.2 . 1 615 . 61 ASN HA H 4.74 . 1 616 . 61 ASN HB2 H 2.77 . 2 617 . 61 ASN HB3 H 2.99 . 2 618 . 61 ASN HD21 H 6.96 . 2 619 . 61 ASN HD22 H 7.68 . 2 620 . 61 ASN CA C 53.4 . 1 621 . 61 ASN CB C 38.6 . 1 622 . 61 ASN ND2 N 114.4 . 1 623 . 62 ASN H H 8.26 . 1 624 . 62 ASN HA H 5.09 . 1 625 . 62 ASN HB2 H 2.76 . 1 626 . 62 ASN HB3 H 2.76 . 1 627 . 62 ASN HD21 H 6.88 . 2 628 . 62 ASN HD22 H 7.42 . 2 629 . 62 ASN CA C 51.6 . 1 630 . 62 ASN CB C 40.8 . 1 631 . 62 ASN N N 121.5 . 1 632 . 62 ASN ND2 N 111.8 . 1 633 . 63 PRO HA H 4.44 . 1 634 . 63 PRO HB2 H 1.98 . 2 635 . 63 PRO HB3 H 2.40 . 2 636 . 63 PRO HG2 H 1.99 . 2 637 . 63 PRO HG3 H 2.13 . 2 638 . 63 PRO HD2 H 3.77 . 2 639 . 63 PRO HD3 H 4.01 . 2 640 . 63 PRO CA C 64.5 . 1 641 . 63 PRO CB C 32.7 . 1 642 . 63 PRO CG C 27.4 . 1 643 . 63 PRO CD C 51.5 . 1 644 . 64 LYS H H 8.15 . 1 645 . 64 LYS HA H 4.35 . 1 646 . 64 LYS HB2 H 1.63 . 1 647 . 64 LYS HB3 H 2.05 . 1 648 . 64 LYS HG2 H 1.31 . 2 649 . 64 LYS HG3 H 1.42 . 2 650 . 64 LYS HD2 H 1.75 . 1 651 . 64 LYS HD3 H 1.75 . 1 652 . 64 LYS HE2 H 3.04 . 1 653 . 64 LYS HE3 H 3.04 . 1 654 . 64 LYS CA C 55.9 . 1 655 . 64 LYS CB C 33.1 . 1 656 . 64 LYS CG C 25.5 . 1 657 . 64 LYS CD C 29.4 . 1 658 . 64 LYS CE C 42.4 . 1 659 . 64 LYS N N 115.3 . 1 660 . 65 ILE H H 7.50 . 1 661 . 65 ILE HA H 5.00 . 1 662 . 65 ILE HB H 2.08 . 1 663 . 65 ILE HG12 H 1.23 . 2 664 . 65 ILE HG13 H 1.43 . 2 665 . 65 ILE HG2 H 1.09 . 1 666 . 65 ILE HD1 H 0.82 . 1 667 . 65 ILE CA C 56.8 . 1 668 . 65 ILE CB C 38.8 . 1 669 . 65 ILE CG1 C 25.8 . 1 670 . 65 ILE CG2 C 18.0 . 1 671 . 65 ILE CD1 C 9.8 . 1 672 . 65 ILE N N 119.1 . 1 673 . 66 GLU H H 9.23 . 1 674 . 66 GLU HA H 4.76 . 1 675 . 66 GLU HB2 H 1.76 . 2 676 . 66 GLU HB3 H 1.86 . 2 677 . 66 GLU HG2 H 2.11 . 1 678 . 66 GLU HG3 H 2.11 . 1 679 . 66 GLU CA C 54.1 . 1 680 . 66 GLU CB C 32.9 . 1 681 . 66 GLU CG C 36.1 . 1 682 . 66 GLU N N 128.4 . 1 683 . 67 VAL H H 8.57 . 1 684 . 67 VAL HA H 4.73 . 1 685 . 67 VAL HB H 2.02 . 1 686 . 67 VAL HG1 H 0.73 . 1 687 . 67 VAL HG2 H 1.00 . 1 688 . 67 VAL CA C 61.2 . 1 689 . 67 VAL CB C 31.7 . 1 690 . 67 VAL CG1 C 20.4 . 1 691 . 67 VAL CG2 C 21.3 . 1 692 . 67 VAL N N 126.2 . 1 693 . 68 ILE H H 8.91 . 1 694 . 68 ILE HA H 4.27 . 1 695 . 68 ILE HB H 1.54 . 1 696 . 68 ILE HG12 H 1.03 . 2 697 . 68 ILE HG13 H 1.33 . 2 698 . 68 ILE HG2 H 0.85 . 1 699 . 68 ILE HD1 H 0.82 . 1 700 . 68 ILE CA C 59.9 . 1 701 . 68 ILE CB C 40.3 . 1 702 . 68 ILE CG1 C 27.2 . 1 703 . 68 ILE CG2 C 16.6 . 1 704 . 68 ILE CD1 C 13.7 . 1 705 . 68 ILE N N 129.5 . 1 706 . 69 ASP H H 9.21 . 1 707 . 69 ASP HA H 4.25 . 1 708 . 69 ASP HB2 H 2.94 . 1 709 . 69 ASP HB3 H 2.55 . 1 710 . 69 ASP CA C 55.3 . 1 711 . 69 ASP CB C 40.0 . 1 712 . 69 ASP N N 128.8 . 1 713 . 70 GLY H H 8.00 . 1 714 . 70 GLY HA2 H 3.42 . 2 715 . 70 GLY HA3 H 4.01 . 2 716 . 70 GLY CA C 45.5 . 1 717 . 70 GLY N N 103.1 . 1 718 . 71 LYS H H 7.62 . 1 719 . 71 LYS HA H 4.33 . 1 720 . 71 LYS HB2 H 1.68 . 1 721 . 71 LYS HB3 H 1.48 . 1 722 . 71 LYS HG2 H 1.62 . 1 723 . 71 LYS HG3 H 1.62 . 1 724 . 71 LYS HD2 H 1.17 . 2 725 . 71 LYS HD3 H 1.42 . 2 726 . 71 LYS HE2 H 3.00 . 1 727 . 71 LYS HE3 H 3.00 . 1 728 . 71 LYS CA C 54.7 . 1 729 . 71 LYS CB C 36.6 . 1 730 . 71 LYS CG C 29.5 . 1 731 . 71 LYS CD C 25.8 . 1 732 . 71 LYS N N 120.6 . 1 733 . 72 TYR H H 9.12 . 1 734 . 72 TYR HA H 5.35 . 1 735 . 72 TYR HB2 H 2.81 . 1 736 . 72 TYR HB3 H 2.81 . 1 737 . 72 TYR HD1 H 7.06 . 1 738 . 72 TYR HD2 H 7.06 . 1 739 . 72 TYR HE1 H 6.74 . 1 740 . 72 TYR HE2 H 6.74 . 1 741 . 72 TYR CA C 57.9 . 1 742 . 72 TYR CB C 41.5 . 1 743 . 72 TYR N N 117.5 . 1 744 . 73 ALA H H 9.09 . 1 745 . 73 ALA HA H 4.76 . 1 746 . 73 ALA HB H 1.49 . 1 747 . 73 ALA CA C 50.3 . 1 748 . 73 ALA CB C 22.9 . 1 749 . 73 ALA N N 122.9 . 1 750 . 74 PHE H H 8.80 . 1 751 . 74 PHE HA H 4.85 . 1 752 . 74 PHE HB2 H 2.93 . 1 753 . 74 PHE HB3 H 2.71 . 1 754 . 74 PHE HD1 H 6.68 . 1 755 . 74 PHE HD2 H 6.68 . 1 756 . 74 PHE HE1 H 7.21 . 1 757 . 74 PHE HE2 H 7.21 . 1 758 . 74 PHE HZ H 7.42 . 1 759 . 74 PHE CA C 57.9 . 1 760 . 74 PHE CB C 41.1 . 1 761 . 74 PHE N N 121.7 . 1 762 . 75 LYS H H 7.38 . 1 763 . 75 LYS HA H 4.47 . 1 764 . 75 LYS HB2 H 1.09 . 1 765 . 75 LYS HB3 H 1.54 . 1 766 . 75 LYS HG2 H 1.14 . 2 767 . 75 LYS HG3 H 1.2 . 2 768 . 75 LYS HD2 H 1.55 . 1 769 . 75 LYS HD3 H 1.55 . 1 770 . 75 LYS HE2 H 2.90 . 1 771 . 75 LYS HE3 H 2.90 . 1 772 . 75 LYS CA C 52.3 . 1 773 . 75 LYS CB C 33.8 . 1 774 . 75 LYS CG C 24.5 . 1 775 . 75 LYS CD C 29.2 . 1 776 . 75 LYS CE C 42.1 . 1 777 . 75 LYS N N 129.2 . 1 778 . 76 PRO HA H 4.17 . 1 779 . 76 PRO HB2 H 1.83 . 2 780 . 76 PRO HB3 H 2.14 . 2 781 . 76 PRO HG2 H 1.82 . 2 782 . 76 PRO HG3 H 1.95 . 2 783 . 76 PRO HD2 H 3.29 . 2 784 . 76 PRO HD3 H 3.60 . 2 785 . 76 PRO CA C 62.5 . 1 786 . 76 PRO CB C 32.4 . 1 787 . 76 PRO CG C 27.0 . 1 788 . 76 PRO CD C 50.6 . 1 789 . 77 LYS H H 8.16 . 1 790 . 77 LYS HA H 4.18 . 1 791 . 77 LYS HB2 H 1.74 . 1 792 . 77 LYS HB3 H 1.74 . 1 793 . 77 LYS HG2 H 1.28 . 2 794 . 77 LYS HG3 H 1.36 . 2 795 . 77 LYS HD2 H 1.70 . 1 796 . 77 LYS HD3 H 1.70 . 1 797 . 77 LYS HE2 H 3.03 . 1 798 . 77 LYS HE3 H 3.03 . 1 799 . 77 LYS CA C 56.6 . 1 800 . 77 LYS CB C 33.1 . 1 801 . 77 LYS CG C 24.6 . 1 802 . 77 LYS CD C 29.1 . 1 803 . 77 LYS CE C 42.3 . 1 804 . 77 LYS N N 120.9 . 1 805 . 78 TYR H H 8.06 . 1 806 . 78 TYR HA H 4.63 . 1 807 . 78 TYR HB2 H 2.98 . 2 808 . 78 TYR HB3 H 3.10 . 2 809 . 78 TYR HD1 H 7.19 . 1 810 . 78 TYR HD2 H 7.19 . 1 811 . 78 TYR HE1 H 6.90 . 1 812 . 78 TYR HE2 H 6.90 . 1 813 . 78 TYR CA C 57.6 . 1 814 . 78 TYR CB C 39.0 . 1 815 . 78 TYR N N 121.1 . 1 816 . 79 ASN H H 8.40 . 1 817 . 79 ASN HA H 4.74 . 1 818 . 79 ASN HB2 H 2.71 . 2 819 . 79 ASN HB3 H 2.81 . 2 820 . 79 ASN HD21 H 6.84 . 2 821 . 79 ASN HD22 H 7.53 . 2 822 . 79 ASN CA C 53.1 . 1 823 . 79 ASN CB C 39.0 . 1 824 . 79 ASN N N 121.3 . 1 825 . 79 ASN ND2 N 113.1 . 1 826 . 80 VAL H H 8.01 . 1 827 . 80 VAL HA H 4.16 . 1 828 . 80 VAL HB H 2.16 . 1 829 . 80 VAL HG1 H 0.99 . 1 830 . 80 VAL HG2 H 0.99 . 1 831 . 80 VAL CA C 62.5 . 1 832 . 80 VAL CB C 32.7 . 1 833 . 80 VAL CG1 C 20.8 . 1 834 . 80 VAL CG2 C 20.8 . 1 835 . 80 VAL N N 120.7 . 1 836 . 81 ARG H H 7.99 . 1 837 . 81 ARG HA H 4.23 . 1 838 . 81 ARG HB2 H 1.79 . 2 839 . 81 ARG HB3 H 1.90 . 2 840 . 81 ARG HG2 H 1.64 . 1 841 . 81 ARG HG3 H 1.64 . 1 842 . 81 ARG HD2 H 3.25 . 1 843 . 81 ARG HD3 H 3.25 . 1 844 . 81 ARG HE H 7.23 . 1 845 . 81 ARG CA C 57.6 . 1 846 . 81 ARG CB C 31.6 . 1 847 . 81 ARG CG C 27.1 . 1 848 . 81 ARG CD C 43.6 . 1 849 . 81 ARG N N 129.7 . 1 850 . 81 ARG NE N 85.5 . 1 stop_ save_