data_10135 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N assignment of reduced Hydrogenobacter thermophilus cytochrome c552 ; _BMRB_accession_number 10135 _BMRB_flat_file_name bmr10135.str _Entry_type original _Submission_date 2007-04-15 _Accession_date 2007-04-16 _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 Takayama Shin-ichi J. . 2 Takahashi Yo-ta . . 3 Mikami Shin-ichi . . 4 Irie Kiyofumi . . 5 Kawano Shin . . 6 Yamamoto Yasuhiko . . 7 Hemmi Hikaru . . 8 Kitahara Ryo . . 9 Yokoyama Shigeyuki . . 10 Akasaka Kazuyuki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 75 "15N chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-02-11 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 10134 '1H and 15N assignment of oxidized form of Hydrogenobacter thermophilus cytochrome c-552' 4578 '1H, 13C and 15N assignment of F7A/V13M/F34Y/E43Y/V78I variant of homologous protein, Pseudomonas aeruginosa cytochrome c-551' 5086 '1H assignment of reduced periplasmic Hydrogenobacter thermophilus cytochrome c-552' 5087 '1H assignment of oxidized periplasmic Hydrogenobacter thermophilus cytochrome c-552' 5088 '1H assignment of reduced cytosolic Hydrogenobacter thermophilus cytochrome c-552' 5089 '1H assignment of oxidized cytosolic Hydrogenobacter thermophilus cytochrome c-552' 6033 '1H and 15N assignment of C10A/C13A variant of Hydrogenobacter thermophilus cytochrome c-552' stop_ _Original_release_date 2008-02-11 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17658890 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takayama Shin-ichi J. . 2 Takahashi Yo-ta . . 3 Mikami Shin-ichi . . 4 Irie Kiyofumi . . 5 Kawano Shin . . 6 Yamamoto Yasuhiko . . 7 Hemmi Hikaru . . 8 Kitahara Ryo . . 9 Yokoyama Shigeyuki . . 10 Akasaka Kazuyuki . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9215 _Page_last 9224 _Year 2007 _Details . loop_ _Keyword 'Cytochrome c' 'High-pressure NMR' 'Hydrogen bond' 'Paramagnetic NMR' 'Redox potential' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'cytochrome c552' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome c' $cytc 'reduced heme' $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c552' _Abbreviation_common 'cyt c-552' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 80 _Mol_residue_sequence ; NEQLAKQKGCMACHDLKAKK VGPAYADVAKKYAGRKDAVD YLAGKIKKGGSGVWGSVPMP PQNVTDAEAKQLAQWILSIK ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 GLU 3 GLN 4 LEU 5 ALA 6 LYS 7 GLN 8 LYS 9 GLY 10 CYS 11 MET 12 ALA 13 CYS 14 HIS 15 ASP 16 LEU 17 LYS 18 ALA 19 LYS 20 LYS 21 VAL 22 GLY 23 PRO 24 ALA 25 TYR 26 ALA 27 ASP 28 VAL 29 ALA 30 LYS 31 LYS 32 TYR 33 ALA 34 GLY 35 ARG 36 LYS 37 ASP 38 ALA 39 VAL 40 ASP 41 TYR 42 LEU 43 ALA 44 GLY 45 LYS 46 ILE 47 LYS 48 LYS 49 GLY 50 GLY 51 SER 52 GLY 53 VAL 54 TRP 55 GLY 56 SER 57 VAL 58 PRO 59 MET 60 PRO 61 PRO 62 GLN 63 ASN 64 VAL 65 THR 66 ASP 67 ALA 68 GLU 69 ALA 70 LYS 71 GLN 72 LEU 73 ALA 74 GLN 75 TRP 76 ILE 77 LEU 78 SER 79 ILE 80 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-20 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 10134 "cytochrome c552" 100.00 80 100.00 100.00 7.15e-49 BMRB 17053 Cc6 100.00 80 100.00 100.00 7.15e-49 BMRB 25389 wt_cytc 100.00 80 100.00 100.00 7.15e-49 BMRB 25390 axxa_cytc 100.00 80 97.50 97.50 6.34e-47 PDB 1AYG "Solution Structure Of Cytochrome C-552, Nmr, 20 Structures" 98.75 80 100.00 100.00 7.67e-48 PDB 1YNR "Crystal Structure Of The Cytochrome C-552 From Hydrogenobacter Thermophilus At 2.0 Resolution" 100.00 80 100.00 100.00 7.15e-49 PDB 2AI5 "Solution Structure Of Cytochrome C552, Determined By Distributed Computing Implementation For Nmr Data" 98.75 80 100.00 100.00 7.67e-48 PDB 3VYM "Dimeric Hydrogenobacter Thermophilus Cytochrome C552" 100.00 80 100.00 100.00 7.15e-49 DBJ BAI69446 "cytochrome c-552 [Hydrogenobacter thermophilus TK-6]" 100.00 98 100.00 100.00 2.95e-49 EMBL CAA40902 "cytochrome c-552 [Hydrogenobacter thermophilus TK-6]" 100.00 98 100.00 100.00 2.95e-49 GB ADO45379 "cytochrome c class I [Hydrogenobacter thermophilus TK-6]" 100.00 98 100.00 100.00 2.95e-49 REF WP_012963626 "cytochrome c-552 [Hydrogenobacter thermophilus]" 100.00 98 100.00 100.00 2.95e-49 SP P15452 "RecName: Full=Cytochrome c-552; AltName: Full=Cytochrome c552; Flags: Precursor" 100.00 98 100.00 100.00 2.95e-49 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Sep 21 16:27:30 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cytc 'Hydrogenobacter thermophilus' 940 Eubacteria . Hydrogenobacter thermophilus 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 $cytc 'recombinant technology' 'E. coli' Escherichia coli . plasmid pKK223-3 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 $cytc 1 mM [U-15N] 'potassium phosphate' 20 mM . 'sodium hydrosulfite' 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label $sample_1 save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH temperature 296 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_Ref_1 _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 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $Ref_1 _Mol_system_component_name 'cytochrome c' _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 2 GLU H H 7.706 0.02 1 2 2 2 GLU N N 119.04 0.05 1 3 3 3 GLN H H 7.814 0.02 1 4 3 3 GLN N N 118.394 0.05 1 5 4 4 LEU H H 7.806 0.02 1 6 4 4 LEU N N 123.518 0.05 1 7 5 5 ALA H H 7.886 0.02 1 8 5 5 ALA N N 121.433 0.05 1 9 6 6 LYS H H 8.143 0.02 1 10 6 6 LYS N N 117.229 0.05 1 11 7 7 GLN H H 8.505 0.02 1 12 7 7 GLN N N 122.115 0.05 1 13 8 8 LYS H H 8.472 0.02 1 14 8 8 LYS N N 115.093 0.05 1 15 9 9 GLY H H 7.923 0.02 1 16 9 9 GLY N N 107.41 0.05 1 17 10 10 CYS H H 8.921 0.02 1 18 10 10 CYS N N 120.21 0.05 1 19 11 11 MET H H 7.948 0.02 1 20 11 11 MET N N 111.896 0.05 1 21 12 12 ALA H H 7.628 0.02 1 22 12 12 ALA N N 121.477 0.05 1 23 13 13 CYS H H 6.544 0.02 1 24 13 13 CYS N N 110.772 0.05 1 25 14 14 HIS H H 6.727 0.02 1 26 14 14 HIS N N 120.441 0.05 1 27 15 15 ASP H H 7.59 0.02 1 28 15 15 ASP N N 119.468 0.05 1 29 16 16 LEU H H 8.281 0.02 1 30 16 16 LEU N N 120.51 0.05 1 31 17 17 LYS H H 8.218 0.02 1 32 17 17 LYS N N 124.948 0.05 1 33 18 18 ALA H H 8.145 0.02 1 34 18 18 ALA N N 124.49 0.05 1 35 19 19 LYS H H 8.375 0.02 1 36 19 19 LYS N N 122.856 0.05 1 37 20 20 LYS H H 7.471 0.02 1 38 20 20 LYS N N 131.075 0.05 1 39 21 21 VAL H H 7.131 0.02 1 40 21 21 VAL N N 122.937 0.05 1 41 22 22 GLY H H 6.58 0.02 1 42 22 22 GLY N N 104.294 0.05 1 43 24 24 ALA H H 8.36 0.02 1 44 24 24 ALA N N 123.556 0.05 1 45 25 25 TYR H H 7.765 0.02 1 46 25 25 TYR N N 123.034 0.05 1 47 26 26 ALA H H 8.769 0.02 1 48 26 26 ALA N N 119.74 0.05 1 49 27 27 ASP H H 6.785 0.02 1 50 27 27 ASP N N 117.649 0.05 1 51 28 28 VAL H H 7.628 0.02 1 52 28 28 VAL N N 124.792 0.05 1 53 29 29 ALA H H 8.423 0.02 1 54 29 29 ALA N N 121.474 0.05 1 55 30 30 LYS H H 7.37 0.02 1 56 30 30 LYS N N 115.459 0.05 1 57 31 31 LYS H H 7.973 0.02 1 58 31 31 LYS N N 117.638 0.05 1 59 32 32 TYR H H 7.492 0.02 1 60 32 32 TYR N N 113.343 0.05 1 61 33 33 ALA H H 7.467 0.02 1 62 33 33 ALA N N 123.928 0.05 1 63 34 34 GLY H H 8.803 0.02 1 64 34 34 GLY N N 109.083 0.05 1 65 35 35 ARG H H 7.873 0.02 1 66 35 35 ARG N N 122.293 0.05 1 67 36 36 LYS H H 9.246 0.02 1 68 36 36 LYS N N 130.002 0.05 1 69 37 37 ASP H H 8.783 0.02 1 70 37 37 ASP N N 118.304 0.05 1 71 38 38 ALA H H 7.452 0.02 1 72 38 38 ALA N N 121.5 0.05 1 73 39 39 VAL H H 8.451 0.02 1 74 39 39 VAL N N 117.028 0.05 1 75 40 40 ASP H H 7.73 0.02 1 76 40 40 ASP N N 119.72 0.05 1 77 41 41 TYR H H 8.518 0.02 1 78 41 41 TYR N N 121.46 0.05 1 79 42 42 LEU H H 8.829 0.02 1 80 42 42 LEU N N 120.659 0.05 1 81 43 43 ALA H H 8.785 0.02 1 82 43 43 ALA N N 121.455 0.05 1 83 44 44 GLY H H 7.355 0.02 1 84 44 44 GLY N N 103.264 0.05 1 85 45 45 LYS H H 7.143 0.02 1 86 45 45 LYS N N 121.455 0.05 1 87 46 46 ILE H H 7.982 0.02 1 88 46 46 ILE N N 120.434 0.05 1 89 47 47 LYS H H 6.788 0.02 1 90 47 47 LYS N N 113.951 0.05 1 91 48 48 LYS H H 7.882 0.02 1 92 48 48 LYS N N 114.58 0.05 1 93 49 49 GLY H H 7.003 0.02 1 94 49 49 GLY N N 108.609 0.05 1 95 50 50 GLY H H 7.44 0.02 1 96 50 50 GLY N N 104.342 0.05 1 97 51 51 SER H H 8.066 0.02 1 98 51 51 SER N N 111.35 0.05 1 99 52 52 GLY H H 8.047 0.02 1 100 52 52 GLY N N 107.375 0.05 1 101 53 53 VAL H H 10.379 0.02 1 102 53 53 VAL N N 127.899 0.05 1 103 54 54 TRP H H 10.56 0.02 1 104 54 54 TRP N N 122.975 0.05 1 105 55 55 GLY H H 8.077 0.02 1 106 55 55 GLY N N 110.145 0.05 1 107 56 56 SER H H 8.881 0.02 1 108 56 56 SER N N 113.421 0.05 1 109 57 57 VAL H H 7.776 0.02 1 110 57 57 VAL N N 125.861 0.05 1 111 59 59 MET H H 8.562 0.02 1 112 59 59 MET N N 122.514 0.05 1 113 62 62 GLN H H 7.281 0.02 1 114 62 62 GLN N N 119.661 0.05 1 115 63 63 ASN H H 8.968 0.02 1 116 63 63 ASN N N 123.62 0.05 1 117 64 64 VAL H H 7.445 0.02 1 118 64 64 VAL N N 114.301 0.05 1 119 65 65 THR H H 9.189 0.02 1 120 65 65 THR N N 114.561 0.05 1 121 66 66 ASP H H 8.927 0.02 1 122 66 66 ASP N N 121.81 0.05 1 123 67 67 ALA H H 8.41 0.02 1 124 67 67 ALA N N 121.865 0.05 1 125 68 68 GLU H H 7.941 0.02 1 126 68 68 GLU N N 120.665 0.05 1 127 69 69 ALA H H 8.89 0.02 1 128 69 69 ALA N N 122.136 0.05 1 129 70 70 LYS H H 8.011 0.02 1 130 70 70 LYS N N 113.505 0.05 1 131 71 71 GLN H H 8.093 0.02 1 132 71 71 GLN N N 120.514 0.05 1 133 72 72 LEU H H 8.956 0.02 1 134 72 72 LEU N N 121.275 0.05 1 135 73 73 ALA H H 8.612 0.02 1 136 73 73 ALA N N 122.398 0.05 1 137 74 74 GLN H H 8.491 0.02 1 138 74 74 GLN N N 115.37 0.05 1 139 75 75 TRP H H 8.127 0.02 1 140 75 75 TRP N N 120.998 0.05 1 141 76 76 ILE H H 8.793 0.02 1 142 76 76 ILE N N 124.174 0.05 1 143 77 77 LEU H H 7.715 0.02 1 144 77 77 LEU N N 114.314 0.05 1 145 78 78 SER H H 7.79 0.02 1 146 78 78 SER N N 116.065 0.05 1 147 79 79 ILE H H 7.227 0.02 1 148 79 79 ILE N N 126.037 0.05 1 149 80 80 LYS H H 7.726 0.02 1 150 80 80 LYS N N 132.494 0.05 1 stop_ save_