data_5466 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural model for an alkaline form of ferricytochrome c ; _BMRB_accession_number 5466 _BMRB_flat_file_name bmr5466.str _Entry_type original _Submission_date 2002-07-16 _Accession_date 2002-07-16 _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 Assfalg M. . . 2 Bertini I. . . 3 Dolfi A. . . 4 Turano P. . . 5 Mauk A. G. . 6 Rosell F. I. . 7 Gray H. B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 348 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-04-23 original author . stop_ _Original_release_date 2003-04-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Model for an Alkaline form of Ferricytochrome C' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22505586 _PubMed_ID 12617658 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Assfalg M. . . 2 Bertini I. . . 3 Dolfi A. . . 4 Turano P. . . 5 Mauk A. G. . 6 Rosell F. I. . 7 Gray H. B. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 125 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2913 _Page_last 2922 _Year 2003 _Details . loop_ _Keyword 'alkaline transition' 'cytochrome c; NMR structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_cytochrome_c _Saveframe_category molecular_system _Mol_system_name 'Cytochrome c, iso-1' _Abbreviation_common 'cyt c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Cytochrome c, iso-1' $cyt_c_iso1 'HEME C reduced' $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c_iso1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cytochrome c, iso-1' _Abbreviation_common 'Cyt c' _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; LFKTRCLQCHTVEKGGPHKV GPNLHGIFGRHSGQAEGYSY TDANIKKNVLWDENNMSEYL TNPAKYIPGTAMAFGGLKKE KDRNDLITYLKKATE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 9 LEU 2 10 PHE 3 11 LYS 4 12 THR 5 13 ARG 6 14 CYS 7 15 LEU 8 16 GLN 9 17 CYS 10 18 HIS 11 19 THR 12 20 VAL 13 21 GLU 14 22 LYS 15 23 GLY 16 24 GLY 17 25 PRO 18 26 HIS 19 27 LYS 20 28 VAL 21 29 GLY 22 30 PRO 23 31 ASN 24 32 LEU 25 33 HIS 26 34 GLY 27 35 ILE 28 36 PHE 29 37 GLY 30 38 ARG 31 39 HIS 32 40 SER 33 41 GLY 34 42 GLN 35 43 ALA 36 44 GLU 37 45 GLY 38 46 TYR 39 47 SER 40 48 TYR 41 49 THR 42 50 ASP 43 51 ALA 44 52 ASN 45 53 ILE 46 54 LYS 47 55 LYS 48 56 ASN 49 57 VAL 50 58 LEU 51 59 TRP 52 60 ASP 53 61 GLU 54 62 ASN 55 63 ASN 56 64 MET 57 65 SER 58 66 GLU 59 67 TYR 60 68 LEU 61 69 THR 62 70 ASN 63 71 PRO 64 72 ALA 65 73 LYS 66 74 TYR 67 75 ILE 68 76 PRO 69 77 GLY 70 78 THR 71 79 ALA 72 80 MET 73 81 ALA 74 82 PHE 75 83 GLY 76 84 GLY 77 85 LEU 78 86 LYS 79 87 LYS 80 88 GLU 81 89 LYS 82 90 ASP 83 91 ARG 84 92 ASN 85 93 ASP 86 94 LEU 87 95 ILE 88 96 THR 89 97 TYR 90 98 LEU 91 99 LYS 92 100 LYS 93 101 ALA 94 102 THR 95 103 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1LMS 'Structural Model For An Alkaline Form Of Ferricytochrome C' 100.00 108 100.00 100.00 1.20e-50 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _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 Fri Jun 10 14:42:48 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 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 . ? 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 . ? 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 . ? 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 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? 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 $cyt_c_iso1 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $cyt_c_iso1 'recombinant technology' 'E. coli' Escherichia coli . . 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 $cyt_c_iso1 2 mM . $HEM . mM . 'phosphate buffer' 50 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details Guentert save_ save_CORMA _Saveframe_category software _Name CORMA _Version . loop_ _Task 'iterative matrix relaxation' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version 6.0 loop_ _Task refinement stop_ _Details 'CASE AND KOLLMAN' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 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 '2D TOCSY' _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_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 11.1 . pH pressure 1 . atm temperature 298 . 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_citation_label _Correction_value_citation_label . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_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 _Mol_system_component_name 'Cytochrome c, iso-1' _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 LEU N N 124.09 . . 2 . 1 LEU H H 7.92 . . 3 . 1 LEU HB2 H 2.16 . . 4 . 1 LEU HB3 H 1.71 . . 5 . 1 LEU HA H 4.02 . . 6 . 1 LEU HG H 1.30 . . 7 . 1 LEU HD1 H 1.10 . . 8 . 1 LEU HD2 H 0.87 . . 9 . 2 PHE N N 120.3 . . 10 . 2 PHE H H 8.8 . . 11 . 2 PHE HB2 H 2.89 . . 12 . 2 PHE HA H 3.93 . . 13 . 2 PHE HD1 H 7.03 . . 14 . 2 PHE HE1 H 6.12 . . 15 . 2 PHE HZ H 8.62 . . 16 . 3 LYS N N 120.3 . . 17 . 3 LYS H H 8.24 . . 18 . 3 LYS HB2 H 1.92 . . 19 . 3 LYS HA H 3.1 . . 20 . 3 LYS HG2 H 1.20 . . 21 . 3 LYS HG3 H 1.07 . . 22 . 3 LYS HD2 H 0.73 . . 23 . 3 LYS HD3 H 0.54 . . 24 . 4 THR N N 107.22 . . 25 . 4 THR H H 7.93 . . 26 . 4 THR HA H 4.27 . . 27 . 4 THR HB H 3.95 . . 28 . 4 THR HG2 H 1.29 . . 29 . 5 ARG N N 116.83 . . 30 . 5 ARG H H 8.55 . . 31 . 5 ARG HA H 5.06 . . 32 . 5 ARG HB2 H 2.2 . . 33 . 5 ARG HB3 H 2.09 . . 34 . 5 ARG HG2 H 2.50 . . 35 . 6 CYS N N 115.18 . . 36 . 6 CYS H H 7.99 . . 37 . 6 CYS HA H 5.18 . . 38 . 6 CYS HB2 H 1.73 . . 39 . 6 CYS HB3 H 0.84 . . 40 . 7 LEU N N 121.37 . . 41 . 7 LEU H H 7.18 . . 42 . 7 LEU HA H 3.95 . . 43 . 7 LEU HD1 H 1.72 . . 44 . 7 LEU HD2 H 1.28 . . 45 . 8 GLN N N 124.18 . . 46 . 8 GLN H H 10.71 . . 47 . 8 GLN HA H 3.87 . . 48 . 8 GLN HB2 H 2.02 . . 49 . 8 GLN HB3 H 1.84 . . 50 . 8 GLN HG2 H 3.06 . . 51 . 8 GLN HG3 H 2.72 . . 52 . 8 GLN HE21 H 7.71 . . 53 . 8 GLN HE22 H 7.36 . . 54 . 8 GLN NE2 N 114.80 . . 55 . 9 CYS N N 113.08 . . 56 . 9 CYS H H 8.98 . . 57 . 9 CYS HA H 5.79 . . 58 . 9 CYS HB2 H 2.01 . . 59 . 10 HIS N N 120.66 . . 60 . 10 HIS H H 11.4 . . 61 . 10 HIS HA H 10.8 . . 62 . 10 HIS HB2 H 15.37 . . 63 . 10 HIS HB3 H 9.74 . . 64 . 10 HIS HD1 H 13.8 . . 65 . 10 HIS HD2 H 21.0 . . 66 . 10 HIS HE1 H -10 . . 67 . 11 THR N N 111.7 . . 68 . 11 THR H H 11.13 . . 69 . 11 THR HA H 6.51 . . 70 . 11 THR HB H 5.63 . . 71 . 11 THR HG2 H 2.39 . . 72 . 12 VAL H H 8.29 . . 73 . 12 VAL HA H 5 . . 74 . 16 GLY N N 108.26 . . 75 . 16 GLY H H 8.19 . . 76 . 16 GLY HA2 H 4.5 . . 77 . 16 GLY HA3 H 3.81 . . 78 . 21 GLY N N 104.13 . . 79 . 21 GLY H H 8.7 . . 80 . 21 GLY HA2 H -1.25 . . 81 . 21 GLY HA3 H 0.79 . . 82 . 22 PRO HA H 5.78 . . 83 . 22 PRO HG2 H 0.40 . . 84 . 22 PRO HG3 H -0.051 . . 85 . 22 PRO HD2 H 4.37 . . 86 . 22 PRO HD3 H -1.76 . . 87 . 23 ASN HA H 5.78 . . 88 . 23 ASN HD21 H 9.08 . . 89 . 23 ASN HD22 H 8.27 . . 90 . 23 ASN ND2 N 115.31 . . 91 . 24 LEU N N 123.05 . . 92 . 24 LEU H H 10.11 . . 93 . 24 LEU HB2 H 2.42 . . 94 . 24 LEU HB3 H 1.64 . . 95 . 24 LEU HA H 4.84 . . 96 . 24 LEU HD1 H 0.84 . . 97 . 24 LEU HD2 H -0.45 . . 98 . 25 HIS N N 119.96 . . 99 . 25 HIS H H 8.3 . . 100 . 25 HIS HA H 3.93 . . 101 . 25 HIS HB2 H 3.27 . . 102 . 25 HIS HB3 H 3.12 . . 103 . 26 GLY HA2 H 3.81 . . 104 . 26 GLY HA3 H 3.68 . . 105 . 27 ILE N N 116.82 . . 106 . 27 ILE H H 7.14 . . 107 . 27 ILE HB H 1.56 . . 108 . 27 ILE HA H 3.59 . . 109 . 27 ILE HG12 H 0.75 . . 110 . 27 ILE HG13 H 0.64 . . 111 . 27 ILE HG2 H 0.13 . . 112 . 27 ILE HD1 H 0.17 . . 113 . 28 PHE N N 115.56 . . 114 . 28 PHE H H 7.84 . . 115 . 28 PHE HA H 4.15 . . 116 . 28 PHE HB2 H 2.86 . . 117 . 28 PHE HD1 H 7.12 . . 118 . 28 PHE HE1 H 6.68 . . 119 . 28 PHE HZ H 7.00 . . 120 . 29 GLY N N 109.7 . . 121 . 29 GLY H H 8.69 . . 122 . 29 GLY HA2 H 4.15 . . 123 . 29 GLY HA3 H 3.63 . . 124 . 30 ARG N N 121.37 . . 125 . 30 ARG H H 8.03 . . 126 . 30 ARG HA H 4.53 . . 127 . 30 ARG HB2 H 2.1 . . 128 . 30 ARG HB3 H 1.84 . . 129 . 30 ARG HG2 H 1.69 . . 130 . 30 ARG HD2 H 1.92 . . 131 . 31 HIS N N 118.25 . . 132 . 31 HIS H H 7.76 . . 133 . 31 HIS HA H 5.35 . . 134 . 31 HIS HB2 H 2.74 . . 135 . 31 HIS HB3 H 2.58 . . 136 . 31 HIS HD1 H 6.50 . . 137 . 32 SER N N 115.49 . . 138 . 32 SER H H 8.63 . . 139 . 32 SER HA H 4.82 . . 140 . 32 SER HB2 H 4.24 . . 141 . 32 SER HB3 H 4.22 . . 142 . 33 GLY N N 112.75 . . 143 . 33 GLY H H 8.13 . . 144 . 33 GLY HA2 H 1.22 . . 145 . 33 GLY HA3 H 3.33 . . 146 . 34 GLN N N 113.38 . . 147 . 34 GLN H H 7.65 . . 148 . 34 GLN HA H 3.82 . . 149 . 35 ALA N N 127.87 . . 150 . 35 ALA H H 7.85 . . 151 . 35 ALA HA H 4.34 . . 152 . 35 ALA HB H 1.67 . . 153 . 36 GLU H H 8.44 . . 154 . 36 GLU HA H 4.61 . . 155 . 37 GLY N N 112.43 . . 156 . 37 GLY H H 9.99 . . 157 . 37 GLY HA2 H 4.34 . . 158 . 37 GLY HA3 H 4.9 . . 159 . 38 TYR H H 6.62 . . 160 . 38 TYR HB2 H 1.71 . . 161 . 38 TYR HA H 3.75 . . 162 . 38 TYR HD1 H 7.04 . . 163 . 38 TYR HD2 H 7.31 . . 164 . 38 TYR HE1 H 6.93 . . 165 . 38 TYR HE2 H 6.24 . . 166 . 40 TYR HB2 H 2.08 . . 167 . 40 TYR HD1 H 6.15 . . 168 . 40 TYR HE1 H 6.73 . . 169 . 41 THR H H 9.42 . . 170 . 41 THR HG2 H 1.35 . . 171 . 44 ASN N N 118.63 . . 172 . 44 ASN H H 8.16 . . 173 . 44 ASN HB2 H 2.97 . . 174 . 44 ASN HB3 H 2.89 . . 175 . 44 ASN HA H 4.03 . . 176 . 44 ASN HD21 H 8.70 . . 177 . 44 ASN HD22 H 7.19 . . 178 . 44 ASN ND2 N 106.55 . . 179 . 45 ILE N N 119.95 . . 180 . 45 ILE H H 7.59 . . 181 . 45 ILE HA H 3.27 . . 182 . 45 ILE HB H 1.76 . . 183 . 45 ILE HG12 H 0.95 . . 184 . 45 ILE HG13 H 1.05 . . 185 . 45 ILE HD1 H 0.82 . . 186 . 46 LYS N N 118.66 . . 187 . 46 LYS H H 8.95 . . 188 . 46 LYS HA H 3.79 . . 189 . 46 LYS HB2 H 1.73 . . 190 . 46 LYS HB3 H 1.62 . . 191 . 46 LYS HG2 H 1.35 . . 192 . 47 LYS N N 119.22 . . 193 . 47 LYS H H 7.33 . . 194 . 47 LYS HA H 3.72 . . 195 . 47 LYS HB2 H 1.65 . . 196 . 47 LYS HG2 H 1.20 . . 197 . 47 LYS HD2 H 0.93 . . 198 . 48 ASN N N 114.45 . . 199 . 48 ASN H H 8.16 . . 200 . 48 ASN HA H 4.36 . . 201 . 49 VAL N N 115.14 . . 202 . 49 VAL H H 7.23 . . 203 . 49 VAL HA H 3.66 . . 204 . 49 VAL HB H 0.97 . . 205 . 49 VAL HG1 H -0.35 . . 206 . 49 VAL HG2 H 0.28 . . 207 . 50 LEU N N 127.87 . . 208 . 50 LEU H H 8.12 . . 209 . 50 LEU HB2 H 1.48 . . 210 . 50 LEU HB3 H 0.71 . . 211 . 50 LEU HA H 3.66 . . 212 . 50 LEU HG H 0.94 . . 213 . 50 LEU HD1 H 0.57 . . 214 . 50 LEU HD2 H 0.13 . . 215 . 51 TRP N N 128.9 . . 216 . 51 TRP H H 7.93 . . 217 . 51 TRP HB2 H 3.66 . . 218 . 51 TRP HB3 H 2.53 . . 219 . 51 TRP HA H 4.89 . . 220 . 51 TRP HD1 H 6.93 . . 221 . 51 TRP HE1 H 8.88 . . 222 . 51 TRP HE3 H 7.50 . . 223 . 51 TRP HZ2 H 6.55 . . 224 . 51 TRP HZ3 H 7.02 . . 225 . 51 TRP HH2 H 5.60 . . 226 . 51 TRP NE1 N 121.00 . . 227 . 52 ASP N N 125.12 . . 228 . 52 ASP H H 9.65 . . 229 . 54 ASN N N 126.15 . . 230 . 54 ASN H H 7.63 . . 231 . 54 ASN HA H 4.47 . . 232 . 54 ASN HB2 H 2.94 . . 233 . 54 ASN HB3 H 1.85 . . 234 . 55 ASN N N 122.71 . . 235 . 55 ASN H H 9.4 . . 236 . 55 ASN HA H 4.43 . . 237 . 55 ASN HB2 H 3 . . 238 . 55 ASN HB3 H 2.77 . . 239 . 55 ASN HD21 H 6.86 . . 240 . 55 ASN HD22 H 6.64 . . 241 . 56 MET N N 123.4 . . 242 . 56 MET H H 8.58 . . 243 . 56 MET HA H 4.02 . . 244 . 56 MET HB2 H 1.6 . . 245 . 56 MET HB3 H 1.32 . . 246 . 56 MET HE H -0.89 . . 247 . 57 SER N N 114.11 . . 248 . 57 SER H H 7.32 . . 249 . 57 SER HA H 3.44 . . 250 . 57 SER HB2 H 3.99 . . 251 . 57 SER HB3 H 3.74 . . 252 . 58 GLU N N 120.3 . . 253 . 58 GLU H H 7.68 . . 254 . 58 GLU HA H 3.69 . . 255 . 58 GLU HB2 H 1.85 . . 256 . 58 GLU HB3 H 1.67 . . 257 . 58 GLU HG2 H 2.17 . . 258 . 59 TYR N N 121.04 . . 259 . 59 TYR H H 8.3 . . 260 . 59 TYR HA H 3.43 . . 261 . 59 TYR HB2 H 2.98 . . 262 . 59 TYR HB3 H 2.9 . . 263 . 60 LEU N N 111.33 . . 264 . 60 LEU H H 8.22 . . 265 . 60 LEU HA H 2.9 . . 266 . 60 LEU HB2 H 1.92 . . 267 . 60 LEU HB3 H 1.64 . . 268 . 60 LEU HG H 1.02 . . 269 . 60 LEU HD1 H 0.03 . . 270 . 61 THR N N 115.56 . . 271 . 61 THR H H 7.25 . . 272 . 61 THR HA H 3.77 . . 273 . 61 THR HB H 4.05 . . 274 . 61 THR HG2 H 1.09 . . 275 . 62 ASN N N 107.22 . . 276 . 62 ASN H H 6.09 . . 277 . 62 ASN HA H 4.06 . . 278 . 62 ASN HB2 H 2.93 . . 279 . 62 ASN HB3 H 2.64 . . 280 . 63 PRO HB2 H 0.08 . . 281 . 63 PRO HG2 H 0.60 . . 282 . 63 PRO HD2 H 1.09 . . 283 . 64 ALA N N 112.83 . . 284 . 64 ALA H H 7.82 . . 285 . 65 LYS N N 122.29 . . 286 . 65 LYS H H 8.19 . . 287 . 65 LYS HB2 H 10.94 . . 288 . 65 LYS HB3 H 9.43 . . 289 . 65 LYS HA H 5.06 . . 290 . 65 LYS HG2 H 6.7 . . 291 . 65 LYS HD2 H 24.5 . . 292 . 67 ILE N N 121.35 . . 293 . 67 ILE H H 7.68 . . 294 . 67 ILE HB H 2.22 . . 295 . 67 ILE HA H 3.86 . . 296 . 67 ILE HG12 H 1.15 . . 297 . 67 ILE HG13 H 0.28 . . 298 . 67 ILE HG2 H -0.73 . . 299 . 67 ILE HD1 H -0.99 . . 300 . 69 GLY H H 8.27 . . 301 . 70 THR H H 8.63 . . 302 . 71 ALA N N 125.12 . . 303 . 71 ALA H H 7.97 . . 304 . 71 ALA HA H 2.36 . . 305 . 71 ALA HB H 1.12 . . 306 . 72 MET N N 112.39 . . 307 . 72 MET H H 6.92 . . 308 . 72 MET HA H 4.15 . . 309 . 72 MET HG2 H 1.89 . . 310 . 72 MET HG3 H 1.41 . . 311 . 73 ALA N N 115.48 . . 312 . 73 ALA H H 6.44 . . 313 . 73 ALA HA H 3.51 . . 314 . 73 ALA HB H 0.67 . . 315 . 74 PHE HB2 H 1.93 . . 316 . 74 PHE HD1 H 6.87 . . 317 . 74 PHE HE1 H 7.02 . . 318 . 74 PHE HZ H 6.86 . . 319 . 75 GLY N N 108.26 . . 320 . 75 GLY H H 9.53 . . 321 . 76 GLY N N 105.5 . . 322 . 76 GLY H H 7.54 . . 323 . 76 GLY HA2 H 3.51 . . 324 . 77 LEU N N 116.46 . . 325 . 77 LEU H H 7.8 . . 326 . 77 LEU HA H 4.08 . . 327 . 77 LEU HB2 H 1.52 . . 328 . 77 LEU HB3 H 0.97 . . 329 . 77 LEU HG H 1.08 . . 330 . 77 LEU HD1 H 0.00 . . 331 . 78 LYS N N 119.15 . . 332 . 78 LYS H H 8.39 . . 333 . 78 LYS HA H 4.21 . . 334 . 78 LYS HG2 H 1.10 . . 335 . 78 LYS HD2 H 0.27 . . 336 . 78 LYS HD3 H -0.03 . . 337 . 79 LYS N N 120.3 . . 338 . 79 LYS H H 7.99 . . 339 . 79 LYS HA H 3.59 . . 340 . 79 LYS HB2 H 2.39 . . 341 . 79 LYS HB3 H 2.27 . . 342 . 79 LYS HG2 H 1.04 . . 343 . 79 LYS HD2 H 1.17 . . 344 . 82 ASP N N 115.55 . . 345 . 82 ASP H H 6.37 . . 346 . 82 ASP HA H 4.28 . . 347 . 82 ASP HB2 H 2.86 . . 348 . 82 ASP HB3 H 2.52 . . 349 . 83 ARG N N 117.9 . . 350 . 83 ARG H H 7.48 . . 351 . 83 ARG HA H 3.78 . . 352 . 83 ARG HB2 H 1.8 . . 353 . 83 ARG HB3 H 1.59 . . 354 . 83 ARG HG2 H 1.04 . . 355 . 84 ASN N N 117.56 . . 356 . 84 ASN H H 8.7 . . 357 . 84 ASN HA H 4.62 . . 358 . 84 ASN HB2 H 2.71 . . 359 . 85 ASP N N 125.09 . . 360 . 85 ASP H H 8.67 . . 361 . 85 ASP HA H 4.19 . . 362 . 85 ASP HB2 H 2.65 . . 363 . 86 LEU N N 120.3 . . 364 . 86 LEU H H 8.55 . . 365 . 86 LEU HA H 4.21 . . 366 . 86 LEU HB2 H 2.12 . . 367 . 86 LEU HB3 H 1.9 . . 368 . 86 LEU HG H 1.08 . . 369 . 86 LEU HD1 H 1.04 . . 370 . 87 ILE N N 119.95 . . 371 . 87 ILE H H 9.12 . . 372 . 87 ILE HB H 2.07 . . 373 . 87 ILE HA H 3.6 . . 374 . 87 ILE HG12 H 0.08 . . 375 . 87 ILE HG2 H 0.98 . . 376 . 87 ILE HD1 H 0.53 . . 377 . 88 THR N N 117.2 . . 378 . 88 THR H H 8.15 . . 379 . 88 THR HA H 3.78 . . 380 . 88 THR HB H 4.39 . . 381 . 88 THR HG2 H 1.18 . . 382 . 89 TYR N N 119.55 . . 383 . 89 TYR H H 7.81 . . 384 . 89 TYR HA H 4.08 . . 385 . 89 TYR HB2 H 3.54 . . 386 . 89 TYR HB3 H 3.09 . . 387 . 90 LEU N N 119.94 . . 388 . 90 LEU H H 9.34 . . 389 . 90 LEU HB2 H 1.95 . . 390 . 90 LEU HB3 H 1.89 . . 391 . 90 LEU HA H 3.33 . . 392 . 90 LEU HG H 1.61 . . 393 . 90 LEU HD1 H 0.79 . . 394 . 90 LEU HD2 H -0.11 . . 395 . 91 LYS N N 120.66 . . 396 . 91 LYS H H 8.67 . . 397 . 91 LYS HA H 3.41 . . 398 . 91 LYS HB2 H 1.9 . . 399 . 91 LYS HB3 H 1.43 . . 400 . 91 LYS HG2 H 0.47 . . 401 . 91 LYS HD2 H 0.83 . . 402 . 92 LYS N N 115.83 . . 403 . 92 LYS H H 6.56 . . 404 . 92 LYS HA H 4.06 . . 405 . 92 LYS HB2 H 1.7 . . 406 . 92 LYS HG2 H 1.30 . . 407 . 93 ALA N N 119.61 . . 408 . 93 ALA H H 8.33 . . 409 . 93 ALA HA H 3.8 . . 410 . 93 ALA HB H 0.46 . . 411 . 94 THR N N 102.41 . . 412 . 94 THR H H 7.26 . . 413 . 94 THR HA H 4.3 . . 414 . 94 THR HG2 H 0.81 . . 415 . 95 GLU N N 125.8 . . 416 . 95 GLU H H 6.65 . . 417 . 95 GLU HA H 3.93 . . 418 . 95 GLU HB2 H 2.16 . . 419 . 95 GLU HB3 H 1.87 . . 420 . 95 GLU HG2 H 2.71 . . stop_ save_