data_5830 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and sidechain heteronuclear resonance assignments and hyperfine nuclear magnetic resonance shifts in horse cytochrome c ; _BMRB_accession_number 5830 _BMRB_flat_file_name bmr5830.str _Entry_type original _Submission_date 2003-06-12 _Accession_date 2003-06-12 _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 Liu Weixia . . 2 Rumbley Jon . . 3 Englander S. Walter . 4 Wand A. Joshua . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5827 'cytochrome c reduced state of H26N, H33N mutant' 5828 'cytochrome c oxidized state of H26N, H33N mutant' 5829 'cytochrome c reduced state of wild type' stop_ _Original_release_date 2003-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22812282 _PubMed_ID 12931009 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Weixia . . 2 Rumbley Jon . . 3 Englander S. Walter . 4 Wand A. Joshua . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 12 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2104 _Page_last 2108 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_cyt_c _Saveframe_category molecular_system _Mol_system_name 'Horse cytochrome c (wt) oxidized form' _Abbreviation_common 'cyt c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome c' $cyt_c heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Horse cytochrome c' _Name_variant 'wild type' _Abbreviation_common 'cyt c' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GDVEKGKKIFVQKCAQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 VAL 4 GLU 5 LYS 6 GLY 7 LYS 8 LYS 9 ILE 10 PHE 11 VAL 12 GLN 13 LYS 14 CYS 15 ALA 16 GLN 17 CYS 18 HIS 19 THR 20 VAL 21 GLU 22 LYS 23 GLY 24 GLY 25 LYS 26 HIS 27 LYS 28 THR 29 GLY 30 PRO 31 ASN 32 LEU 33 HIS 34 GLY 35 LEU 36 PHE 37 GLY 38 ARG 39 LYS 40 THR 41 GLY 42 GLN 43 ALA 44 PRO 45 GLY 46 PHE 47 THR 48 TYR 49 THR 50 ASP 51 ALA 52 ASN 53 LYS 54 ASN 55 LYS 56 GLY 57 ILE 58 THR 59 TRP 60 LYS 61 GLU 62 GLU 63 THR 64 LEU 65 MET 66 GLU 67 TYR 68 LEU 69 GLU 70 ASN 71 PRO 72 LYS 73 LYS 74 TYR 75 ILE 76 PRO 77 GLY 78 THR 79 LYS 80 MET 81 ILE 82 PHE 83 ALA 84 GLY 85 ILE 86 LYS 87 LYS 88 LYS 89 THR 90 GLU 91 ARG 92 GLU 93 ASP 94 LEU 95 ILE 96 ALA 97 TYR 98 LEU 99 LYS 100 LYS 101 ALA 102 THR 103 ASN 104 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 SWISS-PROT P68097 'Cytochrome c' 100.00 105 99.04 100.00 1.64e-53 SWISS-PROT P68096 'Cytochrome c' 100.00 105 99.04 100.00 1.64e-53 SWISS-PROT P00004 'Cytochrome c' 100.00 105 100.00 100.00 9.71e-54 REF XP_001498872 'PREDICTED: similar to Cytochrome c, somatic [Equus caballus]' 100.00 105 99.04 100.00 1.64e-53 PRF 610169A 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 GenBank AAB33495 'apocytochrome c [horses, heart, Peptide, 104 aa]' 100.00 104 98.08 98.08 4.15e-52 PDB 2PCB 'Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 2GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures' 100.00 104 100.00 100.00 1.19e-53 PDB 2FRC 'Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 PDB 1WEJ 'Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution' 100.00 104 100.00 100.00 1.19e-53 PDB 1U75 'Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc-Porphyrin Substituted Cytochrome C Peroxidase' 100.00 104 100.00 100.00 1.19e-53 PDB 1OCD 'Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 PDB 1M60 'Solution Structure Of Zinc-Substituted Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1LC2 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures' 100.00 104 100.00 100.00 1.19e-53 PDB 1LC1 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 PDB 1I5T 'Solution Structure Of Cyanoferricytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1HRC 'High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 99.04 104 100.00 100.00 4.08e-53 PDB 1FI9 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1FI7 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1CRC 'Cytochrome C At Low Ionic Strength' 100.00 104 100.00 100.00 1.19e-53 PDB 1AKK 'Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 BMRB 948 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 947 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 946 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 944 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 673 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 672 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 665 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 645 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 630 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 5829 'Horse cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 5828 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5827 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5660 'oxidized cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 546 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 545 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 544 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 543 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 5372 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 5026 'cytochrome C' 100.00 104 100.00 100.00 1.19e-53 BMRB 499 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 4810 'ferric cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4809 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4808 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4805 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 439 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 438 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 437 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 436 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 4189 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 336 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 317 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 316 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 286 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 285 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 274 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 244 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 243 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 2368 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 2367 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 2366 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 224 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 220 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 216 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1789 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1787 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1785 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1783 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1736 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1404 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1171 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1170 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1116 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1114 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1113 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1112 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1111 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1110 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1109 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1108 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1107 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1058 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 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 14:10:54 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 9796 Horse Eukaryota Metazoa Equus caballus 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 'recombinant technology' . . . . . 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 8.0 mM . 'sodium phosphate' 50 mM . H2O 95 % . D20 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _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 5.8 0.05 n/a temperature 293 0.2 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_cytwt_ox_assignments _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' _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 GLY H H 8.07 0.04 1 2 . 1 GLY N N 113.26 0.19 1 3 . 2 ASP H H 9.49 0.04 1 4 . 2 ASP N N 125.35 0.19 1 5 . 3 VAL H H 8.43 0.04 1 6 . 3 VAL N N 124.03 0.19 1 7 . 4 GLU H H 8.00 0.04 1 8 . 4 GLU N N 120.17 0.19 1 9 . 5 LYS H H 8.02 0.04 1 10 . 5 LYS N N 121.18 0.19 1 11 . 6 GLY H H 8.63 0.04 1 12 . 6 GLY N N 107.57 0.19 1 13 . 7 LYS H H 7.95 0.04 1 14 . 7 LYS N N 124.16 0.19 1 15 . 8 LYS H H 6.84 0.04 1 16 . 8 LYS N N 116.89 0.19 1 17 . 9 ILE H H 7.41 0.04 1 18 . 9 ILE N N 119.03 0.19 1 19 . 10 PHE H H 8.34 0.04 1 20 . 10 PHE N N 120.93 0.19 1 21 . 11 VAL H H 8.80 0.04 1 22 . 11 VAL N N 121.52 0.19 1 23 . 12 GLN H H 7.75 0.04 1 24 . 12 GLN N N 117.42 0.19 1 25 . 13 LYS H H 8.41 0.04 1 26 . 13 LYS N N 112.48 0.19 1 27 . 14 CYS H H 8.01 0.04 1 28 . 14 CYS N N 115.04 0.19 1 29 . 15 ALA H H 8.06 0.04 1 30 . 15 ALA N N 123.43 0.19 1 31 . 16 GLN H H 9.85 0.04 1 32 . 16 GLN N N 117.36 0.19 1 33 . 17 CYS H H 9.58 0.04 1 34 . 17 CYS N N 114.29 0.19 1 35 . 18 HIS H H 10.88 0.04 1 36 . 18 HIS N N 118.63 0.19 1 37 . 19 THR H H 10.64 0.04 1 38 . 19 THR N N 113.97 0.19 1 39 . 20 VAL H H 8.85 0.04 1 40 . 20 VAL N N 111.50 0.19 1 41 . 21 GLU H H 9.56 0.04 1 42 . 21 GLU N N 122.00 0.19 1 43 . 22 LYS H H 9.08 0.04 1 44 . 22 LYS N N 126.67 0.19 1 45 . 23 GLY H H 9.39 0.04 1 46 . 23 GLY N N 117.79 0.19 1 47 . 24 GLY H H 8.16 0.04 1 48 . 24 GLY N N 107.77 0.19 1 49 . 25 LYS H H 8.78 0.04 1 50 . 25 LYS N N 119.08 0.19 1 51 . 26 HIS H H 8.82 0.04 1 52 . 26 HIS N N 122.18 0.19 1 53 . 27 LYS H H 8.00 0.04 1 54 . 27 LYS N N 125.59 0.19 1 55 . 29 GLY H H 6.90 0.04 1 56 . 29 GLY N N 99.67 0.19 1 57 . 31 ASN H H 11.55 0.04 1 58 . 31 ASN N N 127.25 0.19 1 59 . 32 LEU H H 9.21 0.04 1 60 . 32 LEU N N 124.08 0.19 1 61 . 33 HIS H H 8.14 0.04 1 62 . 33 HIS N N 119.90 0.19 1 63 . 34 GLY H H 9.00 0.04 1 64 . 34 GLY N N 115.00 0.19 1 65 . 35 LEU H H 7.03 0.04 1 66 . 35 LEU N N 117.31 0.19 1 67 . 36 PHE H H 8.60 0.04 1 68 . 36 PHE N N 112.38 0.19 1 69 . 37 GLY H H 9.25 0.04 1 70 . 37 GLY N N 111.48 0.19 1 71 . 38 ARG H H 8.13 0.04 1 72 . 38 ARG N N 123.97 0.19 1 73 . 39 LYS H H 8.02 0.04 1 74 . 39 LYS N N 121.18 0.19 1 75 . 40 THR H H 7.49 0.04 1 76 . 40 THR N N 109.05 0.19 1 77 . 41 GLY H H 9.11 0.04 1 78 . 41 GLY N N 109.59 0.19 1 79 . 42 GLN H H 7.66 0.04 1 80 . 42 GLN N N 113.05 0.19 1 81 . 43 ALA H H 8.13 0.04 1 82 . 43 ALA N N 126.22 0.19 1 83 . 45 GLY H H 8.92 0.04 1 84 . 45 GLY N N 111.77 0.19 1 85 . 46 PHE H H 6.79 0.04 1 86 . 46 PHE N N 119.77 0.19 1 87 . 47 THR H H 6.69 0.04 1 88 . 47 THR N N 123.71 0.19 1 89 . 48 TYR H H 7.95 0.04 1 90 . 48 TYR N N 126.61 0.19 1 91 . 49 THR H H 9.57 0.04 1 92 . 49 THR N N 112.62 0.19 1 93 . 50 ASP H H 8.82 0.04 1 94 . 50 ASP N N 122.79 0.19 1 95 . 51 ALA H H 8.03 0.04 1 96 . 51 ALA N N 119.75 0.19 1 97 . 52 ASN H H 8.52 0.04 1 98 . 52 ASN N N 117.25 0.19 1 99 . 53 LYS H H 8.60 0.04 1 100 . 53 LYS N N 121.52 0.19 1 101 . 54 ASN H H 8.13 0.04 1 102 . 54 ASN N N 112.69 0.19 1 103 . 55 LYS H H 6.96 0.04 1 104 . 55 LYS N N 121.64 0.19 1 105 . 56 GLY H H 7.79 0.04 1 106 . 56 GLY N N 103.12 0.19 1 107 . 57 ILE H H 6.50 0.04 1 108 . 57 ILE N N 111.26 0.19 1 109 . 58 THR H H 8.22 0.04 1 110 . 58 THR N N 116.26 0.19 1 111 . 59 TRP H H 8.68 0.04 1 112 . 59 TRP N N 129.31 0.19 1 113 . 60 LYS H H 7.93 0.04 1 114 . 60 LYS N N 120.03 0.19 1 115 . 61 GLU H H 10.64 0.04 1 116 . 61 GLU N N 123.03 0.19 1 117 . 62 GLU H H 9.47 0.04 1 118 . 62 GLU N N 114.58 0.19 1 119 . 63 THR H H 6.99 0.04 1 120 . 63 THR N N 108.54 0.19 1 121 . 64 LEU H H 8.45 0.04 1 122 . 64 LEU N N 122.12 0.19 1 123 . 65 MET H H 8.18 0.04 1 124 . 65 MET N N 118.45 0.19 1 125 . 66 GLU H H 6.57 0.04 1 126 . 66 GLU N N 117.66 0.19 1 127 . 67 TYR H H 8.04 0.04 1 128 . 67 TYR N N 121.42 0.19 1 129 . 68 LEU H H 8.05 0.04 1 130 . 68 LEU N N 111.00 0.19 1 131 . 69 GLU H H 6.74 0.04 1 132 . 69 GLU N N 118.91 0.19 1 133 . 70 ASN H H 6.62 0.04 1 134 . 70 ASN N N 105.55 0.19 1 135 . 72 LYS H H 9.41 0.04 1 136 . 72 LYS N N 115.74 0.19 1 137 . 73 LYS H H 7.76 0.04 1 138 . 73 LYS N N 119.55 0.19 1 139 . 74 TYR H H 8.08 0.04 1 140 . 74 TYR N N 120.39 0.19 1 141 . 75 ILE H H 9.42 0.04 1 142 . 75 ILE N N 115.01 0.19 1 143 . 77 GLY H H 9.30 0.04 1 144 . 77 GLY N N 111.64 0.19 1 145 . 78 THR H H 9.01 0.04 1 146 . 78 THR N N 115.19 0.19 1 147 . 79 LYS H H 8.19 0.04 1 148 . 79 LYS N N 123.61 0.19 1 149 . 80 MET H H 9.20 0.04 1 150 . 80 MET N N 122.77 0.19 1 151 . 81 ILE H H 8.52 0.04 1 152 . 81 ILE N N 135.54 0.19 1 153 . 82 PHE H H 8.96 0.04 1 154 . 82 PHE N N 126.31 0.19 1 155 . 83 ALA H H 8.43 0.04 1 156 . 83 ALA N N 130.98 0.19 1 157 . 85 ILE H H 7.93 0.04 1 158 . 85 ILE N N 120.90 0.19 1 159 . 86 LYS H H 8.38 0.04 1 160 . 86 LYS N N 127.38 0.19 1 161 . 87 LYS H H 8.14 0.04 1 162 . 87 LYS N N 120.21 0.19 1 163 . 88 LYS H H 8.74 0.04 1 164 . 88 LYS N N 129.40 0.19 1 165 . 89 THR H H 8.14 0.04 1 166 . 89 THR N N 109.56 0.19 1 167 . 90 GLU H H 6.00 0.04 1 168 . 90 GLU N N 118.84 0.19 1 169 . 91 ARG H H 7.06 0.04 1 170 . 91 ARG N N 116.92 0.19 1 171 . 92 GLU H H 8.19 0.04 1 172 . 92 GLU N N 117.85 0.19 1 173 . 93 ASP H H 8.19 0.04 1 174 . 93 ASP N N 122.60 0.19 1 175 . 94 LEU H H 7.86 0.04 1 176 . 94 LEU N N 120.43 0.19 1 177 . 95 ILE H H 8.37 0.04 1 178 . 95 ILE N N 119.59 0.19 1 179 . 96 ALA H H 7.77 0.04 1 180 . 96 ALA N N 122.86 0.19 1 181 . 97 TYR H H 7.86 0.04 1 182 . 97 TYR N N 117.89 0.19 1 183 . 98 LEU H H 8.69 0.04 1 184 . 98 LEU N N 118.77 0.19 1 185 . 99 LYS H H 8.81 0.04 1 186 . 99 LYS N N 123.99 0.19 1 187 . 100 LYS H H 6.70 0.04 1 188 . 100 LYS N N 116.95 0.19 1 189 . 101 ALA H H 8.60 0.04 1 190 . 101 ALA N N 119.64 0.19 1 191 . 102 THR H H 7.92 0.04 1 192 . 102 THR N N 102.18 0.19 1 193 . 103 ASN H H 7.07 0.04 1 194 . 103 ASN N N 118.63 0.19 1 195 . 104 GLU H H 7.33 0.04 1 196 . 104 GLU N N 124.97 0.19 1 stop_ save_