data_4208 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Y64A Mutant of Cytochrome c553 from Desulfovibrio vulgaris Hildenborough ; _BMRB_accession_number 4208 _BMRB_flat_file_name bmr4208.str _Entry_type original _Submission_date 1998-03-25 _Accession_date 1998-03-25 _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 SEBBAN-KREUZER C. . . 2 BLACKLEDGE M. J. . 3 DOLLA A. . . 4 MARION D. . . 5 GUERLESQUIN F. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 411 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-07-13 original author . stop_ _Original_release_date 2007-07-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Dynamics of Ferrocytochrome c553 from Desulfovibrio vulgaris Studied by Spectroscopy and Restrained Molecular Dynamics NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 95147286 _PubMed_ID 7844834 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blackledge M. J. . 2 Medvedeva S. . . 3 Poncin M. . . 4 Guerlesquin F. . . 5 Bruschi M. . . 6 Marion D. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 245 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 661 _Page_last 681 _Year 1995 _Details . loop_ _Keyword cytochrome_c 'electron transfer pathway' stop_ save_ ################################## # Molecular system description # ################################## save_system_CytC(Y64A) _Saveframe_category molecular_system _Mol_system_name CytC(Y64A) _Abbreviation_common CytC(Y64A) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CytC(Y64A) $CytC(Y64A) heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CytC(Y64A) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CytC(Y64A) _Name_variant M8L _Abbreviation_common 'cyt c553' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; ADGAALYKSCIGCHGADGSK AAMGSAKPVKGQGAEELYKK MKGYADGSYGGERKAMMTNA VKKASDEELKALADYMSKL ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 GLY 4 ALA 5 ALA 6 LEU 7 TYR 8 LYS 9 SER 10 CYS 11 ILE 12 GLY 13 CYS 14 HIS 15 GLY 16 ALA 17 ASP 18 GLY 19 SER 20 LYS 21 ALA 22 ALA 23 MET 24 GLY 25 SER 26 ALA 27 LYS 28 PRO 29 VAL 30 LYS 31 GLY 32 GLN 33 GLY 34 ALA 35 GLU 36 GLU 37 LEU 38 TYR 39 LYS 40 LYS 41 MET 42 LYS 43 GLY 44 TYR 45 ALA 46 ASP 47 GLY 48 SER 49 TYR 50 GLY 51 GLY 52 GLU 53 ARG 54 LYS 55 ALA 56 MET 57 MET 58 THR 59 ASN 60 ALA 61 VAL 62 LYS 63 LYS 64 ALA 65 SER 66 ASP 67 GLU 68 GLU 69 LEU 70 LYS 71 ALA 72 LEU 73 ALA 74 ASP 75 TYR 76 MET 77 SER 78 LYS 79 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 1DVH "Structure And Dynamics Of Ferrocytochrome C553 From Desulfovibrio Vulgaris Studied By Nmr Spectroscopy And Restrained Molecular" 100.00 79 98.73 98.73 9.88e-45 PDB 1DWL "The Ferredoxin-Cytochrome Complex Using Heteronuclear Nmr And Docking Simulation" 100.00 79 98.73 98.73 9.88e-45 PDB 1E08 "Structural Model Of The [fe]-HydrogenaseCYTOCHROME C553 Complex Combining Nmr And Soft-Docking" 98.73 78 98.72 98.72 2.82e-44 PDB 2DVH "The Y64a Mutant Of Cytochrome C553 From Desulfovibrio Vulgaris Hildenborough, Nmr, 39 Structures" 100.00 79 100.00 100.00 1.03e-45 GB AAA16453 "cytochrome c553 [Desulfovibrio vulgaris]" 100.00 103 98.73 98.73 5.25e-45 GB AAA23356 "cytochrome c-553 precursor [Desulfovibrio vulgaris]" 100.00 103 98.73 98.73 5.25e-45 GB AAS96294 "cytochrome c-553 [Desulfovibrio vulgaris str. Hildenborough]" 100.00 103 98.73 98.73 5.25e-45 GB ABM28361 "cytochrome c, class I [Desulfovibrio vulgaris DP4]" 100.00 103 98.73 98.73 5.25e-45 GB ADP86641 "cytochrome c class I [Desulfovibrio vulgaris RCH1]" 100.00 103 98.73 98.73 5.25e-45 REF WP_010939104 "cytochrome c-553 [Desulfovibrio vulgaris]" 100.00 103 98.73 98.73 5.25e-45 REF YP_011035 "cytochrome c-553 [Desulfovibrio vulgaris str. Hildenborough]" 100.00 103 98.73 98.73 5.25e-45 SP P04032 "RecName: Full=Cytochrome c-553; AltName: Full=Cytochrome c553; AltName: Full=Low-potential cytochrome c; Flags: Precursor" 100.00 103 98.73 98.73 5.25e-45 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 Mon Jun 20 14:47:45 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 _Fraction _Plasmid _Gene_mnemonic $CytC(Y64A) 'Desulfovibrio desulfuricans' 876 Bacteria . Desulfovibrio desulfuricans periplasm pJRD215 M13cyf 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 $CytC(Y64A) 'recombinant technology' 'Desulfovibrio desulfuricans' Desulfovibrio desulfuricans G200 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CytC(Y64A) . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_HOHAHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 10 . mM pH 5.9 . n/a temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 . . . . . . . . $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_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name CytC(Y64A) _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 ASP HA H 4.85 . 1 2 . 2 ASP HB2 H 2.83 . 1 3 . 2 ASP HB3 H 2.83 . 1 4 . 3 GLY H H 8.98 . 1 5 . 3 GLY HA2 H 3.78 . 1 6 . 3 GLY HA3 H 3.53 . 1 7 . 4 ALA H H 7.80 . 1 8 . 4 ALA HA H 2.71 . 1 9 . 4 ALA HB H 1.31 . 1 10 . 5 ALA H H 7.36 . 1 11 . 5 ALA HA H 4.12 . 1 12 . 5 ALA HB H 1.51 . 1 13 . 6 LEU H H 8.10 . 1 14 . 6 LEU HA H 4.24 . 1 15 . 6 LEU HB2 H 2.07 . 1 16 . 6 LEU HB3 H 1.61 . 1 17 . 6 LEU HG H 2.00 . 1 18 . 6 LEU HD1 H 1.48 . 1 19 . 6 LEU HD2 H 1.04 . 1 20 . 7 TYR H H 8.15 . 1 21 . 7 TYR HA H 4.83 . 1 22 . 7 TYR HB2 H 3.09 . 1 23 . 7 TYR HB3 H 2.67 . 1 24 . 7 TYR HD1 H 7.14 . 1 25 . 7 TYR HD2 H 7.14 . 1 26 . 7 TYR HE1 H 6.42 . 1 27 . 7 TYR HE2 H 6.42 . 1 28 . 8 LYS H H 7.43 . 1 29 . 8 LYS HA H 4.03 . 1 30 . 8 LYS HB2 H 2.09 . 1 31 . 8 LYS HB3 H 2.03 . 1 32 . 8 LYS HG2 H 1.83 . 1 33 . 8 LYS HG3 H 1.67 . 1 34 . 8 LYS HD2 H 1.83 . 1 35 . 8 LYS HD3 H 1.83 . 1 36 . 8 LYS HE2 H 3.08 . 1 37 . 8 LYS HE3 H 3.08 . 1 38 . 9 SER H H 7.88 . 1 39 . 9 SER HA H 4.73 . 1 40 . 9 SER HB2 H 4.46 . 1 41 . 9 SER HB3 H 4.46 . 1 42 . 10 CYS H H 8.43 . 1 43 . 10 CYS HA H 5.33 . 1 44 . 10 CYS HB2 H 2.34 . 1 45 . 10 CYS HB3 H 1.65 . 1 46 . 11 ILE H H 6.89 . 1 47 . 11 ILE HA H 2.75 . 1 48 . 11 ILE HB H 1.59 . 1 49 . 11 ILE HG2 H 0.81 . 1 50 . 11 ILE HD1 H 1.04 . 1 51 . 12 GLY H H 8.81 . 1 52 . 12 GLY HA2 H 3.92 . 1 53 . 12 GLY HA3 H 3.72 . 1 54 . 13 CYS H H 6.45 . 1 55 . 13 CYS HA H 4.35 . 1 56 . 13 CYS HB2 H 1.49 . 1 57 . 13 CYS HB3 H 0.77 . 1 58 . 14 HIS H H 6.42 . 1 59 . 14 HIS HA H 3.01 . 1 60 . 14 HIS HB2 H 1.82 . 1 61 . 14 HIS HB3 H 1.10 . 1 62 . 14 HIS HD1 H 8.78 . 1 63 . 14 HIS HD2 H 0.37 . 1 64 . 14 HIS HE1 H 0.99 . 1 65 . 15 GLY H H 7.75 . 1 66 . 15 GLY HA2 H 4.23 . 1 67 . 15 GLY HA3 H 3.78 . 1 68 . 16 ALA HA H 4.13 . 1 69 . 16 ALA HB H 1.47 . 1 70 . 17 ASP H H 7.82 . 1 71 . 17 ASP HA H 4.51 . 1 72 . 17 ASP HB2 H 3.06 . 1 73 . 17 ASP HB3 H 2.48 . 1 74 . 18 GLY H H 7.06 . 1 75 . 18 GLY HA2 H 3.39 . 1 76 . 18 GLY HA3 H 3.39 . 1 77 . 19 SER H H 7.69 . 1 78 . 19 SER HA H 4.01 . 1 79 . 19 SER HB2 H 3.87 . 1 80 . 19 SER HB3 H 3.46 . 1 81 . 20 LYS H H 6.86 . 1 82 . 20 LYS HA H 3.85 . 1 83 . 20 LYS HB2 H 0.96 . 1 84 . 20 LYS HB3 H 0.96 . 1 85 . 20 LYS HG2 H 1.0 . 1 86 . 20 LYS HG3 H 0.9 . 1 87 . 20 LYS HD2 H 1.16 . 1 88 . 20 LYS HD3 H 1.16 . 1 89 . 20 LYS HE2 H 2.77 . 1 90 . 20 LYS HE3 H 2.77 . 1 91 . 21 ALA H H 8.39 . 1 92 . 21 ALA HA H 4.0 . 1 93 . 21 ALA HB H 1.11 . 1 94 . 22 ALA H H 7.2 . 1 95 . 22 ALA HA H 3.39 . 1 96 . 22 ALA HB H -0.83 . 1 97 . 23 MET H H 9.1 . 1 98 . 23 MET HA H 4.32 . 1 99 . 23 MET HB2 H 2.58 . 1 100 . 23 MET HB3 H 2.58 . 1 101 . 23 MET HG2 H 3.22 . 1 102 . 23 MET HG3 H 3.01 . 1 103 . 24 GLY H H 8.43 . 1 104 . 24 GLY HA2 H 4.32 . 1 105 . 24 GLY HA3 H 3.72 . 1 106 . 25 SER H H 7.94 . 1 107 . 25 SER HA H 4.8 . 1 108 . 25 SER HB2 H 4.05 . 1 109 . 25 SER HB3 H 3.98 . 1 110 . 26 ALA H H 7.8 . 1 111 . 26 ALA HA H 4.8 . 1 112 . 26 ALA HB H 1.58 . 1 113 . 27 LYS H H 8.27 . 1 114 . 27 LYS HA H 4.41 . 1 115 . 27 LYS HB2 H 1.78 . 1 116 . 27 LYS HB3 H 1.78 . 1 117 . 27 LYS HG2 H 1.64 . 1 118 . 27 LYS HG3 H 1.59 . 1 119 . 27 LYS HE2 H 3.11 . 1 120 . 27 LYS HE3 H 3.11 . 1 121 . 28 PRO HA H 3.89 . 1 122 . 28 PRO HB2 H 2.01 . 1 123 . 28 PRO HB3 H 1.68 . 1 124 . 29 VAL H H 7.51 . 1 125 . 29 VAL HA H 3.97 . 1 126 . 29 VAL HB H 2.21 . 1 127 . 29 VAL HG1 H 0.38 . 1 128 . 29 VAL HG2 H -0.05 . 1 129 . 30 LYS H H 7.21 . 1 130 . 30 LYS HA H 3.96 . 1 131 . 30 LYS HB2 H 1.63 . 1 132 . 30 LYS HB3 H 1.23 . 1 133 . 30 LYS HG2 H 1.02 . 1 134 . 30 LYS HG3 H 1.02 . 1 135 . 30 LYS HD2 H 1.51 . 1 136 . 30 LYS HD3 H 1.38 . 1 137 . 30 LYS HE2 H 2.92 . 1 138 . 30 LYS HE3 H 2.92 . 1 139 . 31 GLY H H 9.42 . 1 140 . 31 GLY HA2 H 4.13 . 1 141 . 31 GLY HA3 H 3.72 . 1 142 . 32 GLN H H 7.58 . 1 143 . 32 GLN HA H 4.46 . 1 144 . 32 GLN HB2 H 2.03 . 1 145 . 32 GLN HB3 H 2.03 . 1 146 . 32 GLN HG2 H 2.43 . 1 147 . 32 GLN HG3 H 2.08 . 1 148 . 32 GLN HE21 H 8.62 . 1 149 . 32 GLN HE22 H 7.4 . 1 150 . 33 GLY H H 8.88 . 1 151 . 33 GLY HA2 H 4.25 . 1 152 . 33 GLY HA3 H 4.05 . 1 153 . 34 ALA H H 8.9 . 1 154 . 34 ALA HA H 4.08 . 1 155 . 34 ALA HB H 1.54 . 1 156 . 35 GLU H H 8.8 . 1 157 . 35 GLU HA H 4.14 . 1 158 . 35 GLU HB2 H 2.08 . 1 159 . 35 GLU HB3 H 2.15 . 1 160 . 35 GLU HG2 H 2.37 . 1 161 . 35 GLU HG3 H 2.37 . 1 162 . 36 GLU H H 7.89 . 1 163 . 36 GLU HA H 4.17 . 1 164 . 36 GLU HB2 H 2.31 . 1 165 . 36 GLU HB3 H 2.18 . 1 166 . 36 GLU HG2 H 2.64 . 1 167 . 36 GLU HG3 H 2.46 . 1 168 . 37 LEU H H 8.48 . 1 169 . 37 LEU HA H 4.26 . 1 170 . 37 LEU HB2 H 2.31 . 1 171 . 37 LEU HB3 H 1.54 . 1 172 . 37 LEU HG H 2.0 . 1 173 . 37 LEU HD1 H 1.22 . 1 174 . 37 LEU HD2 H 1.02 . 1 175 . 38 TYR H H 8.55 . 1 176 . 38 TYR HA H 4.12 . 1 177 . 38 TYR HB2 H 3.18 . 1 178 . 38 TYR HB3 H 3.07 . 1 179 . 38 TYR HD1 H 6.89 . 1 180 . 38 TYR HD2 H 6.89 . 1 181 . 38 TYR HE1 H 6.89 . 1 182 . 38 TYR HE2 H 6.89 . 1 183 . 39 LYS H H 8.18 . 1 184 . 39 LYS HA H 3.59 . 1 185 . 39 LYS HB2 H 1.97 . 1 186 . 39 LYS HB3 H 1.83 . 1 187 . 39 LYS HG2 H 1.42 . 1 188 . 39 LYS HG3 H 1.42 . 1 189 . 39 LYS HD2 H 1.71 . 1 190 . 39 LYS HD3 H 1.71 . 1 191 . 39 LYS HE2 H 3.0 . 1 192 . 39 LYS HE3 H 3.0 . 1 193 . 40 LYS H H 7.97 . 1 194 . 40 LYS HA H 3.12 . 1 195 . 40 LYS HB2 H 2.12 . 1 196 . 40 LYS HB3 H 1.62 . 1 197 . 40 LYS HG2 H 0.38 . 1 198 . 40 LYS HG3 H 0.38 . 1 199 . 41 MET H H 8.23 . 1 200 . 41 MET HA H 3.7 . 1 201 . 41 MET HB2 H 1.85 . 1 202 . 41 MET HB3 H 2.18 . 1 203 . 41 MET HG2 H 2.42 . 1 204 . 41 MET HG3 H 2.42 . 1 205 . 42 LYS H H 8.38 . 1 206 . 42 LYS HA H 3.62 . 1 207 . 42 LYS HB2 H 1.39 . 1 208 . 42 LYS HB3 H 1.48 . 1 209 . 42 LYS HG2 H 0.95 . 1 210 . 42 LYS HG3 H 0.95 . 1 211 . 43 GLY H H 7.64 . 1 212 . 43 GLY HA2 H 4.03 . 1 213 . 43 GLY HA3 H 3.33 . 1 214 . 44 TYR H H 8.41 . 1 215 . 44 TYR HA H 4.22 . 1 216 . 44 TYR HB2 H 2.18 . 1 217 . 44 TYR HB3 H 1.74 . 1 218 . 44 TYR HD1 H 6.24 . 1 219 . 44 TYR HD2 H 6.24 . 1 220 . 44 TYR HE1 H 6.5 . 1 221 . 44 TYR HE2 H 6.5 . 1 222 . 45 ALA H H 7.86 . 1 223 . 45 ALA HA H 3.71 . 1 224 . 45 ALA HB H 1.33 . 1 225 . 46 ASP H H 7.76 . 1 226 . 46 ASP HA H 4.61 . 1 227 . 46 ASP HB2 H 2.94 . 1 228 . 46 ASP HB3 H 2.54 . 1 229 . 47 GLY H H 7.59 . 1 230 . 47 GLY HA2 H 4.14 . 1 231 . 47 GLY HA3 H 3.71 . 1 232 . 48 SER H H 8.79 . 1 233 . 48 SER HA H 4.35 . 1 234 . 48 SER HB2 H 3.99 . 1 235 . 48 SER HB3 H 3.71 . 1 236 . 49 TYR H H 7.07 . 1 237 . 49 TYR HA H 4.38 . 1 238 . 49 TYR HB2 H 2.81 . 1 239 . 49 TYR HB3 H 1.81 . 1 240 . 49 TYR HD1 H 6.3 . 1 241 . 49 TYR HD2 H 6.3 . 1 242 . 49 TYR HE1 H 7.07 . 1 243 . 49 TYR HE2 H 7.07 . 1 244 . 50 GLY H H 6.44 . 1 245 . 50 GLY HA2 H 4.47 . 1 246 . 50 GLY HA3 H 3.08 . 1 247 . 51 GLY H H 10.41 . 1 248 . 51 GLY HA2 H 4.54 . 1 249 . 51 GLY HA3 H 3.95 . 1 250 . 52 GLU H H 9.0 . 1 251 . 52 GLU HA H 4.16 . 1 252 . 52 GLU HB2 H 2.23 . 1 253 . 52 GLU HB3 H 2.23 . 1 254 . 52 GLU HG2 H 2.47 . 1 255 . 52 GLU HG3 H 2.47 . 1 256 . 53 ARG H H 8.22 . 1 257 . 53 ARG HA H 4.77 . 1 258 . 53 ARG HB2 H 2.22 . 1 259 . 53 ARG HB3 H 2.62 . 1 260 . 53 ARG HG2 H 1.88 . 1 261 . 53 ARG HG3 H 1.82 . 1 262 . 53 ARG HD2 H 3.56 . 1 263 . 53 ARG HD3 H 3.56 . 1 264 . 54 LYS H H 7.44 . 1 265 . 54 LYS HA H 3.57 . 1 266 . 54 LYS HB2 H 2.06 . 1 267 . 54 LYS HB3 H 2.06 . 1 268 . 54 LYS HG2 H 1.45 . 1 269 . 54 LYS HG3 H 1.35 . 1 270 . 54 LYS HE2 H 2.8 . 1 271 . 54 LYS HE3 H 2.8 . 1 272 . 55 ALA H H 8.49 . 1 273 . 55 ALA HA H 3.84 . 1 274 . 55 ALA HB H 1.28 . 1 275 . 56 MET H H 7.4 . 1 276 . 56 MET HA H 3.72 . 1 277 . 56 MET HB2 H 1.91 . 1 278 . 56 MET HB3 H 1.86 . 1 279 . 56 MET HG2 H 2.51 . 1 280 . 56 MET HG3 H 2.51 . 1 281 . 57 MET H H 5.8 . 1 282 . 57 MET HA H 1.75 . 1 283 . 57 MET HB2 H -0.78 . 1 284 . 58 THR H H 8.05 . 1 285 . 58 THR HA H 2.89 . 1 286 . 58 THR HB H 3.65 . 1 287 . 58 THR HG2 H 1.04 . 1 288 . 59 ASN H H 6.93 . 1 289 . 59 ASN HA H 4.04 . 1 290 . 59 ASN HB2 H 2.48 . 1 291 . 59 ASN HB3 H 2.48 . 1 292 . 59 ASN HD21 H 7.41 . 1 293 . 59 ASN HD22 H 6.78 . 1 294 . 60 ALA H H 6.37 . 1 295 . 60 ALA HA H 3.91 . 1 296 . 60 ALA HB H 0.23 . 1 297 . 61 VAL H H 6.49 . 1 298 . 61 VAL HA H 4.29 . 1 299 . 61 VAL HB H 2.15 . 1 300 . 61 VAL HG1 H 0.25 . 1 301 . 61 VAL HG2 H 0.0 . 1 302 . 62 LYS H H 7.45 . 1 303 . 62 LYS HA H 3.9 . 1 304 . 62 LYS HB2 H 1.95 . 1 305 . 62 LYS HB3 H 1.78 . 1 306 . 62 LYS HG2 H 1.25 . 1 307 . 62 LYS HG3 H 1.25 . 1 308 . 62 LYS HD2 H 1.56 . 1 309 . 62 LYS HD3 H 1.56 . 1 310 . 62 LYS HE2 H 2.9 . 1 311 . 62 LYS HE3 H 2.9 . 1 312 . 63 LYS H H 8.04 . 1 313 . 63 LYS HA H 4.33 . 1 314 . 63 LYS HB2 H 1.98 . 1 315 . 63 LYS HB3 H 1.68 . 1 316 . 63 LYS HG2 H 1.36 . 1 317 . 63 LYS HG3 H 1.36 . 1 318 . 63 LYS HD2 H 1.41 . 1 319 . 63 LYS HD3 H 1.41 . 1 320 . 64 ALA H H 7.27 . 1 321 . 64 ALA HA H 4.55 . 1 322 . 64 ALA HB H 1.41 . 1 323 . 65 SER H H 9.10 . 1 324 . 65 SER HA H 4.64 . 1 325 . 65 SER HB2 H 4.46 . 1 326 . 65 SER HB3 H 4.09 . 1 327 . 66 ASP H H 9.02 . 1 328 . 66 ASP HA H 4.53 . 1 329 . 66 ASP HB2 H 2.78 . 1 330 . 66 ASP HB3 H 2.78 . 1 331 . 67 GLU H H 8.54 . 1 332 . 67 GLU HA H 4.01 . 1 333 . 67 GLU HB2 H 2.0 . 1 334 . 67 GLU HB3 H 2.16 . 1 335 . 67 GLU HG2 H 2.40 . 1 336 . 67 GLU HG3 H 2.32 . 1 337 . 68 GLU H H 7.85 . 1 338 . 68 GLU HA H 3.83 . 1 339 . 68 GLU HB2 H 2.65 . 1 340 . 68 GLU HB3 H 1.97 . 1 341 . 68 GLU HG2 H 2.47 . 1 342 . 68 GLU HG3 H 2.32 . 1 343 . 69 LEU H H 8.58 . 1 344 . 69 LEU HA H 4.35 . 1 345 . 69 LEU HB2 H 2.51 . 1 346 . 69 LEU HB3 H 1.51 . 1 347 . 69 LEU HD1 H 0.91 . 1 348 . 69 LEU HD2 H 0.77 . 1 349 . 70 LYS H H 8.7 . 1 350 . 70 LYS HA H 3.92 . 1 351 . 70 LYS HB2 H 1.85 . 1 352 . 70 LYS HB3 H 1.85 . 1 353 . 70 LYS HG2 H 1.45 . 1 354 . 70 LYS HG3 H 0.97 . 1 355 . 70 LYS HD2 H 1.35 . 1 356 . 70 LYS HD3 H 1.35 . 1 357 . 70 LYS HE2 H 2.52 . 1 358 . 70 LYS HE3 H 2.46 . 1 359 . 71 ALA H H 8.02 . 1 360 . 71 ALA HA H 4.38 . 1 361 . 71 ALA HB H 1.53 . 1 362 . 72 LEU H H 8.79 . 1 363 . 72 LEU HA H 4.24 . 1 364 . 72 LEU HB2 H 2.56 . 1 365 . 72 LEU HB3 H 1.99 . 1 366 . 72 LEU HG H 1.8 . 1 367 . 72 LEU HD1 H 1.57 . 1 368 . 72 LEU HD2 H 1.33 . 1 369 . 73 ALA H H 8.7 . 1 370 . 73 ALA HA H 4.18 . 1 371 . 73 ALA HB H 1.92 . 1 372 . 74 ASP H H 8.28 . 1 373 . 74 ASP HA H 4.3 . 1 374 . 74 ASP HB2 H 2.84 . 1 375 . 74 ASP HB3 H 2.84 . 1 376 . 75 TYR H H 8.23 . 1 377 . 75 TYR HA H 4.04 . 1 378 . 75 TYR HB2 H 3.25 . 1 379 . 75 TYR HB3 H 3.01 . 1 380 . 75 TYR HD1 H 6.72 . 1 381 . 75 TYR HD2 H 6.72 . 1 382 . 75 TYR HE1 H 6.52 . 1 383 . 75 TYR HE2 H 6.52 . 1 384 . 76 MET H H 8.93 . 1 385 . 76 MET HA H 3.49 . 1 386 . 76 MET HB2 H 2.4 . 1 387 . 76 MET HB3 H 1.69 . 1 388 . 76 MET HG2 H 3.06 . 1 389 . 76 MET HG3 H 1.95 . 1 390 . 76 MET HE H 2.79 . 1 391 . 77 SER H H 7.95 . 1 392 . 77 SER HA H 4.46 . 1 393 . 77 SER HB2 H 4.28 . 1 394 . 77 SER HB3 H 4.05 . 1 395 . 78 LYS H H 7.07 . 1 396 . 78 LYS HA H 4.35 . 1 397 . 78 LYS HB2 H 1.99 . 1 398 . 78 LYS HB3 H 1.53 . 1 399 . 78 LYS HG2 H 1.37 . 1 400 . 78 LYS HG3 H 1.37 . 1 401 . 78 LYS HD2 H 1.66 . 1 402 . 78 LYS HD3 H 1.66 . 1 403 . 78 LYS HE2 H 2.97 . 1 404 . 78 LYS HE3 H 2.97 . 1 405 . 79 LEU H H 6.86 . 1 406 . 79 LEU HA H 3.67 . 1 407 . 79 LEU HB2 H 1.45 . 1 408 . 79 LEU HB3 H 1.2 . 1 409 . 79 LEU HG H 1.12 . 1 410 . 79 LEU HD1 H 0.38 . 1 411 . 79 LEU HD2 H 0.14 . 1 stop_ save_