data_4268 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 7-Fe Ferredoxin from Bacillus Schlegelii ; _BMRB_accession_number 4268 _BMRB_flat_file_name bmr4268.str _Entry_type original _Submission_date 1998-11-18 _Accession_date 1998-11-18 _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 Aono S. . . 2 Bentrop D. . . 3 Bertini I. . . 4 Donaire A. . . 5 Luchinat C. . . 6 Niikura Y. . . 7 Rosato A. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 351 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-14 original BMRB . stop_ _Original_release_date 1998-11-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Aono, S., Bentrop, D., Bertini, I., Donaire, A., Luchinat, C., Niikura, Y., and Rosato, A., "Solution Structure of the Oxidized Fe7S8 Ferredoxin from the Thermophilic Bacterium Bacillus Schlegelii by 1H NMR Spectroscopy," Biochemistry 37, 9812-9826 (1998). ; _Citation_title ; Solution Structure of the Oxidized Fe7S8 Ferredoxin from the Thermophilic Bacterium Bacillus Schlegelii by 1H NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98322084 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aono S. . . 2 Bentrop D. . . 3 Bertini I. . . 4 Donaire A. . . 5 Luchinat C. . . 6 Niikura Y. . . 7 Rosato A. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9812 _Page_last 9826 _Year 1998 _Details . loop_ _Keyword 'electron transport' iron-sulfur stop_ save_ ################################## # Molecular system description # ################################## save_system_Fd _Saveframe_category molecular_system _Mol_system_name '7-Fe Ferredoxin' _Abbreviation_common Fd _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Fd peptide' $Fe7S8_Fd FS3 $entity_F3S FS4 $entity_SF4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'reduced and oxidized present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Fe7S8_Fd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '7-Fe Ferredoxin' _Abbreviation_common Fd _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; AYVITEPCIGTKDASCVEVC PVDCIHEGEDQYYIDPDVCI DCGACEAVCPVSAIYHEDFV PEEWKSYIQKNRDFFKK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 TYR 3 VAL 4 ILE 5 THR 6 GLU 7 PRO 8 CYS 9 ILE 10 GLY 11 THR 12 LYS 13 ASP 14 ALA 15 SER 16 CYS 17 VAL 18 GLU 19 VAL 20 CYS 21 PRO 22 VAL 23 ASP 24 CYS 25 ILE 26 HIS 27 GLU 28 GLY 29 GLU 30 ASP 31 GLN 32 TYR 33 TYR 34 ILE 35 ASP 36 PRO 37 ASP 38 VAL 39 CYS 40 ILE 41 ASP 42 CYS 43 GLY 44 ALA 45 CYS 46 GLU 47 ALA 48 VAL 49 CYS 50 PRO 51 VAL 52 SER 53 ALA 54 ILE 55 TYR 56 HIS 57 GLU 58 ASP 59 PHE 60 VAL 61 PRO 62 GLU 63 GLU 64 TRP 65 LYS 66 SER 67 TYR 68 ILE 69 GLN 70 LYS 71 ASN 72 ARG 73 ASP 74 PHE 75 PHE 76 LYS 77 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_F3S _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FE3-S4 CLUSTER' _BMRB_code F3S _PDB_code F3S _Molecular_mass 295.795 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE3 FE3 FE . 0 . ? FE4 FE4 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? S3 S3 S . 0 . ? S4 S4 S . 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 FE1 S1 ? ? SING FE1 S2 ? ? SING FE1 S3 ? ? SING FE3 S1 ? ? SING FE3 S3 ? ? SING FE3 S4 ? ? SING FE4 S2 ? ? SING FE4 S3 ? ? SING FE4 S4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_SF4 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'IRON/SULFUR CLUSTER' _BMRB_code SF4 _PDB_code SF4 _Molecular_mass 351.640 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? FE3 FE3 FE . 0 . ? FE4 FE4 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? S3 S3 S . 0 . ? S4 S4 S . 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 FE1 S2 ? ? SING FE1 S3 ? ? SING FE1 S4 ? ? SING FE2 S1 ? ? SING FE2 S3 ? ? SING FE2 S4 ? ? SING FE3 S1 ? ? SING FE3 S2 ? ? SING FE3 S4 ? ? SING FE4 S1 ? ? SING FE4 S2 ? ? SING FE4 S3 ? ? 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 _ATCC_number $Fe7S8_Fd 'B. schlegelli' . Eubacteria . 'Bacillus schlegelii' bacilli 43741 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 $Fe7S8_Fd 'recombinant technology' 'E. coli' Escherichia coli JM_109 plasmid pKKFd54 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Fe7S8_Fd . mM 2 3.5 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_one save_ save_1D-NOE_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1D-NOE _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.020 0.1 M pH 6.5 0.1 na pressure 1 . atm temperature 298 0.05 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; Several resonances corresponding to three spin systems without a detectable backbone amide proton were observed. They could not be assigned sequence specifically due to the absence of interresidual NOEs. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Fd peptide' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 4.13 0.02 1 2 . 1 ALA HB H 1.57 0.02 1 3 . 2 TYR H H 7.05 0.02 9 4 . 2 TYR HA H 5.07 0.02 1 5 . 2 TYR HB2 H 4.11 0.02 2 6 . 2 TYR HD1 H 6.70 0.02 9 7 . 3 VAL H H 8.99 0.02 1 8 . 3 VAL HA H 4.10 0.02 1 9 . 3 VAL HB H 1.94 0.02 1 10 . 3 VAL HG1 H 0.89 0.02 2 11 . 4 ILE H H 7.58 0.02 1 12 . 4 ILE HA H 4.20 0.02 1 13 . 4 ILE HB H 2.78 0.02 1 14 . 4 ILE HG12 H 1.06 0.02 2 15 . 4 ILE HG2 H 0.88 0.02 1 16 . 5 THR H H 8.47 0.02 1 17 . 5 THR HA H 4.08 0.02 1 18 . 5 THR HB H 3.35 0.02 1 19 . 5 THR HG2 H 1.40 0.02 1 20 . 6 GLU HA H 3.33 0.02 1 21 . 6 GLU HB2 H 0.71 0.02 1 22 . 6 GLU HB3 H 0.77 0.02 1 23 . 6 GLU HG2 H 1.94 0.02 1 24 . 6 GLU HG3 H 2.21 0.02 1 25 . 7 PRO HA H 4.32 0.02 1 26 . 7 PRO HB2 H 2.37 0.02 2 27 . 7 PRO HB3 H 1.30 0.02 2 28 . 7 PRO HG2 H 1.96 0.02 2 29 . 7 PRO HD2 H 2.21 0.02 1 30 . 7 PRO HD3 H 2.90 0.02 1 31 . 9 ILE H H 7.98 0.02 1 32 . 9 ILE HA H 4.30 0.02 1 33 . 9 ILE HB H 1.94 0.02 1 34 . 9 ILE HG12 H 1.07 0.02 2 35 . 9 ILE HG13 H 1.55 0.02 2 36 . 9 ILE HG2 H 0.95 0.02 1 37 . 9 ILE HD1 H 0.79 0.02 1 38 . 10 GLY H H 9.17 0.02 1 39 . 10 GLY HA2 H 4.35 0.02 1 40 . 10 GLY HA3 H 3.72 0.02 1 41 . 11 THR H H 8.73 0.02 1 42 . 11 THR HA H 4.72 0.02 1 43 . 11 THR HB H 3.45 0.02 1 44 . 11 THR HG2 H 1.70 0.02 1 45 . 15 SER HA H 3.80 0.02 9 46 . 15 SER HB2 H 3.67 0.02 9 47 . 15 SER HB3 H 3.58 0.02 9 48 . 16 CYS HA H 8.82 0.02 1 49 . 16 CYS HB2 H 18.3 0.02 1 50 . 16 CYS HB3 H 6.6 0.02 1 51 . 17 VAL HA H 4.87 0.02 9 52 . 17 VAL HB H 2.86 0.02 9 53 . 17 VAL HG1 H 0.93 0.02 9 54 . 17 VAL HG2 H 1.01 0.02 9 55 . 18 GLU H H 6.96 0.02 1 56 . 18 GLU HA H 4.10 0.02 1 57 . 18 GLU HB2 H 2.15 0.02 2 58 . 18 GLU HB3 H 2.06 0.02 2 59 . 18 GLU HG2 H 2.38 0.02 1 60 . 18 GLU HG3 H 2.29 0.02 1 61 . 19 VAL H H 6.69 0.02 1 62 . 19 VAL HA H 4.49 0.02 1 63 . 19 VAL HB H 2.22 0.02 1 64 . 19 VAL HG1 H 0.79 0.02 1 65 . 19 VAL HG2 H 0.37 0.02 1 66 . 20 CYS H H 7.20 0.02 1 67 . 20 CYS HB2 H 10.35 0.02 1 68 . 20 CYS HB3 H 9.0 0.02 1 69 . 21 PRO HA H 5.14 0.02 1 70 . 21 PRO HB2 H 2.39 0.02 1 71 . 21 PRO HB3 H 2.75 0.02 1 72 . 21 PRO HD2 H 3.31 0.02 2 73 . 22 VAL HG1 H 1.16 0.02 9 74 . 23 ASP H H 7.48 0.02 1 75 . 23 ASP HA H 4.37 0.02 1 76 . 23 ASP HB2 H 2.97 0.02 1 77 . 23 ASP HB3 H 2.55 0.02 1 78 . 24 CYS HA H 6.27 0.02 1 79 . 24 CYS HB2 H 4.98 0.02 2 80 . 24 CYS HB3 H 2.37 0.02 2 81 . 25 ILE H H 7.99 0.02 1 82 . 25 ILE HA H 5.25 0.02 1 83 . 25 ILE HB H 1.85 0.02 1 84 . 25 ILE HG2 H 0.99 0.02 9 85 . 25 ILE HD1 H 0.83 0.02 9 86 . 26 HIS H H 9.77 0.02 1 87 . 26 HIS HA H 5.05 0.02 1 88 . 26 HIS HB2 H 3.71 0.02 2 89 . 26 HIS HB3 H 3.21 0.02 2 90 . 26 HIS HD2 H 7.28 0.02 1 91 . 26 HIS HE1 H 8.27 0.02 1 92 . 27 GLU H H 9.16 0.02 1 93 . 27 GLU HA H 2.67 0.02 1 94 . 27 GLU HB2 H 1.80 0.02 1 95 . 27 GLU HB3 H 1.20 0.02 1 96 . 27 GLU HG2 H 2.24 0.02 2 97 . 27 GLU HG3 H 1.41 0.02 2 98 . 28 GLY H H 7.78 0.02 1 99 . 28 GLY HA2 H 4.95 0.02 2 100 . 28 GLY HA3 H 3.85 0.02 2 101 . 29 GLU H H 9.23 0.02 1 102 . 29 GLU HA H 3.99 0.02 1 103 . 29 GLU HB2 H 2.08 0.02 1 104 . 29 GLU HB3 H 2.05 0.02 1 105 . 29 GLU HG2 H 2.36 0.02 2 106 . 29 GLU HG3 H 2.29 0.02 2 107 . 30 ASP H H 8.90 0.02 1 108 . 30 ASP HA H 4.56 0.02 1 109 . 30 ASP HB2 H 2.90 0.02 1 110 . 30 ASP HB3 H 2.67 0.02 1 111 . 31 GLN H H 7.32 0.02 1 112 . 31 GLN HA H 4.58 0.02 1 113 . 31 GLN HB2 H 2.05 0.02 1 114 . 31 GLN HB3 H 1.76 0.02 1 115 . 31 GLN HG2 H 0.52 0.02 1 116 . 31 GLN HG3 H 1.38 0.02 1 117 . 31 GLN HE21 H 5.58 0.02 2 118 . 31 GLN HE22 H 7.14 0.02 2 119 . 32 TYR H H 7.38 0.02 1 120 . 32 TYR HA H 5.42 0.02 1 121 . 32 TYR HB2 H 3.03 0.02 1 122 . 32 TYR HB3 H 2.56 0.02 1 123 . 32 TYR HD1 H 6.22 0.02 9 124 . 33 TYR H H 8.89 0.02 1 125 . 33 TYR HA H 4.92 0.02 1 126 . 33 TYR HB2 H 3.00 0.02 1 127 . 33 TYR HB3 H 2.28 0.02 1 128 . 33 TYR HD1 H 6.15 0.02 3 129 . 33 TYR HE1 H 6.22 0.02 3 130 . 33 TYR HH H 5.59 0.02 1 131 . 34 ILE H H 9.12 0.02 1 132 . 34 ILE HA H 5.04 0.02 1 133 . 34 ILE HB H 2.39 0.02 1 134 . 34 ILE HG12 H 1.99 0.02 4 135 . 35 ASP H H 8.45 0.02 1 136 . 35 ASP HA H 4.28 0.02 1 137 . 35 ASP HB2 H 2.55 0.02 2 138 . 35 ASP HB3 H 0.95 0.02 2 139 . 36 PRO HA H 4.25 0.02 1 140 . 36 PRO HB2 H 2.10 0.02 1 141 . 36 PRO HB3 H 2.42 0.02 1 142 . 36 PRO HG2 H 2.00 0.02 1 143 . 36 PRO HG3 H 1.96 0.02 1 144 . 36 PRO HD2 H 4.58 0.02 2 145 . 36 PRO HD3 H 4.23 0.02 2 146 . 37 ASP H H 8.18 0.02 1 147 . 37 ASP HA H 4.74 0.02 1 148 . 37 ASP HB2 H 2.78 0.02 1 149 . 37 ASP HB3 H 2.64 0.02 1 150 . 38 VAL H H 7.03 0.02 1 151 . 38 VAL HA H 4.04 0.02 1 152 . 38 VAL HB H 1.55 0.02 1 153 . 38 VAL HG1 H 0.94 0.02 1 154 . 38 VAL HG2 H 0.78 0.02 1 155 . 39 CYS H H 7.53 0.02 1 156 . 39 CYS HB2 H 11.0 0.02 1 157 . 39 CYS HB3 H 9.0 0.02 1 158 . 40 ILE HA H 5.27 0.02 1 159 . 40 ILE HB H 2.77 0.02 1 160 . 40 ILE HG12 H 1.14 0.02 4 161 . 40 ILE HD1 H 0.88 0.02 9 162 . 41 ASP H H 10.6 0.02 1 163 . 41 ASP HA H 5.34 0.02 1 164 . 41 ASP HB2 H 3.47 0.02 2 165 . 41 ASP HB3 H 3.13 0.02 2 166 . 42 CYS HA H 9.57 0.02 1 167 . 42 CYS HB2 H 9.44 0.02 1 168 . 42 CYS HB3 H 15.8 0.02 1 169 . 43 GLY HA2 H 4.20 0.02 9 170 . 43 GLY HA3 H 3.32 0.02 9 171 . 45 CYS HA H 7.30 0.02 1 172 . 45 CYS HB2 H 15.9 0.02 1 173 . 45 CYS HB3 H 5.2 0.02 1 174 . 46 GLU H H 7.57 0.02 9 175 . 46 GLU HB2 H 2.12 0.02 9 176 . 47 ALA H H 7.23 0.02 1 177 . 47 ALA HA H 4.24 0.02 1 178 . 47 ALA HB H 1.42 0.02 1 179 . 48 VAL H H 6.82 0.02 1 180 . 48 VAL HA H 4.46 0.02 1 181 . 48 VAL HB H 2.21 0.02 1 182 . 48 VAL HG1 H 0.81 0.02 2 183 . 48 VAL HG2 H 0.60 0.02 2 184 . 49 CYS H H 6.36 0.02 9 185 . 49 CYS HA H 3.85 0.02 9 186 . 49 CYS HB2 H 23.4 0.02 1 187 . 49 CYS HB3 H 32.2 0.02 1 188 . 50 PRO HA H 5.25 0.02 9 189 . 50 PRO HB2 H 2.07 0.02 9 190 . 50 PRO HB3 H 2.40 0.02 9 191 . 50 PRO HG2 H 2.23 0.02 9 192 . 51 VAL HA H 3.30 0.02 1 193 . 51 VAL HB H 2.06 0.02 1 194 . 51 VAL HG1 H 0.98 0.02 1 195 . 51 VAL HG2 H 0.88 0.02 1 196 . 52 SER H H 7.47 0.02 1 197 . 52 SER HA H 4.41 0.02 1 198 . 52 SER HB2 H 4.12 0.02 2 199 . 52 SER HB3 H 3.89 0.02 2 200 . 53 ALA H H 8.00 0.02 9 201 . 54 ILE H H 7.97 0.02 1 202 . 54 ILE HA H 5.07 0.02 1 203 . 54 ILE HB H 1.81 0.02 1 204 . 54 ILE HG12 H 1.26 0.02 9 205 . 54 ILE HG2 H 1.10 0.02 9 206 . 54 ILE HD1 H 0.61 0.02 9 207 . 55 TYR H H 8.49 0.02 1 208 . 55 TYR HA H 4.88 0.02 1 209 . 55 TYR HB2 H 2.48 0.02 1 210 . 55 TYR HB3 H 3.13 0.02 1 211 . 55 TYR HD1 H 7.19 0.02 3 212 . 55 TYR HE1 H 7.06 0.02 3 213 . 56 HIS H H 9.45 0.02 1 214 . 56 HIS HA H 3.29 0.02 1 215 . 56 HIS HB2 H 2.80 0.02 2 216 . 56 HIS HB3 H 2.45 0.02 2 217 . 56 HIS HD2 H 6.88 0.02 1 218 . 56 HIS HE1 H 7.74 0.02 1 219 . 57 GLU H H 7.80 0.02 1 220 . 57 GLU HA H 3.89 0.02 1 221 . 57 GLU HB2 H 1.84 0.02 2 222 . 57 GLU HB3 H 1.72 0.02 2 223 . 57 GLU HG2 H 2.14 0.02 2 224 . 57 GLU HG3 H 2.06 0.02 2 225 . 58 ASP H H 10.07 0.02 1 226 . 58 ASP HA H 4.49 0.02 1 227 . 58 ASP HB2 H 2.68 0.02 1 228 . 58 ASP HB3 H 2.35 0.02 1 229 . 59 PHE H H 8.63 0.02 1 230 . 59 PHE HA H 4.70 0.02 1 231 . 59 PHE HB2 H 2.98 0.02 1 232 . 59 PHE HB3 H 3.80 0.02 1 233 . 59 PHE HD1 H 7.40 0.02 3 234 . 60 VAL H H 7.00 0.02 1 235 . 60 VAL HA H 3.42 0.02 1 236 . 60 VAL HB H 1.88 0.02 1 237 . 60 VAL HG1 H 1.40 0.02 1 238 . 60 VAL HG2 H 1.06 0.02 1 239 . 61 PRO HA H 4.14 0.02 1 240 . 61 PRO HB2 H 2.10 0.02 2 241 . 61 PRO HB3 H 1.14 0.02 2 242 . 61 PRO HG2 H 1.78 0.02 2 243 . 61 PRO HG3 H 1.63 0.02 2 244 . 61 PRO HD2 H 2.90 0.02 1 245 . 61 PRO HD3 H 2.69 0.02 1 246 . 62 GLU H H 8.74 0.02 1 247 . 62 GLU HA H 3.87 0.02 1 248 . 62 GLU HB2 H 2.12 0.02 1 249 . 62 GLU HB3 H 1.94 0.02 1 250 . 62 GLU HG2 H 2.33 0.02 2 251 . 62 GLU HG3 H 2.30 0.02 2 252 . 63 GLU H H 9.70 0.02 1 253 . 63 GLU HA H 4.22 0.02 1 254 . 63 GLU HB2 H 1.78 0.02 2 255 . 63 GLU HB3 H 1.49 0.02 2 256 . 63 GLU HG2 H 1.67 0.02 2 257 . 64 TRP H H 8.31 0.02 1 258 . 64 TRP HA H 5.67 0.02 1 259 . 64 TRP HB2 H 3.79 0.02 2 260 . 64 TRP HB3 H 2.95 0.02 2 261 . 64 TRP HD1 H 7.38 0.02 1 262 . 64 TRP HE1 H 9.98 0.02 1 263 . 64 TRP HE3 H 7.23 0.02 1 264 . 64 TRP HZ2 H 7.50 0.02 3 265 . 64 TRP HZ3 H 7.53 0.02 3 266 . 64 TRP HH2 H 7.38 0.02 1 267 . 65 LYS H H 7.84 0.02 1 268 . 65 LYS HA H 4.03 0.02 1 269 . 65 LYS HB2 H 2.12 0.02 1 270 . 65 LYS HB3 H 2.07 0.02 1 271 . 65 LYS HG2 H 1.64 0.02 2 272 . 65 LYS HD2 H 1.72 0.02 2 273 . 65 LYS HE2 H 3.00 0.02 2 274 . 66 SER H H 9.24 0.02 1 275 . 66 SER HA H 4.29 0.02 1 276 . 66 SER HB2 H 4.03 0.02 2 277 . 66 SER HB3 H 3.92 0.02 2 278 . 67 TYR H H 8.83 0.02 1 279 . 67 TYR HA H 4.18 0.02 1 280 . 67 TYR HB2 H 3.43 0.02 1 281 . 67 TYR HB3 H 3.00 0.02 1 282 . 67 TYR HD1 H 7.57 0.02 3 283 . 67 TYR HE1 H 7.09 0.02 3 284 . 68 ILE H H 8.38 0.02 1 285 . 68 ILE HA H 3.88 0.02 1 286 . 68 ILE HB H 2.15 0.02 1 287 . 68 ILE HG12 H 1.27 0.02 2 288 . 68 ILE HG13 H 1.95 0.02 2 289 . 68 ILE HG2 H 1.07 0.02 1 290 . 68 ILE HD1 H 1.14 0.02 1 291 . 69 GLN H H 8.22 0.02 1 292 . 69 GLN HA H 4.08 0.02 1 293 . 69 GLN HB2 H 2.29 0.02 2 294 . 69 GLN HB3 H 2.13 0.02 2 295 . 69 GLN HG2 H 2.54 0.02 1 296 . 69 GLN HG3 H 2.49 0.02 1 297 . 69 GLN HE21 H 6.96 0.02 2 298 . 69 GLN HE22 H 8.26 0.02 2 299 . 70 LYS H H 8.12 0.02 1 300 . 70 LYS HA H 4.08 0.02 1 301 . 70 LYS HB2 H 2.06 0.02 1 302 . 70 LYS HB3 H 1.82 0.02 1 303 . 70 LYS HG2 H 1.57 0.02 1 304 . 70 LYS HG3 H 1.48 0.02 1 305 . 70 LYS HD2 H 2.99 0.02 2 306 . 70 LYS HE2 H 3.66 0.02 2 307 . 71 ASN H H 8.26 0.02 1 308 . 71 ASN HA H 4.92 0.02 1 309 . 71 ASN HB2 H 3.39 0.02 1 310 . 71 ASN HB3 H 3.77 0.02 1 311 . 71 ASN HD21 H 8.73 0.02 2 312 . 72 ARG H H 7.34 0.02 1 313 . 72 ARG HA H 4.03 0.02 1 314 . 72 ARG HB2 H 2.13 0.02 1 315 . 72 ARG HB3 H 2.06 0.02 1 316 . 72 ARG HG2 H 1.83 0.02 1 317 . 72 ARG HG3 H 1.62 0.02 1 318 . 72 ARG HD2 H 3.49 0.02 2 319 . 72 ARG HD3 H 3.15 0.02 2 320 . 72 ARG HE H 7.69 0.02 1 321 . 73 ASP H H 9.36 0.02 1 322 . 73 ASP HA H 4.41 0.02 1 323 . 73 ASP HB2 H 2.73 0.02 1 324 . 73 ASP HB3 H 2.66 0.02 1 325 . 74 PHE H H 7.33 0.02 1 326 . 74 PHE HA H 3.76 0.02 1 327 . 74 PHE HB2 H 2.16 0.02 2 328 . 74 PHE HB3 H 2.13 0.02 2 329 . 74 PHE HD1 H 5.70 0.02 3 330 . 74 PHE HE1 H 6.94 0.02 3 331 . 74 PHE HZ H 7.10 0.02 1 332 . 75 PHE H H 7.06 0.02 1 333 . 75 PHE HA H 4.12 0.02 1 334 . 75 PHE HB2 H 3.50 0.02 2 335 . 75 PHE HB3 H 2.75 0.02 2 336 . 75 PHE HD1 H 7.64 0.02 3 337 . 75 PHE HE1 H 7.31 0.02 3 338 . 75 PHE HZ H 7.46 0.02 1 339 . 76 LYS H H 7.39 0.02 1 340 . 76 LYS HA H 4.32 0.02 1 341 . 76 LYS HB2 H 1.91 0.02 1 342 . 76 LYS HB3 H 1.81 0.02 1 343 . 76 LYS HG2 H 1.54 0.02 2 344 . 76 LYS HG3 H 1.48 0.02 2 345 . 76 LYS HD2 H 1.70 0.02 2 346 . 76 LYS HE2 H 3.00 0.02 2 347 . 77 LYS H H 7.98 0.02 1 348 . 77 LYS HA H 4.16 0.02 1 349 . 77 LYS HB2 H 1.67 0.02 2 350 . 77 LYS HB3 H 1.63 0.02 2 351 . 77 LYS HG2 H 1.37 0.02 2 stop_ save_