data_4325 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of Monomeric and Dimeric B-domain of Staphylococcal Protein A. ; _BMRB_accession_number 4325 _BMRB_flat_file_name bmr4325.str _Entry_type original _Submission_date 1999-03-22 _Accession_date 1999-03-22 _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 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 743 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-09-13 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4324 monomer stop_ _Original_release_date 1999-09-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Karimi, A., Matsumura, M., Wright, P. E., and Dyson, H. J., "Characterization of Monomeric and Dimeric B-domain of Staphylococcal Protein A," J. Pept. Res. 54, 344-352 (1999). ; _Citation_title 'Characterization of Monomeric and Dimeric B-domain of Staphylococcal Protein A.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20000040 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ _Journal_abbreviation 'J. Pept. Res.' _Journal_name_full 'Journal of Peptide Research' _Journal_volume 54 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 344 _Page_last 352 _Year 1999 _Details . loop_ _Keyword NMR 'protein A' stop_ save_ ################################## # Molecular system description # ################################## save_system_FB2 _Saveframe_category molecular_system _Mol_system_name 'dimeric B domain of protein A' _Abbreviation_common FB2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dimeric B domain of protein A one' $FB2 'dimeric B domain of protein A two' $FB2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'dimeric B domain of protein A one' 1 'dimeric B domain of protein A two' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FB2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'dimer of B domain of protein A' _Abbreviation_common FB2 _Molecular_mass 13000 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; MADNKFNKEQQNAFYEILHL PNLNEEQRNGFIQSLKDDPS QSANLLAEAKKLNDAQAPKA DNKFNKEQQNAFYEILHLPN LNEEQRNGFIQSLKDDPSQS ANLLAEAKKLNDAQAPKADN KGS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 ASN 5 LYS 6 PHE 7 ASN 8 LYS 9 GLU 10 GLN 11 GLN 12 ASN 13 ALA 14 PHE 15 TYR 16 GLU 17 ILE 18 LEU 19 HIS 20 LEU 21 PRO 22 ASN 23 LEU 24 ASN 25 GLU 26 GLU 27 GLN 28 ARG 29 ASN 30 GLY 31 PHE 32 ILE 33 GLN 34 SER 35 LEU 36 LYS 37 ASP 38 ASP 39 PRO 40 SER 41 GLN 42 SER 43 ALA 44 ASN 45 LEU 46 LEU 47 ALA 48 GLU 49 ALA 50 LYS 51 LYS 52 LEU 53 ASN 54 ASP 55 ALA 56 GLN 57 ALA 58 PRO 59 LYS 60 ALA 61 ASP 62 ASN 63 LYS 64 PHE 65 ASN 66 LYS 67 GLU 68 GLN 69 GLN 70 ASN 71 ALA 72 PHE 73 TYR 74 GLU 75 ILE 76 LEU 77 HIS 78 LEU 79 PRO 80 ASN 81 LEU 82 ASN 83 GLU 84 GLU 85 GLN 86 ARG 87 ASN 88 GLY 89 PHE 90 ILE 91 GLN 92 SER 93 LEU 94 LYS 95 ASP 96 ASP 97 PRO 98 SER 99 GLN 100 SER 101 ALA 102 ASN 103 LEU 104 LEU 105 ALA 106 GLU 107 ALA 108 LYS 109 LYS 110 LEU 111 ASN 112 ASP 113 ALA 114 GLN 115 ALA 116 PRO 117 LYS 118 ALA 119 ASP 120 ASN 121 LYS 122 GLY 123 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-22 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 4NPF "High-resolution Structure Of Two Tandem B Domains Of Staphylococcal Protein A Connected By The Conserved Linker" 50.41 116 98.39 100.00 9.75e-32 EMBL CUD36484 "immunoglobulin G binding protein A [Staphylococcus aureus]" 71.54 303 98.86 98.86 1.63e-50 GB ACL54840 "truncated protein A, partial [Staphylococcus aureus]" 55.28 281 100.00 100.00 3.92e-35 GB EHS72728 "gram positive anchor, partial [Staphylococcus aureus subsp. aureus IS-157]" 61.79 287 97.37 100.00 2.38e-39 GB EIK36223 "hypothetical protein MQW_02849, partial [Staphylococcus aureus subsp. aureus VRS11b]" 80.49 209 96.97 100.00 1.24e-56 GB EUN97074 "immunoglobulin G-binding protein A, partial [Staphylococcus aureus M0981]" 82.11 336 97.03 100.00 1.85e-57 GB EUO28860 "immunoglobulin G-binding protein A, partial [Staphylococcus aureus M1057]" 82.11 336 97.03 100.00 1.85e-57 REF WP_031792806 "hypothetical protein, partial [Staphylococcus aureus]" 82.11 336 97.03 100.00 1.85e-57 REF WP_031794720 "immunoglobulin G-binding protein A, partial [Staphylococcus aureus]" 82.11 464 97.03 100.00 3.99e-57 REF WP_033863190 "hypothetical protein, partial [Staphylococcus aureus]" 52.85 308 100.00 100.00 3.13e-33 REF WP_049280869 "hypothetical protein, partial [Staphylococcus aureus]" 81.30 335 97.00 100.00 2.53e-56 REF WP_049307830 "hypothetical protein, partial [Staphylococcus aureus]" 79.67 293 96.94 100.00 3.17e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FB2 'golden staph.' 1280 Eubacteria . Staphylococcus aureus 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 _Details $FB2 vendor . . . . . ; commercial construct consists of two identical B domains covalently linked. Used for binding to immunoglobulins ; 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FB2 . mM 1.0 4.0 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H_2QF_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2QF COSY' _Sample_label . save_ save_1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label . save_ save_1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2QF COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 n/a temperature 303 1 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 dioxan H 1 'methylene protons' ppm 3.75 internal direct cylindrical internal parallel_to_Bo stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'dimeric B domain of protein A one' _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 ALA H H 8.37 0.02 1 2 . 2 ALA HA H 4.33 0.02 1 3 . 2 ALA HB H 1.39 0.02 1 4 . 3 ASP H H 8.32 0.02 1 5 . 3 ASP HA H 4.72 0.02 1 6 . 3 ASP HB2 H 2.80 0.02 1 7 . 3 ASP HB3 H 2.80 0.02 1 8 . 4 ASN H H 8.42 0.02 1 9 . 4 ASN HA H 4.60 0.02 1 10 . 4 ASN HB2 H 2.58 0.02 1 11 . 4 ASN HB3 H 2.58 0.02 1 12 . 4 ASN HD21 H 6.87 0.02 2 13 . 4 ASN HD22 H 7.52 0.02 2 14 . 5 LYS H H 8.25 0.02 1 15 . 5 LYS HA H 4.18 0.02 1 16 . 5 LYS HB2 H 1.70 0.02 1 17 . 5 LYS HB3 H 1.70 0.02 1 18 . 5 LYS HG2 H 1.25 0.02 1 19 . 5 LYS HG3 H 1.25 0.02 1 20 . 5 LYS HD2 H 1.60 0.02 1 21 . 5 LYS HD3 H 1.60 0.02 1 22 . 5 LYS HE2 H 2.93 0.02 1 23 . 5 LYS HE3 H 2.93 0.02 1 24 . 6 PHE H H 8.13 0.02 1 25 . 6 PHE HA H 5.03 0.02 1 26 . 6 PHE HB2 H 3.02 0.02 2 27 . 6 PHE HB3 H 3.34 0.02 2 28 . 6 PHE HD1 H 7.13 0.02 1 29 . 6 PHE HD2 H 7.13 0.02 1 30 . 6 PHE HE1 H 7.07 0.02 1 31 . 6 PHE HE2 H 7.07 0.02 1 32 . 7 ASN H H 8.45 0.02 4 33 . 7 ASN HA H 4.72 0.02 4 34 . 7 ASN HB2 H 2.94 0.02 2 35 . 7 ASN HB3 H 3.28 0.02 2 36 . 7 ASN HD21 H 6.92 0.02 4 37 . 7 ASN HD22 H 7.50 0.02 4 38 . 8 LYS H H 8.36 0.02 4 39 . 8 LYS HA H 3.99 0.02 4 40 . 8 LYS HB2 H 1.83 0.02 4 41 . 8 LYS HB3 H 1.88 0.02 4 42 . 8 LYS HG2 H 1.46 0.02 4 43 . 8 LYS HG3 H 1.53 0.02 4 44 . 8 LYS HD2 H 1.72 0.02 4 45 . 8 LYS HD3 H 1.72 0.02 4 46 . 9 GLU H H 8.26 0.02 4 47 . 9 GLU HA H 4.12 0.02 4 48 . 9 GLU HB2 H 2.07 0.02 4 49 . 9 GLU HB3 H 2.13 0.02 4 50 . 9 GLU HG2 H 2.34 0.02 4 51 . 9 GLU HG3 H 2.34 0.02 4 52 . 10 GLN H H 8.51 0.02 4 53 . 10 GLN HA H 3.89 0.02 4 54 . 10 GLN HB2 H 2.21 0.02 4 55 . 10 GLN HB3 H 2.21 0.02 4 56 . 10 GLN HG2 H 2.47 0.02 4 57 . 10 GLN HG3 H 2.47 0.02 4 58 . 10 GLN HE21 H 6.99 0.02 4 59 . 10 GLN HE22 H 7.29 0.02 4 60 . 11 GLN H H 8.66 0.02 1 61 . 11 GLN HA H 3.98 0.02 1 62 . 11 GLN HB2 H 2.21 0.02 1 63 . 11 GLN HB3 H 2.21 0.02 1 64 . 11 GLN HG2 H 2.47 0.02 1 65 . 11 GLN HG3 H 2.47 0.02 1 66 . 11 GLN HE21 H 6.83 0.02 2 67 . 11 GLN HE22 H 7.21 0.02 2 68 . 12 ASN H H 8.32 0.02 1 69 . 12 ASN HA H 4.62 0.02 4 70 . 12 ASN HB2 H 2.93 0.02 4 71 . 12 ASN HB3 H 2.93 0.02 4 72 . 12 ASN HD21 H 7.01 0.02 4 73 . 12 ASN HD22 H 7.73 0.02 4 74 . 13 ALA H H 7.95 0.02 4 75 . 13 ALA HA H 4.09 0.02 4 76 . 13 ALA HB H 1.48 0.02 4 77 . 14 PHE H H 8.17 0.02 4 78 . 14 PHE HA H 3.84 0.02 1 79 . 14 PHE HB2 H 2.97 0.02 2 80 . 14 PHE HB3 H 3.32 0.02 4 81 . 14 PHE HD1 H 7.04 0.02 1 82 . 14 PHE HD2 H 7.04 0.02 1 83 . 14 PHE HE1 H 7.29 0.02 1 84 . 14 PHE HE2 H 7.29 0.02 1 85 . 14 PHE HZ H 7.19 0.02 1 86 . 15 TYR H H 8.13 0.02 4 87 . 15 TYR HA H 3.95 0.02 4 88 . 15 TYR HB2 H 3.18 0.02 4 89 . 15 TYR HB3 H 3.18 0.02 4 90 . 15 TYR HD1 H 6.72 0.02 1 91 . 15 TYR HD2 H 6.72 0.02 1 92 . 15 TYR HE1 H 7.15 0.02 1 93 . 15 TYR HE2 H 7.15 0.02 1 94 . 16 GLU H H 8.57 0.02 4 95 . 16 GLU HA H 4.01 0.02 4 96 . 16 GLU HB2 H 2.01 0.02 4 97 . 16 GLU HB3 H 2.16 0.02 4 98 . 16 GLU HG2 H 2.26 0.02 4 99 . 16 GLU HG3 H 2.48 0.02 4 100 . 17 ILE H H 8.45 0.02 4 101 . 17 ILE HA H 3.41 0.02 4 102 . 17 ILE HB H 1.80 0.02 4 103 . 17 ILE HG12 H 1.87 0.02 4 104 . 17 ILE HG13 H 1.87 0.02 4 105 . 17 ILE HG2 H 0.78 0.02 4 106 . 17 ILE HD1 H 0.51 0.02 4 107 . 18 LEU H H 7.86 0.02 1 108 . 18 LEU HA H 3.71 0.02 4 109 . 18 LEU HB2 H 1.13 0.02 2 110 . 18 LEU HB3 H 1.49 0.02 4 111 . 18 LEU HG H 1.38 0.02 1 112 . 18 LEU HD1 H 0.58 0.02 4 113 . 18 LEU HD2 H 0.67 0.02 4 114 . 19 HIS H H 7.24 0.02 1 115 . 19 HIS HA H 4.49 0.02 1 116 . 19 HIS HB2 H 2.79 0.02 2 117 . 19 HIS HB3 H 3.46 0.02 4 118 . 19 HIS HD2 H 7.09 0.02 1 119 . 19 HIS HE1 H 8.27 0.02 1 120 . 20 LEU H H 7.23 0.02 4 121 . 20 LEU HA H 4.50 0.02 4 122 . 20 LEU HB2 H 1.37 0.02 4 123 . 20 LEU HB3 H 1.73 0.02 4 124 . 20 LEU HG H 2.21 0.02 4 125 . 20 LEU HD1 H 0.68 0.02 4 126 . 20 LEU HD2 H 0.87 0.02 4 127 . 21 PRO HA H 4.42 0.02 4 128 . 21 PRO HB2 H 2.04 0.02 4 129 . 21 PRO HB3 H 2.17 0.02 4 130 . 21 PRO HG2 H 1.98 0.02 4 131 . 21 PRO HG3 H 1.98 0.02 4 132 . 21 PRO HD2 H 3.82 0.02 4 133 . 21 PRO HD3 H 4.07 0.02 4 134 . 22 ASN H H 8.87 0.02 4 135 . 22 ASN HA H 5.01 0.02 4 136 . 22 ASN HB2 H 2.89 0.02 4 137 . 22 ASN HB3 H 2.89 0.02 4 138 . 22 ASN HD21 H 6.99 0.02 2 139 . 22 ASN HD22 H 7.36 0.02 2 140 . 23 LEU H H 6.53 0.02 4 141 . 23 LEU HA H 4.45 0.02 4 142 . 23 LEU HB2 H 1.63 0.02 4 143 . 23 LEU HB3 H 1.71 0.02 4 144 . 23 LEU HG H 1.71 0.02 4 145 . 23 LEU HD1 H 0.90 0.02 4 146 . 23 LEU HD2 H 0.97 0.02 4 147 . 24 ASN H H 8.55 0.02 4 148 . 24 ASN HA H 4.92 0.02 4 149 . 24 ASN HB2 H 2.82 0.02 4 150 . 24 ASN HB3 H 3.29 0.02 4 151 . 24 ASN HD21 H 7.03 0.02 4 152 . 24 ASN HD22 H 7.50 0.02 4 153 . 25 GLU H H 8.62 0.02 4 154 . 25 GLU HA H 3.95 0.02 4 155 . 25 GLU HB2 H 2.04 0.02 4 156 . 25 GLU HB3 H 2.04 0.02 4 157 . 25 GLU HG2 H 2.37 0.02 4 158 . 25 GLU HG3 H 2.37 0.02 4 159 . 26 GLU H H 8.26 0.02 4 160 . 26 GLU HA H 4.07 0.02 4 161 . 26 GLU HB2 H 2.04 0.02 4 162 . 26 GLU HB3 H 2.04 0.02 4 163 . 26 GLU HG2 H 2.30 0.02 4 164 . 26 GLU HG3 H 2.30 0.02 4 165 . 27 GLN H H 8.60 0.02 4 166 . 27 GLN HA H 3.89 0.02 4 167 . 27 GLN HB2 H 2.48 0.02 4 168 . 27 GLN HB3 H 2.48 0.02 4 169 . 27 GLN HG2 H 2.33 0.02 4 170 . 27 GLN HG3 H 2.79 0.02 4 171 . 27 GLN HE21 H 7.61 0.02 4 172 . 27 GLN HE22 H 8.27 0.02 4 173 . 28 ARG H H 8.63 0.02 4 174 . 28 ARG HA H 3.78 0.02 4 175 . 28 ARG HB2 H 1.76 0.02 4 176 . 28 ARG HB3 H 1.88 0.02 4 177 . 28 ARG HG2 H 1.48 0.02 4 178 . 28 ARG HG3 H 1.48 0.02 4 179 . 28 ARG HD2 H 3.25 0.02 4 180 . 28 ARG HD3 H 3.40 0.02 4 181 . 28 ARG HE H 7.58 0.02 4 182 . 29 ASN H H 8.63 0.02 4 183 . 29 ASN HA H 4.42 0.02 4 184 . 29 ASN HB2 H 2.80 0.02 4 185 . 29 ASN HB3 H 2.90 0.02 4 186 . 29 ASN HD21 H 6.99 0.02 4 187 . 29 ASN HD22 H 7.63 0.02 4 188 . 30 GLY H H 8.05 0.02 4 189 . 30 GLY HA2 H 3.89 0.02 4 190 . 30 GLY HA3 H 3.89 0.02 4 191 . 31 PHE H H 7.84 0.02 4 192 . 31 PHE HA H 4.48 0.02 4 193 . 31 PHE HB2 H 3.04 0.02 4 194 . 31 PHE HB3 H 3.04 0.02 4 195 . 31 PHE HD1 H 7.26 0.02 4 196 . 31 PHE HD2 H 7.26 0.02 4 197 . 31 PHE HE1 H 7.28 0.02 4 198 . 31 PHE HE2 H 7.28 0.02 4 199 . 31 PHE HZ H 7.15 0.02 4 200 . 32 ILE H H 8.27 0.02 4 201 . 32 ILE HA H 3.75 0.02 4 202 . 32 ILE HB H 2.13 0.02 4 203 . 32 ILE HG12 H 1.37 0.02 4 204 . 32 ILE HG13 H 1.61 0.02 4 205 . 32 ILE HG2 H 0.99 0.02 4 206 . 32 ILE HD1 H 0.66 0.02 4 207 . 33 GLN H H 8.43 0.02 4 208 . 33 GLN HA H 3.95 0.02 4 209 . 33 GLN HB2 H 2.19 0.02 4 210 . 33 GLN HB3 H 2.23 0.02 4 211 . 33 GLN HG2 H 2.43 0.02 4 212 . 33 GLN HG3 H 2.43 0.02 4 213 . 33 GLN HE21 H 6.91 0.02 4 214 . 33 GLN HE22 H 7.82 0.02 4 215 . 34 SER H H 8.01 0.02 4 216 . 34 SER HA H 4.28 0.02 4 217 . 34 SER HB2 H 4.00 0.02 4 218 . 34 SER HB3 H 4.13 0.02 4 219 . 35 LEU H H 8.17 0.02 4 220 . 35 LEU HA H 3.78 0.02 4 221 . 35 LEU HB2 H 1.68 0.02 4 222 . 35 LEU HB3 H 1.87 0.02 4 223 . 35 LEU HG H 1.68 0.02 4 224 . 35 LEU HD1 H 0.73 0.02 4 225 . 35 LEU HD2 H 0.79 0.02 4 226 . 36 LYS H H 7.99 0.02 4 227 . 36 LYS HA H 4.01 0.02 4 228 . 36 LYS HB2 H 2.00 0.02 4 229 . 36 LYS HB3 H 2.00 0.02 4 230 . 36 LYS HG2 H 1.45 0.02 4 231 . 36 LYS HG3 H 1.45 0.02 4 232 . 36 LYS HD2 H 1.68 0.02 4 233 . 36 LYS HD3 H 1.68 0.02 4 234 . 36 LYS HE2 H 2.89 0.02 4 235 . 36 LYS HE3 H 2.89 0.02 4 236 . 37 ASP H H 8.09 0.02 4 237 . 37 ASP HA H 4.46 0.02 4 238 . 37 ASP HB2 H 2.74 0.02 4 239 . 37 ASP HB3 H 2.79 0.02 4 240 . 38 ASP H H 7.66 0.02 4 241 . 38 ASP HA H 4.96 0.02 4 242 . 38 ASP HB2 H 2.60 0.02 4 243 . 38 ASP HB3 H 3.01 0.02 4 244 . 39 PRO HA H 4.51 0.02 4 245 . 39 PRO HB2 H 1.98 0.02 4 246 . 39 PRO HB3 H 1.98 0.02 4 247 . 39 PRO HG2 H 2.12 0.02 4 248 . 39 PRO HG3 H 2.26 0.02 4 249 . 39 PRO HD2 H 3.69 0.02 4 250 . 39 PRO HD3 H 3.88 0.02 4 251 . 40 SER H H 8.08 0.02 4 252 . 40 SER HA H 4.31 0.02 4 253 . 40 SER HB2 H 3.98 0.02 4 254 . 40 SER HB3 H 4.04 0.02 4 255 . 41 GLN H H 7.87 0.02 4 256 . 41 GLN HA H 4.61 0.02 4 257 . 41 GLN HB2 H 2.00 0.02 4 258 . 41 GLN HB3 H 2.65 0.02 4 259 . 41 GLN HG2 H 2.33 0.02 4 260 . 41 GLN HG3 H 2.48 0.02 4 261 . 41 GLN HE21 H 6.86 0.02 4 262 . 41 GLN HE22 H 7.58 0.02 4 263 . 42 SER H H 7.77 0.02 4 264 . 42 SER HA H 3.73 0.02 4 265 . 42 SER HB2 H 3.96 0.02 4 266 . 42 SER HB3 H 3.96 0.02 4 267 . 43 ALA H H 8.48 0.02 4 268 . 43 ALA HA H 4.13 0.02 4 269 . 43 ALA HB H 1.43 0.02 4 270 . 44 ASN H H 7.91 0.02 4 271 . 44 ASN HA H 4.53 0.02 4 272 . 44 ASN HB2 H 2.89 0.02 4 273 . 44 ASN HB3 H 2.89 0.02 4 274 . 44 ASN HD21 H 6.98 0.02 4 275 . 44 ASN HD22 H 7.76 0.02 4 276 . 45 LEU H H 8.58 0.02 4 277 . 45 LEU HA H 4.16 0.02 4 278 . 45 LEU HB2 H 1.27 0.02 4 279 . 45 LEU HB3 H 1.80 0.02 4 280 . 45 LEU HG H 1.87 0.02 4 281 . 45 LEU HD1 H 0.80 0.02 4 282 . 45 LEU HD2 H 1.13 0.02 4 283 . 46 LEU H H 8.41 0.02 4 284 . 46 LEU HA H 3.81 0.02 4 285 . 46 LEU HB2 H 1.46 0.02 4 286 . 46 LEU HB3 H 1.88 0.02 4 287 . 46 LEU HG H 1.54 0.02 4 288 . 46 LEU HD1 H 0.89 0.02 4 289 . 46 LEU HD2 H 0.89 0.02 4 290 . 47 ALA H H 7.61 0.02 4 291 . 47 ALA HA H 4.03 0.02 4 292 . 47 ALA HB H 1.54 0.02 4 293 . 48 GLU H H 8.07 0.02 4 294 . 48 GLU HA H 4.02 0.02 4 295 . 48 GLU HB2 H 2.24 0.02 4 296 . 48 GLU HB3 H 2.29 0.02 4 297 . 48 GLU HG2 H 2.51 0.02 4 298 . 48 GLU HG3 H 2.58 0.02 4 299 . 49 ALA H H 8.41 0.02 4 300 . 49 ALA HA H 3.48 0.02 4 301 . 49 ALA HB H 0.49 0.02 4 302 . 50 LYS H H 8.49 0.02 4 303 . 50 LYS HA H 3.76 0.02 4 304 . 50 LYS HB2 H 1.78 0.02 4 305 . 50 LYS HB3 H 1.94 0.02 4 306 . 50 LYS HG2 H 1.29 0.02 4 307 . 50 LYS HG3 H 1.29 0.02 4 308 . 50 LYS HD2 H 1.59 0.02 4 309 . 50 LYS HD3 H 1.59 0.02 4 310 . 50 LYS HE2 H 2.82 0.02 4 311 . 50 LYS HE3 H 2.93 0.02 4 312 . 51 LYS H H 7.71 0.02 4 313 . 51 LYS HA H 4.11 0.02 4 314 . 51 LYS HB2 H 1.96 0.02 4 315 . 51 LYS HB3 H 1.96 0.02 4 316 . 51 LYS HG2 H 1.42 0.02 4 317 . 51 LYS HG3 H 1.42 0.02 4 318 . 51 LYS HD2 H 1.62 0.02 4 319 . 51 LYS HD3 H 1.72 0.02 4 320 . 51 LYS HE2 H 2.94 0.02 4 321 . 51 LYS HE3 H 2.94 0.02 4 322 . 52 LEU H H 7.94 0.02 4 323 . 52 LEU HA H 4.18 0.02 4 324 . 52 LEU HB2 H 1.72 0.02 4 325 . 52 LEU HB3 H 1.72 0.02 4 326 . 52 LEU HG H 1.58 0.02 4 327 . 52 LEU HD1 H 1.00 0.02 4 328 . 52 LEU HD2 H 1.02 0.02 4 329 . 53 ASN H H 8.57 0.02 4 330 . 53 ASN HA H 3.96 0.02 4 331 . 53 ASN HB2 H 2.41 0.02 4 332 . 53 ASN HB3 H 3.12 0.02 4 333 . 53 ASN HD21 H 6.86 0.02 4 334 . 53 ASN HD22 H 7.94 0.02 4 335 . 54 ASP H H 8.27 0.02 4 336 . 54 ASP HA H 4.47 0.02 4 337 . 54 ASP HB2 H 2.73 0.02 4 338 . 54 ASP HB3 H 2.79 0.02 4 339 . 55 ALA H H 8.03 0.02 4 340 . 55 ALA HA H 4.26 0.02 4 341 . 55 ALA HB H 1.60 0.02 4 342 . 56 GLN H H 7.54 0.02 4 343 . 56 GLN HA H 4.38 0.02 4 344 . 56 GLN HB2 H 1.83 0.02 4 345 . 56 GLN HB3 H 2.30 0.02 4 346 . 56 GLN HG2 H 2.48 0.02 4 347 . 56 GLN HG3 H 2.65 0.02 4 348 . 56 GLN HE21 H 7.27 0.02 4 349 . 56 GLN HE22 H 8.69 0.02 4 350 . 57 ALA H H 7.15 0.02 4 351 . 57 ALA HA H 4.37 0.02 4 352 . 57 ALA HB H 1.46 0.02 4 353 . 58 PRO HA H 4.44 0.02 1 354 . 58 PRO HB2 H 1.90 0.02 2 355 . 58 PRO HB3 H 2.27 0.02 2 356 . 58 PRO HG2 H 2.08 0.02 4 357 . 58 PRO HG3 H 2.08 0.02 4 358 . 58 PRO HD2 H 3.63 0.02 4 359 . 58 PRO HD3 H 3.79 0.02 4 360 . 59 LYS H H 8.42 0.02 1 361 . 59 LYS HA H 4.38 0.02 1 362 . 59 LYS HB2 H 1.74 0.02 2 363 . 59 LYS HB3 H 1.82 0.02 2 364 . 59 LYS HG2 H 1.49 0.02 4 365 . 59 LYS HG3 H 1.49 0.02 4 366 . 59 LYS HD2 H 1.71 0.02 1 367 . 59 LYS HD3 H 1.71 0.02 1 368 . 59 LYS HE2 H 3.04 0.02 4 369 . 59 LYS HE3 H 3.04 0.02 4 370 . 60 ALA H H 8.29 0.02 1 371 . 60 ALA HA H 4.03 0.02 1 372 . 60 ALA HB H 1.28 0.02 1 373 . 61 ASP H H 7.90 0.02 1 374 . 61 ASP HA H 4.43 0.02 1 375 . 61 ASP HB2 H 2.41 0.02 1 376 . 61 ASP HB3 H 2.41 0.02 1 377 . 62 ASN H H 8.26 0.02 1 378 . 62 ASN HA H 4.54 0.02 1 379 . 62 ASN HB2 H 2.66 0.02 1 380 . 62 ASN HB3 H 2.66 0.02 1 381 . 63 LYS H H 8.30 0.02 1 382 . 63 LYS HA H 4.19 0.02 1 383 . 63 LYS HB2 H 1.69 0.02 1 384 . 63 LYS HB3 H 1.69 0.02 1 385 . 63 LYS HD2 H 1.61 0.02 1 386 . 63 LYS HD3 H 1.61 0.02 1 387 . 63 LYS HE2 H 2.93 0.02 1 388 . 63 LYS HE3 H 2.93 0.02 1 389 . 64 PHE H H 7.94 0.02 1 390 . 64 PHE HA H 5.02 0.02 1 391 . 64 PHE HB2 H 3.10 0.02 1 392 . 64 PHE HB3 H 3.37 0.02 1 393 . 64 PHE HD1 H 7.12 0.02 1 394 . 64 PHE HD2 H 7.12 0.02 1 395 . 64 PHE HE1 H 7.02 0.02 1 396 . 64 PHE HE2 H 7.02 0.02 1 397 . 65 ASN H H 8.45 0.02 4 398 . 65 ASN HA H 4.72 0.02 4 399 . 65 ASN HB2 H 2.96 0.02 2 400 . 65 ASN HB3 H 3.32 0.02 2 401 . 65 ASN HD21 H 6.92 0.02 4 402 . 65 ASN HD22 H 7.50 0.02 4 403 . 66 LYS H H 8.36 0.02 4 404 . 66 LYS HA H 3.99 0.02 4 405 . 66 LYS HB2 H 1.83 0.02 4 406 . 66 LYS HB3 H 1.88 0.02 4 407 . 66 LYS HG2 H 1.46 0.02 4 408 . 66 LYS HG3 H 1.53 0.02 4 409 . 66 LYS HD2 H 1.72 0.02 4 410 . 66 LYS HD3 H 1.72 0.02 4 411 . 67 GLU H H 8.26 0.02 4 412 . 67 GLU HA H 4.12 0.02 4 413 . 67 GLU HB2 H 2.07 0.02 4 414 . 67 GLU HB3 H 2.13 0.02 4 415 . 67 GLU HG2 H 2.34 0.02 4 416 . 67 GLU HG3 H 2.34 0.02 4 417 . 68 GLN H H 8.51 0.02 4 418 . 68 GLN HA H 3.89 0.02 4 419 . 68 GLN HB2 H 2.21 0.02 4 420 . 68 GLN HB3 H 2.21 0.02 4 421 . 68 GLN HG2 H 2.47 0.02 4 422 . 68 GLN HG3 H 2.47 0.02 4 423 . 68 GLN HE21 H 6.99 0.02 4 424 . 68 GLN HE22 H 7.29 0.02 4 425 . 69 GLN H H 8.68 0.02 1 426 . 69 GLN HA H 3.97 0.02 1 427 . 69 GLN HB2 H 2.23 0.02 1 428 . 69 GLN HB3 H 2.23 0.02 1 429 . 69 GLN HG2 H 2.43 0.02 2 430 . 69 GLN HG3 H 2.51 0.02 2 431 . 69 GLN HE21 H 6.85 0.02 2 432 . 69 GLN HE22 H 7.21 0.02 4 433 . 70 ASN H H 8.31 0.02 1 434 . 70 ASN HA H 4.62 0.02 4 435 . 70 ASN HB2 H 2.93 0.02 4 436 . 70 ASN HB3 H 2.93 0.02 4 437 . 70 ASN HD21 H 7.01 0.02 4 438 . 70 ASN HD22 H 7.73 0.02 4 439 . 71 ALA H H 7.95 0.02 4 440 . 71 ALA HA H 4.09 0.02 4 441 . 71 ALA HB H 1.48 0.02 4 442 . 72 PHE H H 8.17 0.02 4 443 . 72 PHE HA H 3.82 0.02 1 444 . 72 PHE HB2 H 2.98 0.02 2 445 . 72 PHE HB3 H 3.32 0.02 4 446 . 72 PHE HD1 H 6.97 0.02 1 447 . 72 PHE HD2 H 6.97 0.02 1 448 . 72 PHE HE1 H 7.23 0.02 1 449 . 72 PHE HE2 H 7.23 0.02 1 450 . 72 PHE HZ H 7.15 0.02 1 451 . 73 TYR H H 8.13 0.02 4 452 . 73 TYR HA H 3.95 0.02 4 453 . 73 TYR HB2 H 3.18 0.02 4 454 . 73 TYR HB3 H 3.18 0.02 4 455 . 73 TYR HD1 H 6.76 0.02 1 456 . 73 TYR HD2 H 6.76 0.02 1 457 . 73 TYR HE1 H 7.18 0.02 1 458 . 73 TYR HE2 H 7.18 0.02 1 459 . 74 GLU H H 8.57 0.02 4 460 . 74 GLU HA H 4.01 0.02 4 461 . 74 GLU HB2 H 2.01 0.02 4 462 . 74 GLU HB3 H 2.16 0.02 4 463 . 74 GLU HG2 H 2.26 0.02 4 464 . 74 GLU HG3 H 2.48 0.02 4 465 . 75 ILE H H 8.45 0.02 4 466 . 75 ILE HA H 3.41 0.02 4 467 . 75 ILE HB H 1.80 0.02 4 468 . 75 ILE HG12 H 1.87 0.02 4 469 . 75 ILE HG13 H 1.87 0.02 4 470 . 75 ILE HG2 H 0.78 0.02 4 471 . 75 ILE HD1 H 0.51 0.02 4 472 . 76 LEU H H 7.91 0.02 1 473 . 76 LEU HA H 3.71 0.02 4 474 . 76 LEU HB2 H 1.18 0.02 2 475 . 76 LEU HB3 H 1.49 0.02 4 476 . 76 LEU HG H 1.39 0.02 1 477 . 76 LEU HD1 H 0.58 0.02 4 478 . 76 LEU HD2 H 0.67 0.02 4 479 . 77 HIS H H 7.28 0.02 1 480 . 77 HIS HA H 4.52 0.02 1 481 . 77 HIS HB2 H 2.84 0.02 2 482 . 77 HIS HB3 H 3.46 0.02 4 483 . 77 HIS HD2 H 7.13 0.02 1 484 . 77 HIS HE1 H 8.29 0.02 1 485 . 78 LEU H H 7.23 0.02 4 486 . 78 LEU HA H 4.50 0.02 4 487 . 78 LEU HB2 H 1.37 0.02 4 488 . 78 LEU HB3 H 1.73 0.02 4 489 . 78 LEU HG H 2.21 0.02 4 490 . 78 LEU HD1 H 0.68 0.02 4 491 . 78 LEU HD2 H 0.87 0.02 4 492 . 79 PRO HA H 4.42 0.02 4 493 . 79 PRO HB2 H 2.04 0.02 4 494 . 79 PRO HB3 H 2.17 0.02 4 495 . 79 PRO HG2 H 1.98 0.02 4 496 . 79 PRO HG3 H 1.98 0.02 4 497 . 79 PRO HD2 H 3.82 0.02 4 498 . 79 PRO HD3 H 4.07 0.02 4 499 . 80 ASN H H 8.87 0.02 4 500 . 80 ASN HA H 5.01 0.02 4 501 . 80 ASN HB2 H 2.89 0.02 4 502 . 80 ASN HB3 H 2.89 0.02 4 503 . 80 ASN HD21 H 7.00 0.02 2 504 . 80 ASN HD22 H 7.40 0.02 2 505 . 81 LEU H H 6.53 0.02 4 506 . 81 LEU HA H 4.45 0.02 4 507 . 81 LEU HB2 H 1.63 0.02 4 508 . 81 LEU HB3 H 1.71 0.02 4 509 . 81 LEU HG H 1.71 0.02 4 510 . 81 LEU HD1 H 0.90 0.02 4 511 . 81 LEU HD2 H 0.97 0.02 4 512 . 82 ASN H H 8.55 0.02 4 513 . 82 ASN HA H 4.92 0.02 4 514 . 82 ASN HB2 H 2.82 0.02 4 515 . 82 ASN HB3 H 3.29 0.02 4 516 . 82 ASN HD21 H 7.03 0.02 4 517 . 82 ASN HD22 H 7.50 0.02 4 518 . 83 GLU H H 8.62 0.02 4 519 . 83 GLU HA H 3.95 0.02 4 520 . 83 GLU HB2 H 2.04 0.02 4 521 . 83 GLU HB3 H 2.04 0.02 4 522 . 83 GLU HG2 H 2.37 0.02 4 523 . 83 GLU HG3 H 2.37 0.02 4 524 . 84 GLU H H 8.26 0.02 4 525 . 84 GLU HA H 4.07 0.02 4 526 . 84 GLU HB2 H 2.04 0.02 4 527 . 84 GLU HB3 H 2.04 0.02 4 528 . 84 GLU HG2 H 2.30 0.02 4 529 . 84 GLU HG3 H 2.30 0.02 4 530 . 85 GLN H H 8.60 0.02 4 531 . 85 GLN HA H 3.89 0.02 4 532 . 85 GLN HB2 H 2.48 0.02 4 533 . 85 GLN HB3 H 2.48 0.02 4 534 . 85 GLN HG2 H 2.33 0.02 4 535 . 85 GLN HG3 H 2.79 0.02 4 536 . 85 GLN HE21 H 7.65 0.02 4 537 . 85 GLN HE22 H 8.25 0.02 4 538 . 86 ARG H H 8.63 0.02 4 539 . 86 ARG HA H 3.78 0.02 4 540 . 86 ARG HB2 H 1.76 0.02 4 541 . 86 ARG HB3 H 1.88 0.02 4 542 . 86 ARG HG2 H 1.48 0.02 4 543 . 86 ARG HG3 H 1.48 0.02 4 544 . 86 ARG HD2 H 3.25 0.02 4 545 . 86 ARG HD3 H 3.40 0.02 4 546 . 86 ARG HE H 7.58 0.02 4 547 . 87 ASN H H 8.63 0.02 4 548 . 87 ASN HA H 4.42 0.02 4 549 . 87 ASN HB2 H 2.80 0.02 4 550 . 87 ASN HB3 H 2.90 0.02 4 551 . 87 ASN HD21 H 7.01 0.02 4 552 . 87 ASN HD22 H 7.63 0.02 4 553 . 88 GLY H H 8.05 0.02 4 554 . 88 GLY HA2 H 3.89 0.02 4 555 . 88 GLY HA3 H 3.89 0.02 4 556 . 89 PHE H H 7.84 0.02 4 557 . 89 PHE HA H 4.48 0.02 4 558 . 89 PHE HB2 H 3.04 0.02 4 559 . 89 PHE HB3 H 3.04 0.02 4 560 . 89 PHE HD1 H 7.26 0.02 4 561 . 89 PHE HD2 H 7.26 0.02 4 562 . 89 PHE HE1 H 7.28 0.02 4 563 . 89 PHE HE2 H 7.28 0.02 4 564 . 89 PHE HZ H 7.15 0.02 4 565 . 90 ILE H H 8.27 0.02 4 566 . 90 ILE HA H 3.75 0.02 4 567 . 90 ILE HB H 2.13 0.02 4 568 . 90 ILE HG12 H 1.37 0.02 4 569 . 90 ILE HG13 H 1.61 0.02 4 570 . 90 ILE HG2 H 0.99 0.02 4 571 . 90 ILE HD1 H 0.66 0.02 4 572 . 91 GLN H H 8.43 0.02 4 573 . 91 GLN HA H 3.95 0.02 4 574 . 91 GLN HB2 H 2.19 0.02 4 575 . 91 GLN HB3 H 2.23 0.02 4 576 . 91 GLN HG2 H 2.43 0.02 4 577 . 91 GLN HG3 H 2.43 0.02 4 578 . 91 GLN HE21 H 6.91 0.02 4 579 . 91 GLN HE22 H 7.82 0.02 4 580 . 92 SER H H 8.03 0.02 4 581 . 92 SER HA H 4.28 0.02 4 582 . 92 SER HB2 H 4.00 0.02 4 583 . 92 SER HB3 H 4.13 0.02 4 584 . 93 LEU H H 8.17 0.02 4 585 . 93 LEU HA H 3.78 0.02 4 586 . 93 LEU HB2 H 1.68 0.02 4 587 . 93 LEU HB3 H 1.87 0.02 4 588 . 93 LEU HG H 1.68 0.02 4 589 . 93 LEU HD1 H 0.73 0.02 4 590 . 93 LEU HD2 H 0.79 0.02 4 591 . 94 LYS H H 8.01 0.02 4 592 . 94 LYS HA H 4.02 0.02 4 593 . 94 LYS HB2 H 2.00 0.02 4 594 . 94 LYS HB3 H 2.00 0.02 4 595 . 94 LYS HG2 H 1.45 0.02 4 596 . 94 LYS HG3 H 1.45 0.02 4 597 . 94 LYS HD2 H 1.68 0.02 4 598 . 94 LYS HD3 H 1.68 0.02 4 599 . 94 LYS HE2 H 2.89 0.02 4 600 . 94 LYS HE3 H 2.89 0.02 4 601 . 95 ASP H H 8.09 0.02 4 602 . 95 ASP HA H 4.46 0.02 4 603 . 95 ASP HB2 H 2.74 0.02 4 604 . 95 ASP HB3 H 2.79 0.02 4 605 . 96 ASP H H 7.66 0.02 4 606 . 96 ASP HA H 4.96 0.02 4 607 . 96 ASP HB2 H 2.60 0.02 4 608 . 96 ASP HB3 H 3.01 0.02 4 609 . 97 PRO HA H 4.51 0.02 4 610 . 97 PRO HB2 H 1.98 0.02 4 611 . 97 PRO HB3 H 1.98 0.02 4 612 . 97 PRO HG2 H 2.12 0.02 4 613 . 97 PRO HG3 H 2.26 0.02 4 614 . 97 PRO HD2 H 3.69 0.02 4 615 . 97 PRO HD3 H 3.88 0.02 4 616 . 98 SER H H 8.08 0.02 4 617 . 98 SER HA H 4.31 0.02 4 618 . 98 SER HB2 H 3.98 0.02 4 619 . 98 SER HB3 H 4.04 0.02 4 620 . 99 GLN H H 7.87 0.02 4 621 . 99 GLN HA H 4.61 0.02 4 622 . 99 GLN HB2 H 2.00 0.02 4 623 . 99 GLN HB3 H 2.65 0.02 4 624 . 99 GLN HG2 H 2.33 0.02 4 625 . 99 GLN HG3 H 2.48 0.02 4 626 . 99 GLN HE21 H 6.86 0.02 4 627 . 99 GLN HE22 H 7.58 0.02 4 628 . 100 SER H H 7.77 0.02 4 629 . 100 SER HA H 3.73 0.02 4 630 . 100 SER HB2 H 3.96 0.02 4 631 . 100 SER HB3 H 3.96 0.02 4 632 . 101 ALA H H 8.48 0.02 4 633 . 101 ALA HA H 4.13 0.02 4 634 . 101 ALA HB H 1.43 0.02 4 635 . 102 ASN H H 7.91 0.02 4 636 . 102 ASN HA H 4.53 0.02 4 637 . 102 ASN HB2 H 2.89 0.02 4 638 . 102 ASN HB3 H 2.89 0.02 4 639 . 102 ASN HD21 H 6.98 0.02 4 640 . 102 ASN HD22 H 7.76 0.02 4 641 . 103 LEU H H 8.58 0.02 4 642 . 103 LEU HA H 4.16 0.02 4 643 . 103 LEU HB2 H 1.27 0.02 4 644 . 103 LEU HB3 H 1.80 0.02 4 645 . 103 LEU HG H 1.87 0.02 4 646 . 103 LEU HD1 H 0.80 0.02 4 647 . 103 LEU HD2 H 1.13 0.02 4 648 . 104 LEU H H 8.41 0.02 4 649 . 104 LEU HA H 3.81 0.02 4 650 . 104 LEU HB2 H 1.46 0.02 4 651 . 104 LEU HB3 H 1.88 0.02 4 652 . 104 LEU HG H 1.54 0.02 4 653 . 104 LEU HD1 H 0.89 0.02 4 654 . 104 LEU HD2 H 0.89 0.02 4 655 . 105 ALA H H 7.61 0.02 4 656 . 105 ALA HA H 4.03 0.02 4 657 . 105 ALA HB H 1.54 0.02 4 658 . 106 GLU H H 8.07 0.02 4 659 . 106 GLU HA H 4.02 0.02 4 660 . 106 GLU HB2 H 2.24 0.02 4 661 . 106 GLU HB3 H 2.29 0.02 4 662 . 106 GLU HG2 H 2.51 0.02 4 663 . 106 GLU HG3 H 2.58 0.02 4 664 . 107 ALA H H 8.41 0.02 4 665 . 107 ALA HA H 3.48 0.02 4 666 . 107 ALA HB H 0.49 0.02 4 667 . 108 LYS H H 8.49 0.02 4 668 . 108 LYS HA H 3.76 0.02 4 669 . 108 LYS HB2 H 1.78 0.02 4 670 . 108 LYS HB3 H 1.94 0.02 4 671 . 108 LYS HG2 H 1.29 0.02 4 672 . 108 LYS HG3 H 1.29 0.02 4 673 . 108 LYS HD2 H 1.59 0.02 4 674 . 108 LYS HD3 H 1.59 0.02 4 675 . 108 LYS HE2 H 2.82 0.02 4 676 . 108 LYS HE3 H 2.93 0.02 4 677 . 109 LYS H H 7.71 0.02 4 678 . 109 LYS HA H 4.11 0.02 4 679 . 109 LYS HB2 H 1.96 0.02 4 680 . 109 LYS HB3 H 1.96 0.02 4 681 . 109 LYS HG2 H 1.42 0.02 4 682 . 109 LYS HG3 H 1.42 0.02 4 683 . 109 LYS HD2 H 1.62 0.02 4 684 . 109 LYS HD3 H 1.72 0.02 4 685 . 109 LYS HE2 H 2.94 0.02 4 686 . 109 LYS HE3 H 2.94 0.02 4 687 . 110 LEU H H 7.94 0.02 4 688 . 110 LEU HA H 4.18 0.02 4 689 . 110 LEU HB2 H 1.72 0.02 4 690 . 110 LEU HB3 H 1.72 0.02 4 691 . 110 LEU HG H 1.58 0.02 4 692 . 110 LEU HD1 H 1.00 0.02 4 693 . 110 LEU HD2 H 1.02 0.02 4 694 . 111 ASN H H 8.57 0.02 4 695 . 111 ASN HA H 3.96 0.02 4 696 . 111 ASN HB2 H 2.41 0.02 4 697 . 111 ASN HB3 H 3.12 0.02 4 698 . 111 ASN HD21 H 6.86 0.02 4 699 . 111 ASN HD22 H 7.94 0.02 4 700 . 112 ASP H H 8.27 0.02 4 701 . 112 ASP HA H 4.47 0.02 4 702 . 112 ASP HB2 H 2.73 0.02 4 703 . 112 ASP HB3 H 2.79 0.02 4 704 . 113 ALA H H 8.03 0.02 4 705 . 113 ALA HA H 4.25 0.02 4 706 . 113 ALA HB H 1.58 0.02 4 707 . 114 GLN H H 7.54 0.02 4 708 . 114 GLN HA H 4.38 0.02 4 709 . 114 GLN HB2 H 1.83 0.02 4 710 . 114 GLN HB3 H 2.30 0.02 4 711 . 114 GLN HG2 H 2.48 0.02 4 712 . 114 GLN HG3 H 2.65 0.02 4 713 . 114 GLN HE21 H 7.27 0.02 4 714 . 114 GLN HE22 H 8.69 0.02 4 715 . 115 ALA H H 7.13 0.02 4 716 . 115 ALA HA H 4.36 0.02 4 717 . 115 ALA HB H 1.45 0.02 4 718 . 116 PRO HA H 4.43 0.02 1 719 . 116 PRO HB2 H 1.91 0.02 2 720 . 116 PRO HB3 H 2.24 0.02 2 721 . 116 PRO HG2 H 2.08 0.02 4 722 . 116 PRO HG3 H 2.08 0.02 4 723 . 116 PRO HD2 H 3.63 0.02 4 724 . 116 PRO HD3 H 3.79 0.02 4 725 . 117 LYS H H 8.44 0.02 1 726 . 117 LYS HA H 4.33 0.02 1 727 . 117 LYS HB2 H 1.75 0.02 2 728 . 117 LYS HB3 H 1.85 0.02 2 729 . 117 LYS HG2 H 1.49 0.02 4 730 . 117 LYS HG3 H 1.49 0.02 4 731 . 117 LYS HD2 H 1.69 0.02 1 732 . 117 LYS HD3 H 1.69 0.02 1 733 . 117 LYS HE2 H 3.04 0.02 4 734 . 117 LYS HE3 H 3.04 0.02 4 735 . 118 ALA HA H 4.09 0.02 1 736 . 118 ALA HB H 1.52 0.02 1 737 . 122 GLY H H 8.43 0.02 1 738 . 122 GLY HA2 H 4.01 0.02 1 739 . 122 GLY HA3 H 4.01 0.02 1 740 . 123 SER H H 7.87 0.02 1 741 . 123 SER HA H 4.32 0.02 1 742 . 123 SER HB2 H 3.88 0.02 1 743 . 123 SER HB3 H 3.88 0.02 1 stop_ save_