data_6379 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone HN, N, C', CA, CB assignments of Escherichia coli SdiA1-171 ; _BMRB_accession_number 6379 _BMRB_flat_file_name bmr6379.str _Entry_type original _Submission_date 2004-11-08 _Accession_date 2004-11-08 _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 Yao Yong . . 2 Martinez-Yamout Maria A. . 3 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" 155 "13C chemical shifts" 468 "15N chemical shifts" 155 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-26 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6454 'assignment of the free form' stop_ _Original_release_date 2005-07-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone and side chain 1H, 13C and 15N assignments for Escherichia coli SdiA1-171, the autoinducer-binding domain of a quorum sensing protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15929010 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yao Yong . . 2 Martinez-Yamout Maria A. . 3 Dyson H. Jane . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 373 _Page_last 374 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_SdiA _Saveframe_category molecular_system _Mol_system_name SdiA _Abbreviation_common SdiA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'quorum sensing protein' $quorum_sensing_protein HSL_2 $HTF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_quorum_sensing_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common sdia _Abbreviation_common SdiA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 171 _Mol_residue_sequence ; MSDKDFFSWRRTMLLRFQRM ETAEEVYHEIELQAQQLEYD YYSLCVRHPVPFTRPKVAFY TNYPEAWVSYYQAKNFLAID PVLNPENFSQGHLMWNDDLF SEAQPLWEAARAHGLRRGVT QYLMLPERALGFLSFSRCSA REIPILSDELQLKMQLLVRE SLMALMRLNDE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ASP 4 LYS 5 ASP 6 PHE 7 PHE 8 SER 9 TRP 10 ARG 11 ARG 12 THR 13 MET 14 LEU 15 LEU 16 ARG 17 PHE 18 GLN 19 ARG 20 MET 21 GLU 22 THR 23 ALA 24 GLU 25 GLU 26 VAL 27 TYR 28 HIS 29 GLU 30 ILE 31 GLU 32 LEU 33 GLN 34 ALA 35 GLN 36 GLN 37 LEU 38 GLU 39 TYR 40 ASP 41 TYR 42 TYR 43 SER 44 LEU 45 CYS 46 VAL 47 ARG 48 HIS 49 PRO 50 VAL 51 PRO 52 PHE 53 THR 54 ARG 55 PRO 56 LYS 57 VAL 58 ALA 59 PHE 60 TYR 61 THR 62 ASN 63 TYR 64 PRO 65 GLU 66 ALA 67 TRP 68 VAL 69 SER 70 TYR 71 TYR 72 GLN 73 ALA 74 LYS 75 ASN 76 PHE 77 LEU 78 ALA 79 ILE 80 ASP 81 PRO 82 VAL 83 LEU 84 ASN 85 PRO 86 GLU 87 ASN 88 PHE 89 SER 90 GLN 91 GLY 92 HIS 93 LEU 94 MET 95 TRP 96 ASN 97 ASP 98 ASP 99 LEU 100 PHE 101 SER 102 GLU 103 ALA 104 GLN 105 PRO 106 LEU 107 TRP 108 GLU 109 ALA 110 ALA 111 ARG 112 ALA 113 HIS 114 GLY 115 LEU 116 ARG 117 ARG 118 GLY 119 VAL 120 THR 121 GLN 122 TYR 123 LEU 124 MET 125 LEU 126 PRO 127 GLU 128 ARG 129 ALA 130 LEU 131 GLY 132 PHE 133 LEU 134 SER 135 PHE 136 SER 137 ARG 138 CYS 139 SER 140 ALA 141 ARG 142 GLU 143 ILE 144 PRO 145 ILE 146 LEU 147 SER 148 ASP 149 GLU 150 LEU 151 GLN 152 LEU 153 LYS 154 MET 155 GLN 156 LEU 157 LEU 158 VAL 159 ARG 160 GLU 161 SER 162 LEU 163 MET 164 ALA 165 LEU 166 MET 167 ARG 168 LEU 169 ASN 170 ASP 171 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 6454 sdia 100.00 171 100.00 100.00 1.33e-122 PDB 2AVX "Solution Structure Of E Coli Sdia1-171" 100.00 171 100.00 100.00 1.33e-122 PDB 4LFU "Crystal Structure Of Escherichia Coli Sdia In The Space Group C2" 100.00 248 98.83 98.83 9.48e-122 PDB 4LGW "Crystal Structure Of Escherichia Coli Sdia In The Space Group P6522" 100.00 248 98.83 98.83 9.48e-122 DBJ BAA15736 "DNA-binding transcriptional activator [Escherichia coli str. K-12 substr. W3110]" 100.00 240 98.83 98.83 5.48e-122 DBJ BAB36077 "transcriptional regulator of ftsQAZ gene cluster [Escherichia coli O157:H7 str. Sakai]" 100.00 240 97.66 98.25 1.30e-120 DBJ BAG77671 "transcriptional regulator of ftsQAZ gene cluster [Escherichia coli SE11]" 100.00 244 97.66 97.66 1.96e-120 DBJ BAI26047 "DNA-binding transcriptional activator SdiA [Escherichia coli O26:H11 str. 11368]" 100.00 240 97.08 97.66 7.07e-120 DBJ BAI30964 "DNA-binding transcriptional activator SdiA [Escherichia coli O103:H2 str. 12009]" 100.00 240 97.08 97.08 6.34e-120 EMBL CAQ98852 "DNA-binding transcriptional activator [Escherichia coli IAI1]" 100.00 240 97.08 97.08 6.34e-120 EMBL CAR08247 "DNA-binding transcriptional activator [Escherichia coli ED1a]" 100.00 240 97.08 97.08 3.33e-119 EMBL CAR13401 "DNA-binding transcriptional activator [Escherichia coli UMN026]" 100.00 240 97.08 97.08 3.33e-119 EMBL CAU98011 "DNA-binding transcriptional activator [Escherichia coli 55989]" 100.00 240 97.08 97.08 2.68e-119 EMBL CBG34902 "regulatory protein [Escherichia coli 042]" 100.00 240 97.08 97.08 6.34e-120 GB AAC74983 "quorum-sensing transcriptional activator [Escherichia coli str. K-12 substr. MG1655]" 100.00 240 98.83 98.83 5.48e-122 GB AAG56931 "transcriptional regulator of ftsQAZ gene cluster [Escherichia coli O157:H7 str. EDL933]" 100.00 240 97.66 98.25 1.30e-120 GB ABV06323 "regulatory protein SdiA [Escherichia coli HS]" 100.00 240 97.08 97.08 3.33e-119 GB ACA77373 "transcriptional regulator, LuxR family [Escherichia coli ATCC 8739]" 100.00 240 97.08 97.08 3.33e-119 GB ACB03106 "DNA-binding transcriptional activator [Escherichia coli str. K-12 substr. DH10B]" 100.00 240 98.83 98.83 5.48e-122 REF NP_288377 "DNA-binding transcriptional activator SdiA [Escherichia coli O157:H7 str. EDL933]" 100.00 240 97.66 98.25 1.30e-120 REF NP_310681 "SdiA family transcriptional regulator [Escherichia coli O157:H7 str. Sakai]" 100.00 240 97.66 98.25 1.30e-120 REF NP_416426 "quorum-sensing transcriptional activator [Escherichia coli str. K-12 substr. MG1655]" 100.00 240 98.83 98.83 5.48e-122 REF WP_001152713 "transcriptional regulator [Escherichia coli]" 100.00 240 97.08 97.08 2.68e-119 REF WP_001152714 "DNA-binding transcriptional activator SdiA [Escherichia coli]" 100.00 240 97.66 97.66 5.81e-120 SP P07026 "RecName: Full=Regulatory protein SdiA [Escherichia coli K-12]" 100.00 240 98.83 98.83 5.48e-122 stop_ save_ ############# # Ligands # ############# save_HTF _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common N-(2-OXOTETRAHYDROFURAN-3-YL)OCTANAMIDE _BMRB_code HTF _PDB_code HTF _Molecular_mass 227.300 _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 C C C . 0 . ? C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? H22 H22 H . 0 . ? H23 H23 H . 0 . ? H32 H32 H . 0 . ? H33 H33 H . 0 . ? H42 H42 H . 0 . ? H43 H43 H . 0 . ? H52 H52 H . 0 . ? H53 H53 H . 0 . ? H62 H62 H . 0 . ? H63 H63 H . 0 . ? H72 H72 H . 0 . ? H73 H73 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H83 H83 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HN HN H . 0 . ? N N N . 0 . ? O O O . 0 . ? O1 O1 O . 0 . ? OD OD O . 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 C8 C7 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C8 H83 ? ? SING C7 C6 ? ? SING C7 H72 ? ? SING C7 H73 ? ? SING C6 C5 ? ? SING C6 H62 ? ? SING C6 H63 ? ? SING C5 C4 ? ? SING C5 H52 ? ? SING C5 H53 ? ? SING C4 C3 ? ? SING C4 H42 ? ? SING C4 H43 ? ? SING C3 C2 ? ? SING C3 H32 ? ? SING C3 H33 ? ? SING C2 C1 ? ? SING C2 H22 ? ? SING C2 H23 ? ? DOUB C1 O1 ? ? SING C1 N ? ? SING N CA ? ? SING N HN ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OD ? ? SING OD CG ? ? SING CG CB ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CB HB2 ? ? SING CB HB3 ? ? 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 $quorum_sensing_protein 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $quorum_sensing_protein '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 $quorum_sensing_protein 0.3 mM '[U-13C; U-15N; U-2H]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 0.2 pH temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 0.01 external direct . . . 1.000000000 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.01 external indirect . . . 0.251449530 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.01 external 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCO HNCA HN(CO)CA HN(CA)CO HNCACB HN(CA)CB stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'quorum sensing protein' _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 SER CA C 56.83 0.1 1 2 . 2 SER C C 171.13 0.1 1 3 . 2 SER CB C 62.82 0.1 1 4 . 3 ASP H H 8.88 0.01 1 5 . 3 ASP N N 121.56 0.1 1 6 . 3 ASP CA C 54.60 0.1 1 7 . 3 ASP C C 176.46 0.1 1 8 . 3 ASP CB C 39.81 0.1 1 9 . 4 LYS H H 8.43 0.01 1 10 . 4 LYS N N 120.68 0.1 1 11 . 4 LYS CA C 57.28 0.1 1 12 . 4 LYS C C 177.34 0.1 1 13 . 4 LYS CB C 31.58 0.1 1 14 . 5 ASP H H 8.03 0.01 1 15 . 5 ASP N N 119.08 0.1 1 16 . 5 ASP CA C 54.47 0.1 1 17 . 5 ASP C C 176.96 0.1 1 18 . 5 ASP CB C 40.57 0.1 1 19 . 6 PHE H H 8.52 0.01 1 20 . 6 PHE N N 121.94 0.1 1 21 . 6 PHE CA C 61.30 0.1 1 22 . 6 PHE C C 176.34 0.1 1 23 . 6 PHE CB C 38.13 0.1 1 24 . 7 PHE H H 8.25 0.01 1 25 . 7 PHE N N 117.54 0.1 1 26 . 7 PHE CA C 60.92 0.1 1 27 . 7 PHE C C 179.07 0.1 1 28 . 7 PHE CB C 37.21 0.1 1 29 . 8 SER H H 8.20 0.01 1 30 . 8 SER N N 116.19 0.1 1 31 . 8 SER CA C 61.08 0.1 1 32 . 8 SER C C 176.37 0.1 1 33 . 8 SER CB C 62.52 0.1 1 34 . 9 TRP H H 8.16 0.01 1 35 . 9 TRP N N 125.34 0.1 1 36 . 9 TRP CA C 61.87 0.1 1 37 . 9 TRP C C 177.46 0.1 1 38 . 9 TRP CB C 28.22 0.1 1 39 . 10 ARG H H 8.95 0.01 1 40 . 10 ARG N N 118.60 0.1 1 41 . 10 ARG CA C 59.13 0.1 1 42 . 10 ARG C C 176.84 0.1 1 43 . 10 ARG CB C 28.68 0.1 1 44 . 11 ARG H H 7.47 0.01 1 45 . 11 ARG N N 117.52 0.1 1 46 . 11 ARG CA C 59.19 0.1 1 47 . 11 ARG C C 178.93 0.1 1 48 . 11 ARG CB C 28.98 0.1 1 49 . 12 THR H H 7.73 0.01 1 50 . 12 THR N N 114.84 0.1 1 51 . 12 THR CA C 65.83 0.1 1 52 . 12 THR C C 176.48 0.1 1 53 . 12 THR CB C 68.16 0.1 1 54 . 13 MET H H 8.22 0.01 1 55 . 13 MET N N 120.32 0.1 1 56 . 13 MET CA C 56.13 0.1 1 57 . 13 MET C C 178.69 0.1 1 58 . 13 MET CB C 31.58 0.1 1 59 . 14 LEU H H 8.37 0.01 1 60 . 14 LEU N N 119.50 0.1 1 61 . 14 LEU CA C 58.30 0.1 1 62 . 14 LEU C C 179.93 0.1 1 63 . 14 LEU CB C 39.96 0.1 1 64 . 15 LEU H H 7.06 0.01 1 65 . 15 LEU N N 117.58 0.1 1 66 . 15 LEU CA C 57.09 0.1 1 67 . 15 LEU C C 179.10 0.1 1 68 . 15 LEU CB C 40.72 0.1 1 69 . 16 ARG H H 7.89 0.01 1 70 . 16 ARG N N 117.52 0.1 1 71 . 16 ARG CA C 59.07 0.1 1 72 . 16 ARG C C 179.96 0.1 1 73 . 16 ARG CB C 28.83 0.1 1 74 . 17 PHE H H 8.48 0.01 1 75 . 17 PHE N N 116.53 0.1 1 76 . 17 PHE CA C 60.98 0.1 1 77 . 17 PHE C C 178.40 0.1 1 78 . 17 PHE CB C 38.13 0.1 1 79 . 18 GLN H H 7.56 0.01 1 80 . 18 GLN N N 116.48 0.1 1 81 . 18 GLN CA C 57.85 0.1 1 82 . 18 GLN C C 176.93 0.1 1 83 . 18 GLN CB C 27.61 0.1 1 84 . 19 ARG H H 7.02 0.01 1 85 . 19 ARG N N 113.58 0.1 1 86 . 19 ARG CA C 55.05 0.1 1 87 . 19 ARG C C 176.63 0.1 1 88 . 19 ARG CB C 30.05 0.1 1 89 . 20 MET H H 7.00 0.01 1 90 . 20 MET N N 119.47 0.1 1 91 . 20 MET CA C 57.66 0.1 1 92 . 20 MET C C 176.63 0.1 1 93 . 20 MET CB C 31.58 0.1 1 94 . 21 GLU H H 8.77 0.01 1 95 . 21 GLU N N 118.48 0.1 1 96 . 21 GLU CA C 55.24 0.1 1 97 . 21 GLU C C 175.37 0.1 1 98 . 21 GLU CB C 30.66 0.1 1 99 . 22 THR H H 7.36 0.01 1 100 . 22 THR N N 108.66 0.1 1 101 . 22 THR CA C 58.75 0.1 1 102 . 22 THR C C 173.78 0.1 1 103 . 22 THR CB C 72.12 0.1 1 104 . 23 ALA H H 8.85 0.01 1 105 . 23 ALA N N 124.13 0.1 1 106 . 23 ALA CA C 54.54 0.1 1 107 . 23 ALA C C 178.19 0.1 1 108 . 23 ALA CB C 16.64 0.1 1 109 . 24 GLU H H 8.26 0.01 1 110 . 24 GLU N N 114.59 0.1 1 111 . 24 GLU CA C 58.43 0.1 1 112 . 24 GLU C C 178.28 0.1 1 113 . 24 GLU CB C 26.85 0.1 1 114 . 25 GLU H H 7.34 0.01 1 115 . 25 GLU N N 117.06 0.1 1 116 . 25 GLU CA C 55.68 0.1 1 117 . 25 GLU C C 178.96 0.1 1 118 . 25 GLU CB C 28.64 0.1 1 119 . 26 VAL H H 7.04 0.01 1 120 . 26 VAL N N 119.94 0.1 1 121 . 26 VAL CA C 65.28 0.1 1 122 . 26 VAL C C 177.75 0.1 1 123 . 26 VAL CB C 30.51 0.1 1 124 . 27 TYR H H 7.59 0.01 1 125 . 27 TYR N N 115.74 0.1 1 126 . 27 TYR CA C 59.00 0.1 1 127 . 27 TYR C C 178.19 0.1 1 128 . 27 TYR CB C 35.54 0.1 1 129 . 28 HIS H H 8.27 0.01 1 130 . 28 HIS N N 117.43 0.1 1 131 . 28 HIS CA C 57.92 0.1 1 132 . 28 HIS C C 176.66 0.1 1 133 . 28 HIS CB C 27.31 0.1 1 134 . 29 GLU H H 7.58 0.01 1 135 . 29 GLU N N 120.03 0.1 1 136 . 29 GLU CA C 58.11 0.1 1 137 . 29 GLU C C 178.60 0.1 1 138 . 29 GLU CB C 28.37 0.1 1 139 . 30 ILE H H 7.83 0.01 1 140 . 30 ILE N N 118.12 0.1 1 141 . 30 ILE CA C 64.93 0.1 1 142 . 30 ILE C C 177.03 0.1 1 143 . 30 ILE CB C 40.72 0.1 1 144 . 31 GLU C C 178.04 0.1 1 145 . 32 LEU H H 7.77 0.01 1 146 . 32 LEU N N 118.82 0.1 1 147 . 32 LEU CA C 57.47 0.1 1 148 . 32 LEU C C 180.35 0.1 1 149 . 32 LEU CB C 40.72 0.1 1 150 . 33 GLN H H 8.46 0.01 1 151 . 33 GLN N N 117.98 0.1 1 152 . 33 GLN CA C 57.28 0.1 1 153 . 33 GLN C C 178.79 0.1 1 154 . 33 GLN CB C 26.70 0.1 1 155 . 34 ALA H H 8.55 0.01 1 156 . 34 ALA N N 122.44 0.1 1 157 . 34 ALA CA C 55.17 0.1 1 158 . 34 ALA C C 179.93 0.1 1 159 . 34 ALA CB C 17.73 0.1 1 160 . 35 GLN H H 7.84 0.01 1 161 . 35 GLN N N 116.97 0.1 1 162 . 35 GLN CA C 58.36 0.1 1 163 . 35 GLN C C 181.58 0.1 1 164 . 35 GLN CB C 27.00 0.1 1 165 . 36 GLN H H 8.27 0.01 1 166 . 36 GLN N N 120.72 0.1 1 167 . 36 GLN CA C 58.17 0.1 1 168 . 36 GLN C C 177.57 0.1 1 169 . 36 GLN CB C 27.92 0.1 1 170 . 37 LEU H H 7.29 0.01 1 171 . 37 LEU N N 119.36 0.1 1 172 . 37 LEU CA C 54.09 0.1 1 173 . 37 LEU C C 177.70 0.1 1 174 . 37 LEU CB C 40.72 0.1 1 175 . 38 GLU H H 7.79 0.01 1 176 . 38 GLU N N 110.33 0.1 1 177 . 38 GLU CA C 56.51 0.1 1 178 . 38 GLU C C 175.63 0.1 1 179 . 38 GLU CB C 23.95 0.1 1 180 . 39 TYR H H 8.38 0.01 1 181 . 39 TYR N N 118.61 0.1 1 182 . 39 TYR CA C 58.43 0.1 1 183 . 39 TYR C C 173.63 0.1 1 184 . 39 TYR CB C 37.67 0.1 1 185 . 40 ASP H H 7.62 0.01 1 186 . 40 ASP N N 118.41 0.1 1 187 . 40 ASP CA C 56.20 0.1 1 188 . 40 ASP C C 176.07 0.1 1 189 . 40 ASP CB C 43.01 0.1 1 190 . 41 TYR H H 8.37 0.01 1 191 . 41 TYR N N 114.40 0.1 1 192 . 41 TYR CA C 54.15 0.1 1 193 . 41 TYR C C 174.81 0.1 1 194 . 41 TYR CB C 41.94 0.1 1 195 . 42 TYR H H 8.93 0.01 1 196 . 42 TYR N N 115.34 0.1 1 197 . 42 TYR CA C 54.73 0.1 1 198 . 42 TYR C C 174.22 0.1 1 199 . 42 TYR CB C 43.77 0.1 1 200 . 43 SER H H 9.37 0.01 1 201 . 43 SER N N 113.41 0.1 1 202 . 43 SER CA C 56.39 0.1 1 203 . 43 SER C C 171.71 0.1 1 204 . 43 SER CB C 66.02 0.1 1 205 . 44 LEU H H 9.81 0.01 1 206 . 44 LEU N N 125.53 0.1 1 207 . 44 LEU CA C 53.32 0.1 1 208 . 44 LEU C C 174.28 0.1 1 209 . 44 LEU CB C 44.23 0.1 1 210 . 45 CYS H H 9.16 0.01 1 211 . 45 CYS N N 126.64 0.1 1 212 . 45 CYS CA C 56.26 0.1 1 213 . 45 CYS C C 172.92 0.1 1 214 . 45 CYS CB C 29.14 0.1 1 215 . 46 VAL H H 9.31 0.01 1 216 . 46 VAL N N 127.44 0.1 1 217 . 46 VAL CA C 59.83 0.1 1 218 . 46 VAL C C 174.78 0.1 1 219 . 46 VAL CB C 34.01 0.1 1 220 . 47 ARG H H 9.36 0.01 1 221 . 47 ARG N N 125.68 0.1 1 222 . 47 ARG CA C 54.09 0.1 1 223 . 47 ARG C C 175.04 0.1 1 224 . 47 ARG CB C 32.95 0.1 1 225 . 48 HIS H H 9.12 0.01 1 226 . 48 HIS N N 122.22 0.1 1 227 . 48 HIS CA C 52.18 0.1 1 228 . 48 HIS C C 171.47 0.1 1 229 . 48 HIS CB C 29.29 0.1 1 230 . 49 PRO C C 175.95 0.1 1 231 . 50 VAL H H 8.45 0.01 1 232 . 50 VAL N N 123.06 0.1 1 233 . 50 VAL CA C 59.12 0.1 1 234 . 50 VAL C C 175.48 0.1 1 235 . 50 VAL CB C 33.57 0.1 1 236 . 51 PRO C C 177.04 0.1 1 237 . 52 PHE H H 8.30 0.01 1 238 . 52 PHE N N 115.36 0.1 1 239 . 52 PHE CA C 58.68 0.1 1 240 . 52 PHE C C 175.22 0.1 1 241 . 52 PHE CB C 36.76 0.1 1 242 . 53 THR H H 7.75 0.01 1 243 . 53 THR N N 113.56 0.1 1 244 . 53 THR CA C 59.90 0.1 1 245 . 53 THR C C 173.54 0.1 1 246 . 53 THR CB C 69.62 0.1 1 247 . 54 ARG H H 8.14 0.01 1 248 . 54 ARG N N 122.51 0.1 1 249 . 54 ARG CA C 53.96 0.1 1 250 . 54 ARG C C 173.51 0.1 1 251 . 54 ARG CB C 28.53 0.1 1 252 . 55 PRO C C 176.61 0.1 1 253 . 56 LYS H H 8.22 0.01 1 254 . 56 LYS N N 122.12 0.1 1 255 . 56 LYS CA C 55.37 0.1 1 256 . 56 LYS C C 176.00 0.1 1 257 . 56 LYS CB C 31.58 0.1 1 258 . 57 VAL H H 8.50 0.01 1 259 . 57 VAL N N 123.98 0.1 1 260 . 57 VAL CA C 60.53 0.1 1 261 . 57 VAL C C 174.58 0.1 1 262 . 57 VAL CB C 33.25 0.1 1 263 . 58 ALA H H 8.82 0.01 1 264 . 58 ALA N N 129.36 0.1 1 265 . 58 ALA CA C 50.39 0.1 1 266 . 58 ALA C C 175.35 0.1 1 267 . 58 ALA CB C 21.67 0.1 1 268 . 59 PHE H H 7.84 0.01 1 269 . 59 PHE N N 115.28 0.1 1 270 . 59 PHE CA C 55.11 0.1 1 271 . 59 PHE C C 172.99 0.1 1 272 . 59 PHE CB C 42.24 0.1 1 273 . 60 TYR H H 8.79 0.01 1 274 . 60 TYR N N 119.70 0.1 1 275 . 60 TYR CA C 56.26 0.1 1 276 . 60 TYR C C 174.49 0.1 1 277 . 60 TYR CB C 40.42 0.1 1 278 . 61 THR H H 8.61 0.01 1 279 . 61 THR N N 118.31 0.1 1 280 . 61 THR CA C 59.70 0.1 1 281 . 61 THR C C 170.79 0.1 1 282 . 61 THR CB C 68.00 0.1 1 283 . 62 ASN H H 6.89 0.01 1 284 . 62 ASN N N 122.32 0.1 1 285 . 62 ASN CA C 51.73 0.1 1 286 . 62 ASN C C 175.76 0.1 1 287 . 62 ASN CB C 37.52 0.1 1 288 . 63 TYR H H 8.64 0.01 1 289 . 63 TYR N N 119.23 0.1 1 290 . 63 TYR CA C 53.64 0.1 1 291 . 63 TYR CB C 36.45 0.1 1 292 . 64 PRO C C 178.70 0.1 1 293 . 65 GLU H H 9.11 0.01 1 294 . 65 GLU N N 126.62 0.1 1 295 . 65 GLU CA C 59.07 0.1 1 296 . 65 GLU C C 178.05 0.1 1 297 . 65 GLU CB C 27.46 0.1 1 298 . 66 ALA H H 9.03 0.01 1 299 . 66 ALA N N 118.66 0.1 1 300 . 66 ALA CA C 54.47 0.1 1 301 . 66 ALA C C 181.18 0.1 1 302 . 66 ALA CB C 17.55 0.1 1 303 . 67 TRP H H 7.53 0.01 1 304 . 67 TRP N N 115.63 0.1 1 305 . 67 TRP CA C 56.90 0.1 1 306 . 67 TRP C C 175.11 0.1 1 307 . 67 TRP CB C 30.20 0.1 1 308 . 68 VAL H H 7.57 0.01 1 309 . 68 VAL N N 118.31 0.1 1 310 . 68 VAL CA C 66.40 0.1 1 311 . 68 VAL C C 178.29 0.1 1 312 . 68 VAL CB C 30.81 0.1 1 313 . 69 SER H H 8.36 0.01 1 314 . 69 SER N N 110.93 0.1 1 315 . 69 SER CA C 60.85 0.1 1 316 . 69 SER C C 176.82 0.1 1 317 . 69 SER CB C 61.91 0.1 1 318 . 70 TYR H H 7.24 0.01 1 319 . 70 TYR N N 125.29 0.1 1 320 . 70 TYR CA C 61.30 0.1 1 321 . 70 TYR C C 176.82 0.1 1 322 . 70 TYR CB C 37.98 0.1 1 323 . 71 TYR H H 8.38 0.01 1 324 . 71 TYR N N 119.20 0.1 1 325 . 71 TYR CA C 59.51 0.1 1 326 . 71 TYR C C 179.82 0.1 1 327 . 71 TYR CB C 37.37 0.1 1 328 . 72 GLN H H 7.82 0.01 1 329 . 72 GLN N N 115.28 0.1 1 330 . 72 GLN CA C 58.49 0.1 1 331 . 72 GLN C C 179.12 0.1 1 332 . 72 GLN CB C 28.68 0.1 1 333 . 73 ALA H H 7.94 0.01 1 334 . 73 ALA N N 123.46 0.1 1 335 . 73 ALA CA C 54.35 0.1 1 336 . 73 ALA C C 179.71 0.1 1 337 . 73 ALA CB C 16.79 0.1 1 338 . 74 LYS H H 7.12 0.01 1 339 . 74 LYS N N 113.22 0.1 1 340 . 74 LYS CA C 53.01 0.1 1 341 . 74 LYS C C 175.70 0.1 1 342 . 74 LYS CB C 28.37 0.1 1 343 . 75 ASN H H 7.42 0.01 1 344 . 75 ASN N N 115.02 0.1 1 345 . 75 ASN CA C 53.32 0.1 1 346 . 75 ASN C C 176.70 0.1 1 347 . 75 ASN CB C 36.00 0.1 1 348 . 76 PHE H H 6.99 0.01 1 349 . 76 PHE N N 114.74 0.1 1 350 . 76 PHE CA C 55.24 0.1 1 351 . 76 PHE C C 177.14 0.1 1 352 . 76 PHE CB C 34.47 0.1 1 353 . 77 LEU H H 8.40 0.01 1 354 . 77 LEU N N 122.58 0.1 1 355 . 77 LEU CA C 57.47 0.1 1 356 . 77 LEU C C 178.73 0.1 1 357 . 77 LEU CB C 41.79 0.1 1 358 . 78 ALA H H 6.93 0.01 1 359 . 78 ALA N N 114.17 0.1 1 360 . 78 ALA CA C 53.32 0.1 1 361 . 78 ALA C C 178.76 0.1 1 362 . 78 ALA CB C 18.77 0.1 1 363 . 79 ILE H H 7.17 0.01 1 364 . 79 ILE N N 106.53 0.1 1 365 . 79 ILE CA C 59.07 0.1 1 366 . 79 ILE C C 175.76 0.1 1 367 . 79 ILE CB C 39.50 0.1 1 368 . 80 ASP H H 7.09 0.01 1 369 . 80 ASP N N 123.20 0.1 1 370 . 80 ASP CA C 51.98 0.1 1 371 . 80 ASP C C 176.67 0.1 1 372 . 80 ASP CB C 40.26 0.1 1 373 . 81 PRO CA C 63.40 0.1 1 374 . 81 PRO C C 178.97 0.1 1 375 . 82 VAL H H 7.88 0.01 1 376 . 82 VAL N N 113.39 0.1 1 377 . 82 VAL CA C 61.17 0.1 1 378 . 82 VAL C C 172.46 0.1 1 379 . 82 VAL CB C 28.37 0.1 1 380 . 83 LEU H H 6.41 0.01 1 381 . 83 LEU N N 112.25 0.1 1 382 . 83 LEU CA C 51.28 0.1 1 383 . 83 LEU C C 175.53 0.1 1 384 . 83 LEU CB C 40.42 0.1 1 385 . 84 ASN H H 6.80 0.01 1 386 . 84 ASN N N 116.59 0.1 1 387 . 84 ASN CA C 48.35 0.1 1 388 . 84 ASN C C 178.07 0.1 1 389 . 84 ASN CB C 38.89 0.1 1 390 . 85 PRO CA C 64.36 0.1 1 391 . 85 PRO C C 177.70 0.1 1 392 . 86 GLU H H 7.75 0.01 1 393 . 86 GLU N N 114.78 0.1 1 394 . 86 GLU CA C 57.28 0.1 1 395 . 86 GLU C C 177.32 0.1 1 396 . 86 GLU CB C 27.76 0.1 1 397 . 87 ASN H H 7.80 0.01 1 398 . 87 ASN N N 113.00 0.1 1 399 . 87 ASN CA C 53.07 0.1 1 400 . 87 ASN C C 174.14 0.1 1 401 . 87 ASN CB C 38.13 0.1 1 402 . 88 PHE H H 7.38 0.01 1 403 . 88 PHE N N 118.31 0.1 1 404 . 88 PHE CA C 58.24 0.1 1 405 . 88 PHE C C 175.41 0.1 1 406 . 88 PHE CB C 40.26 0.1 1 407 . 89 SER H H 8.41 0.01 1 408 . 89 SER N N 115.25 0.1 1 409 . 89 SER CA C 57.34 0.1 1 410 . 89 SER C C 174.91 0.1 1 411 . 89 SER CB C 63.13 0.1 1 412 . 90 GLN H H 9.32 0.01 1 413 . 90 GLN N N 123.81 0.1 1 414 . 90 GLN CA C 56.07 0.1 1 415 . 90 GLN C C 176.73 0.1 1 416 . 91 GLY H H 8.72 0.01 1 417 . 91 GLY N N 103.32 0.1 1 418 . 91 GLY CA C 46.14 0.1 1 419 . 91 GLY C C 172.17 0.1 1 420 . 92 HIS H H 7.96 0.01 1 421 . 92 HIS N N 117.10 0.1 1 422 . 92 HIS CA C 54.09 0.1 1 423 . 92 HIS C C 173.76 0.1 1 424 . 92 HIS CB C 31.88 0.1 1 425 . 93 LEU H H 8.79 0.01 1 426 . 93 LEU N N 121.70 0.1 1 427 . 93 LEU CA C 54.41 0.1 1 428 . 93 LEU C C 174.67 0.1 1 429 . 93 LEU CB C 43.23 0.1 1 430 . 94 MET H H 8.71 0.01 1 431 . 94 MET N N 123.89 0.1 1 432 . 94 MET CA C 53.58 0.1 1 433 . 94 MET C C 175.53 0.1 1 434 . 94 MET CB C 32.95 0.1 1 435 . 95 TRP H H 8.55 0.01 1 436 . 95 TRP N N 123.97 0.1 1 437 . 95 TRP CA C 56.13 0.1 1 438 . 95 TRP C C 175.47 0.1 1 439 . 95 TRP CB C 28.37 0.1 1 440 . 96 ASN H H 6.86 0.01 1 441 . 96 ASN N N 116.78 0.1 1 442 . 96 ASN CA C 51.67 0.1 1 443 . 96 ASN C C 173.67 0.1 1 444 . 96 ASN CB C 39.35 0.1 1 445 . 97 ASP H H 8.74 0.01 1 446 . 97 ASP N N 118.20 0.1 1 447 . 97 ASP CA C 57.73 0.1 1 448 . 97 ASP C C 178.94 0.1 1 449 . 97 ASP CB C 39.35 0.1 1 450 . 98 ASP H H 8.31 0.01 1 451 . 98 ASP N N 119.29 0.1 1 452 . 98 ASP CA C 56.58 0.1 1 453 . 98 ASP C C 178.56 0.1 1 454 . 98 ASP CB C 38.74 0.1 1 455 . 99 LEU H H 7.62 0.01 1 456 . 99 LEU N N 121.58 0.1 1 457 . 99 LEU CA C 56.26 0.1 1 458 . 99 LEU C C 177.18 0.1 1 459 . 99 LEU CB C 40.72 0.1 1 460 . 100 PHE H H 6.80 0.01 1 461 . 100 PHE N N 112.14 0.1 1 462 . 100 PHE CA C 57.15 0.1 1 463 . 100 PHE C C 176.67 0.1 1 464 . 100 PHE CB C 37.45 0.1 1 465 . 101 SER H H 7.53 0.01 1 466 . 101 SER N N 116.87 0.1 1 467 . 101 SER CA C 62.19 0.1 1 468 . 101 SER C C 175.94 0.1 1 469 . 102 GLU H H 8.41 0.01 1 470 . 102 GLU N N 118.61 0.1 1 471 . 102 GLU CA C 54.79 0.1 1 472 . 102 GLU C C 175.14 0.1 1 473 . 102 GLU CB C 27.00 0.1 1 474 . 103 ALA H H 8.06 0.01 1 475 . 103 ALA N N 126.41 0.1 1 476 . 103 ALA CA C 49.82 0.1 1 477 . 103 ALA C C 176.64 0.1 1 478 . 103 ALA CB C 19.08 0.1 1 479 . 104 GLN H H 8.91 0.01 1 480 . 104 GLN N N 121.74 0.1 1 481 . 104 GLN CA C 60.85 0.1 1 482 . 104 GLN CB C 25.33 0.1 1 483 . 105 PRO CA C 65.76 0.1 1 484 . 105 PRO C C 179.85 0.1 1 485 . 106 LEU H H 6.56 0.01 1 486 . 106 LEU N N 117.53 0.1 1 487 . 106 LEU CA C 57.22 0.1 1 488 . 106 LEU C C 177.00 0.1 1 489 . 106 LEU CB C 40.26 0.1 1 490 . 107 TRP H H 7.51 0.01 1 491 . 107 TRP N N 121.30 0.1 1 492 . 107 TRP CA C 57.02 0.1 1 493 . 107 TRP C C 178.25 0.1 1 494 . 107 TRP CB C 31.58 0.1 1 495 . 108 GLU H H 8.77 0.01 1 496 . 108 GLU N N 118.47 0.1 1 497 . 108 GLU CA C 58.68 0.1 1 498 . 108 GLU C C 179.21 0.1 1 499 . 108 GLU CB C 28.07 0.1 1 500 . 109 ALA H H 7.72 0.01 1 501 . 109 ALA N N 120.82 0.1 1 502 . 109 ALA CA C 54.09 0.1 1 503 . 109 ALA C C 180.29 0.1 1 504 . 109 ALA CB C 18.01 0.1 1 505 . 110 ALA H H 9.08 0.01 1 506 . 110 ALA N N 127.67 0.1 1 507 . 110 ALA CA C 54.66 0.1 1 508 . 110 ALA C C 180.03 0.1 1 509 . 110 ALA CB C 16.18 0.1 1 510 . 111 ARG H H 7.41 0.01 1 511 . 111 ARG N N 118.64 0.1 1 512 . 111 ARG CA C 58.62 0.1 1 513 . 111 ARG C C 180.82 0.1 1 514 . 111 ARG CB C 28.53 0.1 1 515 . 112 ALA H H 7.52 0.01 1 516 . 112 ALA N N 121.36 0.1 1 517 . 112 ALA CA C 53.71 0.1 1 518 . 112 ALA C C 178.82 0.1 1 519 . 112 ALA CB C 16.94 0.1 1 520 . 113 HIS H H 7.25 0.01 1 521 . 113 HIS N N 113.00 0.1 1 522 . 113 HIS CA C 56.20 0.1 1 523 . 113 HIS C C 173.23 0.1 1 524 . 113 HIS CB C 27.00 0.1 1 525 . 114 GLY H H 7.42 0.01 1 526 . 114 GLY N N 106.24 0.1 1 527 . 114 GLY CA C 45.29 0.1 1 528 . 114 GLY C C 172.55 0.1 1 529 . 115 LEU H H 7.45 0.01 1 530 . 115 LEU N N 121.07 0.1 1 531 . 115 LEU CA C 54.41 0.1 1 532 . 115 LEU C C 175.38 0.1 1 533 . 115 LEU CB C 39.50 0.1 1 534 . 116 ARG H H 7.72 0.01 1 535 . 116 ARG N N 115.90 0.1 1 536 . 116 ARG CA C 56.45 0.1 1 537 . 116 ARG C C 176.79 0.1 1 538 . 116 ARG CB C 31.42 0.1 1 539 . 117 ARG H H 7.93 0.01 1 540 . 117 ARG N N 115.72 0.1 1 541 . 117 ARG CA C 53.07 0.1 1 542 . 117 ARG C C 175.11 0.1 1 543 . 117 ARG CB C 33.71 0.1 1 544 . 118 GLY H H 8.64 0.01 1 545 . 118 GLY N N 108.05 0.1 1 546 . 118 GLY CA C 45.60 0.1 1 547 . 118 GLY C C 170.31 0.1 1 548 . 119 VAL H H 7.98 0.01 1 549 . 119 VAL N N 115.37 0.1 1 550 . 119 VAL CA C 59.13 0.1 1 551 . 119 VAL C C 173.02 0.1 1 552 . 119 VAL CB C 34.32 0.1 1 553 . 120 THR H H 8.79 0.01 1 554 . 120 THR N N 119.69 0.1 1 555 . 120 THR CA C 61.94 0.1 1 556 . 120 THR C C 171.31 0.1 1 557 . 120 THR CB C 72.58 0.1 1 558 . 121 GLN H H 9.61 0.01 1 559 . 121 GLN N N 128.42 0.1 1 560 . 121 GLN CA C 52.94 0.1 1 561 . 121 GLN C C 173.76 0.1 1 562 . 121 GLN CB C 31.12 0.1 1 563 . 122 TYR H H 9.13 0.01 1 564 . 122 TYR N N 129.33 0.1 1 565 . 122 TYR CA C 53.71 0.1 1 566 . 122 TYR C C 173.88 0.1 1 567 . 122 TYR CB C 41.64 0.1 1 568 . 123 LEU H H 8.02 0.01 1 569 . 123 LEU N N 128.19 0.1 1 570 . 123 LEU CA C 53.77 0.1 1 571 . 123 LEU C C 172.29 0.1 1 572 . 123 LEU CB C 46.21 0.1 1 573 . 124 MET H H 8.01 0.01 1 574 . 124 MET N N 124.07 0.1 1 575 . 124 MET CA C 53.64 0.1 1 576 . 124 MET C C 176.00 0.1 1 577 . 124 MET CB C 33.40 0.1 1 578 . 125 LEU H H 8.78 0.01 1 579 . 125 LEU N N 127.78 0.1 1 580 . 129 ALA CA C 51.98 0.1 1 581 . 129 ALA C C 175.38 0.1 1 582 . 129 ALA CB C 18.47 0.1 1 583 . 130 LEU H H 8.62 0.01 1 584 . 130 LEU N N 119.61 0.1 1 585 . 130 LEU CA C 53.58 0.1 1 586 . 130 LEU C C 175.41 0.1 1 587 . 130 LEU CB C 44.68 0.1 1 588 . 131 GLY H H 8.56 0.01 1 589 . 131 GLY N N 106.68 0.1 1 590 . 131 GLY CA C 43.62 0.1 1 591 . 131 GLY C C 171.02 0.1 1 592 . 132 PHE H H 8.96 0.01 1 593 . 132 PHE N N 117.75 0.1 1 594 . 132 PHE CA C 55.81 0.1 1 595 . 132 PHE C C 175.91 0.1 1 596 . 132 PHE CB C 41.03 0.1 1 597 . 133 LEU H H 9.79 0.01 1 598 . 133 LEU N N 129.96 0.1 1 599 . 133 LEU CA C 52.82 0.1 1 600 . 133 LEU C C 173.70 0.1 1 601 . 133 LEU CB C 44.23 0.1 1 602 . 134 SER H H 9.88 0.01 1 603 . 134 SER N N 122.84 0.1 1 604 . 134 SER CA C 57.22 0.1 1 605 . 134 SER C C 173.88 0.1 1 606 . 134 SER CB C 64.04 0.1 1 607 . 135 PHE H H 8.86 0.01 1 608 . 135 PHE N N 124.18 0.1 1 609 . 135 PHE CA C 51.73 0.1 1 610 . 135 PHE C C 174.20 0.1 1 611 . 135 PHE CB C 39.50 0.1 1 612 . 136 SER H H 8.94 0.01 1 613 . 136 SER N N 110.67 0.1 1 614 . 136 SER CA C 57.34 0.1 1 615 . 136 SER C C 174.82 0.1 1 616 . 136 SER CB C 66.94 0.1 1 617 . 137 ARG H H 9.15 0.01 1 618 . 137 ARG N N 118.49 0.1 1 619 . 137 ARG CA C 53.96 0.1 1 620 . 137 ARG C C 175.05 0.1 1 621 . 137 ARG CB C 34.32 0.1 1 622 . 138 CYS H H 8.93 0.01 1 623 . 138 CYS N N 119.40 0.1 1 624 . 138 CYS CA C 58.17 0.1 1 625 . 138 CYS C C 175.38 0.1 1 626 . 138 CYS CB C 28.37 0.1 1 627 . 139 SER H H 7.84 0.01 1 628 . 139 SER N N 113.76 0.1 1 629 . 139 SER CA C 57.28 0.1 1 630 . 139 SER C C 174.26 0.1 1 631 . 139 SER CB C 63.43 0.1 1 632 . 140 ALA H H 8.56 0.01 1 633 . 140 ALA N N 125.00 0.1 1 634 . 140 ALA CA C 51.73 0.1 1 635 . 140 ALA C C 177.73 0.1 1 636 . 140 ALA CB C 18.31 0.1 1 637 . 141 ARG H H 7.78 0.01 1 638 . 141 ARG N N 119.51 0.1 1 639 . 141 ARG CA C 56.07 0.1 1 640 . 141 ARG C C 176.17 0.1 1 641 . 141 ARG CB C 29.59 0.1 1 642 . 142 GLU H H 8.56 0.01 1 643 . 142 GLU N N 123.37 0.1 1 644 . 142 GLU CA C 55.81 0.1 1 645 . 142 GLU C C 175.92 0.1 1 646 . 142 GLU CB C 28.83 0.1 1 647 . 143 ILE H H 8.24 0.01 1 648 . 143 ILE N N 124.72 0.1 1 649 . 143 ILE CA C 58.36 0.1 1 650 . 143 ILE C C 174.54 0.1 1 651 . 143 ILE CB C 37.98 0.1 1 652 . 144 PRO C C 176.17 0.1 1 653 . 145 ILE H H 7.97 0.01 1 654 . 145 ILE N N 121.24 0.1 1 655 . 145 ILE CA C 60.34 0.1 1 656 . 145 ILE C C 175.88 0.1 1 657 . 145 ILE CB C 38.13 0.1 1 658 . 146 LEU H H 8.45 0.01 1 659 . 146 LEU N N 126.50 0.1 1 660 . 146 LEU CA C 54.41 0.1 1 661 . 146 LEU C C 177.22 0.1 1 662 . 146 LEU CB C 40.42 0.1 1 663 . 147 SER H H 8.24 0.01 1 664 . 147 SER N N 117.46 0.1 1 665 . 147 SER CA C 58.49 0.1 1 666 . 147 SER C C 175.14 0.1 1 667 . 147 SER CB C 63.28 0.1 1 668 . 148 ASP H H 8.65 0.01 1 669 . 148 ASP N N 120.85 0.1 1 670 . 148 ASP CA C 55.62 0.1 1 671 . 148 ASP C C 177.13 0.1 1 672 . 148 ASP CB C 38.74 0.1 1 673 . 149 GLU H H 7.84 0.01 1 674 . 149 GLU N N 119.07 0.1 1 675 . 149 GLU CA C 58.68 0.1 1 676 . 149 GLU C C 178.38 0.1 1 677 . 149 GLU CB C 28.22 0.1 1 678 . 150 LEU H H 7.84 0.01 1 679 . 150 LEU N N 119.07 0.1 1 680 . 150 LEU CA C 58.11 0.1 1 681 . 150 LEU C C 178.42 0.1 1 682 . 150 LEU CB C 40.57 0.1 1 683 . 151 GLN H H 7.91 0.01 1 684 . 151 GLN N N 116.79 0.1 1 685 . 151 GLN CA C 59.00 0.1 1 686 . 151 GLN C C 177.92 0.1 1 687 . 151 GLN CB C 27.31 0.1 1 688 . 153 LYS H H 8.20 0.01 1 689 . 153 LYS N N 117.92 0.1 1 690 . 153 LYS CA C 59.90 0.1 1 691 . 153 LYS C C 179.38 0.1 1 692 . 153 LYS CB C 31.88 0.1 1 693 . 154 MET H H 8.81 0.01 1 694 . 154 MET N N 117.02 0.1 1 695 . 154 MET CA C 60.98 0.1 1 696 . 154 MET C C 178.19 0.1 1 697 . 154 MET CB C 32.03 0.1 1 698 . 155 GLN H H 8.66 0.01 1 699 . 155 GLN N N 119.05 0.1 1 700 . 155 GLN CA C 59.18 0.1 1 701 . 155 GLN C C 178.06 0.1 1 702 . 155 GLN CB C 28.53 0.1 1 703 . 156 LEU H H 7.44 0.01 1 704 . 156 LEU N N 119.66 0.1 1 705 . 156 LEU CA C 58.43 0.1 1 706 . 156 LEU C C 178.83 0.1 1 707 . 156 LEU CB C 40.11 0.1 1 708 . 157 LEU H H 8.68 0.01 1 709 . 157 LEU N N 117.26 0.1 1 710 . 157 LEU CA C 57.72 0.1 1 711 . 157 LEU C C 180.18 0.1 1 712 . 157 LEU CB C 41.51 0.1 1 713 . 158 VAL H H 8.74 0.01 1 714 . 158 VAL N N 120.53 0.1 1 715 . 158 VAL CA C 65.54 0.1 1 716 . 158 VAL C C 174.11 0.1 1 717 . 158 VAL CB C 30.20 0.1 1 718 . 159 ARG H H 6.93 0.01 1 719 . 159 ARG N N 121.11 0.1 1 720 . 159 ARG CA C 59.72 0.1 1 721 . 159 ARG C C 177.88 0.1 1 722 . 159 ARG CB C 29.87 0.1 1 723 . 160 GLU H H 8.70 0.01 1 724 . 160 GLU N N 113.40 0.1 1 725 . 160 GLU CA C 57.42 0.1 1 726 . 160 GLU CB C 26.54 0.1 1 727 . 161 SER H H 7.81 0.01 1 728 . 161 SER N N 115.43 0.1 1 729 . 161 SER C C 175.44 0.1 1 730 . 162 LEU H H 7.52 0.01 1 731 . 162 LEU N N 122.46 0.1 1 732 . 162 LEU CA C 58.00 0.1 1 733 . 162 LEU C C 179.37 0.1 1 734 . 163 MET H H 8.28 0.01 1 735 . 163 MET N N 115.75 0.1 1 736 . 163 MET CA C 57.92 0.1 1 737 . 163 MET C C 179.43 0.1 1 738 . 163 MET CB C 30.81 0.1 1 739 . 164 ALA H H 8.01 0.01 1 740 . 164 ALA N N 122.25 0.1 1 741 . 164 ALA CA C 54.86 0.1 1 742 . 164 ALA C C 179.05 0.1 1 743 . 164 ALA CB C 17.70 0.1 1 744 . 165 LEU H H 8.23 0.01 1 745 . 165 LEU N N 116.19 0.1 1 746 . 165 LEU CA C 57.73 0.1 1 747 . 165 LEU C C 179.88 0.1 1 748 . 165 LEU CB C 39.96 0.1 1 749 . 166 MET H H 8.10 0.01 1 750 . 166 MET N N 117.34 0.1 1 751 . 166 MET CA C 58.05 0.1 1 752 . 166 MET C C 178.78 0.1 1 753 . 166 MET CB C 31.73 0.1 1 754 . 167 ARG H H 7.75 0.01 1 755 . 167 ARG N N 120.25 0.1 1 756 . 167 ARG CA C 58.24 0.1 1 757 . 167 ARG C C 178.25 0.1 1 758 . 167 ARG CB C 28.98 0.1 1 759 . 168 LEU H H 7.84 0.01 1 760 . 168 LEU N N 118.22 0.1 1 761 . 168 LEU CA C 55.17 0.1 1 762 . 168 LEU C C 177.01 0.1 1 763 . 168 LEU CB C 40.72 0.1 1 764 . 169 ASN H H 7.90 0.01 1 765 . 169 ASN N N 115.67 0.1 1 766 . 169 ASN CA C 53.54 0.1 1 767 . 169 ASN C C 174.54 0.1 1 768 . 169 ASN CB C 37.82 0.1 1 769 . 170 ASP H H 8.20 0.01 1 770 . 170 ASP N N 117.92 0.1 1 771 . 170 ASP CA C 53.52 0.1 1 772 . 170 ASP C C 174.45 0.1 1 773 . 170 ASP CB C 38.74 0.1 1 774 . 171 GLU H H 7.80 0.01 1 775 . 171 GLU N N 123.49 0.1 1 776 . 171 GLU CA C 56.39 0.1 1 777 . 171 GLU C C 180.10 0.1 1 778 . 171 GLU CB C 29.29 0.1 1 stop_ save_