data_6271 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N assignments of the ligand binding domain of LasR ; _BMRB_accession_number 6271 _BMRB_flat_file_name bmr6271.str _Entry_type original _Submission_date 2004-07-23 _Accession_date 2004-07-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Chemical shift assignments from the ligand binding domain of the dimeric LasR protein. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bottomley Matthew J. . 2 Muraglia Ester . . 3 Bazzo Renzo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 159 "13C chemical shifts" 499 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-08-24 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5558 'Same first author' 5592 'Same first author' stop_ _Original_release_date 2007-08-24 save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Molecular insights into quorum sensing in the human pathogen Pseudomonas aeruginosa from the structure of the virulence regulator LasR bound to its autoinducer ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17363368 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bottomley Matthew J. . 2 Muraglia E. . . 3 Bazzo R. . . 4 Carf???? A. . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 282 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13592 _Page_last 13600 _Year 2007 _Details . loop_ _Keyword assignment LasR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LasR-LBD dimer' _Abbreviation_common 'LasR-LBD dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LasR-LBD dimer' $LasR-LBD '3-oxo-c12-homoserine lactone' $OHN stop_ _System_molecular_weight 43000 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'regulation of virulence gene expression in Pseudomonas aeruginosa bacteria' stop_ _Database_query_date . _Details 'A Ligand-Binding-Domain fragment of the Pseudomonas aeruginosa LasR protein. It is a dimer.' save_ ######################## # Monomeric polymers # ######################## save_LasR-LBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LasR Ligand binding domain' _Abbreviation_common LasR _Molecular_mass 20500 _Mol_thiol_state 'all free' loop_ _Biological_function 'Binds C12-HSL for activation of gene expression' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; MALVDGFLELERSSGKLEWS AILQKMASDLGFSKILFGLL PKDSQDYENAFIVGNYPAAW REHYDRAGYARVDPTVSHCT QSVLPIFWEPSIYQTRKQHE FFEEASAAGLVYGLTMPLHG ARGELGALSLSVEAENRAEA NRFMESVLPTLWMLKDYALQ SGAGLAFEHPVSK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LEU 4 VAL 5 ASP 6 GLY 7 PHE 8 LEU 9 GLU 10 LEU 11 GLU 12 ARG 13 SER 14 SER 15 GLY 16 LYS 17 LEU 18 GLU 19 TRP 20 SER 21 ALA 22 ILE 23 LEU 24 GLN 25 LYS 26 MET 27 ALA 28 SER 29 ASP 30 LEU 31 GLY 32 PHE 33 SER 34 LYS 35 ILE 36 LEU 37 PHE 38 GLY 39 LEU 40 LEU 41 PRO 42 LYS 43 ASP 44 SER 45 GLN 46 ASP 47 TYR 48 GLU 49 ASN 50 ALA 51 PHE 52 ILE 53 VAL 54 GLY 55 ASN 56 TYR 57 PRO 58 ALA 59 ALA 60 TRP 61 ARG 62 GLU 63 HIS 64 TYR 65 ASP 66 ARG 67 ALA 68 GLY 69 TYR 70 ALA 71 ARG 72 VAL 73 ASP 74 PRO 75 THR 76 VAL 77 SER 78 HIS 79 CYS 80 THR 81 GLN 82 SER 83 VAL 84 LEU 85 PRO 86 ILE 87 PHE 88 TRP 89 GLU 90 PRO 91 SER 92 ILE 93 TYR 94 GLN 95 THR 96 ARG 97 LYS 98 GLN 99 HIS 100 GLU 101 PHE 102 PHE 103 GLU 104 GLU 105 ALA 106 SER 107 ALA 108 ALA 109 GLY 110 LEU 111 VAL 112 TYR 113 GLY 114 LEU 115 THR 116 MET 117 PRO 118 LEU 119 HIS 120 GLY 121 ALA 122 ARG 123 GLY 124 GLU 125 LEU 126 GLY 127 ALA 128 LEU 129 SER 130 LEU 131 SER 132 VAL 133 GLU 134 ALA 135 GLU 136 ASN 137 ARG 138 ALA 139 GLU 140 ALA 141 ASN 142 ARG 143 PHE 144 MET 145 GLU 146 SER 147 VAL 148 LEU 149 PRO 150 THR 151 LEU 152 TRP 153 MET 154 LEU 155 LYS 156 ASP 157 TYR 158 ALA 159 LEU 160 GLN 161 SER 162 GLY 163 ALA 164 GLY 165 LEU 166 ALA 167 PHE 168 GLU 169 HIS 170 PRO 171 VAL 172 SER 173 LYS 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 PDB 2UV0 "Structure Of The P. Aeruginosa Lasr Ligand-Binding Domain Bound To Its Autoinducer" 99.42 175 97.67 97.67 3.13e-118 PDB 3IX3 "Lasr-Oc12 Hsl Complex" 100.00 173 100.00 100.00 2.06e-123 PDB 3IX4 "Lasr-Tp1 Complex" 100.00 173 100.00 100.00 2.06e-123 PDB 3IX8 "Lasr-Tp3 Complex" 100.00 173 100.00 100.00 2.06e-123 PDB 3JPU "Lasr-Tp4 Complex" 100.00 173 100.00 100.00 2.06e-123 PDB 4NG2 "Crystal Structure Of Lasr Lbd-qsla Complex From Pseudomonas Aeruginosa" 98.27 184 100.00 100.00 5.38e-121 DBJ BAA06489 "LasR [Pseudomonas aeruginosa]" 100.00 239 99.42 100.00 1.19e-122 DBJ BAA06490 "LasR [Pseudomonas aeruginosa PA103]" 100.00 239 99.42 100.00 1.31e-122 DBJ BAP24227 "transcriptional regulator [Pseudomonas aeruginosa]" 100.00 194 100.00 100.00 2.42e-123 DBJ BAP51814 "transcriptional regulator [Pseudomonas aeruginosa]" 100.00 194 100.00 100.00 2.42e-123 DBJ GAA16961 "transcriptional regulator LasR [Pseudomonas aeruginosa NCMG1179]" 100.00 239 100.00 100.00 2.07e-123 EMBL CAW28738 "transcriptional regulator LasR [Pseudomonas aeruginosa LESB58]" 100.00 239 100.00 100.00 2.64e-123 EMBL CCQ87458 "N-3-oxododecanoyl-L-homoserine lactone quorum-sensing transcriptional activator @ Transcriptional regulator LasR [Pseudomonas a" 100.00 239 100.00 100.00 2.64e-123 EMBL CDH72122 "Transcriptional activator protein lasR [Pseudomonas aeruginosa MH38]" 100.00 239 99.42 99.42 6.76e-122 EMBL CDH78244 "Transcriptional activator protein lasR [Pseudomonas aeruginosa MH27]" 100.00 239 100.00 100.00 2.64e-123 EMBL CDI89583 "transcriptional regulator LasR [Pseudomonas aeruginosa PA38182]" 100.00 239 100.00 100.00 2.64e-123 GB AAA25874 "transcriptional activator LasR [Pseudomonas aeruginosa PAO1]" 100.00 239 100.00 100.00 2.64e-123 GB AAG04819 "transcriptional regulator LasR [Pseudomonas aeruginosa PAO1]" 100.00 239 100.00 100.00 2.64e-123 GB AAT50467 "PA1430, partial [synthetic construct]" 100.00 240 100.00 100.00 3.63e-123 GB ABJ10611 "transcriptional regulator LasR [Pseudomonas aeruginosa UCBPP-PA14]" 100.00 239 100.00 100.00 2.64e-123 GB ABR86383 "transcriptional regulator LasR [Pseudomonas aeruginosa PA7]" 100.00 239 98.27 100.00 1.85e-121 REF NP_250121 "transcriptional regulator LasR [Pseudomonas aeruginosa PAO1]" 100.00 239 100.00 100.00 2.64e-123 REF WP_003082999 "LuxR family transcriptional regulator [Pseudomonas aeruginosa]" 100.00 239 100.00 100.00 2.64e-123 REF WP_003100458 "MULTISPECIES: LuxR family transcriptional regulator [Pseudomonas]" 90.75 223 99.36 100.00 3.12e-111 REF WP_003133239 "LuxR family transcriptional regulator [Pseudomonas aeruginosa]" 100.00 239 100.00 100.00 2.17e-123 REF WP_010792033 "transcriptional activator protein lasR [Pseudomonas aeruginosa]" 53.76 93 100.00 100.00 1.68e-61 SP P25084 "RecName: Full=Transcriptional activator protein LasR [Pseudomonas aeruginosa PAO1]" 100.00 239 100.00 100.00 2.64e-123 stop_ save_ ############# # Ligands # ############# save_OHN _Saveframe_category ligand _Mol_type non-polymer _Name_common "OHN (N-3-OXO-DODECANOYL-L-HOMOSERINE LACTONE)" _BMRB_code . _PDB_code OHN _Molecular_mass 297.390 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 16 14:27:51 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C21 C21 C . 0 . ? C20 C20 C . 0 . ? C19 C19 C . 0 . ? C18 C18 C . 0 . ? C17 C17 C . 0 . ? C16 C16 C . 0 . ? C15 C15 C . 0 . ? C14 C14 C . 0 . ? C13 C13 C . 0 . ? C11 C11 C . 0 . ? O12 O12 O . 0 . ? C10 C10 C . 0 . ? C8 C8 C . 0 . ? O9 O9 O . 0 . ? N7 N7 N . 0 . ? C1 C1 C . 0 . ? C5 C5 C . 0 . ? C4 C4 C . 0 . ? C2 C2 C . 0 . ? O6 O6 O . 0 . ? OAP OAP O . 0 . ? H211 H211 H . 0 . ? H212 H212 H . 0 . ? H213 H213 H . 0 . ? H201 H201 H . 0 . ? H202 H202 H . 0 . ? H191 H191 H . 0 . ? H192 H192 H . 0 . ? H181 H181 H . 0 . ? H182 H182 H . 0 . ? H171 H171 H . 0 . ? H172 H172 H . 0 . ? H161 H161 H . 0 . ? H162 H162 H . 0 . ? H151 H151 H . 0 . ? H152 H152 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H7 H7 H . 0 . ? H1 H1 H . 0 . ? H5C1 H5C1 H . 0 . ? H5C2 H5C2 H . 0 . ? H4C1 H4C1 H . 0 . ? H4C2 H4C2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C21 C20 ? ? SING C20 C19 ? ? SING C19 C18 ? ? SING C18 C17 ? ? SING C17 C16 ? ? SING C16 C15 ? ? SING C15 C14 ? ? SING C14 C13 ? ? SING C13 C11 ? ? DOUB C11 O12 ? ? SING C11 C10 ? ? SING C10 C8 ? ? DOUB C8 O9 ? ? SING C8 N7 ? ? SING N7 C1 ? ? SING C1 C5 ? ? SING C5 C4 ? ? SING C1 C2 ? ? DOUB C2 O6 ? ? SING C4 OAP ? ? SING C2 OAP ? ? SING C21 H211 ? ? SING C21 H212 ? ? SING C21 H213 ? ? SING C20 H201 ? ? SING C20 H202 ? ? SING C19 H191 ? ? SING C19 H192 ? ? SING C18 H181 ? ? SING C18 H182 ? ? SING C17 H171 ? ? SING C17 H172 ? ? SING C16 H161 ? ? SING C16 H162 ? ? SING C15 H151 ? ? SING C15 H152 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING N7 H7 ? ? SING C1 H1 ? ? SING C5 H5C1 ? ? SING C5 H5C2 ? ? SING C4 H4C1 ? ? SING C4 H4C2 ? ? 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 $LasR-LBD 'Pseudomonas aeruginosa' 287 Bacteria . Pseudomonas aeruginosa 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 $LasR-LBD 'recombinant technology' 'E. coli' . . . . $OHN 'chemical synthesis' . . . . . 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 $LasR-LBD 1.5 mM '[U-2H; U-13C; U-15N]' $OHN 1.8 mM . 'sodium phosphate' 40 mM . 'sodium chloride' 0.15 M . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.14 0.01 M pH 6.4 0.1 pH temperature 303 0.1 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 TSP C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 $citation $citation TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1 $citation $citation TSP N 15 'methyl protons' ppm 0.0 external indirect . . . 0.101329118 $citation $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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'LasR-LBD dimer' _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 MET N N 119.100 0.05 1 2 . 1 MET H H 8.343 0.02 1 3 . 1 MET CA C 55.280 0.15 1 4 . 1 MET CB C 32.610 0.15 1 5 . 1 MET C C 175.610 0.15 1 6 . 2 ALA N N 127.787 0.05 1 7 . 2 ALA H H 8.535 0.02 1 8 . 2 ALA CA C 53.620 0.15 1 9 . 2 ALA CB C 18.210 0.15 1 10 . 2 ALA C C 178.930 0.15 1 11 . 3 LEU N N 119.298 0.05 1 12 . 3 LEU H H 8.179 0.02 1 13 . 3 LEU CA C 56.840 0.15 1 14 . 3 LEU CB C 42.150 0.15 1 15 . 3 LEU C C 177.720 0.15 1 16 . 4 VAL N N 113.699 0.05 1 17 . 4 VAL H H 7.111 0.02 1 18 . 4 VAL CA C 63.020 0.15 1 19 . 4 VAL CB C 31.630 0.15 1 20 . 4 VAL C C 176.680 0.15 1 21 . 5 ASP N N 121.375 0.05 1 22 . 5 ASP H H 7.759 0.02 1 23 . 5 ASP CA C 56.750 0.15 1 24 . 5 ASP CB C 40.270 0.15 1 25 . 5 ASP C C 178.450 0.15 1 26 . 6 GLY N N 107.005 0.05 1 27 . 6 GLY H H 7.832 0.02 1 28 . 6 GLY CA C 46.350 0.15 1 29 . 6 GLY C C 175.340 0.15 1 30 . 7 PHE N N 119.233 0.05 1 31 . 7 PHE H H 7.390 0.02 1 32 . 7 PHE CA C 58.220 0.15 1 33 . 7 PHE CB C 36.890 0.15 1 34 . 7 PHE C C 177.490 0.15 1 35 . 8 LEU N N 119.031 0.05 1 36 . 8 LEU H H 7.557 0.02 1 37 . 8 LEU CA C 57.300 0.15 1 38 . 8 LEU CB C 40.600 0.15 1 39 . 8 LEU C C 178.560 0.15 1 40 . 9 GLU N N 117.919 0.05 1 41 . 9 GLU H H 7.670 0.02 1 42 . 9 GLU CA C 58.960 0.15 1 43 . 9 GLU CB C 28.910 0.15 1 44 . 9 GLU C C 179.280 0.15 1 45 . 10 LEU N N 118.036 0.05 1 46 . 10 LEU H H 7.583 0.02 1 47 . 10 LEU CA C 58.040 0.15 1 48 . 10 LEU CB C 40.980 0.15 1 49 . 10 LEU C C 179.010 0.15 1 50 . 11 GLU N N 117.309 0.05 1 51 . 11 GLU H H 7.793 0.02 1 52 . 11 GLU CA C 58.500 0.15 1 53 . 11 GLU CB C 29.870 0.15 1 54 . 11 GLU C C 177.460 0.15 1 55 . 12 ARG N N 116.688 0.05 1 56 . 12 ARG H H 7.581 0.02 1 57 . 12 ARG CA C 56.070 0.15 1 58 . 12 ARG CB C 30.090 0.15 1 59 . 12 ARG C C 176.020 0.15 1 60 . 13 SER N N 116.656 0.05 1 61 . 13 SER H H 7.368 0.02 1 62 . 13 SER CA C 60.060 0.15 1 63 . 13 SER CB C 64.530 0.15 1 64 . 13 SER C C 174.350 0.15 1 65 . 14 SER CA C 58.550 0.15 1 66 . 14 SER CB C 63.760 0.15 1 67 . 14 SER C C 174.070 0.15 1 68 . 15 GLY N N 108.591 0.05 1 69 . 15 GLY H H 7.523 0.02 1 70 . 15 GLY CA C 44.500 0.15 1 71 . 15 GLY C C 172.470 0.15 1 72 . 16 LYS N N 120.690 0.05 1 73 . 16 LYS H H 8.676 0.02 1 74 . 16 LYS CA C 60.250 0.15 1 75 . 16 LYS CB C 32.620 0.15 1 76 . 16 LYS C C 177.880 0.15 1 77 . 17 LEU N N 121.240 0.05 1 78 . 17 LEU H H 8.481 0.02 1 79 . 17 LEU CA C 58.400 0.15 1 80 . 17 LEU CB C 40.200 0.15 1 81 . 17 LEU C C 179.680 0.15 1 82 . 18 GLU N N 122.333 0.05 1 83 . 18 GLU H H 8.476 0.02 1 84 . 18 GLU CA C 59.600 0.15 1 85 . 18 GLU CB C 29.310 0.15 1 86 . 18 GLU C C 177.820 0.15 1 87 . 19 TRP N N 121.170 0.05 1 88 . 19 TRP H H 8.438 0.02 1 89 . 19 TRP CA C 62.450 0.15 1 90 . 19 TRP CB C 29.590 0.15 1 91 . 19 TRP C C 177.050 0.15 1 92 . 20 SER N N 111.224 0.05 1 93 . 20 SER H H 8.348 0.02 1 94 . 20 SER CA C 61.070 0.15 1 95 . 20 SER CB C 62.980 0.15 1 96 . 20 SER C C 176.400 0.15 1 97 . 21 ALA N N 123.950 0.05 1 98 . 21 ALA H H 7.619 0.02 1 99 . 21 ALA CA C 54.900 0.15 1 100 . 21 ALA CB C 17.440 0.15 1 101 . 21 ALA C C 180.770 0.15 1 102 . 22 ILE N N 121.790 0.05 1 103 . 22 ILE H H 7.925 0.02 1 104 . 22 ILE CA C 64.300 0.15 1 105 . 22 ILE CB C 37.080 0.15 1 106 . 22 ILE C C 177.730 0.15 1 107 . 23 LEU N N 121.551 0.05 1 108 . 23 LEU H H 7.873 0.02 1 109 . 23 LEU CA C 57.940 0.15 1 110 . 23 LEU CB C 40.190 0.15 1 111 . 23 LEU C C 178.030 0.15 1 112 . 24 GLN N N 115.064 0.05 1 113 . 24 GLN H H 7.872 0.02 1 114 . 24 GLN CA C 59.360 0.15 1 115 . 24 GLN CB C 28.710 0.15 1 116 . 24 GLN C C 178.050 0.15 1 117 . 25 LYS N N 122.409 0.05 1 118 . 25 LYS H H 7.794 0.02 1 119 . 25 LYS CA C 58.870 0.15 1 120 . 25 LYS CB C 31.350 0.15 1 121 . 25 LYS C C 177.540 0.15 1 122 . 26 MET N N 118.600 0.05 1 123 . 26 MET H H 8.343 0.02 1 124 . 26 MET CA C 59.510 0.15 1 125 . 26 MET CB C 32.590 0.15 1 126 . 26 MET C C 178.860 0.15 1 127 . 27 ALA N N 119.186 0.05 1 128 . 27 ALA H H 7.852 0.02 1 129 . 27 ALA CA C 55.280 0.15 1 130 . 27 ALA CB C 18.210 0.15 1 131 . 27 ALA C C 179.070 0.15 1 132 . 28 SER N N 114.823 0.05 1 133 . 28 SER H H 8.211 0.02 1 134 . 28 SER CA C 61.170 0.15 1 135 . 28 SER CB C 62.370 0.15 1 136 . 28 SER C C 179.180 0.15 1 137 . 29 ASP N N 125.147 0.05 1 138 . 29 ASP H H 9.001 0.02 1 139 . 29 ASP CA C 57.020 0.15 1 140 . 29 ASP CB C 39.420 0.15 1 141 . 29 ASP C C 178.450 0.15 1 142 . 30 LEU N N 118.458 0.05 1 143 . 30 LEU H H 7.501 0.02 1 144 . 30 LEU CA C 55.920 0.15 1 145 . 30 LEU CB C 42.920 0.15 1 146 . 30 LEU C C 176.590 0.15 1 147 . 31 GLY N N 102.862 0.05 1 148 . 31 GLY H H 7.581 0.02 1 149 . 31 GLY CA C 44.510 0.15 1 150 . 31 GLY C C 174.460 0.15 1 151 . 32 PHE N N 119.256 0.05 1 152 . 32 PHE H H 8.012 0.02 1 153 . 32 PHE CA C 59.230 0.15 1 154 . 32 PHE CB C 39.040 0.15 1 155 . 32 PHE C C 174.360 0.15 1 156 . 33 SER N N 116.121 0.05 1 157 . 33 SER H H 8.640 0.02 1 158 . 33 SER CA C 59.230 0.15 1 159 . 33 SER CB C 63.220 0.15 1 160 . 33 SER C C 174.720 0.15 1 161 . 34 LYS N N 118.413 0.05 1 162 . 34 LYS H H 7.690 0.02 1 163 . 34 LYS CA C 53.530 0.15 1 164 . 34 LYS CB C 35.930 0.15 1 165 . 34 LYS C C 174.510 0.15 1 166 . 35 ILE N N 117.922 0.05 1 167 . 35 ILE H H 9.234 0.02 1 168 . 35 ILE CA C 57.760 0.15 1 169 . 35 ILE CB C 40.780 0.15 1 170 . 35 ILE C C 171.830 0.15 1 171 . 36 LEU N N 125.683 0.05 1 172 . 36 LEU H H 8.631 0.02 1 173 . 36 LEU CA C 54.720 0.15 1 174 . 36 LEU CB C 43.130 0.15 1 175 . 36 LEU C C 173.120 0.15 1 176 . 37 PHE N N 129.217 0.05 1 177 . 37 PHE H H 8.821 0.02 1 178 . 37 PHE CA C 56.200 0.15 1 179 . 37 PHE CB C 41.370 0.15 1 180 . 37 PHE C C 172.750 0.15 1 181 . 38 GLY N N 115.064 0.05 1 182 . 38 GLY H H 8.590 0.02 1 183 . 38 GLY CA C 43.780 0.15 1 184 . 38 GLY C C 171.400 0.15 1 185 . 39 LEU N N 124.141 0.05 1 186 . 39 LEU H H 9.243 0.02 1 187 . 39 LEU CA C 54.540 0.15 1 188 . 39 LEU CB C 48.380 0.15 1 189 . 39 LEU C C 173.680 0.15 1 190 . 40 LEU N N 127.576 0.05 1 191 . 40 LEU H H 9.432 0.02 1 192 . 40 LEU CA C 51.590 0.15 1 193 . 40 LEU CB C 44.490 0.15 1 194 . 40 LEU C C 174.140 0.15 1 195 . 41 PRO CA C 61.450 0.15 1 196 . 41 PRO CB C 31.150 0.15 1 197 . 41 PRO C C 175.030 0.15 1 198 . 42 LYS N N 118.220 0.05 1 199 . 42 LYS H H 7.848 0.02 1 200 . 42 LYS CA C 56.840 0.15 1 201 . 42 LYS CB C 32.120 0.15 1 202 . 42 LYS C C 175.880 0.15 1 203 . 43 ASP N N 118.869 0.05 1 204 . 43 ASP H H 8.406 0.02 1 205 . 43 ASP CA C 55.830 0.15 1 206 . 43 ASP CB C 39.030 0.15 1 207 . 43 ASP C C 174.600 0.15 1 208 . 44 SER N N 113.589 0.05 1 209 . 44 SER H H 7.460 0.02 1 210 . 44 SER CA C 57.400 0.15 1 211 . 44 SER CB C 63.750 0.15 1 212 . 44 SER C C 174.340 0.15 1 213 . 45 GLN N N 124.077 0.05 1 214 . 45 GLN H H 8.483 0.02 1 215 . 45 GLN CA C 54.070 0.15 1 216 . 45 GLN CB C 28.140 0.15 1 217 . 45 GLN C C 174.390 0.15 1 218 . 46 ASP N N 120.960 0.05 1 219 . 46 ASP H H 7.687 0.02 1 220 . 46 ASP CA C 52.340 0.15 1 221 . 46 ASP CB C 38.760 0.15 1 222 . 46 ASP C C 176.090 0.15 1 223 . 47 TYR N N 120.250 0.05 1 224 . 47 TYR H H 7.354 0.02 1 225 . 47 TYR CA C 60.340 0.15 1 226 . 47 TYR CB C 37.670 0.15 1 227 . 47 TYR C C 177.110 0.15 1 228 . 48 GLU N N 117.129 0.05 1 229 . 48 GLU H H 8.865 0.02 1 230 . 48 GLU CA C 58.960 0.15 1 231 . 48 GLU CB C 28.350 0.15 1 232 . 48 GLU C C 176.390 0.15 1 233 . 49 ASN N N 116.540 0.05 1 234 . 49 ASN H H 7.769 0.02 1 235 . 49 ASN CA C 52.330 0.15 1 236 . 49 ASN CB C 38.840 0.15 1 237 . 49 ASN C C 174.290 0.15 1 238 . 50 ALA N N 121.695 0.05 1 239 . 50 ALA H H 7.187 0.02 1 240 . 50 ALA CA C 52.420 0.15 1 241 . 50 ALA CB C 18.800 0.15 1 242 . 50 ALA C C 176.320 0.15 1 243 . 51 PHE N N 123.990 0.05 1 244 . 51 PHE H H 8.698 0.02 1 245 . 51 PHE CA C 57.580 0.15 1 246 . 51 PHE CB C 39.040 0.15 1 247 . 51 PHE C C 173.770 0.15 1 248 . 52 ILE N N 128.235 0.05 1 249 . 52 ILE H H 7.801 0.02 1 250 . 52 ILE CA C 59.690 0.15 1 251 . 52 ILE CB C 40.600 0.15 1 252 . 52 ILE C C 175.860 0.15 1 253 . 53 VAL N N 121.169 0.05 1 254 . 53 VAL H H 8.913 0.02 1 255 . 53 VAL CA C 59.050 0.15 1 256 . 53 VAL CB C 35.720 0.15 1 257 . 53 VAL C C 173.890 0.15 1 258 . 54 GLY N N 107.130 0.05 1 259 . 54 GLY H H 8.003 0.02 1 260 . 54 GLY CA C 44.140 0.15 1 261 . 54 GLY C C 172.550 0.15 1 262 . 55 ASN N N 117.810 0.05 1 263 . 55 ASN H H 8.621 0.02 1 264 . 55 ASN CA C 51.410 0.15 1 265 . 55 ASN CB C 38.200 0.15 1 266 . 55 ASN C C 176.660 0.15 1 267 . 56 TYR N N 120.559 0.05 1 268 . 56 TYR H H 8.159 0.02 1 269 . 56 TYR CA C 59.320 0.15 1 270 . 56 TYR CB C 37.250 0.15 1 271 . 56 TYR C C 177.760 0.15 1 272 . 57 PRO CA C 62.780 0.15 1 273 . 57 PRO CB C 31.240 0.15 1 274 . 57 PRO C C 177.940 0.15 1 275 . 58 ALA N N 129.876 0.05 1 276 . 58 ALA H H 8.827 0.02 1 277 . 58 ALA CA C 55.640 0.15 1 278 . 58 ALA CB C 17.990 0.15 1 279 . 58 ALA C C 180.050 0.15 1 280 . 59 ALA N N 118.868 0.05 1 281 . 59 ALA H H 8.964 0.02 1 282 . 59 ALA CA C 54.820 0.15 1 283 . 59 ALA CB C 17.630 0.15 1 284 . 59 ALA C C 180.930 0.15 1 285 . 60 TRP N N 118.377 0.05 1 286 . 60 TRP H H 6.965 0.02 1 287 . 60 TRP CA C 58.220 0.15 1 288 . 60 TRP CB C 30.280 0.15 1 289 . 60 TRP C C 176.130 0.15 1 290 . 61 ARG N N 117.853 0.05 1 291 . 61 ARG H H 7.902 0.02 1 292 . 61 ARG CA C 59.970 0.15 1 293 . 61 ARG CB C 29.110 0.15 1 294 . 61 ARG C C 177.100 0.15 1 295 . 62 GLU N N 116.025 0.05 1 296 . 62 GLU H H 7.953 0.02 1 297 . 62 GLU CA C 58.960 0.15 1 298 . 62 GLU C C 178.640 0.15 1 299 . 63 HIS N N 119.031 0.05 1 300 . 63 HIS H H 7.548 0.02 1 301 . 63 HIS CA C 58.130 0.15 1 302 . 63 HIS CB C 29.820 0.15 1 303 . 63 HIS C C 174.780 0.15 1 304 . 64 TYR N N 120.169 0.05 1 305 . 64 TYR H H 8.767 0.02 1 306 . 64 TYR CA C 59.600 0.15 1 307 . 64 TYR CB C 37.860 0.15 1 308 . 64 TYR C C 178.270 0.15 1 309 . 65 ASP N N 119.307 0.05 1 310 . 65 ASP H H 7.833 0.02 1 311 . 65 ASP CA C 57.120 0.15 1 312 . 65 ASP CB C 39.220 0.15 1 313 . 65 ASP C C 178.860 0.15 1 314 . 66 ARG N N 121.926 0.05 1 315 . 66 ARG H H 7.987 0.02 1 316 . 66 ARG CA C 58.870 0.15 1 317 . 66 ARG CB C 29.510 0.15 1 318 . 66 ARG C C 178.070 0.15 1 319 . 67 ALA N N 118.854 0.05 1 320 . 67 ALA H H 8.078 0.02 1 321 . 67 ALA CA C 51.410 0.15 1 322 . 67 ALA CB C 16.860 0.15 1 323 . 67 ALA C C 177.420 0.15 1 324 . 68 GLY N N 107.229 0.05 1 325 . 68 GLY H H 7.223 0.02 1 326 . 68 GLY CA C 46.440 0.15 1 327 . 68 GLY C C 177.760 0.15 1 328 . 69 TYR N N 117.140 0.05 1 329 . 69 TYR H H 7.865 0.02 1 330 . 69 TYR CA C 55.650 0.15 1 331 . 69 TYR CB C 33.400 0.15 1 332 . 69 TYR C C 177.000 0.15 1 333 . 70 ALA N N 126.960 0.05 1 334 . 70 ALA H H 9.233 0.02 1 335 . 70 ALA CA C 55.000 0.15 1 336 . 70 ALA CB C 17.800 0.15 1 337 . 70 ALA C C 177.420 0.15 1 338 . 71 ARG N N 109.600 0.05 1 339 . 71 ARG H H 7.020 0.02 1 340 . 71 ARG CA C 56.470 0.15 1 341 . 71 ARG CB C 29.510 0.15 1 342 . 71 ARG C C 175.600 0.15 1 343 . 72 VAL N N 117.045 0.05 1 344 . 72 VAL H H 7.089 0.02 1 345 . 72 VAL CA C 61.720 0.15 1 346 . 72 VAL CB C 34.170 0.15 1 347 . 72 VAL C C 173.810 0.15 1 348 . 73 ASP N N 120.130 0.05 1 349 . 73 ASP H H 7.393 0.02 1 350 . 73 ASP CA C 50.390 0.15 1 351 . 73 ASP CB C 41.580 0.15 1 352 . 73 ASP C C 175.740 0.15 1 353 . 74 PRO CA C 63.570 0.15 1 354 . 74 PRO CB C 31.810 0.15 1 355 . 74 PRO C C 179.110 0.15 1 356 . 75 THR N N 111.647 0.05 1 357 . 75 THR H H 8.516 0.02 1 358 . 75 THR CA C 65.400 0.15 1 359 . 75 THR CB C 67.840 0.15 1 360 . 75 THR C C 176.060 0.15 1 361 . 76 VAL N N 124.797 0.05 1 362 . 76 VAL H H 6.582 0.02 1 363 . 76 VAL CA C 66.500 0.15 1 364 . 76 VAL CB C 31.050 0.15 1 365 . 76 VAL C C 177.620 0.15 1 366 . 77 SER N N 112.530 0.05 1 367 . 77 SER H H 6.903 0.02 1 368 . 77 SER CA C 60.970 0.15 1 369 . 77 SER CB C 62.200 0.15 1 370 . 77 SER C C 178.680 0.15 1 371 . 78 HIS N N 121.080 0.05 1 372 . 78 HIS H H 7.577 0.02 1 373 . 78 HIS CA C 60.710 0.15 1 374 . 78 HIS CB C 31.250 0.15 1 375 . 78 HIS C C 177.200 0.15 1 376 . 79 CYS N N 115.274 0.05 1 377 . 79 CYS H H 7.464 0.02 1 378 . 79 CYS CA C 63.100 0.15 1 379 . 79 CYS CB C 27.170 0.15 1 380 . 79 CYS C C 175.250 0.15 1 381 . 80 THR N N 105.922 0.05 1 382 . 80 THR H H 7.327 0.02 1 383 . 80 THR CA C 63.650 0.15 1 384 . 80 THR CB C 69.590 0.15 1 385 . 80 THR C C 174.300 0.15 1 386 . 81 GLN N N 115.674 0.05 1 387 . 81 GLN H H 7.258 0.02 1 388 . 81 GLN CA C 54.820 0.15 1 389 . 81 GLN CB C 30.950 0.15 1 390 . 81 GLN C C 175.140 0.15 1 391 . 82 SER N N 114.359 0.05 1 392 . 82 SER H H 7.161 0.02 1 393 . 82 SER CA C 55.370 0.15 1 394 . 82 SER CB C 63.750 0.15 1 395 . 82 SER C C 173.240 0.15 1 396 . 83 VAL N N 113.268 0.05 1 397 . 83 VAL H H 7.330 0.02 1 398 . 83 VAL CA C 60.890 0.15 1 399 . 83 VAL CB C 31.450 0.15 1 400 . 83 VAL C C 175.060 0.15 1 401 . 84 LEU N N 122.685 0.05 1 402 . 84 LEU H H 8.754 0.02 1 403 . 84 LEU CA C 52.150 0.15 1 404 . 84 LEU CB C 39.630 0.15 1 405 . 84 LEU C C 174.030 0.15 1 406 . 85 PRO CA C 62.440 0.15 1 407 . 85 PRO CB C 31.640 0.15 1 408 . 85 PRO C C 175.130 0.15 1 409 . 86 ILE N N 117.627 0.05 1 410 . 86 ILE H H 8.255 0.02 1 411 . 86 ILE CA C 58.040 0.15 1 412 . 86 ILE CB C 39.720 0.15 1 413 . 86 ILE C C 173.660 0.15 1 414 . 87 PHE N N 127.635 0.05 1 415 . 87 PHE H H 8.381 0.02 1 416 . 87 PHE CA C 57.390 0.15 1 417 . 87 PHE CB C 39.220 0.15 1 418 . 87 PHE C C 177.240 0.15 1 419 . 88 TRP N N 124.260 0.05 1 420 . 88 TRP H H 8.676 0.02 1 421 . 88 TRP CA C 54.720 0.15 1 422 . 88 TRP CB C 26.770 0.15 1 423 . 88 TRP C C 175.650 0.15 1 424 . 89 GLU N N 124.800 0.05 1 425 . 89 GLU H H 7.628 0.02 1 426 . 89 GLU CA C 53.900 0.15 1 427 . 89 GLU CB C 30.080 0.15 1 428 . 89 GLU C C 174.140 0.15 1 429 . 90 PRO CA C 65.490 0.15 1 430 . 90 PRO CB C 31.220 0.15 1 431 . 90 PRO C C 177.830 0.15 1 432 . 91 SER N N 109.218 0.05 1 433 . 91 SER H H 7.826 0.02 1 434 . 91 SER CA C 60.060 0.15 1 435 . 91 SER CB C 62.200 0.15 1 436 . 91 SER C C 175.890 0.15 1 437 . 92 ILE N N 114.938 0.05 1 438 . 92 ILE H H 7.570 0.02 1 439 . 92 ILE CA C 62.550 0.15 1 440 . 92 ILE CB C 37.090 0.15 1 441 . 92 ILE C C 175.230 0.15 1 442 . 93 TYR N N 122.006 0.05 1 443 . 93 TYR H H 7.194 0.02 1 444 . 93 TYR CA C 56.750 0.15 1 445 . 93 TYR CB C 35.320 0.15 1 446 . 93 TYR C C 174.000 0.15 1 447 . 94 GLN N N 120.834 0.05 1 448 . 94 GLN H H 7.816 0.02 1 449 . 94 GLN CA C 57.760 0.15 1 450 . 94 GLN CB C 31.050 0.15 1 451 . 94 GLN C C 177.000 0.15 1 452 . 95 THR N N 110.619 0.05 1 453 . 95 THR H H 7.963 0.02 1 454 . 95 THR CA C 60.340 0.15 1 455 . 95 THR CB C 70.780 0.15 1 456 . 95 THR C C 175.070 0.15 1 457 . 97 LYS CA C 58.250 0.15 1 458 . 97 LYS CB C 31.150 0.15 1 459 . 97 LYS C C 179.800 0.15 1 460 . 98 GLN N N 118.300 0.05 1 461 . 98 GLN H H 7.848 0.02 1 462 . 98 GLN CA C 58.950 0.15 1 463 . 98 GLN CB C 27.360 0.15 1 464 . 98 GLN C C 178.080 0.15 1 465 . 99 HIS N N 121.129 0.05 1 466 . 99 HIS H H 8.719 0.02 1 467 . 99 HIS CA C 60.060 0.15 1 468 . 99 HIS CB C 28.330 0.15 1 469 . 99 HIS C C 177.070 0.15 1 470 . 100 GLU N N 121.241 0.05 1 471 . 100 GLU H H 7.993 0.02 1 472 . 100 GLU CA C 59.510 0.15 1 473 . 100 GLU CB C 28.920 0.15 1 474 . 100 GLU C C 178.550 0.15 1 475 . 101 PHE N N 120.217 0.05 1 476 . 101 PHE H H 7.925 0.02 1 477 . 101 PHE CA C 61.080 0.15 1 478 . 101 PHE CB C 38.250 0.15 1 479 . 101 PHE C C 175.380 0.15 1 480 . 102 PHE N N 120.559 0.05 1 481 . 102 PHE H H 8.159 0.02 1 482 . 102 PHE CA C 55.920 0.15 1 483 . 102 PHE CB C 35.240 0.15 1 484 . 102 PHE C C 177.720 0.15 1 485 . 103 GLU CA C 59.210 0.15 1 486 . 103 GLU CB C 28.400 0.15 1 487 . 103 GLU C C 179.500 0.15 1 488 . 104 GLU N N 120.690 0.05 1 489 . 104 GLU H H 7.577 0.02 1 490 . 104 GLU CA C 59.330 0.15 1 491 . 104 GLU CB C 29.110 0.15 1 492 . 104 GLU C C 178.410 0.15 1 493 . 105 ALA N N 125.611 0.05 1 494 . 105 ALA H H 8.526 0.02 1 495 . 105 ALA CA C 54.140 0.15 1 496 . 105 ALA CB C 16.260 0.15 1 497 . 105 ALA C C 179.800 0.15 1 498 . 106 SER N N 113.421 0.05 1 499 . 106 SER H H 7.802 0.02 1 500 . 106 SER CA C 61.170 0.15 1 501 . 106 SER CB C 62.210 0.15 1 502 . 106 SER C C 177.760 0.15 1 503 . 107 ALA N N 126.151 0.05 1 504 . 107 ALA H H 7.135 0.02 1 505 . 107 ALA CA C 54.160 0.15 1 506 . 107 ALA CB C 17.030 0.15 1 507 . 107 ALA C C 178.370 0.15 1 508 . 108 ALA N N 119.450 0.05 1 509 . 108 ALA H H 6.820 0.02 1 510 . 108 ALA CA C 51.660 0.15 1 511 . 108 ALA CB C 17.430 0.15 1 512 . 108 ALA C C 176.370 0.15 1 513 . 109 GLY N N 105.304 0.05 1 514 . 109 GLY H H 7.310 0.02 1 515 . 109 GLY CA C 44.460 0.15 1 516 . 109 GLY C C 173.800 0.15 1 517 . 110 LEU N N 125.889 0.05 1 518 . 110 LEU H H 7.496 0.02 1 519 . 110 LEU CA C 52.980 0.15 1 520 . 110 LEU CB C 38.650 0.15 1 521 . 110 LEU C C 172.840 0.15 1 522 . 111 VAL N N 120.309 0.05 1 523 . 111 VAL H H 7.085 0.02 1 524 . 111 VAL CA C 64.390 0.15 1 525 . 111 VAL CB C 33.780 0.15 1 526 . 111 VAL C C 175.950 0.15 1 527 . 112 TYR N N 119.598 0.05 1 528 . 112 TYR H H 8.496 0.02 1 529 . 112 TYR CA C 54.630 0.15 1 530 . 112 TYR CB C 39.620 0.15 1 531 . 112 TYR C C 175.650 0.15 1 532 . 113 GLY N N 112.337 0.05 1 533 . 113 GLY H H 8.762 0.02 1 534 . 113 GLY CA C 45.890 0.15 1 535 . 113 GLY C C 169.200 0.15 1 536 . 114 LEU N N 116.420 0.05 1 537 . 114 LEU H H 7.666 0.02 1 538 . 114 LEU CA C 54.000 0.15 1 539 . 114 LEU CB C 42.930 0.15 1 540 . 114 LEU C C 173.500 0.15 1 541 . 115 THR N N 115.612 0.05 1 542 . 115 THR H H 8.452 0.02 1 543 . 115 THR CA C 62.360 0.15 1 544 . 115 THR CB C 72.120 0.15 1 545 . 115 THR C C 172.760 0.15 1 546 . 116 MET N N 126.967 0.05 1 547 . 116 MET H H 9.487 0.02 1 548 . 116 MET CA C 50.490 0.15 1 549 . 116 MET CB C 32.220 0.15 1 550 . 116 MET C C 172.550 0.15 1 551 . 118 LEU CA C 52.440 0.15 1 552 . 118 LEU CB C 41.990 0.15 1 553 . 118 LEU C C 174.940 0.15 1 554 . 119 HIS N N 121.104 0.05 1 555 . 119 HIS H H 7.982 0.02 1 556 . 119 HIS CA C 54.450 0.15 1 557 . 119 HIS CB C 29.000 0.15 1 558 . 119 HIS C C 173.900 0.15 1 559 . 120 GLY N N 108.343 0.05 1 560 . 120 GLY H H 8.617 0.02 1 561 . 120 GLY CA C 44.420 0.15 1 562 . 120 GLY C C 175.060 0.15 1 563 . 121 ALA N N 121.279 0.05 1 564 . 121 ALA H H 8.987 0.02 1 565 . 121 ALA CA C 53.340 0.15 1 566 . 121 ALA CB C 17.810 0.15 1 567 . 121 ALA C C 177.660 0.15 1 568 . 122 ARG N N 116.559 0.05 1 569 . 122 ARG H H 8.787 0.02 1 570 . 122 ARG CA C 54.170 0.15 1 571 . 122 ARG CB C 27.760 0.15 1 572 . 122 ARG C C 176.610 0.15 1 573 . 123 GLY N N 107.251 0.05 1 574 . 123 GLY H H 7.309 0.02 1 575 . 123 GLY CA C 45.250 0.15 1 576 . 123 GLY C C 173.570 0.15 1 577 . 124 GLU N N 121.774 0.05 1 578 . 124 GLU H H 10.128 0.02 1 579 . 124 GLU CA C 58.500 0.15 1 580 . 124 GLU CB C 28.730 0.15 1 581 . 124 GLU C C 175.970 0.15 1 582 . 125 LEU N N 127.446 0.05 1 583 . 125 LEU H H 8.192 0.02 1 584 . 125 LEU CA C 53.190 0.15 1 585 . 125 LEU CB C 44.280 0.15 1 586 . 125 LEU C C 174.510 0.15 1 587 . 126 GLY N N 113.447 0.05 1 588 . 126 GLY H H 8.909 0.02 1 589 . 126 GLY CA C 46.440 0.15 1 590 . 126 GLY C C 170.350 0.15 1 591 . 127 ALA N N 121.410 0.05 1 592 . 127 ALA H H 8.519 0.02 1 593 . 127 ALA CA C 50.770 0.15 1 594 . 127 ALA CB C 22.700 0.15 1 595 . 127 ALA C C 174.120 0.15 1 596 . 128 LEU N N 122.748 0.05 1 597 . 128 LEU H H 8.563 0.02 1 598 . 128 LEU CA C 53.350 0.15 1 599 . 128 LEU CB C 43.710 0.15 1 600 . 128 LEU C C 174.520 0.15 1 601 . 129 SER N N 126.197 0.05 1 602 . 129 SER H H 9.831 0.02 1 603 . 129 SER CA C 56.650 0.15 1 604 . 129 SER CB C 67.230 0.15 1 605 . 129 SER C C 172.470 0.15 1 606 . 130 LEU CA C 53.680 0.15 1 607 . 130 LEU CB C 45.070 0.15 1 608 . 130 LEU C C 173.710 0.15 1 609 . 131 SER N N 114.152 0.05 1 610 . 131 SER H H 8.906 0.02 1 611 . 131 SER CA C 55.460 0.15 1 612 . 131 SER CB C 66.090 0.15 1 613 . 131 SER C C 173.690 0.15 1 614 . 132 VAL N N 123.702 0.05 1 615 . 132 VAL H H 8.186 0.02 1 616 . 132 VAL CA C 58.960 0.15 1 617 . 132 VAL CB C 35.720 0.15 1 618 . 132 VAL C C 173.680 0.15 1 619 . 133 GLU N N 127.014 0.05 1 620 . 133 GLU H H 8.335 0.02 1 621 . 133 GLU CA C 55.090 0.15 1 622 . 133 GLU CB C 28.910 0.15 1 623 . 133 GLU C C 174.900 0.15 1 624 . 134 ALA N N 124.654 0.05 1 625 . 134 ALA H H 7.963 0.02 1 626 . 134 ALA CA C 50.760 0.15 1 627 . 134 ALA CB C 22.300 0.15 1 628 . 134 ALA C C 175.980 0.15 1 629 . 135 GLU N N 117.672 0.05 1 630 . 135 GLU H H 8.872 0.02 1 631 . 135 GLU CA C 57.670 0.15 1 632 . 135 GLU CB C 30.360 0.15 1 633 . 135 GLU C C 176.300 0.15 1 634 . 136 ASN N N 108.431 0.05 1 635 . 136 ASN H H 7.045 0.02 1 636 . 136 ASN CA C 51.690 0.15 1 637 . 136 ASN CB C 39.610 0.15 1 638 . 136 ASN C C 173.770 0.15 1 639 . 137 ARG N N 120.550 0.05 1 640 . 137 ARG H H 8.667 0.02 1 641 . 137 ARG CA C 59.140 0.15 1 642 . 137 ARG CB C 29.890 0.15 1 643 . 137 ARG C C 176.710 0.15 1 644 . 138 ALA N N 122.638 0.05 1 645 . 138 ALA H H 8.139 0.02 1 646 . 138 ALA CA C 55.180 0.15 1 647 . 138 ALA CB C 17.040 0.15 1 648 . 138 ALA C C 181.140 0.15 1 649 . 139 GLU N N 118.877 0.05 1 650 . 139 GLU H H 8.243 0.02 1 651 . 139 GLU CA C 58.410 0.15 1 652 . 139 GLU CB C 29.120 0.15 1 653 . 139 GLU C C 179.160 0.15 1 654 . 140 ALA N N 122.899 0.05 1 655 . 140 ALA H H 7.521 0.02 1 656 . 140 ALA CA C 55.180 0.15 1 657 . 140 ALA CB C 17.240 0.15 1 658 . 140 ALA C C 178.800 0.15 1 659 . 141 ASN N N 117.910 0.05 1 660 . 141 ASN H H 8.602 0.02 1 661 . 141 ASN CA C 56.010 0.15 1 662 . 141 ASN CB C 37.280 0.15 1 663 . 141 ASN C C 177.480 0.15 1 664 . 142 ARG N N 121.510 0.05 1 665 . 142 ARG H H 7.925 0.02 1 666 . 142 ARG CA C 59.330 0.15 1 667 . 142 ARG CB C 29.630 0.15 1 668 . 142 ARG C C 179.350 0.15 1 669 . 143 PHE N N 119.814 0.05 1 670 . 143 PHE H H 7.881 0.02 1 671 . 143 PHE CA C 60.710 0.15 1 672 . 143 PHE CB C 37.840 0.15 1 673 . 143 PHE C C 178.350 0.15 1 674 . 144 MET N N 119.435 0.05 1 675 . 144 MET H H 8.669 0.02 1 676 . 144 MET CA C 60.710 0.15 1 677 . 144 MET CB C 34.020 0.15 1 678 . 144 MET C C 177.310 0.15 1 679 . 145 GLU N N 116.562 0.05 1 680 . 145 GLU H H 8.345 0.02 1 681 . 145 GLU CA C 59.880 0.15 1 682 . 145 GLU CB C 29.120 0.15 1 683 . 145 GLU C C 178.340 0.15 1 684 . 146 SER N N 113.154 0.05 1 685 . 146 SER H H 7.351 0.02 1 686 . 146 SER CA C 61.170 0.15 1 687 . 146 SER CB C 62.970 0.15 1 688 . 146 SER C C 175.230 0.15 1 689 . 147 VAL N N 112.730 0.05 1 690 . 147 VAL H H 6.868 0.02 1 691 . 147 VAL CA C 60.380 0.15 1 692 . 147 VAL CB C 32.680 0.15 1 693 . 147 VAL C C 176.060 0.15 1 694 . 148 LEU N N 125.673 0.05 1 695 . 148 LEU H H 7.467 0.02 1 696 . 148 LEU CA C 59.440 0.15 1 697 . 148 LEU CB C 39.810 0.15 1 698 . 148 LEU C C 174.100 0.15 1 699 . 149 PRO CA C 66.490 0.15 1 700 . 149 PRO CB C 30.650 0.15 1 701 . 149 PRO C C 177.850 0.15 1 702 . 150 THR N N 110.912 0.05 1 703 . 150 THR H H 7.050 0.02 1 704 . 150 THR CA C 66.510 0.15 1 705 . 150 THR CB C 68.120 0.15 1 706 . 150 THR C C 176.480 0.15 1 707 . 151 LEU N N 121.614 0.05 1 708 . 151 LEU H H 8.188 0.02 1 709 . 151 LEU CA C 56.940 0.15 1 710 . 151 LEU CB C 41.380 0.15 1 711 . 151 LEU C C 176.560 0.15 1 712 . 152 TRP N N 122.921 0.05 1 713 . 152 TRP H H 8.650 0.02 1 714 . 152 TRP CA C 61.620 0.15 1 715 . 152 TRP CB C 27.360 0.15 1 716 . 152 TRP C C 176.960 0.15 1 717 . 153 MET N N 111.481 0.05 1 718 . 153 MET H H 6.533 0.02 1 719 . 153 MET CA C 57.570 0.15 1 720 . 153 MET CB C 33.390 0.15 1 721 . 153 MET C C 177.720 0.15 1 722 . 154 LEU N N 119.239 0.05 1 723 . 154 LEU H H 7.755 0.02 1 724 . 154 LEU CA C 58.220 0.15 1 725 . 154 LEU CB C 41.160 0.15 1 726 . 154 LEU C C 178.140 0.15 1 727 . 155 LYS N N 116.222 0.05 1 728 . 155 LYS H H 8.427 0.02 1 729 . 155 LYS CA C 59.420 0.15 1 730 . 155 LYS CB C 29.110 0.15 1 731 . 155 LYS C C 176.690 0.15 1 732 . 156 ASP N N 119.690 0.05 1 733 . 156 ASP H H 6.865 0.02 1 734 . 156 ASP CA C 57.580 0.15 1 735 . 156 ASP CB C 40.200 0.15 1 736 . 156 ASP C C 178.350 0.15 1 737 . 157 TYR N N 120.108 0.05 1 738 . 157 TYR H H 7.884 0.02 1 739 . 157 TYR CA C 63.930 0.15 1 740 . 157 TYR CB C 38.070 0.15 1 741 . 157 TYR C C 180.710 0.15 1 742 . 158 ALA N N 124.212 0.05 1 743 . 158 ALA H H 9.537 0.02 1 744 . 158 ALA CA C 55.090 0.15 1 745 . 158 ALA CB C 17.070 0.15 1 746 . 158 ALA C C 178.130 0.15 1 747 . 159 LEU N N 120.125 0.05 1 748 . 159 LEU H H 8.219 0.02 1 749 . 159 LEU CA C 58.600 0.15 1 750 . 159 LEU CB C 41.560 0.15 1 751 . 159 LEU C C 176.690 0.15 1 752 . 160 GLN N N 117.336 0.05 1 753 . 160 GLN H H 8.372 0.02 1 754 . 160 GLN CA C 58.780 0.15 1 755 . 160 GLN CB C 27.370 0.15 1 756 . 160 GLN C C 178.350 0.15 1 757 . 161 SER N N 109.830 0.05 1 758 . 161 SER H H 7.729 0.02 1 759 . 161 SER CA C 59.690 0.15 1 760 . 161 SER CB C 62.970 0.15 1 761 . 161 SER C C 177.210 0.15 1 762 . 162 GLY N N 115.459 0.05 1 763 . 162 GLY H H 8.884 0.02 1 764 . 162 GLY CA C 46.440 0.15 1 765 . 162 GLY C C 174.800 0.15 1 766 . 163 ALA N N 121.758 0.05 1 767 . 163 ALA H H 8.441 0.02 1 768 . 163 ALA CA C 54.910 0.15 1 769 . 163 ALA CB C 17.060 0.15 1 770 . 163 ALA C C 179.380 0.15 1 771 . 164 GLY N N 103.060 0.05 1 772 . 164 GLY H H 6.981 0.02 1 773 . 164 GLY CA C 45.790 0.15 1 774 . 164 GLY C C 174.210 0.15 1 775 . 165 LEU N N 118.378 0.05 1 776 . 165 LEU H H 6.697 0.02 1 777 . 165 LEU CA C 54.990 0.15 1 778 . 165 LEU CB C 42.340 0.15 1 779 . 165 LEU C C 177.730 0.15 1 780 . 166 ALA N N 120.138 0.05 1 781 . 166 ALA H H 7.200 0.02 1 782 . 166 ALA CA C 54.170 0.15 1 783 . 166 ALA CB C 17.430 0.15 1 784 . 166 ALA C C 177.360 0.15 1 785 . 167 PHE N N 113.528 0.05 1 786 . 167 PHE H H 7.210 0.02 1 787 . 167 PHE CA C 54.810 0.15 1 788 . 167 PHE CB C 39.230 0.15 1 789 . 167 PHE C C 175.140 0.15 1 790 . 168 GLU N N 121.375 0.05 1 791 . 168 GLU H H 7.759 0.02 1 792 . 168 GLU CA C 56.200 0.15 1 793 . 168 GLU CB C 29.770 0.15 1 794 . 168 GLU C C 174.930 0.15 1 795 . 169 HIS N N 120.167 0.05 1 796 . 169 HIS H H 8.099 0.02 1 797 . 169 HIS CA C 53.810 0.15 1 798 . 169 HIS CB C 31.250 0.15 1 799 . 169 HIS C C 173.150 0.15 1 800 . 170 PRO CA C 62.790 0.15 1 801 . 170 PRO CB C 31.430 0.15 1 802 . 170 PRO C C 176.760 0.15 1 803 . 171 VAL N N 120.878 0.05 1 804 . 171 VAL H H 8.225 0.02 1 805 . 171 VAL CA C 62.090 0.15 1 806 . 171 VAL CB C 32.420 0.15 1 807 . 171 VAL C C 176.000 0.15 1 808 . 172 SER N N 120.418 0.05 1 809 . 172 SER H H 8.268 0.02 1 810 . 172 SER CA C 58.110 0.15 1 811 . 172 SER CB C 63.500 0.15 1 812 . 172 SER C C 173.180 0.15 1 813 . 173 LYS N N 128.963 0.05 1 814 . 173 LYS H H 7.898 0.02 1 815 . 173 LYS CA C 57.590 0.15 1 816 . 173 LYS CB C 33.000 0.15 1 817 . 173 LYS C C 180.980 0.15 1 stop_ save_