data_17695 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignments of the Extracellular domain of GLIC, a prokaryotic nAChR homologue ; _BMRB_accession_number 17695 _BMRB_flat_file_name bmr17695.str _Entry_type original _Submission_date 2011-06-09 _Accession_date 2011-06-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'GLIC ECD (193 a.a) recombionant polypeptide expressed in E.coli studied through NMR spectroscopy' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chasapis Christos T. . 2 Argyriou Aikaterini I. . 3 Corringer Pierre-Jean . . 4 Bentrop Detlef T. . 5 Spyroulias Georgios A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 144 "13C chemical shifts" 354 "15N chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-01-04 original author . stop_ _Original_release_date 2012-01-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Unravelling the conformational plasticity of the extracellular domain of a prokaryotic nAChR homologue in solution by NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22007668 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chasapis Christos T. . 2 Argyriou Aikaterini I. . 3 Corringer Pierre-Jean . . 4 Bentrop Detlef T. . 5 Spyroulias Georgios A. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 50 _Journal_issue 45 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9681 _Page_last 9683 _Year 2011 _Details . loop_ _Keyword 'conformational exchange' 'Cys-loop receptors' 'Gloeobacter violaceus' 'nAChR prokaryotic homologue' 'NMR spectroscopy' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Extracellular domain of GLIC' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GLIC ECD' $GLIC_ECD stop_ _System_molecular_weight 22079.9 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'monomer in solution' save_ ######################## # Monomeric polymers # ######################## save_GLIC_ECD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GLIC_ECD _Molecular_mass 22079.9 _Mol_thiol_state 'all free' loop_ _Biological_function 'Ligand-gated ion Channel (LGIC)' 'Membrane and transport protein' stop_ _Details 'Four hydrophobic residues FRRYPF in the Cys loop were substituted by the corresponding hydrophilic GRRTES' ############################## # Polymer residue sequence # ############################## _Residue_count 195 _Mol_residue_sequence ; MQDMVSPPPPIADEPLTVNT GIYLIECYSLDDKAETFKVN AFLSLSWKDRRLAFDPVRSG VRVKTYEPEAIWIPEIRFVN VENARDADVVDISVSPDGTV QYLERFSARVLSPLDGRRTE SDSQTLHIYLIVRSVDTRNI VLAVDLEKVGKNDDVFLTGW DIESFTAVVKPANFALEDRL ESKLDYQLRISRQGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ASP 4 MET 5 VAL 6 SER 7 PRO 8 PRO 9 PRO 10 PRO 11 ILE 12 ALA 13 ASP 14 GLU 15 PRO 16 LEU 17 THR 18 VAL 19 ASN 20 THR 21 GLY 22 ILE 23 TYR 24 LEU 25 ILE 26 GLU 27 CYS 28 TYR 29 SER 30 LEU 31 ASP 32 ASP 33 LYS 34 ALA 35 GLU 36 THR 37 PHE 38 LYS 39 VAL 40 ASN 41 ALA 42 PHE 43 LEU 44 SER 45 LEU 46 SER 47 TRP 48 LYS 49 ASP 50 ARG 51 ARG 52 LEU 53 ALA 54 PHE 55 ASP 56 PRO 57 VAL 58 ARG 59 SER 60 GLY 61 VAL 62 ARG 63 VAL 64 LYS 65 THR 66 TYR 67 GLU 68 PRO 69 GLU 70 ALA 71 ILE 72 TRP 73 ILE 74 PRO 75 GLU 76 ILE 77 ARG 78 PHE 79 VAL 80 ASN 81 VAL 82 GLU 83 ASN 84 ALA 85 ARG 86 ASP 87 ALA 88 ASP 89 VAL 90 VAL 91 ASP 92 ILE 93 SER 94 VAL 95 SER 96 PRO 97 ASP 98 GLY 99 THR 100 VAL 101 GLN 102 TYR 103 LEU 104 GLU 105 ARG 106 PHE 107 SER 108 ALA 109 ARG 110 VAL 111 LEU 112 SER 113 PRO 114 LEU 115 ASP 116 GLY 117 ARG 118 ARG 119 THR 120 GLU 121 SER 122 ASP 123 SER 124 GLN 125 THR 126 LEU 127 HIS 128 ILE 129 TYR 130 LEU 131 ILE 132 VAL 133 ARG 134 SER 135 VAL 136 ASP 137 THR 138 ARG 139 ASN 140 ILE 141 VAL 142 LEU 143 ALA 144 VAL 145 ASP 146 LEU 147 GLU 148 LYS 149 VAL 150 GLY 151 LYS 152 ASN 153 ASP 154 ASP 155 VAL 156 PHE 157 LEU 158 THR 159 GLY 160 TRP 161 ASP 162 ILE 163 GLU 164 SER 165 PHE 166 THR 167 ALA 168 VAL 169 VAL 170 LYS 171 PRO 172 ALA 173 ASN 174 PHE 175 ALA 176 LEU 177 GLU 178 ASP 179 ARG 180 LEU 181 GLU 182 SER 183 LYS 184 LEU 185 ASP 186 TYR 187 GLN 188 LEU 189 ARG 190 ILE 191 SER 192 ARG 193 GLN 194 GLY 195 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 2XQ3 "Pentameric Ligand Gated Ion Channel Glic In Complex With Br-Lidocaine" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ4 "Pentameric Ligand Gated Ion Channel Glic In Complex With Tetramethylarsonium (Tmas)" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ5 "Pentameric Ligand Gated Ion Channel Glic In Complex With Tetraethylarsonium (Teas)" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ6 "Pentameric Ligand Gated Ion Channel Glic In Complex With Cesium Ion (Cs+)" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ7 "Pentameric Ligand Gated Ion Channel Glic In Complex With Cadmium Ion (Cd2+)" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ8 "Pentameric Ligand Gated Ion Channel Glic In Complex With Zinc Ion (Zn2+)" 98.46 317 97.92 97.92 5.93e-130 PDB 2XQ9 "Pentameric Ligand Gated Ion Channel Glic Mutant E221a In Complex With Tetraethylarsonium (Teas)" 98.46 317 97.92 97.92 7.46e-130 PDB 2XQA "Pentameric Ligand Gated Ion Channel Glic In Complex With Tetrabutylantimony (Tbsb)" 98.46 317 97.92 97.92 5.93e-130 PDB 3EAM "An Open-Pore Structure Of A Bacterial Pentameric Ligand- Gated Ion Channel" 98.46 317 97.92 97.92 4.52e-130 PDB 3EHZ "X-Ray Structure Of The Pentameric Ligand Gated Ion Channel Of Gloebacter Violaceus (Glic) In A Presumptive Open Conformation" 98.46 317 97.92 97.92 5.93e-130 PDB 3EI0 "Structure Of The E221a Mutant Of The Gloebacter Violaceus Pentameric Ligand Gated Ion Channnel (Glic)" 98.46 317 97.92 97.92 4.47e-130 PDB 3IGQ "Crystal Structure Of The Extracellular Domain Of A Bacterial Pentameric Ligand-gated Ion Channel" 99.49 201 100.00 100.00 9.04e-137 PDB 3LSV "Structure Of The A237f Mutant Of The Pentameric Ligand Gated Channel From Gloeobacter Violaceus" 98.46 317 97.92 97.92 4.09e-130 PDB 3P4W "Structure Of Desflurane Bound To A Pentameric Ligand-Gated Ion Channel, Glic" 98.46 318 97.92 97.92 5.38e-130 PDB 3P50 "Structure Of Propofol Bound To A Pentameric Ligand-Gated Ion Channel, Glic" 98.46 318 97.92 97.92 5.38e-130 PDB 3TLS "The Glic Pentameric Ligand-Gated Ion Channel E19'p Mutant In A Locally-Closed Conformation (Lc2 Subtype)" 98.46 321 97.92 97.92 5.06e-130 PDB 3TLT "The Glic Pentameric Ligand-Gated Ion Channel H11'f Mutant In A Locally-Closed Conformation (Lc1 Subtype)" 98.46 321 97.92 97.92 4.44e-130 PDB 4F8H "X-Ray Structure Of The Anesthetic Ketamine Bound To The Glic Pentameric Ligand-Gated Ion Channel" 98.46 317 97.92 97.92 5.93e-130 PDB 4HFB "The Glic Pentameric Ligand-gated Ion Channel F14'a Ethanol-sensitive Mutant (apo)" 98.46 317 97.92 97.92 4.42e-130 PDB 4HFC "The Glic Pentameric Ligand-gated Ion Channel F14'a Ethanol-sensitive Mutant Complexed To 2-bromo-ethanol" 98.46 317 97.92 97.92 4.42e-130 PDB 4HFD "The Glic Pentameric Ligand-gated Ion Channel F14'a Ethanol-sensitive Mutant Complexed To Bromoform" 98.46 317 97.92 97.92 4.42e-130 PDB 4HFE "The Glic Pentameric Ligand-gated Ion Channel F14'a Ethanol-sensitive Mutant Complexed To Ethanol" 98.46 317 97.92 97.92 4.42e-130 PDB 4HFH "The Glic Pentameric Ligand-gated Ion Channel (wild-type) Complexed To Bromoform" 98.46 317 97.92 97.92 4.52e-130 PDB 4HFI "The Glic Pentameric Ligand-gated Ion Channel At 2.4 A Resolution" 98.46 317 97.92 97.92 4.52e-130 PDB 4IL4 "The Pentameric Ligand-gated Ion Channel Glic In Complex With Se-ddm" 98.46 317 97.92 97.92 4.52e-130 PDB 4IL9 "The Pentameric Ligand-gated Ion Channel Glic A237f In Complex With Bromide" 98.46 320 97.92 97.92 3.81e-130 PDB 4ILA "The Pentameric Ligand-gated Ion Channel Glic A237f In Complex With Cesium" 98.46 320 97.92 97.92 3.81e-130 PDB 4ILB "The Pentameric Ligand-gated Ion Channel Glic A237f In Complex With Rubidium" 98.46 320 97.92 97.92 3.81e-130 PDB 4ILC "The Glic Pentameric Ligand-gated Ion Channel In Complex With Sulfates" 98.46 320 97.92 97.92 4.29e-130 PDB 4LMJ "Glic Liganded-closed-channel Conformation, Mutant T25'a" 98.46 318 97.92 97.92 6.21e-130 PDB 4LMK "Glic Liganded-closed-channel Conformation, Mutant Y27'a" 98.46 318 97.92 97.92 5.50e-130 PDB 4LML "Glic Double Mutant I9'a T25'a" 98.46 318 97.92 97.92 4.14e-130 PDB 4NPP "The Glic-his10 Wild-type Structure In Equilibrium Between The Open And Locally-closed (lc) Forms" 98.46 329 97.92 97.92 3.16e-130 PDB 4NPQ "The Resting-state Conformation Of The Glic Ligand-gated Ion Channel" 98.46 318 97.92 97.92 5.38e-130 PDB 4QH1 "The Glic Pentameric Ligand-gated Ion Channel (wild-type) In Complex With Bromoacetate" 98.46 316 97.92 97.92 4.98e-130 PDB 4QH4 "The Glic Pentameric Ligand-gated Ion Channel (wild-type) Crystallized In Acetate Buffer At Ph3" 98.46 316 97.92 97.92 4.98e-130 PDB 4QH5 "The Glic Pentameric Ligand-gated Ion Channel (wild-type) Crystallized In Phosphate Buffer" 98.46 316 97.92 97.92 4.98e-130 PDB 4X5T "Alpha 1 Glycine Receptor Transmembrane Structure Fused To The Extracellular Domain Of Glic" 99.49 330 97.42 97.42 3.13e-130 DBJ BAC92138 "glr4197 [Gloeobacter violaceus PCC 7421]" 98.46 359 97.92 97.92 4.26e-129 REF NP_927143 "hypothetical protein glr4197 [Gloeobacter violaceus PCC 7421]" 98.46 359 97.92 97.92 4.26e-129 REF WP_011144181 "proton-gated ion channel [Gloeobacter violaceus]" 98.46 359 97.92 97.92 4.26e-129 SP Q7NDN8 "RecName: Full=Proton-gated ion channel; AltName: Full=GLIC; AltName: Full=Ligand-gated ion channel; Short=LGIC; Flags: Precurso" 98.46 359 97.92 97.92 4.26e-129 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $GLIC_ECD 'Gloeobacter violaceus' 33072 Bacteria . Gloeobacter violaceus 'PCC 7421' glr4197 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $GLIC_ECD 'recombinant technology' . Escherichia coli BL21 DE3 pET20b+ 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 $GLIC_ECD 0.6 mM '[U-98% 13C; U-98% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Pi 50 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GLIC_ECD 0.6 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Pi 50 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GLIC_ECD 0.6 mM [U-15N]-Leu H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Pi 50 mM 'natural abundance' stop_ save_ save_sample_4-15 _Saveframe_category sample _Sample_type solution _Details ; Specific labeling with [U-15N]-Lys/Phe/Tyr/Ala/Val/Ile/Asp/Glu and reverse labeling 15N-GLIC[U-14N]-Arg/His/Asn ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GLIC_ECD . mM 0.3 0.5 [U-15N] H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' Pi 50 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'equipped with Cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details 'equipped with Cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HN(CO)CA_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_C(CO)NH_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_3 save_ save_2D_1H-15N_HSQC_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_4-15 save_ save_2D_1H-15N_HSQC_16 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_4-15 save_ save_2D_1H-13C_HSQC_17 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.2 . pH pressure 1 . atm temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D C(CO)NH' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_2 $sample_3 $sample_4-15 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'GLIC ECD' _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 3 3 ASP H H 8.457 0.0015 1 2 3 3 ASP C C 176.431 0.0015 1 3 3 3 ASP CA C 54.259 0.0015 1 4 3 3 ASP CB C 40.267 0.0015 1 5 3 3 ASP N N 122.512 0.0015 1 6 4 4 MET H H 8.376 0.0015 1 7 4 4 MET C C 176.146 0.0015 1 8 4 4 MET CA C 55.126 0.0015 1 9 4 4 MET CB C 31.529 0.0015 1 10 4 4 MET N N 120.923 0.0015 1 11 5 5 VAL H H 7.840 0.0015 1 12 5 5 VAL C C 176.063 0.0015 1 13 5 5 VAL CA C 61.717 0.0015 1 14 5 5 VAL CB C 30.756 0.0015 1 15 5 5 VAL N N 117.564 0.0015 1 16 6 6 SER H H 8.036 0.0015 1 17 6 6 SER C C 170.789 0.0015 1 18 6 6 SER CA C 56.114 0.0015 1 19 6 6 SER CB C 62.190 0.0015 1 20 6 6 SER N N 119.491 0.0015 1 21 11 11 ILE H H 10.436 0.0015 1 22 11 11 ILE CA C 62.778 0.0015 1 23 11 11 ILE N N 125.951 0.0015 1 24 12 12 ALA H H 9.680 0.0015 1 25 12 12 ALA C C 175.232 0.0015 1 26 12 12 ALA CA C 51.947 0.0015 1 27 12 12 ALA CB C 17.225 0.0015 1 28 12 12 ALA N N 128.022 0.0015 1 29 13 13 ASP H H 8.153 0.0015 1 30 13 13 ASP C C 175.308 0.0015 1 31 13 13 ASP CA C 52.805 0.0015 1 32 13 13 ASP CB C 40.038 0.0015 1 33 13 13 ASP N N 120.237 0.0015 1 34 14 14 GLU H H 9.654 0.0015 1 35 14 14 GLU CA C 54.490 0.0015 1 36 14 14 GLU N N 125.746 0.0015 1 37 16 16 LEU H H 8.864 0.0015 1 38 16 16 LEU C C 175.107 0.0015 1 39 16 16 LEU CA C 53.982 0.0015 1 40 16 16 LEU CB C 41.805 0.0015 1 41 16 16 LEU N N 125.740 0.0015 1 42 17 17 THR H H 8.150 0.0015 1 43 17 17 THR C C 174.302 0.0015 1 44 17 17 THR CA C 62.633 0.0015 1 45 17 17 THR CB C 68.514 0.0015 1 46 17 17 THR N N 124.903 0.0015 1 47 18 18 VAL H H 9.086 0.0015 1 48 18 18 VAL C C 174.943 0.0015 1 49 18 18 VAL CA C 60.327 0.0015 1 50 18 18 VAL CB C 31.838 0.0015 1 51 18 18 VAL N N 129.676 0.0015 1 52 19 19 ASN H H 9.494 0.0015 1 53 19 19 ASN C C 176.625 0.0015 1 54 19 19 ASN CA C 52.778 0.0015 1 55 19 19 ASN CB C 39.431 0.0015 1 56 19 19 ASN N N 127.765 0.0015 1 57 20 20 THR H H 8.734 0.0015 1 58 20 20 THR CA C 60.618 0.0015 1 59 20 20 THR N N 117.474 0.0015 1 60 21 21 GLY H H 8.613 0.0015 1 61 21 21 GLY CA C 45.624 0.0015 1 62 21 21 GLY N N 108.502 0.0015 1 63 22 22 ILE H H 6.248 0.0015 1 64 22 22 ILE CA C 59.938 0.0015 1 65 22 22 ILE N N 120.702 0.0015 1 66 23 23 TYR H H 8.918 0.0015 1 67 23 23 TYR CA C 55.019 0.0015 1 68 23 23 TYR CB C 40.177 0.0015 1 69 23 23 TYR N N 129.211 0.0015 1 70 24 24 LEU H H 8.521 0.0015 1 71 24 24 LEU CA C 55.334 0.0015 1 72 24 24 LEU CB C 41.163 0.0015 1 73 24 24 LEU N N 127.820 0.0015 1 74 25 25 ILE H H 8.404 0.0015 1 75 25 25 ILE CA C 61.877 0.0015 1 76 25 25 ILE N N 123.789 0.0015 1 77 26 26 GLU H H 8.011 0.0015 1 78 26 26 GLU CA C 55.503 0.0015 1 79 26 26 GLU CB C 33.601 0.0015 1 80 26 26 GLU N N 116.287 0.0015 1 81 27 27 CYS H H 8.772 0.0015 1 82 27 27 CYS CA C 57.062 0.0015 1 83 27 27 CYS CB C 30.714 0.0015 1 84 27 27 CYS N N 122.590 0.0015 1 85 33 33 LYS H H 8.075 0.0015 1 86 33 33 LYS C C 175.655 0.0015 1 87 33 33 LYS CA C 55.905 0.0015 1 88 33 33 LYS CB C 31.642 0.0015 1 89 33 33 LYS N N 118.966 0.0015 1 90 34 34 ALA H H 7.917 0.0015 1 91 34 34 ALA CA C 52.263 0.0015 1 92 34 34 ALA CB C 16.390 0.0015 1 93 34 34 ALA N N 121.962 0.0015 1 94 42 42 PHE H H 8.959 0.0015 1 95 42 42 PHE CA C 56.432 0.0015 1 96 42 42 PHE CB C 40.670 0.0015 1 97 42 42 PHE N N 115.767 0.0015 1 98 44 44 SER H H 9.241 0.0015 1 99 44 44 SER C C 174.195 0.0015 1 100 44 44 SER CA C 55.731 0.0015 1 101 44 44 SER CB C 64.515 0.0015 1 102 44 44 SER N N 122.966 0.0015 1 103 45 45 LEU H H 9.131 0.0015 1 104 45 45 LEU CA C 52.786 0.0015 1 105 45 45 LEU CB C 46.479 0.0015 1 106 45 45 LEU N N 123.059 0.0015 1 107 46 46 SER H H 8.781 0.0015 1 108 46 46 SER C C 173.263 0.0015 1 109 46 46 SER CA C 56.373 0.0015 1 110 46 46 SER CB C 64.784 0.0015 1 111 46 46 SER N N 114.281 0.0015 1 112 47 47 TRP H H 7.939 0.0015 1 113 47 47 TRP C C 171.801 0.0015 1 114 47 47 TRP CA C 56.979 0.0015 1 115 47 47 TRP CB C 31.043 0.0015 1 116 47 47 TRP N N 125.631 0.0015 1 117 48 48 LYS H H 8.494 0.0015 1 118 48 48 LYS C C 175.677 0.0015 1 119 48 48 LYS CA C 54.760 0.0015 1 120 48 48 LYS CB C 32.930 0.0015 1 121 48 48 LYS N N 120.779 0.0015 1 122 49 49 ASP H H 8.833 0.0015 1 123 49 49 ASP C C 176.648 0.0015 1 124 49 49 ASP CA C 52.196 0.0015 1 125 49 49 ASP CB C 40.868 0.0015 1 126 49 49 ASP N N 125.901 0.0015 1 127 50 50 ARG H H 9.199 0.0015 1 128 50 50 ARG C C 178.385 0.0015 1 129 50 50 ARG CA C 58.485 0.0015 1 130 50 50 ARG CB C 28.390 0.0015 1 131 50 50 ARG N N 123.143 0.0015 1 132 51 51 ARG H H 8.271 0.0015 1 133 51 51 ARG C C 177.905 0.0015 1 134 51 51 ARG CA C 57.399 0.0015 1 135 51 51 ARG CB C 28.880 0.0015 1 136 51 51 ARG N N 118.554 0.0015 1 137 52 52 LEU H H 7.902 0.0015 1 138 52 52 LEU C C 176.321 0.0015 1 139 52 52 LEU CA C 52.809 0.0015 1 140 52 52 LEU CB C 41.329 0.0015 1 141 52 52 LEU N N 116.097 0.0015 1 142 53 53 ALA H H 6.765 0.0015 1 143 53 53 ALA C C 176.842 0.0015 1 144 53 53 ALA CA C 52.770 0.0015 1 145 53 53 ALA CB C 18.330 0.0015 1 146 53 53 ALA N N 121.328 0.0015 1 147 54 54 PHE H H 8.938 0.0015 1 148 54 54 PHE C C 172.004 0.0015 1 149 54 54 PHE CA C 55.572 0.0015 1 150 54 54 PHE CB C 39.890 0.0015 1 151 54 54 PHE N N 118.053 0.0015 1 152 55 55 ASP H H 8.597 0.0015 1 153 55 55 ASP C C 176.600 0.0015 1 154 55 55 ASP CA C 49.846 0.0015 1 155 55 55 ASP CB C 41.686 0.0015 1 156 55 55 ASP N N 119.688 0.0015 1 157 57 57 VAL H H 7.984 0.0015 1 158 57 57 VAL C C 178.855 0.0015 1 159 57 57 VAL CA C 65.139 0.0015 1 160 57 57 VAL CB C 30.285 0.0015 1 161 57 57 VAL N N 121.330 0.0015 1 162 58 58 ARG H H 7.600 0.0015 1 163 58 58 ARG C C 178.679 0.0015 1 164 58 58 ARG CA C 57.687 0.0015 1 165 58 58 ARG CB C 29.367 0.0015 1 166 58 58 ARG N N 119.831 0.0015 1 167 59 59 SER H H 8.154 0.0015 1 168 59 59 SER C C 175.185 0.0015 1 169 59 59 SER CA C 60.058 0.0015 1 170 59 59 SER CB C 63.172 0.0015 1 171 59 59 SER N N 111.693 0.0015 1 172 60 60 GLY H H 7.659 0.0015 1 173 60 60 GLY C C 173.155 0.0015 1 174 60 60 GLY CA C 45.499 0.0015 1 175 60 60 GLY N N 110.549 0.0015 1 176 61 61 VAL H H 7.442 0.0015 1 177 61 61 VAL C C 173.860 0.0015 1 178 61 61 VAL CA C 59.158 0.0015 1 179 61 61 VAL CB C 34.674 0.0015 1 180 61 61 VAL N N 113.603 0.0015 1 181 62 62 ARG H H 8.519 0.0015 1 182 62 62 ARG C C 175.531 0.0015 1 183 62 62 ARG CA C 55.784 0.0015 1 184 62 62 ARG CB C 30.058 0.0015 1 185 62 62 ARG N N 118.101 0.0015 1 186 63 63 VAL H H 7.361 0.0015 1 187 63 63 VAL C C 173.974 0.0015 1 188 63 63 VAL CA C 60.131 0.0015 1 189 63 63 VAL CB C 34.751 0.0015 1 190 63 63 VAL N N 116.085 0.0015 1 191 64 64 LYS H H 8.696 0.0015 1 192 64 64 LYS C C 175.293 0.0015 1 193 64 64 LYS CA C 54.725 0.0015 1 194 64 64 LYS CB C 35.326 0.0015 1 195 64 64 LYS N N 125.052 0.0015 1 196 65 65 THR H H 8.045 0.0015 1 197 65 65 THR C C 173.640 0.0015 1 198 65 65 THR CA C 60.111 0.0015 1 199 65 65 THR CB C 70.007 0.0015 1 200 65 65 THR N N 116.033 0.0015 1 201 66 66 TYR H H 7.464 0.0015 1 202 66 66 TYR CA C 56.866 0.0015 1 203 66 66 TYR CB C 42.814 0.0015 1 204 66 66 TYR N N 121.066 0.0015 1 205 67 67 GLU H H 8.334 0.0015 1 206 67 67 GLU C C 176.063 0.0015 1 207 67 67 GLU CA C 53.620 0.0015 1 208 67 67 GLU CB C 27.892 0.0015 1 209 67 67 GLU N N 120.332 0.0015 1 210 69 69 GLU H H 8.304 0.0015 1 211 69 69 GLU C C 176.982 0.0015 1 212 69 69 GLU CA C 57.363 0.0015 1 213 69 69 GLU CB C 27.739 0.0015 1 214 69 69 GLU N N 112.063 0.0015 1 215 70 70 ALA H H 7.826 0.0015 1 216 70 70 ALA C C 176.807 0.0015 1 217 70 70 ALA CA C 52.422 0.0015 1 218 70 70 ALA CB C 20.657 0.0015 1 219 70 70 ALA N N 120.541 0.0015 1 220 71 71 ILE H H 7.082 0.0015 1 221 71 71 ILE CA C 58.219 0.0015 1 222 71 71 ILE CB C 41.983 0.0015 1 223 71 71 ILE N N 110.442 0.0015 1 224 72 72 TRP H H 8.482 0.0015 1 225 72 72 TRP C C 174.846 0.0015 1 226 72 72 TRP CA C 59.380 0.0015 1 227 72 72 TRP CB C 27.718 0.0015 1 228 72 72 TRP N N 123.013 0.0015 1 229 73 73 ILE H H 6.397 0.0015 1 230 73 73 ILE CA C 56.123 0.0015 1 231 73 73 ILE CB C 40.613 0.0015 1 232 73 73 ILE N N 124.915 0.0015 1 233 75 75 GLU H H 8.656 0.0015 1 234 75 75 GLU C C 174.486 0.0015 1 235 75 75 GLU CA C 54.560 0.0015 1 236 75 75 GLU CB C 28.112 0.0015 1 237 75 75 GLU N N 124.033 0.0015 1 238 76 76 ILE H H 8.016 0.0015 1 239 76 76 ILE C C 176.052 0.0015 1 240 76 76 ILE CA C 57.853 0.0015 1 241 76 76 ILE CB C 35.935 0.0015 1 242 76 76 ILE N N 126.937 0.0015 1 243 77 77 ARG H H 8.995 0.0015 1 244 77 77 ARG CA C 54.091 0.0015 1 245 77 77 ARG N N 127.909 0.0015 1 246 78 78 PHE H H 8.586 0.0015 1 247 78 78 PHE N N 126.370 0.0015 1 248 80 80 ASN H H 8.983 0.0015 1 249 80 80 ASN CA C 52.442 0.0015 1 250 80 80 ASN N N 117.111 0.0015 1 251 81 81 VAL H H 6.984 0.0015 1 252 81 81 VAL CA C 59.152 0.0015 1 253 81 81 VAL N N 113.258 0.0015 1 254 82 82 GLU H H 8.597 0.0015 1 255 82 82 GLU C C 175.968 0.0015 1 256 82 82 GLU CA C 56.972 0.0015 1 257 82 82 GLU CB C 29.984 0.0015 1 258 82 82 GLU N N 125.297 0.0015 1 259 84 84 ALA H H 8.129 0.0015 1 260 84 84 ALA C C 177.273 0.0015 1 261 84 84 ALA CA C 51.681 0.0015 1 262 84 84 ALA CB C 18.805 0.0015 1 263 84 84 ALA N N 123.794 0.0015 1 264 85 85 ARG H H 8.353 0.0015 1 265 85 85 ARG C C 174.153 0.0015 1 266 85 85 ARG CA C 54.494 0.0015 1 267 85 85 ARG CB C 28.881 0.0015 1 268 85 85 ARG N N 121.269 0.0015 1 269 86 86 ASP H H 8.531 0.0015 1 270 86 86 ASP CA C 53.360 0.0015 1 271 86 86 ASP CB C 40.805 0.0015 1 272 86 86 ASP N N 123.484 0.0015 1 273 87 87 ALA H H 8.493 0.0015 1 274 87 87 ALA C C 176.346 0.0015 1 275 87 87 ALA CA C 51.188 0.0015 1 276 87 87 ALA CB C 21.983 0.0015 1 277 87 87 ALA N N 127.867 0.0015 1 278 88 88 ASP H H 8.781 0.0015 1 279 88 88 ASP CA C 52.672 0.0015 1 280 88 88 ASP N N 122.028 0.0015 1 281 93 93 SER H H 8.646 0.0015 1 282 93 93 SER C C 173.185 0.0015 1 283 93 93 SER CA C 57.177 0.0015 1 284 93 93 SER CB C 65.711 0.0015 1 285 93 93 SER N N 122.638 0.0015 1 286 94 94 VAL H H 9.420 0.0015 1 287 94 94 VAL C C 175.606 0.0015 1 288 94 94 VAL CA C 60.659 0.0015 1 289 94 94 VAL CB C 33.943 0.0015 1 290 94 94 VAL N N 125.877 0.0015 1 291 95 95 SER H H 8.565 0.0015 1 292 95 95 SER C C 173.119 0.0015 1 293 95 95 SER CA C 57.406 0.0015 1 294 95 95 SER CB C 62.184 0.0015 1 295 95 95 SER N N 123.771 0.0015 1 296 97 97 ASP H H 7.537 0.0015 1 297 97 97 ASP C C 177.148 0.0015 1 298 97 97 ASP CA C 52.919 0.0015 1 299 97 97 ASP CB C 39.189 0.0015 1 300 97 97 ASP N N 111.265 0.0015 1 301 98 98 GLY H H 8.679 0.0015 1 302 98 98 GLY C C 173.663 0.0015 1 303 98 98 GLY CA C 44.009 0.0015 1 304 98 98 GLY N N 109.104 0.0015 1 305 99 99 THR H H 7.553 0.0015 1 306 99 99 THR CA C 64.877 0.0015 1 307 99 99 THR CB C 67.016 0.0015 1 308 99 99 THR N N 118.530 0.0015 1 309 100 100 VAL H H 9.163 0.0015 1 310 100 100 VAL C C 175.321 0.0015 1 311 100 100 VAL CA C 61.290 0.0015 1 312 100 100 VAL CB C 31.390 0.0015 1 313 100 100 VAL N N 133.099 0.0015 1 314 101 101 GLN H H 9.017 0.0015 1 315 101 101 GLN C C 173.420 0.0015 1 316 101 101 GLN CA C 54.720 0.0015 1 317 101 101 GLN CB C 29.294 0.0015 1 318 101 101 GLN N N 125.794 0.0015 1 319 102 102 TYR H H 9.313 0.0015 1 320 102 102 TYR CA C 56.176 0.0015 1 321 102 102 TYR CB C 40.959 0.0015 1 322 102 102 TYR N N 129.862 0.0015 1 323 103 103 LEU H H 8.675 0.0015 1 324 103 103 LEU CA C 53.487 0.0015 1 325 103 103 LEU N N 133.189 0.0015 1 326 105 105 ARG H H 9.111 0.0015 1 327 105 105 ARG N N 126.966 0.0015 1 328 106 106 PHE H H 9.488 0.0015 1 329 106 106 PHE CA C 55.005 0.0015 1 330 106 106 PHE CB C 42.252 0.0015 1 331 106 106 PHE N N 124.494 0.0015 1 332 107 107 SER H H 8.487 0.0015 1 333 107 107 SER C C 174.332 0.0015 1 334 107 107 SER CA C 55.772 0.0015 1 335 107 107 SER CB C 65.314 0.0015 1 336 107 107 SER N N 114.568 0.0015 1 337 108 108 ALA H H 8.566 0.0015 1 338 108 108 ALA N N 127.483 0.0015 1 339 109 109 ARG H H 8.771 0.0015 1 340 109 109 ARG C C 174.447 0.0015 1 341 109 109 ARG CA C 54.778 0.0015 1 342 109 109 ARG CB C 29.677 0.0015 1 343 109 109 ARG N N 122.727 0.0015 1 344 111 111 LEU H H 8.391 0.0015 1 345 111 111 LEU CA C 53.516 0.0015 1 346 111 111 LEU CB C 40.835 0.0015 1 347 111 111 LEU N N 127.098 0.0015 1 348 114 114 LEU H H 8.809 0.0015 1 349 114 114 LEU CA C 54.885 0.0015 1 350 114 114 LEU CB C 41.014 0.0015 1 351 114 114 LEU N N 124.713 0.0015 1 352 115 115 ASP H H 8.522 0.0015 1 353 115 115 ASP C C 177.154 0.0015 1 354 115 115 ASP CA C 53.676 0.0015 1 355 115 115 ASP CB C 40.374 0.0015 1 356 115 115 ASP N N 121.485 0.0015 1 357 116 116 GLY H H 8.432 0.0015 1 358 116 116 GLY C C 174.564 0.0015 1 359 116 116 GLY CA C 45.248 0.0015 1 360 116 116 GLY N N 111.246 0.0015 1 361 117 117 ARG H H 8.161 0.0015 1 362 117 117 ARG C C 176.806 0.0015 1 363 117 117 ARG CA C 55.856 0.0015 1 364 117 117 ARG CB C 29.544 0.0015 1 365 117 117 ARG N N 120.720 0.0015 1 366 118 118 ARG H H 8.236 0.0015 1 367 118 118 ARG C C 176.778 0.0015 1 368 118 118 ARG CA C 55.800 0.0015 1 369 118 118 ARG CB C 29.353 0.0015 1 370 118 118 ARG N N 122.052 0.0015 1 371 119 119 THR H H 8.236 0.0015 1 372 119 119 THR C C 175.056 0.0015 1 373 119 119 THR CA C 61.786 0.0015 1 374 119 119 THR CB C 69.091 0.0015 1 375 119 119 THR N N 115.157 0.0015 1 376 120 120 GLU H H 8.494 0.0015 1 377 120 120 GLU C C 176.382 0.0015 1 378 120 120 GLU CA C 56.560 0.0015 1 379 120 120 GLU CB C 28.642 0.0015 1 380 120 120 GLU N N 121.920 0.0015 1 381 121 121 SER H H 8.025 0.0015 1 382 121 121 SER C C 174.536 0.0015 1 383 121 121 SER CA C 57.859 0.0015 1 384 121 121 SER CB C 63.253 0.0015 1 385 121 121 SER N N 115.431 0.0015 1 386 122 122 ASP H H 8.373 0.0015 1 387 122 122 ASP CA C 54.640 0.0015 1 388 122 122 ASP CB C 40.439 0.0015 1 389 122 122 ASP N N 122.530 0.0015 1 390 123 123 SER H H 8.019 0.0015 1 391 123 123 SER C C 173.541 0.0015 1 392 123 123 SER CA C 57.603 0.0015 1 393 123 123 SER CB C 63.809 0.0015 1 394 123 123 SER N N 115.479 0.0015 1 395 124 124 GLN H H 8.930 0.0015 1 396 124 124 GLN C C 173.911 0.0015 1 397 124 124 GLN CA C 54.100 0.0015 1 398 124 124 GLN CB C 31.518 0.0015 1 399 124 124 GLN N N 121.789 0.0015 1 400 125 125 THR H H 8.536 0.0015 1 401 125 125 THR C C 172.802 0.0015 1 402 125 125 THR CA C 61.135 0.0015 1 403 125 125 THR CB C 69.218 0.0015 1 404 125 125 THR N N 118.083 0.0015 1 405 126 126 LEU H H 8.792 0.0015 1 406 126 126 LEU C C 172.656 0.0015 1 407 126 126 LEU CA C 53.161 0.0015 1 408 126 126 LEU N N 128.638 0.0015 1 409 128 128 ILE H H 9.044 0.0015 1 410 128 128 ILE CA C 61.241 0.0015 1 411 128 128 ILE CB C 39.401 0.0015 1 412 128 128 ILE N N 122.272 0.0015 1 413 129 129 TYR H H 8.297 0.0015 1 414 129 129 TYR CA C 55.940 0.0015 1 415 129 129 TYR N N 124.438 0.0015 1 416 130 130 LEU H H 8.814 0.0015 1 417 130 130 LEU C C 175.692 0.0015 1 418 130 130 LEU CA C 53.530 0.0015 1 419 130 130 LEU CB C 45.292 0.0015 1 420 130 130 LEU N N 124.236 0.0015 1 421 131 131 ILE H H 8.666 0.0015 1 422 131 131 ILE CA C 59.205 0.0015 1 423 131 131 ILE N N 117.331 0.0015 1 424 133 133 ARG H H 8.282 0.0015 1 425 133 133 ARG C C 175.950 0.0015 1 426 133 133 ARG CA C 55.011 0.0015 1 427 133 133 ARG CB C 30.205 0.0015 1 428 133 133 ARG N N 127.796 0.0015 1 429 134 134 SER H H 8.418 0.0015 1 430 134 134 SER C C 173.707 0.0015 1 431 134 134 SER CA C 59.349 0.0015 1 432 134 134 SER CB C 63.150 0.0015 1 433 134 134 SER N N 120.314 0.0015 1 434 135 135 VAL H H 8.124 0.0015 1 435 135 135 VAL C C 176.367 0.0015 1 436 135 135 VAL CA C 59.472 0.0015 1 437 135 135 VAL CB C 32.878 0.0015 1 438 135 135 VAL N N 116.466 0.0015 1 439 136 136 ASP H H 8.562 0.0015 1 440 136 136 ASP CA C 56.318 0.0015 1 441 136 136 ASP CB C 39.917 0.0015 1 442 136 136 ASP N N 121.861 0.0015 1 443 137 137 THR H H 7.492 0.0015 1 444 137 137 THR C C 174.413 0.0015 1 445 137 137 THR CA C 61.651 0.0015 1 446 137 137 THR CB C 68.862 0.0015 1 447 137 137 THR N N 106.982 0.0015 1 448 138 138 ARG H H 7.336 0.0015 1 449 138 138 ARG C C 173.899 0.0015 1 450 138 138 ARG CA C 54.180 0.0015 1 451 138 138 ARG CB C 31.469 0.0015 1 452 138 138 ARG N N 120.762 0.0015 1 453 139 139 ASN H H 8.612 0.0015 1 454 139 139 ASN C C 173.984 0.0015 1 455 139 139 ASN CA C 52.547 0.0015 1 456 139 139 ASN CB C 38.022 0.0015 1 457 139 139 ASN N N 124.712 0.0015 1 458 140 140 ILE H H 8.206 0.0015 1 459 140 140 ILE C C 174.466 0.0015 1 460 140 140 ILE CA C 60.179 0.0015 1 461 140 140 ILE CB C 38.349 0.0015 1 462 140 140 ILE N N 125.356 0.0015 1 463 141 141 VAL H H 8.713 0.0015 1 464 141 141 VAL C C 174.250 0.0015 1 465 141 141 VAL CA C 59.426 0.0015 1 466 141 141 VAL CB C 34.835 0.0015 1 467 141 141 VAL N N 124.968 0.0015 1 468 142 142 LEU H H 8.265 0.0015 1 469 142 142 LEU C C 175.883 0.0015 1 470 142 142 LEU CA C 53.043 0.0015 1 471 142 142 LEU CB C 42.288 0.0015 1 472 142 142 LEU N N 122.697 0.0015 1 473 143 143 ALA H H 8.600 0.0015 1 474 143 143 ALA C C 176.499 0.0015 1 475 143 143 ALA CA C 49.618 0.0015 1 476 143 143 ALA CB C 21.858 0.0015 1 477 143 143 ALA N N 124.372 0.0015 1 478 144 144 VAL H H 8.725 0.0015 1 479 144 144 VAL C C 174.966 0.0015 1 480 144 144 VAL CA C 61.392 0.0015 1 481 144 144 VAL CB C 33.030 0.0015 1 482 144 144 VAL N N 123.416 0.0015 1 483 145 145 ASP H H 8.799 0.0015 1 484 145 145 ASP CA C 51.340 0.0015 1 485 145 145 ASP CB C 39.574 0.0015 1 486 145 145 ASP N N 128.340 0.0015 1 487 146 146 LEU H H 8.478 0.0015 1 488 146 146 LEU CA C 57.456 0.0015 1 489 146 146 LEU CB C 40.595 0.0015 1 490 146 146 LEU N N 124.450 0.0015 1 491 147 147 GLU H H 8.140 0.0015 1 492 147 147 GLU C C 177.782 0.0015 1 493 147 147 GLU CA C 57.673 0.0015 1 494 147 147 GLU CB C 28.594 0.0015 1 495 147 147 GLU N N 116.550 0.0015 1 496 148 148 LYS H H 7.828 0.0015 1 497 148 148 LYS C C 174.744 0.0015 1 498 148 148 LYS CA C 53.605 0.0015 1 499 148 148 LYS CB C 32.007 0.0015 1 500 148 148 LYS N N 117.722 0.0015 1 501 149 149 VAL H H 7.111 0.0015 1 502 149 149 VAL C C 176.324 0.0015 1 503 149 149 VAL CA C 60.362 0.0015 1 504 149 149 VAL CB C 32.425 0.0015 1 505 149 149 VAL N N 120.428 0.0015 1 506 150 150 GLY H H 8.313 0.0015 1 507 150 150 GLY C C 169.988 0.0015 1 508 150 150 GLY CA C 44.840 0.0015 1 509 150 150 GLY N N 112.642 0.0015 1 510 151 151 LYS H H 8.266 0.0015 1 511 151 151 LYS C C 174.171 0.0015 1 512 151 151 LYS CA C 52.989 0.0015 1 513 151 151 LYS CB C 34.165 0.0015 1 514 151 151 LYS N N 116.108 0.0015 1 515 152 152 ASN H H 7.652 0.0015 1 516 152 152 ASN CA C 52.293 0.0015 1 517 152 152 ASN CB C 38.683 0.0015 1 518 152 152 ASN N N 121.652 0.0015 1 519 153 153 ASP H H 8.826 0.0015 1 520 153 153 ASP CA C 56.402 0.0015 1 521 153 153 ASP N N 122.129 0.0015 1 522 154 154 ASP H H 8.161 0.0015 1 523 154 154 ASP CA C 52.883 0.0015 1 524 154 154 ASP CB C 39.647 0.0015 1 525 154 154 ASP N N 116.818 0.0015 1 526 155 155 VAL H H 7.145 0.0015 1 527 155 155 VAL CA C 62.742 0.0015 1 528 155 155 VAL N N 120.081 0.0015 1 529 159 159 GLY H H 8.829 0.0015 1 530 159 159 GLY C C 173.883 0.0015 1 531 159 159 GLY CA C 45.029 0.0015 1 532 159 159 GLY N N 115.307 0.0015 1 533 160 160 TRP H H 8.101 0.0015 1 534 160 160 TRP C C 174.310 0.0015 1 535 160 160 TRP CA C 55.948 0.0015 1 536 160 160 TRP CB C 31.883 0.0015 1 537 160 160 TRP N N 121.103 0.0015 1 538 161 161 ASP H H 9.641 0.0015 1 539 161 161 ASP C C 176.097 0.0015 1 540 161 161 ASP CA C 53.169 0.0015 1 541 161 161 ASP CB C 41.819 0.0015 1 542 161 161 ASP N N 121.962 0.0015 1 543 162 162 ILE H H 8.868 0.0015 1 544 162 162 ILE C C 175.948 0.0015 1 545 162 162 ILE CA C 61.159 0.0015 1 546 162 162 ILE CB C 36.641 0.0015 1 547 162 162 ILE N N 122.594 0.0015 1 548 163 163 GLU H H 9.223 0.0015 1 549 163 163 GLU CA C 57.480 0.0015 1 550 163 163 GLU CB C 29.862 0.0015 1 551 163 163 GLU N N 130.082 0.0015 1 552 164 164 SER H H 7.418 0.0015 1 553 164 164 SER C C 172.045 0.0015 1 554 164 164 SER CA C 57.205 0.0015 1 555 164 164 SER CB C 63.829 0.0015 1 556 164 164 SER N N 108.307 0.0015 1 557 165 165 PHE H H 8.648 0.0015 1 558 165 165 PHE C C 173.302 0.0015 1 559 165 165 PHE CA C 55.385 0.0015 1 560 165 165 PHE CB C 40.236 0.0015 1 561 165 165 PHE N N 123.180 0.0015 1 562 166 166 THR H H 8.115 0.0015 1 563 166 166 THR C C 170.846 0.0015 1 564 166 166 THR CA C 59.275 0.0015 1 565 166 166 THR CB C 71.082 0.0015 1 566 166 166 THR N N 119.318 0.0015 1 567 167 167 ALA H H 8.157 0.0015 1 568 167 167 ALA C C 176.012 0.0015 1 569 167 167 ALA CA C 50.056 0.0015 1 570 167 167 ALA CB C 20.676 0.0015 1 571 167 167 ALA N N 122.643 0.0015 1 572 172 172 ALA H H 8.333 0.0015 1 573 172 172 ALA C C 177.094 0.0015 1 574 172 172 ALA CA C 51.695 0.0015 1 575 172 172 ALA CB C 18.558 0.0015 1 576 172 172 ALA N N 124.974 0.0015 1 577 175 175 ALA H H 8.149 0.0015 1 578 175 175 ALA CA C 52.236 0.0015 1 579 175 175 ALA N N 124.816 0.0015 1 580 176 176 LEU H H 7.887 0.0015 1 581 176 176 LEU C C 177.619 0.0015 1 582 176 176 LEU CA C 55.250 0.0015 1 583 176 176 LEU CB C 41.287 0.0015 1 584 176 176 LEU N N 120.428 0.0015 1 585 177 177 GLU H H 8.341 0.0015 1 586 177 177 GLU C C 176.112 0.0015 1 587 177 177 GLU CA C 56.685 0.0015 1 588 177 177 GLU CB C 28.821 0.0015 1 589 177 177 GLU N N 119.545 0.0015 1 590 178 178 ASP H H 8.052 0.0015 1 591 178 178 ASP CA C 53.997 0.0015 1 592 178 178 ASP N N 119.703 0.0015 1 593 179 179 ARG H H 7.945 0.0015 1 594 179 179 ARG CA C 55.406 0.0015 1 595 179 179 ARG CB C 29.383 0.0015 1 596 179 179 ARG N N 120.320 0.0015 1 597 186 186 TYR H H 8.734 0.0015 1 598 186 186 TYR C C 174.182 0.0015 1 599 186 186 TYR CA C 58.347 0.0015 1 600 186 186 TYR CB C 37.382 0.0015 1 601 186 186 TYR N N 126.030 0.0015 1 602 187 187 GLN H H 8.707 0.0015 1 603 187 187 GLN C C 175.136 0.0015 1 604 187 187 GLN CA C 53.752 0.0015 1 605 187 187 GLN CB C 28.942 0.0015 1 606 187 187 GLN N N 120.911 0.0015 1 607 188 188 LEU H H 9.134 0.0015 1 608 188 188 LEU C C 174.129 0.0015 1 609 188 188 LEU CA C 53.081 0.0015 1 610 188 188 LEU N N 130.434 0.0015 1 611 189 189 ARG H H 8.535 0.0015 1 612 189 189 ARG C C 175.421 0.0015 1 613 189 189 ARG CA C 55.522 0.0015 1 614 189 189 ARG CB C 29.457 0.0015 1 615 189 189 ARG N N 129.085 0.0015 1 616 190 190 ILE H H 8.843 0.0015 1 617 190 190 ILE CA C 58.712 0.0015 1 618 190 190 ILE CB C 40.999 0.0015 1 619 190 190 ILE N N 120.702 0.0015 1 620 191 191 SER H H 9.185 0.0015 1 621 191 191 SER C C 174.074 0.0015 1 622 191 191 SER CA C 56.347 0.0015 1 623 191 191 SER CB C 65.078 0.0015 1 624 191 191 SER N N 116.210 0.0015 1 625 192 192 ARG H H 8.810 0.0015 1 626 192 192 ARG C C 176.969 0.0015 1 627 192 192 ARG CA C 56.552 0.0015 1 628 192 192 ARG CB C 29.512 0.0015 1 629 192 192 ARG N N 127.086 0.0015 1 630 193 193 GLN H H 7.866 0.0015 1 631 193 193 GLN C C 176.811 0.0015 1 632 193 193 GLN CA C 55.749 0.0015 1 633 193 193 GLN CB C 27.782 0.0015 1 634 193 193 GLN N N 124.760 0.0015 1 635 194 194 GLY H H 8.555 0.0015 1 636 194 194 GLY C C 174.605 0.0015 1 637 194 194 GLY CA C 44.797 0.0015 1 638 194 194 GLY N N 111.681 0.0015 1 639 195 195 GLY H H 8.131 0.0015 1 640 195 195 GLY C C 173.884 0.0015 1 641 195 195 GLY CA C 44.657 0.0015 1 642 195 195 GLY N N 108.908 0.0015 1 stop_ save_