data_16160 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for Myosin Phosphatase Trageting Subunit 1 (residues 1-98) ; _BMRB_accession_number 16160 _BMRB_flat_file_name bmr16160.str _Entry_type original _Submission_date 2009-02-04 _Accession_date 2009-02-04 _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 Pinheiro Anderson . . 2 Peti Wolfgang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 333 "13C chemical shifts" 380 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-07 original author . stop_ _Original_release_date 2012-08-07 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Understanding the assembly of the myosin phosphatase holoenzyme' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pinheiro Anderson . . 2 Peti Wolfgang . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'intrinsically unfolded proteins' MYPT1 NMR PP1 targeting stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MYPT1 1-98 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MYPT1 1-98 monomer' $MYPT1_1-98 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MYPT1_1-98 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MYPT1_1-98 _Molecular_mass 11073.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'Regulatory (targeting) subunit of protein phosphatase 1 in the myosin phosphatase holoenzyme.' stop_ _Details ; MYPT1 is a 110 kDa protein. In this study, we used a shorter construct comprising the first 98 residues of the protein. This construct, refered as MYPT1 1-98, is part of the PP1-binding domain of MYPT1. ; ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; GHMKMADAKQKRNEQLKRWI GSETDLEPPVVKRKKTKVKF DDGAVFLAACSSGDTEEVLR LLERGADINYANVDGLTALH QASIDDNVDMVKFLVENGAN ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 LYS 5 MET 6 ALA 7 ASP 8 ALA 9 LYS 10 GLN 11 LYS 12 ARG 13 ASN 14 GLU 15 GLN 16 LEU 17 LYS 18 ARG 19 TRP 20 ILE 21 GLY 22 SER 23 GLU 24 THR 25 ASP 26 LEU 27 GLU 28 PRO 29 PRO 30 VAL 31 VAL 32 LYS 33 ARG 34 LYS 35 LYS 36 THR 37 LYS 38 VAL 39 LYS 40 PHE 41 ASP 42 ASP 43 GLY 44 ALA 45 VAL 46 PHE 47 LEU 48 ALA 49 ALA 50 CYS 51 SER 52 SER 53 GLY 54 ASP 55 THR 56 GLU 57 GLU 58 VAL 59 LEU 60 ARG 61 LEU 62 LEU 63 GLU 64 ARG 65 GLY 66 ALA 67 ASP 68 ILE 69 ASN 70 TYR 71 ALA 72 ASN 73 VAL 74 ASP 75 GLY 76 LEU 77 THR 78 ALA 79 LEU 80 HIS 81 GLN 82 ALA 83 SER 84 ILE 85 ASP 86 ASP 87 ASN 88 VAL 89 ASP 90 MET 91 VAL 92 LYS 93 PHE 94 LEU 95 VAL 96 GLU 97 ASN 98 GLY 99 ALA 100 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 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 1S70 "Complex Between Protein Ser/thr Phosphatase-1 (delta) And The Myosin Phosphatase Targeting Subunit 1 (mypt1)" 98.00 299 98.98 98.98 1.07e-60 DBJ BAA07201 "133kDa myosin-binding subunit of smooth muscle myosin phosphatase (M133) [Gallus gallus]" 98.00 1004 98.98 98.98 2.58e-59 DBJ BAA07202 "130 kDa myosin-binding subunit of smooth muscle myosin phophatase (M130) [Gallus gallus]" 98.00 963 98.98 98.98 2.36e-59 EMBL CAG32302 "hypothetical protein RCJMB04_22k13, partial [Gallus gallus]" 98.00 172 98.98 98.98 2.45e-62 GB KQK73925 "hypothetical protein AAES_00677 [Amazona aestiva]" 80.00 185 98.75 100.00 3.99e-49 GB KQL94224 "protein phosphatase 1, regulatory subunit 12A [Alligator mississippiensis]" 98.00 1036 98.98 98.98 3.85e-59 REF NP_990454 "protein phosphatase 1 regulatory subunit 12A [Gallus gallus]" 98.00 1004 98.98 98.98 2.58e-59 REF XP_002194705 "PREDICTED: protein phosphatase 1 regulatory subunit 12A isoform X1 [Taeniopygia guttata]" 98.00 1033 98.98 98.98 4.30e-59 REF XP_005039540 "PREDICTED: protein phosphatase 1 regulatory subunit 12A isoform X1 [Ficedula albicollis]" 98.00 1033 98.98 98.98 4.05e-59 REF XP_005039541 "PREDICTED: protein phosphatase 1 regulatory subunit 12A isoform X2 [Ficedula albicollis]" 98.00 1008 98.98 98.98 3.18e-59 REF XP_005039542 "PREDICTED: protein phosphatase 1 regulatory subunit 12A isoform X3 [Ficedula albicollis]" 98.00 1002 98.98 98.98 2.78e-59 SP Q90623 "RecName: Full=Protein phosphatase 1 regulatory subunit 12A; AltName: Full=130 kDa myosin-binding subunit of smooth muscle myosi" 98.00 1004 98.98 98.98 2.58e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $MYPT1_1-98 Human 9606 Eukaryota Metazoa Homo sapiens MYPT1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $MYPT1_1-98 'recombinant technology' . Escherichia coli 'BL21 (DE3)-RIL' RP1B 'MYPT1 was expressed as a histag fusion protein with a cleavage site for TEV protease.' 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 $MYPT1_1-98 1.2 mM '[U-100% 15N]' NACL 50 mM 'natural abundance' 'Sodium Phosphate' 20 mM 'natural abundance' PMSF 0.25 mM 'natural abundance' TCEP 0.5 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 $MYPT1_1-98 1.0 mM '[U-100% 13C; U-100% 15N]' NACL 50 mM 'natural abundance' 'Sodium Phosphate' 20 mM 'natural abundance' PMSF 0.25 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' ; Prof. Kurt Wuthrich Institute of Molecular Biology and Biophysics ETH Honggerberg CH-8093 Zurich ; http://www.nmr.ch/ stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' ; Bruker BioSpin GmbH Silberstreifen 4 76287 Rheinstetten Germany ; http://www.bruker-biospin.com/topspin.html stop_ loop_ _Task collection processing stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' ; Prof. Kurt Wuthrich Institute of Molecular Biology and Biophysics ETH Honggerberg CH-8093 Zurich ; . stop_ loop_ _Task 'chemical shift calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . 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_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_2 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_2 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 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 6.8 . pH pressure 1.0 . atm temperature 283 . 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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 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_ _Software_label $CARA $CYANA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HNCACO' '3D HBHA(CO)NH' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'MYPT1 1-98 monomer' _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 MET H H 8.508 0.05 1 2 3 3 MET HA H 4.337 0.05 1 3 3 3 MET HB2 H 1.674 0.05 2 4 3 3 MET HB3 H 1.674 0.05 2 5 3 3 MET C C 175.968 0.6 1 6 3 3 MET CA C 55.422 0.6 1 7 3 3 MET CB C 32.872 0.6 1 8 3 3 MET CG C 31.571 0.6 1 9 3 3 MET N N 122.787 0.05 1 10 4 4 LYS H H 8.564 0.05 1 11 4 4 LYS HA H 4.186 0.05 1 12 4 4 LYS HB2 H 1.476 0.05 2 13 4 4 LYS HB3 H 1.476 0.05 2 14 4 4 LYS C C 176.750 0.6 1 15 4 4 LYS CA C 56.410 0.6 1 16 4 4 LYS CB C 32.776 0.6 1 17 4 4 LYS CD C 29.154 0.6 1 18 4 4 LYS CE C 41.810 0.6 1 19 4 4 LYS CG C 24.532 0.6 1 20 4 4 LYS N N 124.075 0.05 1 21 5 5 MET H H 8.548 0.05 1 22 5 5 MET HA H 4.328 0.05 1 23 5 5 MET HB2 H 1.722 0.05 2 24 5 5 MET HB3 H 1.722 0.05 2 25 5 5 MET C C 176.430 0.6 1 26 5 5 MET CA C 55.576 0.6 1 27 5 5 MET CB C 32.872 0.6 1 28 5 5 MET CG C 31.943 0.6 1 29 5 5 MET N N 122.954 0.05 1 30 6 6 ALA H H 8.463 0.05 1 31 6 6 ALA HA H 4.129 0.05 1 32 6 6 ALA HB H 1.051 0.05 2 33 6 6 ALA C C 177.825 0.6 1 34 6 6 ALA CA C 52.963 0.6 1 35 6 6 ALA CB C 19.045 0.6 1 36 6 6 ALA N N 125.362 0.05 1 37 7 7 ASP H H 8.241 0.05 1 38 7 7 ASP HA H 4.431 0.05 1 39 7 7 ASP HB2 H 2.364 0.05 2 40 7 7 ASP HB3 H 2.364 0.05 2 41 7 7 ASP C C 176.563 0.6 1 42 7 7 ASP CA C 54.434 0.6 1 43 7 7 ASP CB C 41.170 0.6 1 44 7 7 ASP N N 120.030 0.05 1 45 8 8 ALA H H 8.299 0.05 1 46 8 8 ALA HA H 4.120 0.05 1 47 8 8 ALA HB H 1.089 0.05 2 48 8 8 ALA C C 178.661 0.6 1 49 8 8 ALA CA C 53.438 0.6 1 50 8 8 ALA CB C 18.814 0.6 1 51 8 8 ALA N N 124.684 0.05 1 52 9 9 LYS H H 8.256 0.05 1 53 9 9 LYS HA H 4.072 0.05 1 54 9 9 LYS HB2 H 1.514 0.05 2 55 9 9 LYS HB3 H 1.514 0.05 2 56 9 9 LYS C C 177.292 0.6 1 57 9 9 LYS CA C 57.223 0.6 1 58 9 9 LYS CB C 32.500 0.6 1 59 9 9 LYS CD C 29.083 0.6 1 60 9 9 LYS CE C 41.810 0.6 1 61 9 9 LYS CG C 25.030 0.6 1 62 9 9 LYS N N 119.684 0.05 1 63 10 10 GLN H H 8.173 0.05 1 64 10 10 GLN HA H 4.120 0.05 1 65 10 10 GLN HB2 H 1.741 0.05 2 66 10 10 GLN HB3 H 1.741 0.05 2 67 10 10 GLN C C 176.697 0.6 1 68 10 10 GLN CA C 56.564 0.6 1 69 10 10 GLN CB C 28.971 0.6 1 70 10 10 GLN CG C 33.491 0.6 1 71 10 10 GLN N N 120.743 0.05 1 72 11 11 LYS H H 8.333 0.05 1 73 11 11 LYS HA H 4.120 0.05 1 74 11 11 LYS HB2 H 1.476 0.05 2 75 11 11 LYS HB3 H 1.476 0.05 2 76 11 11 LYS C C 177.363 0.6 1 77 11 11 LYS CA C 57.047 0.6 1 78 11 11 LYS CB C 32.748 0.6 1 79 11 11 LYS CD C 29.094 0.6 1 80 11 11 LYS CE C 41.604 0.6 1 81 11 11 LYS CG C 24.883 0.6 1 82 11 11 LYS N N 122.420 0.05 1 83 12 12 ARG H H 8.322 0.05 1 84 12 12 ARG HA H 4.148 0.05 1 85 12 12 ARG HB2 H 1.495 0.05 2 86 12 12 ARG HB3 H 1.495 0.05 2 87 12 12 ARG C C 176.741 0.6 1 88 12 12 ARG CA C 56.937 0.6 1 89 12 12 ARG CB C 30.457 0.6 1 90 12 12 ARG CD C 43.090 0.6 1 91 12 12 ARG CG C 27.092 0.6 1 92 12 12 ARG N N 122.083 0.05 1 93 13 13 ASN H H 8.471 0.05 1 94 13 13 ASN HA H 4.516 0.05 1 95 13 13 ASN HB2 H 2.506 0.05 2 96 13 13 ASN HB3 H 2.506 0.05 2 97 13 13 ASN C C 176.172 0.6 1 98 13 13 ASN CA C 54.029 0.6 1 99 13 13 ASN CB C 38.394 0.6 1 100 13 13 ASN N N 119.771 0.05 1 101 14 14 GLU H H 8.390 0.05 1 102 14 14 GLU HA H 4.120 0.05 1 103 14 14 GLU HB2 H 1.712 0.05 2 104 14 14 GLU HB3 H 1.712 0.05 2 105 14 14 GLU C C 177.150 0.6 1 106 14 14 GLU CA C 57.376 0.6 1 107 14 14 GLU CB C 29.899 0.6 1 108 14 14 GLU CG C 36.216 0.6 1 109 14 14 GLU N N 121.516 0.05 1 110 15 15 GLN H H 8.252 0.05 1 111 15 15 GLN HA H 4.120 0.05 1 112 15 15 GLN HB2 H 1.759 0.05 2 113 15 15 GLN HB3 H 1.759 0.05 2 114 15 15 GLN C C 176.572 0.6 1 115 15 15 GLN CA C 56.542 0.6 1 116 15 15 GLN CB C 28.938 0.6 1 117 15 15 GLN CG C 33.563 0.6 1 118 15 15 GLN N N 120.337 0.05 1 119 16 16 LEU H H 8.079 0.05 1 120 16 16 LEU HA H 4.148 0.05 1 121 16 16 LEU HB2 H 1.278 0.05 2 122 16 16 LEU HB3 H 1.278 0.05 2 123 16 16 LEU C C 177.630 0.6 1 124 16 16 LEU CA C 55.664 0.6 1 125 16 16 LEU CB C 42.161 0.6 1 126 16 16 LEU CD1 C 24.821 0.6 2 127 16 16 LEU CD2 C 24.574 0.6 2 128 16 16 LEU CG C 26.679 0.6 1 129 16 16 LEU N N 122.111 0.05 1 130 17 17 LYS H H 8.123 0.05 1 131 17 17 LYS HA H 4.120 0.05 1 132 17 17 LYS HB2 H 1.400 0.05 2 133 17 17 LYS HB3 H 1.400 0.05 2 134 17 17 LYS C C 176.608 0.6 1 135 17 17 LYS CA C 56.564 0.6 1 136 17 17 LYS CB C 32.638 0.6 1 137 17 17 LYS CD C 28.971 0.6 1 138 17 17 LYS CE C 42.037 0.6 1 139 17 17 LYS CG C 24.512 0.6 1 140 17 17 LYS N N 121.540 0.05 1 141 18 18 ARG H H 8.116 0.05 1 142 18 18 ARG HA H 4.148 0.05 1 143 18 18 ARG HB2 H 1.400 0.05 2 144 18 18 ARG HB3 H 1.400 0.05 2 145 18 18 ARG C C 175.968 0.6 1 146 18 18 ARG CA C 56.498 0.6 1 147 18 18 ARG CB C 30.828 0.6 1 148 18 18 ARG CD C 42.842 0.6 1 149 18 18 ARG CG C 26.741 0.6 1 150 18 18 ARG N N 121.675 0.05 1 151 19 19 TRP H H 8.229 0.05 1 152 19 19 TRP HA H 4.573 0.05 1 153 19 19 TRP HB2 H 2.940 0.05 2 154 19 19 TRP HB3 H 2.940 0.05 2 155 19 19 TRP C C 176.234 0.6 1 156 19 19 TRP CA C 57.396 0.6 1 157 19 19 TRP CB C 29.466 0.6 1 158 19 19 TRP N N 122.618 0.05 1 159 20 20 ILE H H 8.029 0.05 1 160 20 20 ILE HA H 3.952 0.05 1 161 20 20 ILE HB H 1.665 0.05 1 162 20 20 ILE C C 176.279 0.6 1 163 20 20 ILE CA C 61.329 0.6 1 164 20 20 ILE CB C 38.755 0.6 1 165 20 20 ILE CD1 C 12.801 0.6 1 166 20 20 ILE CG1 C 27.051 0.6 1 167 20 20 ILE CG2 C 17.138 0.6 1 168 20 20 ILE N N 123.406 0.05 1 169 21 21 GLY H H 7.918 0.05 1 170 21 21 GLY HA2 H 3.488 0.05 2 171 21 21 GLY HA3 H 3.488 0.05 2 172 21 21 GLY C C 173.986 0.6 1 173 21 21 GLY CA C 45.239 0.6 1 174 21 21 GLY N N 112.357 0.05 1 175 22 22 SER H H 8.192 0.05 1 176 22 22 SER HA H 4.356 0.05 1 177 22 22 SER HB2 H 3.770 0.05 2 178 22 22 SER HB3 H 3.714 0.05 2 179 22 22 SER C C 174.946 0.6 1 180 22 22 SER CA C 58.286 0.6 1 181 22 22 SER CB C 63.982 0.6 1 182 22 22 SER N N 115.692 0.05 1 183 23 23 GLU H H 8.732 0.05 1 184 23 23 GLU HA H 4.190 0.05 1 185 23 23 GLU HB2 H 1.991 0.05 2 186 23 23 GLU HB3 H 1.866 0.05 2 187 23 23 GLU C C 176.892 0.6 1 188 23 23 GLU CA C 57.223 0.6 1 189 23 23 GLU CB C 29.899 0.6 1 190 23 23 GLU CG C 36.216 0.6 1 191 23 23 GLU N N 122.895 0.05 1 192 24 24 THR H H 8.058 0.05 1 193 24 24 THR HA H 4.186 0.05 1 194 24 24 THR HB H 4.110 0.05 1 195 24 24 THR C C 174.279 0.6 1 196 24 24 THR CA C 61.975 0.6 1 197 24 24 THR CB C 69.735 0.6 1 198 24 24 THR CG2 C 21.353 0.6 1 199 24 24 THR N N 113.550 0.05 1 200 25 25 ASP H H 8.219 0.05 1 201 25 25 ASP HA H 4.507 0.05 1 202 25 25 ASP HB2 H 2.608 0.05 2 203 25 25 ASP HB3 H 2.514 0.05 2 204 25 25 ASP C C 175.977 0.6 1 205 25 25 ASP CA C 54.423 0.6 1 206 25 25 ASP CB C 40.861 0.6 1 207 25 25 ASP N N 122.861 0.05 1 208 26 26 LEU H H 8.149 0.05 1 209 26 26 LEU HA H 4.205 0.05 1 210 26 26 LEU HB2 H 1.287 0.05 2 211 26 26 LEU HB3 H 1.287 0.05 2 212 26 26 LEU C C 177.319 0.6 1 213 26 26 LEU CA C 54.895 0.6 1 214 26 26 LEU CB C 42.347 0.6 1 215 26 26 LEU CD1 C 24.759 0.6 2 216 26 26 LEU CD2 C 22.902 0.6 2 217 26 26 LEU CG C 26.617 0.6 1 218 26 26 LEU N N 122.313 0.05 1 219 27 27 GLU H H 8.282 0.05 1 220 27 27 GLU C C 173.879 0.6 1 221 27 27 GLU CA C 54.149 0.6 1 222 27 27 GLU CB C 29.652 0.6 1 223 27 27 GLU N N 123.127 0.05 1 224 29 29 PRO HA H 4.328 0.05 1 225 29 29 PRO HB2 H 2.174 0.05 2 226 29 29 PRO HB3 H 1.730 0.05 2 227 29 29 PRO C C 176.901 0.6 1 228 29 29 PRO CA C 62.726 0.6 1 229 29 29 PRO CB C 31.943 0.6 1 230 29 29 PRO CD C 50.026 0.6 1 231 29 29 PRO CG C 27.175 0.6 1 232 30 30 VAL H H 8.280 0.05 1 233 30 30 VAL HA H 3.912 0.05 1 234 30 30 VAL HB H 1.890 0.05 1 235 30 30 VAL C C 176.394 0.6 1 236 30 30 VAL CA C 62.624 0.6 1 237 30 30 VAL CB C 32.438 0.6 1 238 30 30 VAL CG1 C 20.982 0.6 2 239 30 30 VAL CG2 C 21.106 0.6 2 240 30 30 VAL N N 121.242 0.05 1 241 31 31 VAL H H 8.292 0.05 1 242 31 31 VAL HA H 3.940 0.05 1 243 31 31 VAL HB H 1.890 0.05 1 244 31 31 VAL C C 176.048 0.6 1 245 31 31 VAL CA C 62.471 0.6 1 246 31 31 VAL CB C 32.639 0.6 1 247 31 31 VAL CG1 C 21.229 0.6 2 248 31 31 VAL CG2 C 20.858 0.6 2 249 31 31 VAL N N 125.719 0.05 1 250 32 32 LYS H H 8.462 0.05 1 251 32 32 LYS HA H 4.167 0.05 1 252 32 32 LYS HB2 H 1.438 0.05 2 253 32 32 LYS HB3 H 1.438 0.05 2 254 32 32 LYS C C 176.403 0.6 1 255 32 32 LYS CA C 56.235 0.6 1 256 32 32 LYS CB C 32.872 0.6 1 257 32 32 LYS CD C 29.032 0.6 1 258 32 32 LYS CE C 41.604 0.6 1 259 32 32 LYS CG C 24.759 0.6 1 260 32 32 LYS N N 126.529 0.05 1 261 33 33 ARG H H 8.405 0.05 1 262 33 33 ARG HA H 4.328 0.05 1 263 33 33 ARG HB2 H 1.684 0.05 2 264 33 33 ARG HB3 H 1.684 0.05 2 265 33 33 ARG C C 176.323 0.6 1 266 33 33 ARG CA C 56.059 0.6 1 267 33 33 ARG CB C 30.952 0.6 1 268 33 33 ARG CD C 43.090 0.6 1 269 33 33 ARG CG C 27.175 0.6 1 270 33 33 ARG N N 123.404 0.05 1 271 34 34 LYS H H 8.480 0.05 1 272 34 34 LYS HA H 4.186 0.05 1 273 34 34 LYS HB2 H 1.448 0.05 2 274 34 34 LYS HB3 H 1.448 0.05 2 275 34 34 LYS C C 176.599 0.6 1 276 34 34 LYS CA C 56.257 0.6 1 277 34 34 LYS CB C 33.058 0.6 1 278 34 34 LYS CD C 29.218 0.6 1 279 34 34 LYS CE C 41.975 0.6 1 280 34 34 LYS CG C 24.512 0.6 1 281 34 34 LYS N N 124.011 0.05 1 282 35 35 LYS H H 8.517 0.05 1 283 35 35 LYS HA H 4.261 0.05 1 284 35 35 LYS HB2 H 1.467 0.05 2 285 35 35 LYS HB3 H 1.467 0.05 2 286 35 35 LYS C C 176.688 0.6 1 287 35 35 LYS CA C 56.296 0.6 1 288 35 35 LYS CB C 33.110 0.6 1 289 35 35 LYS CD C 29.083 0.6 1 290 35 35 LYS CE C 41.597 0.6 1 291 35 35 LYS CG C 24.746 0.6 1 292 35 35 LYS N N 124.008 0.05 1 293 36 36 THR H H 8.292 0.05 1 294 36 36 THR HA H 4.186 0.05 1 295 36 36 THR HB H 4.054 0.05 1 296 36 36 THR C C 174.261 0.6 1 297 36 36 THR CA C 61.893 0.6 1 298 36 36 THR CB C 69.905 0.6 1 299 36 36 THR CG2 C 21.787 0.6 1 300 36 36 THR N N 117.561 0.05 1 301 37 37 LYS H H 8.498 0.05 1 302 37 37 LYS HA H 4.186 0.05 1 303 37 37 LYS HB2 H 1.419 0.05 2 304 37 37 LYS HB3 H 1.419 0.05 2 305 37 37 LYS C C 176.430 0.6 1 306 37 37 LYS CA C 56.388 0.6 1 307 37 37 LYS CB C 33.094 0.6 1 308 37 37 LYS CD C 29.296 0.6 1 309 37 37 LYS CE C 42.095 0.6 1 310 37 37 LYS CG C 24.532 0.6 1 311 37 37 LYS N N 125.028 0.05 1 312 38 38 VAL H H 8.248 0.05 1 313 38 38 VAL HA H 3.940 0.05 1 314 38 38 VAL HB H 1.900 0.05 1 315 38 38 VAL C C 175.923 0.6 1 316 38 38 VAL CA C 62.164 0.6 1 317 38 38 VAL CB C 32.872 0.6 1 318 38 38 VAL CG1 C 21.168 0.6 2 319 38 38 VAL CG2 C 20.858 0.6 2 320 38 38 VAL N N 122.822 0.05 1 321 39 39 LYS H H 8.452 0.05 1 322 39 39 LYS C C 176.332 0.6 1 323 39 39 LYS CA C 56.219 0.6 1 324 39 39 LYS CB C 32.934 0.6 1 325 39 39 LYS N N 126.162 0.05 1 326 40 40 PHE HA H 4.431 0.05 1 327 40 40 PHE HB2 H 2.713 0.05 2 328 40 40 PHE HB3 H 2.713 0.05 2 329 40 40 PHE C C 175.372 0.6 1 330 40 40 PHE CA C 58.201 0.6 1 331 40 40 PHE CB C 39.622 0.6 1 332 41 41 ASP H H 8.264 0.05 1 333 41 41 ASP HA H 4.460 0.05 1 334 41 41 ASP HB2 H 2.298 0.05 2 335 41 41 ASP HB3 H 2.298 0.05 2 336 41 41 ASP C C 176.697 0.6 1 337 41 41 ASP CA C 53.804 0.6 1 338 41 41 ASP CB C 41.108 0.6 1 339 41 41 ASP N N 124.132 0.05 1 340 42 42 ASP H H 7.208 0.05 1 341 42 42 ASP HA H 4.348 0.05 1 342 42 42 ASP HB2 H 2.205 0.05 2 343 42 42 ASP HB3 H 2.695 0.05 2 344 42 42 ASP C C 177.185 0.6 1 345 42 42 ASP CA C 54.852 0.6 1 346 42 42 ASP CB C 40.704 0.6 1 347 42 42 ASP N N 120.449 0.05 1 348 43 43 GLY H H 8.154 0.05 1 349 43 43 GLY HA2 H 3.044 0.05 2 350 43 43 GLY HA3 H 3.044 0.05 2 351 43 43 GLY C C 174.972 0.6 1 352 43 43 GLY CA C 46.558 0.6 1 353 43 43 GLY N N 109.771 0.05 1 354 44 44 ALA H H 7.904 0.05 1 355 44 44 ALA C C 181.416 0.6 1 356 44 44 ALA CA C 55.576 0.6 1 357 44 44 ALA CB C 18.009 0.6 1 358 44 44 ALA N N 123.123 0.05 1 359 46 46 PHE HA H 4.025 0.05 1 360 46 46 PHE HB2 H 3.185 0.05 2 361 46 46 PHE HB3 H 3.024 0.05 2 362 46 46 PHE C C 177.728 0.6 1 363 46 46 PHE CA C 62.319 0.6 1 364 46 46 PHE CB C 39.089 0.6 1 365 47 47 LEU H H 8.747 0.05 1 366 47 47 LEU HA H 3.742 0.05 1 367 47 47 LEU HB2 H 1.741 0.05 2 368 47 47 LEU HB3 H 1.741 0.05 2 369 47 47 LEU C C 180.421 0.6 1 370 47 47 LEU CA C 58.387 0.6 1 371 47 47 LEU CB C 40.929 0.6 1 372 47 47 LEU CD1 C 26.594 0.6 2 373 47 47 LEU CD2 C 26.168 0.6 2 374 47 47 LEU N N 119.323 0.05 1 375 48 48 ALA H H 8.063 0.05 1 376 48 48 ALA HA H 4.091 0.05 1 377 48 48 ALA HB H 1.164 0.05 2 378 48 48 ALA C C 180.279 0.6 1 379 48 48 ALA CA C 54.857 0.6 1 380 48 48 ALA CB C 17.638 0.6 1 381 48 48 ALA N N 122.484 0.05 1 382 49 49 ALA H H 7.906 0.05 1 383 49 49 ALA HA H 4.016 0.05 1 384 49 49 ALA HB H 0.994 0.05 2 385 49 49 ALA C C 180.474 0.6 1 386 49 49 ALA CA C 54.917 0.6 1 387 49 49 ALA CB C 17.656 0.6 1 388 49 49 ALA N N 123.546 0.05 1 389 50 50 CYS H H 7.762 0.05 1 390 50 50 CYS HA H 3.666 0.05 1 391 50 50 CYS HB2 H 2.487 0.05 2 392 50 50 CYS HB3 H 2.487 0.05 2 393 50 50 CYS C C 178.456 0.6 1 394 50 50 CYS CA C 63.374 0.6 1 395 50 50 CYS CB C 26.874 0.6 1 396 50 50 CYS N N 116.827 0.05 1 397 51 51 SER H H 8.243 0.05 1 398 51 51 SER HA H 4.054 0.05 1 399 51 51 SER HB2 H 3.630 0.05 2 400 51 51 SER HB3 H 3.630 0.05 2 401 51 51 SER C C 176.563 0.6 1 402 51 51 SER CA C 60.999 0.6 1 403 51 51 SER CB C 62.412 0.6 1 404 51 51 SER N N 116.164 0.05 1 405 52 52 SER H H 7.680 0.05 1 406 52 52 SER HA H 4.230 0.05 1 407 52 52 SER HB2 H 3.718 0.05 2 408 52 52 SER HB3 H 3.718 0.05 2 409 52 52 SER C C 175.434 0.6 1 410 52 52 SER CA C 59.749 0.6 1 411 52 52 SER CB C 63.984 0.6 1 412 52 52 SER N N 114.045 0.05 1 413 53 53 GLY H H 7.460 0.05 1 414 53 53 GLY HA2 H 4.072 0.05 2 415 53 53 GLY HA3 H 3.553 0.05 2 416 53 53 GLY C C 173.257 0.6 1 417 53 53 GLY CA C 45.673 0.6 1 418 53 53 GLY N N 108.739 0.05 1 419 54 54 ASP H H 7.536 0.05 1 420 54 54 ASP HA H 4.545 0.05 1 421 54 54 ASP HB2 H 2.826 0.05 2 422 54 54 ASP HB3 H 2.306 0.05 2 423 54 54 ASP C C 175.702 0.6 1 424 54 54 ASP CA C 52.392 0.6 1 425 54 54 ASP CB C 39.571 0.6 1 426 54 54 ASP N N 119.495 0.05 1 427 55 55 THR H H 7.841 0.05 1 428 55 55 THR HA H 3.166 0.05 1 429 55 55 THR HB H 3.005 0.05 1 430 55 55 THR C C 176.137 0.6 1 431 55 55 THR CA C 65.137 0.6 1 432 55 55 THR CB C 67.441 0.6 1 433 55 55 THR CG2 C 21.831 0.6 1 434 55 55 THR N N 116.984 0.05 1 435 56 56 GLU H H 8.036 0.05 1 436 56 56 GLU HA H 3.893 0.05 1 437 56 56 GLU HB2 H 1.759 0.05 2 438 56 56 GLU HB3 H 1.759 0.05 2 439 56 56 GLU C C 179.265 0.6 1 440 56 56 GLU CA C 59.550 0.6 1 441 56 56 GLU CB C 28.971 0.6 1 442 56 56 GLU CG C 36.549 0.6 1 443 56 56 GLU N N 121.119 0.05 1 444 57 57 GLU H H 7.248 0.05 1 445 57 57 GLU HA H 4.205 0.05 1 446 57 57 GLU HB2 H 1.438 0.05 2 447 57 57 GLU HB3 H 1.438 0.05 2 448 57 57 GLU C C 178.385 0.6 1 449 57 57 GLU CA C 57.794 0.6 1 450 57 57 GLU CB C 28.947 0.6 1 451 57 57 GLU CG C 34.049 0.6 1 452 57 57 GLU N N 121.779 0.05 1 453 58 58 VAL H H 7.870 0.05 1 454 58 58 VAL HA H 3.222 0.05 1 455 58 58 VAL HB H 1.938 0.05 1 456 58 58 VAL C C 178.163 0.6 1 457 58 58 VAL CA C 68.109 0.6 1 458 58 58 VAL CB C 31.448 0.6 1 459 58 58 VAL CG1 C 23.025 0.6 2 460 58 58 VAL CG2 C 24.078 0.6 2 461 58 58 VAL N N 119.088 0.05 1 462 59 59 LEU H H 8.328 0.05 1 463 59 59 LEU HA H 4.082 0.05 1 464 59 59 LEU HB2 H 1.872 0.05 2 465 59 59 LEU HB3 H 1.645 0.05 2 466 59 59 LEU C C 179.425 0.6 1 467 59 59 LEU CA C 58.615 0.6 1 468 59 59 LEU CB C 41.542 0.6 1 469 59 59 LEU CD1 C 24.461 0.6 2 470 59 59 LEU CD2 C 24.035 0.6 2 471 59 59 LEU CG C 26.741 0.6 1 472 59 59 LEU N N 118.655 0.05 1 473 60 60 ARG H H 7.712 0.05 1 474 60 60 ARG HA H 3.969 0.05 1 475 60 60 ARG HB2 H 1.947 0.05 2 476 60 60 ARG HB3 H 1.786 0.05 2 477 60 60 ARG C C 179.790 0.6 1 478 60 60 ARG CA C 59.836 0.6 1 479 60 60 ARG CB C 30.705 0.6 1 480 60 60 ARG CD C 43.090 0.6 1 481 60 60 ARG CG C 28.227 0.6 1 482 60 60 ARG N N 120.028 0.05 1 483 61 61 LEU H H 8.219 0.05 1 484 61 61 LEU HA H 3.931 0.05 1 485 61 61 LEU HB2 H 2.145 0.05 2 486 61 61 LEU HB3 H 1.267 0.05 2 487 61 61 LEU C C 181.016 0.6 1 488 61 61 LEU CA C 57.838 0.6 1 489 61 61 LEU CB C 40.675 0.6 1 490 61 61 LEU CD1 C 21.902 0.6 2 491 61 61 LEU CD2 C 21.759 0.6 2 492 61 61 LEU CG C 27.021 0.6 1 493 61 61 LEU N N 118.945 0.05 1 494 62 62 LEU H H 8.864 0.05 1 495 62 62 LEU HA H 3.997 0.05 1 496 62 62 LEU HB2 H 1.268 0.05 2 497 62 62 LEU HB3 H 1.268 0.05 2 498 62 62 LEU C C 173.070 0.6 1 499 62 62 LEU CA C 58.408 0.6 1 500 62 62 LEU CB C 40.861 0.6 1 501 62 62 LEU N N 122.258 0.05 1 502 63 63 GLU H H 8.545 0.05 1 503 63 63 GLU HA H 3.987 0.05 1 504 63 63 GLU HB2 H 2.145 0.05 2 505 63 63 GLU HB3 H 2.098 0.05 2 506 63 63 GLU C C 178.216 0.6 1 507 63 63 GLU CA C 59.315 0.6 1 508 63 63 GLU CB C 29.156 0.6 1 509 63 63 GLU CG C 36.264 0.6 1 510 63 63 GLU N N 122.527 0.05 1 511 64 64 ARG H H 7.331 0.05 1 512 64 64 ARG HA H 4.262 0.05 1 513 64 64 ARG HB2 H 2.116 0.05 2 514 64 64 ARG HB3 H 1.728 0.05 2 515 64 64 ARG C C 176.101 0.6 1 516 64 64 ARG CA C 56.140 0.6 1 517 64 64 ARG CB C 30.799 0.6 1 518 64 64 ARG CD C 43.659 0.6 1 519 64 64 ARG CG C 27.163 0.6 1 520 64 64 ARG N N 116.319 0.05 1 521 65 65 GLY H H 7.594 0.05 1 522 65 65 GLY HA2 H 4.328 0.05 2 523 65 65 GLY HA3 H 3.591 0.05 2 524 65 65 GLY C C 174.635 0.6 1 525 65 65 GLY CA C 45.242 0.6 1 526 65 65 GLY N N 105.845 0.05 1 527 66 66 ALA H H 7.832 0.05 1 528 66 66 ALA HA H 3.676 0.05 1 529 66 66 ALA HB H 0.324 0.05 2 530 66 66 ALA C C 175.434 0.6 1 531 66 66 ALA CA C 52.985 0.6 1 532 66 66 ALA CB C 18.690 0.6 1 533 66 66 ALA N N 123.264 0.05 1 534 67 67 ASP H H 7.940 0.05 1 535 67 67 ASP HA H 4.384 0.05 1 536 67 67 ASP HB2 H 2.656 0.05 2 537 67 67 ASP HB3 H 2.504 0.05 2 538 67 67 ASP C C 176.670 0.6 1 539 67 67 ASP CA C 51.975 0.6 1 540 67 67 ASP CB C 41.170 0.6 1 541 67 67 ASP N N 120.091 0.05 1 542 68 68 ILE H H 8.605 0.05 1 543 68 68 ILE HA H 3.704 0.05 1 544 68 68 ILE HB H 1.626 0.05 1 545 68 68 ILE C C 175.283 0.6 1 546 68 68 ILE CA C 63.151 0.6 1 547 68 68 ILE CB C 38.507 0.6 1 548 68 68 ILE CD1 C 15.718 0.6 1 549 68 68 ILE CG1 C 30.147 0.6 1 550 68 68 ILE CG2 C 18.938 0.6 1 551 68 68 ILE N N 128.214 0.05 1 552 69 69 ASN H H 8.208 0.05 1 553 69 69 ASN HA H 4.894 0.05 1 554 69 69 ASN HB2 H 2.939 0.05 2 555 69 69 ASN HB3 H 2.599 0.05 2 556 69 69 ASN C C 173.941 0.6 1 557 69 69 ASN CA C 53.117 0.6 1 558 69 69 ASN CB C 39.189 0.6 1 559 69 69 ASN N N 118.603 0.05 1 560 70 70 TYR H H 7.384 0.05 1 561 70 70 TYR HA H 3.855 0.05 1 562 70 70 TYR HB2 H 3.128 0.05 2 563 70 70 TYR HB3 H 2.703 0.05 2 564 70 70 TYR C C 173.426 0.6 1 565 70 70 TYR CA C 60.231 0.6 1 566 70 70 TYR CB C 39.314 0.6 1 567 70 70 TYR N N 121.888 0.05 1 568 71 71 ALA H H 7.313 0.05 1 569 71 71 ALA HA H 4.611 0.05 1 570 71 71 ALA HB H 0.654 0.05 2 571 71 71 ALA C C 175.897 0.6 1 572 71 71 ALA CA C 48.813 0.6 1 573 71 71 ALA CB C 21.353 0.6 1 574 71 71 ALA N N 129.104 0.05 1 575 72 72 ASN H H 7.903 0.05 1 576 72 72 ASN C C 174.048 0.6 1 577 72 72 ASN CA C 51.053 0.6 1 578 72 72 ASN CB C 38.384 0.6 1 579 72 72 ASN N N 118.533 0.05 1 580 74 74 ASP H H 7.210 0.05 1 581 74 74 ASP HA H 4.629 0.05 1 582 74 74 ASP HB2 H 2.766 0.05 2 583 74 74 ASP HB3 H 2.503 0.05 2 584 74 74 ASP C C 176.323 0.6 1 585 74 74 ASP CA C 54.434 0.6 1 586 74 74 ASP CB C 41.356 0.6 1 587 74 74 ASP N N 118.743 0.05 1 588 75 75 GLY H H 8.381 0.05 1 589 75 75 GLY HA2 H 4.082 0.05 2 590 75 75 GLY HA3 H 3.449 0.05 2 591 75 75 GLY C C 174.039 0.6 1 592 75 75 GLY CA C 45.080 0.6 1 593 75 75 GLY N N 108.930 0.05 1 594 76 76 LEU H H 7.809 0.05 1 595 76 76 LEU HA H 4.309 0.05 1 596 76 76 LEU HB2 H 1.550 0.05 2 597 76 76 LEU HB3 H 1.399 0.05 2 598 76 76 LEU C C 175.941 0.6 1 599 76 76 LEU CA C 55.510 0.6 1 600 76 76 LEU CB C 42.904 0.6 1 601 76 76 LEU CD1 C 24.512 0.6 2 602 76 76 LEU CD2 C 24.140 0.6 2 603 76 76 LEU CG C 26.617 0.6 1 604 76 76 LEU N N 124.243 0.05 1 605 77 77 THR H H 7.523 0.05 1 606 77 77 THR HA H 5.045 0.05 1 607 77 77 THR HB H 4.866 0.05 1 608 77 77 THR C C 175.381 0.6 1 609 77 77 THR CA C 58.697 0.6 1 610 77 77 THR CB C 72.073 0.6 1 611 77 77 THR CG2 C 21.601 0.6 1 612 77 77 THR N N 114.505 0.05 1 613 78 78 ALA H H 10.435 0.05 1 614 78 78 ALA HA H 3.940 0.05 1 615 78 78 ALA HB H 1.353 0.05 2 616 78 78 ALA C C 181.079 0.6 1 617 78 78 ALA CA C 55.378 0.6 1 618 78 78 ALA CB C 20.115 0.6 1 619 78 78 ALA N N 125.544 0.05 1 620 79 79 LEU H H 9.170 0.05 1 621 79 79 LEU HA H 3.921 0.05 1 622 79 79 LEU HB2 H 1.212 0.05 2 623 79 79 LEU HB3 H 1.212 0.05 2 624 79 79 LEU C C 178.581 0.6 1 625 79 79 LEU CA C 58.035 0.6 1 626 79 79 LEU CB C 41.418 0.6 1 627 79 79 LEU CD1 C 18.690 0.6 2 628 79 79 LEU CD2 C 18.257 0.6 2 629 79 79 LEU CG C 25.315 0.6 1 630 79 79 LEU N N 120.577 0.05 1 631 80 80 HIS H H 7.921 0.05 1 632 80 80 HIS HA H 4.261 0.05 1 633 80 80 HIS HB2 H 2.931 0.05 2 634 80 80 HIS HB3 H 2.931 0.05 2 635 80 80 HIS C C 177.977 0.6 1 636 80 80 HIS CA C 58.848 0.6 1 637 80 80 HIS CB C 30.705 0.6 1 638 80 80 HIS N N 120.486 0.05 1 639 81 81 GLN H H 8.451 0.05 1 640 81 81 GLN HA H 3.714 0.05 1 641 81 81 GLN HB2 H 1.759 0.05 2 642 81 81 GLN HB3 H 1.759 0.05 2 643 81 81 GLN C C 176.937 0.6 1 644 81 81 GLN CA C 58.848 0.6 1 645 81 81 GLN CB C 29.280 0.6 1 646 81 81 GLN CG C 36.216 0.6 1 647 81 81 GLN N N 118.675 0.05 1 648 82 82 ALA H H 8.293 0.05 1 649 82 82 ALA HA H 4.190 0.05 1 650 82 82 ALA HB H 1.127 0.05 2 651 82 82 ALA C C 179.096 0.6 1 652 82 82 ALA CA C 55.104 0.6 1 653 82 82 ALA CB C 18.009 0.6 1 654 82 82 ALA N N 120.582 0.05 1 655 83 83 SER H H 7.987 0.05 1 656 83 83 SER HA H 4.186 0.05 1 657 83 83 SER HB2 H 3.412 0.05 2 658 83 83 SER HB3 H 3.412 0.05 2 659 83 83 SER C C 178.599 0.6 1 660 83 83 SER CA C 61.812 0.6 1 661 83 83 SER CB C 62.721 0.6 1 662 83 83 SER N N 113.679 0.05 1 663 84 84 ILE H H 8.260 0.05 1 664 84 84 ILE HA H 3.836 0.05 1 665 84 84 ILE HB H 1.815 0.05 1 666 84 84 ILE C C 178.003 0.6 1 667 84 84 ILE CA C 64.641 0.6 1 668 84 84 ILE CB C 37.517 0.6 1 669 84 84 ILE CD1 C 12.872 0.6 1 670 84 84 ILE CG1 C 24.871 0.6 1 671 84 84 ILE CG2 C 17.067 0.6 1 672 84 84 ILE N N 124.658 0.05 1 673 85 85 ASP H H 7.830 0.05 1 674 85 85 ASP HA H 4.422 0.05 1 675 85 85 ASP HB2 H 2.684 0.05 2 676 85 85 ASP HB3 H 2.552 0.05 2 677 85 85 ASP C C 175.434 0.6 1 678 85 85 ASP CA C 54.919 0.6 1 679 85 85 ASP CB C 39.808 0.6 1 680 85 85 ASP N N 119.091 0.05 1 681 86 86 ASP H H 7.890 0.05 1 682 86 86 ASP HA H 4.186 0.05 1 683 86 86 ASP HB2 H 3.052 0.05 2 684 86 86 ASP HB3 H 2.363 0.05 2 685 86 86 ASP C C 174.901 0.6 1 686 86 86 ASP CA C 55.049 0.6 1 687 86 86 ASP CB C 39.808 0.6 1 688 86 86 ASP N N 119.769 0.05 1 689 87 87 ASN H H 8.328 0.05 1 690 87 87 ASN HA H 4.819 0.05 1 691 87 87 ASN HB2 H 3.071 0.05 2 692 87 87 ASN HB3 H 2.467 0.05 2 693 87 87 ASN C C 175.488 0.6 1 694 87 87 ASN CA C 51.141 0.6 1 695 87 87 ASN CB C 36.681 0.6 1 696 87 87 ASN N N 116.496 0.05 1 697 88 88 VAL H H 7.642 0.05 1 698 88 88 VAL HA H 3.525 0.05 1 699 88 88 VAL HB H 2.013 0.05 1 700 88 88 VAL C C 178.323 0.6 1 701 88 88 VAL CA C 65.818 0.6 1 702 88 88 VAL CB C 31.757 0.6 1 703 88 88 VAL CG1 C 21.262 0.6 2 704 88 88 VAL CG2 C 20.906 0.6 2 705 88 88 VAL N N 121.409 0.05 1 706 89 89 ASP H H 8.558 0.05 1 707 89 89 ASP HA H 4.403 0.05 1 708 89 89 ASP HB2 H 2.392 0.05 2 709 89 89 ASP HB3 H 2.392 0.05 2 710 89 89 ASP C C 179.416 0.6 1 711 89 89 ASP CA C 57.442 0.6 1 712 89 89 ASP CB C 39.994 0.6 1 713 89 89 ASP N N 120.819 0.05 1 714 90 90 MET H H 7.535 0.05 1 715 90 90 MET HA H 4.139 0.05 1 716 90 90 MET HB2 H 1.958 0.05 2 717 90 90 MET HB3 H 1.958 0.05 2 718 90 90 MET C C 178.039 0.6 1 719 90 90 MET CA C 55.248 0.6 1 720 90 90 MET CB C 29.749 0.6 1 721 90 90 MET CG C 31.501 0.6 1 722 90 90 MET N N 120.787 0.05 1 723 91 91 VAL H H 8.344 0.05 1 724 91 91 VAL HA H 3.288 0.05 1 725 91 91 VAL HB H 2.032 0.05 1 726 91 91 VAL C C 176.962 0.6 1 727 91 91 VAL CA C 68.109 0.6 1 728 91 91 VAL CB C 31.724 0.6 1 729 91 91 VAL CG1 C 22.902 0.6 2 730 91 91 VAL CG2 C 20.796 0.6 2 731 91 91 VAL N N 121.538 0.05 1 732 92 92 LYS H H 7.665 0.05 1 733 92 92 LYS HA H 3.676 0.05 1 734 92 92 LYS HB2 H 1.599 0.05 2 735 92 92 LYS HB3 H 1.599 0.05 2 736 92 92 LYS C C 178.528 0.6 1 737 92 92 LYS CA C 59.841 0.6 1 738 92 92 LYS CB C 32.754 0.6 1 739 92 92 LYS CD C 29.652 0.6 1 740 92 92 LYS CE C 41.790 0.6 1 741 92 92 LYS CG C 28.289 0.6 1 742 92 92 LYS N N 116.461 0.05 1 743 93 93 PHE H H 7.830 0.05 1 744 93 93 PHE HA H 4.167 0.05 1 745 93 93 PHE HB2 H 3.006 0.05 2 746 93 93 PHE HB3 H 3.006 0.05 2 747 93 93 PHE C C 178.225 0.6 1 748 93 93 PHE CA C 61.285 0.6 1 749 93 93 PHE CB C 39.808 0.6 1 750 93 93 PHE N N 119.091 0.05 1 751 94 94 LEU H H 9.003 0.05 1 752 94 94 LEU HA H 3.817 0.05 1 753 94 94 LEU HB2 H 1.975 0.05 2 754 94 94 LEU HB3 H 1.125 0.05 2 755 94 94 LEU C C 179.816 0.6 1 756 94 94 LEU CA C 58.189 0.6 1 757 94 94 LEU CB C 40.427 0.6 1 758 94 94 LEU CD1 C 22.186 0.6 2 759 94 94 LEU CD2 C 21.831 0.6 2 760 94 94 LEU CG C 26.741 0.6 1 761 94 94 LEU N N 121.532 0.05 1 762 95 95 VAL H H 8.692 0.05 1 763 95 95 VAL HA H 4.110 0.05 1 764 95 95 VAL HB H 2.164 0.05 1 765 95 95 VAL C C 181.203 0.6 1 766 95 95 VAL CA C 67.180 0.6 1 767 95 95 VAL CB C 31.695 0.6 1 768 95 95 VAL CG1 C 23.521 0.6 2 769 95 95 VAL CG2 C 21.168 0.6 2 770 95 95 VAL N N 121.694 0.05 1 771 96 96 GLU H H 8.279 0.05 1 772 96 96 GLU HA H 3.940 0.05 1 773 96 96 GLU HB2 H 2.042 0.05 2 774 96 96 GLU HB3 H 1.834 0.05 2 775 96 96 GLU C C 177.221 0.6 1 776 96 96 GLU CA C 59.068 0.6 1 777 96 96 GLU CB C 28.847 0.6 1 778 96 96 GLU CG C 36.407 0.6 1 779 96 96 GLU N N 120.978 0.05 1 780 97 97 ASN H H 7.175 0.05 1 781 97 97 ASN HA H 4.501 0.05 1 782 97 97 ASN HB2 H 2.552 0.05 2 783 97 97 ASN HB3 H 1.869 0.05 2 784 97 97 ASN C C 173.275 0.6 1 785 97 97 ASN CA C 54.172 0.6 1 786 97 97 ASN CB C 39.782 0.6 1 787 97 97 ASN N N 115.376 0.05 1 788 98 98 GLY H H 7.433 0.05 1 789 98 98 GLY HA2 H 3.969 0.05 2 790 98 98 GLY HA3 H 3.817 0.05 2 791 98 98 GLY C C 174.759 0.6 1 792 98 98 GLY CA C 45.761 0.6 1 793 98 98 GLY N N 104.790 0.05 1 794 99 99 ALA H H 8.269 0.05 1 795 99 99 ALA HA H 4.365 0.05 1 796 99 99 ALA HB H 0.956 0.05 2 797 99 99 ALA C C 176.661 0.6 1 798 99 99 ALA CA C 52.441 0.6 1 799 99 99 ALA CB C 20.734 0.6 1 800 99 99 ALA N N 124.475 0.05 1 801 100 100 ASN H H 8.599 0.05 1 802 100 100 ASN C C 179.079 0.6 1 803 100 100 ASN CA C 54.733 0.6 1 804 100 100 ASN CB C 41.232 0.6 1 805 100 100 ASN N N 125.835 0.05 1 stop_ save_