data_19197 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; C-terminal structure of (Y81F)-EhCaBP1 ; _BMRB_accession_number 19197 _BMRB_flat_file_name bmr19197.str _Entry_type original _Submission_date 2013-04-26 _Accession_date 2013-04-26 _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 Chary Kandala R. . 2 Rout Ashok K. . 3 Patel Sunita . . 4 Bhattacharya Alok . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 303 "13C chemical shifts" 266 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-10-11 update BMRB 'update entry citation' 2013-06-17 origianl author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19193 'N-terminal domain of (Y81F)-EhCaBP1' 19196 'N-terminal domain of (Y81F)-EhCaBP1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Functional manipulation of a calcium-binding protein from Entamoeba histolytica guided by paramagnetic NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23782698 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rout Ashok K. . 2 Patel Sunita . . 3 Somlata . . . 4 Shukla Manish . . 5 Saraswathi Deepa . . 6 Bhattacharya Alok V.R. . 7 Chary Kandala . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 23473 _Page_last 23487 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C-terminal structure of (Y81F)-EhCaBP1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal structure of (Y81F)-EhCaBP1' $(Y81F)-EhCaBP1 'Calcium ions' $entity_CA 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_(Y81F)-EhCaBP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common (Y81F)-EhCaBP1 _Molecular_mass 7592.673 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; MAEALFKEIDVNGDGAVSYE EVKAFVSKKRAIKNEQLLQL IFKSIDADGNGEIDQNEFAK FYGSIQGQDLSDDKIGLKVL FKLMDVDGDGKLTKEEVTSF FKKHGIEKVAEQVMKADANG DGYITLEEFLEFSL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 GLU 4 4 ALA 5 5 LEU 6 6 PHE 7 7 LYS 8 8 GLU 9 9 ILE 10 10 ASP 11 11 VAL 12 12 ASN 13 13 GLY 14 14 ASP 15 15 GLY 16 16 ALA 17 17 VAL 18 18 SER 19 19 TYR 20 20 GLU 21 21 GLU 22 22 VAL 23 23 LYS 24 24 ALA 25 25 PHE 26 26 VAL 27 27 SER 28 28 LYS 29 29 LYS 30 30 ARG 31 31 ALA 32 32 ILE 33 33 LYS 34 34 ASN 35 35 GLU 36 36 GLN 37 37 LEU 38 38 LEU 39 39 GLN 40 40 LEU 41 41 ILE 42 42 PHE 43 43 LYS 44 44 SER 45 45 ILE 46 46 ASP 47 47 ALA 48 48 ASP 49 49 GLY 50 50 ASN 51 51 GLY 52 52 GLU 53 53 ILE 54 54 ASP 55 55 GLN 56 56 ASN 57 57 GLU 58 58 PHE 59 59 ALA 60 60 LYS 61 61 PHE 62 62 TYR 63 63 GLY 64 64 SER 65 65 ILE 66 66 GLN 67 67 GLY 68 68 GLN 69 69 ASP 70 70 LEU 71 71 SER 72 72 ASP 73 73 ASP 74 74 LYS 75 75 ILE 76 76 GLY 77 77 LEU 78 78 LYS 79 79 VAL 80 80 LEU 81 81 PHE 82 82 LYS 83 83 LEU 84 84 MET 85 85 ASP 86 86 VAL 87 87 ASP 88 88 GLY 89 89 ASP 90 90 GLY 91 91 LYS 92 92 LEU 93 93 THR 94 94 LYS 95 95 GLU 96 96 GLU 97 97 VAL 98 98 THR 99 99 SER 100 100 PHE 101 101 PHE 102 102 LYS 103 103 LYS 104 104 HIS 105 105 GLY 106 106 ILE 107 107 GLU 108 108 LYS 109 109 VAL 110 110 ALA 111 111 GLU 112 112 GLN 113 113 VAL 114 114 MET 115 115 LYS 116 116 ALA 117 117 ASP 118 118 ALA 119 119 ASN 120 120 GLY 121 121 ASP 122 122 GLY 123 123 TYR 124 124 ILE 125 125 THR 126 126 LEU 127 127 GLU 128 128 GLU 129 129 PHE 130 130 LEU 131 131 GLU 132 132 PHE 133 133 SER 134 134 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4271 "Entamoeba Histolytica CaBP" 100.00 134 99.25 100.00 4.49e-86 PDB 1JFJ "Nmr Solution Structure Of An Ef-Hand Calcium Binding Protein From Entamoeba Histolytica" 99.25 134 99.25 100.00 4.80e-85 PDB 1JFK "Minimum Energy Representative Structure Of A Calcium Bound Ef-hand Protein From Entamoeba Histolytica" 99.25 134 99.25 100.00 4.80e-85 PDB 2M7N "C-terminal Structure Of (y81f)-ehcabp1" 100.00 134 100.00 100.00 2.41e-86 PDB 2NXQ "Crystal Structure Of Calcium Binding Protein 1 From Entamoeba Histolytica: A Novel Arrangement Of Ef Hand Motifs" 100.00 134 99.25 100.00 4.49e-86 PDB 3PX1 "Structure Of Calcium Binding Protein-1 From Entamoeba Histolytica In Complex With Strontium" 100.00 134 99.25 100.00 4.49e-86 PDB 3QJK "Structure Of Calcium Binding Protein-1 From Entamoeba Histolytica In Complex With Lead" 100.00 134 99.25 100.00 4.49e-86 PDB 3ULG "Crystal Structure Of Calcium-Binding Protein-1 From Entamoeba Histolytica In Complex With Barium" 100.00 134 99.25 100.00 4.49e-86 DBJ BAN39246 "calcium-binding protein 1 (EhCBP1) [Entamoeba histolytica]" 100.00 134 99.25 100.00 4.49e-86 GB AAA29089 "calcium-binding protein 1 [Entamoeba histolytica]" 100.00 134 98.51 99.25 3.53e-85 GB EAL48959 "calcium-binding protein 1 (EhCBP1) [Entamoeba histolytica HM-1:IMSS]" 100.00 134 99.25 100.00 4.49e-86 GB EKE39141 "calcium-binding protein 1 (EhCBP1), putative [Entamoeba nuttalli P19]" 100.00 134 97.76 99.25 1.20e-84 GB EMD43507 "calcium binding protein, putative [Entamoeba histolytica KU27]" 100.00 134 99.25 100.00 4.49e-86 GB EMH75928 "calcium-binding protein 1 (EhCBP1), putative [Entamoeba histolytica HM-1:IMSS-B]" 100.00 134 99.25 100.00 4.49e-86 REF XP_008858522 "calcium-binding protein 1 (EhCBP1), putative [Entamoeba nuttalli P19]" 100.00 134 97.76 99.25 1.20e-84 REF XP_654345 "calcium-binding protein 1 (EhCBP1) [Entamoeba histolytica HM-1:IMSS]" 100.00 134 99.25 100.00 4.49e-86 SP P38505 "RecName: Full=Calcium-binding protein; Short=CABP" 100.00 134 99.25 100.00 4.49e-86 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state 'not present' _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 $(Y81F)-EhCaBP1 Eukaryotes 5759 Eukaryota . Entamoeba histolytica 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 $(Y81F)-EhCaBP1 'recombinant technology' . Escherichia coli . pET30a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details u-15N,(Y81F)-EhCaBP1 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $(Y81F)-EhCaBP1 0.8 mM '[U-99% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details u-15N/13C,(Y81F)-EhCaBP1 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $(Y81F)-EhCaBP1 0.8 mM '[U-99% 13C; U-99% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details u-15N/13C,(Y81F)-EhCaBP1 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $(Y81F)-EhCaBP1 0.8 mM '[U-99% 13C; U-99% 15N]' D2O 100 % '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 'data analysis' processing stop_ _Details . save_ save_Felix _Saveframe_category software _Name FELIX _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'data analysis' 'peak picking' 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' 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_3 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_1H-15N_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_3 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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' 0.05 . M pH 7.4 . pH pressure 1 . atm temperature 298 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCACB' '3D 1H-15N TOCSY' '3D HCCH-TOCSY' '3D 1H-13C NOESY' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 $sample_3 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'C-terminal structure of (Y81F)-EhCaBP1' _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 67 67 GLY H H 8.675 0.02 1 2 67 67 GLY HA2 H 4.410 0.02 1 3 67 67 GLY HA3 H 4.0000 0.02 1 4 67 67 GLY C C 174.410 0.30 1 5 67 67 GLY CA C 45.770 0.30 1 6 67 67 GLY N N 113.075 0.30 1 7 68 68 GLN H H 7.541 0.02 1 8 68 68 GLN HA H 4.410 0.02 1 9 68 68 GLN HB2 H 1.861 0.02 2 10 68 68 GLN HG2 H 2.520 0.02 1 11 68 68 GLN CA C 54.661 0.30 1 12 68 68 GLN CB C 29.902 0.30 1 13 68 68 GLN CG C 33.278 0.30 1 14 68 68 GLN N N 117.838 0.30 1 15 69 69 ASP H H 8.592 0.02 1 16 69 69 ASP HA H 4.720 0.02 1 17 69 69 ASP HB2 H 2.931 0.02 2 18 69 69 ASP HB3 H 2.720 0.02 2 19 69 69 ASP C C 176.940 0.30 1 20 69 69 ASP CA C 53.310 0.30 1 21 69 69 ASP CB C 42.394 0.30 1 22 69 69 ASP N N 122.499 0.30 1 23 70 70 LEU H H 8.773 0.02 1 24 70 70 LEU HA H 4.182 0.02 1 25 70 70 LEU HB2 H 1.810 0.02 2 26 70 70 LEU HB3 H 1.640 0.02 2 27 70 70 LEU HG H 1.630 0.02 1 28 70 70 LEU HD1 H 0.920 0.02 2 29 70 70 LEU HD2 H 0.840 0.02 2 30 70 70 LEU C C 176.300 0.30 1 31 70 70 LEU CA C 57.024 0.30 1 32 70 70 LEU CB C 41.719 0.30 1 33 70 70 LEU CG C 25.625 0.30 1 34 70 70 LEU CD1 C 23.825 0.30 1 35 70 70 LEU CD2 C 21.912 0.30 1 36 70 70 LEU N N 125.492 0.30 1 37 71 71 SER H H 8.622 0.02 1 38 71 71 SER HA H 4.360 0.02 1 39 71 71 SER HB2 H 4.040 0.02 2 40 71 71 SER HB3 H 4.020 0.02 2 41 71 71 SER C C 174.400 0.30 1 42 71 71 SER CA C 58.712 0.30 1 43 71 71 SER CB C 64.114 0.30 1 44 71 71 SER N N 112.915 0.30 1 45 72 72 ASP H H 7.336 0.02 1 46 72 72 ASP HA H 4.520 0.02 1 47 72 72 ASP HB2 H 3.040 0.02 2 48 72 72 ASP HB3 H 2.920 0.02 2 49 72 72 ASP C C 178.350 0.30 1 50 72 72 ASP CA C 54.436 0.30 1 51 72 72 ASP CB C 40.368 0.30 1 52 72 72 ASP N N 124.071 0.30 1 53 73 73 ASP H H 8.795 0.02 1 54 73 73 ASP HA H 4.620 0.02 1 55 73 73 ASP HB2 H 2.780 0.02 2 56 73 73 ASP C C 178.210 0.30 1 57 73 73 ASP CA C 58.375 0.30 1 58 73 73 ASP CB C 41.381 0.30 1 59 73 73 ASP N N 128.287 0.30 1 60 74 74 LYS H H 8.728 0.02 1 61 74 74 LYS HA H 4.740 0.02 1 62 74 74 LYS HB2 H 2.280 0.02 2 63 74 74 LYS HB3 H 1.880 0.02 2 64 74 74 LYS C C 177.320 0.30 1 65 74 74 LYS CA C 54.998 0.30 1 66 74 74 LYS CB C 33.616 0.30 1 67 74 74 LYS N N 117.169 0.30 1 68 75 75 ILE H H 8.196 0.02 1 69 75 75 ILE HA H 4.120 0.02 1 70 75 75 ILE HB H 2.090 0.02 1 71 75 75 ILE HG12 H 1.340 0.02 2 72 75 75 ILE HG2 H 0.840 0.02 1 73 75 75 ILE HD1 H 0.760 0.02 1 74 75 75 ILE C C 175.620 0.30 1 75 75 75 ILE CA C 62.088 0.30 1 76 75 75 ILE CB C 39.243 0.30 1 77 75 75 ILE CG1 C 29.452 0.30 1 78 75 75 ILE CG2 C 18.760 0.30 1 79 75 75 ILE CD1 C 14.596 0.30 1 80 75 75 ILE N N 119.472 0.30 1 81 76 76 GLY H H 8.632 0.02 1 82 76 76 GLY HA2 H 3.730 0.02 1 83 76 76 GLY C C 174.780 0.30 1 84 76 76 GLY CA C 48.246 0.30 1 85 76 76 GLY N N 108.770 0.30 1 86 77 77 LEU H H 7.553 0.02 1 87 77 77 LEU HA H 4.380 0.02 1 88 77 77 LEU HB2 H 2.000 0.02 2 89 77 77 LEU HB3 H 1.680 0.02 2 90 77 77 LEU HG H 1.630 0.02 1 91 77 77 LEU HD1 H 0.860 0.02 2 92 77 77 LEU C C 179.100 0.30 1 93 77 77 LEU CA C 58.262 0.30 1 94 77 77 LEU CB C 42.732 0.30 1 95 77 77 LEU CG C 26.751 0.30 1 96 77 77 LEU CD1 C 22.137 0.30 1 97 77 77 LEU N N 120.431 0.30 1 98 78 78 LYS H H 7.986 0.02 1 99 78 78 LYS HA H 4.100 0.02 1 100 78 78 LYS HB2 H 2.010 0.02 2 101 78 78 LYS HG2 H 1.520 0.02 1 102 78 78 LYS HD2 H 1.430 0.02 1 103 78 78 LYS HE2 H 2.860 0.02 1 104 78 78 LYS C C 179.440 0.30 1 105 78 78 LYS CA C 59.950 0.30 1 106 78 78 LYS CB C 32.940 0.30 1 107 78 78 LYS CG C 25.063 0.30 1 108 78 78 LYS CD C 28.101 0.30 1 109 78 78 LYS CE C 41.494 0.30 1 110 78 78 LYS N N 118.942 0.30 1 111 79 79 VAL H H 8.421 0.02 1 112 79 79 VAL HA H 3.690 0.02 1 113 79 79 VAL HB H 2.276 0.02 1 114 79 79 VAL HG1 H 0.840 0.02 2 115 79 79 VAL HG2 H 0.790 0.02 2 116 79 79 VAL C C 175.280 0.30 1 117 79 79 VAL CA C 66.590 0.30 1 118 79 79 VAL CB C 33.503 0.30 1 119 79 79 VAL CG1 C 23.487 0.30 1 120 79 79 VAL CG2 C 22.137 0.30 1 121 79 79 VAL N N 118.826 0.30 1 122 80 80 LEU H H 8.285 0.02 1 123 80 80 LEU HA H 3.960 0.02 1 124 80 80 LEU HB2 H 2.090 0.02 2 125 80 80 LEU HB3 H 1.830 0.02 2 126 80 80 LEU HG H 1.630 0.02 1 127 80 80 LEU HD1 H 0.860 0.02 2 128 80 80 LEU HD2 H 0.840 0.02 2 129 80 80 LEU C C 177.680 0.30 1 130 80 80 LEU CA C 59.838 0.30 1 131 80 80 LEU CB C 42.169 0.30 1 132 80 80 LEU CG C 29.452 0.30 1 133 80 80 LEU CD1 C 26.976 0.30 1 134 80 80 LEU CD2 C 24.387 0.30 1 135 80 80 LEU N N 119.941 0.30 1 136 81 81 PHE H H 8.378 0.02 1 137 81 81 PHE HA H 4.120 0.02 1 138 81 81 PHE HB2 H 3.120 0.02 2 139 81 81 PHE C C 176.900 0.30 1 140 81 81 PHE CA C 63.777 0.30 1 141 81 81 PHE CB C 39.243 0.30 1 142 81 81 PHE N N 117.668 0.30 1 143 82 82 LYS H H 7.193 0.02 1 144 82 82 LYS HA H 4.060 0.02 1 145 82 82 LYS HB2 H 2.210 0.02 2 146 82 82 LYS HG2 H 1.410 0.02 1 147 82 82 LYS HD2 H 1.590 0.02 1 148 82 82 LYS HE2 H 2.760 0.02 1 149 82 82 LYS C C 179.290 0.30 1 150 82 82 LYS CA C 57.924 0.30 1 151 82 82 LYS CB C 32.040 0.30 1 152 82 82 LYS CG C 25.288 0.30 1 153 82 82 LYS CD C 29.227 0.30 1 154 82 82 LYS CE C 42.056 0.30 1 155 82 82 LYS N N 115.480 0.30 1 156 83 83 LEU H H 7.820 0.02 1 157 83 83 LEU HA H 4.080 0.02 1 158 83 83 LEU HB2 H 1.930 0.02 2 159 83 83 LEU HB3 H 1.540 0.02 2 160 83 83 LEU HG H 1.680 0.02 1 161 83 83 LEU HD1 H 0.900 0.02 2 162 83 83 LEU HD2 H 0.860 0.02 2 163 83 83 LEU C C 179.200 0.30 1 164 83 83 LEU CA C 56.912 0.30 1 165 83 83 LEU CB C 41.268 0.30 1 166 83 83 LEU CG C 26.076 0.30 1 167 83 83 LEU CD1 C 23.262 0.30 1 168 83 83 LEU CD2 C 21.574 0.30 1 169 83 83 LEU N N 117.939 0.30 1 170 84 84 MET H H 7.235 0.02 1 171 84 84 MET HA H 3.650 0.02 1 172 84 84 MET HB2 H 1.460 0.02 2 173 84 84 MET HG2 H 2.430 0.02 1 174 84 84 MET HE H 1.920 0.02 1 175 84 84 MET C C 177.300 0.30 1 176 84 84 MET CA C 56.011 0.30 1 177 84 84 MET CB C 33.728 0.30 1 178 84 84 MET CG C 31.027 0.30 1 179 84 84 MET CE C 18.198 0.30 1 180 84 84 MET N N 115.860 0.30 1 181 85 85 ASP H H 7.355 0.02 1 182 85 85 ASP HA H 4.490 0.02 1 183 85 85 ASP HB2 H 2.060 0.02 2 184 85 85 ASP HB3 H 1.810 0.02 2 185 85 85 ASP C C 178.260 0.30 1 186 85 85 ASP CA C 52.523 0.30 1 187 85 85 ASP CB C 38.342 0.30 1 188 85 85 ASP N N 119.176 0.30 1 189 86 86 VAL H H 7.643 0.02 1 190 86 86 VAL HA H 3.800 0.02 1 191 86 86 VAL HB H 2.410 0.02 1 192 86 86 VAL HG1 H 0.890 0.02 2 193 86 86 VAL HG2 H 0.850 0.02 2 194 86 86 VAL C C 177.600 0.30 1 195 86 86 VAL CA C 65.690 0.30 1 196 86 86 VAL CB C 32.040 0.30 1 197 86 86 VAL CG1 C 21.799 0.30 1 198 86 86 VAL CG2 C 20.899 0.30 1 199 86 86 VAL N N 122.922 0.30 1 200 87 87 ASP H H 7.649 0.02 1 201 87 87 ASP HA H 4.620 0.02 1 202 87 87 ASP HB2 H 3.210 0.02 2 203 87 87 ASP C C 177.810 0.30 1 204 87 87 ASP CA C 52.973 0.30 1 205 87 87 ASP CB C 39.580 0.30 1 206 87 87 ASP N N 115.678 0.30 1 207 88 88 GLY H H 7.591 0.02 1 208 88 88 GLY HA2 H 3.880 0.02 1 209 88 88 GLY HA3 H 4.120 0.02 1 210 88 88 GLY C C 174.860 0.30 1 211 88 88 GLY CA C 47.458 0.30 1 212 88 88 GLY N N 108.707 0.30 1 213 89 89 ASP H H 8.023 0.02 1 214 89 89 ASP HA H 4.462 0.02 1 215 89 89 ASP HB2 H 2.980 0.02 2 216 89 89 ASP HB3 H 2.400 0.02 2 217 89 89 ASP C C 177.780 0.30 1 218 89 89 ASP CA C 51.847 0.30 1 219 89 89 ASP CB C 40.031 0.30 1 220 89 89 ASP N N 119.699 0.30 1 221 90 90 GLY H H 10.547 0.02 1 222 90 90 GLY HA2 H 4.120 0.02 1 223 90 90 GLY HA3 H 3.740 0.02 1 224 90 90 GLY C C 174.210 0.30 1 225 90 90 GLY CA C 47.571 0.30 1 226 90 90 GLY N N 113.310 0.30 1 227 91 91 LYS H H 7.900 0.02 1 228 91 91 LYS HA H 4.470 0.02 1 229 91 91 LYS HB2 H 1.690 0.02 2 230 91 91 LYS HG2 H 1.390 0.02 1 231 91 91 LYS HD2 H 1.562 0.02 1 232 91 91 LYS C C 174.360 0.30 1 233 91 91 LYS CA C 54.661 0.30 1 234 91 91 LYS CB C 42.056 0.30 1 235 91 91 LYS CG C 24.162 0.30 1 236 91 91 LYS CD C 28.889 0.30 1 237 91 91 LYS N N 118.427 0.30 1 238 92 92 LEU H H 9.473 0.02 1 239 92 92 LEU HA H 5.460 0.02 1 240 92 92 LEU HB2 H 1.710 0.02 2 241 92 92 LEU HB3 H 1.410 0.02 2 242 92 92 LEU HG H 1.480 0.02 1 243 92 92 LEU HD1 H 0.750 0.02 2 244 92 92 LEU HD2 H 0.720 0.02 2 245 92 92 LEU C C 177.570 0.30 1 246 92 92 LEU CA C 53.198 0.30 1 247 92 92 LEU CB C 42.844 0.30 1 248 92 92 LEU CG C 25.513 0.30 1 249 92 92 LEU CD1 C 22.699 0.30 1 250 92 92 LEU CD2 C 20.674 0.30 1 251 92 92 LEU N N 124.021 0.30 1 252 93 93 THR H H 8.520 0.02 1 253 93 93 THR HA H 4.820 0.02 1 254 93 93 THR HB H 4.460 0.02 1 255 93 93 THR HG1 H 5.360 0.02 1 256 93 93 THR HG2 H 1.320 0.02 1 257 93 93 THR C C 175.360 0.30 1 258 93 93 THR CA C 66.703 0.30 1 259 93 93 THR CB C 71.767 0.30 1 260 93 93 THR CG2 C 22.474 0.30 1 261 93 93 THR N N 113.350 0.30 1 262 94 94 LYS H H 9.155 0.02 1 263 94 94 LYS HA H 4.350 0.02 1 264 94 94 LYS HB2 H 1.950 0.02 2 265 94 94 LYS HG2 H 1.420 0.02 1 266 94 94 LYS HD3 H 1.590 0.02 1 267 94 94 LYS C C 174.423 0.30 1 268 94 94 LYS CA C 59.838 0.30 1 269 94 94 LYS CB C 42.281 0.30 1 270 94 94 LYS CG C 25.400 0.30 1 271 94 94 LYS CD C 29.452 0.30 1 272 94 94 LYS N N 121.340 0.30 1 273 95 95 GLU H H 8.571 0.02 1 274 95 95 GLU HA H 4.230 0.02 1 275 95 95 GLU HB2 H 2.100 0.02 2 276 95 95 GLU HB3 H 2.030 0.02 2 277 95 95 GLU HG2 H 2.210 0.02 1 278 95 95 GLU C C 179.560 0.30 1 279 95 95 GLU CA C 60.400 0.30 1 280 95 95 GLU CB C 29.452 0.30 1 281 95 95 GLU CG C 36.767 0.30 1 282 95 95 GLU N N 119.826 0.30 1 283 96 96 GLU H H 7.881 0.02 1 284 96 96 GLU HA H 4.080 0.02 1 285 96 96 GLU HB2 H 2.290 0.02 2 286 96 96 GLU HB3 H 2.180 0.02 2 287 96 96 GLU HG2 H 2.460 0.02 1 288 96 96 GLU C C 180.250 0.30 1 289 96 96 GLU CA C 59.950 0.30 1 290 96 96 GLU CB C 30.127 0.30 1 291 96 96 GLU CG C 33.841 0.30 1 292 96 96 GLU N N 121.545 0.30 1 293 97 97 VAL H H 8.241 0.02 1 294 97 97 VAL HA H 3.730 0.02 1 295 97 97 VAL HB H 2.360 0.02 1 296 97 97 VAL HG1 H 0.890 0.02 2 297 97 97 VAL HG2 H 0.860 0.02 2 298 97 97 VAL C C 177.850 0.30 1 299 97 97 VAL CA C 66.928 0.30 1 300 97 97 VAL CB C 33.053 0.30 1 301 97 97 VAL CG1 C 23.825 0.30 1 302 97 97 VAL CG2 C 22.362 0.30 1 303 97 97 VAL N N 119.926 0.30 1 304 98 98 THR H H 8.784 0.02 1 305 98 98 THR HA H 4.330 0.02 1 306 98 98 THR HB H 3.970 0.02 1 307 98 98 THR HG1 H 5.460 0.02 1 308 98 98 THR HG2 H 1.340 0.02 1 309 98 98 THR C C 177.230 0.30 1 310 98 98 THR CA C 67.040 0.30 1 311 98 98 THR CB C 68.953 0.30 1 312 98 98 THR CG2 C 21.686 0.30 1 313 98 98 THR N N 114.169 0.30 1 314 99 99 SER H H 8.294 0.02 1 315 99 99 SER HA H 4.250 0.02 1 316 99 99 SER HB2 H 4.140 0.02 2 317 99 99 SER C C 176.860 0.30 1 318 99 99 SER CA C 61.413 0.30 1 319 99 99 SER CB C 63.101 0.30 1 320 99 99 SER N N 115.706 0.30 1 321 100 100 PHE H H 7.377 0.02 1 322 100 100 PHE HA H 4.120 0.02 1 323 100 100 PHE HB2 H 3.460 0.02 2 324 100 100 PHE HB3 H 2.980 0.02 2 325 100 100 PHE C C 176.640 0.30 1 326 100 100 PHE CA C 64.902 0.30 1 327 100 100 PHE CB C 39.243 0.30 1 328 100 100 PHE N N 122.105 0.30 1 329 101 101 PHE H H 7.755 0.02 1 330 101 101 PHE HA H 4.170 0.02 1 331 101 101 PHE HB2 H 3.660 0.02 2 332 101 101 PHE HB3 H 2.840 0.02 2 333 101 101 PHE C C 178.390 0.30 1 334 101 101 PHE CA C 67.716 0.30 1 335 101 101 PHE CB C 38.342 0.30 1 336 101 101 PHE N N 114.654 0.30 1 337 102 102 LYS H H 8.570 0.02 1 338 102 102 LYS HA H 4.154 0.02 1 339 102 102 LYS HB2 H 1.980 0.02 2 340 102 102 LYS HG2 H 1.510 0.02 1 341 102 102 LYS HD2 H 1.750 0.02 1 342 102 102 LYS C C 180.360 0.30 1 343 102 102 LYS CA C 60.063 0.30 1 344 102 102 LYS CB C 32.265 0.30 1 345 102 102 LYS CG C 25.175 0.30 1 346 102 102 LYS CD C 29.339 0.30 1 347 102 102 LYS N N 120.231 0.30 1 348 103 103 LYS H H 7.551 0.02 1 349 103 103 LYS HA H 3.980 0.02 1 350 103 103 LYS HB2 H 1.790 0.02 2 351 103 103 LYS HB3 H 1.550 0.02 2 352 103 103 LYS HG2 H 1.490 0.02 1 353 103 103 LYS HD2 H 1.980 0.02 1 354 103 103 LYS C C 177.621 0.30 1 355 103 103 LYS CA C 59.050 0.30 1 356 103 103 LYS CB C 31.140 0.30 1 357 103 103 LYS CG C 24.275 0.30 1 358 103 103 LYS CD C 29.227 0.30 1 359 103 103 LYS CE C 41.831 0.30 1 360 103 103 LYS N N 121.298 0.30 1 361 104 104 HIS H H 6.585 0.02 1 362 104 104 HIS HA H 4.670 0.02 1 363 104 104 HIS HB2 H 3.260 0.02 2 364 104 104 HIS HB3 H 2.480 0.02 2 365 104 104 HIS C C 175.069 0.30 1 366 104 104 HIS CA C 56.687 0.30 1 367 104 104 HIS CB C 31.703 0.30 1 368 104 104 HIS N N 114.009 0.30 1 369 105 105 GLY H H 7.737 0.02 1 370 105 105 GLY HA2 H 4.260 0.02 1 371 105 105 GLY C C 174.800 0.30 1 372 105 105 GLY CA C 47.008 0.30 1 373 105 105 GLY N N 108.817 0.30 1 374 106 106 ILE H H 7.939 0.02 1 375 106 106 ILE HA H 4.830 0.02 1 376 106 106 ILE HB H 2.175 0.02 1 377 106 106 ILE HG12 H 1.370 0.02 2 378 106 106 ILE HG2 H 1.100 0.02 1 379 106 106 ILE HD1 H 0.890 0.02 1 380 106 106 ILE C C 176.270 0.30 1 381 106 106 ILE CA C 59.388 0.30 1 382 106 106 ILE CB C 38.455 0.30 1 383 106 106 ILE CG1 C 26.638 0.30 1 384 106 106 ILE CG2 C 18.648 0.30 1 385 106 106 ILE CD1 C 14.146 0.30 1 386 106 106 ILE N N 116.797 0.30 1 387 107 107 GLU H H 8.578 0.02 1 388 107 107 GLU HA H 3.970 0.02 1 389 107 107 GLU HB2 H 2.330 0.02 2 390 107 107 GLU HG2 H 2.300 0.02 1 391 107 107 GLU C C 178.350 0.30 1 392 107 107 GLU CA C 60.063 0.30 1 393 107 107 GLU CB C 30.802 0.30 1 394 107 107 GLU CG C 36.092 0.30 1 395 107 107 GLU N N 123.176 0.30 1 396 108 108 LYS H H 8.682 0.02 1 397 108 108 LYS HA H 4.176 0.02 1 398 108 108 LYS HB2 H 1.940 0.02 2 399 108 108 LYS C C 178.580 0.30 1 400 108 108 LYS CA C 58.487 0.30 1 401 108 108 LYS CB C 32.940 0.30 1 402 108 108 LYS N N 117.642 0.30 1 403 109 109 VAL H H 7.819 0.02 1 404 109 109 VAL HA H 3.690 0.02 1 405 109 109 VAL HB H 1.560 0.02 1 406 109 109 VAL HG1 H 0.920 0.02 2 407 109 109 VAL HG2 H 0.890 0.02 2 408 109 109 VAL C C 177.630 0.30 1 409 109 109 VAL CA C 65.015 0.30 1 410 109 109 VAL CB C 33.841 0.30 1 411 109 109 VAL CG1 C 25.063 0.30 1 412 109 109 VAL CG2 C 23.600 0.30 1 413 109 109 VAL N N 120.354 0.30 1 414 110 110 ALA H H 7.781 0.02 1 415 110 110 ALA HA H 3.670 0.02 1 416 110 110 ALA HB H 1.620 0.02 1 417 110 110 ALA C C 178.890 0.30 1 418 110 110 ALA CA C 55.786 0.30 1 419 110 110 ALA CB C 19.211 0.30 1 420 110 110 ALA N N 121.172 0.30 1 421 111 111 GLU H H 7.502 0.02 1 422 111 111 GLU HA H 3.990 0.02 1 423 111 111 GLU HB2 H 2.480 0.02 2 424 111 111 GLU HB3 H 2.050 0.02 2 425 111 111 GLU HG2 H 2.350 0.02 1 426 111 111 GLU C C 178.930 0.30 1 427 111 111 GLU CA C 59.050 0.30 1 428 111 111 GLU CB C 28.326 0.30 1 429 111 111 GLU CG C 36.204 0.30 1 430 111 111 GLU N N 114.497 0.30 1 431 112 112 GLN H H 7.078 0.02 1 432 112 112 GLN HA H 4.120 0.02 1 433 112 112 GLN HB2 H 2.560 0.02 2 434 112 112 GLN HG2 H 2.360 0.02 1 435 112 112 GLN CA C 58.262 0.30 1 436 112 112 GLN CB C 29.114 0.30 1 437 112 112 GLN CG C 33.503 0.30 1 438 112 112 GLN N N 117.169 0.30 1 439 113 113 VAL H H 7.682 0.02 1 440 113 113 VAL HA H 3.460 0.02 1 441 113 113 VAL HB H 2.010 0.02 1 442 113 113 VAL HG1 H 0.890 0.02 2 443 113 113 VAL HG2 H 0.870 0.02 2 444 113 113 VAL C C 177.560 0.30 1 445 113 113 VAL CA C 66.027 0.30 1 446 113 113 VAL CB C 31.027 0.30 1 447 113 113 VAL CG1 C 23.600 0.30 1 448 113 113 VAL CG2 C 22.249 0.30 1 449 113 113 VAL N N 120.237 0.30 1 450 114 114 MET H H 7.597 0.02 1 451 114 114 MET HA H 4.560 0.02 1 452 114 114 MET HB2 H 2.320 0.02 2 453 114 114 MET HB3 H 2.180 0.02 2 454 114 114 MET HG2 H 2.210 0.02 1 455 114 114 MET HE H 1.860 0.02 1 456 114 114 MET C C 179.490 0.30 1 457 114 114 MET CA C 56.236 0.30 1 458 114 114 MET CB C 31.140 0.30 1 459 114 114 MET CG C 29.002 0.30 1 460 114 114 MET CE C 18.985 0.30 1 461 114 114 MET N N 113.668 0.30 1 462 115 115 LYS H H 7.271 0.02 1 463 115 115 LYS HA H 4.460 0.02 1 464 115 115 LYS HB2 H 2.680 0.02 2 465 115 115 LYS HG2 H 1.480 0.02 1 466 115 115 LYS HD2 H 1.790 0.02 1 467 115 115 LYS C C 176.750 0.30 1 468 115 115 LYS CA C 60.063 0.30 1 469 115 115 LYS CB C 33.841 0.30 1 470 115 115 LYS CG C 25.288 0.30 1 471 115 115 LYS CD C 29.002 0.30 1 472 115 115 LYS N N 119.095 0.30 1 473 116 116 ALA H H 7.943 0.02 1 474 116 116 ALA HA H 4.230 0.02 1 475 116 116 ALA HB H 1.460 0.02 1 476 116 116 ALA C C 177.698 0.30 1 477 116 116 ALA CA C 52.748 0.30 1 478 116 116 ALA CB C 17.635 0.30 1 479 116 116 ALA N N 119.801 0.30 1 480 117 117 ASP H H 7.102 0.02 1 481 117 117 ASP HA H 4.632 0.02 1 482 117 117 ASP HB2 H 2.930 0.02 2 483 117 117 ASP HB3 H 2.360 0.02 2 484 117 117 ASP C C 175.970 0.30 1 485 117 117 ASP CA C 53.535 0.30 1 486 117 117 ASP CB C 38.793 0.30 1 487 117 117 ASP N N 116.229 0.30 1 488 118 118 ALA H H 7.869 0.02 1 489 118 118 ALA HA H 4.300 0.02 1 490 118 118 ALA HB H 1.650 0.02 1 491 118 118 ALA C C 178.650 0.30 1 492 118 118 ALA CA C 54.661 0.30 1 493 118 118 ALA CB C 19.661 0.30 1 494 118 118 ALA N N 132.601 0.30 1 495 119 119 ASN H H 7.840 0.02 1 496 119 119 ASN HA H 4.820 0.02 1 497 119 119 ASN HB2 H 3.360 0.02 2 498 119 119 ASN HB3 H 2.980 0.02 2 499 119 119 ASN C C 176.680 0.30 1 500 119 119 ASN CA C 51.622 0.30 1 501 119 119 ASN CB C 37.365 0.30 1 502 119 119 ASN N N 111.655 0.30 1 503 120 120 GLY H H 7.453 0.02 1 504 120 120 GLY HA2 H 3.890 0.02 1 505 120 120 GLY C C 174.920 0.30 1 506 120 120 GLY CA C 47.346 0.30 1 507 120 120 GLY N N 109.069 0.30 1 508 121 121 ASP H H 7.834 0.02 1 509 121 121 ASP HA H 4.460 0.02 1 510 121 121 ASP HB2 H 3.090 0.02 2 511 121 121 ASP HB3 H 2.530 0.02 2 512 121 121 ASP C C 176.890 0.30 1 513 121 121 ASP CA C 53.423 0.30 1 514 121 121 ASP CB C 40.256 0.30 1 515 121 121 ASP N N 118.335 0.30 1 516 122 122 GLY H H 9.910 0.02 1 517 122 122 GLY HA2 H 4.150 0.02 1 518 122 122 GLY HA3 H 3.460 0.02 1 519 122 122 GLY C C 173.120 0.30 1 520 122 122 GLY CA C 45.095 0.30 1 521 122 122 GLY N N 111.496 0.30 1 522 123 123 TYR H H 7.739 0.02 1 523 123 123 TYR HA H 5.420 0.02 1 524 123 123 TYR HB2 H 2.680 0.02 2 525 123 123 TYR HB3 H 2.730 0.02 2 526 123 123 TYR C C 175.150 0.30 1 527 123 123 TYR CA C 54.886 0.30 1 528 123 123 TYR CB C 41.606 0.30 1 529 123 123 TYR N N 125.275 0.30 1 530 124 124 ILE H H 9.549 0.02 1 531 124 124 ILE HA H 5.280 0.02 1 532 124 124 ILE HB H 2.060 0.02 1 533 124 124 ILE HG12 H 1.320 0.02 2 534 124 124 ILE HG2 H 0.950 0.02 1 535 124 124 ILE HD1 H 0.870 0.02 1 536 124 124 ILE C C 178.460 0.30 1 537 124 124 ILE CA C 58.937 0.30 1 538 124 124 ILE CB C 37.217 0.30 1 539 124 124 ILE CG1 C 29.564 0.30 1 540 124 124 ILE CG2 C 19.211 0.30 1 541 124 124 ILE CD1 C 17.635 0.30 1 542 124 124 ILE N N 125.275 0.30 1 543 125 125 THR H H 8.799 0.02 1 544 125 125 THR HA H 4.880 0.02 1 545 125 125 THR HB H 4.570 0.02 1 546 125 125 THR HG2 H 1.380 0.02 1 547 125 125 THR C C 175.360 0.30 1 548 125 125 THR CA C 61.076 0.30 1 549 125 125 THR CB C 71.092 0.30 1 550 125 125 THR CG2 C 22.924 0.30 1 551 125 125 THR N N 118.691 0.30 1 552 126 126 LEU H H 8.823 0.02 1 553 126 126 LEU HA H 3.330 0.02 1 554 126 126 LEU HB2 H 1.590 0.02 2 555 126 126 LEU HB3 H 1.410 0.02 2 556 126 126 LEU HG H 1.690 0.02 1 557 126 126 LEU HD1 H 0.890 0.02 2 558 126 126 LEU HD2 H 0.840 0.02 2 559 126 126 LEU C C 177.890 0.30 1 560 126 126 LEU CA C 58.825 0.30 1 561 126 126 LEU CB C 40.368 0.30 1 562 126 126 LEU CG C 25.963 0.30 1 563 126 126 LEU CD1 C 22.699 0.30 1 564 126 126 LEU CD2 C 21.686 0.30 1 565 126 126 LEU N N 124.169 0.30 1 566 127 127 GLU H H 8.405 0.02 1 567 127 127 GLU HA H 3.880 0.02 1 568 127 127 GLU HB2 H 2.090 0.02 2 569 127 127 GLU HB3 H 2.040 0.02 2 570 127 127 GLU HG2 H 2.560 0.02 1 571 127 127 GLU C C 180.020 0.30 1 572 127 127 GLU CA C 60.625 0.30 1 573 127 127 GLU CB C 29.227 0.30 1 574 127 127 GLU CG C 36.992 0.30 1 575 127 127 GLU N N 115.092 0.30 1 576 128 128 GLU H H 7.327 0.02 1 577 128 128 GLU HA H 4.130 0.02 1 578 128 128 GLU HB2 H 2.390 0.02 2 579 128 128 GLU HB3 H 2.180 0.02 2 580 128 128 GLU HG2 H 2.460 0.02 1 581 128 128 GLU C C 179.790 0.30 1 582 128 128 GLU CA C 58.712 0.30 1 583 128 128 GLU CB C 29.789 0.30 1 584 128 128 GLU CG C 37.442 0.30 1 585 128 128 GLU N N 117.664 0.30 1 586 129 129 PHE H H 8.735 0.02 1 587 129 129 PHE HA H 4.320 0.02 1 588 129 129 PHE HB2 H 3.260 0.02 2 589 129 129 PHE C C 176.690 0.30 1 590 129 129 PHE CA C 61.638 0.30 1 591 129 129 PHE CB C 40.256 0.30 1 592 129 129 PHE N N 122.042 0.30 1 593 130 130 LEU H H 8.119 0.02 1 594 130 130 LEU HA H 4.490 0.02 1 595 130 130 LEU HB2 H 2.010 0.02 2 596 130 130 LEU HB3 H 1.590 0.02 2 597 130 130 LEU HG H 1.680 0.02 1 598 130 130 LEU HD1 H 0.960 0.02 2 599 130 130 LEU HD2 H 0.880 0.02 2 600 130 130 LEU C C 177.860 0.30 1 601 130 130 LEU CA C 57.024 0.30 1 602 130 130 LEU CB C 41.156 0.30 1 603 130 130 LEU CG C 25.963 0.30 1 604 130 130 LEU CD1 C 23.600 0.30 1 605 130 130 LEU CD2 C 21.686 0.30 1 606 130 130 LEU N N 113.133 0.30 1 607 131 131 GLU H H 7.227 0.02 1 608 131 131 GLU HA H 4.430 0.02 1 609 131 131 GLU HB2 H 2.350 0.02 2 610 131 131 GLU HB3 H 1.920 0.02 2 611 131 131 GLU HG2 H 2.590 0.02 1 612 131 131 GLU C C 176.500 0.30 1 613 131 131 GLU CA C 55.786 0.30 1 614 131 131 GLU CB C 29.002 0.30 1 615 131 131 GLU CG C 35.754 0.30 1 616 131 131 GLU N N 116.192 0.30 1 617 132 132 PHE H H 7.755 0.02 1 618 132 132 PHE HA H 4.470 0.02 1 619 132 132 PHE HB2 H 2.980 0.02 2 620 132 132 PHE C C 173.890 0.30 1 621 132 132 PHE CA C 57.924 0.30 1 622 132 132 PHE CB C 39.918 0.30 1 623 132 132 PHE N N 122.921 0.30 1 624 133 133 SER H H 6.882 0.02 1 625 133 133 SER HA H 4.140 0.02 1 626 133 133 SER HB2 H 3.520 0.02 2 627 133 133 SER C C 171.930 0.30 1 628 133 133 SER CA C 56.687 0.30 1 629 133 133 SER CB C 64.339 0.30 1 630 133 133 SER N N 119.771 0.30 1 631 134 134 LEU H H 7.411 0.02 1 632 134 134 LEU HA H 3.930 0.02 1 633 134 134 LEU HB2 H 1.590 0.02 2 634 134 134 LEU HB3 H 1.370 0.02 2 635 134 134 LEU CA C 57.050 0.30 1 636 134 134 LEU CB C 43.860 0.30 1 637 134 134 LEU N N 130.582 0.30 1 stop_ save_