data_4082 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N NMR Assignments amd Global Folding Pattern ; _BMRB_accession_number 4082 _BMRB_flat_file_name bmr4082.str _Entry_type update _Submission_date 1997-12-22 _Accession_date 1997-12-22 _Entry_origination BMRB _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 Metzler William J. . 2 Constantine Keith L. . 3 Friedrichs Mark S. . 4 Bell Aneka J. . 5 Ernst Eileen G. . 6 Lavoie Thomas B. . 7 Mueller Luciano . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 773 "13C chemical shifts" 440 "15N chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-17 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Metzler, W. J., Constantine, K. L., Friedrichs, M. S., Bell, A. J., Ernst, E. G., Lavoie, T. S., and Mueller, L., "Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N Assignments and Global Folding Pattern," Biochemistry 32, 13818-13829 (1993). ; _Citation_title ; Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N Assignments and Global Folding Pattern ; _Citation_status published _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 Metzler William J. . 2 Constantine Keith L. . 3 Friedrichs Mark S. . 4 Bell Aneka J. . 5 Ernst Eileen G. . 6 Lavoie Thomas B. . 7 Mueller Luciano . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 32 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13818 _Page_last 13829 _Year 1993 _Details . loop_ _Keyword glucoamylase NMR 'nuclear magnetic resonance' 'phosphatidylinositol 4,5-biphosphate' PIP2 'resonance assignments' SBD 'secondary structure' 'starch binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_profilin _Saveframe_category molecular_system _Mol_system_name profilin _Abbreviation_common profilin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label profilin $profilin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function ; Plays a major role in the signaling pathway leading to cytoskeletal rearrangement ; stop_ _Database_query_date . _Details ; Interacts reversibly with actin and phosphoinositides ; save_ ######################## # Monomeric polymers # ######################## save_profilin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common profilin _Molecular_mass 15000 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; AGWNAYIDNLMADGTCQDAA IVGYKDSPSVWAAVPGKTFV NITPAEVGVLVGKDRSSFYV NGLTLGGQKCSVIRDSLLQD GEFSMDLRTKSTGGAPTFNV TVTKTDKTLVLLMGKEGVHG GLINKKCYEMASHLRRSQY ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLY 3 TRP 4 ASN 5 ALA 6 TYR 7 ILE 8 ASP 9 ASN 10 LEU 11 MET 12 ALA 13 ASP 14 GLY 15 THR 16 CYS 17 GLN 18 ASP 19 ALA 20 ALA 21 ILE 22 VAL 23 GLY 24 TYR 25 LYS 26 ASP 27 SER 28 PRO 29 SER 30 VAL 31 TRP 32 ALA 33 ALA 34 VAL 35 PRO 36 GLY 37 LYS 38 THR 39 PHE 40 VAL 41 ASN 42 ILE 43 THR 44 PRO 45 ALA 46 GLU 47 VAL 48 GLY 49 VAL 50 LEU 51 VAL 52 GLY 53 LYS 54 ASP 55 ARG 56 SER 57 SER 58 PHE 59 TYR 60 VAL 61 ASN 62 GLY 63 LEU 64 THR 65 LEU 66 GLY 67 GLY 68 GLN 69 LYS 70 CYS 71 SER 72 VAL 73 ILE 74 ARG 75 ASP 76 SER 77 LEU 78 LEU 79 GLN 80 ASP 81 GLY 82 GLU 83 PHE 84 SER 85 MET 86 ASP 87 LEU 88 ARG 89 THR 90 LYS 91 SER 92 THR 93 GLY 94 GLY 95 ALA 96 PRO 97 THR 98 PHE 99 ASN 100 VAL 101 THR 102 VAL 103 THR 104 LYS 105 THR 106 ASP 107 LYS 108 THR 109 LEU 110 VAL 111 LEU 112 LEU 113 MET 114 GLY 115 LYS 116 GLU 117 GLY 118 VAL 119 HIS 120 GLY 121 GLY 122 LEU 123 ILE 124 ASN 125 LYS 126 LYS 127 CYS 128 TYR 129 GLU 130 MET 131 ALA 132 SER 133 HIS 134 LEU 135 ARG 136 ARG 137 SER 138 GLN 139 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1AWI "Human Platelet Profilin Complexed With The L-Pro10 Peptide" 99.28 138 100.00 100.00 1.48e-96 PDB 1CF0 "Human Platelet Profilin Complexed With An L-Pro10- Iodotyrosine Peptide" 99.28 138 100.00 100.00 1.48e-96 PDB 1CJF "Profilin Binds Proline-Rich Ligands In Two Distinct Amide Backbone Orientations" 100.00 139 100.00 100.00 2.61e-97 PDB 1FIK "Human Platelet Profilin I Crystallized In Low Salt" 100.00 139 100.00 100.00 2.61e-97 PDB 1FIL "Human Platelet Profilin I Crystallized In High Salt Actin- Binding Protein" 100.00 139 100.00 100.00 2.61e-97 PDB 1PFL "Refined Solution Structure Of Human Profilin I" 99.28 139 100.00 100.00 3.18e-96 PDB 2PAV "Ternary Complex Of Profilin-actin With The Last Poly-pro Of Human Vasp" 100.00 139 100.00 100.00 2.61e-97 PDB 2PBD "Ternary Complex Of Profilin-actin With The Poly-pro-gab Domain Of Vasp*" 100.00 139 100.00 100.00 2.61e-97 PDB 3CHW "Complex Of Dictyostelium Discoideum Actin With Profilin And The Last Poly-Pro Of Human Vasp" 100.00 139 100.00 100.00 2.61e-97 PDB 4X1L "Structural Basis For Mutation-induced Destabilization Of Profilin 1 In Als" 100.00 140 100.00 100.00 2.44e-97 PDB 4X1M "Structural Basis For Mutation-induced Destabilization Of Profilin 1 In Als" 100.00 140 99.28 99.28 6.55e-96 PDB 4X25 "Structural Basis For Mutation-induced Destabilization Of Profilin 1 In Als" 100.00 140 99.28 99.28 2.48e-96 DBJ BAE87684 "unnamed protein product [Macaca fascicularis]" 84.89 122 100.00 100.00 6.54e-79 DBJ BAG35102 "unnamed protein product [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 DBJ BAG73580 "profilin 1 [synthetic construct]" 100.00 140 100.00 100.00 2.44e-97 EMBL CAG28598 "PFN1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 GB AAA36486 "profilin [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 GB AAH02475 "Profilin 1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 GB AAH06768 "Profilin 1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 GB AAH13439 "Profilin 1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 GB AAH15164 "Profilin 1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 REF NP_001270319 "profilin 1 [Macaca fascicularis]" 84.89 122 100.00 100.00 6.54e-79 REF NP_005013 "profilin-1 [Homo sapiens]" 100.00 140 100.00 100.00 2.44e-97 REF XP_001099416 "PREDICTED: profilin-1 isoform 1 [Macaca mulatta]" 100.00 221 100.00 100.00 6.59e-98 REF XP_002800300 "PREDICTED: profilin-1 isoform 2 [Macaca mulatta]" 100.00 140 100.00 100.00 2.44e-97 REF XP_003733022 "PREDICTED: profilin-1 [Callithrix jacchus]" 100.00 140 99.28 100.00 8.40e-97 SP P07737 "RecName: Full=Profilin-1; AltName: Full=Epididymis tissue protein Li 184a; AltName: Full=Profilin I" 100.00 140 100.00 100.00 2.44e-97 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $profilin Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $profilin 'recombinant technology' 'E. coli' Escherichia coli . plasmid pGTL-1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM [U-15N] phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM [U-15N] phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . D2O 100 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM [U-13C] phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_four _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM [U-13C] phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . D2O 100 % . stop_ save_ save_sample_five _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM '[U-15N], [U-13C]' phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_six _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $profilin 2.0 mM '[U-15N], [U-13C]' phosphate 10 mM . KCl 25 mM . B-mercaptoethanol 20 mM . EDTA 1.0 mM . D2O 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . n/a temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _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 . C 13 . ppm . . . . . . water H 1 protons ppm 4.85 . . . . . . N 15 . ppm . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_assignment_profilin _Saveframe_category assigned_chemical_shifts _Details ; Actual stereospecific assignments probably were not as extensive as indicated in this list of assigned chemical shifts. ; loop_ _Sample_label $sample_five stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name profilin _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLY HA2 H 3.79 . 1 2 . 2 GLY HA3 H 3.79 . 1 3 . 2 GLY CA C 45.9 . 1 4 . 3 TRP H H 8.00 . 1 5 . 3 TRP HA H 4.59 . 1 6 . 3 TRP HB2 H 3.42 . 1 7 . 3 TRP HB3 H 3.02 . 1 8 . 3 TRP HD1 H 7.34 . 1 9 . 3 TRP HE1 H 9.56 . 1 10 . 3 TRP HE3 H 6.81 . 1 11 . 3 TRP HZ2 H 7.52 . 3 12 . 3 TRP HZ3 H 5.98 . 3 13 . 3 TRP HH2 H 6.61 . 1 14 . 3 TRP CA C 59.1 . 1 15 . 3 TRP CB C 30.2 . 1 16 . 3 TRP CE3 C 115.1 . 1 17 . 3 TRP CZ2 C 119.2 . 3 18 . 3 TRP CZ3 C 123.7 . 3 19 . 3 TRP CH2 C 121.2 . 1 20 . 3 TRP N N 122.0 . 1 21 . 3 TRP NE1 N 129.7 . 1 22 . 4 ASN H H 8.56 . 1 23 . 4 ASN HA H 4.29 . 1 24 . 4 ASN HB2 H 2.90 . 1 25 . 4 ASN HB3 H 2.82 . 1 26 . 4 ASN HD21 H 7.91 . 1 27 . 4 ASN HD22 H 7.09 . 1 28 . 4 ASN CA C 56.6 . 1 29 . 4 ASN CB C 37.7 . 1 30 . 4 ASN N N 116.8 . 1 31 . 4 ASN ND2 N 114.7 . 1 32 . 5 ALA H H 7.70 . 1 33 . 5 ALA HA H 4.09 . 1 34 . 5 ALA HB H 1.16 . 1 35 . 5 ALA CA C 54.8 . 1 36 . 5 ALA CB C 17.7 . 1 37 . 5 ALA N N 122.6 . 1 38 . 6 TYR H H 7.28 . 1 39 . 6 TYR HA H 4.28 . 1 40 . 6 TYR HB2 H 3.22 . 1 41 . 6 TYR HB3 H 3.22 . 1 42 . 6 TYR HD1 H 7.33 . 1 43 . 6 TYR HD2 H 7.33 . 1 44 . 6 TYR HE1 H 6.56 . 1 45 . 6 TYR HE2 H 6.56 . 1 46 . 6 TYR CA C 60.9 . 1 47 . 6 TYR CB C 37.7 . 1 48 . 6 TYR CD1 C 132.5 . 1 49 . 6 TYR CD2 C 132.5 . 1 50 . 6 TYR CE1 C 117.9 . 1 51 . 6 TYR CE2 C 117.9 . 1 52 . 6 TYR N N 117.0 . 1 53 . 7 ILE H H 7.14 . 1 54 . 7 ILE HA H 3.64 . 1 55 . 7 ILE HB H 2.44 . 1 56 . 7 ILE HG12 H 1.83 . 1 57 . 7 ILE HG13 H 1.18 . 1 58 . 7 ILE HG2 H 0.82 . 1 59 . 7 ILE HD1 H 0.60 . 1 60 . 7 ILE CA C 62.0 . 1 61 . 7 ILE CB C 34.5 . 1 62 . 7 ILE CG1 C 28.4 . 1 63 . 7 ILE CG2 C 19.1 . 1 64 . 7 ILE CD1 C 8.6 . 1 65 . 7 ILE N N 119.3 . 1 66 . 8 ASP H H 8.10 . 1 67 . 8 ASP HA H 4.22 . 1 68 . 8 ASP HB2 H 2.71 . 1 69 . 8 ASP HB3 H 2.60 . 1 70 . 8 ASP CA C 57.7 . 1 71 . 8 ASP CB C 39.7 . 1 72 . 8 ASP N N 120.2 . 1 73 . 9 ASN H H 7.76 . 1 74 . 9 ASN HA H 4.36 . 1 75 . 9 ASN HB2 H 2.87 . 1 76 . 9 ASN HB3 H 2.68 . 1 77 . 9 ASN HD21 H 7.44 . 1 78 . 9 ASN HD22 H 6.82 . 1 79 . 9 ASN CA C 56.9 . 1 80 . 9 ASN CB C 38.9 . 1 81 . 9 ASN N N 118.5 . 1 82 . 9 ASN ND2 N 112.0 . 1 83 . 10 LEU H H 8.03 . 1 84 . 10 LEU HA H 4.08 . 1 85 . 10 LEU HB2 H 2.06 . 1 86 . 10 LEU HB3 H 2.06 . 1 87 . 10 LEU HG H 2.00 . 1 88 . 10 LEU HD1 H 0.96 . 1 89 . 10 LEU HD2 H 0.86 . 1 90 . 10 LEU CA C 57.9 . 1 91 . 10 LEU CB C 42.5 . 1 92 . 10 LEU CG C 26.9 . 1 93 . 10 LEU CD1 C 23.3 . 1 94 . 10 LEU CD2 C 25.6 . 1 95 . 10 LEU N N 121.7 . 1 96 . 11 MET H H 7.80 . 1 97 . 11 MET HA H 4.65 . 1 98 . 11 MET HB2 H 2.04 . 1 99 . 11 MET HB3 H 2.04 . 1 100 . 11 MET HG2 H 2.50 . 1 101 . 11 MET HG3 H 2.31 . 1 102 . 11 MET CA C 54.5 . 1 103 . 11 MET CB C 32.1 . 1 104 . 11 MET CG C 33.2 . 1 105 . 11 MET N N 115.0 . 1 106 . 12 ALA H H 7.45 . 1 107 . 12 ALA HA H 4.06 . 1 108 . 12 ALA HB H 1.53 . 1 109 . 12 ALA CA C 56.0 . 1 110 . 12 ALA CB C 19.0 . 1 111 . 12 ALA N N 124.8 . 1 112 . 13 ASP H H 8.59 . 1 113 . 13 ASP HA H 4.47 . 1 114 . 13 ASP HB2 H 3.18 . 1 115 . 13 ASP HB3 H 2.68 . 1 116 . 13 ASP CA C 54.2 . 1 117 . 13 ASP CB C 40.1 . 1 118 . 13 ASP N N 114.8 . 1 119 . 14 GLY H H 7.57 . 1 120 . 14 GLY HA2 H 4.18 . 1 121 . 14 GLY HA3 H 4.18 . 1 122 . 14 GLY CA C 46.7 . 1 123 . 14 GLY N N 107.1 . 1 124 . 15 THR H H 8.00 . 1 125 . 15 THR HA H 4.28 . 1 126 . 15 THR HB H 4.29 . 1 127 . 15 THR HG2 H 1.17 . 1 128 . 15 THR CA C 64.0 . 1 129 . 15 THR CB C 71.1 . 1 130 . 15 THR CG2 C 22.1 . 1 131 . 15 THR N N 111.1 . 1 132 . 16 CYS H H 8.24 . 1 133 . 16 CYS HA H 5.08 . 1 134 . 16 CYS HB2 H 3.05 . 1 135 . 16 CYS HB3 H 2.72 . 1 136 . 16 CYS CA C 59.4 . 1 137 . 16 CYS CB C 30.7 . 1 138 . 16 CYS N N 117.9 . 1 139 . 17 GLN H H 8.77 . 1 140 . 17 GLN HA H 4.69 . 1 141 . 17 GLN HB2 H 2.00 . 1 142 . 17 GLN HB3 H 1.51 . 1 143 . 17 GLN HG2 H 1.40 . 1 144 . 17 GLN HG3 H 1.40 . 1 145 . 17 GLN HE21 H 6.82 . 1 146 . 17 GLN HE22 H 6.82 . 1 147 . 17 GLN CA C 53.7 . 1 148 . 17 GLN CB C 30.7 . 1 149 . 17 GLN CG C 38.0 . 1 150 . 17 GLN N N 116.2 . 1 151 . 17 GLN NE2 N 111.1 . 1 152 . 18 ASP H H 7.66 . 1 153 . 18 ASP HA H 4.69 . 1 154 . 18 ASP HB2 H 2.12 . 1 155 . 18 ASP HB3 H 1.81 . 1 156 . 18 ASP CA C 53.4 . 1 157 . 18 ASP CB C 44.4 . 1 158 . 18 ASP N N 120.7 . 1 159 . 19 ALA H H 9.19 . 1 160 . 19 ALA HA H 5.55 . 1 161 . 19 ALA HB H 1.41 . 1 162 . 19 ALA CA C 51.8 . 1 163 . 19 ALA CB C 23.7 . 1 164 . 19 ALA N N 127.4 . 1 165 . 20 ALA H H 8.78 . 1 166 . 20 ALA HA H 5.13 . 1 167 . 20 ALA HB H 1.28 . 1 168 . 20 ALA CA C 51.8 . 1 169 . 20 ALA CB C 24.1 . 1 170 . 20 ALA N N 118.9 . 1 171 . 21 ILE H H 8.65 . 1 172 . 21 ILE HA H 4.69 . 1 173 . 21 ILE HB H 1.45 . 1 174 . 21 ILE HG12 H 1.60 . 1 175 . 21 ILE HG13 H 1.60 . 1 176 . 21 ILE HG2 H 0.39 . 1 177 . 21 ILE HD1 H 1.02 . 1 178 . 21 ILE CA C 60.6 . 1 179 . 21 ILE CB C 41.2 . 1 180 . 21 ILE CG1 C 28.6 . 1 181 . 21 ILE CG2 C 17.7 . 1 182 . 21 ILE CD1 C 14.9 . 1 183 . 21 ILE N N 119.7 . 1 184 . 22 VAL H H 9.10 . 1 185 . 22 VAL HA H 4.09 . 1 186 . 22 VAL HB H 1.60 . 1 187 . 22 VAL HG1 H 0.59 . 1 188 . 22 VAL HG2 H 0.47 . 1 189 . 22 VAL CA C 60.1 . 1 190 . 22 VAL CB C 36.5 . 1 191 . 22 VAL CG1 C 22.6 . 1 192 . 22 VAL CG2 C 20.7 . 1 193 . 22 VAL N N 129.3 . 1 194 . 23 GLY H H 8.04 . 1 195 . 23 GLY HA2 H 3.66 . 1 196 . 23 GLY HA3 H 2.99 . 1 197 . 23 GLY CA C 45.7 . 1 198 . 23 GLY N N 115.4 . 1 199 . 24 TYR H H 6.73 . 1 200 . 24 TYR HA H 4.72 . 1 201 . 24 TYR HB2 H 2.97 . 1 202 . 24 TYR HB3 H 2.05 . 1 203 . 24 TYR HD1 H 6.60 . 1 204 . 24 TYR HD2 H 6.60 . 1 205 . 24 TYR HE1 H 6.70 . 1 206 . 24 TYR HE2 H 6.70 . 1 207 . 24 TYR CA C 56.0 . 1 208 . 24 TYR CB C 40.6 . 1 209 . 24 TYR CD1 C 133.1 . 1 210 . 24 TYR CD2 C 133.1 . 1 211 . 24 TYR CE1 C 118.0 . 1 212 . 24 TYR CE2 C 118.0 . 1 213 . 24 TYR N N 116.4 . 1 214 . 25 LYS H H 7.59 . 1 215 . 25 LYS HA H 3.98 . 1 216 . 25 LYS HB2 H 1.52 . 1 217 . 25 LYS HB3 H 1.46 . 1 218 . 25 LYS HG2 H 0.81 . 1 219 . 25 LYS HG3 H 0.81 . 1 220 . 25 LYS HD2 H 1.17 . 1 221 . 25 LYS HD3 H 1.17 . 1 222 . 25 LYS HE2 H 2.88 . 1 223 . 25 LYS HE3 H 2.88 . 1 224 . 25 LYS CA C 55.9 . 1 225 . 25 LYS CB C 32.4 . 1 226 . 25 LYS CG C 25.3 . 1 227 . 25 LYS CD C 22.0 . 1 228 . 25 LYS CE C 41.8 . 1 229 . 25 LYS N N 123.8 . 1 230 . 26 ASP H H 8.39 . 1 231 . 26 ASP HA H 4.15 . 1 232 . 26 ASP HB2 H 2.78 . 1 233 . 26 ASP HB3 H 2.67 . 1 234 . 26 ASP CA C 56.6 . 1 235 . 26 ASP CB C 40.1 . 1 236 . 26 ASP N N 118.0 . 1 237 . 27 SER H H 8.10 . 1 238 . 27 SER HA H 4.68 . 1 239 . 27 SER HB2 H 3.89 . 1 240 . 27 SER HB3 H 3.74 . 1 241 . 27 SER CA C 55.4 . 1 242 . 27 SER CB C 63.1 . 1 243 . 27 SER N N 118.7 . 1 244 . 28 PRO HA H 4.52 . 1 245 . 28 PRO HB2 H 2.13 . 1 246 . 28 PRO HB3 H 1.62 . 1 247 . 28 PRO HG2 H 1.98 . 1 248 . 28 PRO HG3 H 1.81 . 1 249 . 28 PRO HD2 H 3.77 . 1 250 . 28 PRO HD3 H 3.73 . 1 251 . 28 PRO CA C 63.2 . 1 252 . 28 PRO CB C 32.7 . 1 253 . 28 PRO CG C 27.8 . 1 254 . 28 PRO CD C 50.3 . 1 255 . 29 SER H H 7.96 . 1 256 . 29 SER HA H 4.51 . 1 257 . 29 SER HB2 H 3.97 . 1 258 . 29 SER HB3 H 3.82 . 1 259 . 29 SER CA C 57.5 . 1 260 . 29 SER CB C 65.5 . 1 261 . 29 SER N N 114.2 . 1 262 . 30 VAL H H 8.91 . 1 263 . 30 VAL HA H 3.75 . 1 264 . 30 VAL HB H 2.17 . 1 265 . 30 VAL HG1 H 0.95 . 1 266 . 30 VAL HG2 H 0.80 . 1 267 . 30 VAL CA C 64.2 . 1 268 . 30 VAL CB C 32.1 . 1 269 . 30 VAL CG1 C 22.5 . 1 270 . 30 VAL CG2 C 23.0 . 1 271 . 30 VAL N N 123.6 . 1 272 . 31 TRP H H 9.07 . 1 273 . 31 TRP HA H 4.76 . 1 274 . 31 TRP HB2 H 2.46 . 1 275 . 31 TRP HB3 H 2.46 . 1 276 . 31 TRP HD1 H 6.81 . 1 277 . 31 TRP HE1 H 10.00 . 1 278 . 31 TRP HE3 H 5.25 . 1 279 . 31 TRP HZ2 H 7.32 . 3 280 . 31 TRP HZ3 H 6.21 . 3 281 . 31 TRP HH2 H 6.97 . 1 282 . 31 TRP CA C 57.0 . 1 283 . 31 TRP CB C 28.4 . 1 284 . 31 TRP CD1 C 124.4 . 1 285 . 31 TRP CZ3 C 122.0 . 1 286 . 31 TRP CH2 C 123.2 . 1 287 . 31 TRP N N 107.2 . 1 288 . 31 TRP NE1 N 127.4 . 1 289 . 32 ALA H H 7.92 . 1 290 . 32 ALA HA H 4.61 . 1 291 . 32 ALA HB H 1.48 . 1 292 . 32 ALA CA C 52.7 . 1 293 . 32 ALA CB C 23.2 . 1 294 . 32 ALA N N 119.3 . 1 295 . 33 ALA H H 8.43 . 1 296 . 33 ALA HA H 5.20 . 1 297 . 33 ALA HB H 1.46 . 1 298 . 33 ALA CA C 51.7 . 1 299 . 33 ALA CB C 22.3 . 1 300 . 33 ALA N N 122.0 . 1 301 . 34 VAL H H 7.49 . 1 302 . 34 VAL HA H 4.24 . 1 303 . 34 VAL HB H 2.35 . 1 304 . 34 VAL HG1 H 1.29 . 1 305 . 34 VAL HG2 H 1.00 . 1 306 . 34 VAL CA C 61.2 . 1 307 . 34 VAL CB C 32.4 . 1 308 . 34 VAL CG1 C 23.4 . 1 309 . 34 VAL CG2 C 21.3 . 1 310 . 34 VAL N N 123.5 . 1 311 . 35 PRO HA H 4.24 . 1 312 . 35 PRO HB2 H 2.28 . 1 313 . 35 PRO HB3 H 1.88 . 1 314 . 35 PRO HG2 H 2.11 . 1 315 . 35 PRO HG3 H 2.02 . 1 316 . 35 PRO HD2 H 4.14 . 1 317 . 35 PRO HD3 H 3.77 . 1 318 . 35 PRO CA C 63.4 . 1 319 . 35 PRO CB C 31.1 . 1 320 . 35 PRO CG C 27.7 . 1 321 . 35 PRO CD C 51.2 . 1 322 . 36 GLY H H 8.77 . 1 323 . 36 GLY HA2 H 3.99 . 1 324 . 36 GLY HA3 H 3.77 . 1 325 . 36 GLY CA C 46.2 . 1 326 . 36 GLY N N 108.3 . 1 327 . 37 LYS H H 6.57 . 1 328 . 37 LYS HA H 4.71 . 1 329 . 37 LYS HB2 H 1.85 . 1 330 . 37 LYS HB3 H 1.85 . 1 331 . 37 LYS HG2 H 1.27 . 1 332 . 37 LYS HG3 H 1.20 . 1 333 . 37 LYS HD2 H 1.56 . 1 334 . 37 LYS HD3 H 1.44 . 1 335 . 37 LYS CA C 53.2 . 1 336 . 37 LYS CB C 27.9 . 1 337 . 37 LYS N N 119.7 . 1 338 . 38 THR H H 8.28 . 1 339 . 38 THR HA H 4.33 . 1 340 . 38 THR HB H 3.62 . 1 341 . 38 THR HG2 H 1.03 . 1 342 . 38 THR CA C 65.1 . 1 343 . 38 THR CB C 70.1 . 1 344 . 38 THR CG2 C 23.2 . 1 345 . 38 THR N N 120.1 . 1 346 . 39 PHE H H 9.84 . 1 347 . 39 PHE HA H 4.18 . 1 348 . 39 PHE HB2 H 2.97 . 1 349 . 39 PHE HB3 H 2.86 . 1 350 . 39 PHE HD1 H 6.67 . 1 351 . 39 PHE HD2 H 6.67 . 1 352 . 39 PHE HE1 H 6.86 . 1 353 . 39 PHE HE2 H 6.86 . 1 354 . 39 PHE HZ H 6.93 . 1 355 . 39 PHE CA C 57.3 . 1 356 . 39 PHE CB C 37.7 . 1 357 . 39 PHE CD1 C 129.2 . 1 358 . 39 PHE CD2 C 129.2 . 1 359 . 39 PHE CE1 C 130.6 . 1 360 . 39 PHE CE2 C 130.6 . 1 361 . 39 PHE CZ C 128.4 . 1 362 . 39 PHE N N 125.9 . 1 363 . 40 VAL H H 9.75 . 1 364 . 40 VAL HA H 3.64 . 1 365 . 40 VAL HB H 2.02 . 1 366 . 40 VAL HG1 H 0.99 . 1 367 . 40 VAL HG2 H 0.75 . 1 368 . 40 VAL CA C 63.5 . 1 369 . 40 VAL CB C 31.2 . 1 370 . 40 VAL CG1 C 22.0 . 1 371 . 40 VAL CG2 C 19.4 . 1 372 . 40 VAL N N 120.3 . 1 373 . 41 ASN H H 7.68 . 1 374 . 41 ASN HA H 4.85 . 1 375 . 41 ASN HB2 H 2.94 . 1 376 . 41 ASN HB3 H 2.79 . 1 377 . 41 ASN HD21 H 7.74 . 1 378 . 41 ASN HD22 H 6.91 . 1 379 . 41 ASN CA C 52.8 . 1 380 . 41 ASN CB C 39.1 . 1 381 . 41 ASN N N 117.2 . 1 382 . 41 ASN ND2 N 118.3 . 1 383 . 42 ILE H H 7.79 . 1 384 . 42 ILE HA H 4.21 . 1 385 . 42 ILE HB H 1.58 . 1 386 . 42 ILE HG12 H 1.89 . 1 387 . 42 ILE HG13 H 1.07 . 1 388 . 42 ILE HG2 H 0.72 . 1 389 . 42 ILE HD1 H 0.58 . 1 390 . 42 ILE CA C 63.2 . 1 391 . 42 ILE CB C 38.4 . 1 392 . 42 ILE CG1 C 31.0 . 1 393 . 42 ILE CG2 C 17.9 . 1 394 . 42 ILE CD1 C 15.8 . 1 395 . 42 ILE N N 124.5 . 1 396 . 43 THR H H 8.36 . 1 397 . 43 THR HA H 4.89 . 1 398 . 43 THR HB H 4.66 . 1 399 . 43 THR HG2 H 1.24 . 1 400 . 43 THR CA C 58.9 . 1 401 . 43 THR CB C 69.7 . 1 402 . 43 THR CG2 C 22.4 . 1 403 . 43 THR N N 119.5 . 1 404 . 44 PRO HA H 3.92 . 1 405 . 44 PRO HB2 H 2.23 . 1 406 . 44 PRO HB3 H 1.96 . 1 407 . 44 PRO HG2 H 1.09 . 1 408 . 44 PRO HG3 H 1.82 . 1 409 . 44 PRO CA C 65.7 . 1 410 . 44 PRO CB C 32.3 . 1 411 . 45 ALA H H 8.21 . 1 412 . 45 ALA HA H 4.08 . 1 413 . 45 ALA HB H 1.36 . 1 414 . 45 ALA CA C 55.8 . 1 415 . 45 ALA CB C 18.1 . 1 416 . 45 ALA N N 121.4 . 1 417 . 46 GLU H H 7.82 . 1 418 . 46 GLU HA H 3.99 . 1 419 . 46 GLU HB2 H 1.79 . 1 420 . 46 GLU HB3 H 1.69 . 1 421 . 46 GLU CA C 59.4 . 1 422 . 46 GLU CB C 33.8 . 1 423 . 46 GLU N N 120.1 . 1 424 . 47 VAL H H 8.03 . 1 425 . 47 VAL HA H 3.23 . 1 426 . 47 VAL HB H 2.06 . 1 427 . 47 VAL HG1 H 0.83 . 1 428 . 47 VAL HG2 H 0.76 . 1 429 . 47 VAL CA C 67.7 . 1 430 . 47 VAL CB C 31.0 . 1 431 . 47 VAL CG1 C 21.8 . 1 432 . 47 VAL CG2 C 24.0 . 1 433 . 47 VAL N N 121.6 . 1 434 . 48 GLY H H 8.16 . 1 435 . 48 GLY HA2 H 3.75 . 1 436 . 48 GLY HA3 H 3.75 . 1 437 . 48 GLY CA C 46.7 . 1 438 . 48 GLY N N 112.1 . 1 439 . 49 VAL H H 7.33 . 1 440 . 49 VAL HA H 3.73 . 1 441 . 49 VAL HB H 2.09 . 1 442 . 49 VAL HG1 H 1.08 . 1 443 . 49 VAL HG2 H 1.08 . 1 444 . 49 VAL CA C 66.0 . 1 445 . 49 VAL CB C 32.1 . 1 446 . 49 VAL CG1 C 22.6 . 1 447 . 49 VAL CG2 C 22.1 . 1 448 . 49 VAL N N 120.9 . 1 449 . 50 LEU H H 7.35 . 1 450 . 50 LEU HA H 3.73 . 1 451 . 50 LEU HB2 H 2.05 . 1 452 . 50 LEU HB3 H 1.06 . 1 453 . 50 LEU HG H 1.68 . 1 454 . 50 LEU HD1 H 0.59 . 1 455 . 50 LEU HD2 H 0.59 . 1 456 . 50 LEU CA C 58.9 . 1 457 . 50 LEU CB C 42.5 . 1 458 . 50 LEU CG C 26.8 . 1 459 . 50 LEU CD1 C 24.8 . 1 460 . 50 LEU CD2 C 26.0 . 1 461 . 50 LEU N N 119.4 . 1 462 . 51 VAL H H 7.55 . 1 463 . 51 VAL HA H 4.32 . 1 464 . 51 VAL HB H 2.25 . 1 465 . 51 VAL HG1 H 0.79 . 1 466 . 51 VAL HG2 H 0.24 . 1 467 . 51 VAL CA C 60.8 . 1 468 . 51 VAL CB C 31.2 . 1 469 . 51 VAL CG1 C 18.1 . 1 470 . 51 VAL CG2 C 21.6 . 1 471 . 51 VAL N N 132.5 . 1 472 . 52 GLY H H 7.18 . 1 473 . 52 GLY HA2 H 4.09 . 1 474 . 52 GLY HA3 H 3.95 . 1 475 . 52 GLY CA C 45.7 . 1 476 . 52 GLY N N 111.1 . 1 477 . 53 LYS H H 8.04 . 1 478 . 53 LYS HA H 3.96 . 1 479 . 53 LYS HB2 H 1.74 . 1 480 . 53 LYS HB3 H 1.74 . 1 481 . 53 LYS HG2 H 1.44 . 1 482 . 53 LYS HG3 H 1.44 . 1 483 . 53 LYS HD2 H 1.65 . 1 484 . 53 LYS HD3 H 1.65 . 1 485 . 53 LYS HE2 H 2.94 . 1 486 . 53 LYS HE3 H 2.94 . 1 487 . 53 LYS CA C 57.9 . 1 488 . 53 LYS CB C 33.2 . 1 489 . 53 LYS CG C 25.1 . 1 490 . 53 LYS CD C 29.2 . 1 491 . 53 LYS CE C 42.1 . 1 492 . 53 LYS N N 117.0 . 1 493 . 54 ASP H H 7.74 . 1 494 . 54 ASP HA H 4.50 . 1 495 . 54 ASP HB2 H 2.78 . 1 496 . 54 ASP HB3 H 2.52 . 1 497 . 54 ASP CA C 53.8 . 1 498 . 54 ASP CB C 40.1 . 1 499 . 54 ASP N N 117.9 . 1 500 . 55 ARG H H 8.63 . 1 501 . 55 ARG HA H 3.86 . 1 502 . 55 ARG HB2 H 2.10 . 1 503 . 55 ARG HB3 H 1.52 . 1 504 . 55 ARG HG2 H 1.09 . 1 505 . 55 ARG HG3 H 1.09 . 1 506 . 55 ARG HD2 H 3.08 . 1 507 . 55 ARG HD3 H 2.92 . 1 508 . 55 ARG CA C 52.5 . 1 509 . 55 ARG CB C 28.0 . 1 510 . 55 ARG CD C 41.9 . 1 511 . 55 ARG N N 127.2 . 1 512 . 56 SER H H 8.29 . 1 513 . 56 SER HA H 4.53 . 1 514 . 56 SER HB2 H 3.84 . 1 515 . 56 SER HB3 H 3.84 . 1 516 . 56 SER CA C 60.1 . 1 517 . 56 SER CB C 64.3 . 1 518 . 56 SER N N 114.4 . 1 519 . 57 SER H H 8.86 . 1 520 . 57 SER HA H 4.31 . 1 521 . 57 SER HB2 H 3.92 . 1 522 . 57 SER HB3 H 3.82 . 1 523 . 57 SER CA C 61.7 . 1 524 . 57 SER CB C 64.0 . 1 525 . 57 SER N N 122.0 . 1 526 . 58 PHE H H 7.86 . 1 527 . 58 PHE HA H 3.97 . 1 528 . 58 PHE HB2 H 2.95 . 1 529 . 58 PHE HB3 H 2.74 . 1 530 . 58 PHE HD1 H 6.72 . 1 531 . 58 PHE HD2 H 6.72 . 1 532 . 58 PHE HE1 H 7.01 . 1 533 . 58 PHE HE2 H 7.01 . 1 534 . 58 PHE HZ H 7.21 . 1 535 . 58 PHE CA C 58.8 . 1 536 . 58 PHE CB C 37.7 . 1 537 . 58 PHE CD1 C 130.3 . 1 538 . 58 PHE CD2 C 130.3 . 1 539 . 58 PHE CE1 C 131.4 . 1 540 . 58 PHE CE2 C 131.4 . 1 541 . 58 PHE CZ C 132.9 . 1 542 . 58 PHE N N 118.7 . 1 543 . 59 TYR H H 8.05 . 1 544 . 59 TYR HA H 4.46 . 1 545 . 59 TYR HB2 H 3.26 . 1 546 . 59 TYR HB3 H 3.04 . 1 547 . 59 TYR HD1 H 7.39 . 1 548 . 59 TYR HD2 H 7.39 . 1 549 . 59 TYR HE1 H 6.96 . 1 550 . 59 TYR HE2 H 6.96 . 1 551 . 59 TYR CA C 61.6 . 1 552 . 59 TYR CB C 37.7 . 1 553 . 59 TYR CD1 C 132.9 . 1 554 . 59 TYR CD2 C 132.9 . 1 555 . 59 TYR CE1 C 118.5 . 1 556 . 59 TYR CE2 C 118.5 . 1 557 . 59 TYR N N 121.6 . 1 558 . 60 VAL H H 7.58 . 1 559 . 60 VAL HA H 4.05 . 1 560 . 60 VAL HB H 2.06 . 1 561 . 60 VAL HG1 H 0.98 . 1 562 . 60 VAL HG2 H 0.98 . 1 563 . 60 VAL CA C 64.0 . 1 564 . 60 VAL CB C 33.0 . 1 565 . 60 VAL CG1 C 21.5 . 1 566 . 60 VAL CG2 C 21.2 . 1 567 . 60 VAL N N 118.3 . 1 568 . 61 ASN H H 8.19 . 1 569 . 61 ASN HA H 4.80 . 1 570 . 61 ASN HB2 H 2.85 . 1 571 . 61 ASN HB3 H 2.67 . 1 572 . 61 ASN HD21 H 7.60 . 1 573 . 61 ASN HD22 H 7.07 . 1 574 . 61 ASN CA C 53.9 . 1 575 . 61 ASN CB C 40.2 . 1 576 . 61 ASN N N 115.8 . 1 577 . 61 ASN ND2 N 113.9 . 1 578 . 62 GLY H H 7.46 . 1 579 . 62 GLY HA2 H 4.42 . 1 580 . 62 GLY HA3 H 3.97 . 1 581 . 62 GLY CA C 45.4 . 1 582 . 62 GLY N N 108.8 . 1 583 . 63 LEU H H 8.07 . 1 584 . 63 LEU HA H 4.66 . 1 585 . 63 LEU HB2 H 1.66 . 1 586 . 63 LEU HB3 H 1.66 . 1 587 . 63 LEU HG H 1.04 . 1 588 . 63 LEU HD1 H 0.33 . 1 589 . 63 LEU HD2 H 0.10 . 1 590 . 63 LEU CA C 54.3 . 1 591 . 63 LEU CB C 42.9 . 1 592 . 63 LEU CG C 25.9 . 1 593 . 63 LEU CD1 C 24.2 . 1 594 . 63 LEU CD2 C 27.1 . 1 595 . 63 LEU N N 115.1 . 1 596 . 64 THR H H 8.30 . 1 597 . 64 THR HA H 5.30 . 1 598 . 64 THR HB H 3.50 . 1 599 . 64 THR HG2 H 0.91 . 1 600 . 64 THR CA C 59.9 . 1 601 . 64 THR CB C 72.0 . 1 602 . 64 THR CG2 C 21.5 . 1 603 . 64 THR N N 111.1 . 1 604 . 65 LEU H H 7.92 . 1 605 . 65 LEU HA H 4.29 . 1 606 . 65 LEU HB2 H 1.64 . 1 607 . 65 LEU HB3 H 0.88 . 1 608 . 65 LEU HG H 1.30 . 1 609 . 65 LEU HD1 H 0.63 . 1 610 . 65 LEU HD2 H 0.63 . 1 611 . 65 LEU CA C 53.3 . 1 612 . 65 LEU CB C 45.3 . 1 613 . 65 LEU CG C 26.0 . 1 614 . 65 LEU CD1 C 24.3 . 1 615 . 65 LEU CD2 C 27.1 . 1 616 . 65 LEU N N 119.7 . 1 617 . 66 GLY H H 10.98 . 1 618 . 66 GLY HA2 H 3.87 . 1 619 . 66 GLY HA3 H 3.40 . 1 620 . 66 GLY CA C 46.5 . 1 621 . 66 GLY N N 118.5 . 1 622 . 67 GLY H H 9.45 . 1 623 . 67 GLY HA2 H 4.25 . 1 624 . 67 GLY HA3 H 3.36 . 1 625 . 67 GLY CA C 44.8 . 1 626 . 67 GLY N N 106.3 . 1 627 . 68 GLN H H 7.72 . 1 628 . 68 GLN HA H 4.36 . 1 629 . 68 GLN HB2 H 2.40 . 1 630 . 68 GLN HB3 H 2.10 . 1 631 . 68 GLN HG2 H 2.14 . 1 632 . 68 GLN HG3 H 2.14 . 1 633 . 68 GLN HE21 H 8.11 . 1 634 . 68 GLN HE22 H 7.02 . 1 635 . 68 GLN CA C 54.0 . 1 636 . 68 GLN CB C 29.3 . 1 637 . 68 GLN CG C 37.0 . 1 638 . 68 GLN N N 122.2 . 1 639 . 68 GLN NE2 N 117.0 . 1 640 . 69 LYS H H 9.25 . 1 641 . 69 LYS HA H 4.30 . 1 642 . 69 LYS HB2 H 1.03 . 1 643 . 69 LYS HB3 H 1.03 . 1 644 . 69 LYS HG2 H 1.53 . 1 645 . 69 LYS HG3 H 1.37 . 1 646 . 69 LYS HD2 H 1.81 . 1 647 . 69 LYS HD3 H 1.62 . 1 648 . 69 LYS HE2 H 2.91 . 1 649 . 69 LYS HE3 H 2.91 . 1 650 . 69 LYS CA C 58.2 . 1 651 . 69 LYS CB C 32.5 . 1 652 . 69 LYS CG C 25.6 . 1 653 . 69 LYS CD C 29.1 . 1 654 . 69 LYS CE C 41.7 . 1 655 . 69 LYS N N 131.3 . 1 656 . 70 CYS H H 9.16 . 1 657 . 70 CYS HA H 5.18 . 1 658 . 70 CYS HB2 H 2.57 . 1 659 . 70 CYS HB3 H 2.43 . 1 660 . 70 CYS CA C 58.2 . 1 661 . 70 CYS CB C 33.3 . 1 662 . 70 CYS N N 121.4 . 1 663 . 71 SER H H 9.51 . 1 664 . 71 SER HA H 4.86 . 1 665 . 71 SER HB2 H 3.75 . 1 666 . 71 SER HB3 H 3.63 . 1 667 . 71 SER CA C 57.1 . 1 668 . 71 SER CB C 65.0 . 1 669 . 71 SER N N 118.5 . 1 670 . 72 VAL H H 9.09 . 1 671 . 72 VAL HA H 3.76 . 1 672 . 72 VAL HB H 1.58 . 1 673 . 72 VAL HG1 H 0.44 . 1 674 . 72 VAL HG2 H 0.28 . 1 675 . 72 VAL CA C 63.5 . 1 676 . 72 VAL CB C 32.1 . 1 677 . 72 VAL CG1 C 21.5 . 1 678 . 72 VAL CG2 C 21.4 . 1 679 . 72 VAL N N 125.3 . 1 680 . 73 ILE H H 8.85 . 1 681 . 73 ILE HA H 4.12 . 1 682 . 73 ILE HB H 1.58 . 1 683 . 73 ILE HG12 H 1.32 . 1 684 . 73 ILE HG13 H 1.11 . 1 685 . 73 ILE HG2 H 0.91 . 1 686 . 73 ILE HD1 H 0.65 . 1 687 . 73 ILE CA C 61.8 . 1 688 . 73 ILE CB C 38.0 . 1 689 . 73 ILE CG1 C 27.8 . 1 690 . 73 ILE CG2 C 17.5 . 1 691 . 73 ILE CD1 C 11.8 . 1 692 . 73 ILE N N 129.1 . 1 693 . 74 ARG H H 7.85 . 1 694 . 74 ARG HA H 4.65 . 1 695 . 74 ARG HB2 H 1.82 . 1 696 . 74 ARG HB3 H 1.82 . 1 697 . 74 ARG HG2 H 1.58 . 1 698 . 74 ARG HG3 H 1.43 . 1 699 . 74 ARG HD2 H 3.21 . 1 700 . 74 ARG HD3 H 3.08 . 1 701 . 74 ARG CA C 56.2 . 1 702 . 74 ARG CB C 33.8 . 1 703 . 74 ARG CG C 26.9 . 1 704 . 74 ARG CD C 42.9 . 1 705 . 74 ARG N N 118.7 . 1 706 . 75 ASP H H 9.03 . 1 707 . 75 ASP HA H 5.03 . 1 708 . 75 ASP HB2 H 3.06 . 1 709 . 75 ASP HB3 H 2.34 . 1 710 . 75 ASP CA C 53.7 . 1 711 . 75 ASP CB C 42.8 . 1 712 . 75 ASP N N 125.3 . 1 713 . 76 SER H H 8.21 . 1 714 . 76 SER HA H 4.92 . 1 715 . 76 SER HB2 H 4.07 . 1 716 . 76 SER HB3 H 3.83 . 1 717 . 76 SER CA C 56.5 . 1 718 . 76 SER CB C 64.3 . 1 719 . 76 SER N N 124.4 . 1 720 . 77 LEU H H 7.91 . 1 721 . 77 LEU HA H 3.67 . 1 722 . 77 LEU HB2 H 1.64 . 1 723 . 77 LEU HB3 H 1.33 . 1 724 . 77 LEU HG H 1.53 . 1 725 . 77 LEU HD1 H 0.63 . 1 726 . 77 LEU HD2 H 0.63 . 1 727 . 77 LEU CA C 57.8 . 1 728 . 77 LEU CB C 43.8 . 1 729 . 77 LEU CG C 27.0 . 1 730 . 77 LEU CD1 C 24.9 . 1 731 . 77 LEU CD2 C 26.5 . 1 732 . 77 LEU N N 124.8 . 1 733 . 78 LEU H H 7.59 . 1 734 . 78 LEU HA H 4.48 . 1 735 . 78 LEU HB2 H 1.76 . 1 736 . 78 LEU HB3 H 1.64 . 1 737 . 78 LEU HG H 1.56 . 1 738 . 78 LEU HD1 H 0.82 . 1 739 . 78 LEU HD2 H 0.66 . 1 740 . 78 LEU CA C 52.9 . 1 741 . 78 LEU CB C 40.7 . 1 742 . 78 LEU CG C 29.5 . 1 743 . 78 LEU CD1 C 25.9 . 1 744 . 78 LEU CD2 C 22.0 . 1 745 . 78 LEU N N 123.5 . 1 746 . 79 GLN H H 7.34 . 1 747 . 79 GLN HA H 4.23 . 1 748 . 79 GLN HB2 H 2.07 . 1 749 . 79 GLN HB3 H 1.98 . 1 750 . 79 GLN HG2 H 2.26 . 1 751 . 79 GLN HG3 H 2.26 . 1 752 . 79 GLN HE21 H 7.58 . 1 753 . 79 GLN HE22 H 6.86 . 1 754 . 79 GLN CA C 55.9 . 1 755 . 79 GLN CB C 30.1 . 1 756 . 79 GLN CG C 33.9 . 1 757 . 79 GLN N N 122.0 . 1 758 . 79 GLN NE2 N 113.3 . 1 759 . 80 ASP H H 8.63 . 1 760 . 80 ASP HA H 3.87 . 1 761 . 80 ASP HB2 H 2.52 . 1 762 . 80 ASP HB3 H 2.52 . 1 763 . 80 ASP CA C 55.9 . 1 764 . 80 ASP CB C 41.0 . 1 765 . 80 ASP N N 128.2 . 1 766 . 81 GLY H H 6.88 . 1 767 . 81 GLY HA2 H 4.12 . 1 768 . 81 GLY HA3 H 3.62 . 1 769 . 81 GLY CA C 45.3 . 1 770 . 82 GLU H H 7.36 . 1 771 . 82 GLU HA H 4.42 . 1 772 . 82 GLU HB2 H 2.07 . 1 773 . 82 GLU HB3 H 1.82 . 1 774 . 82 GLU HG2 H 2.10 . 1 775 . 82 GLU HG3 H 2.10 . 1 776 . 82 GLU CA C 58.0 . 1 777 . 82 GLU CB C 32.1 . 1 778 . 82 GLU CG C 36.5 . 1 779 . 82 GLU N N 121.6 . 1 780 . 83 PHE H H 8.02 . 1 781 . 83 PHE HA H 4.88 . 1 782 . 83 PHE HB2 H 3.60 . 1 783 . 83 PHE HB3 H 3.38 . 1 784 . 83 PHE HD1 H 7.33 . 1 785 . 83 PHE HD2 H 7.33 . 1 786 . 83 PHE HE1 H 7.02 . 1 787 . 83 PHE HE2 H 7.02 . 1 788 . 83 PHE CA C 57.5 . 1 789 . 83 PHE CB C 37.7 . 1 790 . 83 PHE N N 114.0 . 1 791 . 84 SER H H 7.04 . 1 792 . 84 SER HA H 5.78 . 1 793 . 84 SER HB2 H 3.73 . 1 794 . 84 SER HB3 H 3.66 . 1 795 . 84 SER CA C 57.3 . 1 796 . 84 SER CB C 68.2 . 1 797 . 84 SER N N 110.8 . 1 798 . 85 MET H H 9.37 . 1 799 . 85 MET HA H 5.01 . 1 800 . 85 MET HB2 H 2.21 . 1 801 . 85 MET HB3 H 1.89 . 1 802 . 85 MET HG2 H 2.46 . 1 803 . 85 MET HG3 H 2.26 . 1 804 . 85 MET HE H 1.51 . 1 805 . 85 MET CA C 54.8 . 1 806 . 85 MET CB C 39.6 . 1 807 . 85 MET CG C 32.3 . 1 808 . 85 MET CE C 37.4 . 1 809 . 85 MET N N 122.3 . 1 810 . 86 ASP H H 8.89 . 1 811 . 86 ASP HA H 5.80 . 1 812 . 86 ASP HB2 H 3.16 . 1 813 . 86 ASP HB3 H 2.41 . 1 814 . 86 ASP CA C 53.1 . 1 815 . 86 ASP CB C 42.3 . 1 816 . 86 ASP N N 125.6 . 1 817 . 87 LEU H H 9.90 . 1 818 . 87 LEU HA H 5.34 . 1 819 . 87 LEU HB2 H 1.75 . 1 820 . 87 LEU HB3 H 1.35 . 1 821 . 87 LEU HG H 1.44 . 1 822 . 87 LEU HD1 H 0.66 . 1 823 . 87 LEU HD2 H 0.66 . 1 824 . 87 LEU CA C 54.3 . 1 825 . 87 LEU CB C 47.1 . 1 826 . 87 LEU CG C 28.1 . 1 827 . 87 LEU CD1 C 28.1 . 1 828 . 87 LEU CD2 C 28.1 . 1 829 . 87 LEU N N 123.2 . 1 830 . 88 ARG H H 8.69 . 1 831 . 88 ARG HA H 5.43 . 1 832 . 88 ARG HB2 H 1.76 . 1 833 . 88 ARG HB3 H 1.68 . 1 834 . 88 ARG HG2 H 1.85 . 1 835 . 88 ARG HG3 H 1.52 . 1 836 . 88 ARG HD2 H 3.12 . 1 837 . 88 ARG HD3 H 3.12 . 1 838 . 88 ARG CA C 54.8 . 1 839 . 88 ARG CB C 34.3 . 1 840 . 88 ARG CG C 27.4 . 1 841 . 88 ARG CD C 43.7 . 1 842 . 88 ARG N N 121.4 . 1 843 . 89 THR H H 9.19 . 1 844 . 89 THR HA H 4.69 . 1 845 . 89 THR HB H 4.50 . 1 846 . 89 THR HG2 H 1.43 . 1 847 . 89 THR CA C 63.4 . 1 848 . 89 THR CB C 69.7 . 1 849 . 89 THR CG2 C 23.4 . 1 850 . 89 THR N N 117.2 . 1 851 . 90 LYS H H 8.08 . 1 852 . 90 LYS HA H 4.50 . 1 853 . 90 LYS HB2 H 1.70 . 1 854 . 90 LYS HB3 H 1.43 . 1 855 . 90 LYS HG2 H 1.29 . 1 856 . 90 LYS HG3 H 1.29 . 1 857 . 90 LYS HD2 H 1.56 . 1 858 . 90 LYS HD3 H 1.56 . 1 859 . 90 LYS HE2 H 2.80 . 1 860 . 90 LYS HE3 H 2.80 . 1 861 . 90 LYS CA C 55.5 . 1 862 . 90 LYS CB C 34.0 . 1 863 . 90 LYS CG C 25.6 . 1 864 . 90 LYS CD C 29.5 . 1 865 . 90 LYS CE C 42.1 . 1 866 . 90 LYS N N 120.4 . 1 867 . 91 SER H H 8.44 . 1 868 . 91 SER HA H 4.63 . 1 869 . 91 SER HB2 H 3.72 . 1 870 . 91 SER HB3 H 3.53 . 1 871 . 91 SER CA C 56.7 . 1 872 . 91 SER CB C 65.4 . 1 873 . 91 SER N N 120.1 . 1 874 . 92 THR H H 8.28 . 1 875 . 92 THR HA H 4.59 . 1 876 . 92 THR HB H 4.16 . 1 877 . 92 THR HG2 H 1.16 . 1 878 . 92 THR CA C 61.5 . 1 879 . 92 THR CB C 70.6 . 1 880 . 92 THR CG2 C 21.6 . 1 881 . 92 THR N N 115.8 . 1 882 . 93 GLY H H 8.88 . 1 883 . 93 GLY HA2 H 3.87 . 1 884 . 93 GLY HA3 H 3.87 . 1 885 . 93 GLY CA C 46.6 . 1 886 . 93 GLY N N 112.2 . 1 887 . 94 GLY H H 8.68 . 1 888 . 94 GLY HA2 H 3.95 . 1 889 . 94 GLY HA3 H 3.67 . 1 890 . 94 GLY CA C 45.3 . 1 891 . 94 GLY N N 109.9 . 1 892 . 95 ALA H H 7.18 . 1 893 . 95 ALA HA H 4.49 . 1 894 . 95 ALA HB H 1.49 . 1 895 . 95 ALA CA C 51.0 . 1 896 . 95 ALA CB C 17.6 . 1 897 . 95 ALA N N 124.3 . 1 898 . 96 PRO HA H 4.25 . 1 899 . 96 PRO HB2 H 2.00 . 1 900 . 96 PRO HB3 H 1.33 . 1 901 . 96 PRO HG2 H 1.92 . 1 902 . 96 PRO HG3 H 1.92 . 1 903 . 96 PRO HD2 H 3.75 . 1 904 . 96 PRO HD3 H 3.54 . 1 905 . 96 PRO CA C 63.2 . 1 906 . 96 PRO CB C 32.5 . 1 907 . 96 PRO CG C 27.5 . 1 908 . 96 PRO CD C 50.3 . 1 909 . 97 THR H H 7.69 . 1 910 . 97 THR HA H 3.67 . 1 911 . 97 THR HB H 4.11 . 1 912 . 97 THR HG2 H 1.00 . 1 913 . 97 THR CA C 59.7 . 1 914 . 97 THR CB C 71.5 . 1 915 . 97 THR CG2 C 21.9 . 1 916 . 97 THR N N 111.5 . 1 917 . 98 PHE H H 8.35 . 1 918 . 98 PHE HA H 4.90 . 1 919 . 98 PHE HB2 H 3.43 . 1 920 . 98 PHE HB3 H 2.65 . 1 921 . 98 PHE HD1 H 7.08 . 1 922 . 98 PHE HD2 H 7.08 . 1 923 . 98 PHE HE1 H 7.22 . 1 924 . 98 PHE HE2 H 7.22 . 1 925 . 98 PHE HZ H 7.31 . 1 926 . 98 PHE CA C 55.5 . 1 927 . 98 PHE CB C 41.8 . 1 928 . 98 PHE CE1 C 130.6 . 1 929 . 98 PHE CE2 C 130.6 . 1 930 . 98 PHE N N 119.7 . 1 931 . 99 ASN H H 8.90 . 1 932 . 99 ASN HA H 5.25 . 1 933 . 99 ASN HB2 H 3.11 . 1 934 . 99 ASN HB3 H 2.48 . 1 935 . 99 ASN HD21 H 7.71 . 1 936 . 99 ASN HD22 H 6.99 . 1 937 . 99 ASN CA C 54.7 . 1 938 . 99 ASN CB C 40.3 . 1 939 . 99 ASN N N 121.4 . 1 940 . 99 ASN ND2 N 115.1 . 1 941 . 100 VAL H H 8.59 . 1 942 . 100 VAL HA H 5.56 . 1 943 . 100 VAL HB H 1.79 . 1 944 . 100 VAL HG1 H 1.05 . 1 945 . 100 VAL HG2 H 0.88 . 1 946 . 100 VAL CA C 59.5 . 1 947 . 100 VAL CB C 37.5 . 1 948 . 100 VAL CG1 C 23.0 . 1 949 . 100 VAL CG2 C 21.5 . 1 950 . 100 VAL N N 123.6 . 1 951 . 101 THR H H 8.45 . 1 952 . 101 THR HA H 5.62 . 1 953 . 101 THR HB H 3.54 . 1 954 . 101 THR HG2 H 1.43 . 1 955 . 101 THR CA C 63.1 . 1 956 . 101 THR CB C 73.8 . 1 957 . 101 THR CG2 C 23.6 . 1 958 . 101 THR N N 123.0 . 1 959 . 102 VAL H H 9.08 . 1 960 . 102 VAL HA H 5.15 . 1 961 . 102 VAL HB H 1.76 . 1 962 . 102 VAL HG1 H 0.74 . 1 963 . 102 VAL HG2 H 0.67 . 1 964 . 102 VAL CA C 59.7 . 1 965 . 102 VAL CB C 35.0 . 1 966 . 102 VAL CG1 C 22.4 . 1 967 . 102 VAL CG2 C 21.5 . 1 968 . 102 VAL N N 127.8 . 1 969 . 103 THR H H 9.25 . 1 970 . 103 THR HA H 5.39 . 1 971 . 103 THR HB H 3.88 . 1 972 . 103 THR HG2 H 1.15 . 1 973 . 103 THR CA C 60.3 . 1 974 . 103 THR CB C 72.0 . 1 975 . 103 THR CG2 C 22.9 . 1 976 . 103 THR N N 120.5 . 1 977 . 104 LYS H H 8.20 . 1 978 . 104 LYS HA H 5.09 . 1 979 . 104 LYS HB2 H 1.68 . 1 980 . 104 LYS HB3 H 1.14 . 1 981 . 104 LYS HG2 H 1.52 . 1 982 . 104 LYS HG3 H 0.95 . 1 983 . 104 LYS HD2 H 1.27 . 1 984 . 104 LYS HD3 H 1.04 . 1 985 . 104 LYS HE2 H 2.73 . 1 986 . 104 LYS HE3 H 2.60 . 1 987 . 104 LYS CA C 55.1 . 1 988 . 104 LYS CB C 37.4 . 1 989 . 104 LYS CG C 23.9 . 1 990 . 104 LYS CD C 30.0 . 1 991 . 104 LYS CE C 41.0 . 1 992 . 104 LYS N N 124.7 . 1 993 . 105 THR H H 9.63 . 1 994 . 105 THR HA H 4.51 . 1 995 . 105 THR HB H 4.79 . 1 996 . 105 THR HG2 H 1.02 . 1 997 . 105 THR CA C 60.8 . 1 998 . 105 THR CB C 67.5 . 1 999 . 105 THR CG2 C 22.5 . 1 1000 . 105 THR N N 121.0 . 1 1001 . 106 ASP H H 9.08 . 1 1002 . 106 ASP HA H 4.39 . 1 1003 . 106 ASP HB2 H 2.57 . 1 1004 . 106 ASP HB3 H 2.34 . 1 1005 . 106 ASP CA C 59.0 . 1 1006 . 106 ASP CB C 41.9 . 1 1007 . 106 ASP N N 122.2 . 1 1008 . 107 LYS H H 8.50 . 1 1009 . 107 LYS HA H 4.04 . 1 1010 . 107 LYS HB2 H 1.95 . 1 1011 . 107 LYS HB3 H 1.95 . 1 1012 . 107 LYS HG2 H 1.39 . 1 1013 . 107 LYS HG3 H 1.24 . 1 1014 . 107 LYS HD2 H 1.83 . 1 1015 . 107 LYS HD3 H 1.65 . 1 1016 . 107 LYS HE2 H 3.00 . 1 1017 . 107 LYS HE3 H 3.00 . 1 1018 . 107 LYS CA C 55.6 . 1 1019 . 107 LYS CB C 36.4 . 1 1020 . 107 LYS CG C 26.0 . 1 1021 . 107 LYS CD C 29.2 . 1 1022 . 107 LYS CE C 42.1 . 1 1023 . 107 LYS N N 111.9 . 1 1024 . 108 THR H H 7.77 . 1 1025 . 108 THR HA H 5.27 . 1 1026 . 108 THR HB H 3.27 . 1 1027 . 108 THR HG2 H 0.25 . 1 1028 . 108 THR CA C 60.0 . 1 1029 . 108 THR CB C 72.1 . 1 1030 . 108 THR CG2 C 21.5 . 1 1031 . 108 THR N N 112.7 . 1 1032 . 109 LEU H H 9.04 . 1 1033 . 109 LEU HA H 5.14 . 1 1034 . 109 LEU HB2 H 1.34 . 1 1035 . 109 LEU HB3 H 0.82 . 1 1036 . 109 LEU HG H 1.38 . 1 1037 . 109 LEU HD1 H 0.44 . 1 1038 . 109 LEU HD2 H 0.28 . 1 1039 . 109 LEU CA C 55.3 . 1 1040 . 109 LEU CB C 44.3 . 1 1041 . 109 LEU CG C 26.7 . 1 1042 . 109 LEU CD1 C 27.3 . 1 1043 . 109 LEU CD2 C 23.2 . 1 1044 . 109 LEU N N 117.2 . 1 1045 . 110 VAL H H 8.73 . 1 1046 . 110 VAL HA H 4.53 . 1 1047 . 110 VAL HB H 2.00 . 1 1048 . 110 VAL HG1 H 0.82 . 1 1049 . 110 VAL HG2 H 0.64 . 1 1050 . 110 VAL CA C 61.2 . 1 1051 . 110 VAL CB C 32.2 . 1 1052 . 110 VAL CG1 C 22.0 . 1 1053 . 110 VAL CG2 C 21.9 . 1 1054 . 110 VAL N N 123.5 . 1 1055 . 111 LEU H H 8.83 . 1 1056 . 111 LEU HA H 5.09 . 1 1057 . 111 LEU HB2 H 0.48 . 1 1058 . 111 LEU HB3 H 0.48 . 1 1059 . 111 LEU HG H 1.16 . 1 1060 . 111 LEU HD1 H 0.33 . 1 1061 . 111 LEU HD2 H 0.04 . 1 1062 . 111 LEU CA C 55.6 . 1 1063 . 111 LEU CB C 44.3 . 1 1064 . 111 LEU CG C 29.2 . 1 1065 . 111 LEU CD1 C 27.2 . 1 1066 . 111 LEU CD2 C 29.2 . 1 1067 . 111 LEU N N 125.9 . 1 1068 . 112 LEU H H 8.21 . 1 1069 . 112 LEU HA H 5.20 . 1 1070 . 112 LEU HB2 H 1.82 . 1 1071 . 112 LEU HB3 H 1.44 . 1 1072 . 112 LEU HG H 1.73 . 1 1073 . 112 LEU HD1 H 1.23 . 1 1074 . 112 LEU HD2 H 1.20 . 1 1075 . 112 LEU CA C 54.1 . 1 1076 . 112 LEU CB C 49.0 . 1 1077 . 112 LEU CG C 27.8 . 1 1078 . 112 LEU CD1 C 27.1 . 1 1079 . 112 LEU CD2 C 25.6 . 1 1080 . 112 LEU N N 120.7 . 1 1081 . 113 MET H H 8.60 . 1 1082 . 113 MET HA H 5.44 . 1 1083 . 113 MET HB2 H 1.98 . 1 1084 . 113 MET HB3 H 1.64 . 1 1085 . 113 MET HG2 H 2.46 . 1 1086 . 113 MET HG3 H 2.32 . 1 1087 . 113 MET HE H 2.18 . 1 1088 . 113 MET CA C 53.9 . 1 1089 . 113 MET CB C 38.0 . 1 1090 . 113 MET CG C 30.2 . 1 1091 . 113 MET CE C 35.1 . 1 1092 . 113 MET N N 123.8 . 1 1093 . 114 GLY H H 9.58 . 1 1094 . 114 GLY HA2 H 4.72 . 1 1095 . 114 GLY HA3 H 4.01 . 1 1096 . 114 GLY CA C 46.3 . 1 1097 . 114 GLY N N 115.9 . 1 1098 . 115 LYS H H 7.84 . 1 1099 . 115 LYS HA H 4.10 . 1 1100 . 115 LYS HB2 H 1.98 . 1 1101 . 115 LYS HB3 H 1.68 . 1 1102 . 115 LYS HG2 H 1.14 . 1 1103 . 115 LYS HG3 H 1.03 . 1 1104 . 115 LYS HD2 H 1.68 . 1 1105 . 115 LYS HD3 H 1.59 . 1 1106 . 115 LYS HE2 H 2.81 . 1 1107 . 115 LYS HE3 H 2.61 . 1 1108 . 115 LYS CA C 57.5 . 1 1109 . 115 LYS CB C 34.3 . 1 1110 . 115 LYS CG C 28.2 . 1 1111 . 115 LYS CD C 29.5 . 1 1112 . 115 LYS CE C 42.0 . 1 1113 . 115 LYS N N 118.7 . 1 1114 . 116 GLU H H 9.20 . 1 1115 . 116 GLU HA H 4.13 . 1 1116 . 116 GLU HB2 H 2.21 . 1 1117 . 116 GLU HB3 H 2.02 . 1 1118 . 116 GLU HG2 H 2.29 . 1 1119 . 116 GLU HG3 H 2.29 . 1 1120 . 116 GLU CA C 58.4 . 1 1121 . 116 GLU CB C 29.8 . 1 1122 . 116 GLU N N 123.9 . 1 1123 . 117 GLY H H 9.26 . 1 1124 . 117 GLY HA2 H 4.15 . 1 1125 . 117 GLY HA3 H 3.72 . 1 1126 . 117 GLY CA C 45.7 . 1 1127 . 117 GLY N N 115.1 . 1 1128 . 118 VAL H H 7.44 . 1 1129 . 118 VAL HA H 4.01 . 1 1130 . 118 VAL HB H 2.08 . 1 1131 . 118 VAL HG1 H 1.19 . 1 1132 . 118 VAL HG2 H 1.11 . 1 1133 . 118 VAL CA C 63.7 . 1 1134 . 118 VAL CB C 32.1 . 1 1135 . 118 VAL CG1 C 18.1 . 1 1136 . 118 VAL CG2 C 22.1 . 1 1137 . 118 VAL N N 122.4 . 1 1138 . 119 HIS H H 8.82 . 1 1139 . 119 HIS HA H 4.25 . 1 1140 . 119 HIS HB2 H 3.28 . 1 1141 . 119 HIS HB3 H 3.12 . 1 1142 . 119 HIS CA C 58.4 . 1 1143 . 119 HIS CB C 32.1 . 1 1144 . 119 HIS N N 130.6 . 1 1145 . 120 GLY H H 8.81 . 1 1146 . 120 GLY HA2 H 3.89 . 1 1147 . 120 GLY HA3 H 3.63 . 1 1148 . 120 GLY CA C 47.3 . 1 1149 . 120 GLY N N 113.5 . 1 1150 . 121 GLY H H 9.73 . 1 1151 . 121 GLY HA2 H 3.93 . 1 1152 . 121 GLY HA3 H 3.93 . 1 1153 . 121 GLY CA C 46.9 . 1 1154 . 121 GLY N N 113.3 . 1 1155 . 122 LEU H H 7.15 . 1 1156 . 122 LEU HA H 4.18 . 1 1157 . 122 LEU HB2 H 1.75 . 1 1158 . 122 LEU HB3 H 1.75 . 1 1159 . 122 LEU HG H 1.59 . 1 1160 . 122 LEU HD1 H 1.00 . 1 1161 . 122 LEU HD2 H 0.90 . 1 1162 . 122 LEU CA C 58.0 . 1 1163 . 122 LEU CB C 41.9 . 1 1164 . 122 LEU CG C 27.5 . 1 1165 . 122 LEU CD1 C 24.4 . 1 1166 . 122 LEU CD2 C 25.2 . 1 1167 . 122 LEU N N 124.7 . 1 1168 . 123 ILE H H 7.00 . 1 1169 . 123 ILE HA H 3.57 . 1 1170 . 123 ILE HB H 2.13 . 1 1171 . 123 ILE HG12 H 1.55 . 1 1172 . 123 ILE HG13 H 1.29 . 1 1173 . 123 ILE HG2 H 0.88 . 1 1174 . 123 ILE HD1 H 0.80 . 1 1175 . 123 ILE CA C 62.2 . 1 1176 . 123 ILE CB C 36.4 . 1 1177 . 123 ILE CG1 C 27.6 . 1 1178 . 123 ILE CG2 C 18.7 . 1 1179 . 123 ILE CD1 C 12.9 . 1 1180 . 123 ILE N N 119.9 . 1 1181 . 124 ASN H H 8.24 . 1 1182 . 124 ASN HA H 4.30 . 1 1183 . 124 ASN HB2 H 2.85 . 1 1184 . 124 ASN HB3 H 2.62 . 1 1185 . 124 ASN HD21 H 9.36 . 1 1186 . 124 ASN HD22 H 6.30 . 1 1187 . 124 ASN CA C 57.6 . 1 1188 . 124 ASN CB C 40.0 . 1 1189 . 124 ASN N N 120.1 . 1 1190 . 124 ASN ND2 N 116.6 . 1 1191 . 125 LYS H H 7.81 . 1 1192 . 125 LYS HA H 4.01 . 1 1193 . 125 LYS HB2 H 1.94 . 1 1194 . 125 LYS HB3 H 1.94 . 1 1195 . 125 LYS HG2 H 1.53 . 1 1196 . 125 LYS HG3 H 1.53 . 1 1197 . 125 LYS HD2 H 2.20 . 1 1198 . 125 LYS HD3 H 2.07 . 1 1199 . 125 LYS HE2 H 2.63 . 1 1200 . 125 LYS HE3 H 2.36 . 1 1201 . 125 LYS CA C 59.5 . 1 1202 . 125 LYS CB C 32.6 . 1 1203 . 125 LYS CD C 29.6 . 1 1204 . 125 LYS CE C 37.0 . 1 1205 . 125 LYS N N 120.0 . 1 1206 . 126 LYS H H 8.04 . 1 1207 . 126 LYS HA H 4.04 . 1 1208 . 126 LYS HB2 H 1.76 . 1 1209 . 126 LYS HB3 H 1.68 . 1 1210 . 126 LYS HG2 H 1.44 . 1 1211 . 126 LYS HG3 H 1.44 . 1 1212 . 126 LYS HD2 H 1.66 . 1 1213 . 126 LYS HD3 H 1.66 . 1 1214 . 126 LYS HE2 H 2.95 . 1 1215 . 126 LYS HE3 H 2.95 . 1 1216 . 126 LYS CA C 59.7 . 1 1217 . 126 LYS CB C 33.5 . 1 1218 . 126 LYS CG C 25.1 . 1 1219 . 126 LYS CD C 29.1 . 1 1220 . 126 LYS CE C 41.9 . 1 1221 . 126 LYS N N 119.5 . 1 1222 . 127 CYS H H 8.35 . 1 1223 . 127 CYS HA H 3.81 . 1 1224 . 127 CYS HB2 H 3.02 . 1 1225 . 127 CYS HB3 H 2.92 . 1 1226 . 127 CYS CA C 62.3 . 1 1227 . 127 CYS CB C 26.5 . 1 1228 . 127 CYS N N 121.2 . 1 1229 . 128 TYR H H 9.13 . 1 1230 . 128 TYR HA H 4.04 . 1 1231 . 128 TYR HB2 H 3.18 . 1 1232 . 128 TYR HB3 H 3.18 . 1 1233 . 128 TYR HD1 H 7.07 . 1 1234 . 128 TYR HD2 H 7.07 . 1 1235 . 128 TYR HE1 H 6.88 . 1 1236 . 128 TYR HE2 H 6.88 . 1 1237 . 128 TYR CA C 62.0 . 1 1238 . 128 TYR CB C 38.7 . 1 1239 . 128 TYR CD1 C 133.2 . 1 1240 . 128 TYR CD2 C 133.2 . 1 1241 . 128 TYR CE1 C 118.2 . 1 1242 . 128 TYR CE2 C 118.2 . 1 1243 . 128 TYR N N 121.6 . 1 1244 . 129 GLU H H 8.75 . 1 1245 . 129 GLU HA H 3.99 . 1 1246 . 129 GLU HB2 H 2.20 . 1 1247 . 129 GLU HB3 H 2.08 . 1 1248 . 129 GLU HG2 H 2.61 . 1 1249 . 129 GLU HG3 H 2.36 . 1 1250 . 129 GLU CA C 59.9 . 1 1251 . 129 GLU CB C 29.3 . 1 1252 . 129 GLU CG C 37.1 . 1 1253 . 129 GLU N N 121.3 . 1 1254 . 130 MET H H 7.57 . 1 1255 . 130 MET HA H 4.72 . 1 1256 . 130 MET HB2 H 2.18 . 1 1257 . 130 MET HB3 H 2.18 . 1 1258 . 130 MET HG2 H 2.63 . 1 1259 . 130 MET HG3 H 2.28 . 1 1260 . 130 MET CA C 56.9 . 1 1261 . 130 MET CB C 31.2 . 1 1262 . 130 MET CG C 31.9 . 1 1263 . 130 MET N N 120.4 . 1 1264 . 131 ALA H H 8.45 . 1 1265 . 131 ALA HA H 3.77 . 1 1266 . 131 ALA HB H 1.38 . 1 1267 . 131 ALA CA C 55.6 . 1 1268 . 131 ALA CB C 17.6 . 1 1269 . 131 ALA N N 123.0 . 1 1270 . 132 SER H H 8.38 . 1 1271 . 132 SER HA H 3.98 . 1 1272 . 132 SER HB2 H 3.83 . 1 1273 . 132 SER HB3 H 3.83 . 1 1274 . 132 SER CA C 61.7 . 1 1275 . 132 SER CB C 63.6 . 1 1276 . 132 SER N N 113.7 . 1 1277 . 133 HIS H H 7.73 . 1 1278 . 133 HIS HA H 4.31 . 1 1279 . 133 HIS HB2 H 3.48 . 1 1280 . 133 HIS HB3 H 3.28 . 1 1281 . 133 HIS CA C 59.8 . 1 1282 . 133 HIS CB C 30.0 . 1 1283 . 133 HIS N N 122.7 . 1 1284 . 134 LEU H H 8.30 . 1 1285 . 134 LEU HA H 3.97 . 1 1286 . 134 LEU HB2 H 1.97 . 1 1287 . 134 LEU HB3 H 1.36 . 1 1288 . 134 LEU HG H 1.68 . 1 1289 . 134 LEU HD1 H 0.67 . 1 1290 . 134 LEU HD2 H 0.67 . 1 1291 . 134 LEU CA C 59.1 . 1 1292 . 134 LEU CB C 41.4 . 1 1293 . 134 LEU CG C 28.0 . 1 1294 . 134 LEU CD1 C 26.3 . 1 1295 . 134 LEU CD2 C 23.4 . 1 1296 . 134 LEU N N 121.8 . 1 1297 . 135 ARG H H 8.75 . 1 1298 . 135 ARG HA H 4.41 . 1 1299 . 135 ARG HB2 H 1.88 . 1 1300 . 135 ARG HB3 H 1.88 . 1 1301 . 135 ARG HG2 H 1.61 . 1 1302 . 135 ARG HG3 H 1.56 . 1 1303 . 135 ARG HD2 H 3.11 . 1 1304 . 135 ARG HD3 H 2.96 . 1 1305 . 135 ARG CA C 59.9 . 1 1306 . 135 ARG CB C 29.6 . 1 1307 . 135 ARG CG C 27.4 . 1 1308 . 135 ARG CD C 43.1 . 1 1309 . 135 ARG N N 121.0 . 1 1310 . 136 ARG H H 7.90 . 1 1311 . 136 ARG HA H 4.16 . 1 1312 . 136 ARG HB2 H 1.98 . 1 1313 . 136 ARG HB3 H 1.98 . 1 1314 . 136 ARG HG2 H 1.89 . 1 1315 . 136 ARG HG3 H 1.67 . 1 1316 . 136 ARG HD2 H 3.26 . 1 1317 . 136 ARG HD3 H 3.19 . 1 1318 . 136 ARG CA C 58.9 . 1 1319 . 136 ARG CB C 30.2 . 1 1320 . 136 ARG CG C 28.4 . 1 1321 . 136 ARG CD C 43.4 . 1 1322 . 136 ARG N N 120.7 . 1 1323 . 137 SER H H 7.50 . 1 1324 . 137 SER HA H 4.57 . 1 1325 . 137 SER HB2 H 4.14 . 1 1326 . 137 SER HB3 H 4.01 . 1 1327 . 137 SER CA C 58.1 . 1 1328 . 137 SER CB C 63.8 . 1 1329 . 137 SER N N 115.4 . 1 1330 . 138 GLN H H 7.74 . 1 1331 . 138 GLN HA H 3.96 . 1 1332 . 138 GLN HB2 H 2.19 . 1 1333 . 138 GLN HB3 H 2.19 . 1 1334 . 138 GLN HG2 H 2.20 . 1 1335 . 138 GLN HG3 H 2.20 . 1 1336 . 138 GLN HE21 H 7.45 . 1 1337 . 138 GLN HE22 H 6.75 . 1 1338 . 138 GLN CA C 58.0 . 1 1339 . 138 GLN CB C 25.5 . 1 1340 . 138 GLN CG C 34.7 . 1 1341 . 138 GLN N N 111.9 . 1 1342 . 138 GLN NE2 N 113.1 . 1 1343 . 139 TYR H H 8.12 . 1 1344 . 139 TYR HA H 4.45 . 1 1345 . 139 TYR HB2 H 2.63 . 1 1346 . 139 TYR HB3 H 2.63 . 1 1347 . 139 TYR HD1 H 7.21 . 1 1348 . 139 TYR HD2 H 7.21 . 1 1349 . 139 TYR HE1 H 6.98 . 1 1350 . 139 TYR HE2 H 6.98 . 1 1351 . 139 TYR CA C 59.9 . 1 1352 . 139 TYR CB C 41.5 . 1 1353 . 139 TYR CD1 C 132.9 . 1 1354 . 139 TYR CD2 C 132.9 . 1 1355 . 139 TYR CE1 C 117.9 . 1 1356 . 139 TYR CE2 C 117.9 . 1 1357 . 139 TYR N N 124.9 . 1 stop_ save_