data_4080 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of Calcium-Saturated Skeletal Muscle Troponin C ; _BMRB_accession_number 4080 _BMRB_flat_file_name bmr4080.str _Entry_type update _Submission_date 1997-12-07 _Accession_date 1997-12-07 _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 Slupsky Carolyn M. . 2 Sykes Brian D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 541 "13C chemical shifts" 272 "15N chemical shifts" 8 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 ; Slupsky, C. M. and Sykes, B. D., "NMR Solution Structure of Calcium-Saturated Skeletal Muscle Troponin C," Biochemistry 34, 15953-15964 (1995). ; _Citation_title 'NMR Solution Structure of Calcium-Saturated Skeletal Muscle Troponin C' _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 Slupsky Carolyn M. . 2 Sykes Brian D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 34 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14953 _Page_last 15964 _Year 1995 _Details . loop_ _Keyword 'Troponin C' TnC stop_ save_ ################################## # Molecular system description # ################################## save_system_TnC _Saveframe_category molecular_system _Mol_system_name 'Troponin C' _Abbreviation_common TnC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TnC $TnC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function ; Troponin C is a a thin filament calcium-binding protein responsible for triggering muscle contraction from the sarcoplasmic reticulum ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TnC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Troponin C' _Abbreviation_common TnC _Molecular_mass 18000 _Mol_thiol_state 'all free' _Details ; Troponin C (TnC) is a member of a trimer of proteins called Troponin complex (TnI and TnT are the other two components) ; ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; ASMTDQQAEARAFLSEEMIA EFKAAFDMFDADGGGDISTK ELGTVMRMLGQNPTKEELDA IIEEVDEDGSGTIDFEEFLV MMVRQMKEDAKGKSEEELAN CFRIFDKNADGFIDIEELGE ILRATGEHVIEEDIEDLMKD SDKNNDGRIDFDEFLKMMEG VQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 MET 4 THR 5 ASP 6 GLN 7 GLN 8 ALA 9 GLU 10 ALA 11 ARG 12 ALA 13 PHE 14 LEU 15 SER 16 GLU 17 GLU 18 MET 19 ILE 20 ALA 21 GLU 22 PHE 23 LYS 24 ALA 25 ALA 26 PHE 27 ASP 28 MET 29 PHE 30 ASP 31 ALA 32 ASP 33 GLY 34 GLY 35 GLY 36 ASP 37 ILE 38 SER 39 THR 40 LYS 41 GLU 42 LEU 43 GLY 44 THR 45 VAL 46 MET 47 ARG 48 MET 49 LEU 50 GLY 51 GLN 52 ASN 53 PRO 54 THR 55 LYS 56 GLU 57 GLU 58 LEU 59 ASP 60 ALA 61 ILE 62 ILE 63 GLU 64 GLU 65 VAL 66 ASP 67 GLU 68 ASP 69 GLY 70 SER 71 GLY 72 THR 73 ILE 74 ASP 75 PHE 76 GLU 77 GLU 78 PHE 79 LEU 80 VAL 81 MET 82 MET 83 VAL 84 ARG 85 GLN 86 MET 87 LYS 88 GLU 89 ASP 90 ALA 91 LYS 92 GLY 93 LYS 94 SER 95 GLU 96 GLU 97 GLU 98 LEU 99 ALA 100 ASN 101 CYS 102 PHE 103 ARG 104 ILE 105 PHE 106 ASP 107 LYS 108 ASN 109 ALA 110 ASP 111 GLY 112 PHE 113 ILE 114 ASP 115 ILE 116 GLU 117 GLU 118 LEU 119 GLY 120 GLU 121 ILE 122 LEU 123 ARG 124 ALA 125 THR 126 GLY 127 GLU 128 HIS 129 VAL 130 ILE 131 GLU 132 GLU 133 ASP 134 ILE 135 GLU 136 ASP 137 LEU 138 MET 139 LYS 140 ASP 141 SER 142 ASP 143 LYS 144 ASN 145 ASN 146 ASP 147 GLY 148 ARG 149 ILE 150 ASP 151 PHE 152 ASP 153 GLU 154 PHE 155 LEU 156 LYS 157 MET 158 MET 159 GLU 160 GLY 161 VAL 162 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-02 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 1NCX "Troponin C" 100.00 162 99.38 99.38 1.09e-106 PDB 1NCY "Troponin-C, Complex With Manganese" 100.00 162 99.38 99.38 1.09e-106 PDB 1NCZ "Troponin C" 100.00 162 99.38 99.38 1.09e-106 PDB 1TNW "Nmr Solution Structure Of Calcium Saturated Skeletal Muscle Troponin C" 100.00 162 100.00 100.00 2.39e-107 PDB 1TNX "Nmr Solution Structure Of Calcium Saturated Skeletal Muscle Troponin C" 100.00 162 100.00 100.00 2.39e-107 PDB 1TOP "Structure Of Chicken Skeletal Muscle Troponin-C At 1.78 Angstroms Resolution" 100.00 162 99.38 99.38 1.09e-106 PDB 1YTZ "Crystal Structure Of Skeletal Muscle Troponin In The Ca2+- Activated State" 100.00 162 99.38 99.38 1.09e-106 PDB 1YV0 "Crystal Structure Of Skeletal Muscle Troponin In The Ca2+- Free State" 100.00 162 99.38 99.38 1.09e-106 PDB 2W49 "Isometrically Contracting Insect Asynchronous Flight Muscle" 98.15 159 99.37 99.37 1.51e-104 PDB 2W4U "Isometrically Contracting Insect Asynchronous Flight Muscle Quick Frozen After A Length Step" 98.15 159 99.37 99.37 1.51e-104 PDB 4TNC "Refined Structure Of Chicken Skeletal Muscle Troponin C In The Two-Calcium State At 2-Angstroms Resolution" 100.00 162 96.91 97.53 2.75e-103 PDB 5TNC "Refined Crystal Structure Of Troponin C From Turkey Skeletal Muscle At 2.0 Angstroms Resolution" 100.00 162 98.15 98.77 7.31e-105 GB AAA49097 "troponin C [Gallus gallus]" 100.00 163 100.00 100.00 3.46e-107 GB AAB19538 "troponin C, partial [Phasianidae]" 100.00 162 98.15 98.77 2.30e-105 GB KFM07723 "Troponin C, skeletal muscle, partial [Aptenodytes forsteri]" 100.00 162 97.53 98.15 9.00e-105 GB KFO77465 "Troponin C, skeletal muscle, partial [Cuculus canorus]" 100.00 163 97.53 98.15 2.96e-104 GB KFR04283 "Troponin C, skeletal muscle, partial [Nipponia nippon]" 100.00 163 97.53 98.15 2.96e-104 REF NP_990781 "troponin C, skeletal muscle [Gallus gallus]" 100.00 163 100.00 100.00 3.46e-107 REF XP_005240050 "PREDICTED: troponin C, skeletal muscle [Falco peregrinus]" 100.00 163 98.15 98.77 1.60e-105 REF XP_005445015 "PREDICTED: troponin C, skeletal muscle [Falco cherrug]" 100.00 163 98.15 98.77 1.60e-105 REF XP_009277803 "PREDICTED: troponin C, skeletal muscle isoform X1 [Aptenodytes forsteri]" 100.00 163 97.53 98.15 4.19e-105 REF XP_009277805 "PREDICTED: troponin C, skeletal muscle isoform X2 [Aptenodytes forsteri]" 100.00 163 97.53 98.15 4.19e-105 SP P02588 "RecName: Full=Troponin C, skeletal muscle" 100.00 163 99.38 99.38 1.14e-106 SP P10246 "RecName: Full=Troponin C, skeletal muscle" 100.00 162 98.15 98.77 2.30e-105 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $TnC chicken 9031 Eukaryota Metazoa Gallus gallus 'skeletal muscle' 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 _Details $TnC 'E. coli' 'recombinant technology' Escherichia coli . plasmid pET3a native stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_TnC _Saveframe_category sample _Sample_type solution _Details ; Chemical shifts are for E. coli expressed chicken skeletal Troponin C (modified at cysteine 101 with a carboxamidomethyl group) in solutions described above ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TnC 1.4 mM [U-15N] D2O 10 % . H2O 90 % . KCl 150 mM . CaCl2 16 mM . TFE 15 '% v/v' . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_TnC save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . n/a temperature 313 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal . . . . $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 external . . . . $entry_citation $entry_citation NH4Cl N 15 nitrogen ppm 24.93 external . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_TnC stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name TnC _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HB H 1.56 . 1 2 . 1 ALA CB C 20.0 . 1 3 . 2 SER HB2 H 3.90 . 1 4 . 2 SER CB C 64.4 . 1 5 . 3 MET HE H 2.07 . 1 6 . 3 MET CE C 16.9 . 1 7 . 4 THR HB H 4.29 . 1 8 . 4 THR HG2 H 1.20 . 1 9 . 4 THR CB C 69.9 . 1 10 . 4 THR CG2 C 21.7 . 1 11 . 5 ASP HB2 H 2.73 . 2 12 . 5 ASP HB3 H 2.62 . 2 13 . 5 ASP CB C 40.5 . 1 14 . 6 GLN HB2 H 2.25 . 2 15 . 6 GLN HB3 H 2.06 . 2 16 . 6 GLN HG2 H 2.44 . 2 17 . 6 GLN HG3 H 2.34 . 2 18 . 6 GLN CB C 31.2 . 1 19 . 8 ALA HB H 1.55 . 1 20 . 8 ALA CB C 17.8 . 1 21 . 9 GLU HB2 H 2.07 . 1 22 . 9 GLU HB3 H 2.07 . 1 23 . 9 GLU HG2 H 2.31 . 1 24 . 9 GLU HG3 H 2.21 . 2 25 . 9 GLU CB C 30.4 . 1 26 . 9 GLU CG C 36.1 . 1 27 . 10 ALA HB H 1.42 . 1 28 . 10 ALA CB C 17.7 . 1 29 . 11 ARG HB2 H 1.84 . 1 30 . 11 ARG HB3 H 1.84 . 1 31 . 11 ARG HG2 H 1.92 . 2 32 . 11 ARG HG3 H 1.71 . 2 33 . 11 ARG HD2 H 3.21 . 1 34 . 11 ARG HD3 H 3.21 . 1 35 . 11 ARG CG C 28.3 . 1 36 . 11 ARG CD C 44.0 . 1 37 . 12 ALA HB H 1.35 . 1 38 . 12 ALA CB C 19.0 . 1 39 . 13 PHE HB2 H 3.19 . 2 40 . 13 PHE HB3 H 3.14 . 2 41 . 13 PHE HD1 H 7.28 . 1 42 . 13 PHE HD2 H 7.28 . 1 43 . 13 PHE HE1 H 7.37 . 1 44 . 13 PHE HE2 H 7.37 . 1 45 . 13 PHE CB C 40.9 . 1 46 . 14 LEU HB2 H 1.97 . 2 47 . 14 LEU HB3 H 1.57 . 2 48 . 14 LEU HG H 1.90 . 1 49 . 14 LEU HD1 H 0.88 . 2 50 . 14 LEU HD2 H 0.92 . 2 51 . 14 LEU CB C 44.4 . 1 52 . 14 LEU CG C 27.8 . 1 53 . 14 LEU CD1 C 26.04 . 2 54 . 14 LEU CD2 C 23.87 . 2 55 . 15 SER HB2 H 4.39 . 2 56 . 15 SER HB3 H 4.01 . 2 57 . 15 SER CB C 65.9 . 1 58 . 16 GLU HB2 H 2.07 . 1 59 . 16 GLU HB3 H 2.07 . 1 60 . 16 GLU HG2 H 2.36 . 1 61 . 16 GLU HG3 H 2.36 . 1 62 . 16 GLU CB C 29.6 . 1 63 . 16 GLU CG C 37.5 . 1 64 . 17 GLU HB2 H 2.07 . 2 65 . 17 GLU HB3 H 1.95 . 2 66 . 17 GLU HG2 H 2.50 . 1 67 . 17 GLU HG3 H 2.30 . 2 68 . 17 GLU CB C 29.1 . 1 69 . 17 GLU CG C 37.8 . 1 70 . 18 MET HB2 H 2.14 . 2 71 . 18 MET HB3 H 1.93 . 2 72 . 18 MET HG2 H 2.48 . 2 73 . 18 MET HG3 H 2.35 . 2 74 . 18 MET HE H 1.98 . 1 75 . 18 MET CB C 32.6 . 1 76 . 18 MET CG C 32.7 . 1 77 . 18 MET CE C 16.7 . 1 78 . 19 ILE HB H 2.04 . 1 79 . 19 ILE HG12 H 1.64 . 2 80 . 19 ILE HG13 H 0.98 . 2 81 . 19 ILE HG2 H 1.15 . 1 82 . 19 ILE HD1 H 0.85 . 1 83 . 19 ILE CB C 37.8 . 1 84 . 19 ILE CG1 C 29.1 . 2 85 . 19 ILE CG2 C 17.7 . 2 86 . 19 ILE CD1 C 13.8 . 1 87 . 20 ALA HB H 1.52 . 1 88 . 20 ALA CB C 18.2 . 1 89 . 22 PHE HB2 H 3.56 . 2 90 . 22 PHE HB3 H 3.49 . 2 91 . 22 PHE HD1 H 7.18 . 1 92 . 22 PHE HD2 H 7.18 . 1 93 . 22 PHE HE1 H 7.34 . 1 94 . 22 PHE HE2 H 7.34 . 1 95 . 22 PHE CB C 38.3 . 1 96 . 23 LYS HB2 H 1.91 . 1 97 . 23 LYS HB3 H 1.91 . 1 98 . 23 LYS HG2 H 1.20 . 1 99 . 23 LYS HG3 H 1.20 . 1 100 . 23 LYS HD2 H 1.46 . 2 101 . 23 LYS HD3 H 0.38 . 2 102 . 23 LYS HE2 H 2.65 . 2 103 . 23 LYS HE3 H 2.62 . 2 104 . 23 LYS CB C 32.2 . 1 105 . 23 LYS CD C 27.4 . 1 106 . 23 LYS CE C 42.3 . 1 107 . 24 ALA HB H 1.46 . 1 108 . 24 ALA CB C 19.0 . 1 109 . 25 ALA HB H 1.72 . 1 110 . 25 ALA CB C 17.8 . 1 111 . 26 PHE HB2 H 2.77 . 1 112 . 26 PHE HB3 H 2.77 . 1 113 . 26 PHE HD1 H 6.74 . 1 114 . 26 PHE HD2 H 6.74 . 1 115 . 26 PHE HE1 H 7.12 . 1 116 . 26 PHE HE2 H 7.12 . 1 117 . 26 PHE HZ H 7.29 . 1 118 . 26 PHE CB C 40.1 . 1 119 . 27 ASP HB2 H 2.64 . 2 120 . 27 ASP HB3 H 2.61 . 2 121 . 28 MET HB2 H 2.15 . 2 122 . 28 MET HB3 H 2.09 . 2 123 . 28 MET HG2 H 2.63 . 2 124 . 28 MET HG3 H 2.40 . 2 125 . 28 MET HE H 2.09 . 1 126 . 28 MET CG C 32.4 . 1 127 . 28 MET CE C 16.9 . 1 128 . 29 PHE HB2 H 2.90 . 2 129 . 29 PHE HB3 H 2.70 . 2 130 . 29 PHE HD1 H 7.14 . 1 131 . 29 PHE HD2 H 7.14 . 1 132 . 29 PHE HE1 H 7.28 . 1 133 . 29 PHE HE2 H 7.28 . 1 134 . 29 PHE CB C 40.1 . 1 135 . 30 ASP HB2 H 2.46 . 2 136 . 30 ASP HB3 H 1.46 . 2 137 . 30 ASP CB C 38.9 . 1 138 . 31 ALA HB H 1.54 . 1 139 . 31 ALA CB C 19.9 . 1 140 . 32 ASP HB2 H 3.11 . 2 141 . 32 ASP HB3 H 2.72 . 2 142 . 32 ASP CB C 40.2 . 1 143 . 36 ASP HB2 H 3.04 . 2 144 . 36 ASP HB3 H 2.29 . 2 145 . 36 ASP CB C 41.7 . 1 146 . 37 ILE HB H 1.88 . 1 147 . 37 ILE HG12 H 1.21 . 1 148 . 37 ILE HG13 H 1.21 . 1 149 . 37 ILE HG2 H 1.01 . 1 150 . 37 ILE HD1 H 0.45 . 1 151 . 37 ILE CB C 40.1 . 1 152 . 37 ILE CG1 C 27.4 . 2 153 . 37 ILE CG2 C 18.1 . 2 154 . 37 ILE CD1 C 15.2 . 1 155 . 38 SER HB2 H 4.48 . 2 156 . 38 SER HB3 H 4.03 . 2 157 . 38 SER CB C 66.8 . 1 158 . 39 THR HB H 4.17 . 1 159 . 39 THR HG2 H 1.36 . 1 160 . 39 THR CB C 68.6 . 1 161 . 39 THR CG2 C 23.4 . 1 162 . 40 LYS HB2 H 1.93 . 2 163 . 40 LYS HB3 H 1.78 . 2 164 . 40 LYS HG2 H 1.47 . 2 165 . 40 LYS HG3 H 1.41 . 2 166 . 40 LYS HD2 H 1.70 . 1 167 . 40 LYS HD3 H 1.70 . 1 168 . 40 LYS HE2 H 3.00 . 1 169 . 40 LYS HE3 H 3.00 . 1 170 . 40 LYS CB C 33.0 . 1 171 . 40 LYS CG C 25.2 . 1 172 . 40 LYS CD C 29.5 . 1 173 . 40 LYS CE C 42.3 . 1 174 . 42 LEU HB2 H 1.94 . 2 175 . 42 LEU HB3 H 1.50 . 2 176 . 42 LEU HG H 1.61 . 1 177 . 42 LEU HD1 H 0.85 . 1 178 . 42 LEU HD2 H 0.85 . 1 179 . 42 LEU CB C 42.7 . 1 180 . 42 LEU CG C 27.0 . 1 181 . 42 LEU CD1 C 26.2 . 2 182 . 42 LEU CD2 C 23.1 . 2 183 . 44 THR HB H 4.35 . 1 184 . 44 THR HG2 H 1.27 . 1 185 . 44 THR CB C 69.2 . 1 186 . 44 THR CG2 C 21.6 . 1 187 . 45 VAL HB H 1.95 . 1 188 . 45 VAL HG1 H 0.66 . 2 189 . 45 VAL HG2 H 0.36 . 2 190 . 45 VAL CB C 31.7 . 1 191 . 45 VAL CG1 C 23.0 . 2 192 . 45 VAL CG2 C 20.8 . 2 193 . 46 MET HB2 H 2.07 . 2 194 . 46 MET HB3 H 1.81 . 2 195 . 46 MET HG2 H 2.71 . 2 196 . 46 MET HG3 H 2.49 . 2 197 . 46 MET HE H 1.93 . 1 198 . 46 MET CB C 30.4 . 1 199 . 46 MET CG C 33.5 . 1 200 . 46 MET CE C 17.3 . 1 201 . 47 ARG HB2 H 1.99 . 2 202 . 47 ARG HB3 H 1.94 . 2 203 . 47 ARG HG2 H 1.93 . 2 204 . 47 ARG HG3 H 1.81 . 2 205 . 47 ARG HD2 H 3.23 . 1 206 . 47 ARG HD3 H 3.23 . 1 207 . 47 ARG CB C 30.3 . 1 208 . 47 ARG CG C 28.9 . 1 209 . 47 ARG CD C 43.7 . 1 210 . 48 MET HB2 H 2.38 . 2 211 . 48 MET HB3 H 2.27 . 2 212 . 48 MET HG2 H 2.78 . 2 213 . 48 MET HG3 H 2.66 . 2 214 . 48 MET HE H 2.20 . 1 215 . 48 MET CB C 32.2 . 1 216 . 48 MET CG C 32.2 . 1 217 . 48 MET CE C 17.3 . 1 218 . 49 LEU HB2 H 1.90 . 2 219 . 49 LEU HB3 H 1.78 . 2 220 . 49 LEU HD1 H 0.86 . 1 221 . 49 LEU HD2 H 0.86 . 1 222 . 49 LEU CB C 42.2 . 1 223 . 49 LEU CD1 C 21.7 . 1 224 . 49 LEU CD2 C 21.7 . 1 225 . 51 GLN HB2 H 2.15 . 2 226 . 51 GLN HB3 H 1.66 . 2 227 . 51 GLN HG2 H 2.23 . 1 228 . 51 GLN HG3 H 2.23 . 1 229 . 51 GLN HE21 H 7.18 . 2 230 . 51 GLN HE22 H 6.65 . 2 231 . 51 GLN CB C 30.5 . 1 232 . 51 GLN CG C 33.1 . 1 233 . 51 GLN CD C 182.6 . 1 234 . 51 GLN NE2 N 112.52 . 1 235 . 52 ASN HB2 H 2.82 . 2 236 . 52 ASN HB3 H 2.53 . 2 237 . 52 ASN HD21 H 7.48 . 2 238 . 52 ASN HD22 H 6.69 . 2 239 . 52 ASN CB C 39.6 . 1 240 . 52 ASN CG C 176.7 . 1 241 . 52 ASN ND2 N 113.18 . 1 242 . 53 PRO HB2 H 2.18 . 2 243 . 53 PRO HB3 H 1.96 . 2 244 . 53 PRO HG2 H 2.02 . 1 245 . 53 PRO HG3 H 2.02 . 1 246 . 53 PRO HD2 H 3.67 . 2 247 . 53 PRO HD3 H 3.27 . 2 248 . 53 PRO CB C 32.6 . 1 249 . 53 PRO CD C 50.5 . 1 250 . 54 THR HB H 4.71 . 1 251 . 54 THR HG2 H 1.36 . 1 252 . 54 THR CB C 72.0 . 1 253 . 54 THR CG2 C 22.3 . 1 254 . 55 LYS HB2 H 1.96 . 2 255 . 55 LYS HB3 H 1.80 . 2 256 . 55 LYS HG2 H 1.50 . 1 257 . 55 LYS HG3 H 1.50 . 1 258 . 55 LYS HD2 H 1.72 . 1 259 . 55 LYS HD3 H 1.72 . 1 260 . 55 LYS HE2 H 2.99 . 1 261 . 55 LYS HE3 H 2.99 . 1 262 . 55 LYS CB C 32.6 . 1 263 . 55 LYS CG C 25.2 . 1 264 . 55 LYS CD C 29.5 . 1 265 . 55 LYS CE C 41.8 . 1 266 . 56 GLU HB2 H 2.81 . 2 267 . 56 GLU HB3 H 1.95 . 2 268 . 56 GLU HG2 H 2.50 . 1 269 . 56 GLU HG3 H 2.30 . 2 270 . 56 GLU CG C 37.4 . 1 271 . 58 LEU HB2 H 2.12 . 1 272 . 58 LEU HB3 H 2.12 . 1 273 . 58 LEU HG H 1.80 . 1 274 . 58 LEU HD1 H 0.84 . 2 275 . 58 LEU HD2 H 0.79 . 2 276 . 58 LEU CG C 27.8 . 1 277 . 58 LEU CD1 C 27.0 . 2 278 . 58 LEU CD2 C 22.6 . 2 279 . 59 ASP HB2 H 2.73 . 2 280 . 59 ASP HB3 H 2.62 . 2 281 . 59 ASP CB C 40.5 . 1 282 . 60 ALA HB H 1.53 . 1 283 . 60 ALA CB C 18.3 . 1 284 . 61 ILE HB H 1.96 . 1 285 . 61 ILE HG12 H 1.84 . 2 286 . 61 ILE HG13 H 1.15 . 2 287 . 61 ILE HG2 H 0.82 . 1 288 . 61 ILE HD1 H 0.89 . 1 289 . 61 ILE CB C 38.4 . 1 290 . 61 ILE CG1 C 30.5 . 1 291 . 61 ILE CG2 C 17.3 . 1 292 . 61 ILE CD1 C 13.0 . 1 293 . 62 ILE HB H 2.04 . 1 294 . 62 ILE HG12 H 1.68 . 2 295 . 62 ILE HG13 H 1.17 . 2 296 . 62 ILE HG2 H 0.72 . 1 297 . 62 ILE HD1 H 0.73 . 1 298 . 62 ILE CB C 37.1 . 1 299 . 62 ILE CG1 C 29.5 . 2 300 . 62 ILE CG2 C 17.0 . 2 301 . 62 ILE CD1 C 12.1 . 1 302 . 63 GLU HB2 H 2.16 . 2 303 . 63 GLU HB3 H 2.08 . 2 304 . 63 GLU CB C 29.6 . 1 305 . 64 GLU HB2 H 2.15 . 2 306 . 64 GLU HB3 H 2.09 . 2 307 . 64 GLU HG2 H 2.64 . 1 308 . 64 GLU HG3 H 2.58 . 2 309 . 64 GLU CB C 33.5 . 1 310 . 65 VAL HB H 2.26 . 1 311 . 65 VAL HG1 H 0.92 . 2 312 . 65 VAL HG2 H 0.97 . 2 313 . 65 VAL CB C 33.5 . 1 314 . 65 VAL CG1 C 22.6 . 2 315 . 65 VAL CG2 C 20.4 . 2 316 . 66 ASP HB2 H 2.69 . 1 317 . 66 ASP HB3 H 2.69 . 1 318 . 66 ASP CB C 41.4 . 1 319 . 67 GLU HB2 H 2.24 . 2 320 . 67 GLU HB3 H 2.06 . 2 321 . 67 GLU HG2 H 2.32 . 2 322 . 67 GLU HG3 H 2.24 . 2 323 . 68 ASP HB2 H 3.13 . 2 324 . 68 ASP HB3 H 2.76 . 2 325 . 68 ASP CB C 40.9 . 1 326 . 70 SER HB2 H 4.22 . 2 327 . 70 SER HB3 H 4.03 . 2 328 . 70 SER CB C 65.0 . 1 329 . 72 THR HB H 3.68 . 1 330 . 72 THR HG2 H 1.04 . 1 331 . 72 THR CB C 73.8 . 1 332 . 72 THR CG2 C 22.6 . 1 333 . 73 ILE HB H 2.04 . 1 334 . 73 ILE HG12 H 1.59 . 2 335 . 73 ILE HG13 H 0.90 . 2 336 . 73 ILE HG2 H 1.29 . 1 337 . 73 ILE HD1 H 0.86 . 1 338 . 73 ILE CB C 40.6 . 1 339 . 73 ILE CG1 C 27.1 . 2 340 . 73 ILE CG2 C 18.5 . 2 341 . 73 ILE CD1 C 14.1 . 1 342 . 74 ASP HB2 H 3.38 . 2 343 . 74 ASP HB3 H 2.81 . 2 344 . 74 ASP CB C 41.8 . 1 345 . 75 PHE HB2 H 2.48 . 2 346 . 75 PHE HB3 H 2.08 . 2 347 . 75 PHE HD1 H 6.70 . 1 348 . 75 PHE HD2 H 6.70 . 1 349 . 75 PHE HE1 H 7.11 . 1 350 . 75 PHE HE2 H 7.11 . 1 351 . 75 PHE HZ H 7.39 . 1 352 . 75 PHE CB C 38.8 . 1 353 . 76 GLU HB2 H 1.96 . 2 354 . 76 GLU HB3 H 1.89 . 2 355 . 78 PHE HB2 H 3.44 . 2 356 . 78 PHE HB3 H 3.23 . 2 357 . 78 PHE HD1 H 7.04 . 1 358 . 78 PHE HD2 H 7.04 . 1 359 . 78 PHE HE1 H 7.28 . 1 360 . 78 PHE HE2 H 7.28 . 1 361 . 78 PHE CB C 40.4 . 1 362 . 79 LEU HB2 H 1.64 . 2 363 . 79 LEU HB3 H 1.13 . 2 364 . 79 LEU HG H 1.16 . 1 365 . 79 LEU HD1 H 0.57 . 2 366 . 79 LEU HD2 H 0.67 . 2 367 . 79 LEU CG C 26.4 . 1 368 . 79 LEU CD1 C 25.6 . 2 369 . 79 LEU CD2 C 24.4 . 2 370 . 80 VAL HB H 2.23 . 1 371 . 80 VAL HG1 H 1.05 . 2 372 . 80 VAL HG2 H 0.88 . 2 373 . 80 VAL CB C 31.7 . 1 374 . 80 VAL CG1 C 23.4 . 2 375 . 80 VAL CG2 C 21.6 . 2 376 . 81 MET HB2 H 2.25 . 2 377 . 81 MET HB3 H 2.01 . 2 378 . 82 MET HB2 H 1.51 . 2 379 . 82 MET HB3 H 1.22 . 2 380 . 82 MET CB C 32.1 . 1 381 . 83 VAL HB H 2.08 . 1 382 . 83 VAL HG1 H 1.08 . 2 383 . 83 VAL HG2 H 0.78 . 2 384 . 83 VAL CB C 31.7 . 1 385 . 83 VAL CG1 C 23.9 . 2 386 . 83 VAL CG2 C 21.7 . 2 387 . 84 ARG HB2 H 1.88 . 1 388 . 84 ARG HB3 H 1.88 . 1 389 . 84 ARG HG2 H 1.74 . 2 390 . 84 ARG HG3 H 1.62 . 2 391 . 84 ARG HD2 H 3.18 . 1 392 . 84 ARG HD3 H 3.18 . 1 393 . 84 ARG CB C 30.0 . 1 394 . 84 ARG CG C 28.3 . 1 395 . 84 ARG CD C 43.6 . 1 396 . 85 GLN HB2 H 2.17 . 1 397 . 85 GLN HB3 H 2.17 . 1 398 . 85 GLN HG2 H 2.44 . 2 399 . 85 GLN HG3 H 2.36 . 2 400 . 85 GLN HE21 H 7.24 . 2 401 . 85 GLN HE22 H 6.50 . 2 402 . 85 GLN CB C 28.7 . 1 403 . 85 GLN CG C 34.3 . 1 404 . 85 GLN CD C 182.0 . 1 405 . 85 GLN NE2 N 112.0 . 1 406 . 86 MET HB2 H 2.38 . 2 407 . 86 MET HB3 H 2.27 . 2 408 . 86 MET HG2 H 2.77 . 2 409 . 86 MET HG3 H 2.64 . 2 410 . 86 MET HE H 2.20 . 1 411 . 86 MET CB C 32.2 . 1 412 . 86 MET CG C 32.6 . 1 413 . 86 MET CE C 17.3 . 1 414 . 87 LYS HG2 H 1.27 . 2 415 . 87 LYS HG3 H 1.22 . 2 416 . 87 LYS HD2 H 2.48 . 2 417 . 87 LYS HD3 H 2.17 . 2 418 . 87 LYS CG C 26.1 . 1 419 . 88 GLU HB2 H 2.07 . 2 420 . 88 GLU HB3 H 1.87 . 2 421 . 89 ASP HB2 H 2.76 . 2 422 . 89 ASP HB3 H 2.69 . 2 423 . 89 ASP CB C 41.0 . 1 424 . 90 ALA HB H 1.36 . 1 425 . 91 LYS HB2 H 2.26 . 2 426 . 91 LYS HB3 H 2.15 . 2 427 . 91 LYS HG2 H 2.44 . 2 428 . 91 LYS HG3 H 2.35 . 2 429 . 91 LYS CB C 30.0 . 1 430 . 93 LYS HB2 H 1.90 . 2 431 . 93 LYS HB3 H 1.84 . 2 432 . 93 LYS HG2 H 1.49 . 1 433 . 93 LYS HG3 H 1.49 . 1 434 . 93 LYS HD2 H 1.66 . 2 435 . 93 LYS HD3 H 1.56 . 2 436 . 93 LYS HE2 H 2.97 . 1 437 . 93 LYS HE3 H 2.97 . 1 438 . 93 LYS CB C 33.5 . 1 439 . 93 LYS CD C 28.9 . 1 440 . 94 SER HB2 H 4.16 . 2 441 . 94 SER HB3 H 4.02 . 2 442 . 94 SER CB C 64.3 . 1 443 . 95 GLU HB2 H 2.18 . 1 444 . 95 GLU HB3 H 2.18 . 1 445 . 97 GLU HB2 H 2.26 . 1 446 . 97 GLU HB3 H 2.26 . 1 447 . 98 LEU HB2 H 2.23 . 2 448 . 98 LEU HB3 H 2.06 . 2 449 . 98 LEU HG H 1.83 . 1 450 . 98 LEU HD1 H 0.83 . 1 451 . 98 LEU HD2 H 0.83 . 1 452 . 98 LEU CG C 26.6 . 1 453 . 98 LEU CD1 C 25.6 . 1 454 . 98 LEU CD2 C 25.6 . 1 455 . 99 ALA HB H 1.40 . 1 456 . 99 ALA CB C 18.6 . 1 457 . 100 ASN HB2 H 3.01 . 2 458 . 100 ASN HB3 H 2.86 . 2 459 . 100 ASN HD21 H 7.67 . 2 460 . 100 ASN HD22 H 6.94 . 2 461 . 100 ASN CB C 38.4 . 1 462 . 100 ASN CG C 177.7 . 1 463 . 100 ASN ND2 N 114.3 . 1 464 . 101 CYS HB2 H 3.38 . 2 465 . 101 CYS HB3 H 3.18 . 2 466 . 101 CYS CB C 35.6 . 1 467 . 102 PHE HB2 H 3.14 . 2 468 . 102 PHE HB3 H 2.78 . 2 469 . 102 PHE HD1 H 6.44 . 1 470 . 102 PHE HD2 H 6.44 . 1 471 . 102 PHE HE1 H 6.93 . 1 472 . 102 PHE HE2 H 6.93 . 1 473 . 102 PHE HZ H 7.20 . 1 474 . 102 PHE CB C 40.5 . 1 475 . 103 ARG HB2 H 1.92 . 1 476 . 103 ARG HB3 H 1.92 . 1 477 . 103 ARG HG2 H 1.93 . 2 478 . 103 ARG HG3 H 1.81 . 2 479 . 103 ARG HD2 H 3.23 . 1 480 . 103 ARG HD3 H 3.23 . 1 481 . 103 ARG CB C 30.5 . 1 482 . 103 ARG CG C 28.9 . 1 483 . 103 ARG CD C 43.7 . 1 484 . 104 ILE HB H 1.80 . 1 485 . 104 ILE HG12 H 1.62 . 2 486 . 104 ILE HG13 H 1.10 . 2 487 . 104 ILE HG2 H 0.66 . 1 488 . 104 ILE HD1 H 0.76 . 1 489 . 104 ILE CB C 37.9 . 1 490 . 104 ILE CG1 C 29.1 . 2 491 . 104 ILE CG2 C 17.0 . 2 492 . 104 ILE CD1 C 13.0 . 1 493 . 105 PHE HB2 H 3.02 . 2 494 . 105 PHE HB3 H 2.55 . 2 495 . 105 PHE HD1 H 7.41 . 1 496 . 105 PHE HD2 H 7.41 . 1 497 . 105 PHE HE1 H 7.32 . 1 498 . 105 PHE HE2 H 7.32 . 1 499 . 105 PHE HZ H 7.26 . 1 500 . 105 PHE CB C 38.8 . 1 501 . 106 ASP HB2 H 2.47 . 2 502 . 106 ASP HB3 H 1.47 . 2 503 . 106 ASP CB C 39.1 . 1 504 . 107 LYS HB2 H 1.92 . 1 505 . 107 LYS HB3 H 1.92 . 1 506 . 107 LYS HG2 H 1.66 . 2 507 . 107 LYS HG3 H 1.55 . 2 508 . 107 LYS HD2 H 1.80 . 1 509 . 107 LYS HD3 H 1.80 . 1 510 . 107 LYS HE2 H 3.07 . 1 511 . 107 LYS HE3 H 3.07 . 1 512 . 107 LYS CB C 33.4 . 1 513 . 107 LYS CG C 25.2 . 1 514 . 107 LYS CD C 29.2 . 1 515 . 107 LYS CE C 42.2 . 1 516 . 108 ASN HB2 H 3.30 . 2 517 . 108 ASN HB3 H 2.84 . 2 518 . 108 ASN HD21 H 7.79 . 2 519 . 108 ASN HD22 H 6.72 . 2 520 . 108 ASN CB C 37.1 . 1 521 . 108 ASN CG C 179.0 . 1 522 . 108 ASN ND2 N 113.6 . 1 523 . 109 ALA HB H 1.37 . 1 524 . 109 ALA CB C 17.3 . 1 525 . 110 ASP HB2 H 3.24 . 2 526 . 110 ASP HB3 H 2.47 . 2 527 . 110 ASP CB C 41.4 . 1 528 . 112 PHE HB2 H 2.77 . 2 529 . 112 PHE HB3 H 2.73 . 2 530 . 112 PHE CB C 44.4 . 1 531 . 112 PHE HD1 H 6.93 . 1 532 . 112 PHE HD2 H 6.93 . 1 533 . 112 PHE HE1 H 7.40 . 1 534 . 112 PHE HE2 H 7.40 . 1 535 . 112 PHE HZ H 7.34 . 1 536 . 113 ILE HB H 1.92 . 1 537 . 113 ILE HG12 H 1.05 . 2 538 . 113 ILE HG13 H 0.51 . 2 539 . 113 ILE HG2 H 0.92 . 1 540 . 113 ILE HD1 H 0.35 . 1 541 . 113 ILE CB C 39.2 . 1 542 . 113 ILE CG1 C 27.4 . 2 543 . 113 ILE CG2 C 18.2 . 2 544 . 113 ILE CD1 C 14.2 . 1 545 . 114 ASP HB2 H 3.38 . 2 546 . 114 ASP HB3 H 2.58 . 2 547 . 114 ASP CB C 42.3 . 1 548 . 115 ILE HB H 1.92 . 1 549 . 115 ILE HG12 H 1.49 . 2 550 . 115 ILE HG13 H 1.40 . 2 551 . 115 ILE HG2 H 1.00 . 1 552 . 115 ILE HD1 H 0.92 . 1 553 . 115 ILE CB C 38.8 . 1 554 . 115 ILE CG1 C 30.1 . 2 555 . 115 ILE CG2 C 17.7 . 2 556 . 115 ILE CD1 C 14.7 . 1 557 . 116 GLU HB2 H 2.17 . 2 558 . 116 GLU HB3 H 1.93 . 2 559 . 116 GLU HG2 H 2.32 . 1 560 . 116 GLU HG3 H 2.07 . 2 561 . 116 GLU CB C 30.5 . 1 562 . 117 GLU HB2 H 2.48 . 1 563 . 117 GLU HB3 H 2.48 . 1 564 . 117 GLU HG2 H 2.85 . 1 565 . 117 GLU HG3 H 2.85 . 1 566 . 117 GLU CB C 30.1 . 1 567 . 118 LEU HB2 H 1.81 . 2 568 . 118 LEU HB3 H 1.43 . 2 569 . 118 LEU HG H 1.80 . 1 570 . 118 LEU HD1 H 0.86 . 2 571 . 118 LEU HD2 H 0.82 . 2 572 . 118 LEU CB C 41.8 . 1 573 . 118 LEU CG C 27.0 . 1 574 . 118 LEU CD1 C 26.0 . 2 575 . 118 LEU CD2 C 23.0 . 2 576 . 120 GLU HB2 H 2.25 . 2 577 . 120 GLU HB3 H 2.10 . 2 578 . 120 GLU HG2 H 2.41 . 1 579 . 120 GLU HG3 H 2.41 . 1 580 . 120 GLU CB C 29.9 . 1 581 . 121 ILE HB H 1.88 . 1 582 . 121 ILE HG12 H 1.31 . 2 583 . 121 ILE HG13 H 0.42 . 2 584 . 121 ILE HG2 H 0.46 . 1 585 . 121 ILE HD1 H 0.50 . 1 586 . 121 ILE CB C 37.5 . 1 587 . 121 ILE CG1 C 27.8 . 2 588 . 121 ILE CG2 C 16.8 . 2 589 . 121 ILE CD1 C 13.2 . 1 590 . 122 LEU HB2 H 1.81 . 2 591 . 122 LEU HB3 H 1.47 . 2 592 . 122 LEU HG H 1.82 . 1 593 . 122 LEU HD1 H 0.83 . 1 594 . 122 LEU HD2 H 0.83 . 1 595 . 122 LEU CB C 44.4 . 1 596 . 122 LEU CG C 27.8 . 1 597 . 122 LEU CD1 C 25.7 . 2 598 . 122 LEU CD2 C 23.9 . 2 599 . 123 ARG HB2 H 1.91 . 1 600 . 123 ARG HB3 H 1.91 . 1 601 . 123 ARG HG2 H 1.84 . 2 602 . 123 ARG HG3 H 1.60 . 2 603 . 123 ARG HD2 H 3.24 . 2 604 . 123 ARG HD3 H 3.18 . 2 605 . 123 ARG CB C 30.6 . 1 606 . 123 ARG CG C 29.2 . 1 607 . 124 ALA HB H 1.62 . 1 608 . 124 ALA CB C 18.7 . 1 609 . 125 THR HB H 4.40 . 1 610 . 125 THR HG2 H 1.36 . 1 611 . 125 THR CB C 70.7 . 1 612 . 125 THR CG2 C 21.3 . 1 613 . 127 GLU HB2 H 1.96 . 2 614 . 127 GLU HB3 H 1.75 . 2 615 . 127 GLU HG2 H 2.22 . 1 616 . 127 GLU HG3 H 2.16 . 2 617 . 127 GLU CB C 30.9 . 1 618 . 127 GLU CG C 36.1 . 1 619 . 128 HIS HB2 H 3.15 . 2 620 . 128 HIS HB3 H 3.07 . 2 621 . 128 HIS CB C 30.0 . 1 622 . 129 VAL HB H 1.96 . 1 623 . 129 VAL HG1 H 0.86 . 2 624 . 129 VAL HG2 H 0.80 . 2 625 . 129 VAL CB C 34.0 . 1 626 . 129 VAL CG1 C 22.1 . 2 627 . 129 VAL CG2 C 20.8 . 2 628 . 130 ILE HB H 2.13 . 1 629 . 130 ILE HG12 H 1.33 . 1 630 . 130 ILE HG13 H 1.33 . 1 631 . 130 ILE HG2 H 0.97 . 1 632 . 130 ILE HD1 H 0.93 . 1 633 . 130 ILE CB C 40.1 . 1 634 . 130 ILE CG1 C 27.3 . 1 635 . 130 ILE CG2 C 18.2 . 1 636 . 130 ILE CD1 C 13.8 . 1 637 . 131 GLU HB2 H 2.06 . 2 638 . 131 GLU HB3 H 2.04 . 2 639 . 131 GLU HG2 H 2.36 . 1 640 . 131 GLU HG3 H 2.35 . 2 641 . 131 GLU CB C 29.7 . 1 642 . 132 GLU HB2 H 1.99 . 1 643 . 132 GLU HB3 H 1.99 . 1 644 . 132 GLU HG2 H 2.39 . 2 645 . 132 GLU HG3 H 2.30 . 2 646 . 132 GLU CB C 29.7 . 1 647 . 132 GLU CG C 37.3 . 1 648 . 133 ASP HB2 H 2.94 . 2 649 . 133 ASP HB3 H 2.67 . 2 650 . 133 ASP CB C 41.0 . 1 651 . 134 ILE HB H 2.03 . 1 652 . 134 ILE HG12 H 1.65 . 1 653 . 134 ILE HG13 H 1.65 . 1 654 . 134 ILE HG2 H 0.92 . 1 655 . 134 ILE HD1 H 0.86 . 1 656 . 134 ILE CB C 37.9 . 1 657 . 134 ILE CG1 C 29.1 . 2 658 . 134 ILE CG2 C 18.2 . 2 659 . 134 ILE CD1 C 13.8 . 1 660 . 135 GLU HB2 H 2.09 . 2 661 . 135 GLU HB3 H 2.05 . 2 662 . 135 GLU HG2 H 2.33 . 1 663 . 135 GLU HG3 H 2.23 . 2 664 . 135 GLU CB C 29.6 . 1 665 . 136 ASP HB2 H 2.83 . 2 666 . 136 ASP HB3 H 2.68 . 2 667 . 136 ASP CB C 41.0 . 1 668 . 137 LEU HB2 H 1.86 . 2 669 . 137 LEU HB3 H 1.67 . 2 670 . 137 LEU HG H 1.57 . 1 671 . 137 LEU HD1 H 0.89 . 2 672 . 137 LEU HD2 H 0.91 . 2 673 . 137 LEU CB C 41.9 . 1 674 . 137 LEU CG C 27.4 . 1 675 . 137 LEU CD1 C 26.4 . 2 676 . 137 LEU CD2 C 23.6 . 2 677 . 138 MET HB2 H 2.21 . 2 678 . 138 MET HB3 H 2.18 . 2 679 . 138 MET HG2 H 2.63 . 2 680 . 138 MET HG3 H 2.50 . 2 681 . 138 MET HE H 2.07 . 1 682 . 138 MET CB C 33.8 . 1 683 . 138 MET CG C 31.8 . 1 684 . 138 MET CE C 17.4 . 1 685 . 139 LYS HB2 H 1.96 . 1 686 . 139 LYS HB3 H 1.96 . 1 687 . 139 LYS HG2 H 1.66 . 2 688 . 139 LYS HG3 H 1.52 . 2 689 . 139 LYS HD2 H 1.66 . 1 690 . 139 LYS HD3 H 1.66 . 1 691 . 139 LYS HE2 H 3.03 . 1 692 . 139 LYS HE3 H 3.03 . 1 693 . 139 LYS CB C 32.6 . 1 694 . 139 LYS CG C 25.3 . 1 695 . 139 LYS CD C 29.1 . 1 696 . 139 LYS CE C 43.1 . 1 697 . 140 ASP HB2 H 2.97 . 2 698 . 140 ASP HB3 H 2.82 . 2 699 . 140 ASP CB C 38.3 . 1 700 . 141 SER HB2 H 3.93 . 2 701 . 141 SER HB3 H 3.84 . 2 702 . 141 SER CB C 65.0 . 1 703 . 142 ASP HB2 H 2.99 . 2 704 . 142 ASP HB3 H 2.53 . 2 705 . 142 ASP CB C 40.1 . 1 706 . 143 LYS HG2 H 1.53 . 2 707 . 143 LYS HG3 H 1.67 . 2 708 . 143 LYS HD2 H 1.98 . 2 709 . 143 LYS HD3 H 1.74 . 2 710 . 143 LYS CG C 25.6 . 1 711 . 144 ASN HB2 H 3.31 . 2 712 . 144 ASN HB3 H 2.81 . 2 713 . 144 ASN HD21 H 7.85 . 2 714 . 144 ASN HD22 H 6.68 . 2 715 . 144 ASN CB C 37.5 . 1 716 . 144 ASN CG C 178.7 . 1 717 . 144 ASN ND2 N 113.8 . 1 718 . 145 ASN HB2 H 3.07 . 2 719 . 145 ASN HB3 H 2.69 . 2 720 . 145 ASN HD21 H 7.37 . 2 721 . 145 ASN HD22 H 6.67 . 2 722 . 145 ASN CB C 37.9 . 1 723 . 145 ASN CG C 178.2 . 1 724 . 145 ASN ND2 N 112.9 . 1 725 . 146 ASP HB2 H 2.97 . 2 726 . 146 ASP HB3 H 2.40 . 2 727 . 146 ASP CB C 41.3 . 1 728 . 148 ARG HB2 H 1.63 . 2 729 . 148 ARG HB3 H 1.50 . 2 730 . 148 ARG HG2 H 1.27 . 2 731 . 148 ARG HG3 H 1.22 . 2 732 . 148 ARG HD2 H 2.47 . 2 733 . 148 ARG HD3 H 2.16 . 2 734 . 148 ARG CB C 34.5 . 1 735 . 148 ARG CG C 26.0 . 1 736 . 148 ARG CD C 43.2 . 1 737 . 149 ILE HB H 2.24 . 1 738 . 149 ILE HG12 H 1.04 . 1 739 . 149 ILE HG13 H 1.04 . 1 740 . 149 ILE HG2 H 1.30 . 1 741 . 149 ILE HD1 H 0.92 . 1 742 . 149 ILE CB C 40.0 . 1 743 . 149 ILE CG1 C 28.3 . 2 744 . 149 ILE CG2 C 18.5 . 2 745 . 149 ILE CD1 C 14.2 . 2 746 . 150 ASP HB2 H 3.32 . 2 747 . 150 ASP HB3 H 2.93 . 2 748 . 150 ASP CB C 42.7 . 1 749 . 151 PHE HB2 H 2.56 . 2 750 . 151 PHE HB3 H 2.27 . 2 751 . 151 PHE HD1 H 6.61 . 1 752 . 151 PHE HD2 H 6.61 . 1 753 . 151 PHE HE1 H 7.17 . 1 754 . 151 PHE HE2 H 7.17 . 1 755 . 151 PHE HZ H 7.28 . 1 756 . 151 PHE CB C 39.1 . 1 757 . 152 ASP HB2 H 2.75 . 2 758 . 152 ASP HB3 H 2.63 . 2 759 . 152 ASP CB C 41.4 . 1 760 . 154 PHE HB2 H 3.43 . 2 761 . 154 PHE HB3 H 3.28 . 2 762 . 154 PHE HD1 H 7.11 . 1 763 . 154 PHE HD2 H 7.11 . 1 764 . 154 PHE HE1 H 7.38 . 1 765 . 154 PHE HE2 H 7.38 . 1 766 . 154 PHE HZ H 7.42 . 1 767 . 154 PHE CB C 40.2 . 1 768 . 155 LEU HB2 H 1.72 . 2 769 . 155 LEU HB3 H 1.28 . 2 770 . 155 LEU HG H 1.20 . 1 771 . 155 LEU HD1 H 0.64 . 2 772 . 155 LEU HD2 H 0.68 . 2 773 . 155 LEU CB C 41.8 . 1 774 . 155 LEU CG C 26.5 . 1 775 . 155 LEU CD1 C 26.1 . 2 776 . 155 LEU CD2 C 24.4 . 2 777 . 156 LYS HB2 H 1.88 . 1 778 . 156 LYS HB3 H 1.88 . 1 779 . 156 LYS HG2 H 1.58 . 2 780 . 156 LYS HG3 H 1.56 . 2 781 . 156 LYS HD2 H 1.84 . 2 782 . 156 LYS HD3 H 1.55 . 2 783 . 156 LYS HE2 H 3.10 . 2 784 . 156 LYS HE3 H 3.03 . 2 785 . 156 LYS CB C 30.5 . 1 786 . 156 LYS CD C 28.2 . 1 787 . 156 LYS CE C 44.0 . 1 788 . 157 MET HB2 H 2.16 . 1 789 . 157 MET HB3 H 2.16 . 1 790 . 157 MET HG2 H 2.59 . 2 791 . 157 MET HG3 H 2.40 . 2 792 . 157 MET HE H 1.98 . 1 793 . 157 MET CB C 32.4 . 1 794 . 157 MET CG C 32.4 . 1 795 . 157 MET CE C 17.7 . 1 796 . 158 MET HB2 H 1.85 . 2 797 . 158 MET HB3 H 1.74 . 2 798 . 158 MET HE H 2.05 . 1 799 . 158 MET CB C 32.3 . 1 800 . 158 MET CE C 17.2 . 1 801 . 159 GLU HB2 H 2.05 . 1 802 . 159 GLU HB3 H 2.05 . 1 803 . 159 GLU HG2 H 2.42 . 1 804 . 159 GLU HG3 H 2.24 . 2 805 . 159 GLU CB C 31.4 . 1 806 . 161 VAL HB H 2.16 . 1 807 . 161 VAL HG1 H 0.93 . 2 808 . 161 VAL HG2 H 0.95 . 2 809 . 161 VAL CB C 32.8 . 1 810 . 161 VAL CG1 C 21.7 . 2 811 . 161 VAL CG2 C 21.2 . 2 812 . 162 GLN HB2 H 2.11 . 2 813 . 162 GLN HB3 H 1.93 . 2 814 . 162 GLN HG2 H 2.31 . 1 815 . 162 GLN HG3 H 2.31 . 1 816 . 162 GLN HE21 H 7.52 . 2 817 . 162 GLN HE22 H 6.88 . 2 818 . 162 GLN CB C 30.9 . 1 819 . 162 GLN CG C 34.7 . 1 820 . 162 GLN CD C 181.6 . 1 821 . 162 GLN NE2 N 112.5 . 1 stop_ save_