data_5794 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N Chemical Shift Assignments for the SH3-SH2 domain pair of the tyrosin kinase Lck ; _BMRB_accession_number 5794 _BMRB_flat_file_name bmr5794.str _Entry_type original _Submission_date 2003-05-10 _Accession_date 2003-05-12 _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 Schweimer Kristian . . 2 Kiessling Anke . . 3 Bauer Finn . . 4 Hor Simon . . 5 Hoffmann Silke . . 6 Roesch Paul . . 7 Sticht Heinrich . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 827 "13C chemical shifts" 618 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-10-16 original author . stop_ _Original_release_date 2003-10-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair of the human tyrosine kinase Lck ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22874493 _PubMed_ID 14512743 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schweimer Kristian . . 2 Kiessling Anke . . 3 Bauer Finn . . 4 Hor Simon . . 5 Hoffmann Silke . . 6 Roesch Paul . . 7 Sticht Heinrich . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 405 _Page_last 406 _Year 2003 _Details . loop_ _Keyword kinase Lck Src-kinases stop_ save_ ################################## # Molecular system description # ################################## save_system_LckSH32 _Saveframe_category molecular_system _Mol_system_name 'Lck SH3-SH2 domain pair' _Abbreviation_common LckSH32 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LckSH32 $LckSH32 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LckSH32 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Tyrosine kinase' _Abbreviation_common Lck _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 169 _Mol_residue_sequence ; ASPLQDNLVIALHSYEPSHD GDLGFEKGEQLRILEQSGEW WKAQSLTTGQEGFIPFNFVA KANSLEPEPWFFKNLSRKDA ERQLLAPGNTHGSFLIRESE STAGSFSLSVRDFDQNQGEV VKHYKIRNLDNGGFYISPRI TFPGLHELVRHYTNASDGLC TRLSRPCQT ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 PRO 4 LEU 5 GLN 6 ASP 7 ASN 8 LEU 9 VAL 10 ILE 11 ALA 12 LEU 13 HIS 14 SER 15 TYR 16 GLU 17 PRO 18 SER 19 HIS 20 ASP 21 GLY 22 ASP 23 LEU 24 GLY 25 PHE 26 GLU 27 LYS 28 GLY 29 GLU 30 GLN 31 LEU 32 ARG 33 ILE 34 LEU 35 GLU 36 GLN 37 SER 38 GLY 39 GLU 40 TRP 41 TRP 42 LYS 43 ALA 44 GLN 45 SER 46 LEU 47 THR 48 THR 49 GLY 50 GLN 51 GLU 52 GLY 53 PHE 54 ILE 55 PRO 56 PHE 57 ASN 58 PHE 59 VAL 60 ALA 61 LYS 62 ALA 63 ASN 64 SER 65 LEU 66 GLU 67 PRO 68 GLU 69 PRO 70 TRP 71 PHE 72 PHE 73 LYS 74 ASN 75 LEU 76 SER 77 ARG 78 LYS 79 ASP 80 ALA 81 GLU 82 ARG 83 GLN 84 LEU 85 LEU 86 ALA 87 PRO 88 GLY 89 ASN 90 THR 91 HIS 92 GLY 93 SER 94 PHE 95 LEU 96 ILE 97 ARG 98 GLU 99 SER 100 GLU 101 SER 102 THR 103 ALA 104 GLY 105 SER 106 PHE 107 SER 108 LEU 109 SER 110 VAL 111 ARG 112 ASP 113 PHE 114 ASP 115 GLN 116 ASN 117 GLN 118 GLY 119 GLU 120 VAL 121 VAL 122 LYS 123 HIS 124 TYR 125 LYS 126 ILE 127 ARG 128 ASN 129 LEU 130 ASP 131 ASN 132 GLY 133 GLY 134 PHE 135 TYR 136 ILE 137 SER 138 PRO 139 ARG 140 ILE 141 THR 142 PHE 143 PRO 144 GLY 145 LEU 146 HIS 147 GLU 148 LEU 149 VAL 150 ARG 151 HIS 152 TYR 153 THR 154 ASN 155 ALA 156 SER 157 ASP 158 GLY 159 LEU 160 CYS 161 THR 162 ARG 163 LEU 164 SER 165 ARG 166 PRO 167 CYS 168 GLN 169 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1BHF "P56lck Sh2 Domain Inhibitor Complex" 63.91 108 100.00 100.00 5.60e-73 PDB 1BHH "Free P56lck Sh2 Domain" 63.91 108 100.00 100.00 5.60e-73 PDB 1CWD "Human P56lck Tyrosine Kinase Complexed With Phosphopeptide" 56.80 98 100.00 100.00 6.45e-63 PDB 1CWE "Human P56lck Tyrosine Kinase Complexed With Phosphopeptide" 56.80 98 100.00 100.00 6.45e-63 PDB 1FBZ "Structure-Based Design Of A Novel, Osteoclast-Selective, Nonpeptide Src Sh2 Inhibitor With In Vivo Anti-Resorptive Activity" 61.54 104 99.04 99.04 2.10e-69 PDB 1IJR "Crystal Structure Of Lck Sh2 Complexed With Nonpeptide Phosphotyrosine Mimetic" 60.95 104 99.03 99.03 8.38e-69 PDB 1LCJ "Sh2 (Src Homology-2) Domain Of Human P56-Lck Tyrosine Kinase Complexed With The 11 Residue Phosphotyrosyl Peptide Epqpyeeipiyl" 63.91 109 100.00 100.00 4.30e-73 PDB 1LCK "Sh3-Sh2 Domain Fragment Of Human P56-Lck Tyrosine Kinase Complexed With The 10 Residue Synthetic Phosphotyrosyl Peptide Tegqpyq" 100.00 175 100.00 100.00 5.54e-121 PDB 1LKK "Human P56-Lck Tyrosine Kinase Sh2 Domain In Complex With The Phosphotyrosyl Peptide Ac-Ptyr-Glu-Glu-Ile (Pyeei Peptide)" 62.13 105 100.00 100.00 7.74e-71 PDB 1LKL "Human P56-Lck Tyrosine Kinase Sh2 Domain In Complex With The Phosphotyrosyl Peptide Ac-Ptyr-Glu-Glu-Gly (Pyeeg Peptide)" 61.54 104 100.00 100.00 3.88e-70 PDB 1X27 "Crystal Structure Of Lck Sh2-Sh3 With Sh2 Binding Site Of P130cas" 96.45 167 100.00 100.00 1.17e-116 PDB 4D8K "Crystal Structure Of A Sh3-Sh2 Domains Of A Lymphocyte-Specific Protein Tyrosine Kinase (Lck) From Homo Sapiens At 2.36 A Resol" 100.00 175 100.00 100.00 8.21e-121 DBJ BAC40086 "unnamed protein product [Mus musculus]" 100.00 509 98.82 100.00 6.64e-116 DBJ BAG64189 "unnamed protein product [Homo sapiens]" 100.00 536 99.41 99.41 6.14e-115 DBJ BAI45973 "lymphocyte-specific protein tyrosine kinase [synthetic construct]" 100.00 509 100.00 100.00 6.69e-117 EMBL CAA27234 "unnamed protein product [Mus musculus]" 100.00 509 98.82 100.00 6.64e-116 EMBL CAA31884 "unnamed protein product [Homo sapiens]" 100.00 509 99.41 99.41 9.19e-116 EMBL CAA32211 "unnamed protein product [Homo sapiens]" 100.00 509 100.00 100.00 6.69e-117 EMBL CAC38871 "Lck tyrosine kinase [Saimiri sciureus]" 100.00 509 97.63 98.82 3.65e-114 EMBL CAC44027 "lck protein [Hylobates sp.]" 100.00 509 100.00 100.00 5.94e-117 GB AAA18225 "lymphocyte-specific protein tyrosine kinase [Homo sapiens]" 100.00 512 100.00 100.00 7.15e-117 GB AAA59502 "lymphocyte-specific protein tyrosine kinase [Homo sapiens]" 100.00 509 99.41 99.41 6.23e-116 GB AAB59674 "lymphocyte-specific protein tyrosine kinase [Mus musculus]" 100.00 509 98.82 100.00 6.64e-116 GB AAC50287 "p56lck [Homo sapiens]" 100.00 363 100.00 100.00 1.14e-118 GB AAF34794 "tyrosine kinase LCK, partial [Homo sapiens]" 100.00 496 100.00 100.00 2.30e-117 PRF 1203381A "kinase p56tck,protein Tyr" 100.00 509 98.82 100.00 6.64e-116 PRF 2201317A "protein Tyr kinase p56lck" 100.00 363 100.00 100.00 1.14e-118 REF NP_001036236 "tyrosine-protein kinase Lck [Homo sapiens]" 100.00 509 100.00 100.00 6.69e-117 REF NP_001094179 "proto-oncogene tyrosine-protein kinase LCK [Rattus norvegicus]" 100.00 509 98.82 100.00 5.53e-116 REF NP_001155904 "proto-oncogene tyrosine-protein kinase LCK isoform a [Mus musculus]" 100.00 520 98.82 100.00 5.39e-116 REF NP_001155905 "proto-oncogene tyrosine-protein kinase LCK isoform b [Mus musculus]" 100.00 509 98.82 100.00 6.64e-116 REF NP_005347 "tyrosine-protein kinase Lck [Homo sapiens]" 100.00 509 100.00 100.00 6.69e-117 SP P06239 "RecName: Full=Tyrosine-protein kinase Lck; AltName: Full=Leukocyte C-terminal Src kinase; Short=LSK; AltName: Full=Lymphocyte c" 100.00 509 100.00 100.00 6.69e-117 SP P06240 "RecName: Full=Proto-oncogene tyrosine-protein kinase LCK; AltName: Full=Leukocyte C-terminal Src kinase; Short=LSK; AltName: Fu" 100.00 509 98.82 100.00 6.64e-116 SP Q01621 "RecName: Full=Proto-oncogene tyrosine-protein kinase LCK; AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase; AltNa" 100.00 509 98.82 100.00 5.53e-116 SP Q5PXS1 "RecName: Full=Tyrosine-protein kinase Lck; AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase; AltName: Full=Proto-" 100.00 509 98.82 100.00 1.07e-115 SP Q95KR7 "RecName: Full=Proto-oncogene tyrosine-protein kinase LCK; AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase; AltNa" 100.00 509 97.63 98.82 3.65e-114 TPE CAD55807 "TPA: protein tyrosine kinase [Homo sapiens]" 100.00 509 100.00 100.00 6.69e-117 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LckSH32 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_name $LckSH32 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $LckSH32 . mM 0.5 0.7 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'visual analysis of the NMR spectra' stop_ _Details . save_ save_home_written_software _Saveframe_category software _Name 'home written software' _Version . loop_ _Task 'processing of the NMR raw data' 'automatic assignment of the backbone resonances' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_constant_time_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C constant time HSQC' _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CCCONH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name CCCONH-TOCSY _Sample_label . save_ save_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HCCH-COSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C constant time HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CCCONH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.2 n/a temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name LckSH32 _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 HA H 4.110 0.03 1 2 . 1 ALA HB H 1.510 0.03 1 3 . 1 ALA CA C 51.800 0.25 1 4 . 1 ALA CB C 19.500 0.25 1 5 . 2 SER HA H 4.810 0.03 1 6 . 2 SER HB2 H 3.870 0.03 1 7 . 2 SER HB3 H 3.870 0.03 1 8 . 2 SER CA C 56.500 0.25 1 9 . 2 SER CB C 63.300 0.25 1 10 . 3 PRO HA H 4.440 0.03 1 11 . 3 PRO HB2 H 2.310 0.03 2 12 . 3 PRO HB3 H 1.910 0.03 2 13 . 3 PRO HG2 H 2.010 0.03 1 14 . 3 PRO HG3 H 2.010 0.03 1 15 . 3 PRO HD2 H 3.740 0.03 2 16 . 3 PRO HD3 H 3.820 0.03 2 17 . 3 PRO CA C 63.500 0.25 1 18 . 3 PRO CB C 32.100 0.25 1 19 . 3 PRO CG C 27.400 0.25 1 20 . 3 PRO CD C 50.800 0.25 1 21 . 4 LEU HA H 4.280 0.03 1 22 . 4 LEU HD1 H 0.910 0.03 2 23 . 4 LEU HD2 H 0.870 0.03 2 24 . 4 LEU CA C 55.500 0.25 1 25 . 6 ASP HA H 4.608 0.03 1 26 . 6 ASP HB2 H 2.629 0.03 1 27 . 6 ASP HB3 H 2.629 0.03 1 28 . 6 ASP C C 175.645 0.25 1 29 . 6 ASP CA C 54.450 0.25 1 30 . 6 ASP CB C 41.350 0.25 1 31 . 7 ASN H H 8.479 0.03 1 32 . 7 ASN HA H 4.716 0.03 1 33 . 7 ASN HB2 H 2.979 0.03 1 34 . 7 ASN HB3 H 2.979 0.03 1 35 . 7 ASN C C 175.118 0.25 1 36 . 7 ASN CA C 52.580 0.25 1 37 . 7 ASN CB C 38.095 0.25 1 38 . 7 ASN N N 119.307 0.20 1 39 . 8 LEU H H 7.878 0.03 1 40 . 8 LEU HA H 5.234 0.03 1 41 . 8 LEU HB2 H 1.487 0.03 2 42 . 8 LEU HB3 H 1.704 0.03 2 43 . 8 LEU HD1 H 0.800 0.03 2 44 . 8 LEU HD2 H 0.890 0.03 2 45 . 8 LEU C C 177.706 0.25 1 46 . 8 LEU CA C 54.315 0.25 1 47 . 8 LEU CB C 43.715 0.25 1 48 . 8 LEU CD1 C 24.000 0.25 2 49 . 8 LEU CD2 C 25.000 0.25 2 50 . 8 LEU N N 121.379 0.20 1 51 . 9 VAL H H 9.087 0.03 1 52 . 9 VAL HA H 4.972 0.03 1 53 . 9 VAL HB H 2.050 0.03 1 54 . 9 VAL HG1 H 0.647 0.03 2 55 . 9 VAL HG2 H 0.836 0.03 2 56 . 9 VAL C C 173.528 0.25 1 57 . 9 VAL CA C 58.800 0.25 1 58 . 9 VAL CB C 36.395 0.25 1 59 . 9 VAL CG1 C 19.329 0.25 2 60 . 9 VAL CG2 C 21.848 0.25 2 61 . 9 VAL N N 116.348 0.20 1 62 . 10 ILE H H 8.965 0.03 1 63 . 10 ILE HA H 4.932 0.03 1 64 . 10 ILE HB H 1.605 0.03 1 65 . 10 ILE HG12 H 1.097 0.03 2 66 . 10 ILE HG13 H 1.392 0.03 2 67 . 10 ILE HG2 H 0.818 0.03 1 68 . 10 ILE HD1 H 0.842 0.03 1 69 . 10 ILE C C 175.670 0.25 1 70 . 10 ILE CA C 58.455 0.25 1 71 . 10 ILE CB C 41.330 0.25 1 72 . 10 ILE CG1 C 28.142 0.25 1 73 . 10 ILE CG2 C 17.208 0.25 1 74 . 10 ILE CD1 C 13.137 0.25 1 75 . 10 ILE N N 118.542 0.20 1 76 . 11 ALA H H 8.571 0.03 1 77 . 11 ALA HA H 4.555 0.03 1 78 . 11 ALA HB H 1.699 0.03 1 79 . 11 ALA C C 179.274 0.25 1 80 . 11 ALA CA C 52.540 0.25 1 81 . 11 ALA CB C 21.080 0.25 1 82 . 11 ALA N N 126.369 0.20 1 83 . 12 LEU H H 9.456 0.03 1 84 . 12 LEU HA H 4.056 0.03 1 85 . 12 LEU HB2 H 1.080 0.03 2 86 . 12 LEU HB3 H 1.242 0.03 2 87 . 12 LEU HD1 H 0.680 0.03 2 88 . 12 LEU HD2 H 0.690 0.03 2 89 . 12 LEU C C 175.620 0.25 1 90 . 12 LEU CA C 55.540 0.25 1 91 . 12 LEU CB C 43.275 0.25 1 92 . 12 LEU CD1 C 25.300 0.25 2 93 . 12 LEU CD2 C 22.200 0.25 2 94 . 12 LEU N N 126.543 0.20 1 95 . 13 HIS H H 7.539 0.03 1 96 . 13 HIS HA H 4.691 0.03 1 97 . 13 HIS HB2 H 2.451 0.03 2 98 . 13 HIS HB3 H 3.034 0.03 2 99 . 13 HIS C C 175.620 0.25 1 100 . 13 HIS CA C 53.140 0.25 1 101 . 13 HIS CB C 33.585 0.25 1 102 . 13 HIS N N 112.474 0.20 1 103 . 14 SER H H 8.822 0.03 1 104 . 14 SER HA H 4.662 0.03 1 105 . 14 SER HB2 H 3.962 0.03 2 106 . 14 SER HB3 H 4.137 0.03 2 107 . 14 SER C C 173.100 0.25 1 108 . 14 SER CA C 58.635 0.25 1 109 . 14 SER CB C 64.050 0.25 1 110 . 14 SER N N 116.285 0.20 1 111 . 15 TYR H H 8.511 0.03 1 112 . 15 TYR HA H 4.676 0.03 1 113 . 15 TYR HB2 H 1.120 0.03 2 114 . 15 TYR HB3 H 2.305 0.03 2 115 . 15 TYR C C 173.579 0.25 1 116 . 15 TYR CA C 57.470 0.25 1 117 . 15 TYR CB C 42.330 0.25 1 118 . 15 TYR N N 123.076 0.20 1 119 . 16 GLU H H 7.634 0.03 1 120 . 16 GLU HA H 4.550 0.03 1 121 . 16 GLU HB2 H 1.680 0.03 2 122 . 16 GLU HB3 H 1.750 0.03 2 123 . 16 GLU HG2 H 2.080 0.03 1 124 . 16 GLU HG3 H 2.080 0.03 1 125 . 16 GLU CA C 51.870 0.25 1 126 . 16 GLU CB C 30.100 0.25 1 127 . 16 GLU CG C 36.200 0.25 1 128 . 16 GLU N N 129.229 0.20 1 129 . 17 PRO HA H 4.039 0.03 1 130 . 17 PRO HB2 H 2.030 0.03 1 131 . 17 PRO HB3 H 2.030 0.03 1 132 . 17 PRO C C 176.843 0.25 1 133 . 17 PRO CA C 63.370 0.25 1 134 . 17 PRO CB C 33.020 0.25 1 135 . 17 PRO CG C 27.677 0.25 1 136 . 17 PRO CD C 50.475 0.25 1 137 . 18 SER H H 8.646 0.03 1 138 . 18 SER HA H 4.460 0.03 1 139 . 18 SER HB2 H 3.640 0.03 2 140 . 18 SER HB3 H 3.720 0.03 2 141 . 18 SER C C 173.276 0.25 1 142 . 18 SER CA C 58.625 0.25 1 143 . 18 SER CB C 64.645 0.25 1 144 . 18 SER N N 116.533 0.20 1 145 . 19 HIS H H 7.816 0.03 1 146 . 19 HIS HA H 4.770 0.03 1 147 . 19 HIS HB2 H 2.925 0.03 2 148 . 19 HIS HB3 H 3.167 0.03 2 149 . 19 HIS C C 174.562 0.25 1 150 . 19 HIS CA C 53.735 0.25 1 151 . 19 HIS CB C 30.410 0.25 1 152 . 19 HIS N N 118.557 0.20 1 153 . 20 ASP H H 8.790 0.03 1 154 . 20 ASP HA H 4.458 0.03 1 155 . 20 ASP HB2 H 2.640 0.03 1 156 . 20 ASP HB3 H 2.640 0.03 1 157 . 20 ASP C C 177.132 0.25 1 158 . 20 ASP CA C 56.415 0.25 1 159 . 20 ASP CB C 40.415 0.25 1 160 . 20 ASP N N 123.876 0.20 1 161 . 21 GLY H H 8.911 0.03 1 162 . 21 GLY HA2 H 3.975 0.03 2 163 . 21 GLY HA3 H 4.406 0.03 2 164 . 21 GLY C C 173.663 0.25 1 165 . 21 GLY CA C 45.280 0.25 1 166 . 21 GLY N N 112.718 0.20 1 167 . 22 ASP H H 7.878 0.03 1 168 . 22 ASP HA H 5.336 0.03 1 169 . 22 ASP HB2 H 2.992 0.03 1 170 . 22 ASP HB3 H 2.992 0.03 1 171 . 22 ASP C C 175.706 0.25 1 172 . 22 ASP CA C 54.440 0.25 1 173 . 22 ASP CB C 42.975 0.25 1 174 . 22 ASP N N 121.621 0.20 1 175 . 23 LEU H H 9.127 0.03 1 176 . 23 LEU HA H 4.592 0.03 1 177 . 23 LEU HB2 H 1.839 0.03 1 178 . 23 LEU HB3 H 1.839 0.03 1 179 . 23 LEU HG H 1.771 0.03 1 180 . 23 LEU HD1 H 0.830 0.03 2 181 . 23 LEU HD2 H 0.680 0.03 2 182 . 23 LEU C C 174.589 0.25 1 183 . 23 LEU CA C 54.035 0.25 1 184 . 23 LEU CB C 44.590 0.25 1 185 . 23 LEU CG C 26.632 0.25 1 186 . 23 LEU CD1 C 24.400 0.25 2 187 . 23 LEU CD2 C 26.400 0.25 2 188 . 23 LEU N N 125.658 0.20 1 189 . 24 GLY H H 8.201 0.03 1 190 . 24 GLY HA2 H 3.593 0.03 2 191 . 24 GLY HA3 H 4.408 0.03 2 192 . 24 GLY C C 173.259 0.25 1 193 . 24 GLY CA C 44.660 0.25 1 194 . 24 GLY N N 109.532 0.20 1 195 . 25 PHE H H 7.912 0.03 1 196 . 25 PHE HA H 5.093 0.03 1 197 . 25 PHE HB2 H 2.952 0.03 2 198 . 25 PHE HB3 H 3.329 0.03 2 199 . 25 PHE C C 174.083 0.25 1 200 . 25 PHE CA C 56.225 0.25 1 201 . 25 PHE CB C 40.195 0.25 1 202 . 25 PHE N N 113.705 0.20 1 203 . 26 GLU H H 9.012 0.03 1 204 . 26 GLU HA H 4.811 0.03 1 205 . 26 GLU HB2 H 1.969 0.03 2 206 . 26 GLU HB3 H 2.157 0.03 2 207 . 26 GLU HG2 H 2.402 0.03 2 208 . 26 GLU C C 175.847 0.25 1 209 . 26 GLU CA C 53.740 0.25 1 210 . 26 GLU CB C 32.780 0.25 1 211 . 26 GLU CG C 36.284 0.25 1 212 . 26 GLU N N 119.825 0.20 1 213 . 27 LYS H H 8.368 0.03 1 214 . 27 LYS HA H 3.419 0.03 1 215 . 27 LYS HB2 H 1.709 0.03 1 216 . 27 LYS HB3 H 1.709 0.03 1 217 . 27 LYS HG2 H 1.130 0.03 2 218 . 27 LYS HG3 H 1.220 0.03 2 219 . 27 LYS HD2 H 1.692 0.03 1 220 . 27 LYS HD3 H 1.692 0.03 1 221 . 27 LYS HE2 H 3.001 0.03 1 222 . 27 LYS HE3 H 3.001 0.03 1 223 . 27 LYS C C 177.183 0.25 1 224 . 27 LYS CA C 59.080 0.25 1 225 . 27 LYS CB C 32.610 0.25 1 226 . 27 LYS CG C 24.745 0.25 1 227 . 27 LYS CD C 30.003 0.25 1 228 . 27 LYS CE C 42.216 0.25 1 229 . 27 LYS N N 122.285 0.20 1 230 . 28 GLY H H 8.866 0.03 1 231 . 28 GLY HA2 H 3.518 0.03 2 232 . 28 GLY HA3 H 4.393 0.03 2 233 . 28 GLY C C 173.226 0.25 1 234 . 28 GLY CA C 45.085 0.25 1 235 . 28 GLY N N 115.369 0.20 1 236 . 29 GLU H H 8.140 0.03 1 237 . 29 GLU HA H 4.245 0.03 1 238 . 29 GLU HB2 H 2.130 0.03 2 239 . 29 GLU HB3 H 2.427 0.03 2 240 . 29 GLU HG2 H 2.411 0.03 2 241 . 29 GLU HG3 H 2.508 0.03 2 242 . 29 GLU C C 175.192 0.25 1 243 . 29 GLU CA C 57.905 0.25 1 244 . 29 GLU CB C 31.965 0.25 1 245 . 29 GLU CG C 36.982 0.25 1 246 . 29 GLU N N 122.716 0.20 1 247 . 30 GLN H H 8.447 0.03 1 248 . 30 GLN HA H 5.255 0.03 1 249 . 30 GLN HB2 H 2.050 0.03 1 250 . 30 GLN HB3 H 2.050 0.03 1 251 . 30 GLN HG2 H 2.136 0.03 2 252 . 30 GLN HG3 H 2.499 0.03 2 253 . 30 GLN C C 175.326 0.25 1 254 . 30 GLN CA C 55.125 0.25 1 255 . 30 GLN CB C 30.850 0.25 1 256 . 30 GLN CG C 34.888 0.25 1 257 . 30 GLN N N 121.850 0.20 1 258 . 31 LEU H H 8.818 0.03 1 259 . 31 LEU HA H 5.066 0.03 1 260 . 31 LEU HB2 H 1.161 0.03 1 261 . 31 LEU HB3 H 1.161 0.03 1 262 . 31 LEU HG H 1.387 0.03 1 263 . 31 LEU HD1 H 0.072 0.03 2 264 . 31 LEU HD2 H 0.671 0.03 2 265 . 31 LEU C C 174.436 0.25 1 266 . 31 LEU CA C 53.445 0.25 1 267 . 31 LEU CB C 45.945 0.25 1 268 . 31 LEU CG C 27.183 0.25 1 269 . 31 LEU CD1 C 25.699 0.25 2 270 . 31 LEU CD2 C 25.040 0.25 2 271 . 31 LEU N N 122.565 0.20 1 272 . 32 ARG H H 8.784 0.03 1 273 . 32 ARG HA H 5.039 0.03 1 274 . 32 ARG HB2 H 1.659 0.03 2 275 . 32 ARG HB3 H 1.710 0.03 2 276 . 32 ARG HG2 H 1.095 0.03 2 277 . 32 ARG HG3 H 1.395 0.03 2 278 . 32 ARG HD2 H 3.157 0.03 2 279 . 32 ARG HD3 H 3.223 0.03 2 280 . 32 ARG C C 175.872 0.25 1 281 . 32 ARG CA C 54.145 0.25 1 282 . 32 ARG CB C 32.830 0.25 1 283 . 32 ARG CG C 28.142 0.25 1 284 . 32 ARG CD C 43.233 0.25 1 285 . 32 ARG N N 120.267 0.20 1 286 . 33 ILE H H 8.992 0.03 1 287 . 33 ILE HA H 4.285 0.03 1 288 . 33 ILE HB H 2.009 0.03 1 289 . 33 ILE HG12 H 1.320 0.03 2 290 . 33 ILE HG13 H 1.620 0.03 2 291 . 33 ILE HG2 H 0.582 0.03 1 292 . 33 ILE HD1 H 0.790 0.03 1 293 . 33 ILE C C 175.645 0.25 1 294 . 33 ILE CA C 58.925 0.25 1 295 . 33 ILE CB C 35.575 0.25 1 296 . 33 ILE CG1 C 27.560 0.25 1 297 . 33 ILE CG2 C 18.836 0.25 1 298 . 33 ILE CD1 C 10.545 0.25 1 299 . 33 ILE N N 124.861 0.20 1 300 . 34 LEU H H 9.254 0.03 1 301 . 34 LEU HA H 4.393 0.03 1 302 . 34 LEU HB2 H 1.295 0.03 2 303 . 34 LEU HB3 H 1.592 0.03 2 304 . 34 LEU HG H 1.490 0.03 1 305 . 34 LEU HD1 H 0.700 0.03 2 306 . 34 LEU HD2 H 0.723 0.03 2 307 . 34 LEU C C 177.207 0.25 1 308 . 34 LEU CA C 55.570 0.25 1 309 . 34 LEU CB C 43.130 0.25 1 310 . 34 LEU CG C 26.752 0.25 1 311 . 34 LEU CD1 C 22.000 0.25 2 312 . 34 LEU CD2 C 25.400 0.25 2 313 . 34 LEU N N 128.566 0.20 1 314 . 35 GLU H H 7.713 0.03 1 315 . 35 GLU HA H 4.366 0.03 1 316 . 35 GLU HB2 H 1.982 0.03 2 317 . 35 GLU HB3 H 2.110 0.03 2 318 . 35 GLU HG2 H 2.234 0.03 1 319 . 35 GLU HG3 H 2.234 0.03 1 320 . 35 GLU C C 174.184 0.25 1 321 . 35 GLU CA C 56.425 0.25 1 322 . 35 GLU CB C 33.555 0.25 1 323 . 35 GLU CG C 36.284 0.25 1 324 . 35 GLU N N 117.611 0.20 1 325 . 36 GLN H H 8.605 0.03 1 326 . 36 GLN HA H 3.659 0.03 1 327 . 36 GLN HB2 H 1.053 0.03 2 328 . 36 GLN HB3 H 1.215 0.03 2 329 . 36 GLN HG2 H 0.826 0.03 2 330 . 36 GLN HG3 H 1.024 0.03 2 331 . 36 GLN C C 174.511 0.25 1 332 . 36 GLN CA C 53.525 0.25 1 333 . 36 GLN CB C 28.845 0.25 1 334 . 36 GLN CG C 33.260 0.25 1 335 . 36 GLN N N 124.884 0.20 1 336 . 37 SER H H 8.156 0.03 1 337 . 37 SER HA H 4.664 0.03 1 338 . 37 SER HB2 H 3.883 0.03 1 339 . 37 SER HB3 H 3.883 0.03 1 340 . 37 SER C C 174.385 0.25 1 341 . 37 SER CA C 56.965 0.25 1 342 . 37 SER CB C 63.975 0.25 1 343 . 37 SER N N 118.070 0.20 1 344 . 38 GLY H H 8.518 0.03 1 345 . 38 GLY HA2 H 3.787 0.03 2 346 . 38 GLY HA3 H 4.110 0.03 2 347 . 38 GLY C C 174.083 0.25 1 348 . 38 GLY CA C 46.005 0.25 1 349 . 38 GLY N N 112.210 0.20 1 350 . 39 GLU H H 8.659 0.03 1 351 . 39 GLU HA H 3.841 0.03 1 352 . 39 GLU HB2 H 1.720 0.03 2 353 . 39 GLU HB3 H 1.875 0.03 2 354 . 39 GLU HG2 H 1.797 0.03 2 355 . 39 GLU HG3 H 2.016 0.03 2 356 . 39 GLU C C 175.494 0.25 1 357 . 39 GLU CA C 56.855 0.25 1 358 . 39 GLU CB C 30.175 0.25 1 359 . 39 GLU CG C 36.633 0.25 1 360 . 39 GLU N N 120.797 0.20 1 361 . 40 TRP H H 7.780 0.03 1 362 . 40 TRP HA H 5.349 0.03 1 363 . 40 TRP HB2 H 2.992 0.03 1 364 . 40 TRP HB3 H 2.992 0.03 1 365 . 40 TRP HE1 H 9.980 0.03 1 366 . 40 TRP C C 175.593 0.25 1 367 . 40 TRP CA C 55.425 0.25 1 368 . 40 TRP CB C 30.270 0.25 1 369 . 40 TRP N N 120.872 0.20 1 370 . 40 TRP NE1 N 128.830 0.20 1 371 . 41 TRP H H 9.042 0.03 1 372 . 41 TRP HA H 5.484 0.03 1 373 . 41 TRP HB2 H 3.019 0.03 2 374 . 41 TRP HB3 H 3.356 0.03 2 375 . 41 TRP HE1 H 9.250 0.03 1 376 . 41 TRP C C 175.721 0.25 1 377 . 41 TRP CA C 54.065 0.25 1 378 . 41 TRP CB C 30.760 0.25 1 379 . 41 TRP N N 125.736 0.20 1 380 . 41 TRP NE1 N 128.590 0.20 1 381 . 42 LYS H H 8.747 0.03 1 382 . 42 LYS HA H 4.500 0.03 1 383 . 42 LYS HB2 H 1.642 0.03 2 384 . 42 LYS HB3 H 1.722 0.03 2 385 . 42 LYS HG2 H 0.868 0.03 2 386 . 42 LYS HG3 H 0.900 0.03 2 387 . 42 LYS HD2 H 1.426 0.03 1 388 . 42 LYS HD3 H 1.426 0.03 1 389 . 42 LYS HE2 H 2.631 0.03 2 390 . 42 LYS HE3 H 2.679 0.03 2 391 . 42 LYS C C 175.015 0.25 1 392 . 42 LYS CA C 56.225 0.25 1 393 . 42 LYS CB C 33.990 0.25 1 394 . 42 LYS CG C 25.710 0.25 1 395 . 42 LYS CD C 29.030 0.25 1 396 . 42 LYS CE C 41.738 0.25 1 397 . 42 LYS N N 123.722 0.20 1 398 . 43 ALA H H 9.442 0.03 1 399 . 43 ALA HA H 5.480 0.03 1 400 . 43 ALA HB H 1.261 0.03 1 401 . 43 ALA C C 173.931 0.25 1 402 . 43 ALA CA C 50.435 0.25 1 403 . 43 ALA CB C 25.655 0.25 1 404 . 43 ALA N N 131.286 0.20 1 405 . 44 GLN H H 8.997 0.03 1 406 . 44 GLN HA H 5.336 0.03 1 407 . 44 GLN HB2 H 1.767 0.03 1 408 . 44 GLN HB3 H 1.767 0.03 1 409 . 44 GLN HG2 H 2.018 0.03 2 410 . 44 GLN HG3 H 2.137 0.03 2 411 . 44 GLN C C 175.645 0.25 1 412 . 44 GLN CA C 53.285 0.25 1 413 . 44 GLN CB C 33.805 0.25 1 414 . 44 GLN CG C 33.563 0.25 1 415 . 44 GLN N N 117.489 0.20 1 416 . 45 SER H H 8.795 0.03 1 417 . 45 SER HA H 4.745 0.03 1 418 . 45 SER HB2 H 4.082 0.03 2 419 . 45 SER HB3 H 4.269 0.03 2 420 . 45 SER C C 177.737 0.25 1 421 . 45 SER CA C 57.875 0.25 1 422 . 45 SER CB C 63.455 0.25 1 423 . 45 SER N N 119.141 0.20 1 424 . 46 LEU H H 8.906 0.03 1 425 . 46 LEU HA H 4.339 0.03 1 426 . 46 LEU HB2 H 1.780 0.03 1 427 . 46 LEU HB3 H 1.780 0.03 1 428 . 46 LEU HG H 1.762 0.03 1 429 . 46 LEU HD1 H 0.827 0.03 2 430 . 46 LEU HD2 H 0.889 0.03 2 431 . 46 LEU C C 178.241 0.25 1 432 . 46 LEU CA C 57.245 0.25 1 433 . 46 LEU CB C 41.040 0.25 1 434 . 46 LEU CG C 28.978 0.25 1 435 . 46 LEU CD1 C 23.600 0.25 2 436 . 46 LEU CD2 C 25.492 0.25 2 437 . 46 LEU N N 130.960 0.20 1 438 . 47 THR H H 8.511 0.03 1 439 . 47 THR HA H 4.333 0.03 1 440 . 47 THR HB H 4.155 0.03 1 441 . 47 THR HG2 H 1.326 0.03 1 442 . 47 THR C C 176.779 0.25 1 443 . 47 THR CA C 64.810 0.25 1 444 . 47 THR CB C 69.370 0.25 1 445 . 47 THR N N 114.019 0.20 1 446 . 48 THR H H 8.156 0.03 1 447 . 48 THR HA H 4.533 0.03 1 448 . 48 THR HB H 4.537 0.03 1 449 . 48 THR HG2 H 1.308 0.03 1 450 . 48 THR CA C 61.775 0.25 1 451 . 48 THR CB C 71.375 0.25 1 452 . 48 THR N N 108.440 0.20 1 453 . 49 GLY H H 7.691 0.03 1 454 . 49 GLY HA2 H 3.881 0.03 2 455 . 49 GLY HA3 H 4.299 0.03 2 456 . 49 GLY C C 173.906 0.25 1 457 . 49 GLY CA C 45.795 0.25 1 458 . 49 GLY N N 110.478 0.20 1 459 . 50 GLN H H 7.956 0.03 1 460 . 50 GLN HA H 4.285 0.03 1 461 . 50 GLN HB2 H 1.982 0.03 2 462 . 50 GLN HB3 H 2.117 0.03 2 463 . 50 GLN HG2 H 2.237 0.03 1 464 . 50 GLN HG3 H 2.237 0.03 1 465 . 50 GLN C C 174.193 0.25 1 466 . 50 GLN CA C 56.570 0.25 1 467 . 50 GLN CB C 29.510 0.25 1 468 . 50 GLN CG C 34.074 0.25 1 469 . 50 GLN N N 120.786 0.20 1 470 . 51 GLU H H 8.566 0.03 1 471 . 51 GLU HA H 5.740 0.03 1 472 . 51 GLU HB2 H 1.863 0.03 2 473 . 51 GLU HB3 H 1.926 0.03 2 474 . 51 GLU HG2 H 2.066 0.03 2 475 . 51 GLU HG3 H 2.288 0.03 2 476 . 51 GLU C C 176.679 0.25 1 477 . 51 GLU CA C 53.775 0.25 1 478 . 51 GLU CB C 34.145 0.25 1 479 . 51 GLU CG C 36.168 0.25 1 480 . 51 GLU N N 119.811 0.20 1 481 . 52 GLY H H 8.758 0.03 1 482 . 52 GLY HA2 H 3.975 0.03 2 483 . 52 GLY HA3 H 4.157 0.03 2 484 . 52 GLY C C 171.058 0.25 1 485 . 52 GLY CA C 45.610 0.25 1 486 . 52 GLY N N 107.510 0.20 1 487 . 53 PHE H H 8.731 0.03 1 488 . 53 PHE HA H 5.686 0.03 1 489 . 53 PHE HB2 H 3.181 0.03 1 490 . 53 PHE HB3 H 3.181 0.03 1 491 . 53 PHE C C 176.603 0.25 1 492 . 53 PHE CA C 58.805 0.25 1 493 . 53 PHE CB C 41.415 0.25 1 494 . 53 PHE N N 119.343 0.20 1 495 . 54 ILE H H 9.593 0.03 1 496 . 54 ILE HA H 5.200 0.03 1 497 . 54 ILE HB H 1.700 0.03 1 498 . 54 ILE HG12 H 1.070 0.03 2 499 . 54 ILE HG13 H 1.470 0.03 2 500 . 54 ILE HG2 H 1.180 0.03 1 501 . 54 ILE HD1 H 0.480 0.03 1 502 . 54 ILE CA C 57.320 0.25 1 503 . 54 ILE CB C 41.090 0.25 1 504 . 54 ILE CG2 C 21.300 0.25 1 505 . 54 ILE CD1 C 15.700 0.25 1 506 . 54 ILE N N 113.087 0.20 1 507 . 55 PRO HA H 3.760 0.03 1 508 . 55 PRO HB2 H 1.255 0.03 1 509 . 55 PRO HB3 H 1.255 0.03 1 510 . 55 PRO HG2 H 0.698 0.03 1 511 . 55 PRO HG3 H 0.698 0.03 1 512 . 55 PRO HD2 H 2.858 0.03 1 513 . 55 PRO HD3 H 2.858 0.03 1 514 . 55 PRO C C 179.627 0.25 1 515 . 55 PRO CA C 61.660 0.25 1 516 . 55 PRO CB C 30.400 0.25 1 517 . 55 PRO CG C 26.961 0.25 1 518 . 55 PRO CD C 49.838 0.25 1 519 . 56 PHE H H 7.548 0.03 1 520 . 56 PHE HA H 2.925 0.03 1 521 . 56 PHE HB2 H 1.155 0.03 2 522 . 56 PHE HB3 H 1.606 0.03 2 523 . 56 PHE C C 173.931 0.25 1 524 . 56 PHE CA C 59.440 0.25 1 525 . 56 PHE CB C 35.625 0.25 1 526 . 56 PHE N N 123.641 0.20 1 527 . 57 ASN H H 7.271 0.03 1 528 . 57 ASN HA H 4.056 0.03 1 529 . 57 ASN HB2 H 1.511 0.03 2 530 . 57 ASN HB3 H 2.561 0.03 2 531 . 57 ASN C C 175.746 0.25 1 532 . 57 ASN CA C 52.230 0.25 1 533 . 57 ASN CB C 35.680 0.25 1 534 . 57 ASN N N 113.460 0.20 1 535 . 58 PHE H H 7.678 0.03 1 536 . 58 PHE HA H 4.568 0.03 1 537 . 58 PHE HB2 H 3.659 0.03 1 538 . 58 PHE HB3 H 3.659 0.03 1 539 . 58 PHE C C 174.562 0.25 1 540 . 58 PHE CA C 58.170 0.25 1 541 . 58 PHE CB C 39.340 0.25 1 542 . 58 PHE N N 119.753 0.20 1 543 . 59 VAL H H 7.047 0.03 1 544 . 59 VAL HA H 5.270 0.03 1 545 . 59 VAL HB H 1.771 0.03 1 546 . 59 VAL HG1 H 0.438 0.03 2 547 . 59 VAL HG2 H 0.722 0.03 2 548 . 59 VAL C C 173.605 0.25 1 549 . 59 VAL CA C 58.485 0.25 1 550 . 59 VAL CB C 35.780 0.25 1 551 . 59 VAL CG1 C 21.896 0.25 2 552 . 59 VAL CG2 C 17.852 0.25 2 553 . 59 VAL N N 108.958 0.20 1 554 . 60 ALA H H 8.579 0.03 1 555 . 60 ALA HA H 4.757 0.03 1 556 . 60 ALA HB H 1.403 0.03 1 557 . 60 ALA C C 176.351 0.25 1 558 . 60 ALA CA C 50.710 0.25 1 559 . 60 ALA CB C 23.190 0.25 1 560 . 60 ALA N N 121.548 0.20 1 561 . 61 LYS H H 8.730 0.03 1 562 . 61 LYS HA H 4.313 0.03 1 563 . 61 LYS HB2 H 1.910 0.03 2 564 . 61 LYS HB3 H 1.826 0.03 2 565 . 61 LYS HG2 H 1.584 0.03 2 566 . 61 LYS HG3 H 1.669 0.03 2 567 . 61 LYS HD2 H 1.785 0.03 1 568 . 61 LYS HD3 H 1.785 0.03 1 569 . 61 LYS HE2 H 3.039 0.03 1 570 . 61 LYS HE3 H 3.039 0.03 1 571 . 61 LYS C C 176.824 0.25 1 572 . 61 LYS CA C 57.435 0.25 1 573 . 61 LYS CB C 32.675 0.25 1 574 . 61 LYS CG C 25.135 0.25 1 575 . 61 LYS CD C 29.283 0.25 1 576 . 61 LYS CE C 42.077 0.25 1 577 . 61 LYS N N 120.578 0.20 1 578 . 62 ALA H H 8.417 0.03 1 579 . 62 ALA HA H 4.270 0.03 1 580 . 62 ALA HB H 1.324 0.03 1 581 . 62 ALA C C 177.226 0.25 1 582 . 62 ALA CA C 52.930 0.25 1 583 . 62 ALA CB C 19.315 0.25 1 584 . 62 ALA N N 126.095 0.20 1 585 . 63 ASN H H 8.507 0.03 1 586 . 63 ASN HA H 4.647 0.03 1 587 . 63 ASN HB2 H 2.817 0.03 1 588 . 63 ASN HB3 H 2.817 0.03 1 589 . 63 ASN C C 175.192 0.25 1 590 . 63 ASN CA C 53.205 0.25 1 591 . 63 ASN CB C 38.625 0.25 1 592 . 63 ASN N N 117.201 0.20 1 593 . 64 SER H H 8.159 0.03 1 594 . 64 SER HA H 4.447 0.03 1 595 . 64 SER HB2 H 3.820 0.03 2 596 . 64 SER HB3 H 3.920 0.03 2 597 . 64 SER C C 174.461 0.25 1 598 . 64 SER CA C 58.585 0.25 1 599 . 64 SER CB C 64.090 0.25 1 600 . 64 SER N N 115.678 0.20 1 601 . 65 LEU H H 8.226 0.03 1 602 . 65 LEU HA H 4.280 0.03 1 603 . 65 LEU HB2 H 1.570 0.03 1 604 . 65 LEU HB3 H 1.570 0.03 1 605 . 65 LEU HG H 1.387 0.03 1 606 . 65 LEU HD1 H 0.680 0.03 2 607 . 65 LEU HD2 H 0.700 0.03 2 608 . 65 LEU C C 177.435 0.25 1 609 . 65 LEU CA C 55.300 0.25 1 610 . 65 LEU CB C 42.115 0.25 1 611 . 65 LEU CG C 27.328 0.25 1 612 . 65 LEU CD1 C 23.400 0.25 2 613 . 65 LEU CD2 C 25.200 0.25 2 614 . 65 LEU N N 123.415 0.20 1 615 . 66 GLU H H 8.216 0.03 1 616 . 66 GLU CA C 55.770 0.25 1 617 . 66 GLU CB C 35.920 0.25 1 618 . 66 GLU N N 120.243 0.20 1 619 . 67 PRO HA H 4.366 0.03 1 620 . 67 PRO HB2 H 1.807 0.03 2 621 . 67 PRO HB3 H 2.225 0.03 2 622 . 67 PRO HG2 H 1.919 0.03 1 623 . 67 PRO HG3 H 1.919 0.03 1 624 . 67 PRO HD2 H 3.667 0.03 1 625 . 67 PRO HD3 H 3.667 0.03 1 626 . 67 PRO C C 176.962 0.25 1 627 . 67 PRO CA C 63.440 0.25 1 628 . 67 PRO CB C 32.000 0.25 1 629 . 67 PRO CG C 27.560 0.25 1 630 . 67 PRO CD C 50.591 0.25 1 631 . 68 GLU H H 7.990 0.03 1 632 . 68 GLU CA C 53.500 0.25 1 633 . 68 GLU CB C 29.765 0.25 1 634 . 68 GLU N N 119.616 0.20 1 635 . 69 PRO HA H 4.256 0.03 1 636 . 69 PRO HB2 H 1.781 0.03 2 637 . 69 PRO HB3 H 1.931 0.03 2 638 . 69 PRO HG2 H 1.915 0.03 1 639 . 69 PRO HG3 H 1.915 0.03 1 640 . 69 PRO C C 175.645 0.25 1 641 . 69 PRO CA C 64.170 0.25 1 642 . 69 PRO CB C 31.650 0.25 1 643 . 69 PRO CG C 27.535 0.25 1 644 . 69 PRO CD C 50.591 0.25 1 645 . 70 TRP H H 5.911 0.03 1 646 . 70 TRP HA H 4.622 0.03 1 647 . 70 TRP HB2 H 2.575 0.03 2 648 . 70 TRP HB3 H 3.679 0.03 2 649 . 70 TRP C C 174.814 0.25 1 650 . 70 TRP CA C 53.235 0.25 1 651 . 70 TRP CB C 31.910 0.25 1 652 . 70 TRP N N 108.983 0.20 1 653 . 71 PHE H H 7.409 0.03 1 654 . 71 PHE HA H 5.390 0.03 1 655 . 71 PHE HB2 H 2.810 0.03 2 656 . 71 PHE HB3 H 2.440 0.03 2 657 . 71 PHE C C 174.209 0.25 1 658 . 71 PHE CA C 57.865 0.25 1 659 . 71 PHE CB C 39.605 0.25 1 660 . 71 PHE N N 123.159 0.20 1 661 . 72 PHE H H 8.698 0.03 1 662 . 72 PHE HA H 4.490 0.03 1 663 . 72 PHE HB2 H 2.970 0.03 2 664 . 72 PHE HB3 H 2.680 0.03 2 665 . 72 PHE C C 175.793 0.25 1 666 . 72 PHE CA C 56.315 0.25 1 667 . 72 PHE CB C 41.050 0.25 1 668 . 72 PHE N N 129.575 0.20 1 669 . 73 LYS H H 7.661 0.03 1 670 . 73 LYS HA H 3.810 0.03 1 671 . 73 LYS HB2 H 1.725 0.03 1 672 . 73 LYS HB3 H 1.725 0.03 1 673 . 73 LYS HG2 H 1.429 0.03 2 674 . 73 LYS HG3 H 1.483 0.03 2 675 . 73 LYS HD2 H 1.714 0.03 1 676 . 73 LYS HD3 H 1.714 0.03 1 677 . 73 LYS HE2 H 3.082 0.03 1 678 . 73 LYS HE3 H 3.082 0.03 1 679 . 73 LYS C C 175.967 0.25 1 680 . 73 LYS CA C 57.455 0.25 1 681 . 73 LYS CB C 33.280 0.25 1 682 . 73 LYS CG C 24.900 0.25 1 683 . 73 LYS CD C 29.816 0.25 1 684 . 73 LYS CE C 42.200 0.25 1 685 . 73 LYS N N 119.952 0.20 1 686 . 74 ASN H H 8.551 0.03 1 687 . 74 ASN HA H 4.635 0.03 1 688 . 74 ASN HB2 H 2.844 0.03 2 689 . 74 ASN HB3 H 2.938 0.03 2 690 . 74 ASN C C 173.679 0.25 1 691 . 74 ASN CA C 53.710 0.25 1 692 . 74 ASN CB C 37.800 0.25 1 693 . 74 ASN N N 116.973 0.20 1 694 . 75 LEU H H 7.579 0.03 1 695 . 75 LEU HA H 4.662 0.03 1 696 . 75 LEU HB2 H 1.390 0.03 2 697 . 75 LEU HB3 H 1.605 0.03 2 698 . 75 LEU HD1 H 0.580 0.03 2 699 . 75 LEU HD2 H 0.860 0.03 2 700 . 75 LEU C C 175.927 0.25 1 701 . 75 LEU CA C 54.255 0.25 1 702 . 75 LEU CB C 44.780 0.25 1 703 . 75 LEU CG C 26.513 0.25 1 704 . 75 LEU CD1 C 26.900 0.25 2 705 . 75 LEU CD2 C 25.200 0.25 2 706 . 75 LEU N N 121.455 0.20 1 707 . 76 SER H H 9.169 0.03 1 708 . 76 SER HA H 4.380 0.03 1 709 . 76 SER HB2 H 4.050 0.03 1 710 . 76 SER HB3 H 4.050 0.03 1 711 . 76 SER C C 173.969 0.25 1 712 . 76 SER CA C 57.410 0.25 1 713 . 76 SER CB C 65.535 0.25 1 714 . 76 SER N N 123.139 0.20 1 715 . 77 ARG H H 8.833 0.03 1 716 . 77 ARG HA H 3.440 0.03 1 717 . 77 ARG HB2 H 1.620 0.03 2 718 . 77 ARG HB3 H 1.720 0.03 2 719 . 77 ARG HG2 H 1.469 0.03 2 720 . 77 ARG HG3 H 1.592 0.03 2 721 . 77 ARG HD2 H 3.070 0.03 1 722 . 77 ARG HD3 H 3.070 0.03 1 723 . 77 ARG C C 177.964 0.25 1 724 . 77 ARG CA C 60.665 0.25 1 725 . 77 ARG CB C 30.500 0.25 1 726 . 77 ARG CG C 27.560 0.25 1 727 . 77 ARG CD C 43.031 0.25 1 728 . 77 ARG N N 122.423 0.20 1 729 . 78 LYS H H 8.372 0.03 1 730 . 78 LYS HA H 3.960 0.03 1 731 . 78 LYS HB2 H 1.725 0.03 2 732 . 78 LYS HB3 H 1.934 0.03 2 733 . 78 LYS HG2 H 1.429 0.03 2 734 . 78 LYS HG3 H 1.482 0.03 2 735 . 78 LYS HD2 H 1.685 0.03 1 736 . 78 LYS HD3 H 1.685 0.03 1 737 . 78 LYS HE2 H 2.968 0.03 1 738 . 78 LYS HE3 H 2.968 0.03 1 739 . 78 LYS C C 173.935 0.25 1 740 . 78 LYS CA C 59.090 0.25 1 741 . 78 LYS CB C 32.155 0.25 1 742 . 78 LYS CG C 24.900 0.25 1 743 . 78 LYS CD C 29.072 0.25 1 744 . 78 LYS CE C 41.984 0.25 1 745 . 78 LYS N N 116.861 0.20 1 746 . 79 ASP H H 7.954 0.03 1 747 . 79 ASP HA H 4.474 0.03 1 748 . 79 ASP HB2 H 2.640 0.03 2 749 . 79 ASP HB3 H 2.740 0.03 2 750 . 79 ASP C C 178.493 0.25 1 751 . 79 ASP CA C 57.205 0.25 1 752 . 79 ASP CB C 40.310 0.25 1 753 . 79 ASP N N 120.653 0.20 1 754 . 80 ALA H H 8.645 0.03 1 755 . 80 ALA HA H 3.800 0.03 1 756 . 80 ALA HB H 1.470 0.03 1 757 . 80 ALA C C 179.022 0.25 1 758 . 80 ALA CA C 55.230 0.25 1 759 . 80 ALA CB C 18.555 0.25 1 760 . 80 ALA N N 123.298 0.20 1 761 . 81 GLU H H 7.812 0.03 1 762 . 81 GLU HA H 3.827 0.03 1 763 . 81 GLU HB2 H 2.050 0.03 2 764 . 81 GLU HB3 H 2.319 0.03 2 765 . 81 GLU HG2 H 2.877 0.03 1 766 . 81 GLU HG3 H 2.877 0.03 1 767 . 81 GLU C C 177.057 0.25 1 768 . 81 GLU CA C 60.200 0.25 1 769 . 81 GLU CB C 28.650 0.25 1 770 . 81 GLU CG C 36.733 0.25 1 771 . 81 GLU N N 115.648 0.20 1 772 . 82 ARG H H 7.565 0.03 1 773 . 82 ARG HA H 3.890 0.03 1 774 . 82 ARG HB2 H 1.935 0.03 1 775 . 82 ARG HB3 H 1.935 0.03 1 776 . 82 ARG HG2 H 1.468 0.03 2 777 . 82 ARG HG3 H 1.594 0.03 2 778 . 82 ARG HD2 H 3.157 0.03 1 779 . 82 ARG HD3 H 3.157 0.03 1 780 . 82 ARG C C 179.501 0.25 1 781 . 82 ARG CA C 59.395 0.25 1 782 . 82 ARG CB C 30.045 0.25 1 783 . 82 ARG CG C 27.444 0.25 1 784 . 82 ARG CD C 43.342 0.25 1 785 . 82 ARG N N 116.708 0.20 1 786 . 83 GLN H H 8.265 0.03 1 787 . 83 GLN HA H 3.890 0.03 1 788 . 83 GLN HB2 H 1.900 0.03 2 789 . 83 GLN HB3 H 1.803 0.03 2 790 . 83 GLN HG2 H 2.215 0.03 2 791 . 83 GLN HG3 H 2.290 0.03 2 792 . 83 GLN C C 178.972 0.25 1 793 . 83 GLN CA C 58.855 0.25 1 794 . 83 GLN CB C 28.655 0.25 1 795 . 83 GLN CG C 34.539 0.25 1 796 . 83 GLN N N 116.892 0.20 1 797 . 84 LEU H H 8.002 0.03 1 798 . 84 LEU HA H 4.056 0.03 1 799 . 84 LEU HB2 H 1.653 0.03 2 800 . 84 LEU HB3 H 1.740 0.03 2 801 . 84 LEU HG H 1.645 0.03 1 802 . 84 LEU HD1 H 0.560 0.03 1 803 . 84 LEU HD2 H 0.560 0.03 1 804 . 84 LEU C C 178.292 0.25 1 805 . 84 LEU CA C 57.265 0.25 1 806 . 84 LEU CB C 43.137 0.25 1 807 . 84 LEU CG C 27.095 0.25 1 808 . 84 LEU CD1 C 23.500 0.25 2 809 . 84 LEU CD2 C 27.000 0.25 2 810 . 84 LEU N N 117.977 0.20 1 811 . 85 LEU H H 7.661 0.03 1 812 . 85 LEU HA H 4.067 0.03 1 813 . 85 LEU HB2 H 1.785 0.03 1 814 . 85 LEU HB3 H 1.785 0.03 1 815 . 85 LEU HG H 1.278 0.03 1 816 . 85 LEU HD1 H 0.600 0.03 2 817 . 85 LEU HD2 H 0.850 0.03 2 818 . 85 LEU C C 176.023 0.25 1 819 . 85 LEU CA C 55.680 0.25 1 820 . 85 LEU CB C 41.020 0.25 1 821 . 85 LEU CG C 25.467 0.25 1 822 . 85 LEU CD1 C 21.900 0.25 2 823 . 85 LEU CD2 C 25.400 0.25 2 824 . 85 LEU N N 117.251 0.20 1 825 . 86 ALA H H 7.040 0.03 1 826 . 86 ALA HA H 4.460 0.03 1 827 . 86 ALA HB H 1.450 0.03 1 828 . 86 ALA CA C 51.400 0.25 1 829 . 86 ALA CB C 17.400 0.25 1 830 . 86 ALA N N 124.485 0.20 1 831 . 87 PRO HA H 4.498 0.03 1 832 . 87 PRO HB2 H 1.912 0.03 2 833 . 87 PRO HB3 H 2.310 0.03 2 834 . 87 PRO HG2 H 1.493 0.03 1 835 . 87 PRO HG3 H 1.493 0.03 1 836 . 87 PRO C C 176.628 0.25 1 837 . 87 PRO CA C 64.070 0.25 1 838 . 87 PRO CB C 32.166 0.25 1 839 . 87 PRO CG C 27.909 0.25 1 840 . 88 GLY H H 8.604 0.03 1 841 . 88 GLY HA2 H 3.666 0.03 2 842 . 88 GLY HA3 H 4.299 0.03 2 843 . 88 GLY C C 174.324 0.25 1 844 . 88 GLY CA C 44.790 0.25 1 845 . 88 GLY N N 109.373 0.20 1 846 . 89 ASN H H 7.248 0.03 1 847 . 89 ASN HA H 4.840 0.03 1 848 . 89 ASN HB2 H 2.663 0.03 2 849 . 89 ASN HB3 H 2.884 0.03 2 850 . 89 ASN C C 172.712 0.25 1 851 . 89 ASN CA C 52.725 0.25 1 852 . 89 ASN CB C 42.130 0.25 1 853 . 89 ASN N N 116.173 0.20 1 854 . 90 THR H H 8.932 0.03 1 855 . 90 THR HA H 4.600 0.03 1 856 . 90 THR HB H 4.100 0.03 1 857 . 90 THR HG2 H 1.070 0.03 1 858 . 90 THR CA C 59.480 0.25 1 859 . 90 THR CB C 70.900 0.25 1 860 . 90 THR N N 111.899 0.20 1 861 . 91 HIS HA H 4.324 0.03 1 862 . 91 HIS HB2 H 3.080 0.03 2 863 . 91 HIS HB3 H 3.190 0.03 2 864 . 91 HIS C C 176.931 0.25 1 865 . 91 HIS CA C 57.130 0.25 1 866 . 91 HIS CB C 29.350 0.25 1 867 . 92 GLY H H 9.396 0.03 1 868 . 92 GLY HA2 H 3.420 0.03 2 869 . 92 GLY HA3 H 4.460 0.03 2 870 . 92 GLY C C 175.393 0.25 1 871 . 92 GLY CA C 46.110 0.25 1 872 . 92 GLY N N 116.550 0.20 1 873 . 93 SER H H 8.602 0.03 1 874 . 93 SER HA H 5.722 0.03 1 875 . 93 SER HB2 H 3.771 0.03 2 876 . 93 SER HB3 H 3.971 0.03 2 877 . 93 SER C C 174.385 0.25 1 878 . 93 SER CA C 61.280 0.25 1 879 . 93 SER CB C 63.525 0.25 1 880 . 93 SER N N 121.215 0.20 1 881 . 94 PHE H H 7.854 0.03 1 882 . 94 PHE HA H 6.011 0.03 1 883 . 94 PHE HB2 H 2.960 0.03 1 884 . 94 PHE HB3 H 2.960 0.03 1 885 . 94 PHE C C 172.697 0.25 1 886 . 94 PHE CA C 55.915 0.25 1 887 . 94 PHE CB C 44.380 0.25 1 888 . 94 PHE N N 116.884 0.20 1 889 . 95 LEU H H 9.169 0.03 1 890 . 95 LEU HA H 4.956 0.03 1 891 . 95 LEU HB2 H 1.630 0.03 1 892 . 95 LEU HB3 H 1.630 0.03 1 893 . 95 LEU HD1 H 0.200 0.03 2 894 . 95 LEU HD2 H 0.800 0.03 2 895 . 95 LEU C C 174.511 0.25 1 896 . 95 LEU CA C 54.620 0.25 1 897 . 95 LEU CB C 45.600 0.25 1 898 . 95 LEU CD1 C 27.600 0.25 2 899 . 95 LEU CD2 C 25.300 0.25 2 900 . 95 LEU N N 115.338 0.20 1 901 . 96 ILE H H 9.678 0.03 1 902 . 96 ILE HA H 5.400 0.03 1 903 . 96 ILE HB H 2.130 0.03 1 904 . 96 ILE HG12 H 0.910 0.03 2 905 . 96 ILE HG13 H 1.700 0.03 2 906 . 96 ILE HG2 H 1.080 0.03 1 907 . 96 ILE HD1 H 0.460 0.03 1 908 . 96 ILE C C 172.848 0.25 1 909 . 96 ILE CA C 60.550 0.25 1 910 . 96 ILE CB C 39.880 0.25 1 911 . 96 ILE CG1 C 29.654 0.25 1 912 . 96 ILE CG2 C 18.200 0.25 1 913 . 96 ILE CD1 C 13.200 0.25 1 914 . 96 ILE N N 121.132 0.20 1 915 . 97 ARG H H 9.022 0.03 1 916 . 97 ARG HA H 5.484 0.03 1 917 . 97 ARG HB2 H 1.969 0.03 2 918 . 97 ARG HB3 H 2.113 0.03 2 919 . 97 ARG HG2 H 1.099 0.03 1 920 . 97 ARG HG3 H 1.099 0.03 1 921 . 97 ARG C C 175.066 0.25 1 922 . 97 ARG CA C 52.065 0.25 1 923 . 97 ARG CB C 33.525 0.25 1 924 . 97 ARG CG C 26.630 0.25 1 925 . 97 ARG N N 122.430 0.20 1 926 . 98 GLU H H 8.800 0.03 1 927 . 98 GLU HA H 4.595 0.03 1 928 . 98 GLU HB2 H 2.130 0.03 1 929 . 98 GLU HB3 H 2.130 0.03 1 930 . 98 GLU HG2 H 2.330 0.03 2 931 . 98 GLU HG3 H 2.528 0.03 2 932 . 98 GLU C C 176.023 0.25 1 933 . 98 GLU CA C 56.290 0.25 1 934 . 98 GLU CB C 31.305 0.25 1 935 . 98 GLU CG C 36.866 0.25 1 936 . 98 GLU N N 123.015 0.20 1 937 . 99 SER H H 8.379 0.03 1 938 . 99 SER HA H 4.310 0.03 1 939 . 99 SER HB2 H 3.750 0.03 2 940 . 99 SER HB3 H 3.940 0.03 2 941 . 99 SER C C 175.444 0.25 1 942 . 99 SER CA C 58.260 0.25 1 943 . 99 SER CB C 63.595 0.25 1 944 . 99 SER N N 119.397 0.20 1 945 . 100 GLU H H 9.480 0.03 1 946 . 100 GLU HA H 4.245 0.03 1 947 . 100 GLU HB2 H 2.090 0.03 1 948 . 100 GLU HB3 H 2.090 0.03 1 949 . 100 GLU HG2 H 2.296 0.03 2 950 . 100 GLU HG3 H 2.422 0.03 2 951 . 100 GLU C C 177.283 0.25 1 952 . 100 GLU CA C 57.975 0.25 1 953 . 100 GLU CB C 30.310 0.25 1 954 . 100 GLU CG C 36.633 0.25 1 955 . 100 GLU N N 126.973 0.20 1 956 . 101 SER H H 8.307 0.03 1 957 . 101 SER HA H 4.460 0.03 1 958 . 101 SER HB2 H 3.841 0.03 1 959 . 101 SER HB3 H 3.841 0.03 1 960 . 101 SER C C 175.166 0.25 1 961 . 101 SER CA C 59.255 0.25 1 962 . 101 SER CB C 64.380 0.25 1 963 . 101 SER N N 113.403 0.20 1 964 . 102 THR H H 7.704 0.03 1 965 . 102 THR HA H 4.393 0.03 1 966 . 102 THR HB H 3.949 0.03 1 967 . 102 THR HG2 H 1.182 0.03 1 968 . 102 THR C C 172.772 0.25 1 969 . 102 THR CA C 61.145 0.25 1 970 . 102 THR CB C 70.190 0.25 1 971 . 102 THR N N 119.009 0.20 1 972 . 103 ALA H H 8.396 0.03 1 973 . 103 ALA HA H 4.223 0.03 1 974 . 103 ALA HB H 1.363 0.03 1 975 . 103 ALA C C 179.426 0.25 1 976 . 103 ALA CA C 53.290 0.25 1 977 . 103 ALA CB C 18.355 0.25 1 978 . 103 ALA N N 128.964 0.20 1 979 . 104 GLY H H 9.501 0.03 1 980 . 104 GLY HA2 H 3.598 0.03 2 981 . 104 GLY HA3 H 4.151 0.03 2 982 . 104 GLY C C 173.095 0.25 1 983 . 104 GLY CA C 45.660 0.25 1 984 . 104 GLY N N 111.256 0.20 1 985 . 105 SER H H 7.410 0.03 1 986 . 105 SER HA H 4.986 0.03 1 987 . 105 SER HB2 H 4.043 0.03 2 988 . 105 SER HB3 H 3.753 0.03 2 989 . 105 SER C C 173.453 0.25 1 990 . 105 SER CA C 56.745 0.25 1 991 . 105 SER CB C 64.730 0.25 1 992 . 105 SER N N 113.381 0.20 1 993 . 106 PHE H H 9.337 0.03 1 994 . 106 PHE HA H 5.580 0.03 1 995 . 106 PHE HB2 H 2.710 0.03 2 996 . 106 PHE HB3 H 3.143 0.03 2 997 . 106 PHE C C 175.116 0.25 1 998 . 106 PHE CA C 57.070 0.25 1 999 . 106 PHE CB C 43.605 0.25 1 1000 . 106 PHE N N 123.233 0.20 1 1001 . 107 SER H H 9.236 0.03 1 1002 . 107 SER HA H 5.349 0.03 1 1003 . 107 SER HB2 H 3.423 0.03 2 1004 . 107 SER HB3 H 3.773 0.03 2 1005 . 107 SER C C 171.285 0.25 1 1006 . 107 SER CA C 58.290 0.25 1 1007 . 107 SER CB C 66.500 0.25 1 1008 . 107 SER N N 115.506 0.20 1 1009 . 108 LEU H H 9.430 0.03 1 1010 . 108 LEU HA H 5.322 0.03 1 1011 . 108 LEU HB2 H 1.292 0.03 2 1012 . 108 LEU HB3 H 1.942 0.03 2 1013 . 108 LEU HD1 H 0.770 0.03 2 1014 . 108 LEU HD2 H 0.430 0.03 2 1015 . 108 LEU C C 175.066 0.25 1 1016 . 108 LEU CA C 53.540 0.25 1 1017 . 108 LEU CB C 45.420 0.25 1 1018 . 108 LEU CD1 C 24.200 0.25 2 1019 . 108 LEU CD2 C 27.000 0.25 2 1020 . 108 LEU N N 126.838 0.20 1 1021 . 109 SER H H 9.306 0.03 1 1022 . 109 SER HA H 5.578 0.03 1 1023 . 109 SER HB2 H 3.410 0.03 1 1024 . 109 SER HB3 H 3.410 0.03 1 1025 . 109 SER C C 172.293 0.25 1 1026 . 109 SER CA C 58.635 0.25 1 1027 . 109 SER CB C 65.675 0.25 1 1028 . 109 SER N N 124.515 0.20 1 1029 . 110 VAL H H 9.138 0.03 1 1030 . 110 VAL HA H 4.986 0.03 1 1031 . 110 VAL HB H 1.794 0.03 1 1032 . 110 VAL HG1 H 0.826 0.03 2 1033 . 110 VAL HG2 H 0.800 0.03 2 1034 . 110 VAL C C 173.352 0.25 1 1035 . 110 VAL CA C 59.880 0.25 1 1036 . 110 VAL CB C 36.450 0.25 1 1037 . 110 VAL CG1 C 21.800 0.25 2 1038 . 110 VAL CG2 C 20.500 0.25 2 1039 . 110 VAL N N 122.778 0.20 1 1040 . 111 ARG H H 8.894 0.03 1 1041 . 111 ARG HA H 4.703 0.03 1 1042 . 111 ARG HB2 H 1.910 0.03 2 1043 . 111 ARG HB3 H 2.305 0.03 2 1044 . 111 ARG HG2 H 1.592 0.03 1 1045 . 111 ARG HG3 H 1.592 0.03 1 1046 . 111 ARG HD2 H 3.140 0.03 2 1047 . 111 ARG HD3 H 3.021 0.03 2 1048 . 111 ARG C C 173.478 0.25 1 1049 . 111 ARG CA C 55.840 0.25 1 1050 . 111 ARG CB C 31.790 0.25 1 1051 . 111 ARG CG C 27.305 0.25 1 1052 . 111 ARG CD C 43.833 0.25 1 1053 . 111 ARG N N 128.033 0.20 1 1054 . 112 ASP H H 9.303 0.03 1 1055 . 112 ASP HA H 5.070 0.03 1 1056 . 112 ASP HB2 H 2.620 0.03 2 1057 . 112 ASP HB3 H 2.400 0.03 2 1058 . 112 ASP C C 174.864 0.25 1 1059 . 112 ASP CA C 52.630 0.25 1 1060 . 112 ASP CB C 45.295 0.25 1 1061 . 112 ASP N N 129.177 0.20 1 1062 . 113 PHE H H 8.868 0.03 1 1063 . 113 PHE HA H 4.857 0.03 1 1064 . 113 PHE HB2 H 2.770 0.03 1 1065 . 113 PHE HB3 H 2.770 0.03 1 1066 . 113 PHE C C 174.286 0.25 1 1067 . 113 PHE CA C 57.515 0.25 1 1068 . 113 PHE CB C 41.585 0.25 1 1069 . 113 PHE N N 121.642 0.20 1 1070 . 114 ASP H H 8.414 0.03 1 1071 . 114 ASP HA H 4.630 0.03 1 1072 . 114 ASP HB2 H 2.570 0.03 1 1073 . 114 ASP HB3 H 2.570 0.03 1 1074 . 114 ASP C C 176.124 0.25 1 1075 . 114 ASP CA C 52.900 0.25 1 1076 . 114 ASP CB C 44.255 0.25 1 1077 . 114 ASP N N 125.893 0.20 1 1078 . 115 GLN H H 8.689 0.03 1 1079 . 115 GLN HA H 4.016 0.03 1 1080 . 115 GLN HB2 H 2.077 0.03 1 1081 . 115 GLN HB3 H 2.077 0.03 1 1082 . 115 GLN HG2 H 2.418 0.03 1 1083 . 115 GLN HG3 H 2.418 0.03 1 1084 . 115 GLN C C 176.023 0.25 1 1085 . 115 GLN CA C 58.100 0.25 1 1086 . 115 GLN CB C 28.655 0.25 1 1087 . 115 GLN CG C 33.609 0.25 1 1088 . 115 GLN N N 121.903 0.20 1 1089 . 116 ASN H H 8.339 0.03 1 1090 . 116 ASN HA H 4.780 0.03 1 1091 . 116 ASN HB2 H 2.790 0.03 1 1092 . 116 ASN HB3 H 2.790 0.03 1 1093 . 116 ASN C C 175.771 0.25 1 1094 . 116 ASN CA C 54.275 0.25 1 1095 . 116 ASN CB C 39.645 0.25 1 1096 . 116 ASN N N 115.894 0.20 1 1097 . 117 GLN H H 8.513 0.03 1 1098 . 117 GLN HA H 4.200 0.03 1 1099 . 117 GLN HB2 H 1.786 0.03 2 1100 . 117 GLN HB3 H 2.057 0.03 2 1101 . 117 GLN HG2 H 2.237 0.03 1 1102 . 117 GLN HG3 H 2.237 0.03 1 1103 . 117 GLN C C 175.645 0.25 1 1104 . 117 GLN CA C 56.695 0.25 1 1105 . 117 GLN CB C 30.175 0.25 1 1106 . 117 GLN CG C 34.074 0.25 1 1107 . 117 GLN N N 116.629 0.20 1 1108 . 118 GLY H H 8.458 0.03 1 1109 . 118 GLY HA2 H 3.571 0.03 2 1110 . 118 GLY HA3 H 4.040 0.03 2 1111 . 118 GLY C C 173.494 0.25 1 1112 . 118 GLY CA C 44.690 0.25 1 1113 . 118 GLY N N 110.074 0.20 1 1114 . 119 GLU H H 8.570 0.03 1 1115 . 119 GLU HA H 4.568 0.03 1 1116 . 119 GLU HB2 H 1.860 0.03 2 1117 . 119 GLU HB3 H 1.990 0.03 2 1118 . 119 GLU HG2 H 2.360 0.03 1 1119 . 119 GLU HG3 H 2.360 0.03 1 1120 . 119 GLU C C 176.326 0.25 1 1121 . 119 GLU CA C 57.155 0.25 1 1122 . 119 GLU CB C 30.075 0.25 1 1123 . 119 GLU CG C 36.401 0.25 1 1124 . 119 GLU N N 122.851 0.20 1 1125 . 120 VAL H H 8.377 0.03 1 1126 . 120 VAL HA H 4.460 0.03 1 1127 . 120 VAL HB H 2.000 0.03 1 1128 . 120 VAL HG1 H 0.700 0.03 2 1129 . 120 VAL HG2 H 0.780 0.03 2 1130 . 120 VAL CA C 60.060 0.25 1 1131 . 120 VAL CB C 32.990 0.25 1 1132 . 120 VAL CG1 C 19.500 0.25 2 1133 . 120 VAL CG2 C 21.400 0.25 2 1134 . 120 VAL N N 118.702 0.20 1 1135 . 121 VAL H H 8.360 0.03 1 1136 . 121 VAL HA H 4.635 0.03 1 1137 . 121 VAL HB H 1.672 0.03 1 1138 . 121 VAL HG1 H 0.820 0.03 2 1139 . 121 VAL HG2 H 0.300 0.03 2 1140 . 121 VAL C C 174.562 0.25 1 1141 . 121 VAL CA C 60.860 0.25 1 1142 . 121 VAL CB C 33.480 0.25 1 1143 . 121 VAL CG1 C 22.700 0.25 2 1144 . 121 VAL CG2 C 22.500 0.25 2 1145 . 121 VAL N N 121.100 0.20 1 1146 . 122 LYS H H 8.862 0.03 1 1147 . 122 LYS HA H 4.357 0.03 1 1148 . 122 LYS HB2 H 1.520 0.03 2 1149 . 122 LYS HB3 H 1.610 0.03 2 1150 . 122 LYS HG2 H 1.289 0.03 2 1151 . 122 LYS HG3 H 1.413 0.03 2 1152 . 122 LYS HD2 H 1.421 0.03 2 1153 . 122 LYS HD3 H 1.683 0.03 2 1154 . 122 LYS HE2 H 2.811 0.03 2 1155 . 122 LYS HE3 H 2.959 0.03 2 1156 . 122 LYS C C 174.108 0.25 1 1157 . 122 LYS CA C 53.925 0.25 1 1158 . 122 LYS CB C 35.355 0.25 1 1159 . 122 LYS CG C 26.281 0.25 1 1160 . 122 LYS CD C 28.956 0.25 1 1161 . 122 LYS CE C 42.565 0.25 1 1162 . 122 LYS N N 127.468 0.20 1 1163 . 123 HIS H H 8.176 0.03 1 1164 . 123 HIS HA H 5.565 0.03 1 1165 . 123 HIS HB2 H 2.650 0.03 2 1166 . 123 HIS HB3 H 2.720 0.03 2 1167 . 123 HIS C C 175.393 0.25 1 1168 . 123 HIS CA C 54.265 0.25 1 1169 . 123 HIS CB C 33.780 0.25 1 1170 . 123 HIS N N 118.799 0.20 1 1171 . 124 TYR H H 9.873 0.03 1 1172 . 124 TYR HA H 4.743 0.03 1 1173 . 124 TYR HB2 H 2.870 0.03 2 1174 . 124 TYR HB3 H 2.776 0.03 2 1175 . 124 TYR C C 175.166 0.25 1 1176 . 124 TYR CA C 56.850 0.25 1 1177 . 124 TYR CB C 41.375 0.25 1 1178 . 124 TYR N N 121.750 0.20 1 1179 . 125 LYS H H 8.929 0.03 1 1180 . 125 LYS HA H 4.420 0.03 1 1181 . 125 LYS HB2 H 1.810 0.03 1 1182 . 125 LYS HB3 H 1.810 0.03 1 1183 . 125 LYS HG2 H 1.430 0.03 2 1184 . 125 LYS HG3 H 1.477 0.03 2 1185 . 125 LYS HD2 H 1.740 0.03 1 1186 . 125 LYS HD3 H 1.740 0.03 1 1187 . 125 LYS HE2 H 3.043 0.03 1 1188 . 125 LYS HE3 H 3.043 0.03 1 1189 . 125 LYS C C 175.696 0.25 1 1190 . 125 LYS CA C 56.735 0.25 1 1191 . 125 LYS CB C 32.510 0.25 1 1192 . 125 LYS CG C 24.885 0.25 1 1193 . 125 LYS CD C 28.840 0.25 1 1194 . 125 LYS CE C 42.100 0.25 1 1195 . 125 LYS N N 125.367 0.20 1 1196 . 126 ILE H H 8.442 0.03 1 1197 . 126 ILE HA H 4.250 0.03 1 1198 . 126 ILE HB H 1.942 0.03 1 1199 . 126 ILE HG13 H 1.720 0.03 2 1200 . 126 ILE HG2 H 0.990 0.03 1 1201 . 126 ILE HD1 H 0.731 0.03 1 1202 . 126 ILE C C 175.998 0.25 1 1203 . 126 ILE CA C 61.160 0.25 1 1204 . 126 ILE CB C 37.590 0.25 1 1205 . 126 ILE CG2 C 19.400 0.25 1 1206 . 126 ILE CD1 C 14.900 0.25 1 1207 . 126 ILE N N 126.549 0.20 1 1208 . 127 ARG H H 9.112 0.03 1 1209 . 127 ARG HA H 4.400 0.03 1 1210 . 127 ARG HB2 H 1.392 0.03 2 1211 . 127 ARG HB3 H 1.390 0.03 2 1212 . 127 ARG HG2 H 1.486 0.03 1 1213 . 127 ARG HG3 H 1.486 0.03 1 1214 . 127 ARG HD2 H 2.961 0.03 1 1215 . 127 ARG HD3 H 2.961 0.03 1 1216 . 127 ARG C C 174.612 0.25 1 1217 . 127 ARG CA C 54.740 0.25 1 1218 . 127 ARG CB C 30.700 0.25 1 1219 . 127 ARG CG C 27.444 0.25 1 1220 . 127 ARG CD C 43.147 0.25 1 1221 . 127 ARG N N 130.078 0.20 1 1222 . 128 ASN H H 8.406 0.03 1 1223 . 128 ASN HA H 5.320 0.03 1 1224 . 128 ASN HB2 H 2.760 0.03 2 1225 . 128 ASN HB3 H 2.600 0.03 2 1226 . 128 ASN C C 176.223 0.25 1 1227 . 128 ASN CA C 52.345 0.25 1 1228 . 128 ASN CB C 40.335 0.25 1 1229 . 128 ASN N N 116.995 0.20 1 1230 . 129 LEU H H 8.127 0.03 1 1231 . 129 LEU HA H 4.610 0.03 1 1232 . 129 LEU HB2 H 1.560 0.03 2 1233 . 129 LEU HB3 H 1.400 0.03 2 1234 . 129 LEU HG H 1.564 0.03 1 1235 . 129 LEU C C 178.518 0.25 1 1236 . 129 LEU CA C 53.660 0.25 1 1237 . 129 LEU CB C 43.730 0.25 1 1238 . 129 LEU N N 123.347 0.20 1 1239 . 130 ASP H H 8.853 0.03 1 1240 . 130 ASP HA H 4.314 0.03 1 1241 . 130 ASP HB2 H 2.671 0.03 1 1242 . 130 ASP HB3 H 2.671 0.03 1 1243 . 130 ASP C C 176.830 0.25 1 1244 . 130 ASP CA C 56.965 0.25 1 1245 . 130 ASP CB C 40.165 0.25 1 1246 . 130 ASP N N 123.612 0.20 1 1247 . 131 ASN H H 8.028 0.03 1 1248 . 131 ASN HA H 4.646 0.03 1 1249 . 131 ASN HB2 H 2.868 0.03 2 1250 . 131 ASN HB3 H 3.044 0.03 2 1251 . 131 ASN C C 175.544 0.25 1 1252 . 131 ASN CA C 53.025 0.25 1 1253 . 131 ASN CB C 37.675 0.25 1 1254 . 131 ASN N N 114.561 0.20 1 1255 . 132 GLY H H 7.716 0.03 1 1256 . 132 GLY HA2 H 3.675 0.03 2 1257 . 132 GLY HA3 H 4.331 0.03 2 1258 . 132 GLY C C 173.710 0.25 1 1259 . 132 GLY CA C 45.065 0.25 1 1260 . 132 GLY N N 108.043 0.20 1 1261 . 133 GLY H H 7.744 0.03 1 1262 . 133 GLY HA2 H 4.080 0.03 2 1263 . 133 GLY HA3 H 4.200 0.03 2 1264 . 133 GLY C C 173.201 0.25 1 1265 . 133 GLY CA C 44.535 0.25 1 1266 . 133 GLY N N 108.216 0.20 1 1267 . 134 PHE H H 9.163 0.03 1 1268 . 134 PHE HA H 5.928 0.03 1 1269 . 134 PHE HB2 H 2.467 0.03 2 1270 . 134 PHE HB3 H 3.087 0.03 2 1271 . 134 PHE C C 175.923 0.25 1 1272 . 134 PHE CA C 57.115 0.25 1 1273 . 134 PHE CB C 45.795 0.25 1 1274 . 134 PHE N N 116.411 0.20 1 1275 . 135 TYR H H 8.947 0.03 1 1276 . 135 TYR HA H 5.134 0.03 1 1277 . 135 TYR HB2 H 3.356 0.03 1 1278 . 135 TYR HB3 H 3.356 0.03 1 1279 . 135 TYR C C 172.268 0.25 1 1280 . 135 TYR CA C 58.295 0.25 1 1281 . 135 TYR CB C 40.815 0.25 1 1282 . 135 TYR N N 114.501 0.20 1 1283 . 136 ILE H H 9.864 0.03 1 1284 . 136 ILE HA H 4.474 0.03 1 1285 . 136 ILE HB H 1.727 0.03 1 1286 . 136 ILE HG12 H 1.720 0.03 2 1287 . 136 ILE HG13 H 1.050 0.03 2 1288 . 136 ILE HG2 H 0.910 0.03 1 1289 . 136 ILE HD1 H 0.430 0.03 1 1290 . 136 ILE C C 176.779 0.25 1 1291 . 136 ILE CA C 63.750 0.25 1 1292 . 136 ILE CB C 40.305 0.25 1 1293 . 136 ILE CG1 C 29.654 0.25 1 1294 . 136 ILE CG2 C 17.000 0.25 1 1295 . 136 ILE CD1 C 14.200 0.25 1 1296 . 136 ILE N N 119.890 0.20 1 1297 . 137 SER H H 9.348 0.03 1 1298 . 137 SER HA H 4.760 0.03 1 1299 . 137 SER HB2 H 3.880 0.03 1 1300 . 137 SER HB3 H 3.880 0.03 1 1301 . 137 SER CA C 54.170 0.25 1 1302 . 137 SER CB C 63.7 0.25 1 1303 . 137 SER N N 117.681 0.20 1 1304 . 138 PRO HA H 4.214 0.03 1 1305 . 138 PRO HB2 H 1.777 0.03 2 1306 . 138 PRO HB3 H 1.931 0.03 2 1307 . 138 PRO C C 175.861 0.25 1 1308 . 138 PRO CA C 64.190 0.25 1 1309 . 138 PRO CB C 31.570 0.25 1 1310 . 138 PRO CG C 27.560 0.25 1 1311 . 138 PRO CD C 50.591 0.25 1 1312 . 139 ARG H H 7.541 0.03 1 1313 . 139 ARG HA H 3.989 0.03 1 1314 . 139 ARG HB2 H 1.760 0.03 1 1315 . 139 ARG HB3 H 1.760 0.03 1 1316 . 139 ARG HG2 H 1.593 0.03 1 1317 . 139 ARG HG3 H 1.593 0.03 1 1318 . 139 ARG HD2 H 3.107 0.03 1 1319 . 139 ARG HD3 H 3.107 0.03 1 1320 . 139 ARG C C 175.948 0.25 1 1321 . 139 ARG CA C 57.495 0.25 1 1322 . 139 ARG CB C 30.675 0.25 1 1323 . 139 ARG CG C 27.560 0.25 1 1324 . 139 ARG CD C 43.031 0.25 1 1325 . 139 ARG N N 114.809 0.20 1 1326 . 140 ILE H H 7.642 0.03 1 1327 . 140 ILE HA H 4.202 0.03 1 1328 . 140 ILE HB H 1.621 0.03 1 1329 . 140 ILE HG13 H 1.110 0.03 2 1330 . 140 ILE HG2 H 0.550 0.03 1 1331 . 140 ILE HD1 H 0.610 0.03 1 1332 . 140 ILE C C 175.858 0.25 1 1333 . 140 ILE CA C 60.445 0.25 1 1334 . 140 ILE CB C 39.530 0.25 1 1335 . 140 ILE CG1 C 27.444 0.25 1 1336 . 140 ILE CG2 C 16.743 0.25 1 1337 . 140 ILE CD1 C 13.900 0.25 1 1338 . 140 ILE N N 118.742 0.20 1 1339 . 141 THR H H 7.543 0.03 1 1340 . 141 THR HA H 4.921 0.03 1 1341 . 141 THR HB H 4.025 0.03 1 1342 . 141 THR HG2 H 0.827 0.03 1 1343 . 141 THR C C 172.772 0.25 1 1344 . 141 THR CA C 58.815 0.25 1 1345 . 141 THR CB C 71.035 0.25 1 1346 . 141 THR N N 114.895 0.20 1 1347 . 142 PHE H H 9.037 0.03 1 1348 . 142 PHE HA H 5.210 0.03 1 1349 . 142 PHE HB2 H 2.760 0.03 2 1350 . 142 PHE HB3 H 3.440 0.03 2 1351 . 142 PHE CA C 55.090 0.25 1 1352 . 142 PHE CB C 43.700 0.25 1 1353 . 142 PHE N N 115.675 0.20 1 1354 . 143 PRO HA H 4.710 0.03 1 1355 . 143 PRO HB2 H 2.050 0.03 2 1356 . 143 PRO HB3 H 2.351 0.03 2 1357 . 143 PRO C C 175.872 0.25 1 1358 . 143 PRO CA C 63.750 0.25 1 1359 . 143 PRO CB C 32.020 0.25 1 1360 . 143 PRO CG C 27.560 0.25 1 1361 . 144 GLY H H 7.097 0.03 1 1362 . 144 GLY HA2 H 4.395 0.03 2 1363 . 144 GLY HA3 H 4.635 0.03 2 1364 . 144 GLY C C 172.744 0.25 1 1365 . 144 GLY CA C 45.080 0.25 1 1366 . 144 GLY N N 103.086 0.20 1 1367 . 145 LEU H H 8.841 0.03 1 1368 . 145 LEU HA H 4.310 0.03 1 1369 . 145 LEU HB2 H 1.588 0.03 2 1370 . 145 LEU HB3 H 1.646 0.03 2 1371 . 145 LEU HD1 H -0.010 0.03 2 1372 . 145 LEU HD2 H -0.040 0.03 2 1373 . 145 LEU C C 178.656 0.25 1 1374 . 145 LEU CA C 56.850 0.25 1 1375 . 145 LEU CB C 41.915 0.25 1 1376 . 145 LEU CD1 C 22.300 0.25 2 1377 . 145 LEU CD2 C 24.500 0.25 2 1378 . 145 LEU N N 119.485 0.20 1 1379 . 146 HIS H H 8.948 0.03 1 1380 . 146 HIS HA H 4.016 0.03 1 1381 . 146 HIS HB2 H 3.170 0.03 1 1382 . 146 HIS HB3 H 3.170 0.03 1 1383 . 146 HIS C C 178.216 0.25 1 1384 . 146 HIS CA C 61.010 0.25 1 1385 . 146 HIS CB C 29.195 0.25 1 1386 . 146 HIS N N 118.343 0.20 1 1387 . 147 GLU H H 9.287 0.03 1 1388 . 147 GLU HA H 3.841 0.03 1 1389 . 147 GLU HB2 H 2.332 0.03 1 1390 . 147 GLU HB3 H 2.332 0.03 1 1391 . 147 GLU HG2 H 2.753 0.03 1 1392 . 147 GLU HG3 H 2.753 0.03 1 1393 . 147 GLU C C 177.989 0.25 1 1394 . 147 GLU CA C 61.125 0.25 1 1395 . 147 GLU CB C 29.040 0.25 1 1396 . 147 GLU CG C 38.145 0.25 1 1397 . 147 GLU N N 120.008 0.20 1 1398 . 148 LEU H H 6.932 0.03 1 1399 . 148 LEU HA H 1.930 0.03 1 1400 . 148 LEU HB2 H 1.130 0.03 2 1401 . 148 LEU HB3 H 1.630 0.03 2 1402 . 148 LEU HG H 0.890 0.03 1 1403 . 148 LEU HD1 H 0.490 0.03 2 1404 . 148 LEU HD2 H 0.870 0.03 2 1405 . 148 LEU C C 177.309 0.25 1 1406 . 148 LEU CA C 58.915 0.25 1 1407 . 148 LEU CB C 42.055 0.25 1 1408 . 148 LEU CG C 28.026 0.25 1 1409 . 148 LEU CD1 C 23.900 0.25 2 1410 . 148 LEU CD2 C 27.800 0.25 2 1411 . 148 LEU N N 123.834 0.20 1 1412 . 149 VAL H H 7.862 0.03 1 1413 . 149 VAL HA H 2.770 0.03 1 1414 . 149 VAL HB H 1.420 0.03 1 1415 . 149 VAL HG1 H -0.430 0.03 2 1416 . 149 VAL HG2 H 0.200 0.03 2 1417 . 149 VAL C C 178.796 0.25 1 1418 . 149 VAL CA C 66.710 0.25 1 1419 . 149 VAL CB C 31.225 0.25 1 1420 . 149 VAL CG1 C 22.600 0.25 2 1421 . 149 VAL CG2 C 21.200 0.25 2 1422 . 149 VAL N N 119.451 0.20 1 1423 . 150 ARG H H 7.894 0.03 1 1424 . 150 ARG HA H 4.050 0.03 1 1425 . 150 ARG HB2 H 0.980 0.03 2 1426 . 150 ARG HB3 H 1.910 0.03 2 1427 . 150 ARG HD2 H 3.223 0.03 1 1428 . 150 ARG HD3 H 3.223 0.03 1 1429 . 150 ARG C C 178.558 0.25 1 1430 . 150 ARG CA C 59.490 0.25 1 1431 . 150 ARG CB C 30.145 0.25 1 1432 . 150 ARG CG C 27.222 0.25 1 1433 . 150 ARG CD C 43.223 0.25 1 1434 . 150 ARG N N 120.311 0.20 1 1435 . 151 HIS H H 7.710 0.03 1 1436 . 151 HIS HA H 4.060 0.03 1 1437 . 151 HIS HB2 H 2.804 0.03 2 1438 . 151 HIS HB3 H 3.046 0.03 2 1439 . 151 HIS C C 178.040 0.25 1 1440 . 151 HIS CA C 60.545 0.25 1 1441 . 151 HIS CB C 31.275 0.25 1 1442 . 151 HIS N N 117.874 0.20 1 1443 . 152 TYR H H 7.505 0.03 1 1444 . 152 TYR HA H 5.145 0.03 1 1445 . 152 TYR HB2 H 2.222 0.03 2 1446 . 152 TYR HB3 H 3.124 0.03 2 1447 . 152 TYR C C 176.134 0.25 1 1448 . 152 TYR CA C 60.300 0.25 1 1449 . 152 TYR CB C 37.645 0.25 1 1450 . 152 TYR N N 115.456 0.20 1 1451 . 153 THR H H 7.510 0.03 1 1452 . 153 THR HA H 4.703 0.03 1 1453 . 153 THR HB H 4.151 0.03 1 1454 . 153 THR HG2 H 1.138 0.03 1 1455 . 153 THR C C 175.242 0.25 1 1456 . 153 THR CA C 64.325 0.25 1 1457 . 153 THR CB C 69.390 0.25 1 1458 . 153 THR N N 114.900 0.20 1 1459 . 154 ASN H H 7.125 0.03 1 1460 . 154 ASN HA H 4.595 0.03 1 1461 . 154 ASN HB2 H 2.710 0.03 1 1462 . 154 ASN HB3 H 2.710 0.03 1 1463 . 154 ASN C C 175.025 0.25 1 1464 . 154 ASN CA C 54.855 0.25 1 1465 . 154 ASN CB C 39.955 0.25 1 1466 . 154 ASN N N 119.496 0.20 1 1467 . 155 ALA H H 7.749 0.03 1 1468 . 155 ALA HA H 4.311 0.03 1 1469 . 155 ALA HB H 1.091 0.03 1 1470 . 155 ALA C C 174.108 0.25 1 1471 . 155 ALA CA C 51.615 0.25 1 1472 . 155 ALA CB C 21.260 0.25 1 1473 . 155 ALA N N 121.744 0.20 1 1474 . 156 SER H H 8.485 0.03 1 1475 . 156 SER HA H 3.970 0.03 1 1476 . 156 SER HB2 H 3.670 0.03 1 1477 . 156 SER HB3 H 3.670 0.03 1 1478 . 156 SER C C 175.267 0.25 1 1479 . 156 SER CA C 60.890 0.25 1 1480 . 156 SER CB C 61.475 0.25 1 1481 . 156 SER N N 114.714 0.20 1 1482 . 157 ASP H H 8.284 0.03 1 1483 . 157 ASP HA H 4.420 0.03 1 1484 . 157 ASP HB2 H 2.252 0.03 2 1485 . 157 ASP HB3 H 3.167 0.03 2 1486 . 157 ASP C C 175.343 0.25 1 1487 . 157 ASP CA C 54.560 0.25 1 1488 . 157 ASP CB C 41.225 0.25 1 1489 . 157 ASP N N 118.926 0.20 1 1490 . 158 GLY H H 8.599 0.03 1 1491 . 158 GLY HA2 H 3.663 0.03 2 1492 . 158 GLY HA3 H 4.517 0.03 2 1493 . 158 GLY C C 176.074 0.25 1 1494 . 158 GLY CA C 45.170 0.25 1 1495 . 158 GLY N N 106.222 0.20 1 1496 . 159 LEU H H 8.346 0.03 1 1497 . 159 LEU HA H 4.110 0.03 1 1498 . 159 LEU HB2 H 1.130 0.03 2 1499 . 159 LEU HB3 H 1.790 0.03 2 1500 . 159 LEU HG H 1.390 0.03 1 1501 . 159 LEU HD1 H -0.290 0.03 2 1502 . 159 LEU HD2 H -0.130 0.03 2 1503 . 159 LEU C C 177.409 0.25 1 1504 . 159 LEU CA C 54.490 0.25 1 1505 . 159 LEU CB C 42.560 0.25 1 1506 . 159 LEU CD1 C 20.500 0.25 2 1507 . 159 LEU CD2 C 24.900 0.25 2 1508 . 159 LEU N N 121.070 0.20 1 1509 . 160 CYS H H 7.489 0.03 1 1510 . 160 CYS HA H 4.272 0.03 1 1511 . 160 CYS HB2 H 2.898 0.03 2 1512 . 160 CYS HB3 H 3.302 0.03 2 1513 . 160 CYS C C 173.402 0.25 1 1514 . 160 CYS CA C 58.590 0.25 1 1515 . 160 CYS CB C 28.105 0.25 1 1516 . 160 CYS N N 115.890 0.20 1 1517 . 161 THR H H 7.193 0.03 1 1518 . 161 THR HA H 4.366 0.03 1 1519 . 161 THR HB H 4.245 0.03 1 1520 . 161 THR HG2 H 0.924 0.03 1 1521 . 161 THR C C 170.907 0.25 1 1522 . 161 THR CA C 60.120 0.25 1 1523 . 161 THR CB C 69.080 0.25 1 1524 . 161 THR N N 114.251 0.20 1 1525 . 162 ARG H H 7.430 0.03 1 1526 . 162 ARG HA H 4.124 0.03 1 1527 . 162 ARG HB2 H 1.646 0.03 1 1528 . 162 ARG HB3 H 1.646 0.03 1 1529 . 162 ARG HG2 H 2.116 0.03 2 1530 . 162 ARG HG3 H 2.212 0.03 2 1531 . 162 ARG HD2 H 3.001 0.03 2 1532 . 162 ARG HD3 H 3.267 0.03 2 1533 . 162 ARG C C 176.578 0.25 1 1534 . 162 ARG CA C 56.230 0.25 1 1535 . 162 ARG CB C 31.465 0.25 1 1536 . 162 ARG CG C 27.677 0.25 1 1537 . 162 ARG CD C 43.496 0.25 1 1538 . 162 ARG N N 120.037 0.20 1 1539 . 163 LEU H H 7.944 0.03 1 1540 . 163 LEU HA H 4.020 0.03 1 1541 . 163 LEU HD1 H 0.230 0.03 2 1542 . 163 LEU HD2 H -0.210 0.03 2 1543 . 163 LEU C C 176.578 0.25 1 1544 . 163 LEU CA C 54.780 0.25 1 1545 . 163 LEU CB C 38.735 0.25 1 1546 . 163 LEU CD1 C 21.500 0.25 2 1547 . 163 LEU CD2 C 24.600 0.25 2 1548 . 163 LEU N N 122.939 0.20 1 1549 . 164 SER H H 8.682 0.03 1 1550 . 164 SER HA H 4.703 0.03 1 1551 . 164 SER HB2 H 3.830 0.03 2 1552 . 164 SER HB3 H 3.910 0.03 2 1553 . 164 SER C C 174.889 0.25 1 1554 . 164 SER CA C 57.350 0.25 1 1555 . 164 SER CB C 64.190 0.25 1 1556 . 164 SER N N 116.537 0.20 1 1557 . 165 ARG H H 7.797 0.03 1 1558 . 165 ARG HA H 4.990 0.03 1 1559 . 165 ARG HB2 H 1.720 0.03 2 1560 . 165 ARG HB3 H 1.910 0.03 2 1561 . 165 ARG CA C 53.560 0.25 1 1562 . 165 ARG CB C 31.800 0.25 1 1563 . 165 ARG N N 120.448 0.20 1 1564 . 166 PRO HA H 3.730 0.03 1 1565 . 166 PRO HB2 H 1.800 0.03 1 1566 . 166 PRO HB3 H 1.800 0.03 1 1567 . 166 PRO HG2 H 1.713 0.03 1 1568 . 166 PRO HG3 H 1.713 0.03 1 1569 . 166 PRO HD2 H 3.480 0.03 1 1570 . 166 PRO HD3 H 3.480 0.03 1 1571 . 166 PRO C C 177.258 0.25 1 1572 . 166 PRO CA C 62.240 0.25 1 1573 . 166 PRO CB C 31.970 0.25 1 1574 . 166 PRO CG C 28.491 0.25 1 1575 . 166 PRO CD C 50.708 0.25 1 1576 . 167 CYS H H 8.673 0.03 1 1577 . 167 CYS HA H 3.895 0.03 1 1578 . 167 CYS HB2 H 2.050 0.03 2 1579 . 167 CYS HB3 H 2.656 0.03 2 1580 . 167 CYS C C 172.066 0.25 1 1581 . 167 CYS CA C 60.090 0.25 1 1582 . 167 CYS CB C 28.615 0.25 1 1583 . 167 CYS N N 124.400 0.20 1 1584 . 168 GLN H H 9.126 0.03 1 1585 . 168 GLN HA H 4.530 0.03 1 1586 . 168 GLN HB2 H 1.996 0.03 2 1587 . 168 GLN HB3 H 2.144 0.03 2 1588 . 168 GLN HG2 H 2.370 0.03 1 1589 . 168 GLN HG3 H 2.370 0.03 1 1590 . 168 GLN C C 175.862 0.25 1 1591 . 168 GLN CA C 55.965 0.25 1 1592 . 168 GLN CB C 30.090 0.25 1 1593 . 168 GLN CG C 33.842 0.25 1 1594 . 168 GLN N N 129.222 0.20 1 1595 . 169 THR H H 8.113 0.03 1 1596 . 169 THR HA H 4.200 0.03 1 1597 . 169 THR HB H 4.300 0.03 1 1598 . 169 THR HG2 H 1.180 0.03 1 1599 . 169 THR CA C 63.160 0.25 1 1600 . 169 THR CB C 70.790 0.25 1 1601 . 169 THR N N 121.478 0.20 1 stop_ save_