data_4081 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N NMR Assignments of Recombinant Human Interferon Alpha-2a ; _BMRB_accession_number 4081 _BMRB_flat_file_name bmr4081.str _Entry_type original _Submission_date 1997-12-15 _Accession_date 1997-12-23 _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 Werner Klaus . . 2 Grzesiek Stephan S. . 3 Labhardt Alexander M. . 4 Senn Hans . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1003 "13C chemical shifts" 724 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-03-20 original author . stop_ _Original_release_date 1998-03-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Werner, K., Gsell, B., Labhardt, A. M., Wipf, B., and Senn, H., "The Three-dimensional High Resolution Structure of Human Interferon alpha-2a Determined by Hetero-nuclear NMR Spectroscopy in Solution," J. Mol. Biol. 274, 661-675 (1997). ; _Citation_title ; The Three-dimensional High Resolution Structure of Human Interferon alpha-2a Determined by Hetero-nuclear NMR Spectroscopy in Solution ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98118493 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Werner Klaus . . 2 Gsell Bernard . . 3 Labhardt Alexander M. . 4 Wipf Beat . . 5 Senn Hans . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 274 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 661 _Page_last 675 _Year 1997 _Details . loop_ _Keyword cytokine 'interferon alpha' 'NMR assignments' 'protein structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'J. Mol. Biol. , vol. 274(4), 661-675"' _Citation_title 'The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9417943 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Klaus W . . 2 Gsell B . . 3 Labhardt 'A M' M. . 4 Wipf B . . 5 Senn H . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 274 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 661 _Page_last 675 _Year 1997 _Details ; The solution structure of recombinant human interferon alpha-2a (Roferon-A) has been determined by multidimensional heteronuclear NMR spectroscopy. The calculations using simulated annealing produced a family of 24 convergent structures which satisfy the experimental restraints comprising 1541 NOE-derived inter-proton distances, 187 dihedral restraints, 66 pairs of hydrogen bond restraints, and six upper and lower limits for two disulfide bridges. The fractional labeling of methyl groups allowed their direct and unambiguous stereospecific assignment which proved to be essential for obtaining a high resolution of the structures. A best fit superposition of residues 10 to 47, 50 to 101 and 111 to 157 gives an rms deviation of 0.62 A for the backbone heavy atoms and 1.39 A for all heavy atoms of these segments. The dominant feature of the structure is a cluster of five alpha-helices, four of which are arranged to form a left-handed helix bundle with an up-up-down-down topology and two over-hand connections. The interpretation of heteronuclear 15N-1H NOE data shows the co-existence of flexible regions within an otherwise rigid framework of the protein. Four stretches of pronounced flexibility can be located: Cys1-Ser8, Gly44-Ala50, Ile100-Lys112, and Ser160-Glu165. Among the structurally related four-helical bundle cytokines, the structure of IFN alpha-2a is most similar to that of human interferon alpha-2b and murine interferon-beta. From this structural information and mutagenesis data, areas on the surface of the protein are identified which seem to be important in receptor interactions. ; save_ save_citation_two _Saveframe_category citation _Citation_full 'J. Biomol. NMR 6, 135-140 (1995).' _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_INF-alpha-2a _Saveframe_category molecular_system _Mol_system_name Interferon-alpha-2a _Abbreviation_common INF-alpha-2a _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label INF-alpha-2a $INF-alpha-2a stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function cytokine stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_INF-alpha-2a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Interferon_alpha-2a _Abbreviation_common INFA _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; CDLPQTHSLGSRRTLMLLAQ MRKISLFSCLKDRHDFGFPQ EEFGNQFQKAETIPVLHEMI QQIFNLFSTKDSSAAWDETL LDKFYTELYQQLNDLEACVI QGVGVTETPLMKEDSILAVR KYFQRITLYLKEKKYSPCAW EVVRAEIMRSFSLSTNLQES LRSKE ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 ASP 3 LEU 4 PRO 5 GLN 6 THR 7 HIS 8 SER 9 LEU 10 GLY 11 SER 12 ARG 13 ARG 14 THR 15 LEU 16 MET 17 LEU 18 LEU 19 ALA 20 GLN 21 MET 22 ARG 23 LYS 24 ILE 25 SER 26 LEU 27 PHE 28 SER 29 CYS 30 LEU 31 LYS 32 ASP 33 ARG 34 HIS 35 ASP 36 PHE 37 GLY 38 PHE 39 PRO 40 GLN 41 GLU 42 GLU 43 PHE 44 GLY 45 ASN 46 GLN 47 PHE 48 GLN 49 LYS 50 ALA 51 GLU 52 THR 53 ILE 54 PRO 55 VAL 56 LEU 57 HIS 58 GLU 59 MET 60 ILE 61 GLN 62 GLN 63 ILE 64 PHE 65 ASN 66 LEU 67 PHE 68 SER 69 THR 70 LYS 71 ASP 72 SER 73 SER 74 ALA 75 ALA 76 TRP 77 ASP 78 GLU 79 THR 80 LEU 81 LEU 82 ASP 83 LYS 84 PHE 85 TYR 86 THR 87 GLU 88 LEU 89 TYR 90 GLN 91 GLN 92 LEU 93 ASN 94 ASP 95 LEU 96 GLU 97 ALA 98 CYS 99 VAL 100 ILE 101 GLN 102 GLY 103 VAL 104 GLY 105 VAL 106 THR 107 GLU 108 THR 109 PRO 110 LEU 111 MET 112 LYS 113 GLU 114 ASP 115 SER 116 ILE 117 LEU 118 ALA 119 VAL 120 ARG 121 LYS 122 TYR 123 PHE 124 GLN 125 ARG 126 ILE 127 THR 128 LEU 129 TYR 130 LEU 131 LYS 132 GLU 133 LYS 134 LYS 135 TYR 136 SER 137 PRO 138 CYS 139 ALA 140 TRP 141 GLU 142 VAL 143 VAL 144 ARG 145 ALA 146 GLU 147 ILE 148 MET 149 ARG 150 SER 151 PHE 152 SER 153 LEU 154 SER 155 THR 156 ASN 157 LEU 158 GLN 159 GLU 160 SER 161 LEU 162 ARG 163 SER 164 LYS 165 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-28 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 BMRB 16677 entity_1 100.00 165 100.00 100.00 4.16e-118 BMRB 18135 Interferon_Alpha-2a 100.00 165 100.00 100.00 4.16e-118 BMRB 18344 ggIFN_alpha-2a 100.00 165 100.00 100.00 4.16e-118 PDB 1ITF "Interferon Alpha-2a, Nmr, 24 Structures" 100.00 165 100.00 100.00 4.16e-118 PDB 1RH2 "Recombinant Human Interferon-Alpha 2b" 100.00 165 98.79 99.39 5.03e-117 PDB 2HYM "Nmr Based Docking Model Of The Complex Between The Human Type I Interferon Receptor And Human Interferon Alpha-2" 100.00 165 100.00 100.00 4.16e-118 PDB 2KZ1 "Inter-Molecular Interactions In A 44 Kda Interferon-Receptor Complex Detected By Asymmetric Back-Protonation And 2d Noesy" 100.00 165 100.00 100.00 4.16e-118 PDB 2LAG "Structure Of The 44 Kda Complex Of Interferon-Alpha2 With The Extracellular Part Of Ifnar2 Obtained By 2d-Double Difference Noe" 100.00 165 100.00 100.00 4.16e-118 PDB 2LMS "A Single Galnac Residue On Threonine-106 Modifies The Dynamics And The Structure Of Interferon Alpha-2a Around The Glycosylatio" 100.00 166 100.00 100.00 3.99e-118 PDB 3S9D "Binary Complex Between Ifna2 And Ifnar2" 100.00 168 97.58 98.18 1.11e-114 PDB 3SE3 "Human Ifna2-ifnar Ternary Complex" 100.00 166 97.58 98.79 2.19e-115 PDB 4YPG "Structural Insights Into The Neutralization Properties Of A Human Anti-interferon Monoclonal Antibody" 96.36 161 100.00 100.00 5.22e-114 PDB 4Z5R "Rontalizumab Fab Bound To Interferon-a2" 100.00 165 100.00 100.00 4.16e-118 DBJ BAJ20902 "interferon, alpha 2 [synthetic construct]" 100.00 188 99.39 100.00 7.30e-118 EMBL CAA23805 "unnamed protein product [Homo sapiens]" 100.00 188 100.00 100.00 2.70e-118 EMBL CAA23809 "interferon alpha-2 precursor [Homo sapiens]" 100.00 182 99.39 100.00 1.07e-117 EMBL CAA23810 "unnamed protein product [Homo sapiens]" 100.00 188 100.00 100.00 2.70e-118 EMBL CAA25770 "unnamed protein product [synthetic construct]" 100.00 166 99.39 100.00 1.14e-117 EMBL CAA46954 "leukocytic interferon alpha-2 [synthetic construct]" 100.00 166 99.39 100.00 1.14e-117 GB AAA52715 "alpha 2 interferon, partial [Homo sapiens]" 100.00 165 99.39 100.00 1.12e-117 GB AAA59181 "interferon [Homo sapiens]" 100.00 188 100.00 100.00 2.70e-118 GB AAB59402 "interferon alpha-a [Homo sapiens]" 100.00 188 99.39 100.00 7.30e-118 GB AAC64915 "interferon alpha 2b- 44LQ [synthetic construct]" 100.00 165 98.18 98.79 4.30e-115 GB AAH74936 "Interferon, alpha 2 [Homo sapiens]" 100.00 188 99.39 100.00 7.30e-118 PRF 0611561A interferon 100.00 188 100.00 100.00 2.70e-118 PRF 0906342A "interferon C term modified" 93.33 164 100.00 100.00 9.81e-110 REF NP_000596 "interferon alpha-2 precursor [Homo sapiens]" 100.00 188 99.39 100.00 7.30e-118 REF XP_003830724 "PREDICTED: interferon alpha-2 [Pan paniscus]" 100.00 188 98.18 100.00 8.73e-117 REF XP_004047919 "PREDICTED: interferon alpha-2 [Gorilla gorilla gorilla]" 100.00 188 98.18 100.00 1.17e-116 REF XP_528568 "PREDICTED: interferon alpha-2 [Pan troglodytes]" 100.00 188 98.18 100.00 8.73e-117 SP P01563 "RecName: Full=Interferon alpha-2; Short=IFN-alpha-2; AltName: Full=Interferon alpha-A; Short=LeIF A; Flags: Precursor" 100.00 188 100.00 100.00 2.70e-118 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $INF-alpha-2a 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 $INF-alpha-2a 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $INF-alpha-2a 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMR-Pipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX500 _Field_strength 500 _Details . save_ save_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX2-500 _Field_strength 500 _Details . save_ save_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_HOHAHA_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-1H_HOHAHA _Sample_label $sample_one save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-1H_NOESY _Sample_label $sample_one save_ save_2D_1H-1H_CLEAN-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-1H_CLEAN-TOCSY _Sample_label $sample_one save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-13C_HSQC _Sample_label $sample_one save_ save_2D_1H-13C_CT-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-13C_CT-HSQC _Sample_label $sample_one save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-15N_HSQC _Sample_label $sample_one save_ save_Three-dimensional_experiments_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'Three-dimensional experiments' _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.2 . n/a temperature 298 0.1 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 DSS C 13 . ppm 0.00 . indirect . . . 0.251449 DSS H 1 . ppm 0.00 internal direct . . . . DSS N 15 . ppm 0.00 . indirect . . . 0.101329 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_INF-alpha-2a _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name INF-alpha-2a _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 CYS HA H 4.26 0.03 1 2 . 1 CYS HB2 H 3.31 0.03 2 3 . 1 CYS HB3 H 3.13 0.03 2 4 . 1 CYS C C 169.97 0.12 1 5 . 1 CYS CA C 54.97 0.12 1 6 . 1 CYS CB C 41.00 0.12 1 7 . 2 ASP H H 9.19 0.03 1 8 . 2 ASP HA H 4.82 0.03 1 9 . 2 ASP HB2 H 2.60 0.03 2 10 . 2 ASP HB3 H 2.57 0.03 2 11 . 2 ASP C C 174.50 0.12 1 12 . 2 ASP CA C 53.20 0.12 1 13 . 2 ASP CB C 40.65 0.12 1 14 . 2 ASP N N 127.74 0.15 1 15 . 3 LEU H H 8.38 0.03 1 16 . 3 LEU HA H 4.44 0.03 1 17 . 3 LEU HB2 H 1.62 0.03 2 18 . 3 LEU HB3 H 1.36 0.03 2 19 . 3 LEU HG H 1.66 0.03 1 20 . 3 LEU HD1 H 0.81 0.03 1 21 . 3 LEU HD2 H 0.80 0.03 1 22 . 3 LEU CA C 53.80 0.12 1 23 . 3 LEU CB C 41.40 0.12 1 24 . 3 LEU CG C 27.00 0.12 1 25 . 3 LEU CD1 C 25.45 0.12 1 26 . 3 LEU CD2 C 24.00 0.12 1 27 . 3 LEU N N 124.12 0.15 1 28 . 4 PRO HA H 4.41 0.03 1 29 . 4 PRO HB2 H 1.85 0.03 2 30 . 4 PRO HB3 H 2.33 0.03 2 31 . 4 PRO HG2 H 1.99 0.03 2 32 . 4 PRO HG3 H 1.99 0.03 2 33 . 4 PRO HD2 H 3.53 0.03 1 34 . 4 PRO HD3 H 3.83 0.03 1 35 . 4 PRO C C 177.69 0.12 1 36 . 4 PRO CA C 63.84 0.12 1 37 . 4 PRO CB C 31.96 0.12 1 38 . 4 PRO CG C 27.86 0.12 1 39 . 4 PRO CD C 50.55 0.12 1 40 . 5 GLN H H 8.74 0.03 1 41 . 5 GLN HA H 4.26 0.03 1 42 . 5 GLN HB2 H 2.13 0.03 2 43 . 5 GLN HB3 H 2.06 0.03 2 44 . 5 GLN HG2 H 2.41 0.03 2 45 . 5 GLN HG3 H 2.41 0.03 2 46 . 5 GLN C C 177.15 0.12 1 47 . 5 GLN CA C 57.50 0.12 1 48 . 5 GLN CB C 28.93 0.12 1 49 . 5 GLN CG C 33.71 0.12 1 50 . 5 GLN N N 119.62 0.15 1 51 . 6 THR H H 7.83 0.03 1 52 . 6 THR HA H 4.20 0.03 1 53 . 6 THR HB H 4.22 0.03 1 54 . 6 THR HG2 H 1.15 0.03 1 55 . 6 THR C C 175.49 0.12 1 56 . 6 THR CA C 62.74 0.12 1 57 . 6 THR CB C 69.17 0.12 1 58 . 6 THR CG2 C 22.03 0.12 1 59 . 6 THR N N 110.25 0.15 1 60 . 7 HIS H H 8.27 0.03 1 61 . 7 HIS HA H 4.68 0.03 1 62 . 7 HIS HB2 H 3.18 0.03 1 63 . 7 HIS HB3 H 3.40 0.03 1 64 . 7 HIS HD2 H 7.33 0.03 1 65 . 7 HIS HE1 H 8.55 0.03 1 66 . 7 HIS C C 175.41 0.12 1 67 . 7 HIS CA C 56.41 0.12 1 68 . 7 HIS CB C 28.40 0.12 1 69 . 7 HIS CD2 C 120.20 0.12 1 70 . 7 HIS CE1 C 136.00 0.12 1 71 . 7 HIS N N 119.48 0.15 0 72 . 8 SER H H 8.20 0.03 1 73 . 8 SER HA H 4.38 0.03 1 74 . 8 SER HB2 H 3.98 0.03 2 75 . 8 SER HB3 H 3.94 0.03 2 76 . 8 SER C C 175.71 0.12 1 77 . 8 SER CA C 59.66 0.12 1 78 . 8 SER CB C 63.62 0.12 1 79 . 8 SER N N 115.67 0.15 1 80 . 9 LEU H H 8.31 0.03 1 81 . 9 LEU HA H 4.18 0.03 1 82 . 9 LEU HB2 H 1.68 0.03 2 83 . 9 LEU HB3 H 1.63 0.03 2 84 . 9 LEU HG H 1.59 0.03 1 85 . 9 LEU HD1 H 0.91 0.03 1 86 . 9 LEU HD2 H 0.86 0.03 1 87 . 9 LEU C C 178.87 0.12 1 88 . 9 LEU CA C 57.32 0.12 1 89 . 9 LEU CB C 41.65 0.12 1 90 . 9 LEU CG C 27.07 0.12 1 91 . 9 LEU CD1 C 24.54 0.12 1 92 . 9 LEU CD2 C 24.01 0.12 1 93 . 9 LEU N N 123.48 0.15 1 94 . 10 GLY H H 8.36 0.03 1 95 . 10 GLY HA2 H 3.89 0.03 2 96 . 10 GLY HA3 H 3.93 0.03 2 97 . 10 GLY C C 176.85 0.12 1 98 . 10 GLY CA C 47.10 0.12 1 99 . 10 GLY N N 107.35 0.15 1 100 . 11 SER H H 8.28 0.03 1 101 . 11 SER HA H 4.28 0.03 1 102 . 11 SER HB2 H 3.96 0.03 2 103 . 11 SER HB3 H 3.96 0.03 2 104 . 11 SER C C 175.79 0.12 2 105 . 11 SER CA C 61.49 0.12 2 106 . 11 SER CB C 62.84 0.12 2 107 . 11 SER N N 119.31 0.15 2 108 . 12 ARG H H 7.95 0.03 1 109 . 12 ARG HA H 3.98 0.03 1 110 . 12 ARG HB2 H 1.94 0.03 2 111 . 12 ARG HB3 H 1.94 0.03 2 112 . 12 ARG HG2 H 1.68 0.03 2 113 . 12 ARG HG3 H 1.47 0.03 2 114 . 12 ARG HD2 H 3.15 0.03 2 115 . 12 ARG HD3 H 3.15 0.03 2 116 . 12 ARG C C 179.28 0.12 1 117 . 12 ARG CA C 59.82 0.12 1 118 . 12 ARG CB C 30.29 0.12 1 119 . 12 ARG CG C 27.94 0.12 1 120 . 12 ARG N N 121.66 0.15 1 121 . 13 ARG H H 8.49 0.03 1 122 . 13 ARG HA H 4.01 0.03 1 123 . 13 ARG HG2 H 1.40 0.03 2 124 . 13 ARG HG3 H 1.40 0.03 2 125 . 13 ARG HD2 H 3.15 0.03 2 126 . 13 ARG HD3 H 3.15 0.03 2 127 . 13 ARG C C 178.67 0.12 1 128 . 13 ARG CA C 59.79 0.12 1 129 . 13 ARG CB C 30.01 0.12 1 130 . 13 ARG CD C 43.44 0.12 1 131 . 14 THR H H 7.99 0.03 1 132 . 14 THR HA H 3.56 0.03 1 133 . 14 THR HB H 4.26 0.03 1 134 . 14 THR HG2 H 0.53 0.03 1 135 . 14 THR C C 175.65 0.12 1 136 . 14 THR CA C 68.29 0.12 1 137 . 14 THR CB C 67.89 0.12 1 138 . 14 THR CG2 C 21.35 0.12 1 139 . 14 THR N N 116.64 0.15 1 140 . 15 LEU H H 7.55 0.03 1 141 . 15 LEU HA H 3.89 0.03 1 142 . 15 LEU HB2 H 1.86 0.03 2 143 . 15 LEU HB3 H 1.51 0.03 2 144 . 15 LEU HG H 1.76 0.03 1 145 . 15 LEU HD1 H 0.91 0.03 1 146 . 15 LEU HD2 H 1.00 0.03 1 147 . 15 LEU C C 178.68 0.12 1 148 . 15 LEU CA C 58.13 0.12 1 149 . 15 LEU CB C 41.51 0.12 1 150 . 15 LEU CG C 27.55 0.12 1 151 . 15 LEU CD1 C 25.95 0.12 1 152 . 15 LEU CD2 C 25.06 0.12 1 153 . 15 LEU N N 119.99 0.15 1 154 . 16 MET H H 7.98 0.03 1 155 . 16 MET HA H 4.04 0.03 1 156 . 16 MET HB2 H 2.17 0.03 2 157 . 16 MET HB3 H 2.17 0.03 2 158 . 16 MET HG2 H 2.60 0.03 2 159 . 16 MET HG3 H 2.60 0.03 2 160 . 16 MET HE H 2.01 0.03 1 161 . 16 MET C C 178.80 0.12 1 162 . 16 MET CA C 58.64 0.12 1 163 . 16 MET CB C 32.35 0.12 1 164 . 16 MET CG C 31.83 0.12 1 165 . 16 MET CE C 16.94 0.12 1 166 . 16 MET N N 118.48 0.15 1 167 . 17 LEU H H 7.85 0.03 1 168 . 17 LEU HA H 3.91 0.03 1 169 . 17 LEU HB2 H 1.92 0.03 1 170 . 17 LEU HB3 H 0.93 0.03 1 171 . 17 LEU HG H 1.74 0.03 1 172 . 17 LEU HD1 H 0.78 0.03 1 173 . 17 LEU HD2 H 0.82 0.03 1 174 . 17 LEU C C 178.30 0.12 1 175 . 17 LEU CA C 57.94 0.12 1 176 . 17 LEU CB C 42.34 0.12 1 177 . 17 LEU CG C 23.45 0.12 1 178 . 17 LEU CD1 C 26.37 0.12 1 179 . 17 LEU CD2 C 25.13 0.12 1 180 . 17 LEU N N 120.51 0.15 1 181 . 18 LEU H H 7.51 0.03 1 182 . 18 LEU HA H 3.55 0.03 1 183 . 18 LEU HB2 H 1.63 0.03 1 184 . 18 LEU HB3 H 1.13 0.03 1 185 . 18 LEU HG H 1.14 0.03 1 186 . 18 LEU HD1 H 0.43 0.03 1 187 . 18 LEU HD2 H 0.21 0.03 1 188 . 18 LEU C C 180.31 0.12 1 189 . 18 LEU CA C 57.71 0.12 1 190 . 18 LEU CB C 42.37 0.12 1 191 . 18 LEU CG C 27.39 0.12 1 192 . 18 LEU CD1 C 25.43 0.12 1 193 . 18 LEU CD2 C 23.84 0.12 1 194 . 18 LEU N N 117.97 0.15 1 195 . 19 ALA H H 7.93 0.03 1 196 . 19 ALA HA H 3.89 0.03 1 197 . 19 ALA HB H 1.46 0.03 1 198 . 19 ALA C C 180.75 0.12 1 199 . 19 ALA CA C 55.37 0.12 1 200 . 19 ALA CB C 18.07 0.12 1 201 . 19 ALA N N 121.60 0.15 1 202 . 20 GLN H H 7.99 0.03 1 203 . 20 GLN HA H 3.94 0.03 1 204 . 20 GLN HB2 H 2.00 0.03 1 205 . 20 GLN HB3 H 2.17 0.03 1 206 . 20 GLN HG2 H 2.58 0.03 2 207 . 20 GLN HG3 H 2.34 0.03 2 208 . 20 GLN C C 177.03 0.12 1 209 . 20 GLN CA C 58.06 0.12 1 210 . 20 GLN CB C 29.11 0.12 1 211 . 20 GLN CG C 34.50 0.12 1 212 . 20 GLN N N 118.34 0.15 1 213 . 21 MET H H 7.45 0.03 1 214 . 21 MET HA H 3.89 0.03 1 215 . 21 MET HB2 H 1.61 0.03 2 216 . 21 MET HB3 H 1.56 0.03 2 217 . 21 MET HG2 H 2.11 0.03 2 218 . 21 MET HG3 H 2.11 0.03 2 219 . 21 MET HE H 0.42 0.03 1 220 . 21 MET C C 174.77 0.12 1 221 . 21 MET CA C 57.26 0.12 1 222 . 21 MET CB C 34.16 0.12 1 223 . 21 MET CG C 32.92 0.12 1 224 . 21 MET CE C 15.31 0.12 1 225 . 21 MET N N 116.41 0.15 1 226 . 22 ARG H H 6.49 0.03 1 227 . 22 ARG HA H 3.87 0.03 1 228 . 22 ARG HB2 H 1.78 0.03 2 229 . 22 ARG HB3 H 1.44 0.03 2 230 . 22 ARG HG2 H 2.10 0.03 2 231 . 22 ARG HG3 H 1.44 0.03 2 232 . 22 ARG HD2 H 3.36 0.03 2 233 . 22 ARG HD3 H 3.07 0.03 2 234 . 22 ARG C C 176.02 0.12 1 235 . 22 ARG CA C 58.94 0.12 1 236 . 22 ARG CB C 31.86 0.12 1 237 . 22 ARG CG C 27.05 0.12 1 238 . 22 ARG CD C 44.07 0.12 1 239 . 22 ARG N N 115.06 0.15 1 240 . 23 LYS H H 10.24 0.03 1 241 . 23 LYS HA H 4.54 0.03 1 242 . 23 LYS HB2 H 1.94 0.03 2 243 . 23 LYS HB3 H 1.79 0.03 2 244 . 23 LYS HG2 H 1.54 0.03 2 245 . 23 LYS HG3 H 2.02 0.03 2 246 . 23 LYS HD2 H 1.69 0.03 2 247 . 23 LYS HD3 H 1.80 0.03 2 248 . 23 LYS HE2 H 3.06 0.03 2 249 . 23 LYS HE3 H 3.06 0.03 2 250 . 23 LYS C C 176.75 0.12 1 251 . 23 LYS CA C 57.49 0.12 1 252 . 23 LYS CB C 36.37 0.12 1 253 . 23 LYS CG C 25.37 0.12 1 254 . 23 LYS CD C 29.84 0.12 1 255 . 23 LYS CE C 41.95 0.12 1 256 . 23 LYS N N 128.26 0.15 1 257 . 24 ILE H H 8.49 0.03 1 258 . 24 ILE HA H 4.57 0.03 1 259 . 24 ILE HB H 1.90 0.03 1 260 . 24 ILE HG12 H 1.26 0.03 2 261 . 24 ILE HG13 H 1.22 0.03 2 262 . 24 ILE HG2 H 0.88 0.03 1 263 . 24 ILE HD1 H 0.74 0.03 1 264 . 24 ILE C C 173.90 0.12 1 265 . 24 ILE CA C 59.73 0.12 1 266 . 24 ILE CB C 41.49 0.12 1 267 . 24 ILE CG1 C 26.57 0.12 1 268 . 24 ILE CG2 C 17.61 0.12 1 269 . 24 ILE CD1 C 14.56 0.12 1 270 . 24 ILE N N 118.35 0.15 1 271 . 25 SER H H 8.10 0.03 1 272 . 25 SER HA H 4.55 0.03 1 273 . 25 SER HB2 H 3.91 0.03 2 274 . 25 SER HB3 H 3.78 0.03 2 275 . 25 SER C C 176.55 0.12 1 276 . 25 SER CA C 56.62 0.12 1 277 . 25 SER CB C 64.28 0.12 1 278 . 25 SER N N 113.20 0.15 1 279 . 26 LEU H H 8.81 0.03 1 280 . 26 LEU HA H 3.89 0.03 1 281 . 26 LEU HB2 H 1.70 0.03 2 282 . 26 LEU HB3 H 1.42 0.03 2 283 . 26 LEU HG H 1.65 0.03 1 284 . 26 LEU HD1 H 0.87 0.03 1 285 . 26 LEU HD2 H 0.82 0.03 1 286 . 26 LEU C C 178.99 0.12 1 287 . 26 LEU CA C 57.50 0.12 1 288 . 26 LEU CB C 41.93 0.12 1 289 . 26 LEU CG C 27.08 0.12 1 290 . 26 LEU CD1 C 24.92 0.12 1 291 . 26 LEU CD2 C 25.13 0.12 1 292 . 26 LEU N N 127.35 0.15 1 293 . 27 PHE H H 7.99 0.03 1 294 . 27 PHE HA H 4.28 0.03 1 295 . 27 PHE HB2 H 3.19 0.03 2 296 . 27 PHE HB3 H 3.08 0.03 2 297 . 27 PHE HD1 H 7.25 0.03 3 298 . 27 PHE HD2 H 7.25 0.03 3 299 . 27 PHE HE1 H 7.36 0.03 3 300 . 27 PHE HE2 H 7.36 0.03 3 301 . 27 PHE HZ H 7.32 0.03 1 302 . 27 PHE C C 177.14 0.12 1 303 . 27 PHE CA C 60.01 0.12 1 304 . 27 PHE CB C 38.16 0.12 1 305 . 27 PHE N N 116.68 0.15 1 306 . 28 SER H H 7.94 0.03 1 307 . 28 SER HA H 4.57 0.03 1 308 . 28 SER HB2 H 4.04 0.03 2 309 . 28 SER HB3 H 4.10 0.03 2 310 . 28 SER C C 174.58 0.12 1 311 . 28 SER CA C 59.39 0.12 1 312 . 28 SER CB C 63.58 0.12 1 313 . 28 SER N N 114.92 0.15 1 314 . 29 CYS H H 7.87 0.03 1 315 . 29 CYS HA H 5.12 0.03 1 316 . 29 CYS HB2 H 2.62 0.03 1 317 . 29 CYS HB3 H 3.46 0.03 1 318 . 29 CYS C C 176.58 0.12 1 319 . 29 CYS CA C 53.46 0.12 1 320 . 29 CYS CB C 37.19 0.12 1 321 . 29 CYS N N 119.70 0.15 1 322 . 30 LEU H H 7.81 0.03 1 323 . 30 LEU HA H 3.97 0.03 1 324 . 30 LEU HB2 H 1.76 0.03 2 325 . 30 LEU HB3 H 1.50 0.03 2 326 . 30 LEU HG H 1.77 0.03 1 327 . 30 LEU HD1 H 0.94 0.03 1 328 . 30 LEU HD2 H 0.82 0.03 1 329 . 30 LEU C C 179.88 0.12 1 330 . 30 LEU CA C 58.28 0.12 1 331 . 30 LEU CB C 41.63 0.12 1 332 . 30 LEU CG C 24.95 0.12 1 333 . 30 LEU CD1 C 24.97 0.12 1 334 . 30 LEU CD2 C 23.44 0.12 1 335 . 30 LEU N N 121.86 0.15 1 336 . 31 LYS H H 8.59 0.03 1 337 . 31 LYS HA H 4.15 0.03 1 338 . 31 LYS HB2 H 1.78 0.03 2 339 . 31 LYS HB3 H 1.78 0.03 2 340 . 31 LYS HG2 H 1.38 0.03 2 341 . 31 LYS HG3 H 1.38 0.03 2 342 . 31 LYS HD2 H 1.36 0.03 2 343 . 31 LYS HD3 H 1.36 0.03 2 344 . 31 LYS HE2 H 2.98 0.03 2 345 . 31 LYS HE3 H 2.98 0.03 2 346 . 31 LYS C C 176.81 0.12 1 347 . 31 LYS CA C 58.01 0.12 1 348 . 31 LYS CB C 31.76 0.12 1 349 . 31 LYS CG C 24.78 0.12 1 350 . 31 LYS CD C 28.94 0.12 1 351 . 31 LYS CE C 42.46 0.12 1 352 . 31 LYS N N 117.38 0.15 1 353 . 32 ASP H H 7.80 0.03 1 354 . 32 ASP HA H 4.72 0.03 1 355 . 32 ASP HB2 H 2.38 0.03 1 356 . 32 ASP HB3 H 2.80 0.03 1 357 . 32 ASP C C 175.64 0.12 1 358 . 32 ASP CA C 54.44 0.12 1 359 . 32 ASP CB C 42.27 0.12 1 360 . 32 ASP CG C 175.64 0.12 1 361 . 32 ASP N N 117.51 0.15 1 362 . 33 ARG H H 7.38 0.03 1 363 . 33 ARG HA H 4.04 0.03 1 364 . 33 ARG HB2 H 1.82 0.03 2 365 . 33 ARG HB3 H 1.82 0.03 2 366 . 33 ARG HG2 H 1.79 0.03 2 367 . 33 ARG HG3 H 1.71 0.03 2 368 . 33 ARG HD2 H 3.14 0.03 2 369 . 33 ARG HD3 H 3.14 0.03 2 370 . 33 ARG C C 175.35 0.12 1 371 . 33 ARG CA C 57.89 0.12 1 372 . 33 ARG CB C 30.24 0.12 1 373 . 33 ARG CG C 26.99 0.12 1 374 . 33 ARG CD C 43.39 0.12 1 375 . 33 ARG N N 120.46 0.15 1 376 . 34 HIS H H 7.94 0.03 1 377 . 34 HIS HA H 4.25 0.03 1 378 . 34 HIS HB2 H 2.68 0.03 2 379 . 34 HIS HB3 H 2.68 0.03 2 380 . 34 HIS HD2 H 7.38 0.03 1 381 . 34 HIS HE1 H 8.62 0.03 1 382 . 34 HIS C C 170.60 0.12 1 383 . 34 HIS CA C 55.23 0.12 1 384 . 34 HIS CB C 31.74 0.12 1 385 . 34 HIS CD2 C 120.20 0.12 1 386 . 34 HIS N N 120.28 0.15 1 387 . 35 ASP H H 7.79 0.03 1 388 . 35 ASP HA H 4.70 0.03 1 389 . 35 ASP HB2 H 2.31 0.03 1 390 . 35 ASP HB3 H 2.52 0.03 1 391 . 35 ASP C C 176.06 0.12 1 392 . 35 ASP CA C 52.56 0.12 1 393 . 35 ASP CB C 41.43 0.12 1 394 . 35 ASP N N 124.76 0.15 1 395 . 36 PHE H H 8.94 0.03 1 396 . 36 PHE HA H 4.38 0.03 1 397 . 36 PHE HB2 H 2.79 0.03 1 398 . 36 PHE HB3 H 3.30 0.03 1 399 . 36 PHE HD1 H 6.98 0.03 3 400 . 36 PHE HD2 H 6.98 0.03 3 401 . 36 PHE HE1 H 6.80 0.03 3 402 . 36 PHE HE2 H 6.80 0.03 3 403 . 36 PHE HZ H 5.66 0.03 1 404 . 36 PHE C C 176.75 0.12 1 405 . 36 PHE CA C 59.53 0.12 1 406 . 36 PHE CB C 40.96 0.12 1 407 . 36 PHE CD1 C 132.50 0.12 3 408 . 36 PHE CD2 C 132.50 0.12 3 409 . 36 PHE CE1 C 131.00 0.12 3 410 . 36 PHE CE2 C 131.00 0.12 3 411 . 36 PHE CZ C 129.55 0.12 1 412 . 36 PHE N N 122.45 0.15 1 413 . 37 GLY H H 8.76 0.03 1 414 . 37 GLY HA2 H 3.95 0.03 2 415 . 37 GLY HA3 H 3.71 0.03 2 416 . 37 GLY C C 175.24 0.12 1 417 . 37 GLY CA C 48.31 0.12 1 418 . 37 GLY N N 111.47 0.15 1 419 . 38 PHE H H 9.18 0.03 1 420 . 38 PHE HA H 3.93 0.03 1 421 . 38 PHE HB2 H 2.94 0.03 1 422 . 38 PHE HB3 H 2.72 0.03 1 423 . 38 PHE HD1 H 6.17 0.03 3 424 . 38 PHE HD2 H 6.17 0.03 3 425 . 38 PHE HE1 H 6.88 0.03 3 426 . 38 PHE HE2 H 6.88 0.03 3 427 . 38 PHE HZ H 6.68 0.03 1 428 . 38 PHE CA C 55.82 0.12 1 429 . 38 PHE CB C 38.82 0.12 1 430 . 38 PHE CD1 C 131.75 0.12 3 431 . 38 PHE CD2 C 131.75 0.12 3 432 . 38 PHE CE1 C 130.55 0.12 3 433 . 38 PHE CE2 C 130.55 0.12 3 434 . 38 PHE N N 122.81 0.15 1 435 . 39 PRO HA H 4.62 0.03 1 436 . 39 PRO HB2 H 1.73 0.03 2 437 . 39 PRO HB3 H 2.03 0.03 2 438 . 39 PRO HG2 H 1.28 0.03 2 439 . 39 PRO HG3 H 1.54 0.03 2 440 . 39 PRO HD2 H 3.36 0.03 1 441 . 39 PRO HD3 H 2.62 0.03 1 442 . 39 PRO C C 174.79 0.12 1 443 . 39 PRO CA C 61.89 0.12 1 444 . 39 PRO CB C 28.59 0.12 1 445 . 39 PRO CD C 50.90 0.12 1 446 . 40 GLN H H 7.97 0.03 1 447 . 40 GLN HA H 3.64 0.03 1 448 . 40 GLN HB2 H 2.10 0.03 2 449 . 40 GLN HB3 H 2.04 0.03 2 450 . 40 GLN HG2 H 2.34 0.03 2 451 . 40 GLN HG3 H 2.34 0.03 2 452 . 40 GLN HE21 H 6.79 0.03 2 453 . 40 GLN HE22 H 7.58 0.03 2 454 . 40 GLN C C 177.07 0.12 1 455 . 40 GLN CA C 58.20 0.12 1 456 . 40 GLN CB C 28.97 0.12 1 457 . 40 GLN CG C 33.06 0.12 1 458 . 40 GLN N N 123.38 0.15 1 459 . 40 GLN NE2 N 111.19 0.15 1 460 . 41 GLU H H 9.12 0.03 1 461 . 41 GLU HA H 4.14 0.03 1 462 . 41 GLU HB2 H 2.34 0.03 2 463 . 41 GLU HB3 H 1.96 0.03 2 464 . 41 GLU HG2 H 2.20 0.03 2 465 . 41 GLU HG3 H 2.20 0.03 2 466 . 41 GLU C C 177.48 0.12 1 467 . 41 GLU CA C 58.00 0.12 1 468 . 41 GLU CB C 27.76 0.12 1 469 . 41 GLU CG C 34.30 0.12 1 470 . 41 GLU N N 119.22 0.15 1 471 . 42 GLU H H 7.68 0.03 1 472 . 42 GLU HA H 4.10 0.03 1 473 . 42 GLU HB2 H 1.68 0.03 2 474 . 42 GLU HB3 H 1.49 0.03 2 475 . 42 GLU HG2 H 2.14 0.03 2 476 . 42 GLU HG3 H 2.29 0.03 2 477 . 42 GLU C C 175.13 0.12 1 478 . 42 GLU CA C 56.28 0.12 1 479 . 42 GLU CB C 27.73 0.12 1 480 . 42 GLU CG C 33.02 0.12 1 481 . 42 GLU N N 116.97 0.15 1 482 . 43 PHE H H 7.60 0.03 1 483 . 43 PHE HA H 4.51 0.03 1 484 . 43 PHE HB2 H 2.75 0.03 1 485 . 43 PHE HB3 H 3.35 0.03 1 486 . 43 PHE HD1 H 7.11 0.03 3 487 . 43 PHE HD2 H 7.11 0.03 3 488 . 43 PHE HE1 H 6.97 0.03 3 489 . 43 PHE HE2 H 6.97 0.03 3 490 . 43 PHE HZ H 7.08 0.03 1 491 . 43 PHE C C 175.73 0.12 1 492 . 43 PHE CA C 57.48 0.12 1 493 . 43 PHE CB C 39.87 0.12 1 494 . 43 PHE CD1 C 132.20 0.12 3 495 . 43 PHE CD2 C 132.20 0.12 3 496 . 43 PHE CZ C 129.20 0.12 1 497 . 43 PHE N N 115.34 0.15 1 498 . 44 GLY H H 7.78 0.03 1 499 . 44 GLY HA2 H 4.04 0.03 2 500 . 44 GLY HA3 H 3.99 0.03 2 501 . 44 GLY C C 174.12 0.12 1 502 . 44 GLY CA C 45.61 0.12 1 503 . 44 GLY N N 107.00 0.15 1 504 . 45 ASN H H 8.35 0.03 1 505 . 45 ASN HA H 4.59 0.03 1 506 . 45 ASN HB2 H 2.82 0.03 2 507 . 45 ASN HB3 H 2.82 0.03 2 508 . 45 ASN HD21 H 7.56 0.03 2 509 . 45 ASN HD22 H 6.91 0.03 2 510 . 45 ASN C C 175.89 0.12 1 511 . 45 ASN CA C 54.04 0.12 1 512 . 45 ASN CB C 38.68 0.12 1 513 . 45 ASN N N 117.58 0.15 1 514 . 45 ASN ND2 N 112.14 0.15 1 515 . 46 GLN H H 8.61 0.03 1 516 . 46 GLN HA H 4.14 0.03 1 517 . 46 GLN HB2 H 1.82 0.03 2 518 . 46 GLN HB3 H 1.82 0.03 2 519 . 46 GLN HG2 H 1.95 0.03 2 520 . 46 GLN HG3 H 1.95 0.03 2 521 . 46 GLN HE21 H 6.78 0.03 2 522 . 46 GLN HE22 H 7.27 0.03 2 523 . 46 GLN C C 175.93 0.12 1 524 . 46 GLN CA C 56.77 0.12 1 525 . 46 GLN CB C 28.35 0.12 1 526 . 46 GLN CG C 33.20 0.12 1 527 . 46 GLN N N 118.79 0.15 1 528 . 46 GLN NE2 N 111.84 0.15 1 529 . 47 PHE H H 7.93 0.03 1 530 . 47 PHE HA H 4.59 0.03 1 531 . 47 PHE HB2 H 2.92 0.03 1 532 . 47 PHE HB3 H 3.16 0.03 1 533 . 47 PHE HD1 H 7.19 0.03 3 534 . 47 PHE HD2 H 7.19 0.03 3 535 . 47 PHE HE1 H 7.26 0.03 3 536 . 47 PHE HE2 H 7.26 0.03 3 537 . 47 PHE HZ H 7.30 0.03 1 538 . 47 PHE C C 175.95 0.12 1 539 . 47 PHE CA C 57.87 0.12 1 540 . 47 PHE CB C 39.62 0.12 1 541 . 47 PHE CD1 C 132.10 0.12 3 542 . 47 PHE CD2 C 132.10 0.12 3 543 . 47 PHE CE1 C 130.20 0.12 3 544 . 47 PHE CE2 C 130.20 0.12 3 545 . 47 PHE N N 119.24 0.15 3 546 . 48 GLN H H 8.29 0.03 1 547 . 48 GLN HA H 4.36 0.03 1 548 . 48 GLN HB2 H 2.21 0.03 2 549 . 48 GLN HB3 H 1.95 0.03 2 550 . 48 GLN HG2 H 2.34 0.03 2 551 . 48 GLN HG3 H 2.34 0.03 2 552 . 48 GLN HE21 H 6.84 0.03 2 553 . 48 GLN HE22 H 7.51 0.03 2 554 . 48 GLN C C 176.71 0.12 1 555 . 48 GLN CA C 55.62 0.12 1 556 . 48 GLN CB C 29.20 0.12 1 557 . 48 GLN CG C 33.71 0.12 1 558 . 48 GLN N N 119.99 0.15 1 559 . 48 GLN NE2 N 111.95 0.15 1 560 . 49 LYS H H 8.42 0.03 1 561 . 49 LYS HA H 4.17 0.03 1 562 . 49 LYS HB2 H 1.85 0.03 2 563 . 49 LYS HB3 H 1.73 0.03 2 564 . 49 LYS HG2 H 1.48 0.03 2 565 . 49 LYS HG3 H 1.48 0.03 2 566 . 49 LYS HD2 H 1.63 0.03 2 567 . 49 LYS HD3 H 1.63 0.03 2 568 . 49 LYS HE2 H 2.98 0.03 2 569 . 49 LYS HE3 H 2.98 0.03 2 570 . 49 LYS C C 177.91 0.12 1 571 . 49 LYS CA C 58.25 0.12 1 572 . 49 LYS CB C 32.49 0.12 1 573 . 49 LYS CG C 24.86 0.12 1 574 . 49 LYS CD C 28.90 0.12 1 575 . 49 LYS CE C 41.99 0.12 1 576 . 49 LYS N N 121.96 0.15 1 577 . 50 ALA H H 8.58 0.03 1 578 . 50 ALA HA H 4.15 0.03 1 579 . 50 ALA HB H 1.40 0.03 1 580 . 50 ALA C C 178.76 0.12 1 581 . 50 ALA CA C 54.04 0.12 1 582 . 50 ALA CB C 18.97 0.12 1 583 . 50 ALA N N 121.04 0.15 1 584 . 51 GLU H H 8.08 0.03 1 585 . 51 GLU HA H 4.27 0.03 1 586 . 51 GLU HB2 H 2.14 0.03 2 587 . 51 GLU HB3 H 2.14 0.03 2 588 . 51 GLU HG2 H 2.38 0.03 2 589 . 51 GLU HG3 H 2.38 0.03 2 590 . 51 GLU C C 176.94 0.12 1 591 . 51 GLU CA C 57.13 0.12 1 592 . 51 GLU CB C 29.29 0.12 1 593 . 51 GLU CG C 34.66 0.12 1 594 . 51 GLU N N 115.05 0.15 1 595 . 52 THR H H 7.85 0.03 1 596 . 52 THR HA H 4.13 0.03 1 597 . 52 THR HB H 4.27 0.03 1 598 . 52 THR HG2 H 1.26 0.03 1 599 . 52 THR C C 175.78 0.12 1 600 . 52 THR CA C 63.82 0.12 1 601 . 52 THR CB C 69.61 0.12 1 602 . 52 THR CG2 C 22.62 0.12 1 603 . 52 THR N N 111.56 0.15 1 604 . 53 ILE H H 8.12 0.03 1 605 . 53 ILE HA H 3.90 0.03 1 606 . 53 ILE HB H 2.12 0.03 1 607 . 53 ILE HG12 H 1.75 0.03 1 608 . 53 ILE HG13 H 1.22 0.03 1 609 . 53 ILE HG2 H 0.90 0.03 1 610 . 53 ILE HD1 H 0.89 0.03 1 611 . 53 ILE CA C 66.84 0.12 1 612 . 53 ILE CB C 34.90 0.12 1 613 . 53 ILE CG1 C 30.00 0.12 1 614 . 53 ILE CG2 C 17.95 0.12 1 615 . 53 ILE CD1 C 12.81 0.12 1 616 . 53 ILE N N 121.50 0.15 1 617 . 54 PRO HA H 4.31 0.03 1 618 . 54 PRO HB2 H 1.81 0.03 2 619 . 54 PRO HB3 H 2.37 0.03 2 620 . 54 PRO HG2 H 1.95 0.03 2 621 . 54 PRO HG3 H 2.15 0.03 2 622 . 54 PRO HD2 H 3.68 0.03 2 623 . 54 PRO HD3 H 3.63 0.03 2 624 . 54 PRO C C 179.58 0.12 1 625 . 54 PRO CA C 66.07 0.12 1 626 . 54 PRO CB C 31.45 0.12 1 627 . 54 PRO CG C 28.61 0.12 1 628 . 54 PRO CD C 49.84 0.12 1 629 . 55 VAL H H 7.23 0.03 1 630 . 55 VAL HA H 3.72 0.03 1 631 . 55 VAL HB H 2.07 0.03 1 632 . 55 VAL HG1 H 0.68 0.03 1 633 . 55 VAL HG2 H 0.84 0.03 1 634 . 55 VAL C C 177.68 0.12 1 635 . 55 VAL CA C 65.86 0.12 1 636 . 55 VAL CB C 31.51 0.12 1 637 . 55 VAL CG1 C 22.39 0.12 1 638 . 55 VAL CG2 C 22.70 0.12 1 639 . 55 VAL N N 116.37 0.15 1 640 . 56 LEU H H 8.52 0.03 1 641 . 56 LEU HA H 4.30 0.03 1 642 . 56 LEU HB2 H 1.79 0.03 1 643 . 56 LEU HB3 H 1.57 0.03 1 644 . 56 LEU HG H 1.75 0.03 1 645 . 56 LEU HD1 H 0.91 0.03 1 646 . 56 LEU HD2 H 0.94 0.03 1 647 . 56 LEU C C 178.69 0.12 1 648 . 56 LEU CA C 58.03 0.12 1 649 . 56 LEU CB C 42.09 0.12 1 650 . 56 LEU CG C 24.37 0.12 1 651 . 56 LEU CD1 C 24.08 0.12 1 652 . 56 LEU CD2 C 24.97 0.12 1 653 . 56 LEU N N 122.43 0.15 1 654 . 57 HIS H H 9.05 0.03 1 655 . 57 HIS HA H 3.81 0.03 1 656 . 57 HIS HB2 H 3.08 0.03 1 657 . 57 HIS HB3 H 3.39 0.03 1 658 . 57 HIS HD2 H 7.20 0.03 1 659 . 57 HIS HE1 H 8.62 0.03 1 660 . 57 HIS C C 175.69 0.12 1 661 . 57 HIS CA C 60.63 0.12 1 662 . 57 HIS CB C 28.07 0.12 1 663 . 57 HIS CD2 C 119.70 0.12 1 664 . 57 HIS N N 116.64 0.15 1 665 . 58 GLU H H 7.89 0.03 1 666 . 58 GLU HA H 4.04 0.03 1 667 . 58 GLU HB2 H 2.14 0.03 2 668 . 58 GLU HB3 H 2.14 0.03 2 669 . 58 GLU HG2 H 2.32 0.03 2 670 . 58 GLU HG3 H 2.32 0.03 2 671 . 58 GLU C C 177.85 0.12 1 672 . 58 GLU CA C 59.20 0.12 1 673 . 58 GLU CB C 29.05 0.12 1 674 . 58 GLU N N 119.32 0.15 1 675 . 59 MET H H 8.61 0.03 1 676 . 59 MET HA H 4.09 0.03 1 677 . 59 MET HB2 H 2.52 0.03 1 678 . 59 MET HB3 H 2.67 0.03 1 679 . 59 MET HE H 2.05 0.03 1 680 . 59 MET C C 177.13 0.12 1 681 . 59 MET CA C 59.18 0.12 1 682 . 59 MET CB C 32.76 0.12 1 683 . 59 MET CG C 32.56 0.12 1 684 . 59 MET CE C 18.10 0.12 1 685 . 59 MET N N 118.25 0.15 1 686 . 60 ILE H H 8.36 0.03 1 687 . 60 ILE HA H 3.47 0.03 1 688 . 60 ILE HB H 1.73 0.03 1 689 . 60 ILE HG12 H 1.76 0.03 2 690 . 60 ILE HG13 H 1.22 0.03 2 691 . 60 ILE HG2 H 0.78 0.03 1 692 . 60 ILE HD1 H 0.81 0.03 1 693 . 60 ILE CA C 65.18 0.12 1 694 . 60 ILE CB C 36.94 0.12 1 695 . 60 ILE CG1 C 29.66 0.12 1 696 . 60 ILE CG2 C 19.38 0.12 1 697 . 60 ILE CD1 C 12.77 0.12 1 698 . 60 ILE N N 116.75 0.15 1 699 . 61 GLN H H 8.26 0.03 1 700 . 61 GLN HA H 3.72 0.03 1 701 . 61 GLN HB2 H 2.00 0.03 2 702 . 61 GLN HB3 H 1.77 0.03 2 703 . 61 GLN HG2 H 2.30 0.03 2 704 . 61 GLN HG3 H 2.30 0.03 2 705 . 61 GLN HE21 H 7.19 0.03 2 706 . 61 GLN HE22 H 6.74 0.03 2 707 . 61 GLN C C 178.34 0.12 1 708 . 61 GLN CA C 58.76 0.12 1 709 . 61 GLN CB C 28.95 0.12 1 710 . 61 GLN CG C 33.75 0.12 1 711 . 61 GLN N N 119.90 0.15 1 712 . 61 GLN NE2 N 113.19 0.15 1 713 . 62 GLN H H 8.42 0.03 1 714 . 62 GLN HA H 3.68 0.03 1 715 . 62 GLN HB2 H 0.95 0.03 1 716 . 62 GLN HB3 H 0.54 0.03 1 717 . 62 GLN HG2 H 1.87 0.03 2 718 . 62 GLN HG3 H 2.64 0.03 2 719 . 62 GLN HE21 H 7.06 0.03 2 720 . 62 GLN HE22 H 8.28 0.03 2 721 . 62 GLN C C 179.76 0.12 1 722 . 62 GLN CA C 57.80 0.12 1 723 . 62 GLN CB C 24.53 0.12 1 724 . 62 GLN CG C 32.88 0.12 1 725 . 62 GLN N N 116.43 0.15 1 726 . 62 GLN NE2 N 114.18 0.15 1 727 . 63 ILE H H 8.16 0.03 1 728 . 63 ILE HA H 3.69 0.03 1 729 . 63 ILE HB H 1.95 0.03 1 730 . 63 ILE HG12 H 1.75 0.03 2 731 . 63 ILE HG13 H 1.27 0.03 2 732 . 63 ILE HG2 H 0.97 0.03 1 733 . 63 ILE HD1 H 0.82 0.03 1 734 . 63 ILE C C 177.34 0.12 1 735 . 63 ILE CA C 67.05 0.12 1 736 . 63 ILE CB C 38.10 0.12 1 737 . 63 ILE CG1 C 29.15 0.12 1 738 . 63 ILE CG2 C 19.21 0.12 1 739 . 63 ILE CD1 C 14.63 0.12 1 740 . 63 ILE N N 122.43 0.15 1 741 . 64 PHE H H 8.43 0.03 1 742 . 64 PHE HA H 3.74 0.03 1 743 . 64 PHE HB2 H 2.76 0.03 1 744 . 64 PHE HB3 H 3.33 0.03 1 745 . 64 PHE HD1 H 6.93 0.03 3 746 . 64 PHE HD2 H 6.93 0.03 3 747 . 64 PHE HE1 H 6.89 0.03 3 748 . 64 PHE HE2 H 6.89 0.03 3 749 . 64 PHE HZ H 6.98 0.03 1 750 . 64 PHE C C 178.48 0.12 1 751 . 64 PHE CA C 62.14 0.12 1 752 . 64 PHE CB C 38.41 0.12 1 753 . 64 PHE N N 120.48 0.15 1 754 . 65 ASN H H 8.83 0.03 1 755 . 65 ASN HA H 4.08 0.03 1 756 . 65 ASN HB2 H 2.87 0.03 2 757 . 65 ASN HB3 H 2.78 0.03 2 758 . 65 ASN C C 178.03 0.12 1 759 . 65 ASN CA C 55.81 0.12 1 760 . 65 ASN CB C 37.46 0.12 1 761 . 65 ASN N N 119.50 0.15 1 762 . 66 LEU H H 8.17 0.03 1 763 . 66 LEU HA H 4.26 0.03 1 764 . 66 LEU HB2 H 1.74 0.03 1 765 . 66 LEU HB3 H 2.24 0.03 1 766 . 66 LEU HG H 1.28 0.03 1 767 . 66 LEU HD1 H 0.89 0.03 1 768 . 66 LEU HD2 H 0.91 0.03 1 769 . 66 LEU C C 177.88 0.12 1 770 . 66 LEU CA C 58.15 0.12 1 771 . 66 LEU CB C 42.70 0.12 1 772 . 66 LEU CG C 27.01 0.12 1 773 . 66 LEU CD1 C 23.11 0.12 1 774 . 66 LEU CD2 C 27.40 0.12 1 775 . 66 LEU N N 121.17 0.15 1 776 . 67 PHE H H 8.17 0.03 1 777 . 67 PHE HA H 4.95 0.03 1 778 . 67 PHE HB2 H 2.98 0.03 1 779 . 67 PHE HB3 H 3.43 0.03 1 780 . 67 PHE HD1 H 7.49 0.03 3 781 . 67 PHE HD2 H 7.49 0.03 3 782 . 67 PHE HE1 H 6.84 0.03 3 783 . 67 PHE HE2 H 6.84 0.03 3 784 . 67 PHE HZ H 6.78 0.03 1 785 . 67 PHE C C 178.00 0.12 1 786 . 67 PHE CA C 59.36 0.12 1 787 . 67 PHE CB C 38.76 0.12 1 788 . 67 PHE CD1 C 132.30 0.12 3 789 . 67 PHE CD2 C 132.30 0.12 3 790 . 67 PHE CE1 C 130.90 0.12 3 791 . 67 PHE CE2 C 130.90 0.12 3 792 . 67 PHE CZ C 127.65 0.12 1 793 . 67 PHE N N 110.49 0.15 1 794 . 68 SER H H 8.03 0.03 1 795 . 68 SER HA H 4.64 0.03 1 796 . 68 SER HB2 H 3.65 0.03 1 797 . 68 SER HB3 H 3.12 0.03 1 798 . 68 SER C C 173.55 0.12 1 799 . 68 SER CA C 59.43 0.12 1 800 . 68 SER CB C 63.22 0.12 1 801 . 68 SER N N 118.74 0.15 1 802 . 69 THR H H 6.99 0.03 1 803 . 69 THR HA H 4.41 0.03 1 804 . 69 THR HB H 4.73 0.03 1 805 . 69 THR HG2 H 1.57 0.03 1 806 . 69 THR C C 175.80 0.12 1 807 . 69 THR CA C 61.39 0.12 1 808 . 69 THR CB C 72.44 0.12 1 809 . 69 THR CG2 C 21.47 0.12 1 810 . 69 THR N N 110.98 0.15 1 811 . 70 LYS H H 9.08 0.03 1 812 . 70 LYS HA H 4.14 0.03 1 813 . 70 LYS HB2 H 1.79 0.03 2 814 . 70 LYS HB3 H 1.79 0.03 2 815 . 70 LYS HG2 H 1.44 0.03 2 816 . 70 LYS HG3 H 1.44 0.03 2 817 . 70 LYS HD2 H 1.57 0.03 2 818 . 70 LYS HD3 H 1.57 0.03 2 819 . 70 LYS HE2 H 2.93 0.03 2 820 . 70 LYS HE3 H 2.93 0.03 2 821 . 70 LYS C C 179.26 0.12 1 822 . 70 LYS CA C 58.61 0.12 1 823 . 70 LYS CB C 31.69 0.12 1 824 . 70 LYS CG C 24.82 0.12 1 825 . 70 LYS CD C 28.85 0.12 1 826 . 70 LYS CE C 41.38 0.12 1 827 . 70 LYS N N 120.78 0.15 1 828 . 71 ASP H H 7.48 0.03 1 829 . 71 ASP HA H 4.18 0.03 1 830 . 71 ASP HB2 H 2.31 0.03 2 831 . 71 ASP HB3 H 2.31 0.03 2 832 . 71 ASP C C 178.56 0.12 1 833 . 71 ASP CA C 57.12 0.12 1 834 . 71 ASP CB C 40.96 0.12 1 835 . 71 ASP N N 116.11 0.15 1 836 . 72 SER H H 8.07 0.03 1 837 . 72 SER HA H 3.75 0.03 1 838 . 72 SER HB2 H 4.08 0.03 2 839 . 72 SER HB3 H 4.08 0.03 2 840 . 72 SER C C 176.95 0.12 1 841 . 72 SER CA C 60.32 0.12 1 842 . 72 SER CB C 62.58 0.12 1 843 . 72 SER N N 116.85 0.15 1 844 . 73 SER H H 7.98 0.03 1 845 . 73 SER HA H 4.12 0.03 1 846 . 73 SER HB2 H 3.96 0.03 2 847 . 73 SER HB3 H 3.96 0.03 2 848 . 73 SER C C 174.93 0.12 1 849 . 73 SER CA C 61.28 0.12 1 850 . 73 SER CB C 62.90 0.12 1 851 . 73 SER N N 112.99 0.15 1 852 . 74 ALA H H 7.11 0.03 1 853 . 74 ALA HA H 4.23 0.03 1 854 . 74 ALA HB H 1.34 0.03 1 855 . 74 ALA C C 177.69 0.12 1 856 . 74 ALA CA C 52.77 0.12 1 857 . 74 ALA CB C 18.82 0.12 1 858 . 74 ALA N N 119.08 0.15 1 859 . 75 ALA H H 7.17 0.03 1 860 . 75 ALA HA H 3.74 0.03 1 861 . 75 ALA HB H -0.26 0.03 1 862 . 75 ALA C C 177.26 0.12 1 863 . 75 ALA CA C 53.06 0.12 1 864 . 75 ALA CB C 18.26 0.12 1 865 . 75 ALA N N 121.08 0.15 1 866 . 76 TRP H H 7.08 0.03 1 867 . 76 TRP HA H 5.13 0.03 1 868 . 76 TRP HB2 H 2.69 0.03 1 869 . 76 TRP HB3 H 3.05 0.03 1 870 . 76 TRP HD1 H 7.33 0.03 1 871 . 76 TRP HE1 H 6.79 0.03 1 872 . 76 TRP HE3 H 7.63 0.03 1 873 . 76 TRP HZ2 H 7.82 0.03 1 874 . 76 TRP HZ3 H 7.33 0.03 1 875 . 76 TRP HH2 H 7.17 0.03 1 876 . 76 TRP C C 174.81 0.12 1 877 . 76 TRP CA C 53.46 0.12 1 878 . 76 TRP CB C 33.42 0.12 1 879 . 76 TRP CD1 C 129.75 0.12 1 880 . 76 TRP CE3 C 122.95 0.12 1 881 . 76 TRP CZ2 C 114.20 0.12 1 882 . 76 TRP CZ3 C 122.40 0.12 1 883 . 76 TRP CH2 C 124.31 0.12 1 884 . 76 TRP N N 116.44 0.15 1 885 . 76 TRP NE1 N 121.68 0.15 1 886 . 77 ASP H H 8.25 0.03 1 887 . 77 ASP HA H 4.39 0.03 1 888 . 77 ASP HB2 H 2.59 0.03 1 889 . 77 ASP HB3 H 2.70 0.03 1 890 . 77 ASP C C 176.97 0.12 1 891 . 77 ASP CA C 55.00 0.12 1 892 . 77 ASP CB C 42.78 0.12 1 893 . 77 ASP N N 119.68 0.15 1 894 . 78 GLU H H 8.92 0.03 1 895 . 78 GLU HA H 3.93 0.03 1 896 . 78 GLU HB2 H 2.09 0.03 1 897 . 78 GLU HB3 H 2.26 0.03 1 898 . 78 GLU HG2 H 2.48 0.03 2 899 . 78 GLU HG3 H 2.59 0.03 2 900 . 78 GLU C C 177.61 0.12 1 901 . 78 GLU CA C 59.37 0.12 1 902 . 78 GLU CB C 28.95 0.12 1 903 . 78 GLU CG C 34.68 0.12 1 904 . 78 GLU N N 126.81 0.15 1 905 . 79 THR H H 8.17 0.03 1 906 . 79 THR HA H 3.97 0.03 1 907 . 79 THR HB H 4.25 0.03 1 908 . 79 THR HG2 H 1.20 0.03 1 909 . 79 THR C C 177.36 0.12 1 910 . 79 THR CA C 66.15 0.12 1 911 . 79 THR CB C 67.91 0.12 1 912 . 79 THR CG2 C 21.82 0.12 1 913 . 79 THR N N 115.18 0.15 1 914 . 80 LEU H H 7.77 0.03 1 915 . 80 LEU HA H 3.90 0.03 1 916 . 80 LEU HB2 H 1.79 0.03 1 917 . 80 LEU HB3 H 1.09 0.03 1 918 . 80 LEU HG H 1.64 0.03 1 919 . 80 LEU HD1 H 0.77 0.03 1 920 . 80 LEU HD2 H 0.68 0.03 1 921 . 80 LEU C C 179.10 0.12 1 922 . 80 LEU CA C 57.54 0.12 1 923 . 80 LEU CB C 41.71 0.12 1 924 . 80 LEU CG C 25.96 0.12 1 925 . 80 LEU CD1 C 26.50 0.12 1 926 . 80 LEU CD2 C 22.79 0.12 1 927 . 80 LEU N N 121.53 0.15 1 928 . 81 LEU H H 8.34 0.03 1 929 . 81 LEU HA H 3.51 0.03 1 930 . 81 LEU HB2 H 1.72 0.03 1 931 . 81 LEU HB3 H 1.10 0.03 1 932 . 81 LEU HG H 1.53 0.03 1 933 . 81 LEU HD1 H 0.93 0.03 1 934 . 81 LEU HD2 H 0.77 0.03 1 935 . 81 LEU C C 177.15 0.12 1 936 . 81 LEU CA C 57.66 0.12 1 937 . 81 LEU CB C 41.22 0.12 1 938 . 81 LEU CG C 26.57 0.12 1 939 . 81 LEU CD1 C 25.64 0.12 1 940 . 81 LEU CD2 C 22.81 0.12 1 941 . 81 LEU N N 118.88 0.15 1 942 . 82 ASP H H 7.96 0.03 1 943 . 82 ASP HA H 4.31 0.03 1 944 . 82 ASP HB2 H 2.85 0.03 2 945 . 82 ASP HB3 H 2.85 0.03 2 946 . 82 ASP C C 179.13 0.12 1 947 . 82 ASP CA C 56.89 0.12 1 948 . 82 ASP CB C 38.72 0.12 1 949 . 82 ASP N N 115.13 0.15 1 950 . 83 LYS H H 7.34 0.03 1 951 . 83 LYS HA H 4.03 0.03 1 952 . 83 LYS HB2 H 1.88 0.03 2 953 . 83 LYS HB3 H 1.71 0.03 2 954 . 83 LYS HG2 H 1.53 0.03 2 955 . 83 LYS HG3 H 1.53 0.03 2 956 . 83 LYS HE2 H 3.09 0.03 2 957 . 83 LYS HE3 H 3.09 0.03 2 958 . 83 LYS C C 178.65 0.12 1 959 . 83 LYS CA C 59.36 0.12 1 960 . 83 LYS CB C 33.18 0.12 1 961 . 83 LYS CG C 29.63 0.12 1 962 . 83 LYS CE C 38.78 0.12 1 963 . 83 LYS N N 118.94 0.15 1 964 . 84 PHE H H 8.49 0.03 1 965 . 84 PHE HA H 4.05 0.03 1 966 . 84 PHE HB2 H 3.10 0.03 1 967 . 84 PHE HB3 H 2.76 0.03 1 968 . 84 PHE HD1 H 6.68 0.03 3 969 . 84 PHE HD2 H 6.68 0.03 3 970 . 84 PHE HE1 H 6.46 0.03 3 971 . 84 PHE HE2 H 6.46 0.03 3 972 . 84 PHE HZ H 6.20 0.03 1 973 . 84 PHE C C 177.26 0.12 1 974 . 84 PHE CA C 60.33 0.12 1 975 . 84 PHE CB C 39.44 0.12 1 976 . 84 PHE CD1 C 130.20 0.12 3 977 . 84 PHE CD2 C 130.20 0.12 3 978 . 84 PHE CE1 C 130.90 0.12 3 979 . 84 PHE CE2 C 130.90 0.12 3 980 . 84 PHE CZ C 128.40 0.12 1 981 . 84 PHE N N 123.57 0.15 1 982 . 85 TYR H H 9.03 0.03 1 983 . 85 TYR HA H 4.07 0.03 1 984 . 85 TYR HB2 H 3.25 0.03 2 985 . 85 TYR HB3 H 3.25 0.03 2 986 . 85 TYR HD1 H 6.88 0.03 3 987 . 85 TYR HD2 H 6.88 0.03 3 988 . 85 TYR HE1 H 6.49 0.03 3 989 . 85 TYR HE2 H 6.49 0.03 3 990 . 85 TYR C C 178.15 0.12 1 991 . 85 TYR CA C 58.65 0.12 1 992 . 85 TYR CB C 36.83 0.12 1 993 . 85 TYR CD1 C 132.30 0.12 3 994 . 85 TYR CD2 C 132.30 0.12 3 995 . 85 TYR N N 118.02 0.15 1 996 . 86 THR H H 7.62 0.03 1 997 . 86 THR HA H 4.00 0.03 1 998 . 86 THR HB H 4.31 0.03 1 999 . 86 THR HG2 H 1.25 0.03 1 1000 . 86 THR C C 176.82 0.12 1 1001 . 86 THR CA C 66.97 0.12 1 1002 . 86 THR CB C 68.79 0.12 1 1003 . 86 THR CG2 C 21.79 0.12 1 1004 . 86 THR N N 113.68 0.15 1 1005 . 87 GLU H H 7.69 0.03 1 1006 . 87 GLU HA H 4.07 0.03 1 1007 . 87 GLU HB2 H 2.09 0.03 2 1008 . 87 GLU HB3 H 1.86 0.03 2 1009 . 87 GLU HG2 H 2.34 0.03 2 1010 . 87 GLU HG3 H 2.34 0.03 2 1011 . 87 GLU C C 180.01 0.12 1 1012 . 87 GLU CA C 58.38 0.12 1 1013 . 87 GLU CB C 28.60 0.12 1 1014 . 87 GLU CG C 34.70 0.12 1 1015 . 87 GLU N N 120.33 0.15 1 1016 . 88 LEU H H 8.38 0.03 1 1017 . 88 LEU HA H 3.74 0.03 1 1018 . 88 LEU HB2 H 1.75 0.03 1 1019 . 88 LEU HB3 H 0.95 0.03 1 1020 . 88 LEU HG H 1.16 0.03 1 1021 . 88 LEU HD1 H 0.11 0.03 1 1022 . 88 LEU HD2 H 0.31 0.03 1 1023 . 88 LEU C C 178.74 0.12 1 1024 . 88 LEU CA C 58.08 0.12 1 1025 . 88 LEU CB C 41.37 0.12 1 1026 . 88 LEU CG C 25.93 0.12 1 1027 . 88 LEU CD1 C 26.13 0.12 1 1028 . 88 LEU CD2 C 21.52 0.12 1 1029 . 88 LEU N N 120.36 0.15 1 1030 . 89 TYR H H 8.69 0.03 1 1031 . 89 TYR HA H 4.02 0.03 1 1032 . 89 TYR HB2 H 3.04 0.03 2 1033 . 89 TYR HB3 H 3.04 0.03 2 1034 . 89 TYR HD1 H 6.89 0.03 3 1035 . 89 TYR HD2 H 6.89 0.03 3 1036 . 89 TYR HE1 H 6.45 0.03 3 1037 . 89 TYR HE2 H 6.45 0.03 3 1038 . 89 TYR C C 178.48 0.12 1 1039 . 89 TYR CA C 61.30 0.12 1 1040 . 89 TYR CB C 37.83 0.12 1 1041 . 89 TYR CE1 C 118.05 0.12 3 1042 . 89 TYR CE2 C 118.05 0.12 3 1043 . 89 TYR N N 118.29 0.15 1 1044 . 90 GLN H H 7.74 0.03 1 1045 . 90 GLN HA H 3.99 0.03 1 1046 . 90 GLN HB2 H 2.20 0.03 2 1047 . 90 GLN HB3 H 2.20 0.03 2 1048 . 90 GLN HG2 H 2.38 0.03 2 1049 . 90 GLN HG3 H 2.48 0.03 2 1050 . 90 GLN HE21 H 6.83 0.03 2 1051 . 90 GLN HE22 H 7.48 0.03 2 1052 . 90 GLN C C 178.45 0.12 1 1053 . 90 GLN CA C 59.07 0.12 1 1054 . 90 GLN CB C 28.37 0.12 1 1055 . 90 GLN CG C 34.26 0.12 1 1056 . 90 GLN N N 117.83 0.15 1 1057 . 90 GLN NE2 N 112.80 0.15 1 1058 . 91 GLN H H 7.70 0.03 1 1059 . 91 GLN HA H 4.10 0.03 1 1060 . 91 GLN HG2 H 2.30 0.03 2 1061 . 91 GLN HG3 H 2.30 0.03 2 1062 . 91 GLN C C 178.77 0.12 1 1063 . 91 GLN CA C 59.28 0.12 1 1064 . 91 GLN CB C 29.63 0.12 1 1065 . 91 GLN N N 117.53 0.15 1 1066 . 92 LEU H H 8.46 0.03 1 1067 . 92 LEU HA H 3.76 0.03 1 1068 . 92 LEU HB2 H 1.78 0.03 2 1069 . 92 LEU HB3 H 1.43 0.03 2 1070 . 92 LEU HG H 1.50 0.03 1 1071 . 92 LEU HD1 H 0.37 0.03 1 1072 . 92 LEU HD2 H 0.36 0.03 1 1073 . 92 LEU C C 178.39 0.12 1 1074 . 92 LEU CA C 58.90 0.12 1 1075 . 92 LEU CB C 41.40 0.12 1 1076 . 92 LEU CG C 26.49 0.12 1 1077 . 92 LEU CD1 C 24.49 0.12 1 1078 . 92 LEU CD2 C 23.85 0.12 1 1079 . 92 LEU N N 119.44 0.15 1 1080 . 93 ASN H H 8.15 0.03 1 1081 . 93 ASN HA H 4.32 0.03 1 1082 . 93 ASN HB2 H 2.74 0.03 2 1083 . 93 ASN HB3 H 2.74 0.03 2 1084 . 93 ASN HD21 H 6.41 0.03 2 1085 . 93 ASN HD22 H 7.37 0.03 2 1086 . 93 ASN C C 176.68 0.12 1 1087 . 93 ASN CA C 56.19 0.12 1 1088 . 93 ASN CB C 38.35 0.12 1 1089 . 93 ASN N N 117.55 0.15 1 1090 . 93 ASN ND2 N 111.48 0.15 1 1091 . 94 ASP H H 8.32 0.03 1 1092 . 94 ASP HA H 4.43 0.03 1 1093 . 94 ASP HB2 H 2.72 0.03 1 1094 . 94 ASP HB3 H 2.96 0.03 1 1095 . 94 ASP C C 178.45 0.12 1 1096 . 94 ASP CA C 56.81 0.12 1 1097 . 94 ASP CB C 39.77 0.12 1 1098 . 94 ASP N N 120.48 0.15 1 1099 . 95 LEU H H 8.02 0.03 1 1100 . 95 LEU HA H 4.06 0.03 1 1101 . 95 LEU HB2 H 1.46 0.03 1 1102 . 95 LEU HB3 H 2.01 0.03 1 1103 . 95 LEU HG H 1.73 0.03 1 1104 . 95 LEU HD1 H 0.87 0.03 1 1105 . 95 LEU HD2 H 0.95 0.03 1 1106 . 95 LEU C C 178.74 0.12 1 1107 . 95 LEU CA C 57.49 0.12 1 1108 . 95 LEU CB C 42.55 0.12 1 1109 . 95 LEU CG C 26.94 0.12 1 1110 . 95 LEU CD1 C 26.49 0.12 1 1111 . 95 LEU CD2 C 23.76 0.12 1 1112 . 95 LEU N N 118.46 0.15 1 1113 . 96 GLU H H 8.16 0.03 1 1114 . 96 GLU HA H 3.99 0.03 1 1115 . 96 GLU HB2 H 2.09 0.03 2 1116 . 96 GLU HB3 H 2.09 0.03 2 1117 . 96 GLU HG2 H 2.46 0.03 2 1118 . 96 GLU HG3 H 2.46 0.03 2 1119 . 96 GLU C C 177.62 0.12 1 1120 . 96 GLU CA C 57.75 0.12 1 1121 . 96 GLU CB C 28.16 0.12 1 1122 . 96 GLU CG C 33.65 0.12 1 1123 . 96 GLU N N 118.66 0.15 1 1124 . 97 ALA H H 7.80 0.03 1 1125 . 97 ALA HA H 4.18 0.03 1 1126 . 97 ALA HB H 1.50 0.03 1 1127 . 97 ALA C C 179.20 0.12 1 1128 . 97 ALA CA C 54.40 0.12 1 1129 . 97 ALA CB C 18.16 0.12 1 1130 . 97 ALA N N 120.47 0.15 1 1131 . 98 CYS H H 7.62 0.03 1 1132 . 98 CYS HA H 4.53 0.03 1 1133 . 98 CYS HB2 H 3.28 0.03 1 1134 . 98 CYS HB3 H 3.19 0.03 1 1135 . 98 CYS C C 175.33 0.12 1 1136 . 98 CYS CA C 57.40 0.12 1 1137 . 98 CYS CB C 42.40 0.12 1 1138 . 98 CYS N N 114.50 0.15 1 1139 . 99 VAL H H 7.83 0.03 1 1140 . 99 VAL HA H 3.84 0.03 1 1141 . 99 VAL HB H 2.10 0.03 1 1142 . 99 VAL HG1 H 0.84 0.03 1 1143 . 99 VAL HG2 H 0.87 0.03 1 1144 . 99 VAL C C 177.53 0.12 1 1145 . 99 VAL CA C 64.47 0.12 1 1146 . 99 VAL CB C 32.09 0.12 1 1147 . 99 VAL CG1 C 21.16 0.12 1 1148 . 99 VAL CG2 C 21.84 0.12 1 1149 . 99 VAL N N 121.27 0.15 1 1150 . 100 ILE H H 8.12 0.03 1 1151 . 100 ILE HA H 3.99 0.03 1 1152 . 100 ILE HB H 1.89 0.03 1 1153 . 100 ILE HG12 H 1.22 0.03 1 1154 . 100 ILE HG13 H 1.50 0.03 1 1155 . 100 ILE HG2 H 0.89 0.03 1 1156 . 100 ILE HD1 H 0.82 0.03 1 1157 . 100 ILE C C 176.86 0.12 1 1158 . 100 ILE CA C 62.28 0.12 1 1159 . 100 ILE CB C 38.24 0.12 1 1160 . 100 ILE CG1 C 27.96 0.12 1 1161 . 100 ILE CG2 C 17.55 0.12 1 1162 . 100 ILE CD1 C 12.83 0.12 1 1163 . 100 ILE N N 122.43 0.15 1 1164 . 101 GLN H H 8.06 0.03 1 1165 . 101 GLN HA H 4.25 0.03 1 1166 . 101 GLN HB2 H 2.07 0.03 2 1167 . 101 GLN HB3 H 2.15 0.03 2 1168 . 101 GLN HG2 H 2.43 0.03 2 1169 . 101 GLN HG3 H 2.43 0.03 2 1170 . 101 GLN HE21 H 6.89 0.03 2 1171 . 101 GLN HE22 H 7.46 0.03 2 1172 . 101 GLN C C 176.48 0.12 1 1173 . 101 GLN CA C 56.42 0.12 1 1174 . 101 GLN CB C 29.29 0.12 1 1175 . 101 GLN CG C 33.84 0.12 1 1176 . 101 GLN N N 121.38 0.15 1 1177 . 101 GLN NE2 N 111.62 0.15 1 1178 . 102 GLY H H 8.12 0.03 1 1179 . 102 GLY HA2 H 4.02 0.03 2 1180 . 102 GLY HA3 H 3.89 0.03 2 1181 . 102 GLY C C 174.14 0.12 1 1182 . 102 GLY CA C 45.53 0.12 1 1183 . 102 GLY N N 108.67 0.15 1 1184 . 103 VAL H H 8.01 0.03 1 1185 . 103 VAL HA H 4.11 0.03 1 1186 . 103 VAL HB H 2.07 0.03 1 1187 . 103 VAL HG1 H 0.92 0.03 1 1188 . 103 VAL HG2 H 0.93 0.03 1 1189 . 103 VAL C C 176.42 0.12 1 1190 . 103 VAL CA C 62.50 0.12 1 1191 . 103 VAL CB C 32.59 0.12 1 1192 . 103 VAL CG1 C 21.41 0.12 1 1193 . 103 VAL CG2 C 20.66 0.12 1 1194 . 103 VAL N N 119.43 0.15 1 1195 . 104 GLY H H 8.51 0.03 1 1196 . 104 GLY HA2 H 4.02 0.03 2 1197 . 104 GLY HA3 H 3.89 0.03 2 1198 . 104 GLY C C 174.28 0.12 1 1199 . 104 GLY CA C 45.55 0.12 1 1200 . 104 GLY N N 111.92 0.15 1 1201 . 105 VAL H H 7.86 0.03 1 1202 . 105 VAL HA H 4.19 0.03 1 1203 . 105 VAL HB H 2.11 0.03 1 1204 . 105 VAL HG1 H 0.91 0.03 1 1205 . 105 VAL HG2 H 0.89 0.03 1 1206 . 105 VAL C C 176.35 0.12 1 1207 . 105 VAL CA C 62.09 0.12 1 1208 . 105 VAL CB C 32.75 0.12 1 1209 . 105 VAL CG1 C 21.33 0.12 1 1210 . 105 VAL CG2 C 20.43 0.12 1 1211 . 105 VAL N N 118.10 0.15 1 1212 . 106 THR H H 8.21 0.03 1 1213 . 106 THR HA H 4.33 0.03 1 1214 . 106 THR HB H 4.20 0.03 1 1215 . 106 THR HG2 H 1.16 0.03 1 1216 . 106 THR C C 174.31 0.12 1 1217 . 106 THR CA C 61.97 0.12 1 1218 . 106 THR CB C 69.62 0.12 1 1219 . 106 THR CG2 C 21.67 0.12 1 1220 . 106 THR N N 116.54 0.15 1 1221 . 107 GLU H H 8.21 0.03 1 1222 . 107 GLU HA H 4.48 0.03 1 1223 . 107 GLU HB2 H 2.05 0.03 2 1224 . 107 GLU HB3 H 1.97 0.03 2 1225 . 107 GLU HG2 H 2.39 0.03 2 1226 . 107 GLU HG3 H 2.39 0.03 2 1227 . 107 GLU C C 175.77 0.12 1 1228 . 107 GLU CA C 55.74 0.12 1 1229 . 107 GLU CB C 29.66 0.12 1 1230 . 107 GLU CG C 33.55 0.12 1 1231 . 107 GLU N N 122.39 0.15 1 1232 . 108 THR H H 8.15 0.03 1 1233 . 108 THR HA H 4.59 0.03 1 1234 . 108 THR HB H 4.42 0.03 1 1235 . 108 THR HG2 H 1.29 0.03 1 1236 . 108 THR CA C 60.35 0.12 1 1237 . 108 THR CB C 68.99 0.12 1 1238 . 108 THR CG2 C 21.79 0.12 1 1239 . 108 THR N N 116.44 0.15 1 1240 . 109 PRO HA H 4.30 0.03 1 1241 . 109 PRO HB2 H 2.34 0.03 2 1242 . 109 PRO HB3 H 1.90 0.03 2 1243 . 109 PRO HG2 H 2.07 0.03 2 1244 . 109 PRO HG3 H 1.92 0.03 2 1245 . 109 PRO HD2 H 3.80 0.03 2 1246 . 109 PRO HD3 H 3.80 0.03 2 1247 . 109 PRO C C 177.89 0.12 1 1248 . 109 PRO CA C 64.58 0.12 1 1249 . 109 PRO CB C 32.00 0.12 1 1250 . 109 PRO CG C 27.58 0.12 1 1251 . 109 PRO CD C 50.91 0.12 1 1252 . 110 LEU H H 8.06 0.03 1 1253 . 110 LEU HA H 4.18 0.03 1 1254 . 110 LEU HB2 H 1.58 0.03 2 1255 . 110 LEU HB3 H 1.58 0.03 2 1256 . 110 LEU HD1 H 0.89 0.03 1 1257 . 110 LEU HD2 H 0.85 0.03 1 1258 . 110 LEU C C 177.99 0.12 1 1259 . 110 LEU CA C 56.74 0.12 1 1260 . 110 LEU CB C 42.08 0.12 1 1261 . 110 LEU CG C 26.99 0.12 1 1262 . 110 LEU CD1 C 24.38 0.12 1 1263 . 110 LEU CD2 C 24.21 0.12 1 1264 . 110 LEU N N 119.37 0.15 1 1265 . 111 MET H H 7.88 0.03 1 1266 . 111 MET HA H 4.28 0.03 1 1267 . 111 MET HB2 H 2.08 0.03 2 1268 . 111 MET HB3 H 2.08 0.03 2 1269 . 111 MET HG2 H 2.55 0.03 2 1270 . 111 MET HG3 H 2.55 0.03 2 1271 . 111 MET HE H 2.08 0.03 1 1272 . 111 MET C C 177.64 0.12 1 1273 . 111 MET CA C 57.15 0.12 1 1274 . 111 MET CB C 32.75 0.12 1 1275 . 111 MET CG C 32.37 0.12 1 1276 . 111 MET CE C 17.21 0.12 1 1277 . 111 MET N N 119.03 0.15 1 1278 . 112 LYS H H 8.17 0.03 1 1279 . 112 LYS HA H 4.15 0.03 1 1280 . 112 LYS HB2 H 1.89 0.03 2 1281 . 112 LYS HB3 H 1.79 0.03 2 1282 . 112 LYS HE2 H 2.73 0.03 2 1283 . 112 LYS HE3 H 2.73 0.03 2 1284 . 112 LYS C C 178.27 0.12 1 1285 . 112 LYS CA C 56.56 0.12 1 1286 . 112 LYS CB C 38.34 0.12 1 1287 . 112 LYS N N 120.67 0.15 1 1288 . 113 GLU H H 8.31 0.03 1 1289 . 113 GLU HA H 4.14 0.03 1 1290 . 113 GLU HB2 H 2.07 0.03 2 1291 . 113 GLU HB3 H 2.07 0.03 2 1292 . 113 GLU HG2 H 2.41 0.03 2 1293 . 113 GLU HG3 H 2.36 0.03 2 1294 . 113 GLU C C 177.75 0.12 1 1295 . 113 GLU CA C 57.93 0.12 1 1296 . 113 GLU CB C 28.74 0.12 1 1297 . 113 GLU CG C 33.73 0.12 1 1298 . 113 GLU N N 120.48 0.15 1 1299 . 114 ASP H H 8.60 0.03 1 1300 . 114 ASP HA H 4.42 0.03 1 1301 . 114 ASP HB2 H 2.76 0.03 2 1302 . 114 ASP HB3 H 2.76 0.03 2 1303 . 114 ASP C C 179.01 0.12 1 1304 . 114 ASP CA C 56.52 0.12 1 1305 . 114 ASP CB C 39.28 0.12 1 1306 . 114 ASP N N 119.38 0.15 1 1307 . 115 SER H H 8.14 0.03 1 1308 . 115 SER HA H 4.21 0.03 1 1309 . 115 SER HB2 H 3.80 0.03 2 1310 . 115 SER HB3 H 3.80 0.03 2 1311 . 115 SER C C 176.04 0.12 1 1312 . 115 SER CA C 61.46 0.12 1 1313 . 115 SER CB C 62.84 0.12 1 1314 . 115 SER N N 117.53 0.15 1 1315 . 116 ILE H H 7.63 0.03 1 1316 . 116 ILE HA H 3.67 0.03 1 1317 . 116 ILE HB H 2.06 0.03 1 1318 . 116 ILE HG12 H 1.21 0.03 1 1319 . 116 ILE HG13 H 1.62 0.03 1 1320 . 116 ILE HG2 H 0.83 0.03 1 1321 . 116 ILE HD1 H 0.78 0.03 1 1322 . 116 ILE C C 178.59 0.12 1 1323 . 116 ILE CA C 64.52 0.12 1 1324 . 116 ILE CB C 37.35 0.12 1 1325 . 116 ILE CG1 C 29.02 0.12 1 1326 . 116 ILE CG2 C 17.11 0.12 1 1327 . 116 ILE CD1 C 12.59 0.12 1 1328 . 116 ILE N N 122.40 0.15 1 1329 . 117 LEU H H 8.28 0.03 1 1330 . 117 LEU HA H 4.03 0.03 1 1331 . 117 LEU HB2 H 1.68 0.03 2 1332 . 117 LEU HB3 H 1.85 0.03 2 1333 . 117 LEU HG H 1.74 0.03 1 1334 . 117 LEU HD1 H 0.96 0.03 1 1335 . 117 LEU HD2 H 0.91 0.03 1 1336 . 117 LEU C C 178.89 0.12 1 1337 . 117 LEU CA C 57.95 0.12 1 1338 . 117 LEU CB C 41.34 0.12 1 1339 . 117 LEU CG C 26.86 0.12 1 1340 . 117 LEU CD1 C 24.32 0.12 1 1341 . 117 LEU CD2 C 23.87 0.12 1 1342 . 117 LEU N N 120.68 0.15 1 1343 . 118 ALA H H 7.97 0.03 1 1344 . 118 ALA HA H 4.16 0.03 1 1345 . 118 ALA HB H 1.52 0.03 1 1346 . 118 ALA C C 181.68 0.12 1 1347 . 118 ALA CA C 55.70 0.12 1 1348 . 118 ALA CB C 18.10 0.12 1 1349 . 118 ALA N N 120.07 0.15 1 1350 . 119 VAL H H 7.63 0.03 1 1351 . 119 VAL HA H 3.81 0.03 1 1352 . 119 VAL HB H 2.52 0.03 1 1353 . 119 VAL HG1 H 1.36 0.03 1 1354 . 119 VAL HG2 H 1.26 0.03 1 1355 . 119 VAL C C 177.91 0.12 1 1356 . 119 VAL CA C 67.38 0.12 1 1357 . 119 VAL CB C 32.07 0.12 1 1358 . 119 VAL CG1 C 22.52 0.12 1 1359 . 119 VAL CG2 C 23.86 0.12 1 1360 . 119 VAL N N 118.66 0.15 1 1361 . 120 ARG H H 8.57 0.03 1 1362 . 120 ARG HA H 4.04 0.03 1 1363 . 120 ARG HB2 H 2.10 0.03 2 1364 . 120 ARG HB3 H 2.10 0.03 2 1365 . 120 ARG HG2 H 1.94 0.03 2 1366 . 120 ARG HG3 H 1.94 0.03 2 1367 . 120 ARG C C 179.92 0.12 1 1368 . 120 ARG CA C 61.83 0.12 1 1369 . 120 ARG CB C 29.86 0.12 1 1370 . 120 ARG N N 121.04 0.15 1 1371 . 121 LYS H H 8.98 0.03 1 1372 . 121 LYS HA H 4.12 0.03 1 1373 . 121 LYS HB2 H 1.98 0.03 2 1374 . 121 LYS HB3 H 1.98 0.03 2 1375 . 121 LYS HE2 H 3.41 0.03 2 1376 . 121 LYS HE3 H 3.41 0.03 2 1377 . 121 LYS C C 178.56 0.12 1 1378 . 121 LYS CA C 59.90 0.12 1 1379 . 121 LYS CB C 32.37 0.12 1 1380 . 121 LYS CG C 29.49 0.12 1 1381 . 121 LYS N N 119.40 0.15 1 1382 . 122 TYR H H 7.52 0.03 1 1383 . 122 TYR HA H 4.34 0.03 1 1384 . 122 TYR HB2 H 3.62 0.03 1 1385 . 122 TYR HB3 H 3.18 0.03 1 1386 . 122 TYR HD1 H 6.98 0.03 3 1387 . 122 TYR HD2 H 6.98 0.03 3 1388 . 122 TYR C C 176.59 0.12 1 1389 . 122 TYR CA C 60.84 0.12 1 1390 . 122 TYR CB C 38.06 0.12 1 1391 . 122 TYR N N 121.28 0.15 1 1392 . 123 PHE H H 7.95 0.03 1 1393 . 123 PHE HA H 3.76 0.03 1 1394 . 123 PHE HB2 H 2.94 0.03 1 1395 . 123 PHE HB3 H 3.22 0.03 1 1396 . 123 PHE HD1 H 7.58 0.03 3 1397 . 123 PHE HD2 H 7.58 0.03 3 1398 . 123 PHE HE1 H 7.44 0.03 3 1399 . 123 PHE HE2 H 7.44 0.03 3 1400 . 123 PHE C C 179.08 0.12 1 1401 . 123 PHE CA C 63.31 0.12 1 1402 . 123 PHE CB C 39.23 0.12 1 1403 . 123 PHE N N 115.66 0.15 1 1404 . 124 GLN H H 8.45 0.03 1 1405 . 124 GLN HA H 4.21 0.03 1 1406 . 124 GLN HB2 H 2.42 0.03 1 1407 . 124 GLN HB3 H 2.23 0.03 1 1408 . 124 GLN HG2 H 2.60 0.03 2 1409 . 124 GLN HG3 H 2.41 0.03 2 1410 . 124 GLN HE21 H 6.80 0.03 2 1411 . 124 GLN HE22 H 7.48 0.03 2 1412 . 124 GLN C C 178.87 0.12 1 1413 . 124 GLN CA C 59.32 0.12 1 1414 . 124 GLN CB C 27.81 0.12 1 1415 . 124 GLN CG C 34.05 0.12 1 1416 . 124 GLN N N 122.75 0.15 1 1417 . 124 GLN NE2 N 110.53 0.15 1 1418 . 125 ARG H H 8.14 0.03 1 1419 . 125 ARG HA H 4.10 0.03 1 1420 . 125 ARG HB2 H 2.60 0.03 1 1421 . 125 ARG HB3 H 1.96 0.03 1 1422 . 125 ARG C C 180.38 0.12 1 1423 . 125 ARG CA C 61.02 0.12 1 1424 . 125 ARG CB C 30.39 0.12 1 1425 . 125 ARG N N 119.93 0.15 1 1426 . 126 ILE H H 7.54 0.03 1 1427 . 126 ILE HA H 3.39 0.03 1 1428 . 126 ILE HB H 1.69 0.03 1 1429 . 126 ILE HG12 H -0.54 0.03 1 1430 . 126 ILE HG13 H 0.74 0.03 1 1431 . 126 ILE HG2 H 0.55 0.03 1 1432 . 126 ILE HD1 H -0.45 0.03 1 1433 . 126 ILE C C 176.91 0.12 1 1434 . 126 ILE CA C 65.71 0.12 1 1435 . 126 ILE CB C 37.69 0.12 1 1436 . 126 ILE CG1 C 28.60 0.12 1 1437 . 126 ILE CG2 C 18.81 0.12 1 1438 . 126 ILE CD1 C 12.15 0.12 1 1439 . 126 ILE N N 121.56 0.15 1 1440 . 127 THR H H 8.28 0.03 1 1441 . 127 THR HA H 3.66 0.03 1 1442 . 127 THR HB H 4.26 0.03 1 1443 . 127 THR HG2 H 1.27 0.03 1 1444 . 127 THR C C 176.74 0.12 1 1445 . 127 THR CA C 67.69 0.12 1 1446 . 127 THR CB C 68.65 0.12 1 1447 . 127 THR CG2 C 21.97 0.12 1 1448 . 127 THR N N 115.32 0.15 1 1449 . 128 LEU H H 8.28 0.03 1 1450 . 128 LEU HA H 3.99 0.03 1 1451 . 128 LEU HB2 H 1.73 0.03 2 1452 . 128 LEU HB3 H 1.64 0.03 2 1453 . 128 LEU HG H 1.67 0.03 1 1454 . 128 LEU HD1 H 0.88 0.03 2 1455 . 128 LEU HD2 H 0.86 0.03 2 1456 . 128 LEU C C 178.45 0.12 1 1457 . 128 LEU CA C 58.16 0.12 1 1458 . 128 LEU CB C 41.74 0.12 1 1459 . 128 LEU CG C 27.08 0.12 1 1460 . 128 LEU CD1 C 24.35 0.12 2 1461 . 128 LEU CD2 C 24.25 0.12 2 1462 . 128 LEU N N 122.28 0.15 1 1463 . 129 TYR H H 7.52 0.03 1 1464 . 129 TYR HA H 3.99 0.03 1 1465 . 129 TYR HB2 H 2.80 0.03 1 1466 . 129 TYR HB3 H 3.30 0.03 1 1467 . 129 TYR HD1 H 6.43 0.03 3 1468 . 129 TYR HD2 H 6.43 0.03 3 1469 . 129 TYR HE1 H 6.45 0.03 3 1470 . 129 TYR HE2 H 6.45 0.03 3 1471 . 129 TYR C C 176.15 0.12 1 1472 . 129 TYR CA C 60.99 0.12 1 1473 . 129 TYR CB C 38.95 0.12 1 1474 . 129 TYR CD1 C 133.20 0.12 3 1475 . 129 TYR CD2 C 133.20 0.12 3 1476 . 129 TYR CE1 C 118.20 0.12 3 1477 . 129 TYR CE2 C 118.20 0.12 3 1478 . 129 TYR N N 120.69 0.15 1 1479 . 130 LEU H H 7.72 0.03 1 1480 . 130 LEU HA H 2.88 0.03 1 1481 . 130 LEU HB2 H 1.33 0.03 1 1482 . 130 LEU HB3 H 0.33 0.03 1 1483 . 130 LEU HG H 1.21 0.03 1 1484 . 130 LEU HD1 H -0.01 0.03 1 1485 . 130 LEU HD2 H -0.45 0.03 1 1486 . 130 LEU C C 177.99 0.12 1 1487 . 130 LEU CA C 58.37 0.12 1 1488 . 130 LEU CB C 41.43 0.12 1 1489 . 130 LEU CG C 26.70 0.12 1 1490 . 130 LEU CD1 C 25.30 0.12 1 1491 . 130 LEU CD2 C 21.70 0.12 1 1492 . 130 LEU N N 118.87 0.15 1 1493 . 131 LYS H H 7.49 0.03 1 1494 . 131 LYS HA H 3.47 0.03 1 1495 . 131 LYS HB2 H 1.83 0.03 2 1496 . 131 LYS HB3 H 1.79 0.03 2 1497 . 131 LYS HG2 H 1.37 0.03 2 1498 . 131 LYS HG3 H 1.54 0.03 2 1499 . 131 LYS HD2 H 1.65 0.03 2 1500 . 131 LYS HD3 H 1.65 0.03 2 1501 . 131 LYS HE2 H 2.95 0.03 2 1502 . 131 LYS HE3 H 2.95 0.03 2 1503 . 131 LYS C C 181.29 0.12 1 1504 . 131 LYS CA C 59.68 0.12 1 1505 . 131 LYS CB C 32.74 0.12 1 1506 . 131 LYS CG C 25.61 0.12 1 1507 . 131 LYS CD C 29.72 0.12 1 1508 . 131 LYS CE C 42.05 0.12 1 1509 . 131 LYS N N 116.45 0.15 1 1510 . 132 GLU H H 8.42 0.03 1 1511 . 132 GLU HA H 3.87 0.03 1 1512 . 132 GLU HB2 H 2.07 0.03 2 1513 . 132 GLU HB3 H 1.92 0.03 2 1514 . 132 GLU HG2 H 2.27 0.03 2 1515 . 132 GLU HG3 H 2.42 0.03 2 1516 . 132 GLU C C 178.52 0.12 1 1517 . 132 GLU CA C 58.94 0.12 1 1518 . 132 GLU CB C 28.35 0.12 1 1519 . 132 GLU CG C 34.86 0.12 1 1520 . 132 GLU N N 121.90 0.15 1 1521 . 133 LYS H H 7.41 0.03 1 1522 . 133 LYS HA H 3.99 0.03 1 1523 . 133 LYS HB2 H 1.04 0.03 1 1524 . 133 LYS HB3 H 1.72 0.03 1 1525 . 133 LYS HG2 H 1.28 0.03 2 1526 . 133 LYS HG3 H 1.12 0.03 2 1527 . 133 LYS HD2 H 0.78 0.03 2 1528 . 133 LYS HD3 H 0.40 0.03 2 1529 . 133 LYS HE2 H 2.68 0.03 2 1530 . 133 LYS HE3 H 2.68 0.03 2 1531 . 133 LYS C C 175.39 0.12 1 1532 . 133 LYS CA C 54.45 0.12 1 1533 . 133 LYS CB C 32.09 0.12 1 1534 . 133 LYS CG C 27.87 0.12 1 1535 . 133 LYS CD C 23.50 0.12 1 1536 . 133 LYS CE C 42.54 0.12 1 1537 . 133 LYS N N 115.70 0.15 1 1538 . 134 LYS H H 7.73 0.03 1 1539 . 134 LYS HA H 3.64 0.03 1 1540 . 134 LYS HB2 H 1.92 0.03 2 1541 . 134 LYS HB3 H 1.92 0.03 2 1542 . 134 LYS HG2 H 1.29 0.03 2 1543 . 134 LYS HG3 H 1.29 0.03 2 1544 . 134 LYS HD2 H 1.63 0.03 2 1545 . 134 LYS HD3 H 1.63 0.03 2 1546 . 134 LYS HE2 H 2.98 0.03 2 1547 . 134 LYS HE3 H 2.98 0.03 2 1548 . 134 LYS C C 176.35 0.12 1 1549 . 134 LYS CA C 57.45 0.12 1 1550 . 134 LYS CB C 29.01 0.12 1 1551 . 134 LYS CG C 25.20 0.12 1 1552 . 134 LYS N N 117.51 0.15 1 1553 . 135 TYR H H 8.44 0.03 1 1554 . 135 TYR HA H 2.92 0.03 1 1555 . 135 TYR HB2 H 2.98 0.03 1 1556 . 135 TYR HB3 H 3.37 0.03 1 1557 . 135 TYR HD1 H 6.66 0.03 3 1558 . 135 TYR HD2 H 6.66 0.03 3 1559 . 135 TYR HE1 H 6.55 0.03 3 1560 . 135 TYR HE2 H 6.55 0.03 3 1561 . 135 TYR C C 174.21 0.12 1 1562 . 135 TYR CA C 59.81 0.12 1 1563 . 135 TYR CB C 34.85 0.12 1 1564 . 135 TYR CD1 C 133.30 0.12 3 1565 . 135 TYR CD2 C 133.30 0.12 3 1566 . 135 TYR CE1 C 118.50 0.12 3 1567 . 135 TYR CE2 C 118.50 0.12 3 1568 . 135 TYR N N 110.25 0.15 1 1569 . 136 SER H H 6.75 0.03 1 1570 . 136 SER HA H 4.55 0.03 1 1571 . 136 SER HB2 H 4.41 0.03 1 1572 . 136 SER HB3 H 4.02 0.03 1 1573 . 136 SER CA C 57.27 0.12 1 1574 . 136 SER CB C 62.59 0.12 1 1575 . 136 SER N N 113.34 0.15 1 1576 . 137 PRO HA H 4.34 0.03 1 1577 . 137 PRO HB2 H 2.17 0.03 2 1578 . 137 PRO HB3 H 2.17 0.03 2 1579 . 137 PRO HD2 H 3.93 0.03 2 1580 . 137 PRO HD3 H 3.93 0.03 2 1581 . 137 PRO C C 180.71 0.12 1 1582 . 137 PRO CA C 66.33 0.12 1 1583 . 137 PRO CB C 32.18 0.12 1 1584 . 137 PRO CD C 50.10 0.12 1 1585 . 138 CYS H H 8.56 0.03 1 1586 . 138 CYS HA H 4.72 0.03 1 1587 . 138 CYS HB2 H 2.95 0.03 1 1588 . 138 CYS HB3 H 2.80 0.03 1 1589 . 138 CYS C C 176.12 0.12 1 1590 . 138 CYS CA C 57.40 0.12 1 1591 . 138 CYS CB C 36.84 0.12 1 1592 . 138 CYS N N 113.58 0.15 1 1593 . 139 ALA H H 8.11 0.03 1 1594 . 139 ALA HA H 4.49 0.03 1 1595 . 139 ALA HB H 1.08 0.03 1 1596 . 139 ALA C C 180.26 0.12 1 1597 . 139 ALA CA C 54.84 0.12 1 1598 . 139 ALA CB C 19.00 0.12 1 1599 . 139 ALA N N 124.94 0.15 1 1600 . 140 TRP H H 8.52 0.03 1 1601 . 140 TRP HA H 4.63 0.03 1 1602 . 140 TRP HB2 H 3.40 0.03 1 1603 . 140 TRP HB3 H 2.91 0.03 1 1604 . 140 TRP HD1 H 6.80 0.03 1 1605 . 140 TRP HE1 H 9.63 0.03 1 1606 . 140 TRP HE3 H 8.23 0.03 1 1607 . 140 TRP HZ2 H 7.01 0.03 1 1608 . 140 TRP HZ3 H 6.46 0.03 1 1609 . 140 TRP HH2 H 7.02 0.03 1 1610 . 140 TRP C C 179.14 0.12 1 1611 . 140 TRP CA C 60.28 0.12 1 1612 . 140 TRP CB C 29.95 0.12 1 1613 . 140 TRP CD1 C 127.20 0.12 1 1614 . 140 TRP CE3 C 121.90 0.12 1 1615 . 140 TRP CZ2 C 114.65 0.12 1 1616 . 140 TRP CZ3 C 120.40 0.12 1 1617 . 140 TRP CH2 C 124.65 0.12 1 1618 . 140 TRP N N 116.19 0.15 1 1619 . 140 TRP NE1 N 126.56 0.15 1 1620 . 141 GLU H H 8.18 0.03 1 1621 . 141 GLU HA H 5.30 0.03 1 1622 . 141 GLU HB2 H 2.20 0.03 1 1623 . 141 GLU HB3 H 2.13 0.03 1 1624 . 141 GLU HG2 H 2.42 0.03 1 1625 . 141 GLU HG3 H 2.42 0.03 1 1626 . 141 GLU C C 178.17 0.12 1 1627 . 141 GLU CA C 57.90 0.12 1 1628 . 141 GLU CB C 28.17 0.12 1 1629 . 141 GLU CG C 34.75 0.12 1 1630 . 141 GLU N N 121.34 0.15 1 1631 . 142 VAL H H 8.64 0.03 1 1632 . 142 VAL HA H 3.67 0.03 1 1633 . 142 VAL HB H 2.72 0.03 1 1634 . 142 VAL HG1 H 1.05 0.03 1 1635 . 142 VAL HG2 H 0.99 0.03 1 1636 . 142 VAL C C 180.37 0.12 1 1637 . 142 VAL CA C 67.03 0.12 1 1638 . 142 VAL CB C 31.78 0.12 1 1639 . 142 VAL CG1 C 20.68 0.12 1 1640 . 142 VAL CG2 C 23.23 0.12 1 1641 . 142 VAL N N 120.89 0.15 1 1642 . 143 VAL H H 8.33 0.03 1 1643 . 143 VAL HA H 3.35 0.03 1 1644 . 143 VAL HB H 2.47 0.03 1 1645 . 143 VAL HG1 H 0.88 0.03 1 1646 . 143 VAL HG2 H 0.92 0.03 1 1647 . 143 VAL C C 176.51 0.12 1 1648 . 143 VAL CA C 67.85 0.12 1 1649 . 143 VAL CB C 31.77 0.12 1 1650 . 143 VAL CG1 C 22.32 0.12 1 1651 . 143 VAL CG2 C 25.30 0.12 1 1652 . 143 VAL N N 119.84 0.15 1 1653 . 144 ARG H H 9.64 0.03 1 1654 . 144 ARG HA H 3.72 0.03 1 1655 . 144 ARG HB2 H 2.48 0.03 1 1656 . 144 ARG HB3 H 2.26 0.03 1 1657 . 144 ARG C C 178.25 0.12 1 1658 . 144 ARG CA C 61.12 0.12 1 1659 . 144 ARG CB C 29.87 0.12 1 1660 . 144 ARG N N 123.75 0.15 1 1661 . 145 ALA H H 8.87 0.03 1 1662 . 145 ALA HA H 3.90 0.03 1 1663 . 145 ALA HB H 1.55 0.03 1 1664 . 145 ALA C C 180.82 0.12 1 1665 . 145 ALA CA C 55.51 0.12 1 1666 . 145 ALA CB C 18.31 0.12 1 1667 . 145 ALA N N 119.07 0.15 1 1668 . 146 GLU H H 8.12 0.03 1 1669 . 146 GLU HA H 4.23 0.03 1 1670 . 146 GLU HB2 H 2.08 0.03 1 1671 . 146 GLU HB3 H 2.30 0.03 1 1672 . 146 GLU HG2 H 2.29 0.03 2 1673 . 146 GLU HG3 H 2.29 0.03 2 1674 . 146 GLU C C 177.40 0.12 1 1675 . 146 GLU CA C 58.51 0.12 1 1676 . 146 GLU CB C 28.10 0.12 1 1677 . 146 GLU CG C 33.33 0.12 1 1678 . 146 GLU N N 121.49 0.15 1 1679 . 147 ILE H H 8.76 0.03 1 1680 . 147 ILE HA H 3.99 0.03 1 1681 . 147 ILE HB H 2.25 0.03 1 1682 . 147 ILE HG12 H 1.78 0.03 1 1683 . 147 ILE HG13 H 1.52 0.03 1 1684 . 147 ILE HG2 H 0.99 0.03 1 1685 . 147 ILE HD1 H 0.85 0.03 1 1686 . 147 ILE C C 178.30 0.12 1 1687 . 147 ILE CA C 61.47 0.12 1 1688 . 147 ILE CB C 35.49 0.12 1 1689 . 147 ILE CG1 C 28.20 0.12 1 1690 . 147 ILE CG2 C 18.26 0.12 1 1691 . 147 ILE CD1 C 11.11 0.12 1 1692 . 147 ILE N N 119.17 0.15 1 1693 . 148 MET H H 8.47 0.03 1 1694 . 148 MET HA H 3.83 0.03 1 1695 . 148 MET HB2 H 2.21 0.03 1 1696 . 148 MET HB3 H 2.05 0.03 1 1697 . 148 MET HG2 H 2.55 0.03 2 1698 . 148 MET HG3 H 2.36 0.03 2 1699 . 148 MET HE H 2.10 0.03 1 1700 . 148 MET C C 178.27 0.12 1 1701 . 148 MET CA C 60.49 0.12 1 1702 . 148 MET CB C 32.65 0.12 1 1703 . 148 MET CG C 32.79 0.12 1 1704 . 148 MET CE C 17.46 0.12 1 1705 . 148 MET N N 119.23 0.15 1 1706 . 149 ARG H H 7.65 0.03 1 1707 . 149 ARG HA H 3.97 0.03 1 1708 . 149 ARG HB2 H 2.09 0.03 1 1709 . 149 ARG HB3 H 1.91 0.03 1 1710 . 149 ARG HG2 H 1.34 0.03 2 1711 . 149 ARG HG3 H 1.66 0.03 2 1712 . 149 ARG HD2 H 3.15 0.03 2 1713 . 149 ARG HD3 H 3.31 0.03 2 1714 . 149 ARG C C 179.04 0.12 1 1715 . 149 ARG CA C 59.54 0.12 1 1716 . 149 ARG CB C 30.38 0.12 1 1717 . 149 ARG CG C 27.37 0.12 1 1718 . 149 ARG CD C 43.18 0.12 1 1719 . 149 ARG N N 119.40 0.15 1 1720 . 150 SER H H 9.17 0.03 1 1721 . 150 SER HA H 3.37 0.03 1 1722 . 150 SER HB2 H 2.26 0.03 2 1723 . 150 SER HB3 H 2.78 0.03 2 1724 . 150 SER C C 177.31 0.12 1 1725 . 150 SER CA C 61.39 0.12 1 1726 . 150 SER CB C 60.65 0.12 1 1727 . 150 SER N N 117.79 0.15 1 1728 . 151 PHE H H 9.49 0.03 1 1729 . 151 PHE HA H 4.05 0.03 1 1730 . 151 PHE HB2 H 3.02 0.03 2 1731 . 151 PHE HB3 H 3.02 0.03 2 1732 . 151 PHE HD1 H 6.92 0.03 3 1733 . 151 PHE HD2 H 6.92 0.03 3 1734 . 151 PHE HE1 H 7.24 0.03 3 1735 . 151 PHE HE2 H 7.24 0.03 3 1736 . 151 PHE HZ H 7.31 0.03 1 1737 . 151 PHE C C 178.81 0.12 1 1738 . 151 PHE CA C 61.60 0.12 1 1739 . 151 PHE CB C 39.34 0.12 1 1740 . 151 PHE N N 124.78 0.15 1 1741 . 152 SER H H 7.85 0.03 1 1742 . 152 SER HA H 3.99 0.03 1 1743 . 152 SER HB2 H 3.95 0.03 2 1744 . 152 SER HB3 H 3.95 0.03 2 1745 . 152 SER C C 175.95 0.12 1 1746 . 152 SER CA C 62.15 0.12 1 1747 . 152 SER CB C 62.65 0.12 1 1748 . 152 SER N N 115.54 0.15 1 1749 . 153 LEU H H 7.76 0.03 1 1750 . 153 LEU HA H 4.10 0.03 1 1751 . 153 LEU HB2 H 1.74 0.03 1 1752 . 153 LEU HB3 H 1.48 0.03 1 1753 . 153 LEU HD1 H 0.82 0.03 1 1754 . 153 LEU HD2 H 0.85 0.03 1 1755 . 153 LEU C C 179.56 0.12 1 1756 . 153 LEU CA C 57.78 0.12 1 1757 . 153 LEU CB C 42.36 0.12 1 1758 . 153 LEU CG C 25.52 0.12 1 1759 . 153 LEU CD1 C 25.60 0.12 1 1760 . 153 LEU CD2 C 23.52 0.12 1 1761 . 153 LEU N N 121.18 0.15 1 1762 . 154 SER H H 7.88 0.03 1 1763 . 154 SER HA H 3.82 0.03 1 1764 . 154 SER HB2 H 3.45 0.03 2 1765 . 154 SER HB3 H 3.36 0.03 2 1766 . 154 SER C C 174.34 0.12 1 1767 . 154 SER CA C 61.50 0.12 1 1768 . 154 SER CB C 63.12 0.12 1 1769 . 154 SER N N 113.70 0.15 1 1770 . 155 THR H H 7.20 0.03 1 1771 . 155 THR HA H 4.09 0.03 1 1772 . 155 THR HB H 4.06 0.03 1 1773 . 155 THR HG2 H 0.67 0.03 1 1774 . 155 THR C C 174.91 0.12 1 1775 . 155 THR CA C 62.33 0.12 1 1776 . 155 THR CB C 69.40 0.12 1 1777 . 155 THR CG2 C 21.67 0.12 1 1778 . 155 THR N N 109.53 0.15 1 1779 . 156 ASN H H 7.77 0.03 1 1780 . 156 ASN HA H 4.58 0.03 1 1781 . 156 ASN HB2 H 2.94 0.03 2 1782 . 156 ASN HB3 H 2.74 0.03 2 1783 . 156 ASN HD21 H 6.82 0.03 2 1784 . 156 ASN HD22 H 7.49 0.03 2 1785 . 156 ASN C C 175.76 0.12 1 1786 . 156 ASN CA C 54.39 0.12 1 1787 . 156 ASN CB C 38.33 0.12 1 1788 . 156 ASN N N 119.39 0.15 1 1789 . 156 ASN ND2 N 111.60 0.15 1 1790 . 157 LEU H H 8.11 0.03 1 1791 . 157 LEU HA H 4.27 0.03 1 1792 . 157 LEU HB2 H 1.59 0.03 2 1793 . 157 LEU HB3 H 1.59 0.03 2 1794 . 157 LEU HG H 1.67 0.03 1 1795 . 157 LEU HD1 H 0.81 0.03 1 1796 . 157 LEU HD2 H 0.79 0.03 1 1797 . 157 LEU C C 177.83 0.12 1 1798 . 157 LEU CA C 55.83 0.12 1 1799 . 157 LEU CB C 42.42 0.12 1 1800 . 157 LEU CG C 25.31 0.12 1 1801 . 157 LEU CD1 C 25.46 0.12 1 1802 . 157 LEU CD2 C 23.80 0.12 1 1803 . 157 LEU N N 120.38 0.15 1 1804 . 158 GLN H H 8.23 0.03 1 1805 . 158 GLN HA H 4.13 0.03 1 1806 . 158 GLN HB2 H 1.98 0.03 2 1807 . 158 GLN HB3 H 2.08 0.03 2 1808 . 158 GLN HG2 H 2.31 0.03 2 1809 . 158 GLN HG3 H 2.31 0.03 2 1810 . 158 GLN HE21 H 6.77 0.03 2 1811 . 158 GLN HE22 H 7.43 0.03 2 1812 . 158 GLN C C 177.56 0.12 1 1813 . 158 GLN CA C 57.10 0.12 1 1814 . 158 GLN CB C 29.01 0.12 1 1815 . 158 GLN CG C 32.20 0.12 1 1816 . 158 GLN N N 119.58 0.15 1 1817 . 158 GLN NE2 N 111.26 0.15 1 1818 . 159 GLU H H 8.28 0.03 1 1819 . 159 GLU HA H 4.23 0.03 1 1820 . 159 GLU HB2 H 2.05 0.03 2 1821 . 159 GLU HB3 H 1.98 0.03 2 1822 . 159 GLU HG2 H 2.36 0.03 2 1823 . 159 GLU HG3 H 2.36 0.03 2 1824 . 159 GLU C C 176.89 0.12 1 1825 . 159 GLU CA C 57.00 0.12 1 1826 . 159 GLU CB C 29.32 0.12 1 1827 . 159 GLU CG C 34.71 0.12 1 1828 . 159 GLU N N 119.96 0.15 1 1829 . 160 SER H H 8.15 0.03 1 1830 . 160 SER HA H 4.37 0.03 1 1831 . 160 SER HB2 H 3.87 0.03 2 1832 . 160 SER HB3 H 3.87 0.03 2 1833 . 160 SER C C 174.75 0.12 1 1834 . 160 SER CA C 59.10 0.12 1 1835 . 160 SER CB C 63.68 0.12 1 1836 . 160 SER N N 115.61 0.15 1 1837 . 161 LEU H H 8.00 0.03 1 1838 . 161 LEU HA H 4.32 0.03 1 1839 . 161 LEU HB2 H 1.64 0.03 2 1840 . 161 LEU HB3 H 1.52 0.03 2 1841 . 161 LEU HG H 1.66 0.03 1 1842 . 161 LEU HD1 H 0.87 0.03 1 1843 . 161 LEU HD2 H 0.83 0.03 1 1844 . 161 LEU C C 177.34 0.12 1 1845 . 161 LEU CA C 55.43 0.12 1 1846 . 161 LEU CB C 42.45 0.12 1 1847 . 161 LEU CG C 27.06 0.12 1 1848 . 161 LEU CD1 C 25.23 0.12 1 1849 . 161 LEU CD2 C 23.29 0.12 1 1850 . 161 LEU N N 122.82 0.15 1 1851 . 162 ARG H H 8.06 0.03 1 1852 . 162 ARG HA H 4.31 0.03 1 1853 . 162 ARG HB2 H 1.85 0.03 2 1854 . 162 ARG HB3 H 1.75 0.03 2 1855 . 162 ARG HG2 H 1.62 0.03 2 1856 . 162 ARG HG3 H 1.62 0.03 2 1857 . 162 ARG HD2 H 3.17 0.03 2 1858 . 162 ARG HD3 H 3.17 0.03 2 1859 . 162 ARG C C 176.35 0.12 1 1860 . 162 ARG CA C 56.18 0.12 1 1861 . 162 ARG CB C 30.80 0.12 1 1862 . 162 ARG CG C 27.01 0.12 1 1863 . 162 ARG CD C 43.30 0.12 1 1864 . 162 ARG N N 120.43 0.15 1 1865 . 163 SER H H 8.21 0.03 1 1866 . 163 SER HA H 4.39 0.03 1 1867 . 163 SER HB2 H 3.85 0.03 2 1868 . 163 SER HB3 H 3.85 0.03 2 1869 . 163 SER C C 174.24 0.12 1 1870 . 163 SER CA C 58.64 0.12 1 1871 . 163 SER CB C 63.87 0.12 1 1872 . 163 SER N N 116.54 0.15 1 1873 . 164 LYS H H 8.25 0.03 1 1874 . 164 LYS HA H 4.31 0.03 1 1875 . 164 LYS HB2 H 1.84 0.03 2 1876 . 164 LYS HB3 H 1.72 0.03 2 1877 . 164 LYS HG2 H 1.41 0.03 2 1878 . 164 LYS HG3 H 1.41 0.03 2 1879 . 164 LYS HD2 H 1.65 0.03 2 1880 . 164 LYS HD3 H 1.65 0.03 2 1881 . 164 LYS HE2 H 2.97 0.03 2 1882 . 164 LYS HE3 H 2.97 0.03 2 1883 . 164 LYS C C 175.66 0.12 1 1884 . 164 LYS CA C 56.42 0.12 1 1885 . 164 LYS CB C 33.07 0.12 1 1886 . 164 LYS CG C 24.67 0.12 1 1887 . 164 LYS CD C 29.00 0.12 1 1888 . 164 LYS CE C 42.13 0.12 1 1889 . 164 LYS N N 122.82 0.15 1 1890 . 165 GLU H H 7.99 0.03 1 1891 . 165 GLU HA H 4.14 0.03 1 1892 . 165 GLU HB2 H 2.07 0.03 2 1893 . 165 GLU HB3 H 1.89 0.03 2 1894 . 165 GLU HG2 H 2.33 0.03 2 1895 . 165 GLU HG3 H 2.33 0.03 2 1896 . 165 GLU CA C 57.24 0.12 1 1897 . 165 GLU CB C 29.90 0.12 1 1898 . 165 GLU CG C 34.31 0.12 1 1899 . 165 GLU N N 125.78 0.15 1 stop_ save_