data_18344 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Gal-GalNac-Interferon Alpha-2a ; _BMRB_accession_number 18344 _BMRB_flat_file_name bmr18344.str _Entry_type original _Submission_date 2012-03-21 _Accession_date 2012-03-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Interferon Alpha-2a, where Thr106 is glycosylated with a 2-unit saccharide moiety, a Gal-GalNac.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ghasriani Houman . . 2 Belcourt Pascal 'J. F.' . 3 Sauve Simon . . 4 Hodgson Derek J. . 5 Gingras Genevieve . . 6 Brochu Denis . . 7 Gilbert Michel . . 8 Aubin Yves . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 192 "13C chemical shifts" 487 "15N chemical shifts" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-03-25 update BMRB 'update entry citation' 2013-01-03 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18135 'Interferon Alpha-2A, with GalNac at Thr106.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23184955 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ghasriani Houman . . 2 Belcourt Pascal J.F. . 3 Sauve Simon . . 4 Hodgson Derek J. . 5 Brochu Denis . . 6 Gilbert Michel . . 7 Aubin Yves . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 247 _Page_last 254 _Year 2013 _Details . loop_ _Keyword CYTOKINE DYNAMICS GLYCOPROTEIN INTERFERON NMR O-GLYCOSYLATION 'SIGNALING PROTEIN' STRUCTURE 'TYPE I INTERFERONS' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name assembly _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Entity_1 $ggIFN_alpha-2a GalGalNac $ligand stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ggIFN_alpha-2a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ggIFN_alpha-2a _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _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 2015-07-22 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 4081 Interferon_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 $ggIFN_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 _Variant _Vector_name _Details $ggIFN_alpha-2a 'recombinant technology' . Escherichia coli BL21 DE3 pET-15b 'The N-terminal His-tag of the protein (10 Histidines) was cleaved and removed before glycosylation and prior to NMR experiments.' 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 _Isotopic_labeling $ggIFN_alpha-2a 0.85 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'Buffer: 25mM deuturated sodium acetate (NaOAc, d3) at pH 3.5.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 3.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Entity_1 _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 1 CYS H H 8.926 0.020 1 2 1 1 CYS C C 173.065 0.400 1 3 1 1 CYS CA C 55.284 0.400 1 4 1 1 CYS CB C 41.087 0.400 1 5 1 1 CYS N N 121.035 0.400 1 6 2 2 ASP H H 8.787 0.020 1 7 2 2 ASP C C 174.767 0.400 1 8 2 2 ASP CA C 52.238 0.400 1 9 2 2 ASP CB C 38.956 0.400 1 10 2 2 ASP N N 125.390 0.400 1 11 3 3 LEU H H 8.162 0.020 1 12 3 3 LEU C C 175.391 0.400 1 13 3 3 LEU CA C 53.803 0.400 1 14 3 3 LEU CB C 40.634 0.400 1 15 3 3 LEU N N 123.792 0.400 1 16 4 4 PRO C C 176.174 0.400 1 17 4 4 PRO CA C 62.155 0.400 1 18 4 4 PRO CB C 34.025 0.400 1 19 5 5 GLN H H 8.772 0.020 1 20 5 5 GLN HE21 H 6.849 0.020 2 21 5 5 GLN HE22 H 6.217 0.020 2 22 5 5 GLN C C 176.368 0.400 1 23 5 5 GLN CA C 55.800 0.400 1 24 5 5 GLN CB C 28.950 0.400 1 25 5 5 GLN N N 121.463 0.400 1 26 5 5 GLN NE2 N 107.971 0.400 1 27 6 6 THR H H 7.879 0.020 1 28 6 6 THR C C 174.727 0.400 1 29 6 6 THR CA C 62.198 0.400 1 30 6 6 THR CB C 68.702 0.400 1 31 6 6 THR N N 111.416 0.400 1 32 7 7 HIS H H 8.595 0.020 1 33 7 7 HIS C C 175.070 0.400 1 34 7 7 HIS CA C 55.784 0.400 1 35 7 7 HIS CB C 27.614 0.400 1 36 7 7 HIS N N 119.065 0.400 1 37 8 8 SER H H 8.187 0.020 1 38 8 8 SER C C 175.378 0.400 1 39 8 8 SER CA C 58.660 0.400 1 40 8 8 SER CB C 63.263 0.400 1 41 8 8 SER N N 115.697 0.400 1 42 9 9 LEU H H 8.415 0.020 1 43 9 9 LEU C C 178.606 0.400 1 44 9 9 LEU CA C 56.489 0.400 1 45 9 9 LEU CB C 41.164 0.400 1 46 9 9 LEU N N 123.751 0.400 1 47 10 10 GLY H H 8.453 0.020 1 48 10 10 GLY C C 176.428 0.400 1 49 10 10 GLY CA C 46.285 0.400 1 50 10 10 GLY N N 107.445 0.400 1 51 11 11 SER H H 8.253 0.020 1 52 11 11 SER C C 175.704 0.400 1 53 11 11 SER CA C 60.634 0.400 1 54 11 11 SER CB C 62.391 0.400 1 55 11 11 SER N N 118.700 0.400 1 56 12 12 ARG H H 8.020 0.020 1 57 12 12 ARG C C 179.066 0.400 1 58 12 12 ARG CA C 59.101 0.400 1 59 12 12 ARG CB C 29.206 0.400 1 60 12 12 ARG N N 121.947 0.400 1 61 13 13 ARG H H 8.482 0.020 1 62 13 13 ARG C C 178.494 0.400 1 63 13 13 ARG CA C 59.111 0.400 1 64 13 13 ARG CB C 29.180 0.400 1 65 13 13 ARG N N 119.397 0.400 1 66 14 14 THR H H 7.952 0.020 1 67 14 14 THR C C 175.617 0.400 1 68 14 14 THR CA C 67.512 0.400 1 69 14 14 THR CB C 67.027 0.400 1 70 14 14 THR N N 116.679 0.400 1 71 15 15 LEU H H 7.564 0.020 1 72 15 15 LEU C C 178.637 0.400 1 73 15 15 LEU CA C 57.530 0.400 1 74 15 15 LEU CB C 41.174 0.400 1 75 15 15 LEU N N 120.053 0.400 1 76 16 16 MET H H 8.003 0.020 1 77 16 16 MET C C 178.733 0.400 1 78 16 16 MET CA C 57.999 0.400 1 79 16 16 MET CB C 31.891 0.400 1 80 16 16 MET N N 118.642 0.400 1 81 17 17 LEU H H 7.837 0.020 1 82 17 17 LEU C C 178.241 0.400 1 83 17 17 LEU CA C 57.589 0.400 1 84 17 17 LEU CB C 41.690 0.400 1 85 17 17 LEU N N 120.640 0.400 1 86 18 18 LEU H H 7.501 0.020 1 87 18 18 LEU C C 180.306 0.400 1 88 18 18 LEU CA C 57.173 0.400 1 89 18 18 LEU CB C 41.721 0.400 1 90 18 18 LEU N N 118.140 0.400 1 91 19 19 ALA H H 7.967 0.020 1 92 19 19 ALA C C 180.742 0.400 1 93 19 19 ALA CA C 54.603 0.400 1 94 19 19 ALA CB C 17.398 0.400 1 95 19 19 ALA N N 121.850 0.400 1 96 20 20 GLN H H 7.975 0.020 1 97 20 20 GLN HE21 H 7.192 0.020 2 98 20 20 GLN HE22 H 6.477 0.020 2 99 20 20 GLN C C 176.954 0.400 1 100 20 20 GLN CA C 57.370 0.400 1 101 20 20 GLN CB C 28.381 0.400 1 102 20 20 GLN N N 118.557 0.400 1 103 20 20 GLN NE2 N 109.050 0.400 1 104 21 21 MET H H 7.426 0.020 1 105 21 21 MET C C 174.778 0.400 1 106 21 21 MET CA C 56.649 0.400 1 107 21 21 MET CB C 33.359 0.400 1 108 21 21 MET N N 116.567 0.400 1 109 22 22 ARG H H 6.497 0.020 1 110 22 22 ARG C C 175.949 0.400 1 111 22 22 ARG CA C 58.429 0.400 1 112 22 22 ARG CB C 30.979 0.400 1 113 22 22 ARG N N 115.328 0.400 1 114 23 23 LYS H H 10.218 0.020 1 115 23 23 LYS C C 176.654 0.400 1 116 23 23 LYS CA C 56.753 0.400 1 117 23 23 LYS CB C 35.679 0.400 1 118 23 23 LYS N N 128.349 0.400 1 119 24 24 ILE H H 8.472 0.020 1 120 24 24 ILE C C 173.910 0.400 1 121 24 24 ILE CA C 59.206 0.400 1 122 24 24 ILE CB C 40.810 0.400 1 123 24 24 ILE N N 118.439 0.400 1 124 25 25 SER H H 8.112 0.020 1 125 25 25 SER C C 176.509 0.400 1 126 25 25 SER CA C 56.241 0.400 1 127 25 25 SER CB C 63.751 0.400 1 128 25 25 SER N N 113.498 0.400 1 129 26 26 LEU H H 8.809 0.020 1 130 26 26 LEU C C 178.924 0.400 1 131 26 26 LEU CA C 56.972 0.400 1 132 26 26 LEU CB C 41.184 0.400 1 133 26 26 LEU N N 127.532 0.400 1 134 27 27 PHE H H 7.993 0.020 1 135 27 27 PHE C C 177.141 0.400 1 136 27 27 PHE CA C 59.478 0.400 1 137 27 27 PHE CB C 37.511 0.400 1 138 27 27 PHE N N 116.920 0.400 1 139 28 28 SER H H 7.936 0.020 1 140 28 28 SER C C 174.543 0.400 1 141 28 28 SER CA C 59.156 0.400 1 142 28 28 SER CB C 63.093 0.400 1 143 28 28 SER N N 115.031 0.400 1 144 29 29 CYS H H 7.879 0.020 1 145 29 29 CYS C C 176.532 0.400 1 146 29 29 CYS CA C 52.672 0.400 1 147 29 29 CYS CB C 36.558 0.400 1 148 29 29 CYS N N 119.727 0.400 1 149 30 30 LEU H H 7.818 0.020 1 150 30 30 LEU C C 179.838 0.400 1 151 30 30 LEU CA C 57.682 0.400 1 152 30 30 LEU CB C 40.940 0.400 1 153 30 30 LEU N N 122.084 0.400 1 154 31 31 LYS H H 8.608 0.020 1 155 31 31 LYS C C 176.769 0.400 1 156 31 31 LYS CA C 57.442 0.400 1 157 31 31 LYS CB C 31.032 0.400 1 158 31 31 LYS N N 117.517 0.400 1 159 32 32 ASP H H 7.822 0.020 1 160 32 32 ASP C C 175.534 0.400 1 161 32 32 ASP CA C 53.502 0.400 1 162 32 32 ASP CB C 41.059 0.400 1 163 32 32 ASP N N 117.548 0.400 1 164 33 33 ARG H H 7.389 0.020 1 165 33 33 ARG C C 175.309 0.400 1 166 33 33 ARG CA C 57.315 0.400 1 167 33 33 ARG CB C 29.649 0.400 1 168 33 33 ARG N N 120.725 0.400 1 169 34 34 HIS H H 7.983 0.020 1 170 34 34 HIS C C 170.566 0.400 1 171 34 34 HIS CA C 54.650 0.400 1 172 34 34 HIS CB C 30.994 0.400 1 173 34 34 HIS N N 120.423 0.400 1 174 35 35 ASP H H 7.820 0.020 1 175 35 35 ASP C C 175.959 0.400 1 176 35 35 ASP CA C 51.760 0.400 1 177 35 35 ASP CB C 40.235 0.400 1 178 35 35 ASP N N 124.823 0.400 1 179 36 36 PHE H H 8.986 0.020 1 180 36 36 PHE C C 176.673 0.400 1 181 36 36 PHE CA C 59.049 0.400 1 182 36 36 PHE CB C 40.272 0.400 1 183 36 36 PHE N N 122.732 0.400 1 184 37 37 GLY H H 8.730 0.020 1 185 37 37 GLY C C 175.137 0.400 1 186 37 37 GLY CA C 47.601 0.400 1 187 37 37 GLY N N 111.680 0.400 1 188 38 38 PHE H H 9.180 0.020 1 189 38 38 PHE C C 176.244 0.400 1 190 38 38 PHE CA C 55.111 0.400 1 191 38 38 PHE CB C 38.055 0.400 1 192 38 38 PHE N N 122.939 0.400 1 193 39 39 PRO C C 174.707 0.400 1 194 39 39 PRO CA C 61.079 0.400 1 195 39 39 PRO CB C 27.754 0.400 1 196 40 40 GLN H H 7.978 0.020 1 197 40 40 GLN HE21 H 6.807 0.020 2 198 40 40 GLN HE22 H 7.587 0.020 2 199 40 40 GLN C C 177.001 0.400 1 200 40 40 GLN CA C 57.650 0.400 1 201 40 40 GLN CB C 28.266 0.400 1 202 40 40 GLN N N 123.513 0.400 1 203 40 40 GLN NE2 N 111.465 0.400 1 204 41 41 GLU H H 9.038 0.020 1 205 41 41 GLU C C 177.385 0.400 1 206 41 41 GLU CA C 57.320 0.400 1 207 41 41 GLU CB C 26.854 0.400 1 208 41 41 GLU N N 119.258 0.400 1 209 42 42 GLU H H 7.655 0.020 1 210 42 42 GLU C C 175.065 0.400 1 211 42 42 GLU CA C 55.714 0.400 1 212 42 42 GLU CB C 26.859 0.400 1 213 42 42 GLU N N 116.994 0.400 1 214 43 43 PHE H H 7.619 0.020 1 215 43 43 PHE C C 175.677 0.400 1 216 43 43 PHE CA C 56.887 0.400 1 217 43 43 PHE CB C 39.250 0.400 1 218 43 43 PHE N N 115.507 0.400 1 219 44 44 GLY H H 7.745 0.020 1 220 44 44 GLY C C 174.104 0.400 1 221 44 44 GLY CA C 44.951 0.400 1 222 44 44 GLY N N 107.095 0.400 1 223 45 45 ASN H H 8.354 0.020 1 224 45 45 ASN HD21 H 7.552 0.020 2 225 45 45 ASN HD22 H 6.909 0.020 2 226 45 45 ASN C C 175.933 0.400 1 227 45 45 ASN CA C 53.322 0.400 1 228 45 45 ASN CB C 37.883 0.400 1 229 45 45 ASN N N 117.414 0.400 1 230 45 45 ASN ND2 N 112.301 0.400 1 231 46 46 GLN H H 8.671 0.020 1 232 46 46 GLN HE21 H 6.776 0.020 2 233 46 46 GLN HE22 H 7.234 0.020 2 234 46 46 GLN C C 175.845 0.400 1 235 46 46 GLN CA C 56.231 0.400 1 236 46 46 GLN CB C 27.691 0.400 1 237 46 46 GLN N N 118.777 0.400 1 238 46 46 GLN NE2 N 112.145 0.400 1 239 47 47 PHE H H 7.911 0.020 1 240 47 47 PHE C C 175.920 0.400 1 241 47 47 PHE CA C 57.211 0.400 1 242 47 47 PHE CB C 39.132 0.400 1 243 47 47 PHE N N 119.354 0.400 1 244 48 48 GLN H H 8.232 0.020 1 245 48 48 GLN HE21 H 6.862 0.020 2 246 48 48 GLN HE22 H 7.509 0.020 2 247 48 48 GLN C C 174.315 0.400 1 248 48 48 GLN CA C 54.992 0.400 1 249 48 48 GLN CB C 28.196 0.400 1 250 48 48 GLN N N 119.917 0.400 1 251 48 48 GLN NE2 N 112.287 0.400 1 252 49 49 LYS H H 8.435 0.020 1 253 49 49 LYS C C 175.806 0.400 1 254 49 49 LYS CA C 58.077 0.400 1 255 49 49 LYS CB C 31.685 0.400 1 256 49 49 LYS N N 121.711 0.400 1 257 50 50 ALA H H 8.586 0.020 1 258 50 50 ALA C C 178.754 0.400 1 259 50 50 ALA CA C 53.698 0.400 1 260 50 50 ALA CB C 18.244 0.400 1 261 50 50 ALA N N 120.227 0.400 1 262 51 51 GLU H H 7.897 0.020 1 263 51 51 GLU C C 177.224 0.400 1 264 51 51 GLU CA C 56.544 0.400 1 265 51 51 GLU CB C 28.333 0.400 1 266 51 51 GLU N N 114.753 0.400 1 267 52 52 THR H H 7.878 0.020 1 268 52 52 THR C C 175.320 0.400 1 269 52 52 THR CA C 62.427 0.400 1 270 52 52 THR CB C 68.835 0.400 1 271 52 52 THR N N 111.325 0.400 1 272 53 53 ILE H H 8.353 0.020 1 273 53 53 ILE CA C 55.620 0.400 1 274 53 53 ILE CB C 27.487 0.400 1 275 53 53 ILE N N 119.000 0.400 1 276 54 54 PRO C C 179.635 0.400 1 277 54 54 PRO CA C 65.434 0.400 1 278 54 54 PRO CB C 30.704 0.400 1 279 55 55 VAL H H 7.122 0.020 1 280 55 55 VAL C C 177.704 0.400 1 281 55 55 VAL CA C 65.314 0.400 1 282 55 55 VAL CB C 30.768 0.400 1 283 55 55 VAL N N 116.054 0.400 1 284 56 56 LEU H H 8.546 0.020 1 285 56 56 LEU C C 178.640 0.400 1 286 56 56 LEU CA C 57.478 0.400 1 287 56 56 LEU CB C 41.352 0.400 1 288 56 56 LEU N N 122.938 0.400 1 289 57 57 HIS H H 9.057 0.020 1 290 57 57 HIS C C 175.718 0.400 1 291 57 57 HIS CA C 59.987 0.400 1 292 57 57 HIS CB C 27.440 0.400 1 293 57 57 HIS N N 116.914 0.400 1 294 58 58 GLU H H 7.861 0.020 1 295 58 58 GLU C C 177.778 0.400 1 296 58 58 GLU CA C 58.653 0.400 1 297 58 58 GLU CB C 28.230 0.400 1 298 58 58 GLU N N 119.466 0.400 1 299 59 59 MET H H 8.638 0.020 1 300 59 59 MET C C 177.100 0.400 1 301 59 59 MET CA C 58.649 0.400 1 302 59 59 MET CB C 32.096 0.400 1 303 59 59 MET N N 118.598 0.400 1 304 60 60 ILE H H 8.351 0.020 1 305 60 60 ILE C C 177.360 0.400 1 306 60 60 ILE CA C 64.841 0.400 1 307 60 60 ILE CB C 36.193 0.400 1 308 60 60 ILE N N 117.037 0.400 1 309 61 61 GLN H H 8.229 0.020 1 310 61 61 GLN HE21 H 6.753 0.020 2 311 61 61 GLN HE22 H 7.206 0.020 2 312 61 61 GLN C C 178.277 0.400 1 313 61 61 GLN CA C 58.157 0.400 1 314 61 61 GLN CB C 28.309 0.400 1 315 61 61 GLN N N 119.984 0.400 1 316 61 61 GLN NE2 N 113.596 0.400 1 317 62 62 GLN H H 8.435 0.020 1 318 62 62 GLN HE21 H 7.078 0.020 2 319 62 62 GLN HE22 H 8.217 0.020 2 320 62 62 GLN C C 179.702 0.400 1 321 62 62 GLN CA C 57.335 0.400 1 322 62 62 GLN CB C 23.870 0.400 1 323 62 62 GLN N N 116.625 0.400 1 324 62 62 GLN NE2 N 114.454 0.400 1 325 63 63 ILE H H 8.177 0.020 1 326 63 63 ILE C C 177.320 0.400 1 327 63 63 ILE CA C 66.562 0.400 1 328 63 63 ILE CB C 37.491 0.400 1 329 63 63 ILE N N 122.679 0.400 1 330 64 64 PHE H H 8.417 0.020 1 331 64 64 PHE C C 178.477 0.400 1 332 64 64 PHE CA C 61.604 0.400 1 333 64 64 PHE CB C 37.673 0.400 1 334 64 64 PHE N N 120.727 0.400 1 335 65 65 ASN H H 8.820 0.020 1 336 65 65 ASN HD21 H 7.132 0.020 2 337 65 65 ASN HD22 H 7.105 0.020 2 338 65 65 ASN C C 178.007 0.400 1 339 65 65 ASN CA C 55.312 0.400 1 340 65 65 ASN CB C 36.688 0.400 1 341 65 65 ASN N N 119.808 0.400 1 342 65 65 ASN ND2 N 108.837 0.400 1 343 66 66 LEU H H 8.183 0.020 1 344 66 66 LEU C C 177.830 0.400 1 345 66 66 LEU CA C 57.436 0.400 1 346 66 66 LEU CB C 42.083 0.400 1 347 66 66 LEU N N 121.431 0.400 1 348 67 67 PHE H H 8.169 0.020 1 349 67 67 PHE C C 177.954 0.400 1 350 67 67 PHE CA C 59.057 0.400 1 351 67 67 PHE CB C 38.077 0.400 1 352 67 67 PHE N N 110.696 0.400 1 353 68 68 SER H H 8.025 0.020 1 354 68 68 SER C C 173.517 0.400 1 355 68 68 SER CA C 58.718 0.400 1 356 68 68 SER CB C 62.809 0.400 1 357 68 68 SER N N 119.005 0.400 1 358 69 69 THR H H 6.985 0.020 1 359 69 69 THR C C 175.750 0.400 1 360 69 69 THR CA C 60.757 0.400 1 361 69 69 THR CB C 71.905 0.400 1 362 69 69 THR N N 111.191 0.400 1 363 70 70 LYS H H 9.070 0.020 1 364 70 70 LYS C C 179.266 0.400 1 365 70 70 LYS CA C 58.090 0.400 1 366 70 70 LYS CB C 30.982 0.400 1 367 70 70 LYS N N 120.974 0.400 1 368 71 71 ASP H H 7.535 0.020 1 369 71 71 ASP C C 178.370 0.400 1 370 71 71 ASP CA C 56.336 0.400 1 371 71 71 ASP CB C 39.838 0.400 1 372 71 71 ASP N N 116.175 0.400 1 373 72 72 SER H H 8.072 0.020 1 374 72 72 SER C C 176.890 0.400 1 375 72 72 SER CA C 59.713 0.400 1 376 72 72 SER CB C 62.186 0.400 1 377 72 72 SER N N 117.135 0.400 1 378 73 73 SER H H 7.991 0.020 1 379 73 73 SER C C 174.848 0.400 1 380 73 73 SER CA C 60.750 0.400 1 381 73 73 SER CB C 62.268 0.400 1 382 73 73 SER N N 113.190 0.400 1 383 74 74 ALA H H 7.106 0.020 1 384 74 74 ALA C C 177.641 0.400 1 385 74 74 ALA CA C 52.241 0.400 1 386 74 74 ALA CB C 18.051 0.400 1 387 74 74 ALA N N 119.293 0.400 1 388 75 75 ALA H H 7.169 0.020 1 389 75 75 ALA C C 177.212 0.400 1 390 75 75 ALA CA C 52.499 0.400 1 391 75 75 ALA CB C 17.607 0.400 1 392 75 75 ALA N N 121.276 0.400 1 393 76 76 TRP H H 7.092 0.020 1 394 76 76 TRP HE1 H 6.784 0.020 1 395 76 76 TRP C C 174.793 0.400 1 396 76 76 TRP CA C 52.880 0.400 1 397 76 76 TRP CB C 32.822 0.400 1 398 76 76 TRP N N 116.629 0.400 1 399 76 76 TRP NE1 N 121.914 0.400 1 400 77 77 ASP H H 8.231 0.020 1 401 77 77 ASP C C 176.884 0.400 1 402 77 77 ASP CA C 54.259 0.400 1 403 77 77 ASP CB C 41.812 0.400 1 404 77 77 ASP N N 119.888 0.400 1 405 78 78 GLU H H 8.928 0.020 1 406 78 78 GLU C C 177.496 0.400 1 407 78 78 GLU CA C 59.004 0.400 1 408 78 78 GLU CB C 28.036 0.400 1 409 78 78 GLU N N 127.097 0.400 1 410 79 79 THR H H 8.124 0.020 1 411 79 79 THR C C 177.404 0.400 1 412 79 79 THR CA C 65.701 0.400 1 413 79 79 THR CB C 67.367 0.400 1 414 79 79 THR N N 115.274 0.400 1 415 80 80 LEU H H 7.726 0.020 1 416 80 80 LEU C C 179.048 0.400 1 417 80 80 LEU CA C 57.059 0.400 1 418 80 80 LEU CB C 41.015 0.400 1 419 80 80 LEU N N 121.582 0.400 1 420 81 81 LEU H H 8.347 0.020 1 421 81 81 LEU C C 177.120 0.400 1 422 81 81 LEU CA C 57.099 0.400 1 423 81 81 LEU CB C 40.515 0.400 1 424 81 81 LEU N N 119.157 0.400 1 425 82 82 ASP H H 8.010 0.020 1 426 82 82 ASP C C 179.020 0.400 1 427 82 82 ASP CA C 56.022 0.400 1 428 82 82 ASP CB C 37.485 0.400 1 429 82 82 ASP N N 115.193 0.400 1 430 83 83 LYS H H 7.351 0.020 1 431 83 83 LYS C C 178.583 0.400 1 432 83 83 LYS CA C 58.946 0.400 1 433 83 83 LYS CB C 32.562 0.400 1 434 83 83 LYS N N 119.453 0.400 1 435 84 84 PHE H H 8.482 0.020 1 436 84 84 PHE C C 177.229 0.400 1 437 84 84 PHE CA C 59.695 0.400 1 438 84 84 PHE CB C 38.671 0.400 1 439 84 84 PHE N N 123.708 0.400 1 440 85 85 TYR H H 9.017 0.020 1 441 85 85 TYR C C 178.188 0.400 1 442 85 85 TYR CA C 58.042 0.400 1 443 85 85 TYR CB C 36.216 0.400 1 444 85 85 TYR N N 118.185 0.400 1 445 86 86 THR H H 7.620 0.020 1 446 86 86 THR C C 176.751 0.400 1 447 86 86 THR CA C 66.504 0.400 1 448 86 86 THR CB C 68.340 0.400 1 449 86 86 THR N N 113.903 0.400 1 450 87 87 GLU H H 7.730 0.020 1 451 87 87 GLU C C 179.640 0.400 1 452 87 87 GLU CA C 57.775 0.400 1 453 87 87 GLU CB C 27.678 0.400 1 454 87 87 GLU N N 120.723 0.400 1 455 88 88 LEU H H 8.398 0.020 1 456 88 88 LEU C C 178.639 0.400 1 457 88 88 LEU CA C 57.517 0.400 1 458 88 88 LEU CB C 40.624 0.400 1 459 88 88 LEU N N 120.663 0.400 1 460 89 89 TYR H H 8.634 0.020 1 461 89 89 TYR C C 178.476 0.400 1 462 89 89 TYR CA C 60.906 0.400 1 463 89 89 TYR CB C 37.143 0.400 1 464 89 89 TYR N N 118.540 0.400 1 465 90 90 GLN H H 7.815 0.020 1 466 90 90 GLN HE21 H 6.839 0.020 2 467 90 90 GLN HE22 H 7.480 0.020 2 468 90 90 GLN C C 178.484 0.400 1 469 90 90 GLN CA C 58.498 0.400 1 470 90 90 GLN CB C 27.700 0.400 1 471 90 90 GLN N N 118.121 0.400 1 472 90 90 GLN NE2 N 112.983 0.400 1 473 91 91 GLN H H 7.751 0.020 1 474 91 91 GLN HE21 H 6.817 0.020 2 475 91 91 GLN HE22 H 7.569 0.020 2 476 91 91 GLN C C 178.687 0.400 1 477 91 91 GLN CA C 58.806 0.400 1 478 91 91 GLN CB C 29.497 0.400 1 479 91 91 GLN N N 117.845 0.400 1 480 91 91 GLN NE2 N 112.176 0.400 1 481 92 92 LEU H H 8.477 0.020 1 482 92 92 LEU C C 178.991 0.400 1 483 92 92 LEU CA C 58.101 0.400 1 484 92 92 LEU CB C 40.671 0.400 1 485 92 92 LEU N N 119.862 0.400 1 486 93 93 ASN H H 8.095 0.020 1 487 93 93 ASN HD21 H 6.407 0.020 2 488 93 93 ASN HD22 H 7.345 0.020 2 489 93 93 ASN C C 178.201 0.400 1 490 93 93 ASN CA C 55.737 0.400 1 491 93 93 ASN CB C 37.577 0.400 1 492 93 93 ASN N N 117.635 0.400 1 493 93 93 ASN ND2 N 111.923 0.400 1 494 94 94 ASP H H 8.382 0.020 1 495 94 94 ASP C C 178.311 0.400 1 496 94 94 ASP CA C 56.167 0.400 1 497 94 94 ASP CB C 38.578 0.400 1 498 94 94 ASP N N 120.974 0.400 1 499 95 95 LEU H H 8.162 0.020 1 500 95 95 LEU C C 178.889 0.400 1 501 95 95 LEU CA C 57.275 0.400 1 502 95 95 LEU CB C 41.742 0.400 1 503 95 95 LEU N N 119.125 0.400 1 504 96 96 GLU H H 8.100 0.020 1 505 96 96 GLU C C 177.677 0.400 1 506 96 96 GLU CA C 57.408 0.400 1 507 96 96 GLU CB C 27.334 0.400 1 508 96 96 GLU N N 118.609 0.400 1 509 97 97 ALA H H 7.828 0.020 1 510 97 97 ALA C C 179.198 0.400 1 511 97 97 ALA CA C 53.576 0.400 1 512 97 97 ALA CB C 17.674 0.400 1 513 97 97 ALA N N 120.491 0.400 1 514 98 98 CYS H H 7.609 0.020 1 515 98 98 CYS C C 175.243 0.400 1 516 98 98 CYS CA C 56.727 0.400 1 517 98 98 CYS CB C 41.587 0.400 1 518 98 98 CYS N N 115.372 0.400 1 519 99 99 VAL H H 7.834 0.020 1 520 99 99 VAL C C 177.416 0.400 1 521 99 99 VAL CA C 64.129 0.400 1 522 99 99 VAL CB C 31.303 0.400 1 523 99 99 VAL N N 121.409 0.400 1 524 100 100 ILE H H 8.067 0.020 1 525 100 100 ILE C C 176.851 0.400 1 526 100 100 ILE CA C 61.738 0.400 1 527 100 100 ILE CB C 37.639 0.400 1 528 100 100 ILE N N 122.262 0.400 1 529 101 101 GLN H H 8.065 0.020 1 530 101 101 GLN C C 176.519 0.400 1 531 101 101 GLN CA C 55.985 0.400 1 532 101 101 GLN CB C 28.905 0.400 1 533 101 101 GLN N N 121.514 0.400 1 534 102 102 GLY H H 8.080 0.020 1 535 102 102 GLY C C 173.842 0.400 1 536 102 102 GLY CA C 44.688 0.400 1 537 102 102 GLY N N 109.125 0.400 1 538 103 103 VAL H H 8.100 0.020 1 539 103 103 VAL C C 176.262 0.400 1 540 103 103 VAL CA C 61.300 0.400 1 541 103 103 VAL CB C 32.277 0.400 1 542 103 103 VAL N N 118.611 0.400 1 543 104 104 GLY H H 8.432 0.020 1 544 104 104 GLY C C 173.688 0.400 1 545 104 104 GLY CA C 44.530 0.400 1 546 104 104 GLY N N 111.867 0.400 1 547 105 105 VAL H H 7.894 0.020 1 548 105 105 VAL C C 176.009 0.400 1 549 105 105 VAL CA C 61.612 0.400 1 550 105 105 VAL CB C 32.280 0.400 1 551 105 105 VAL N N 120.678 0.400 1 552 106 106 THR H H 8.712 0.020 1 553 106 106 THR C C 173.788 0.400 1 554 106 106 THR CA C 59.027 0.400 1 555 106 106 THR CB C 79.116 0.400 1 556 106 106 THR N N 116.440 0.400 1 557 107 107 GLU H H 8.487 0.020 1 558 107 107 GLU C C 175.680 0.400 1 559 107 107 GLU CA C 54.170 0.400 1 560 107 107 GLU CB C 29.668 0.400 1 561 107 107 GLU N N 119.243 0.400 1 562 108 108 THR H H 8.135 0.020 1 563 108 108 THR C C 173.452 0.400 1 564 108 108 THR CA C 59.701 0.400 1 565 108 108 THR CB C 68.225 0.400 1 566 108 108 THR N N 113.929 0.400 1 567 109 109 PRO C C 178.745 0.400 1 568 109 109 PRO CA C 64.899 0.400 1 569 109 109 PRO CB C 31.234 0.400 1 570 110 110 LEU H H 8.019 0.020 1 571 110 110 LEU C C 178.304 0.400 1 572 110 110 LEU CA C 56.996 0.400 1 573 110 110 LEU CB C 41.493 0.400 1 574 110 110 LEU N N 118.317 0.400 1 575 111 111 MET H H 7.682 0.020 1 576 111 111 MET C C 178.915 0.400 1 577 111 111 MET CA C 57.523 0.400 1 578 111 111 MET CB C 31.847 0.400 1 579 111 111 MET N N 118.764 0.400 1 580 112 112 LYS H H 8.295 0.020 1 581 112 112 LYS C C 178.074 0.400 1 582 112 112 LYS CA C 58.868 0.400 1 583 112 112 LYS CB C 31.775 0.400 1 584 112 112 LYS N N 121.228 0.400 1 585 113 113 GLU H H 8.281 0.020 1 586 113 113 GLU C C 178.310 0.400 1 587 113 113 GLU CA C 57.757 0.400 1 588 113 113 GLU CB C 27.522 0.400 1 589 113 113 GLU N N 118.870 0.400 1 590 114 114 ASP H H 8.624 0.020 1 591 114 114 ASP C C 178.402 0.400 1 592 114 114 ASP CA C 55.818 0.400 1 593 114 114 ASP CB C 37.642 0.400 1 594 114 114 ASP N N 118.974 0.400 1 595 115 115 SER H H 8.196 0.020 1 596 115 115 SER C C 176.113 0.400 1 597 115 115 SER CA C 61.130 0.400 1 598 115 115 SER CB C 62.391 0.400 1 599 115 115 SER N N 118.023 0.400 1 600 116 116 ILE H H 7.809 0.020 1 601 116 116 ILE C C 178.567 0.400 1 602 116 116 ILE CA C 64.302 0.400 1 603 116 116 ILE CB C 36.548 0.400 1 604 116 116 ILE N N 123.280 0.400 1 605 117 117 LEU H H 8.422 0.020 1 606 117 117 LEU C C 178.787 0.400 1 607 117 117 LEU CA C 57.433 0.400 1 608 117 117 LEU CB C 40.807 0.400 1 609 117 117 LEU N N 121.029 0.400 1 610 118 118 ALA H H 7.897 0.020 1 611 118 118 ALA C C 181.622 0.400 1 612 118 118 ALA CA C 55.000 0.400 1 613 118 118 ALA CB C 17.351 0.400 1 614 118 118 ALA N N 120.065 0.400 1 615 119 119 VAL H H 7.584 0.020 1 616 119 119 VAL C C 177.827 0.400 1 617 119 119 VAL CA C 66.669 0.400 1 618 119 119 VAL CB C 31.366 0.400 1 619 119 119 VAL N N 118.712 0.400 1 620 120 120 ARG H H 8.651 0.020 1 621 120 120 ARG C C 179.869 0.400 1 622 120 120 ARG CA C 61.251 0.400 1 623 120 120 ARG CB C 29.211 0.400 1 624 120 120 ARG N N 121.348 0.400 1 625 121 121 LYS H H 9.020 0.020 1 626 121 121 LYS C C 178.500 0.400 1 627 121 121 LYS CA C 59.403 0.400 1 628 121 121 LYS CB C 31.639 0.400 1 629 121 121 LYS N N 119.575 0.400 1 630 122 122 TYR H H 7.483 0.020 1 631 122 122 TYR C C 176.549 0.400 1 632 122 122 TYR CA C 60.314 0.400 1 633 122 122 TYR CB C 37.332 0.400 1 634 122 122 TYR N N 121.333 0.400 1 635 123 123 PHE H H 7.943 0.020 1 636 123 123 PHE C C 179.032 0.400 1 637 123 123 PHE CA C 62.825 0.400 1 638 123 123 PHE CB C 38.482 0.400 1 639 123 123 PHE N N 115.876 0.400 1 640 124 124 GLN H H 8.486 0.020 1 641 124 124 GLN HE21 H 6.809 0.020 2 642 124 124 GLN HE22 H 7.483 0.020 2 643 124 124 GLN C C 178.834 0.400 1 644 124 124 GLN CA C 58.875 0.400 1 645 124 124 GLN CB C 27.199 0.400 1 646 124 124 GLN N N 122.933 0.400 1 647 124 124 GLN NE2 N 110.727 0.400 1 648 125 125 ARG H H 8.142 0.020 1 649 125 125 ARG C C 180.284 0.400 1 650 125 125 ARG CA C 60.586 0.400 1 651 125 125 ARG CB C 29.691 0.400 1 652 125 125 ARG N N 120.197 0.400 1 653 126 126 ILE H H 7.533 0.020 1 654 126 126 ILE C C 176.897 0.400 1 655 126 126 ILE CA C 65.177 0.400 1 656 126 126 ILE CB C 36.915 0.400 1 657 126 126 ILE N N 121.695 0.400 1 658 127 127 THR H H 8.298 0.020 1 659 127 127 THR C C 176.816 0.400 1 660 127 127 THR CA C 66.869 0.400 1 661 127 127 THR CB C 68.239 0.400 1 662 127 127 THR N N 115.417 0.400 1 663 128 128 LEU H H 8.274 0.020 1 664 128 128 LEU C C 178.341 0.400 1 665 128 128 LEU CA C 57.550 0.400 1 666 128 128 LEU CB C 41.002 0.400 1 667 128 128 LEU N N 122.605 0.400 1 668 129 129 TYR H H 7.530 0.020 1 669 129 129 TYR C C 176.116 0.400 1 670 129 129 TYR CA C 60.547 0.400 1 671 129 129 TYR CB C 38.272 0.400 1 672 129 129 TYR N N 120.780 0.400 1 673 130 130 LEU H H 7.727 0.020 1 674 130 130 LEU C C 177.946 0.400 1 675 130 130 LEU CA C 57.588 0.400 1 676 130 130 LEU CB C 40.856 0.400 1 677 130 130 LEU N N 119.015 0.400 1 678 131 131 LYS H H 7.503 0.020 1 679 131 131 LYS C C 181.292 0.400 1 680 131 131 LYS CA C 59.245 0.400 1 681 131 131 LYS CB C 32.007 0.400 1 682 131 131 LYS N N 116.716 0.400 1 683 132 132 GLU H H 8.447 0.020 1 684 132 132 GLU C C 178.368 0.400 1 685 132 132 GLU CA C 58.229 0.400 1 686 132 132 GLU CB C 27.385 0.400 1 687 132 132 GLU N N 121.715 0.400 1 688 133 133 LYS H H 7.397 0.020 1 689 133 133 LYS C C 175.332 0.400 1 690 133 133 LYS CA C 53.589 0.400 1 691 133 133 LYS CB C 31.456 0.400 1 692 133 133 LYS N N 115.915 0.400 1 693 134 134 LYS H H 7.724 0.020 1 694 134 134 LYS C C 176.256 0.400 1 695 134 134 LYS CA C 56.755 0.400 1 696 134 134 LYS CB C 28.302 0.400 1 697 134 134 LYS N N 117.641 0.400 1 698 135 135 TYR H H 8.443 0.020 1 699 135 135 TYR C C 174.175 0.400 1 700 135 135 TYR CA C 59.264 0.400 1 701 135 135 TYR CB C 34.135 0.400 1 702 135 135 TYR N N 110.376 0.400 1 703 136 136 SER H H 6.752 0.020 1 704 136 136 SER C C 172.351 0.400 1 705 136 136 SER CA C 56.517 0.400 1 706 136 136 SER CB C 62.215 0.400 1 707 136 136 SER N N 113.528 0.400 1 708 137 137 PRO C C 180.654 0.400 1 709 137 137 PRO CA C 65.767 0.400 1 710 137 137 PRO CB C 31.471 0.400 1 711 138 138 CYS H H 8.591 0.020 1 712 138 138 CYS C C 176.102 0.400 1 713 138 138 CYS CA C 56.658 0.400 1 714 138 138 CYS CB C 36.098 0.400 1 715 138 138 CYS N N 113.721 0.400 1 716 139 139 ALA H H 8.094 0.020 1 717 139 139 ALA C C 180.192 0.400 1 718 139 139 ALA CA C 54.097 0.400 1 719 139 139 ALA CB C 18.313 0.400 1 720 139 139 ALA N N 125.161 0.400 1 721 140 140 TRP H H 8.515 0.020 1 722 140 140 TRP HE1 H 9.650 0.020 1 723 140 140 TRP C C 179.101 0.400 1 724 140 140 TRP CA C 59.723 0.400 1 725 140 140 TRP CB C 29.174 0.400 1 726 140 140 TRP N N 116.435 0.400 1 727 140 140 TRP NE1 N 126.810 0.400 1 728 141 141 GLU H H 8.188 0.020 1 729 141 141 GLU C C 178.134 0.400 1 730 141 141 GLU CA C 57.331 0.400 1 731 141 141 GLU CB C 27.698 0.400 1 732 141 141 GLU N N 121.451 0.400 1 733 142 142 VAL H H 8.631 0.020 1 734 142 142 VAL C C 180.252 0.400 1 735 142 142 VAL CA C 66.593 0.400 1 736 142 142 VAL CB C 31.153 0.400 1 737 142 142 VAL N N 121.076 0.400 1 738 143 143 VAL H H 8.336 0.020 1 739 143 143 VAL C C 176.484 0.400 1 740 143 143 VAL CA C 67.285 0.400 1 741 143 143 VAL CB C 30.944 0.400 1 742 143 143 VAL N N 120.060 0.400 1 743 144 144 ARG H H 9.625 0.020 1 744 144 144 ARG C C 178.202 0.400 1 745 144 144 ARG CA C 60.624 0.400 1 746 144 144 ARG CB C 29.251 0.400 1 747 144 144 ARG N N 123.917 0.400 1 748 145 145 ALA H H 8.872 0.020 1 749 145 145 ALA C C 180.773 0.400 1 750 145 145 ALA CA C 54.890 0.400 1 751 145 145 ALA CB C 17.647 0.400 1 752 145 145 ALA N N 119.254 0.400 1 753 146 146 GLU H H 8.150 0.020 1 754 146 146 GLU C C 177.354 0.400 1 755 146 146 GLU CA C 57.872 0.400 1 756 146 146 GLU CB C 27.200 0.400 1 757 146 146 GLU N N 121.700 0.400 1 758 147 147 ILE H H 8.741 0.020 1 759 147 147 ILE C C 178.289 0.400 1 760 147 147 ILE CA C 60.860 0.400 1 761 147 147 ILE CB C 34.709 0.400 1 762 147 147 ILE N N 119.378 0.400 1 763 148 148 MET H H 8.452 0.020 1 764 148 148 MET C C 178.208 0.400 1 765 148 148 MET CA C 59.590 0.400 1 766 148 148 MET CB C 31.753 0.400 1 767 148 148 MET N N 119.314 0.400 1 768 149 149 ARG H H 7.663 0.020 1 769 149 149 ARG C C 178.942 0.400 1 770 149 149 ARG CA C 59.026 0.400 1 771 149 149 ARG CB C 29.647 0.400 1 772 149 149 ARG N N 119.592 0.400 1 773 150 150 SER H H 9.204 0.020 1 774 150 150 SER C C 177.292 0.400 1 775 150 150 SER CA C 60.719 0.400 1 776 150 150 SER N N 117.925 0.400 1 777 151 151 PHE H H 9.458 0.020 1 778 151 151 PHE C C 178.730 0.400 1 779 151 151 PHE CA C 61.110 0.400 1 780 151 151 PHE CB C 38.626 0.400 1 781 151 151 PHE N N 125.098 0.400 1 782 152 152 SER H H 7.852 0.020 1 783 152 152 SER C C 175.909 0.400 1 784 152 152 SER CA C 61.828 0.400 1 785 152 152 SER N N 115.801 0.400 1 786 153 153 LEU H H 7.790 0.020 1 787 153 153 LEU C C 179.574 0.400 1 788 153 153 LEU CA C 57.255 0.400 1 789 153 153 LEU CB C 41.835 0.400 1 790 153 153 LEU N N 121.275 0.400 1 791 154 154 SER H H 7.888 0.020 1 792 154 154 SER C C 174.238 0.400 1 793 154 154 SER CA C 60.883 0.400 1 794 154 154 SER CB C 62.691 0.400 1 795 154 154 SER N N 113.810 0.400 1 796 155 155 THR H H 7.179 0.020 1 797 155 155 THR C C 174.831 0.400 1 798 155 155 THR CA C 61.613 0.400 1 799 155 155 THR CB C 68.939 0.400 1 800 155 155 THR N N 109.305 0.400 1 801 156 156 ASN H H 7.754 0.020 1 802 156 156 ASN HD21 H 6.835 0.020 2 803 156 156 ASN HD22 H 7.484 0.020 2 804 156 156 ASN C C 175.563 0.400 1 805 156 156 ASN CA C 53.768 0.400 1 806 156 156 ASN CB C 37.537 0.400 1 807 156 156 ASN N N 119.563 0.400 1 808 156 156 ASN ND2 N 111.888 0.400 1 809 157 157 LEU H H 8.101 0.020 1 810 157 157 LEU C C 174.763 0.400 1 811 157 157 LEU CA C 55.578 0.400 1 812 157 157 LEU CB C 41.858 0.400 1 813 157 157 LEU N N 120.455 0.400 1 814 158 158 GLN H H 8.257 0.020 1 815 158 158 GLN HE21 H 6.749 0.020 2 816 158 158 GLN HE22 H 7.447 0.020 2 817 158 158 GLN C C 176.445 0.400 1 818 158 158 GLN CA C 56.148 0.400 1 819 158 158 GLN CB C 28.378 0.400 1 820 158 158 GLN N N 119.914 0.400 1 821 158 158 GLN NE2 N 111.543 0.400 1 822 159 159 GLU H H 8.303 0.020 1 823 159 159 GLU C C 176.195 0.400 1 824 159 159 GLU CA C 55.996 0.400 1 825 159 159 GLU CB C 28.560 0.400 1 826 159 159 GLU N N 120.433 0.400 1 827 160 160 SER H H 8.124 0.020 1 828 160 160 SER C C 174.231 0.400 1 829 160 160 SER CA C 57.905 0.400 1 830 160 160 SER CB C 63.303 0.400 1 831 160 160 SER N N 115.564 0.400 1 832 161 161 LEU H H 8.037 0.020 1 833 161 161 LEU C C 177.306 0.400 1 834 161 161 LEU CA C 54.858 0.400 1 835 161 161 LEU CB C 41.710 0.400 1 836 161 161 LEU N N 123.702 0.400 1 837 162 162 ARG H H 8.101 0.020 1 838 162 162 ARG C C 176.314 0.400 1 839 162 162 ARG CA C 55.624 0.400 1 840 162 162 ARG CB C 30.163 0.400 1 841 162 162 ARG N N 120.585 0.400 1 842 163 163 SER H H 8.199 0.020 1 843 163 163 SER C C 174.215 0.400 1 844 163 163 SER CA C 57.845 0.400 1 845 163 163 SER CB C 63.342 0.400 1 846 163 163 SER N N 116.624 0.400 1 847 164 164 LYS H H 8.253 0.020 1 848 164 164 LYS C C 175.679 0.400 1 849 164 164 LYS CA C 55.833 0.400 1 850 164 164 LYS CB C 32.428 0.400 1 851 164 164 LYS N N 122.900 0.400 1 852 165 165 GLU H H 8.029 0.020 1 853 165 165 GLU C C 179.933 0.400 1 854 165 165 GLU CA C 56.379 0.400 1 855 165 165 GLU CB C 29.016 0.400 1 856 165 165 GLU N N 125.351 0.400 1 stop_ save_