data_4086 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism ; _BMRB_accession_number 4086 _BMRB_flat_file_name bmr4086.str _Entry_type update _Submission_date 1997-12-23 _Accession_date 1997-12-23 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tevelev Anton . . 2 Byeon In-Ja L. . 3 Selby Thomas . . 4 Ericson Karen . . 5 Kim Hee-Jung . . 6 Kraynov Vadim . . 7 Tsai Ming-Daw . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 512 "13C chemical shifts" 330 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1997-12-23 original author 'Original release.' 2001-02-16 reformat BMRB 'Format updated to NMR-STAR version 2.1' 2002-07-17 update BMRB 'Modify the saveframe name.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Tevlev, A., Byeion, I. L., Selby, T., Ericson, K., Kim, H-J., Kraynov, V., and Tsai M-D., "Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism," Biochemistry 35, 9475-9487 (1996). ; _Citation_title ; Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8755727 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tevelev Anton . . 2 Byeon In-Ja L. . 3 Selby Thomas . . 4 Ericson Karen . . 5 Kim Hee-Jung . . 6 Kraynov Vadim . . 7 Tsai Ming-Daw . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 35 _Journal_issue 29 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9475 _Page_last 9487 _Year 1996 _Details . loop_ _Keyword 'multiple tumor suppressor (MTS1)' NMR 'Nuclear Magnetic Resonance' 'p16/delta 1-8' stop_ save_ ################################## # Molecular system description # ################################## save_system_p16(INK4)_delta_1-8 _Saveframe_category molecular_system _Mol_system_name p16(INK4)/delta_1-8 _Abbreviation_common p16(INK4)/delta_1-8 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label p16(INK4)/delta_1-8 $p16(INK4)_delta_1-8 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'All free' loop_ _Biological_function 'p16 is a multiple tumor suppressor' stop_ _Database_query_date . _Details ; The tumor suppressor p16_INK4 with eight N-terminal amino acids deleted was expressed in E. coli (p16/delta1-8) ; save_ ######################## # Monomeric polymers # ######################## save_p16(INK4)_delta_1-8 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p16(INK4)/delta_1-8 _Name_variant 'p16-delta 1-8' _Abbreviation_common p16(INK4)/delta_1-8 _Molecular_mass 16569 _Mol_thiol_state 'All free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; MEPSADWLATAAARGRVEEV RALLEAGALPNAPNSYGRRP IQVMMMGSARVAELLLLHGA EPNCADPATLTRPVHDAARE GFLDTLVVLHRAGARLDVRD AWGRLPVDLAEELGHRDVAR YLRAAAGGTRGSNHARIDAA EGPSDIPD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 9 MET 2 10 GLU 3 11 PRO 4 12 SER 5 13 ALA 6 14 ASP 7 15 TRP 8 16 LEU 9 17 ALA 10 18 THR 11 19 ALA 12 20 ALA 13 21 ALA 14 22 ARG 15 23 GLY 16 24 ARG 17 25 VAL 18 26 GLU 19 27 GLU 20 28 VAL 21 29 ARG 22 30 ALA 23 31 LEU 24 32 LEU 25 33 GLU 26 34 ALA 27 35 GLY 28 36 ALA 29 37 LEU 30 38 PRO 31 39 ASN 32 40 ALA 33 41 PRO 34 42 ASN 35 43 SER 36 44 TYR 37 45 GLY 38 46 ARG 39 47 ARG 40 48 PRO 41 49 ILE 42 50 GLN 43 51 VAL 44 52 MET 45 53 MET 46 54 MET 47 55 GLY 48 56 SER 49 57 ALA 50 58 ARG 51 59 VAL 52 60 ALA 53 61 GLU 54 62 LEU 55 63 LEU 56 64 LEU 57 65 LEU 58 66 HIS 59 67 GLY 60 68 ALA 61 69 GLU 62 70 PRO 63 71 ASN 64 72 CYS 65 73 ALA 66 74 ASP 67 75 PRO 68 76 ALA 69 77 THR 70 78 LEU 71 79 THR 72 80 ARG 73 81 PRO 74 82 VAL 75 83 HIS 76 84 ASP 77 85 ALA 78 86 ALA 79 87 ARG 80 88 GLU 81 89 GLY 82 90 PHE 83 91 LEU 84 92 ASP 85 93 THR 86 94 LEU 87 95 VAL 88 96 VAL 89 97 LEU 90 98 HIS 91 99 ARG 92 100 ALA 93 101 GLY 94 102 ALA 95 103 ARG 96 104 LEU 97 105 ASP 98 106 VAL 99 107 ARG 100 108 ASP 101 109 ALA 102 110 TRP 103 111 GLY 104 112 ARG 105 113 LEU 106 114 PRO 107 115 VAL 108 116 ASP 109 117 LEU 110 118 ALA 111 119 GLU 112 120 GLU 113 121 LEU 114 122 GLY 115 123 HIS 116 124 ARG 117 125 ASP 118 126 VAL 119 127 ALA 120 128 ARG 121 129 TYR 122 130 LEU 123 131 ARG 124 132 ALA 125 133 ALA 126 134 ALA 127 135 GLY 128 136 GLY 129 137 THR 130 138 ARG 131 139 GLY 132 140 SER 133 141 ASN 134 142 HIS 135 143 ALA 136 144 ARG 137 145 ILE 138 146 ASP 139 147 ALA 140 148 ALA 141 149 GLU 142 150 GLY 143 151 PRO 144 152 SER 145 153 ASP 146 154 ILE 147 155 PRO 148 156 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4526 "CYCLIN-DEPENDENT KINASE 4 INHIBITOR A (P16INK4A)" 100.00 156 100.00 100.00 1.07e-97 PDB 1A5E "Solution Nmr Structure Of Tumor Suppressor P16ink4a, 18 Structures" 100.00 156 100.00 100.00 1.07e-97 PDB 1BI7 "Mechanism Of G1 Cyclin Dependent Kinase Inhibition From The Structure Of The Cdk6-P16ink4a Tumor Suppressor Complex" 100.00 156 99.32 99.32 1.04e-96 PDB 1DC2 "Solution Nmr Structure Of Tumor Suppressor P16ink4a, 20 Structures" 100.00 156 100.00 100.00 1.07e-97 PDB 2A5E "Solution Nmr Structure Of Tumor Suppressor P16ink4a, Restrained Minimized Mean Structure" 100.00 156 100.00 100.00 1.07e-97 DBJ BAA33541 "p15/MTS2/CDKN2B [Felis catus]" 57.43 86 97.65 98.82 2.42e-48 DBJ BAB91133 "p16/CDKN2A [Homo sapiens]" 100.00 156 100.00 100.00 1.07e-97 EMBL CCQ43815 "alternative protein CDKN2A [Homo sapiens]" 72.97 108 98.15 100.00 7.63e-67 GB AAA92554 "p16-INK4 [Homo sapiens]" 100.00 156 100.00 100.00 1.07e-97 GB AAB32713 "cyclin D-dependent kinases 4 and 6-binding protein/p16 product [human, brain tumors, Peptide, 156 aa]" 100.00 156 98.65 98.65 2.56e-95 GB AAB60645 "p16-INK4 [Homo sapiens]" 100.00 148 100.00 100.00 1.50e-97 GB AAD14048 "multiple tumor suppressor 1/cyclin-dependent kinase 4 inhibitor p16 [Homo sapiens]" 68.92 102 100.00 100.00 6.09e-63 GB AAD14050 "cyclin-dependent kinase 4 inhibitor [Homo sapiens]" 71.62 106 100.00 100.00 3.09e-66 PRF 2002364A "p16ink4 protein" 100.00 148 99.32 99.32 2.23e-96 REF NP_000068 "cyclin-dependent kinase inhibitor 2A isoform p16INK4a [Homo sapiens]" 100.00 156 100.00 100.00 1.07e-97 REF NP_001139762 "cyclin-dependent kinase inhibitor 2A [Pan troglodytes]" 100.00 156 99.32 99.32 1.63e-96 REF NP_001182061 "cyclin-dependent kinase inhibitor 2A isoform p16gamma [Homo sapiens]" 98.65 167 98.63 100.00 2.03e-94 REF XP_003830733 "PREDICTED: cyclin-dependent kinase inhibitor 2A isoform X2 [Pan paniscus]" 100.00 156 99.32 99.32 1.63e-96 REF XP_005251400 "PREDICTED: cyclin-dependent kinase inhibitor 2A isoform X5 [Homo sapiens]" 70.95 105 100.00 100.00 1.47e-65 SP P42771 "RecName: Full=Cyclin-dependent kinase inhibitor 2A; AltName: Full=Cyclin-dependent kinase 4 inhibitor A; Short=CDK4I; AltName: " 100.00 156 100.00 100.00 1.07e-97 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Cell_line _Details $p16(INK4)_delta_1-8 human 9606 Eukaryota Metazoa Homo sapiens 'Hela cells' ; p16 was cloned by RT-PCR from total RNA from Hela cells with primers using GeneAmp RT-PCR into NdeI and Bam HI sites of pET-21b phagemid (Novagen). ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $p16(INK4)_delta_1-8 'recombinant technology' 'E. coli' Escherichia coli B834(DE3) phagemid pET-MTS1/delta1-8 natural 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 $p16(INK4)_delta_1-8 0.2 mM . HEPES 4 mM . DTT 1 mM . EDTA 5 uM . D2O 10 % . H2O 90 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p16(INK4)_delta_1-8 0.2 mM . HEPES 4 mM . DTT 1 mM . EDTA 5 uM . D2O 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 300 . 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 DSS C 13 'methyl protons' ppm 0.0 external/internal . . . . DSS H 1 'methyl protons' ppm 0.0 external/internal . . . . NH4NO3 N 15 . ppm 21.6 external . . . . 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_assignments _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 p16(INK4)/delta_1-8 _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 . 4 SER CA C 58.2 . 1 2 . 5 ALA H H 8.07 . 1 3 . 5 ALA HA H 3.74 . 1 4 . 5 ALA HB H 1.57 . 1 5 . 5 ALA CA C 55.9 . 1 6 . 5 ALA CB C 18.2 . 1 7 . 5 ALA N N 121.4 . 1 8 . 6 ASP CA C 56.4 . 1 9 . 7 TRP H H 7.73 . 1 10 . 7 TRP HA H 4.62 . 1 11 . 7 TRP HB2 H 3.29 . 2 12 . 7 TRP HB3 H 3.37 . 2 13 . 7 TRP HD1 H 7.22 . 1 14 . 7 TRP HE1 H 10.14 . 1 15 . 7 TRP HE3 H 7.49 . 1 16 . 7 TRP HZ2 H 7.48 . 1 17 . 7 TRP HZ3 H 7.14 . 1 18 . 7 TRP HH2 H 7.24 . 1 19 . 7 TRP CA C 58.5 . 1 20 . 7 TRP CB C 29.2 . 1 21 . 8 LEU H H 8.85 . 1 22 . 8 LEU HA H 4.60 . 1 23 . 8 LEU HB2 H 1.75 . 1 24 . 8 LEU HB3 H 1.75 . 1 25 . 8 LEU HG H 1.83 . 1 26 . 8 LEU HD1 H 0.94 . 2 27 . 8 LEU HD2 H 0.99 . 2 28 . 8 LEU CA C 52.6 . 1 29 . 8 LEU CB C 40.4 . 1 30 . 8 LEU CG C 27.0 . 1 31 . 8 LEU CD1 C 23.1 . 2 32 . 8 LEU CD2 C 25.6 . 2 33 . 8 LEU N N 121.4 . 1 34 . 9 ALA H H 8.30 . 1 35 . 9 ALA CA C 55.9 . 1 36 . 9 ALA CB C 19.3 . 1 37 . 9 ALA N N 121.5 . 1 38 . 10 THR H H 8.50 . 1 39 . 10 THR HA H 3.90 . 1 40 . 10 THR HB H 4.25 . 1 41 . 10 THR HG2 H 1.18 . 1 42 . 10 THR CA C 66.9 . 1 43 . 10 THR CB C 68.6 . 1 44 . 10 THR N N 116.8 . 1 45 . 11 ALA H H 8.22 . 1 46 . 11 ALA HA H 4.18 . 1 47 . 11 ALA HB H 1.15 . 1 48 . 11 ALA CA C 55.6 . 1 49 . 11 ALA CB C 18.2 . 1 50 . 11 ALA N N 124.6 . 1 51 . 12 ALA H H 8.40 . 1 52 . 12 ALA HA H 4.01 . 1 53 . 12 ALA HB H 1.24 . 1 54 . 12 ALA CA C 55.2 . 1 55 . 12 ALA CB C 17.5 . 1 56 . 12 ALA N N 120.1 . 1 57 . 13 ALA H H 8.75 . 1 58 . 13 ALA HA H 4.48 . 1 59 . 13 ALA HB H 1.48 . 1 60 . 13 ALA CA C 55.2 . 1 61 . 13 ALA CB C 18.8 . 1 62 . 13 ALA N N 126.2 . 1 63 . 14 ARG H H 7.82 . 1 64 . 14 ARG HA H 4.37 . 1 65 . 14 ARG HD2 H 3.10 . 1 66 . 14 ARG HD3 H 3.10 . 1 67 . 14 ARG CA C 55.4 . 1 68 . 14 ARG CB C 31.2 . 1 69 . 14 ARG N N 114.7 . 1 70 . 15 GLY H H 8.01 . 1 71 . 15 GLY HA2 H 3.55 . 2 72 . 15 GLY HA3 H 4.31 . 2 73 . 15 GLY CA C 47.0 . 1 74 . 15 GLY N N 110.1 . 1 75 . 16 ARG H H 7.96 . 1 76 . 16 ARG HA H 4.41 . 1 77 . 16 ARG HD2 H 3.18 . 1 78 . 16 ARG HD3 H 3.18 . 1 79 . 16 ARG CA C 54.5 . 1 80 . 16 ARG CB C 32.3 . 1 81 . 16 ARG CD C 43.6 . 1 82 . 16 ARG N N 120.5 . 1 83 . 17 VAL H H 7.91 . 1 84 . 17 VAL HA H 3.07 . 1 85 . 17 VAL HB H 1.95 . 1 86 . 17 VAL HG1 H 0.83 . 2 87 . 17 VAL HG2 H 0.94 . 2 88 . 17 VAL CA C 67.3 . 1 89 . 17 VAL CB C 32.4 . 1 90 . 17 VAL CG1 C 21.4 . 2 91 . 17 VAL CG2 C 23.0 . 2 92 . 17 VAL N N 126.2 . 1 93 . 18 GLU H H 8.85 . 1 94 . 18 GLU HA H 4.03 . 1 95 . 18 GLU CA C 58.9 . 1 96 . 18 GLU N N 117.5 . 1 97 . 19 GLU H H 8.32 . 1 98 . 19 GLU HA H 4.07 . 1 99 . 19 GLU CA C 58.9 . 1 100 . 19 GLU CB C 30.3 . 1 101 . 19 GLU N N 122.6 . 1 102 . 20 VAL H H 8.16 . 1 103 . 20 VAL HA H 3.27 . 1 104 . 20 VAL HB H 2.18 . 1 105 . 20 VAL HG1 H 0.82 . 2 106 . 20 VAL HG2 H 0.87 . 2 107 . 20 VAL CA C 67.2 . 1 108 . 20 VAL CB C 31.4 . 1 109 . 20 VAL CG1 C 22.3 . 1 110 . 20 VAL CG2 C 22.3 . 1 111 . 20 VAL N N 120.0 . 1 112 . 21 ARG H H 8.32 . 1 113 . 21 ARG CA C 60.4 . 1 114 . 21 ARG CB C 29.9 . 1 115 . 21 ARG N N 118.6 . 1 116 . 22 ALA H H 7.87 . 1 117 . 22 ALA HA H 4.01 . 1 118 . 22 ALA HB H 1.44 . 1 119 . 22 ALA CA C 54.8 . 1 120 . 22 ALA CB C 18.2 . 1 121 . 22 ALA N N 120.6 . 1 122 . 23 LEU H H 8.31 . 1 123 . 23 LEU HA H 3.97 . 1 124 . 23 LEU HG H 1.80 . 1 125 . 23 LEU HD1 H 0.83 . 2 126 . 23 LEU HD2 H 0.63 . 2 127 . 23 LEU CA C 57.6 . 1 128 . 23 LEU CB C 42.2 . 1 129 . 23 LEU CG C 27.6 . 1 130 . 23 LEU CD1 C 23.5 . 2 131 . 23 LEU CD2 C 26.5 . 2 132 . 23 LEU N N 120.1 . 1 133 . 24 LEU H H 8.19 . 1 134 . 24 LEU HA H 3.96 . 1 135 . 24 LEU HB2 H 0.20 . 2 136 . 24 LEU HB3 H 1.45 . 2 137 . 24 LEU HG H 1.71 . 1 138 . 24 LEU HD1 H 0.69 . 2 139 . 24 LEU HD2 H 0.52 . 2 140 . 24 LEU CA C 57.8 . 1 141 . 24 LEU CB C 40.1 . 1 142 . 24 LEU CG C 26.2 . 1 143 . 24 LEU CD1 C 23.1 . 2 144 . 24 LEU CD2 C 27.6 . 2 145 . 24 LEU N N 121.5 . 1 146 . 25 GLU H H 8.59 . 1 147 . 25 GLU HA H 4.02 . 1 148 . 25 GLU CA C 59.0 . 1 149 . 25 GLU CB C 28.9 . 1 150 . 25 GLU N N 121.4 . 1 151 . 26 ALA H H 7.49 . 1 152 . 26 ALA HA H 4.47 . 1 153 . 26 ALA HB H 1.54 . 1 154 . 26 ALA CA C 51.9 . 1 155 . 26 ALA CB C 18.9 . 1 156 . 26 ALA N N 120.6 . 1 157 . 27 GLY H H 7.60 . 1 158 . 27 GLY HA2 H 3.71 . 2 159 . 27 GLY HA3 H 4.41 . 2 160 . 27 GLY CA C 45.0 . 1 161 . 27 GLY N N 106.2 . 1 162 . 28 ALA H H 8.18 . 1 163 . 28 ALA HA H 4.17 . 1 164 . 28 ALA HB H 1.15 . 1 165 . 28 ALA CA C 52.7 . 1 166 . 28 ALA CB C 19.3 . 1 167 . 28 ALA N N 124.5 . 1 168 . 29 LEU H H 8.23 . 1 169 . 29 LEU HA H 4.12 . 1 170 . 29 LEU HG H 1.39 . 1 171 . 29 LEU HD1 H 0.93 . 2 172 . 29 LEU HD2 H 0.76 . 2 173 . 29 LEU CA C 58.5 . 1 174 . 29 LEU CB C 41.2 . 1 175 . 29 LEU CG C 27.6 . 1 176 . 29 LEU CD1 C 25.0 . 2 177 . 29 LEU CD2 C 27.4 . 2 178 . 29 LEU N N 124.5 . 1 179 . 30 PRO CA C 64.4 . 1 180 . 31 ASN H H 8.52 . 1 181 . 31 ASN HA H 4.68 . 1 182 . 31 ASN HB2 H 2.72 . 2 183 . 31 ASN HB3 H 2.80 . 2 184 . 31 ASN CA C 52.9 . 1 185 . 31 ASN CB C 39.4 . 1 186 . 31 ASN N N 113.4 . 1 187 . 32 ALA H H 7.04 . 1 188 . 32 ALA HA H 4.60 . 1 189 . 32 ALA HB H 1.45 . 1 190 . 32 ALA CA C 50.3 . 1 191 . 32 ALA CB C 18.6 . 1 192 . 32 ALA N N 125.6 . 1 193 . 33 PRO CA C 63.6 . 1 194 . 34 ASN H H 7.63 . 1 195 . 34 ASN N N 115.7 . 1 196 . 35 SER CA C 61.8 . 1 197 . 36 TYR H H 7.34 . 1 198 . 36 TYR HA H 4.61 . 1 199 . 36 TYR HB2 H 3.33 . 2 200 . 36 TYR HB3 H 2.76 . 2 201 . 36 TYR HD1 H 7.03 . 2 202 . 36 TYR HD2 H 6.79 . 2 203 . 36 TYR CA C 57.1 . 1 204 . 36 TYR CB C 38.3 . 1 205 . 36 TYR N N 119.5 . 1 206 . 37 GLY H H 8.23 . 1 207 . 37 GLY HA2 H 3.70 . 2 208 . 37 GLY HA3 H 4.28 . 2 209 . 37 GLY CA C 45.9 . 1 210 . 37 GLY N N 108.7 . 1 211 . 38 ARG H H 7.97 . 1 212 . 38 ARG HA H 4.61 . 1 213 . 38 ARG HB2 H 1.53 . 1 214 . 38 ARG HB3 H 1.53 . 1 215 . 38 ARG HD2 H 3.04 . 2 216 . 38 ARG HD3 H 3.07 . 2 217 . 38 ARG CA C 54.5 . 1 218 . 38 ARG CB C 32.3 . 1 219 . 38 ARG CD C 43.5 . 1 220 . 38 ARG N N 120.6 . 1 221 . 39 ARG H H 8.96 . 1 222 . 39 ARG HA H 4.65 . 1 223 . 39 ARG N N 123.1 . 1 224 . 40 PRO CA C 66.6 . 1 225 . 41 ILE H H 8.83 . 1 226 . 41 ILE HA H 4.05 . 1 227 . 41 ILE HB H 1.67 . 1 228 . 41 ILE HG12 H 1.10 . 2 229 . 41 ILE HG13 H 1.77 . 2 230 . 41 ILE HG2 H 0.83 . 1 231 . 41 ILE HD1 H 0.77 . 1 232 . 41 ILE CA C 60.9 . 1 233 . 41 ILE CB C 39.4 . 1 234 . 41 ILE CG2 C 20.0 . 1 235 . 41 ILE CD1 C 15.7 . 1 236 . 41 ILE N N 115.2 . 1 237 . 42 GLN H H 7.59 . 1 238 . 42 GLN HA H 4.25 . 1 239 . 42 GLN CA C 57.1 . 1 240 . 42 GLN N N 113.8 . 1 241 . 43 VAL H H 7.05 . 1 242 . 43 VAL HA H 4.38 . 1 243 . 43 VAL HB H 2.40 . 1 244 . 43 VAL HG1 H 0.88 . 2 245 . 43 VAL HG2 H 0.83 . 2 246 . 43 VAL CA C 60.1 . 1 247 . 43 VAL CB C 32.4 . 1 248 . 43 VAL CG1 C 19.4 . 2 249 . 43 VAL CG2 C 22.5 . 2 250 . 43 VAL N N 109.0 . 1 251 . 44 MET H H 7.16 . 1 252 . 44 MET HA H 4.46 . 1 253 . 44 MET CA C 55.0 . 1 254 . 44 MET CB C 32.7 . 1 255 . 44 MET N N 118.8 . 1 256 . 45 MET H H 7.50 . 1 257 . 45 MET HA H 4.20 . 1 258 . 45 MET CA C 56.1 . 1 259 . 45 MET N N 123.8 . 1 260 . 46 MET H H 9.00 . 1 261 . 46 MET HA H 4.28 . 1 262 . 46 MET CA C 56.6 . 1 263 . 46 MET CB C 31.8 . 1 264 . 46 MET N N 131.0 . 1 265 . 47 GLY H H 7.84 . 1 266 . 47 GLY CA C 43.7 . 1 267 . 47 GLY N N 107.3 . 1 268 . 48 SER H H 7.57 . 1 269 . 48 SER HA H 4.63 . 1 270 . 48 SER HB2 H 3.97 . 1 271 . 48 SER HB3 H 3.97 . 1 272 . 48 SER CA C 55.0 . 1 273 . 48 SER CB C 61.8 . 1 274 . 48 SER N N 117.1 . 1 275 . 49 ALA H H 8.91 . 1 276 . 49 ALA CA C 55.4 . 1 277 . 49 ALA N N 124.5 . 1 278 . 50 ARG H H 8.20 . 1 279 . 50 ARG HA H 4.15 . 1 280 . 50 ARG HB2 H 1.80 . 1 281 . 50 ARG HB3 H 1.80 . 1 282 . 50 ARG HG2 H 1.71 . 2 283 . 50 ARG HG3 H 1.75 . 2 284 . 50 ARG HD2 H 3.18 . 2 285 . 50 ARG HD3 H 3.40 . 2 286 . 50 ARG CA C 58.1 . 1 287 . 50 ARG CB C 30.4 . 1 288 . 50 ARG CD C 43.3 . 1 289 . 50 ARG N N 115.8 . 1 290 . 51 VAL H H 7.65 . 1 291 . 51 VAL HA H 3.49 . 1 292 . 51 VAL HB H 2.41 . 1 293 . 51 VAL HG1 H 1.01 . 1 294 . 51 VAL HG2 H 1.01 . 1 295 . 51 VAL CA C 67.6 . 1 296 . 51 VAL CB C 31.0 . 1 297 . 51 VAL CG1 C 22.7 . 2 298 . 51 VAL CG2 C 25.0 . 2 299 . 51 VAL N N 120.0 . 1 300 . 52 ALA H H 7.26 . 1 301 . 52 ALA HA H 3.82 . 1 302 . 52 ALA HB H 1.41 . 1 303 . 52 ALA CA C 55.8 . 1 304 . 52 ALA CB C 17.9 . 1 305 . 52 ALA N N 122.0 . 1 306 . 53 GLU H H 8.56 . 1 307 . 53 GLU CA C 59.6 . 1 308 . 53 GLU CB C 30.8 . 1 309 . 53 GLU N N 117.0 . 1 310 . 54 LEU H H 7.91 . 1 311 . 54 LEU HA H 4.05 . 1 312 . 54 LEU HB2 H 1.94 . 1 313 . 54 LEU HB3 H 1.94 . 1 314 . 54 LEU HG H 1.73 . 1 315 . 54 LEU HD1 H 0.89 . 2 316 . 54 LEU HD2 H 0.83 . 2 317 . 54 LEU CA C 58.2 . 1 318 . 54 LEU CB C 43.2 . 1 319 . 54 LEU CG C 27.6 . 1 320 . 54 LEU CD1 C 24.1 . 2 321 . 54 LEU CD2 C 27.4 . 2 322 . 54 LEU N N 120.1 . 1 323 . 55 LEU H H 8.06 . 1 324 . 55 LEU HA H 3.80 . 1 325 . 55 LEU HB2 H 1.94 . 1 326 . 55 LEU HB3 H 1.94 . 1 327 . 55 LEU HG H 1.86 . 1 328 . 55 LEU HD1 H 0.80 . 2 329 . 55 LEU HD2 H 0.66 . 2 330 . 55 LEU CA C 58.4 . 1 331 . 55 LEU CB C 40.9 . 1 332 . 55 LEU CG C 27.1 . 1 333 . 55 LEU CD1 C 23.8 . 2 334 . 55 LEU CD2 C 27.0 . 2 335 . 55 LEU N N 118.0 . 1 336 . 56 LEU H H 8.46 . 1 337 . 56 LEU HA H 4.05 . 1 338 . 56 LEU HD1 H 0.78 . 2 339 . 56 LEU HD2 H 0.72 . 2 340 . 56 LEU CA C 58.0 . 1 341 . 56 LEU CB C 40.9 . 1 342 . 56 LEU CD1 C 22.7 . 2 343 . 56 LEU CD2 C 27.4 . 2 344 . 56 LEU N N 120.2 . 1 345 . 57 LEU H H 8.69 . 1 346 . 57 LEU HA H 4.11 . 1 347 . 57 LEU HB2 H 1.80 . 1 348 . 57 LEU HB3 H 1.80 . 1 349 . 57 LEU HG H 1.42 . 1 350 . 57 LEU HD1 H 0.83 . 2 351 . 57 LEU HD2 H 0.81 . 2 352 . 57 LEU CA C 57.7 . 1 353 . 57 LEU CB C 42.2 . 1 354 . 57 LEU CG C 26.8 . 1 355 . 57 LEU CD1 C 24.8 . 2 356 . 57 LEU CD2 C 25.1 . 2 357 . 57 LEU N N 125.2 . 1 358 . 58 HIS H H 7.37 . 1 359 . 58 HIS HA H 4.42 . 1 360 . 58 HIS HB2 H 2.85 . 1 361 . 58 HIS HB3 H 2.85 . 1 362 . 58 HIS HD2 H 7.31 . 1 363 . 58 HIS HE1 H 7.64 . 1 364 . 58 HIS CA C 57.2 . 1 365 . 58 HIS CB C 30.7 . 1 366 . 58 HIS N N 115.7 . 1 367 . 59 GLY H H 7.69 . 1 368 . 59 GLY HA2 H 3.78 . 2 369 . 59 GLY HA3 H 4.38 . 2 370 . 59 GLY CA C 45.4 . 1 371 . 59 GLY N N 106.3 . 1 372 . 60 ALA H H 8.56 . 1 373 . 60 ALA HA H 4.13 . 1 374 . 60 ALA HB H 1.04 . 1 375 . 60 ALA CA C 52.2 . 1 376 . 60 ALA CB C 19.5 . 1 377 . 60 ALA N N 124.1 . 1 378 . 61 GLU H H 8.91 . 1 379 . 61 GLU N N 126.8 . 1 380 . 63 ASN H H 9.22 . 1 381 . 63 ASN HA H 4.86 . 1 382 . 63 ASN CA C 54.0 . 1 383 . 63 ASN N N 120.4 . 1 384 . 64 CYS H H 7.16 . 1 385 . 64 CYS HA H 4.44 . 1 386 . 64 CYS HB2 H 2.78 . 2 387 . 64 CYS HB3 H 2.80 . 2 388 . 64 CYS CA C 56.2 . 1 389 . 64 CYS CB C 28.5 . 1 390 . 64 CYS N N 118.8 . 1 391 . 65 ALA H H 8.18 . 1 392 . 65 ALA HA H 4.88 . 1 393 . 65 ALA HB H 1.04 . 1 394 . 65 ALA CA C 49.5 . 1 395 . 65 ALA CB C 21.8 . 1 396 . 65 ALA N N 121.5 . 1 397 . 66 ASP H H 8.04 . 1 398 . 66 ASP HA H 4.96 . 1 399 . 66 ASP HB2 H 2.71 . 2 400 . 66 ASP HB3 H 2.95 . 2 401 . 66 ASP CA C 52.2 . 1 402 . 66 ASP CB C 43.0 . 1 403 . 66 ASP N N 125.0 . 1 404 . 67 PRO CA C 63.8 . 1 405 . 68 ALA H H 8.22 . 1 406 . 68 ALA HA H 4.37 . 1 407 . 68 ALA HB H 1.49 . 1 408 . 68 ALA CA C 54.0 . 1 409 . 68 ALA CB C 19.9 . 1 410 . 68 ALA N N 119.4 . 1 411 . 69 THR H H 8.12 . 1 412 . 69 THR HA H 3.98 . 1 413 . 69 THR HB H 3.98 . 1 414 . 69 THR CA C 61.3 . 1 415 . 69 THR CB C 67.0 . 1 416 . 69 THR N N 107.6 . 1 417 . 70 LEU H H 8.36 . 1 418 . 70 LEU HA H 3.98 . 1 419 . 70 LEU HB2 H 1.77 . 1 420 . 70 LEU HB3 H 1.77 . 1 421 . 70 LEU HG H 1.38 . 1 422 . 70 LEU HD1 H 0.77 . 2 423 . 70 LEU HD2 H 0.73 . 2 424 . 70 LEU CA C 55.9 . 1 425 . 70 LEU CB C 39.5 . 1 426 . 70 LEU CG C 27.5 . 1 427 . 70 LEU CD1 C 22.7 . 2 428 . 70 LEU CD2 C 25.5 . 2 429 . 70 LEU N N 119.5 . 1 430 . 71 THR H H 7.72 . 1 431 . 71 THR HA H 3.93 . 1 432 . 71 THR HB H 3.99 . 1 433 . 71 THR HG2 H 1.33 . 1 434 . 71 THR CA C 64.4 . 1 435 . 71 THR CB C 69.0 . 1 436 . 71 THR CG2 C 23.1 . 1 437 . 71 THR N N 117.9 . 1 438 . 73 PRO CA C 66.6 . 1 439 . 74 VAL H H 8.39 . 1 440 . 74 VAL HA H 3.80 . 1 441 . 74 VAL HB H 1.88 . 1 442 . 74 VAL HG1 H 0.85 . 1 443 . 74 VAL HG2 H 0.85 . 1 444 . 74 VAL CA C 65.5 . 1 445 . 74 VAL CG1 C 19.1 . 1 446 . 74 VAL CG2 C 19.1 . 1 447 . 74 VAL N N 107.7 . 1 448 . 75 HIS H H 7.93 . 1 449 . 75 HIS HA H 4.00 . 1 450 . 75 HIS HB2 H 3.22 . 2 451 . 75 HIS HB3 H 3.25 . 2 452 . 75 HIS HD2 H 6.57 . 1 453 . 75 HIS HE1 H 7.47 . 1 454 . 75 HIS CA C 63.7 . 1 455 . 75 HIS CB C 31.8 . 1 456 . 75 HIS N N 120.0 . 1 457 . 76 ASP H H 7.14 . 1 458 . 76 ASP HA H 4.69 . 1 459 . 76 ASP HB2 H 2.75 . 2 460 . 76 ASP HB3 H 2.85 . 2 461 . 76 ASP CA C 58.0 . 1 462 . 76 ASP CB C 41.3 . 1 463 . 76 ASP N N 119.0 . 1 464 . 77 ALA H H 8.85 . 1 465 . 77 ALA HA H 4.02 . 1 466 . 77 ALA HB H 1.41 . 1 467 . 77 ALA CA C 55.9 . 1 468 . 77 ALA CB C 17.7 . 1 469 . 77 ALA N N 122.8 . 1 470 . 78 ALA H H 7.74 . 1 471 . 78 ALA HA H 3.92 . 1 472 . 78 ALA HB H 1.48 . 1 473 . 78 ALA CA C 55.1 . 1 474 . 78 ALA CB C 19.6 . 1 475 . 78 ALA N N 119.0 . 1 476 . 79 ARG H H 8.60 . 1 477 . 79 ARG HA H 3.81 . 1 478 . 79 ARG HD2 H 3.27 . 2 479 . 79 ARG HD3 H 3.40 . 2 480 . 79 ARG CA C 58.7 . 1 481 . 79 ARG CB C 30.7 . 1 482 . 79 ARG CD C 43.3 . 1 483 . 79 ARG N N 117.9 . 1 484 . 80 GLU H H 7.87 . 1 485 . 80 GLU HA H 4.12 . 1 486 . 80 GLU CA C 56.6 . 1 487 . 80 GLU CB C 30.8 . 1 488 . 80 GLU N N 115.2 . 1 489 . 81 GLY H H 7.15 . 1 490 . 81 GLY HA2 H 2.48 . 2 491 . 81 GLY HA3 H 2.74 . 2 492 . 81 GLY CA C 44.7 . 1 493 . 81 GLY N N 107.7 . 1 494 . 82 PHE H H 7.64 . 1 495 . 82 PHE HA H 4.79 . 1 496 . 82 PHE HB2 H 3.35 . 2 497 . 82 PHE HB3 H 2.54 . 2 498 . 82 PHE HD1 H 7.02 . 1 499 . 82 PHE HD2 H 7.02 . 1 500 . 82 PHE HE1 H 7.49 . 1 501 . 82 PHE HE2 H 7.49 . 1 502 . 82 PHE HZ H 7.28 . 1 503 . 82 PHE CA C 56.4 . 1 504 . 82 PHE CB C 38.5 . 1 505 . 82 PHE N N 121.6 . 1 506 . 83 LEU H H 8.20 . 1 507 . 83 LEU HA H 3.71 . 1 508 . 83 LEU HG H 1.37 . 1 509 . 83 LEU HD1 H 0.57 . 2 510 . 83 LEU HD2 H 0.78 . 2 511 . 83 LEU CA C 58.0 . 1 512 . 83 LEU CB C 44.4 . 1 513 . 83 LEU CG C 26.8 . 1 514 . 83 LEU CD1 C 23.7 . 1 515 . 83 LEU CD2 C 23.7 . 1 516 . 83 LEU N N 127.4 . 1 517 . 84 ASP H H 8.73 . 1 518 . 84 ASP HA H 4.12 . 1 519 . 84 ASP CA C 57.6 . 1 520 . 84 ASP CB C 38.6 . 1 521 . 84 ASP N N 117.2 . 1 522 . 85 THR H H 7.44 . 1 523 . 85 THR HA H 3.61 . 1 524 . 85 THR HB H 4.08 . 1 525 . 85 THR HG2 H 1.13 . 1 526 . 85 THR CA C 65.9 . 1 527 . 85 THR CB C 67.8 . 1 528 . 85 THR CG2 C 23.4 . 1 529 . 85 THR N N 118.4 . 1 530 . 86 LEU H H 7.71 . 1 531 . 86 LEU HA H 3.78 . 1 532 . 86 LEU HB2 H 1.86 . 2 533 . 86 LEU HB3 H 1.49 . 2 534 . 86 LEU HG H 1.54 . 1 535 . 86 LEU HD1 H 0.88 . 2 536 . 86 LEU HD2 H 0.86 . 2 537 . 86 LEU CA C 58.9 . 1 538 . 86 LEU CB C 42.1 . 1 539 . 86 LEU CG C 27.3 . 1 540 . 86 LEU CD1 C 25.6 . 2 541 . 86 LEU CD2 C 26.7 . 2 542 . 86 LEU N N 123.6 . 1 543 . 87 VAL H H 8.61 . 1 544 . 87 VAL HA H 3.55 . 1 545 . 87 VAL HB H 1.98 . 1 546 . 87 VAL HG1 H 0.86 . 2 547 . 87 VAL HG2 H 0.49 . 2 548 . 87 VAL CA C 67.2 . 1 549 . 87 VAL CB C 31.5 . 1 550 . 87 VAL CG1 C 21.1 . 2 551 . 87 VAL CG2 C 22.2 . 2 552 . 87 VAL N N 120.3 . 1 553 . 88 VAL H H 6.67 . 1 554 . 88 VAL HA H 3.64 . 1 555 . 88 VAL HB H 2.24 . 1 556 . 88 VAL HG1 H 0.93 . 2 557 . 88 VAL HG2 H 1.11 . 2 558 . 88 VAL CA C 66.5 . 1 559 . 88 VAL CB C 31.4 . 1 560 . 88 VAL CG1 C 22.0 . 2 561 . 88 VAL CG2 C 23.0 . 2 562 . 88 VAL N N 119.3 . 1 563 . 89 LEU H H 8.05 . 1 564 . 89 LEU HA H 3.85 . 1 565 . 89 LEU HB2 H 2.07 . 1 566 . 89 LEU HB3 H 2.07 . 1 567 . 89 LEU HG H 1.73 . 1 568 . 89 LEU HD1 H 0.87 . 2 569 . 89 LEU HD2 H 0.64 . 2 570 . 89 LEU CA C 58.3 . 1 571 . 89 LEU CB C 41.7 . 1 572 . 89 LEU CG C 26.9 . 1 573 . 89 LEU CD1 C 23.7 . 2 574 . 89 LEU CD2 C 26.2 . 2 575 . 89 LEU N N 120.5 . 1 576 . 90 HIS H H 9.08 . 1 577 . 90 HIS HA H 4.62 . 1 578 . 90 HIS HB2 H 3.18 . 2 579 . 90 HIS HB3 H 3.56 . 2 580 . 90 HIS HD2 H 7.38 . 1 581 . 90 HIS HE1 H 7.69 . 1 582 . 90 HIS CA C 58.1 . 1 583 . 90 HIS CB C 31.9 . 1 584 . 90 HIS N N 121.4 . 1 585 . 91 ARG H H 9.12 . 1 586 . 91 ARG HA H 3.78 . 1 587 . 91 ARG HB2 H 1.90 . 1 588 . 91 ARG HB3 H 1.90 . 1 589 . 91 ARG HG2 H 1.70 . 2 590 . 91 ARG HG3 H 2.14 . 2 591 . 91 ARG HD2 H 3.11 . 1 592 . 91 ARG HD3 H 3.11 . 1 593 . 91 ARG CA C 58.9 . 1 594 . 91 ARG CB C 30.1 . 1 595 . 91 ARG CG C 31.9 . 1 596 . 91 ARG CD C 44.0 . 1 597 . 91 ARG N N 121.4 . 1 598 . 92 ALA H H 7.33 . 1 599 . 92 ALA HA H 4.47 . 1 600 . 92 ALA HB H 1.62 . 1 601 . 92 ALA CA C 51.8 . 1 602 . 92 ALA CB C 21.2 . 1 603 . 92 ALA N N 119.8 . 1 604 . 93 GLY H H 7.89 . 1 605 . 93 GLY HA2 H 3.68 . 2 606 . 93 GLY HA3 H 4.41 . 2 607 . 93 GLY CA C 44.7 . 1 608 . 93 GLY N N 105.6 . 1 609 . 94 ALA H H 8.41 . 1 610 . 94 ALA HA H 4.23 . 1 611 . 94 ALA HB H 1.11 . 1 612 . 94 ALA CA C 52.4 . 1 613 . 94 ALA CB C 19.8 . 1 614 . 94 ALA N N 125.2 . 1 615 . 95 ARG H H 7.09 . 1 616 . 95 ARG HA H 4.29 . 1 617 . 95 ARG CA C 55.8 . 1 618 . 95 ARG N N 117.8 . 1 619 . 96 LEU H H 8.90 . 1 620 . 96 LEU HA H 4.33 . 1 621 . 96 LEU HG H 1.55 . 1 622 . 96 LEU HD1 H 0.52 . 2 623 . 96 LEU HD2 H 0.17 . 2 624 . 96 LEU CA C 54.3 . 1 625 . 96 LEU CB C 42.0 . 1 626 . 96 LEU CG C 26.7 . 1 627 . 96 LEU CD1 C 21.9 . 2 628 . 96 LEU CD2 C 24.7 . 2 629 . 96 LEU N N 119.6 . 1 630 . 97 ASP H H 8.94 . 1 631 . 97 ASP HA H 4.65 . 1 632 . 97 ASP HB2 H 2.88 . 1 633 . 97 ASP HB3 H 2.88 . 1 634 . 97 ASP CA C 52.6 . 1 635 . 97 ASP CB C 38.8 . 1 636 . 97 ASP N N 120.9 . 1 637 . 98 VAL H H 6.67 . 1 638 . 98 VAL HA H 4.36 . 1 639 . 98 VAL HB H 1.89 . 1 640 . 98 VAL HG1 H 0.67 . 2 641 . 98 VAL HG2 H 0.86 . 2 642 . 98 VAL CA C 58.6 . 1 643 . 98 VAL CB C 33.6 . 1 644 . 98 VAL CG1 C 17.7 . 2 645 . 98 VAL CG2 C 22.6 . 2 646 . 98 VAL N N 111.5 . 1 647 . 99 ARG H H 8.62 . 1 648 . 99 ARG HA H 4.96 . 1 649 . 99 ARG HB2 H 1.36 . 1 650 . 99 ARG HB3 H 1.36 . 1 651 . 99 ARG HD2 H 3.11 . 1 652 . 99 ARG HD3 H 3.11 . 1 653 . 99 ARG CA C 54.6 . 1 654 . 99 ARG N N 123.4 . 1 655 . 100 ASP H H 8.27 . 1 656 . 100 ASP HA H 4.61 . 1 657 . 100 ASP HB2 H 2.13 . 2 658 . 100 ASP HB3 H 2.39 . 2 659 . 100 ASP CA C 53.0 . 1 660 . 100 ASP CB C 37.0 . 1 661 . 100 ASP N N 123.8 . 1 662 . 101 ALA HA H 3.77 . 1 663 . 101 ALA HB H 0.49 . 1 664 . 101 ALA CA C 54.2 . 1 665 . 101 ALA CB C 17.5 . 1 666 . 102 TRP H H 8.24 . 1 667 . 102 TRP HA H 4.57 . 1 668 . 102 TRP HB2 H 3.12 . 2 669 . 102 TRP HB3 H 3.51 . 2 670 . 102 TRP CA C 58.6 . 1 671 . 102 TRP N N 119.4 . 1 672 . 103 GLY H H 8.30 . 1 673 . 103 GLY HA2 H 3.74 . 2 674 . 103 GLY HA3 H 4.30 . 2 675 . 103 GLY CA C 45.7 . 1 676 . 103 GLY N N 119.4 . 1 677 . 104 ARG H H 8.76 . 1 678 . 104 ARG HA H 4.66 . 1 679 . 104 ARG CA C 56.8 . 1 680 . 104 ARG CB C 30.4 . 1 681 . 104 ARG N N 122.1 . 1 682 . 105 LEU H H 9.68 . 1 683 . 105 LEU HA H 5.25 . 1 684 . 105 LEU HG H 1.77 . 1 685 . 105 LEU HD1 H 0.82 . 2 686 . 105 LEU HD2 H 0.95 . 2 687 . 105 LEU CA C 53.1 . 1 688 . 105 LEU CG C 27.7 . 1 689 . 105 LEU CD1 C 23.8 . 2 690 . 105 LEU CD2 C 26.2 . 2 691 . 105 LEU N N 125.9 . 1 692 . 106 PRO CA C 66.9 . 1 693 . 107 VAL H H 8.10 . 1 694 . 107 VAL HA H 3.76 . 1 695 . 107 VAL HB H 2.01 . 1 696 . 107 VAL HG1 H 0.90 . 2 697 . 107 VAL HG2 H 1.02 . 2 698 . 107 VAL CA C 64.9 . 1 699 . 107 VAL CB C 30.6 . 1 700 . 107 VAL CG1 C 19.2 . 2 701 . 107 VAL CG2 C 22.9 . 2 702 . 107 VAL N N 114.8 . 1 703 . 108 ASP H H 6.99 . 1 704 . 108 ASP HA H 4.49 . 1 705 . 108 ASP CA C 57.2 . 1 706 . 108 ASP CB C 40.8 . 1 707 . 108 ASP N N 122.9 . 1 708 . 109 LEU H H 7.31 . 1 709 . 109 LEU HA H 4.12 . 1 710 . 109 LEU HG H 1.80 . 1 711 . 109 LEU CA C 57.2 . 1 712 . 109 LEU CB C 42.0 . 1 713 . 109 LEU CG C 27.4 . 1 714 . 109 LEU N N 120.4 . 1 715 . 110 ALA H H 7.78 . 1 716 . 110 ALA HA H 4.12 . 1 717 . 110 ALA HB H 1.52 . 1 718 . 110 ALA CA C 55.0 . 1 719 . 110 ALA CB C 18.6 . 1 720 . 110 ALA N N 119.5 . 1 721 . 111 GLU H H 8.36 . 1 722 . 111 GLU HA H 3.94 . 1 723 . 111 GLU CA C 59.1 . 1 724 . 111 GLU CB C 29.7 . 1 725 . 111 GLU N N 116.9 . 1 726 . 112 GLU H H 8.07 . 1 727 . 112 GLU CA C 59.1 . 1 728 . 112 GLU CB C 29.5 . 1 729 . 112 GLU N N 121.8 . 1 730 . 113 LEU H H 7.33 . 1 731 . 113 LEU HA H 4.22 . 1 732 . 113 LEU HG H 1.80 . 1 733 . 113 LEU HD1 H 1.02 . 2 734 . 113 LEU HD2 H 0.84 . 2 735 . 113 LEU CA C 53.8 . 1 736 . 113 LEU CB C 40.9 . 1 737 . 113 LEU CG C 27.9 . 1 738 . 113 LEU CD1 C 26.2 . 2 739 . 113 LEU CD2 C 22.7 . 2 740 . 113 LEU N N 117.6 . 1 741 . 114 GLY H H 7.33 . 1 742 . 114 GLY HA2 H 3.71 . 2 743 . 114 GLY HA3 H 3.94 . 2 744 . 114 GLY CA C 46.0 . 1 745 . 114 GLY N N 107.4 . 1 746 . 115 HIS H H 8.15 . 1 747 . 115 HIS HA H 5.19 . 1 748 . 115 HIS HB2 H 3.04 . 2 749 . 115 HIS HB3 H 3.08 . 2 750 . 115 HIS HD2 H 7.24 . 1 751 . 115 HIS HE1 H 7.59 . 1 752 . 115 HIS CA C 53.1 . 1 753 . 115 HIS CB C 28.7 . 1 754 . 115 HIS N N 121.6 . 1 755 . 116 ARG H H 8.08 . 1 756 . 116 ARG N N 125.6 . 1 757 . 117 ASP CA C 57.4 . 1 758 . 118 VAL H H 7.88 . 1 759 . 118 VAL HA H 3.64 . 1 760 . 118 VAL HB H 2.15 . 1 761 . 118 VAL HG1 H 0.82 . 2 762 . 118 VAL HG2 H 0.92 . 2 763 . 118 VAL CA C 66.1 . 1 764 . 118 VAL CB C 31.4 . 1 765 . 118 VAL CG1 C 22.6 . 2 766 . 118 VAL CG2 C 23.0 . 2 767 . 118 VAL N N 122.9 . 1 768 . 119 ALA H H 8.49 . 1 769 . 119 ALA HA H 3.94 . 1 770 . 119 ALA HB H 1.46 . 1 771 . 119 ALA CA C 55.8 . 1 772 . 119 ALA CB C 18.3 . 1 773 . 119 ALA N N 122.3 . 1 774 . 120 ARG H H 8.23 . 1 775 . 120 ARG HA H 3.91 . 1 776 . 120 ARG CA C 59.7 . 1 777 . 120 ARG CB C 29.9 . 1 778 . 120 ARG N N 117.8 . 1 779 . 121 TYR H H 7.67 . 1 780 . 121 TYR HA H 4.03 . 1 781 . 121 TYR HB2 H 3.04 . 2 782 . 121 TYR HB3 H 3.10 . 2 783 . 121 TYR HD1 H 6.81 . 1 784 . 121 TYR HD2 H 6.81 . 1 785 . 121 TYR HE1 H 6.57 . 1 786 . 121 TYR HE2 H 6.57 . 1 787 . 121 TYR CA C 61.7 . 1 788 . 121 TYR CB C 38.8 . 1 789 . 121 TYR N N 121.5 . 1 790 . 122 LEU H H 8.35 . 1 791 . 122 LEU HA H 3.75 . 1 792 . 122 LEU HB2 H 1.72 . 1 793 . 122 LEU HB3 H 1.72 . 1 794 . 122 LEU HG H 1.95 . 1 795 . 122 LEU HD1 H 0.99 . 2 796 . 122 LEU HD2 H 0.70 . 2 797 . 122 LEU CA C 57.6 . 1 798 . 122 LEU CB C 41.7 . 1 799 . 122 LEU CG C 26.9 . 1 800 . 122 LEU CD1 C 25.2 . 2 801 . 122 LEU CD2 C 26.4 . 2 802 . 122 LEU N N 119.6 . 1 803 . 123 ARG H H 8.60 . 1 804 . 123 ARG HA H 4.02 . 1 805 . 123 ARG HB2 H 1.77 . 2 806 . 123 ARG HB3 H 1.90 . 2 807 . 123 ARG HD2 H 3.05 . 2 808 . 123 ARG HD3 H 3.16 . 2 809 . 123 ARG CA C 58.8 . 1 810 . 123 ARG CB C 30.0 . 1 811 . 123 ARG CD C 43.3 . 1 812 . 123 ARG N N 120.4 . 1 813 . 124 ALA H H 7.65 . 1 814 . 124 ALA HA H 4.13 . 1 815 . 124 ALA HB H 1.35 . 1 816 . 124 ALA CA C 54.0 . 1 817 . 124 ALA CB C 18.1 . 1 818 . 124 ALA N N 122.8 . 1 819 . 125 ALA H H 7.84 . 1 820 . 125 ALA HA H 4.01 . 1 821 . 125 ALA HB H 0.95 . 1 822 . 125 ALA CA C 53.4 . 1 823 . 125 ALA CB C 18.4 . 1 824 . 125 ALA N N 121.4 . 1 825 . 126 ALA H H 7.41 . 1 826 . 126 ALA HA H 4.28 . 1 827 . 126 ALA HB H 1.41 . 1 828 . 126 ALA CA C 52.8 . 1 829 . 126 ALA CB C 19.1 . 1 830 . 126 ALA N N 120.9 . 1 831 . 127 GLY H H 7.90 . 1 832 . 127 GLY N N 107.6 . 1 833 . 128 GLY H H 8.13 . 1 834 . 128 GLY N N 108.8 . 1 835 . 129 THR HA H 4.34 . 1 836 . 129 THR HB H 4.20 . 1 837 . 129 THR HG2 H 1.17 . 1 838 . 129 THR CA C 62.2 . 1 839 . 129 THR CB C 69.7 . 1 840 . 129 THR CG2 C 21.7 . 1 841 . 130 ARG CA C 56.4 . 1 842 . 131 GLY H H 8.16 . 1 843 . 131 GLY HA2 H 3.71 . 2 844 . 131 GLY HA3 H 4.06 . 2 845 . 131 GLY CA C 44.3 . 1 846 . 131 GLY N N 110.5 . 1 847 . 132 SER CA C 61.5 . 1 848 . 133 ASN H H 8.64 . 1 849 . 133 ASN HA H 4.44 . 1 850 . 133 ASN CA C 50.8 . 1 851 . 133 ASN CB C 38.5 . 1 852 . 133 ASN N N 119.1 . 1 853 . 134 HIS HA H 4.51 . 1 854 . 134 HIS HB2 H 3.01 . 2 855 . 134 HIS HB3 H 3.11 . 2 856 . 134 HIS HD2 H 6.95 . 1 857 . 134 HIS HE1 H 7.74 . 1 858 . 134 HIS CA C 57.2 . 1 859 . 134 HIS CB C 30.7 . 1 860 . 136 ARG HA H 4.30 . 1 861 . 136 ARG CA C 55.9 . 1 862 . 136 ARG CB C 30.8 . 1 863 . 137 ILE H H 8.28 . 1 864 . 137 ILE HA H 4.15 . 1 865 . 137 ILE HB H 1.84 . 1 866 . 137 ILE HG12 H 1.13 . 2 867 . 137 ILE HG13 H 1.41 . 2 868 . 137 ILE HG2 H 0.89 . 1 869 . 137 ILE HD1 H 0.83 . 1 870 . 137 ILE CA C 61.1 . 1 871 . 137 ILE CB C 38.6 . 1 872 . 137 ILE CG1 C 27.5 . 1 873 . 137 ILE CG2 C 17.7 . 1 874 . 137 ILE CD1 C 13.3 . 1 875 . 137 ILE N N 123.1 . 1 876 . 138 ASP H H 8.40 . 1 877 . 138 ASP HA H 4.58 . 1 878 . 138 ASP HB2 H 2.63 . 2 879 . 138 ASP HB3 H 2.67 . 2 880 . 138 ASP CA C 54.1 . 1 881 . 138 ASP CB C 41.1 . 1 882 . 138 ASP N N 124.6 . 1 883 . 139 ALA H H 8.11 . 1 884 . 139 ALA HA H 4.27 . 1 885 . 139 ALA HB H 1.32 . 1 886 . 139 ALA CA C 52.5 . 1 887 . 139 ALA CB C 19.3 . 1 888 . 139 ALA N N 125.1 . 1 889 . 140 ALA H H 8.29 . 1 890 . 140 ALA HA H 4.28 . 1 891 . 140 ALA HB H 1.37 . 1 892 . 140 ALA CA C 52.5 . 1 893 . 140 ALA CB C 19.3 . 1 894 . 140 ALA N N 124.0 . 1 895 . 141 GLU H H 8.31 . 1 896 . 141 GLU HA H 4.30 . 1 897 . 141 GLU HB2 H 1.94 . 2 898 . 141 GLU HB3 H 2.08 . 2 899 . 141 GLU HG2 H 2.27 . 1 900 . 141 GLU HG3 H 2.27 . 1 901 . 141 GLU CA C 56.3 . 1 902 . 141 GLU CB C 30.6 . 1 903 . 141 GLU CG C 36.4 . 1 904 . 141 GLU N N 120.5 . 1 905 . 142 GLY H H 8.21 . 1 906 . 142 GLY HA2 H 4.04 . 2 907 . 142 GLY HA3 H 4.18 . 2 908 . 142 GLY CA C 44.5 . 1 909 . 142 GLY N N 111.0 . 1 910 . 143 PRO HA H 4.45 . 1 911 . 143 PRO HB2 H 2.00 . 2 912 . 143 PRO HB3 H 2.29 . 2 913 . 143 PRO HG2 H 2.00 . 1 914 . 143 PRO HG3 H 2.00 . 1 915 . 143 PRO HD2 H 3.64 . 1 916 . 143 PRO HD3 H 3.64 . 1 917 . 143 PRO CA C 63.0 . 1 918 . 143 PRO CB C 32.1 . 1 919 . 143 PRO CG C 27.2 . 1 920 . 143 PRO CD C 49.7 . 1 921 . 144 SER H H 8.48 . 1 922 . 144 SER HA H 4.47 . 1 923 . 144 SER HB2 H 3.86 . 1 924 . 144 SER HB3 H 3.86 . 1 925 . 144 SER CA C 58.0 . 1 926 . 144 SER CB C 63.7 . 1 927 . 144 SER N N 117.0 . 1 928 . 145 ASP H H 8.37 . 1 929 . 145 ASP HA H 4.60 . 1 930 . 145 ASP HB2 H 2.59 . 2 931 . 145 ASP HB3 H 2.62 . 2 932 . 145 ASP CA C 54.1 . 1 933 . 145 ASP CB C 41.1 . 1 934 . 145 ASP N N 123.4 . 1 935 . 146 ILE H H 8.10 . 1 936 . 146 ILE HA H 4.45 . 1 937 . 146 ILE HB H 1.83 . 1 938 . 146 ILE HG12 H 1.14 . 2 939 . 146 ILE HG13 H 1.50 . 2 940 . 146 ILE HG2 H 0.95 . 1 941 . 146 ILE HD1 H 0.84 . 1 942 . 146 ILE CA C 58.4 . 1 943 . 146 ILE CB C 38.7 . 1 944 . 146 ILE CG1 C 26.8 . 1 945 . 146 ILE CG2 C 17.2 . 1 946 . 146 ILE CD1 C 12.7 . 1 947 . 146 ILE N N 123.4 . 1 948 . 147 PRO HA H 4.40 . 1 949 . 147 PRO HB2 H 1.99 . 2 950 . 147 PRO HB3 H 2.27 . 2 951 . 147 PRO HG2 H 1.97 . 1 952 . 147 PRO HG3 H 1.97 . 1 953 . 147 PRO HD2 H 3.70 . 2 954 . 147 PRO HD3 H 3.87 . 2 955 . 147 PRO CA C 63.2 . 1 956 . 147 PRO CB C 32.0 . 1 957 . 147 PRO CG C 27.3 . 1 958 . 147 PRO CD C 51.2 . 1 959 . 148 ASP H H 7.95 . 1 960 . 148 ASP HA H 4.33 . 1 961 . 148 ASP HB2 H 2.52 . 2 962 . 148 ASP HB3 H 2.64 . 2 963 . 148 ASP CA C 55.9 . 1 964 . 148 ASP CB C 42.1 . 1 965 . 148 ASP N N 127.2 . 1 stop_ save_