data_2031 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Secondary Structure and Topology of Human Interleukin 4 in Solution ; _BMRB_accession_number 2031 _BMRB_flat_file_name bmr2031.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Redfield Christina . . 2 Smith Lorna J. . 3 Boyd Jonathan . . 4 Lawrence G. Mark.P. . 5 Edwards Robert G. . 6 Smith Richard A.G. . 7 Dobson Christopher M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 566 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-16 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Redfield, Christina, Smith, Lorna J., Boyd, Jonathan, Lawrence, G. Mark P., Edwards, Robert G., Smith, Richard A.G., Dobson, Christopher M., "Secondary Structure and Topology of Human Interleukin 4 in Solution," Biochemistry 30 (46), 11029-11035 (1991). ; _Citation_title 'Secondary Structure and Topology of Human Interleukin 4 in Solution' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Redfield Christina . . 2 Smith Lorna J. . 3 Boyd Jonathan . . 4 Lawrence G. Mark.P. . 5 Edwards Robert G. . 6 Smith Richard A.G. . 7 Dobson Christopher M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue 46 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11029 _Page_last 11035 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_interleukin_4 _Saveframe_category molecular_system _Mol_system_name 'interleukin 4' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'interleukin 4' $interleukin_4 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_interleukin_4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'interleukin 4' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MHKCDITLQEIIKTLNSLTE QKTLCTELTVTDIFAASKNT TEKETFCRAATVLXQFYSHH EKDTRCLGATAQQFHRHKQL IRFLKRLDRNLWGLAGLNSC PVKEANQSTLENFLERLKTI MREKYSKCSS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 LYS 4 CYS 5 ASP 6 ILE 7 THR 8 LEU 9 GLN 10 GLU 11 ILE 12 ILE 13 LYS 14 THR 15 LEU 16 ASN 17 SER 18 LEU 19 THR 20 GLU 21 GLN 22 LYS 23 THR 24 LEU 25 CYS 26 THR 27 GLU 28 LEU 29 THR 30 VAL 31 THR 32 ASP 33 ILE 34 PHE 35 ALA 36 ALA 37 SER 38 LYS 39 ASN 40 THR 41 THR 42 GLU 43 LYS 44 GLU 45 THR 46 PHE 47 CYS 48 ARG 49 ALA 50 ALA 51 THR 52 VAL 53 LEU 54 X 55 GLN 56 PHE 57 TYR 58 SER 59 HIS 60 HIS 61 GLU 62 LYS 63 ASP 64 THR 65 ARG 66 CYS 67 LEU 68 GLY 69 ALA 70 THR 71 ALA 72 GLN 73 GLN 74 PHE 75 HIS 76 ARG 77 HIS 78 LYS 79 GLN 80 LEU 81 ILE 82 ARG 83 PHE 84 LEU 85 LYS 86 ARG 87 LEU 88 ASP 89 ARG 90 ASN 91 LEU 92 TRP 93 GLY 94 LEU 95 ALA 96 GLY 97 LEU 98 ASN 99 SER 100 CYS 101 PRO 102 VAL 103 LYS 104 GLU 105 ALA 106 ASN 107 GLN 108 SER 109 THR 110 LEU 111 GLU 112 ASN 113 PHE 114 LEU 115 GLU 116 ARG 117 LEU 118 LYS 119 THR 120 ILE 121 MET 122 ARG 123 GLU 124 LYS 125 TYR 126 SER 127 LYS 128 CYS 129 SER 130 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 4094 "human Interleukin 4" 99.23 133 97.67 99.22 3.14e-86 PDB 1BBN "Three-Dimensional Solution Structure Of Human Interleukin-4 By Multi- Dimensional Heteronuclear Magnetic Resonance Spectroscopy" 99.23 133 97.67 99.22 3.14e-86 PDB 1BCN "Three-Dimensional Solution Structure Of Human Interleukin-4 By Multi-Dimensional Heteronuclear Magnetic Resonance Spectroscopy" 99.23 133 97.67 99.22 3.14e-86 PDB 1CYL "Aspects Of Receptor Binding And Signalling Of Interleukin-4 Investigated By Site-Directed Mutagenesis And Nmr Spectroscopy" 99.23 129 99.22 99.22 2.75e-87 PDB 1HIJ "Interleukin-4 Mutant With Arg 88 Replaced With Gln (R88q)" 99.23 129 98.45 99.22 1.16e-86 PDB 1HIK "Interleukin-4 (Wild-Type)" 99.23 129 99.22 99.22 2.75e-87 PDB 1HZI "Interleukin-4 Mutant E9a" 99.23 129 98.45 98.45 1.90e-86 PDB 1IAR "Interleukin-4 RECEPTOR ALPHA CHAIN COMPLEX" 99.23 129 99.22 99.22 2.75e-87 PDB 1ITI "The High Resolution Three-Dimensional Solution Structure Of Human Interleukin-4 Determined By Multi-Dimensional Heteronuclear M" 99.23 133 97.67 99.22 3.14e-86 PDB 1ITL "Human Interleukin 4: The Solution Structure Of A Four-Helix- Bundle Protein" 100.00 130 99.23 99.23 2.41e-88 PDB 1ITM "Analysis Of The Solution Structure Of Human Interleukin 4 Determined By Heteronuclear Three-Dimensional Nuclear Magnetic Resona" 100.00 130 99.23 99.23 2.41e-88 PDB 1RCB "Crystal Structure Of Human Recombinant Interleukin-4 At 2.25 Angstroms Resolution" 99.23 129 99.22 99.22 2.75e-87 PDB 2B8U "Crystal Structure Of Wildtype Human Interleukin-4" 99.23 129 99.22 99.22 2.75e-87 PDB 2B8X "Crystal Stucture Of The Interleukin-4 Variant F82d" 99.23 129 98.45 98.45 6.89e-86 PDB 2B8Y "Crystal Structure Of The Interleukin-4 Variant T13df82d" 99.23 129 97.67 97.67 3.91e-85 PDB 2B8Z "Crystal Structure Of The Interleukin-4 Variant R85a" 99.23 129 98.45 98.45 2.69e-86 PDB 2B90 "Crystal Structure Of The Interleukin-4 Variant T13dr85a" 99.23 129 97.67 97.67 1.94e-85 PDB 2B91 "Crystal Structure Of The Interleukin-4 Variant F82dr85a" 99.23 129 97.67 97.67 5.85e-85 PDB 2CYK "Aspects Of Receptor Binding And Signalling Of Interleukin-4 Investigated By Site-Directed Mutagenesis And Nmr Spectroscopy" 99.23 129 99.22 99.22 2.75e-87 PDB 2D48 "Crystal Structure Of The Interleukin-4 Variant T13d" 99.23 129 98.45 98.45 1.82e-86 PDB 2INT "Crystal Structure Of Recombinant Human Interleukin-4" 99.23 129 99.22 99.22 2.75e-87 PDB 3BPL "Crystal Structure Of The Il4-Il4r-Common Gamma Ternary Complex" 99.23 129 99.22 99.22 2.75e-87 PDB 3BPN "Crystal Structure Of The Il4-Il4r-Il13ra Ternary Complex" 99.23 129 99.22 99.22 2.75e-87 PDB 4YDY "Crystal Structure Of Darpin 44c12v5 In Complex With Human Il-4" 100.00 130 99.23 99.23 2.41e-88 EMBL CAA34682 "alpha mating factor prepropropeptide/interleukin 4 [synthetic construct]" 99.23 136 99.22 99.22 2.36e-87 EMBL CAP72493 "interleukin 4 [Homo sapiens]" 99.23 153 98.45 98.45 4.71e-86 GB AAA59149 "interleukin 4 [Homo sapiens]" 99.23 153 99.22 99.22 6.75e-87 GB AAA59150 "interleukin 4 [Homo sapiens]" 99.23 153 99.22 99.22 6.75e-87 GB AAH66277 "Interleukin 4, isoform 1 precursor [Homo sapiens]" 99.23 153 98.45 98.45 5.79e-86 GB AAH67514 "Interleukin 4 [Homo sapiens]" 99.23 153 99.22 99.22 6.75e-87 GB AAH67515 "Interleukin 4, isoform 1 precursor [Homo sapiens]" 99.23 153 98.45 98.45 9.26e-86 REF NP_000580 "interleukin-4 isoform 1 precursor [Homo sapiens]" 99.23 153 99.22 99.22 6.75e-87 REF NP_001011714 "interleukin-4 isoform 1 precursor [Pan troglodytes]" 99.23 153 98.45 98.45 3.55e-86 REF XP_002815914 "PREDICTED: interleukin-4 isoform X1 [Pongo abelii]" 99.23 153 97.67 98.45 1.34e-85 REF XP_003829346 "PREDICTED: interleukin-4 isoform X1 [Pan paniscus]" 99.23 153 98.45 99.22 3.25e-86 REF XP_004042527 "PREDICTED: interleukin-4 isoform 1 [Gorilla gorilla gorilla]" 99.23 153 97.67 98.45 1.55e-85 SP P05112 "RecName: Full=Interleukin-4; Short=IL-4; AltName: Full=B-cell stimulatory factor 1; Short=BSF-1; AltName: Full=Binetrakin; AltN" 99.23 153 99.22 99.22 6.75e-87 SP P79339 "RecName: Full=Interleukin-4; Short=IL-4; AltName: Full=B-cell stimulatory factor 1; Short=BSF-1; AltName: Full=Lymphocyte stimu" 99.23 153 96.90 98.45 4.00e-85 SP Q8HYB1 "RecName: Full=Interleukin-4; Short=IL-4; AltName: Full=B-cell stimulatory factor 1; Short=BSF-1; AltName: Full=Lymphocyte stimu" 99.23 153 99.22 99.22 6.75e-87 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $interleukin_4 human 9606 Eukaryota Metazoa Homo sapiens generic 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 $interleukin_4 'not available' . Escherichia coli generic . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.3 . na temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 'liquid NH3' N . . ppm 0 . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'interleukin 4' _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 . 3 LYS H H 8.45 . 1 2 . 3 LYS HA H 4.47 . 1 3 . 3 LYS N N 122.6 . 1 4 . 4 CYS H H 8.67 . 1 5 . 4 CYS HA H 4.65 . 1 6 . 4 CYS HB2 H 2.91 . 2 7 . 4 CYS HB3 H 3.1 . 2 8 . 4 CYS N N 120.9 . 1 9 . 5 ASP H H 8.51 . 1 10 . 5 ASP HA H 4.56 . 1 11 . 5 ASP HB2 H 2.68 . 2 12 . 5 ASP HB3 H 2.76 . 2 13 . 5 ASP N N 123.4 . 1 14 . 6 ILE H H 8.47 . 1 15 . 6 ILE HA H 4 . 1 16 . 6 ILE HB H 1.97 . 1 17 . 6 ILE HG12 H 1.35 . 2 18 . 6 ILE HG13 H 1.51 . 2 19 . 6 ILE HG2 H .99 . 1 20 . 6 ILE HD1 H .89 . 1 21 . 6 ILE N N 123.9 . 1 22 . 7 THR H H 8.31 . 1 23 . 7 THR HA H 3.93 . 1 24 . 7 THR HB H 4.09 . 1 25 . 7 THR HG2 H 1.2 . 1 26 . 7 THR N N 117 . 1 27 . 8 LEU H H 7.7 . 1 28 . 8 LEU HA H 3.9 . 1 29 . 8 LEU N N 121.2 . 1 30 . 9 GLN H H 7.85 . 1 31 . 9 GLN HA H 3.69 . 1 32 . 9 GLN HB2 H 2.14 . 1 33 . 9 GLN HB3 H 2.14 . 1 34 . 9 GLN HG2 H 2.25 . 2 35 . 9 GLN HG3 H 2.37 . 2 36 . 9 GLN NE2 N 111.1 . 1 37 . 9 GLN HE21 H 7.16 . 2 38 . 9 GLN HE22 H 6.83 . 2 39 . 9 GLN N N 116.7 . 1 40 . 10 GLU H H 7.97 . 1 41 . 10 GLU HA H 3.99 . 1 42 . 10 GLU N N 119.2 . 1 43 . 11 ILE H H 8.12 . 1 44 . 11 ILE HA H 3.52 . 1 45 . 11 ILE HB H 1.96 . 1 46 . 11 ILE HG12 H 1.89 . 1 47 . 11 ILE HG13 H 1.89 . 1 48 . 11 ILE HG2 H .78 . 1 49 . 11 ILE HD1 H .61 . 1 50 . 11 ILE N N 122.3 . 1 51 . 12 ILE H H 7.95 . 1 52 . 12 ILE HA H 3.4 . 1 53 . 12 ILE HB H 1.71 . 1 54 . 12 ILE HG12 H .93 . 2 55 . 12 ILE HG13 H 1.25 . 2 56 . 12 ILE HG2 H .64 . 1 57 . 12 ILE HD1 H .51 . 1 58 . 12 ILE N N 120.4 . 1 59 . 13 LYS H H 7.97 . 1 60 . 13 LYS HA H 3.92 . 1 61 . 13 LYS N N 119.5 . 1 62 . 14 THR H H 8.13 . 1 63 . 14 THR HA H 3.59 . 1 64 . 14 THR HB H 4.22 . 1 65 . 14 THR HG2 H 1.12 . 1 66 . 14 THR N N 117 . 1 67 . 15 LEU H H 8.56 . 1 68 . 15 LEU HA H 3.95 . 1 69 . 15 LEU N N 121.5 . 1 70 . 16 ASN H H 8.45 . 1 71 . 16 ASN HA H 4.27 . 1 72 . 16 ASN HB2 H 2.79 . 2 73 . 16 ASN HB3 H 2.91 . 2 74 . 16 ASN ND2 N 110.3 . 1 75 . 16 ASN HD21 H 7.48 . 2 76 . 16 ASN HD22 H 6.55 . 2 77 . 16 ASN N N 120 . 1 78 . 17 SER H H 7.77 . 1 79 . 17 SER HA H 4.18 . 1 80 . 17 SER HB2 H 3.55 . 2 81 . 17 SER HB3 H 3.61 . 2 82 . 17 SER N N 115.8 . 1 83 . 18 LEU H H 8.04 . 1 84 . 18 LEU HA H 4.02 . 1 85 . 18 LEU HB2 H 1.9 . 2 86 . 18 LEU HB3 H 1.47 . 2 87 . 18 LEU HG H 1.64 . 1 88 . 18 LEU HD1 H .82 . 2 89 . 18 LEU HD2 H 1.01 . 2 90 . 18 LEU N N 120.5 . 1 91 . 19 THR H H 7.67 . 1 92 . 19 THR HA H 4.34 . 1 93 . 19 THR HB H 4.48 . 1 94 . 19 THR HG2 H 1.17 . 1 95 . 19 THR N N 107.4 . 1 96 . 20 GLU H H 7.37 . 1 97 . 20 GLU HA H 4.22 . 1 98 . 20 GLU HB2 H 2.09 . 1 99 . 20 GLU HB3 H 2.09 . 1 100 . 20 GLU HG2 H 2.31 . 2 101 . 20 GLU HG3 H 2.39 . 2 102 . 20 GLU N N 120 . 1 103 . 21 GLN H H 7.42 . 1 104 . 21 GLN HA H 4.47 . 1 105 . 21 GLN HB2 H 1.96 . 1 106 . 21 GLN HB3 H 1.96 . 1 107 . 21 GLN HG2 H 2.3 . 1 108 . 21 GLN HG3 H 2.3 . 1 109 . 21 GLN NE2 N 110.6 . 1 110 . 21 GLN HE21 H 7.4 . 2 111 . 21 GLN HE22 H 6.55 . 2 112 . 21 GLN N N 117.1 . 1 113 . 22 LYS H H 8.16 . 1 114 . 22 LYS HA H 4.42 . 1 115 . 22 LYS N N 122.9 . 1 116 . 23 THR H H 8.23 . 1 117 . 23 THR HA H 4.87 . 1 118 . 23 THR HB H 4.58 . 1 119 . 23 THR HG2 H 1.27 . 1 120 . 23 THR N N 115 . 1 121 . 24 LEU H H 8.47 . 1 122 . 24 LEU HA H 4.22 . 1 123 . 24 LEU HB2 H 1.87 . 2 124 . 24 LEU HB3 H 1.68 . 2 125 . 24 LEU HG H 1.79 . 1 126 . 24 LEU HD1 H .94 . 1 127 . 24 LEU HD2 H .94 . 1 128 . 24 LEU N N 121.6 . 1 129 . 25 CYS H H 8.41 . 1 130 . 25 CYS HA H 4.5 . 1 131 . 25 CYS HB2 H 3.11 . 2 132 . 25 CYS HB3 H 3.62 . 2 133 . 25 CYS N N 114.4 . 1 134 . 26 THR H H 7.75 . 1 135 . 26 THR HA H 4.18 . 1 136 . 26 THR HB H 4.5 . 1 137 . 26 THR HG2 H 1.31 . 1 138 . 26 THR N N 108.1 . 1 139 . 28 LEU H H 7.04 . 1 140 . 28 LEU HA H 4.41 . 1 141 . 28 LEU HB2 H 2.02 . 2 142 . 28 LEU HB3 H 1.57 . 2 143 . 28 LEU HG H 1.79 . 1 144 . 28 LEU HD1 H .81 . 2 145 . 28 LEU HD2 H .58 . 2 146 . 28 LEU N N 118.6 . 1 147 . 29 THR H H 7.78 . 1 148 . 29 THR HA H 4.99 . 1 149 . 29 THR HB H 4.18 . 1 150 . 29 THR HG2 H 1.1 . 1 151 . 29 THR N N 108.1 . 1 152 . 30 VAL H H 8.99 . 1 153 . 30 VAL HA H 4.62 . 1 154 . 30 VAL HB H 1.86 . 1 155 . 30 VAL HG1 H .26 . 2 156 . 30 VAL HG2 H .66 . 2 157 . 30 VAL N N 113.9 . 1 158 . 31 THR H H 7.78 . 1 159 . 31 THR HA H 4.08 . 1 160 . 31 THR HB H 3.82 . 1 161 . 31 THR HG2 H 1.07 . 1 162 . 31 THR N N 118.4 . 1 163 . 32 ASP H H 8.58 . 1 164 . 32 ASP HA H 4.68 . 1 165 . 32 ASP HB2 H 2.31 . 2 166 . 32 ASP HB3 H 2.77 . 2 167 . 32 ASP N N 123.8 . 1 168 . 33 ILE H H 7.01 . 1 169 . 33 ILE HA H 4.04 . 1 170 . 33 ILE HB H 1.92 . 1 171 . 33 ILE HG12 H .45 . 2 172 . 33 ILE HG13 H .69 . 2 173 . 33 ILE HG2 H .87 . 1 174 . 33 ILE HD1 H .27 . 1 175 . 33 ILE N N 116.3 . 1 176 . 34 PHE H H 8.14 . 1 177 . 34 PHE HA H 4.42 . 1 178 . 34 PHE HB2 H 3.08 . 2 179 . 34 PHE HB3 H 3.23 . 2 180 . 34 PHE HD1 H 7.22 . 1 181 . 34 PHE HD2 H 7.22 . 1 182 . 34 PHE HE1 H 6.58 . 1 183 . 34 PHE HE2 H 6.58 . 1 184 . 34 PHE HZ H 6.51 . 1 185 . 34 PHE N N 120.2 . 1 186 . 35 ALA H H 7.44 . 1 187 . 35 ALA HA H 4.22 . 1 188 . 35 ALA HB H 1.39 . 1 189 . 35 ALA N N 123.6 . 1 190 . 36 ALA H H 7.67 . 1 191 . 36 ALA HA H 4.42 . 1 192 . 36 ALA HB H 1.37 . 1 193 . 36 ALA N N 120.5 . 1 194 . 37 SER H H 7.81 . 1 195 . 37 SER HA H 4.36 . 1 196 . 37 SER HB2 H 3.87 . 2 197 . 37 SER HB3 H 3.94 . 2 198 . 37 SER N N 114.1 . 1 199 . 38 LYS H H 8.14 . 1 200 . 38 LYS HA H 4.26 . 1 201 . 38 LYS HB2 H 1.79 . 1 202 . 38 LYS HB3 H 1.79 . 1 203 . 38 LYS N N 122.4 . 1 204 . 39 ASN H H 8.41 . 1 205 . 39 ASN HA H 4.71 . 1 206 . 39 ASN HB2 H 2.74 . 2 207 . 39 ASN HB3 H 2.9 . 2 208 . 39 ASN ND2 N 112.4 . 1 209 . 39 ASN HD21 H 7.52 . 2 210 . 39 ASN HD22 H 6.83 . 2 211 . 39 ASN N N 117.9 . 1 212 . 40 THR H H 7.73 . 1 213 . 40 THR HA H 4.54 . 1 214 . 40 THR HB H 4.09 . 1 215 . 40 THR HG2 H 1.14 . 1 216 . 40 THR N N 114.3 . 1 217 . 41 THR H H 8.43 . 1 218 . 41 THR HA H 4.46 . 1 219 . 41 THR HG2 H 1.31 . 1 220 . 41 THR N N 114.7 . 1 221 . 42 GLU H H 8.73 . 1 222 . 42 GLU HA H 4.62 . 1 223 . 42 GLU HB2 H 1.84 . 1 224 . 42 GLU HB3 H 1.84 . 1 225 . 42 GLU N N 123.1 . 1 226 . 43 LYS H H 7.99 . 1 227 . 43 LYS HA H 3.79 . 1 228 . 43 LYS N N 116.1 . 1 229 . 44 GLU H H 7.5 . 1 230 . 44 GLU HA H 3.82 . 1 231 . 44 GLU HB2 H 2.18 . 1 232 . 44 GLU HB3 H 2.18 . 1 233 . 44 GLU N N 117.8 . 1 234 . 45 THR H H 8.1 . 1 235 . 45 THR HA H 3.7 . 1 236 . 45 THR HB H 4.11 . 1 237 . 45 THR HG2 H 1.06 . 1 238 . 45 THR N N 118.2 . 1 239 . 46 PHE H H 8.3 . 1 240 . 46 PHE HA H 4.49 . 1 241 . 46 PHE HB2 H 3.17 . 2 242 . 46 PHE HB3 H 3.29 . 2 243 . 46 PHE HD1 H 6.9 . 1 244 . 46 PHE HD2 H 6.9 . 1 245 . 46 PHE HE1 H 7.2 . 1 246 . 46 PHE HE2 H 7.2 . 1 247 . 46 PHE HZ H 7.04 . 1 248 . 46 PHE N N 119.9 . 1 249 . 47 CYS H H 8.16 . 1 250 . 47 CYS HA H 3.97 . 1 251 . 47 CYS HB2 H 3.04 . 2 252 . 47 CYS HB3 H 3.27 . 2 253 . 47 CYS N N 119.8 . 1 254 . 48 ARG H H 9.02 . 1 255 . 48 ARG HA H 3.86 . 1 256 . 48 ARG HD2 H 2.97 . 2 257 . 48 ARG HD3 H 3.2 . 2 258 . 48 ARG HE H 7.38 . 1 259 . 48 ARG N N 124 . 1 260 . 49 ALA H H 8.79 . 1 261 . 49 ALA HA H 4.19 . 1 262 . 49 ALA HB H 1.61 . 1 263 . 49 ALA N N 121.5 . 1 264 . 50 ALA H H 8.2 . 1 265 . 50 ALA HA H 3.97 . 1 266 . 50 ALA N N 120.3 . 1 267 . 51 THR H H 8.18 . 1 268 . 51 THR HA H 3.76 . 1 269 . 51 THR HB H 4.55 . 1 270 . 51 THR HG2 H 1.29 . 1 271 . 51 THR N N 114.4 . 1 272 . 52 VAL H H 8.2 . 1 273 . 52 VAL HA H 3.81 . 1 274 . 52 VAL HB H 2.2 . 1 275 . 52 VAL HG1 H .8 . 2 276 . 52 VAL HG2 H 1.08 . 2 277 . 52 VAL N N 120.7 . 1 278 . 53 LEU H H 8.14 . 1 279 . 53 LEU HA H 3.96 . 1 280 . 53 LEU HB2 H 2.15 . 1 281 . 53 LEU HB3 H 2.15 . 1 282 . 53 LEU HG H 2.15 . 1 283 . 53 LEU HD1 H 2.15 . 1 284 . 53 LEU HD2 H 2.15 . 1 285 . 53 LEU N N 120.9 . 1 286 . 55 GLN H H 8.06 . 1 287 . 55 GLN HA H 3.83 . 1 288 . 55 GLN HB2 H 2.09 . 1 289 . 55 GLN HB3 H 2.09 . 1 290 . 55 GLN HG2 H 2.32 . 2 291 . 55 GLN HG3 H 2.51 . 2 292 . 55 GLN NE2 N 110.2 . 1 293 . 55 GLN HE21 H 6.72 . 2 294 . 55 GLN HE22 H 7.27 . 2 295 . 55 GLN N N 120.6 . 1 296 . 56 PHE H H 8.03 . 1 297 . 56 PHE HA H 4.32 . 1 298 . 56 PHE HB2 H 3.16 . 2 299 . 56 PHE HB3 H 3.41 . 2 300 . 56 PHE HD1 H 7.12 . 1 301 . 56 PHE HD2 H 7.12 . 1 302 . 56 PHE HE1 H 6.94 . 1 303 . 56 PHE HE2 H 6.94 . 1 304 . 56 PHE HZ H 7.31 . 1 305 . 56 PHE N N 119.2 . 1 306 . 57 TYR H H 9.22 . 1 307 . 57 TYR HA H 4.26 . 1 308 . 57 TYR HB2 H 2.91 . 2 309 . 57 TYR HB3 H 3.4 . 2 310 . 57 TYR HD1 H 6.94 . 1 311 . 57 TYR HD2 H 6.94 . 1 312 . 57 TYR HE1 H 6.82 . 1 313 . 57 TYR HE2 H 6.82 . 1 314 . 57 TYR N N 117.3 . 1 315 . 58 SER H H 7.97 . 1 316 . 58 SER HA H 4.4 . 1 317 . 58 SER HB2 H 3.76 . 2 318 . 58 SER HB3 H 3.81 . 2 319 . 58 SER N N 118.9 . 1 320 . 59 HIS H H 7.54 . 1 321 . 59 HIS HA H 4.55 . 1 322 . 59 HIS HB2 H 2.77 . 2 323 . 59 HIS HB3 H 2.71 . 2 324 . 59 HIS N N 116.3 . 1 325 . 60 HIS H H 7.9 . 1 326 . 60 HIS HA H 5.01 . 1 327 . 60 HIS HB2 H 3.45 . 2 328 . 60 HIS HB3 H 2.21 . 2 329 . 60 HIS HD2 H 6.05 . 1 330 . 60 HIS HE1 H 8.47 . 1 331 . 60 HIS N N 111.4 . 1 332 . 61 GLU H H 8.08 . 1 333 . 61 GLU HA H 3.95 . 1 334 . 61 GLU N N 124.5 . 1 335 . 62 LYS H H 8.59 . 1 336 . 62 LYS HA H 4.48 . 1 337 . 62 LYS N N 116.5 . 1 338 . 63 ASP H H 6.6 . 1 339 . 63 ASP HA H 4.58 . 1 340 . 63 ASP HB2 H 2.7 . 2 341 . 63 ASP HB3 H 2.99 . 2 342 . 63 ASP N N 119.2 . 1 343 . 64 THR H H 8.79 . 1 344 . 64 THR HA H 3.84 . 1 345 . 64 THR HB H 4.29 . 1 346 . 64 THR HG2 H 1.34 . 1 347 . 64 THR N N 122.7 . 1 348 . 65 ARG H H 8.49 . 1 349 . 65 ARG HA H 4.08 . 1 350 . 65 ARG HD2 H 3.2 . 2 351 . 65 ARG HD3 H 3.26 . 2 352 . 65 ARG HE H 7.51 . 1 353 . 65 ARG N N 121.5 . 1 354 . 66 CYS H H 7.43 . 1 355 . 66 CYS HA H 4.39 . 1 356 . 66 CYS HB2 H 2.6 . 2 357 . 66 CYS HB3 H 3.1 . 2 358 . 66 CYS N N 113.6 . 1 359 . 67 LEU H H 7.38 . 1 360 . 67 LEU HA H 3.74 . 1 361 . 67 LEU HD1 H .73 . 1 362 . 67 LEU HD2 H .73 . 1 363 . 67 LEU N N 119.4 . 1 364 . 68 GLY H H 7.08 . 1 365 . 68 GLY HA2 H 3.68 . 2 366 . 68 GLY HA3 H 3.91 . 2 367 . 68 GLY N N 99.6 . 1 368 . 69 ALA H H 8.4 . 1 369 . 69 ALA HA H 4.7 . 1 370 . 69 ALA HB H 1.45 . 1 371 . 69 ALA N N 120.8 . 1 372 . 70 THR H H 7.59 . 1 373 . 70 THR HA H 4.71 . 1 374 . 70 THR HB H 4.62 . 1 375 . 70 THR HG2 H 1.25 . 1 376 . 70 THR N N 107.7 . 1 377 . 71 ALA H H 8.93 . 1 378 . 71 ALA HA H 4.12 . 1 379 . 71 ALA HB H 1.47 . 1 380 . 71 ALA N N 124.9 . 1 381 . 72 GLN H H 8.5 . 1 382 . 72 GLN HA H 4.21 . 1 383 . 72 GLN HB2 H 2.08 . 2 384 . 72 GLN HB3 H 2.18 . 2 385 . 72 GLN HG2 H 2.49 . 1 386 . 72 GLN HG3 H 2.49 . 1 387 . 72 GLN NE2 N 111.9 . 1 388 . 72 GLN HE21 H 6.92 . 2 389 . 72 GLN HE22 H 7.52 . 2 390 . 72 GLN N N 117 . 1 391 . 73 GLN H H 7.81 . 1 392 . 73 GLN HA H 4.12 . 1 393 . 73 GLN NE2 N 112.6 . 1 394 . 73 GLN HE21 H 7.04 . 2 395 . 73 GLN HE22 H 7.54 . 2 396 . 73 GLN N N 119.8 . 1 397 . 74 PHE H H 8.41 . 1 398 . 74 PHE HA H 4.52 . 1 399 . 74 PHE HB2 H 3.27 . 2 400 . 74 PHE HB3 H 3.48 . 2 401 . 74 PHE HD1 H 7.23 . 1 402 . 74 PHE HD2 H 7.23 . 1 403 . 74 PHE HE1 H 7.34 . 1 404 . 74 PHE HE2 H 7.34 . 1 405 . 74 PHE N N 122.9 . 1 406 . 75 HIS H H 8.46 . 1 407 . 75 HIS HA H 4.26 . 1 408 . 75 HIS HB2 H 3.35 . 2 409 . 75 HIS HB3 H 3.28 . 2 410 . 75 HIS N N 117.5 . 1 411 . 76 ARG H H 8.21 . 1 412 . 76 ARG HA H 4.02 . 1 413 . 76 ARG N N 119.2 . 1 414 . 77 HIS H H 8.33 . 1 415 . 77 HIS HA H 4.59 . 1 416 . 77 HIS HB2 H 3.2 . 2 417 . 77 HIS HB3 H 3.32 . 2 418 . 77 HIS N N 120.8 . 1 419 . 78 LYS H H 8.16 . 1 420 . 78 LYS HA H 3.63 . 1 421 . 78 LYS N N 117.5 . 1 422 . 79 GLN H H 7.9 . 1 423 . 79 GLN HA H 3.74 . 1 424 . 79 GLN NE2 N 112 . 1 425 . 79 GLN HE21 H 6.82 . 2 426 . 79 GLN HE22 H 7.08 . 2 427 . 79 GLN N N 118.5 . 1 428 . 80 LEU H H 7.89 . 1 429 . 80 LEU HA H 4.02 . 1 430 . 80 LEU HD1 H 1 . 2 431 . 80 LEU HD2 H .91 . 2 432 . 80 LEU N N 121.7 . 1 433 . 81 ILE H H 8.1 . 1 434 . 81 ILE HA H 3.53 . 1 435 . 81 ILE HB H 2.06 . 1 436 . 81 ILE HG12 H 1.02 . 2 437 . 81 ILE HG13 H 1.35 . 2 438 . 81 ILE HG2 H .76 . 1 439 . 81 ILE HD1 H .69 . 1 440 . 81 ILE N N 116.4 . 1 441 . 82 ARG H H 7.84 . 1 442 . 82 ARG HA H 3.79 . 1 443 . 82 ARG N N 119.4 . 1 444 . 83 PHE H H 8.51 . 1 445 . 83 PHE HA H 4.45 . 1 446 . 83 PHE HB2 H 2.97 . 2 447 . 83 PHE HB3 H 3.42 . 2 448 . 83 PHE HD1 H 7.19 . 1 449 . 83 PHE HD2 H 7.19 . 1 450 . 83 PHE HE1 H 7.36 . 1 451 . 83 PHE HE2 H 7.36 . 1 452 . 83 PHE N N 119 . 1 453 . 84 LEU H H 8.81 . 1 454 . 84 LEU HA H 4.1 . 1 455 . 84 LEU HD1 H 1.02 . 2 456 . 84 LEU HD2 H .96 . 2 457 . 84 LEU N N 120.4 . 1 458 . 85 LYS H H 8.14 . 1 459 . 85 LYS HA H 3.78 . 1 460 . 85 LYS N N 119 . 1 461 . 86 ARG H H 7.64 . 1 462 . 86 ARG HA H 4.01 . 1 463 . 86 ARG HG2 H 1.58 . 2 464 . 86 ARG HG3 H 1.75 . 2 465 . 86 ARG N N 120.5 . 1 466 . 87 LEU H H 8.51 . 1 467 . 87 LEU HA H 4.09 . 1 468 . 87 LEU N N 120.3 . 1 469 . 88 ASP H H 8.36 . 1 470 . 88 ASP HA H 4.27 . 1 471 . 88 ASP HB2 H 3.16 . 2 472 . 88 ASP HB3 H 3.29 . 2 473 . 88 ASP N N 117.5 . 1 474 . 89 ARG H H 7.59 . 1 475 . 89 ARG HA H 4.02 . 1 476 . 89 ARG N N 115.2 . 1 477 . 90 ASN H H 8.21 . 1 478 . 90 ASN HA H 4.57 . 1 479 . 90 ASN HB2 H 2.46 . 2 480 . 90 ASN HB3 H 2.73 . 2 481 . 90 ASN ND2 N 108.8 . 1 482 . 90 ASN HD21 H 7.17 . 2 483 . 90 ASN HD22 H 7.01 . 2 484 . 90 ASN N N 116.9 . 1 485 . 91 LEU H H 8.81 . 1 486 . 91 LEU HA H 3.83 . 1 487 . 91 LEU N N 121.7 . 1 488 . 92 TRP H H 9.04 . 1 489 . 92 TRP HA H 4.25 . 1 490 . 92 TRP HB2 H 3.35 . 2 491 . 92 TRP HB3 H 3.38 . 2 492 . 92 TRP HD1 H 7.27 . 1 493 . 92 TRP HE1 H 9.83 . 1 494 . 92 TRP HE3 H 7.57 . 1 495 . 92 TRP HZ2 H 7.43 . 1 496 . 92 TRP HZ3 H 7.23 . 1 497 . 92 TRP HH2 H 7.17 . 1 498 . 92 TRP N N 119.3 . 1 499 . 93 GLY H H 8.03 . 1 500 . 93 GLY HA2 H 3.81 . 2 501 . 93 GLY HA3 H 3.98 . 2 502 . 93 GLY N N 106.2 . 1 503 . 94 LEU H H 7.68 . 1 504 . 94 LEU HA H 4.15 . 1 505 . 94 LEU HB2 H 1.59 . 1 506 . 94 LEU HB3 H 1.59 . 1 507 . 94 LEU HG H 1.59 . 1 508 . 94 LEU HD1 H .53 . 1 509 . 94 LEU HD2 H .53 . 1 510 . 94 LEU N N 121.2 . 1 511 . 95 ALA H H 7.98 . 1 512 . 95 ALA HA H 4.19 . 1 513 . 95 ALA HB H 1.57 . 1 514 . 95 ALA N N 119.8 . 1 515 . 96 GLY H H 7.59 . 1 516 . 96 GLY HA2 H 3.64 . 2 517 . 96 GLY HA3 H 3.78 . 2 518 . 96 GLY N N 102.1 . 1 519 . 97 LEU H H 7.51 . 1 520 . 97 LEU HA H 4.39 . 1 521 . 97 LEU HB2 H 1.43 . 1 522 . 97 LEU HB3 H 1.43 . 1 523 . 97 LEU HG H 1.57 . 1 524 . 97 LEU HD1 H .83 . 1 525 . 97 LEU HD2 H .83 . 1 526 . 97 LEU N N 118.6 . 1 527 . 98 ASN H H 8.42 . 1 528 . 98 ASN HA H 4.82 . 1 529 . 98 ASN HB2 H 2.72 . 1 530 . 98 ASN HB3 H 2.72 . 1 531 . 98 ASN ND2 N 112.3 . 1 532 . 98 ASN HD21 H 7.37 . 2 533 . 98 ASN HD22 H 6.81 . 2 534 . 98 ASN N N 117.2 . 1 535 . 99 SER H H 7.48 . 1 536 . 99 SER HA H 4.61 . 1 537 . 99 SER HB2 H 3.81 . 2 538 . 99 SER HB3 H 3.82 . 2 539 . 99 SER N N 112 . 1 540 . 100 CYS H H 8.93 . 1 541 . 100 CYS HA H 4.93 . 1 542 . 100 CYS HB2 H 3.08 . 2 543 . 100 CYS HB3 H 3.49 . 2 544 . 100 CYS N N 118.9 . 1 545 . 101 PRO HA H 4.31 . 1 546 . 101 PRO HB2 H 3.56 . 2 547 . 101 PRO HB3 H 3.66 . 2 548 . 102 VAL H H 8.41 . 1 549 . 102 VAL HA H 4.12 . 1 550 . 102 VAL HB H 1.93 . 1 551 . 102 VAL HG1 H .82 . 2 552 . 102 VAL HG2 H .95 . 2 553 . 102 VAL N N 122.3 . 1 554 . 103 LYS H H 8.51 . 1 555 . 103 LYS HA H 4.38 . 1 556 . 103 LYS N N 128.1 . 1 557 . 104 GLU H H 8.26 . 1 558 . 104 GLU HA H 4.17 . 1 559 . 104 GLU HB2 H 1.91 . 2 560 . 104 GLU HB3 H 2.22 . 2 561 . 104 GLU HG2 H 2.22 . 1 562 . 104 GLU HG3 H 2.22 . 1 563 . 104 GLU N N 123.4 . 1 564 . 105 ALA H H 8.15 . 1 565 . 105 ALA HA H 4.43 . 1 566 . 105 ALA HB H 1.36 . 1 567 . 105 ALA N N 125.5 . 1 568 . 106 ASN H H 8.3 . 1 569 . 106 ASN HA H 4.64 . 1 570 . 106 ASN HB2 H 2.77 . 2 571 . 106 ASN HB3 H 2.92 . 2 572 . 106 ASN ND2 N 113.8 . 1 573 . 106 ASN HD21 H 7.78 . 2 574 . 106 ASN HD22 H 6.99 . 2 575 . 106 ASN N N 117.9 . 1 576 . 107 GLN H H 8.7 . 1 577 . 107 GLN HA H 5.06 . 1 578 . 107 GLN NE2 N 113.3 . 1 579 . 107 GLN HE21 H 6.61 . 2 580 . 107 GLN HE22 H 7.27 . 2 581 . 107 GLN N N 119.3 . 1 582 . 108 SER H H 9.1 . 1 583 . 108 SER HA H 4.99 . 1 584 . 108 SER HB2 H 3.7 . 2 585 . 108 SER HB3 H 3.99 . 2 586 . 108 SER N N 116 . 1 587 . 109 THR H H 8.9 . 1 588 . 109 THR HA H 4.41 . 1 589 . 109 THR HB H 4.72 . 1 590 . 109 THR HG2 H 1.39 . 1 591 . 109 THR N N 113.4 . 1 592 . 110 LEU H H 8.87 . 1 593 . 110 LEU HA H 3.95 . 1 594 . 110 LEU HB2 H .93 . 2 595 . 110 LEU HB3 H 1.77 . 2 596 . 110 LEU HG H 1.37 . 1 597 . 110 LEU HD1 H .3 . 2 598 . 110 LEU HD2 H .1 . 2 599 . 110 LEU N N 125.3 . 1 600 . 111 GLU H H 8.54 . 1 601 . 111 GLU HA H 3.94 . 1 602 . 111 GLU N N 117.3 . 1 603 . 112 ASN H H 7.9 . 1 604 . 112 ASN HA H 4.4 . 1 605 . 112 ASN HB2 H 2.81 . 2 606 . 112 ASN HB3 H 2.86 . 2 607 . 112 ASN ND2 N 112.4 . 1 608 . 112 ASN HD21 H 7.67 . 2 609 . 112 ASN HD22 H 6.92 . 2 610 . 112 ASN N N 117.9 . 1 611 . 113 PHE H H 8.38 . 1 612 . 113 PHE HA H 4.37 . 1 613 . 113 PHE HB2 H 2.99 . 2 614 . 113 PHE HB3 H 3.46 . 2 615 . 113 PHE HD1 H 7.2 . 1 616 . 113 PHE HD2 H 7.2 . 1 617 . 113 PHE N N 123 . 1 618 . 114 LEU H H 8.91 . 1 619 . 114 LEU HA H 3.87 . 1 620 . 114 LEU N N 118.2 . 1 621 . 115 GLU H H 7.97 . 1 622 . 115 GLU HA H 4.4 . 1 623 . 115 GLU HB2 H 2.39 . 1 624 . 115 GLU HB3 H 2.39 . 1 625 . 115 GLU N N 118.9 . 1 626 . 116 ARG H H 7.94 . 1 627 . 116 ARG HA H 3.83 . 1 628 . 116 ARG HD2 H 2.93 . 2 629 . 116 ARG HD3 H 3.01 . 2 630 . 116 ARG HE H 6.9 . 1 631 . 116 ARG N N 121.1 . 1 632 . 117 LEU H H 8.09 . 1 633 . 117 LEU HA H 3.76 . 1 634 . 117 LEU N N 119.7 . 1 635 . 118 LYS H H 8.51 . 1 636 . 118 LYS HA H 3.62 . 1 637 . 118 LYS HB2 H 2.09 . 1 638 . 118 LYS HB3 H 2.09 . 1 639 . 118 LYS HG2 H 2.09 . 1 640 . 118 LYS HG3 H 2.09 . 1 641 . 118 LYS HD2 H 2.09 . 1 642 . 118 LYS HD3 H 2.09 . 1 643 . 118 LYS N N 119.8 . 1 644 . 119 THR H H 7.92 . 1 645 . 119 THR HA H 3.79 . 1 646 . 119 THR HB H 4.27 . 1 647 . 119 THR HG2 H 1.18 . 1 648 . 119 THR N N 116.4 . 1 649 . 120 ILE H H 7.71 . 1 650 . 120 ILE HA H 3.82 . 1 651 . 120 ILE HB H 1.89 . 1 652 . 120 ILE HG12 H 1.11 . 2 653 . 120 ILE HG13 H 1.56 . 2 654 . 120 ILE HG2 H 1.01 . 1 655 . 120 ILE HD1 H .67 . 1 656 . 120 ILE N N 121.5 . 1 657 . 121 MET H H 8.44 . 1 658 . 121 MET HA H 4.4 . 1 659 . 121 MET HB2 H 1.73 . 2 660 . 121 MET HB3 H 2.02 . 2 661 . 121 MET HG2 H 2.31 . 2 662 . 121 MET HG3 H 2.71 . 2 663 . 121 MET N N 118.2 . 1 664 . 122 ARG H H 8.64 . 1 665 . 122 ARG HA H 3.96 . 1 666 . 122 ARG N N 120.2 . 1 667 . 123 GLU H H 7.87 . 1 668 . 123 GLU HA H 4.1 . 1 669 . 123 GLU N N 120.1 . 1 670 . 124 LYS H H 7.88 . 1 671 . 124 LYS HA H 4.1 . 1 672 . 124 LYS N N 119.3 . 1 673 . 125 TYR H H 8.55 . 1 674 . 125 TYR HA H 4.5 . 1 675 . 125 TYR HB2 H 2.98 . 2 676 . 125 TYR HB3 H 3.1 . 2 677 . 125 TYR HD1 H 7.04 . 1 678 . 125 TYR HD2 H 7.04 . 1 679 . 125 TYR HE1 H 6.73 . 1 680 . 125 TYR HE2 H 6.73 . 1 681 . 125 TYR N N 120.1 . 1 682 . 126 SER H H 8.1 . 1 683 . 126 SER HA H 4.17 . 1 684 . 126 SER HB2 H 4.03 . 2 685 . 126 SER HB3 H 4.04 . 2 686 . 126 SER N N 114.8 . 1 687 . 127 LYS H H 7.53 . 1 688 . 127 LYS HA H 4.3 . 1 689 . 127 LYS N N 119 . 1 690 . 128 CYS H H 7.75 . 1 691 . 128 CYS HA H 4.71 . 1 692 . 128 CYS HB2 H 3.12 . 2 693 . 128 CYS HB3 H 3.13 . 2 694 . 128 CYS N N 115.6 . 1 695 . 129 SER H H 7.97 . 1 696 . 129 SER HA H 4.43 . 1 697 . 129 SER HB2 H 3.63 . 2 698 . 129 SER HB3 H 3.78 . 2 699 . 129 SER N N 116.1 . 1 700 . 130 SER H H 7.77 . 1 701 . 130 SER HA H 4.26 . 1 702 . 130 SER HB2 H 3.85 . 1 703 . 130 SER HB3 H 3.85 . 1 704 . 130 SER N N 123.3 . 1 stop_ save_