data_1663 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Polypeptide Backbone Resonance Assignments and Secondary Structure of Bacillus subtilis Enzyme III(glc) Determined by Two-Dimensional and Three-Dimensional Heteronuclear NMR Spectroscopy ; _BMRB_accession_number 1663 _BMRB_flat_file_name bmr1663.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Fairbrother Wayne J. . 2 Cavanagh John . . 3 Dyson H. J. . 4 Palmer Arthur G. . 5 Sutrina Sarah L. . 6 Reizer Jonathan . . 7 Saier MIlton H. Jr 8 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 652 "15N chemical shifts" 149 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Fairbrother, Wayne J., Cavanagh, John, Dyson, H. Jane, Palmer, Arthur G., III, Sutrina, Sarah L., Reizer, Jonathan, Saier, MIlton H. Jr., Wright, Peter E., "Polypeptide Backbone Resonance Assignments and Secondary Structure of Bacillus subtilis Enzyme III(glc) Determined by Two-Dimensional and Three-Dimensional Heteronuclear NMR Spectroscopy," Biochemistry 30, 6896-6907 (1991). ; _Citation_title 'Polypeptide Backbone Resonance Assignments and Secondary Structure of Bacillus subtilis Enzyme III(glc) Determined by Two-Dimensional and Three-Dimensional Heteronuclear NMR Spectroscopy' _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 Fairbrother Wayne J. . 2 Cavanagh John . . 3 Dyson H. J. . 4 Palmer Arthur G. . 5 Sutrina Sarah L. . 6 Reizer Jonathan . . 7 Saier MIlton H. Jr 8 Wright Peter E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6896 _Page_last 6907 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_glucose_permease _Saveframe_category molecular_system _Mol_system_name 'glucose permease' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'glucose permease' $glucose_permease stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_glucose_permease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'glucose permease' _Name_variant 'enzyme IIIglc' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; MIAEPLQNEIGEEVFVSPIT GEIHPITDVPDQVFSGKMMG DGFAILPSEGIVVSPVRGKI LNVFPTKHAIGLQSDGGREI LIHFGIDTVSLKGEGFTSFV SEGDRVEPGQKLLEVDLDAV KPNVPSLMTPIVFTNLAEGE TVSIKASGSVNREQEDIVKI EK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 1 ILE 3 2 ALA 4 3 GLU 5 4 PRO 6 5 LEU 7 6 GLN 8 7 ASN 9 8 GLU 10 9 ILE 11 10 GLY 12 11 GLU 13 12 GLU 14 13 VAL 15 14 PHE 16 15 VAL 17 16 SER 18 17 PRO 19 18 ILE 20 19 THR 21 20 GLY 22 21 GLU 23 22 ILE 24 23 HIS 25 24 PRO 26 25 ILE 27 26 THR 28 27 ASP 29 28 VAL 30 29 PRO 31 30 ASP 32 31 GLN 33 32 VAL 34 33 PHE 35 34 SER 36 35 GLY 37 36 LYS 38 37 MET 39 38 MET 40 39 GLY 41 40 ASP 42 41 GLY 43 42 PHE 44 43 ALA 45 44 ILE 46 45 LEU 47 46 PRO 48 47 SER 49 48 GLU 50 49 GLY 51 50 ILE 52 51 VAL 53 52 VAL 54 53 SER 55 54 PRO 56 55 VAL 57 56 ARG 58 57 GLY 59 58 LYS 60 59 ILE 61 60 LEU 62 61 ASN 63 62 VAL 64 63 PHE 65 64 PRO 66 65 THR 67 66 LYS 68 67 HIS 69 68 ALA 70 69 ILE 71 70 GLY 72 71 LEU 73 72 GLN 74 73 SER 75 74 ASP 76 75 GLY 77 76 GLY 78 77 ARG 79 78 GLU 80 79 ILE 81 80 LEU 82 81 ILE 83 82 HIS 84 83 PHE 85 84 GLY 86 85 ILE 87 86 ASP 88 87 THR 89 88 VAL 90 89 SER 91 90 LEU 92 91 LYS 93 92 GLY 94 93 GLU 95 94 GLY 96 95 PHE 97 96 THR 98 97 SER 99 98 PHE 100 99 VAL 101 100 SER 102 101 GLU 103 102 GLY 104 103 ASP 105 104 ARG 106 105 VAL 107 106 GLU 108 107 PRO 109 108 GLY 110 109 GLN 111 110 LYS 112 111 LEU 113 112 LEU 114 113 GLU 115 114 VAL 116 115 ASP 117 116 LEU 118 117 ASP 119 118 ALA 120 119 VAL 121 120 LYS 122 121 PRO 123 122 ASN 124 123 VAL 125 124 PRO 126 125 SER 127 126 LEU 128 127 MET 129 128 THR 130 129 PRO 131 130 ILE 132 131 VAL 133 132 PHE 134 133 THR 135 134 ASN 136 135 LEU 137 136 ALA 138 137 GLU 139 138 GLY 140 139 GLU 141 140 THR 142 141 VAL 143 142 SER 144 143 ILE 145 144 LYS 146 145 ALA 147 146 SER 148 147 GLY 149 148 SER 150 149 VAL 151 150 ASN 152 151 ARG 153 152 GLU 154 153 GLN 155 154 GLU 156 155 ASP 157 156 ILE 158 157 VAL 159 158 LYS 160 159 ILE 161 160 GLU 162 161 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-01 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1AX3 "Solution Nmr Structure Of B. Subtilis Iiaglc, 16 Structures" 100.00 162 100.00 100.00 3.87e-108 PDB 1GPR "Refined Crystal Structure Of Iia Domain Of The Glucose Permease Of Bacillus Subtilis At 1.9 Angstroms Resolution" 100.00 162 100.00 100.00 3.87e-108 DBJ BAI84998 "phosphotransferase system (PTS) glucose-specific enzyme IICBA component [Bacillus subtilis subsp. natto BEST195]" 100.00 699 98.77 99.38 1.18e-101 DBJ BAM52032 "phosphotransferase system (PTS)glucose-specific enzyme IICBA component [Synechocystis sp. PCC 6803]" 100.00 699 99.38 100.00 1.83e-102 DBJ BAM57609 "phosphotransferase system (PTS)glucose-specific enzyme IICBA component [Bacillus subtilis BEST7003]" 100.00 699 99.38 100.00 1.83e-102 DBJ GAK78203 "phosphotransferase system (PTS) glucose-specific enzyme IICBA component [Bacillus subtilis Miyagi-4]" 100.00 699 98.77 99.38 1.18e-101 EMBL CAA31316 "protein-N(pi)-phosphohistidine-sugar phosphotransferase [Bacillus subtilis]" 100.00 162 100.00 100.00 3.87e-108 EMBL CAA77803 "IIGlc [Bacillus subtilis]" 100.00 699 99.38 100.00 1.83e-102 EMBL CAB13262 "phosphotransferase system (PTS) glucose-specific enzyme IICBA component [Bacillus subtilis subsp. subtilis str. 168]" 100.00 699 99.38 100.00 1.83e-102 EMBL CCU57950 "PTS system, glucose-specific IIC component / PTS system, glucose-specific IIB component / PTS system, glucose-specific IIA comp" 100.00 699 99.38 100.00 1.83e-102 EMBL CEI56550 "PTS system glucose-specific EIICBA component [Bacillus subtilis]" 100.00 699 99.38 100.00 1.83e-102 GB AAA06088 "glucose permease [Bacillus subtilis]" 100.00 451 99.38 100.00 8.24e-105 GB ADM37476 "phosphotransferase system (PTS) glucose-specific enzyme IICBA component [Bacillus subtilis subsp. spizizenii str. W23]" 100.00 699 98.15 99.38 2.08e-101 GB ADV96408 "phosphotransferase system (PTS) glucose-specific enzyme IICBA component [Bacillus subtilis BSn5]" 100.00 699 99.38 100.00 1.83e-102 GB AEP86363 "PTS system glucose-specific EIICBA component [Bacillus subtilis subsp. spizizenii TU-B-10]" 100.00 699 98.15 99.38 3.74e-101 GB AEP90534 "pts system, glucose-specific iibc component [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 100.00 659 99.38 100.00 1.15e-102 REF NP_389272 "PTS system-glucose-specific transporter subunit EIICBA [Bacillus subtilis subsp. subtilis str. 168]" 100.00 699 99.38 100.00 1.83e-102 REF WP_003218636 "MULTISPECIES: PTS glucose transporter subunit IIABC [Bacillus]" 100.00 699 98.15 99.38 2.08e-101 REF WP_003232428 "PTS glucose transporter subunit IIABC [Bacillus subtilis]" 100.00 699 98.77 99.38 2.29e-101 REF WP_003238960 "PTS glucose transporter subunit IICBA [Bacillus subtilis]" 100.00 699 99.38 100.00 1.89e-102 REF WP_003244661 "MULTISPECIES: PTS glucose EIICBA component [Bacillus]" 100.00 699 99.38 100.00 1.83e-102 SP P20166 "RecName: Full=PTS system glucose-specific EIICBA component; AltName: Full=EII-Glc/EIII-Glc; AltName: Full=EIICBA-Glc; Includes:" 100.00 699 99.38 100.00 1.83e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $glucose_permease . 1423 Bacteria . Bacillus subtilis 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 $glucose_permease 'not available' . . . . . 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 6.6 . 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 . . . 0 . . . . . $entry_citation $entry_citation 'liquid ammonia' N . . . 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 'glucose permease' _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 2 ILE H H 8.12 . 1 2 1 2 ILE HA H 4.19 . 1 3 1 2 ILE HG2 H .93 . 1 4 1 2 ILE N N 120.9 . 1 5 2 3 ALA H H 8.33 . 1 6 2 3 ALA HA H 4.35 . 1 7 2 3 ALA HB H 1.36 . 1 8 2 3 ALA N N 128.1 . 1 9 3 4 GLU H H 8.24 . 1 10 3 4 GLU HA H 4.58 . 1 11 3 4 GLU HB2 H 1.86 . 2 12 3 4 GLU HB3 H 2.04 . 2 13 3 4 GLU N N 121.6 . 1 14 4 5 PRO HA H 4.42 . 1 15 5 6 LEU H H 8.34 . 1 16 5 6 LEU HA H 4.36 . 1 17 5 6 LEU HB2 H 1.6 . 2 18 5 6 LEU HB3 H 1.69 . 2 19 5 6 LEU HG H 1.62 . 1 20 5 6 LEU HD1 H .9 . 2 21 5 6 LEU HD2 H .95 . 2 22 5 6 LEU N N 122.5 . 1 23 6 7 GLN H H 8.34 . 1 24 6 7 GLN HA H 4.51 . 1 25 6 7 GLN HB2 H 1.98 . 2 26 6 7 GLN HB3 H 2.05 . 2 27 6 7 GLN HG2 H 2.26 . 2 28 6 7 GLN HG3 H 2.32 . 2 29 6 7 GLN N N 121.3 . 1 30 7 8 ASN H H 8.41 . 1 31 7 8 ASN HA H 4.68 . 1 32 7 8 ASN HB2 H 2.83 . 2 33 7 8 ASN HB3 H 2.9 . 2 34 7 8 ASN N N 119.5 . 1 35 8 9 GLU H H 8.45 . 1 36 8 9 GLU HA H 4.28 . 1 37 8 9 GLU HB2 H 1.96 . 2 38 8 9 GLU HB3 H 2.06 . 2 39 8 9 GLU HG2 H 2.25 . 1 40 8 9 GLU HG3 H 2.25 . 1 41 8 9 GLU N N 120.1 . 1 42 9 10 ILE H H 7.97 . 1 43 9 10 ILE HA H 4.25 . 1 44 9 10 ILE HB H 1.95 . 1 45 9 10 ILE HG12 H 1.18 . 2 46 9 10 ILE HG13 H 1.45 . 2 47 9 10 ILE HG2 H .92 . 1 48 9 10 ILE HD1 H .84 . 1 49 9 10 ILE N N 119.3 . 1 50 10 11 GLY H H 8.25 . 1 51 10 11 GLY HA2 H 3.97 . 1 52 10 11 GLY HA3 H 3.97 . 1 53 10 11 GLY N N 111.5 . 1 54 11 12 GLU H H 8.09 . 1 55 11 12 GLU HA H 4.39 . 1 56 11 12 GLU HB2 H 1.94 . 2 57 11 12 GLU HB3 H 2.04 . 2 58 11 12 GLU HG2 H 2.27 . 2 59 11 12 GLU HG3 H 2.3 . 2 60 11 12 GLU N N 120.8 . 1 61 12 13 GLU H H 8.49 . 1 62 12 13 GLU HA H 4.51 . 1 63 12 13 GLU HB2 H 2.08 . 1 64 12 13 GLU HB3 H 2.08 . 1 65 12 13 GLU N N 123.2 . 1 66 13 14 VAL H H 8.31 . 1 67 13 14 VAL HA H 4.03 . 1 68 13 14 VAL HB H 2.03 . 1 69 13 14 VAL HG1 H .94 . 2 70 13 14 VAL HG2 H 1.02 . 2 71 13 14 VAL N N 125.3 . 1 72 14 15 PHE H H 8.1 . 1 73 14 15 PHE HA H 5.03 . 1 74 14 15 PHE HB2 H 2.87 . 2 75 14 15 PHE HB3 H 3.26 . 2 76 14 15 PHE HD1 H 7.18 . 1 77 14 15 PHE HD2 H 7.18 . 1 78 14 15 PHE N N 127.3 . 1 79 15 16 VAL H H 9.09 . 1 80 15 16 VAL HA H 5.16 . 1 81 15 16 VAL HB H 1.61 . 1 82 15 16 VAL HG1 H .57 . 2 83 15 16 VAL HG2 H .75 . 2 84 15 16 VAL N N 123.2 . 1 85 16 17 SER H H 8.61 . 1 86 16 17 SER HA H 4.37 . 1 87 16 17 SER HB2 H 3.76 . 2 88 16 17 SER HB3 H 4.58 . 2 89 16 17 SER N N 110.2 . 1 90 18 19 ILE H H 7.17 . 1 91 18 19 ILE HA H 4.62 . 1 92 18 19 ILE HB H 1.37 . 1 93 18 19 ILE HG2 H 1.13 . 1 94 18 19 ILE N N 115.3 . 1 95 19 20 THR H H 9.32 . 1 96 19 20 THR HA H 4.97 . 1 97 19 20 THR HB H 4.1 . 1 98 19 20 THR HG2 H 1.44 . 1 99 19 20 THR N N 125 . 1 100 20 21 GLY H H 8.8 . 1 101 20 21 GLY HA2 H 4.09 . 2 102 20 21 GLY HA3 H 4.72 . 2 103 20 21 GLY N N 115.3 . 1 104 21 22 GLU H H 8.07 . 1 105 21 22 GLU HA H 4.85 . 1 106 21 22 GLU HB2 H 2.1 . 2 107 21 22 GLU HB3 H 2.18 . 2 108 21 22 GLU N N 120.4 . 1 109 22 23 ILE H H 8.8 . 1 110 22 23 ILE HA H 4.95 . 1 111 22 23 ILE HB H 1.66 . 1 112 22 23 ILE HG2 H .86 . 1 113 22 23 ILE N N 128.7 . 1 114 23 24 HIS H H 9.48 . 1 115 23 24 HIS HA H 5.01 . 1 116 23 24 HIS HB2 H 2.64 . 2 117 23 24 HIS HB3 H 3.41 . 2 118 23 24 HIS HD2 H 7.12 . 1 119 23 24 HIS HE1 H 8.53 . 1 120 23 24 HIS N N 125.1 . 1 121 24 25 PRO HA H 5.03 . 1 122 24 25 PRO HD2 H 3.78 . 2 123 24 25 PRO HD3 H 4.04 . 2 124 25 26 ILE H H 9.48 . 1 125 25 26 ILE HA H 3.82 . 1 126 25 26 ILE HB H 1.59 . 1 127 25 26 ILE HG2 H 1.16 . 1 128 25 26 ILE N N 122.8 . 1 129 26 27 THR H H 7.09 . 1 130 26 27 THR HA H 4.15 . 1 131 26 27 THR HB H 4.52 . 1 132 26 27 THR HG2 H 1.43 . 1 133 26 27 THR N N 107.4 . 1 134 27 28 ASP H H 7.53 . 1 135 27 28 ASP HA H 4.74 . 1 136 27 28 ASP HB2 H 2.74 . 2 137 27 28 ASP HB3 H 2.81 . 2 138 27 28 ASP N N 119.5 . 1 139 28 29 VAL H H 7.41 . 1 140 28 29 VAL HA H 3.8 . 1 141 28 29 VAL HB H 2.09 . 1 142 28 29 VAL HG1 H .82 . 2 143 28 29 VAL HG2 H .74 . 2 144 28 29 VAL N N 121.7 . 1 145 30 31 ASP H H 8.29 . 1 146 30 31 ASP HA H 4.69 . 1 147 30 31 ASP HB2 H 2.58 . 2 148 30 31 ASP HB3 H 2.96 . 2 149 30 31 ASP N N 123.5 . 1 150 32 33 VAL H H 7.9 . 1 151 32 33 VAL HA H 3.73 . 1 152 32 33 VAL HB H 1.65 . 1 153 32 33 VAL HG1 H .33 . 2 154 32 33 VAL HG2 H .79 . 2 155 32 33 VAL N N 120 . 1 156 33 34 PHE H H 9.18 . 1 157 33 34 PHE HA H 4.36 . 1 158 33 34 PHE HB2 H 2.65 . 2 159 33 34 PHE HB3 H 2.9 . 2 160 33 34 PHE HD1 H 7.07 . 1 161 33 34 PHE HD2 H 7.07 . 1 162 33 34 PHE HE1 H 6.71 . 1 163 33 34 PHE HE2 H 6.71 . 1 164 33 34 PHE HZ H 6.51 . 1 165 33 34 PHE N N 119.2 . 1 166 34 35 SER H H 9.32 . 1 167 34 35 SER HA H 4.26 . 1 168 34 35 SER N N 116.4 . 1 169 35 36 GLY H H 7.36 . 1 170 35 36 GLY HA2 H 3.6 . 2 171 35 36 GLY HA3 H 4.26 . 2 172 35 36 GLY N N 107 . 1 173 36 37 LYS H H 8.07 . 1 174 36 37 LYS HA H 4.12 . 1 175 36 37 LYS HB2 H 2.08 . 1 176 36 37 LYS HB3 H 2.08 . 1 177 36 37 LYS N N 112.9 . 1 178 37 38 MET H H 7.84 . 1 179 37 38 MET HA H 4.15 . 1 180 37 38 MET N N 116.4 . 1 181 38 39 MET H H 8.24 . 1 182 38 39 MET HA H 4.58 . 1 183 38 39 MET HB2 H 1.94 . 2 184 38 39 MET HB3 H 2.06 . 2 185 38 39 MET N N 114.7 . 1 186 39 40 GLY H H 6.74 . 1 187 39 40 GLY HA2 H 3.73 . 2 188 39 40 GLY HA3 H 4.65 . 2 189 39 40 GLY N N 105.1 . 1 190 40 41 ASP H H 7.37 . 1 191 40 41 ASP HA H 5 . 1 192 40 41 ASP HB2 H 2.72 . 2 193 40 41 ASP HB3 H 2.88 . 2 194 40 41 ASP N N 117.6 . 1 195 41 42 GLY H H 9.22 . 1 196 41 42 GLY HA2 H 4.05 . 2 197 41 42 GLY HA3 H 5.28 . 2 198 41 42 GLY N N 106.3 . 1 199 42 43 PHE H H 9.16 . 1 200 42 43 PHE HA H 4.89 . 1 201 42 43 PHE HB2 H 3.15 . 2 202 42 43 PHE HB3 H 3.3 . 2 203 42 43 PHE HD1 H 7.1 . 1 204 42 43 PHE HD2 H 7.1 . 1 205 42 43 PHE N N 119.6 . 1 206 43 44 ALA H H 9.26 . 1 207 43 44 ALA HA H 5.2 . 1 208 43 44 ALA HB H .81 . 1 209 43 44 ALA N N 120.8 . 1 210 44 45 ILE H H 8.05 . 1 211 44 45 ILE HA H 5.03 . 1 212 44 45 ILE HB H 1.21 . 1 213 44 45 ILE HG2 H .4 . 1 214 44 45 ILE N N 118.1 . 1 215 45 46 LEU H H 9.44 . 1 216 45 46 LEU HA H 4.85 . 1 217 45 46 LEU HB2 H 2.22 . 1 218 45 46 LEU HB3 H 2.22 . 1 219 45 46 LEU N N 131.6 . 1 220 46 47 PRO HD2 H 3.28 . 2 221 46 47 PRO HD3 H 4.43 . 2 222 47 48 SER H H 9.54 . 1 223 47 48 SER HA H 4.6 . 1 224 47 48 SER HB2 H 3.88 . 2 225 47 48 SER HB3 H 4 . 2 226 47 48 SER N N 115.5 . 1 227 48 49 GLU H H 7.42 . 1 228 48 49 GLU HA H 4.7 . 1 229 48 49 GLU HB2 H 1.95 . 1 230 48 49 GLU HB3 H 1.95 . 1 231 48 49 GLU N N 118.1 . 1 232 49 50 GLY H H 9.57 . 1 233 49 50 GLY HA2 H 4.17 . 2 234 49 50 GLY HA3 H 4.23 . 2 235 49 50 GLY N N 112.2 . 1 236 50 51 ILE H H 6.81 . 1 237 50 51 ILE HA H 4.61 . 1 238 50 51 ILE HB H 1.61 . 1 239 50 51 ILE HG12 H 1.1 . 2 240 50 51 ILE HG13 H 1.6 . 2 241 50 51 ILE HG2 H .78 . 1 242 50 51 ILE N N 118.9 . 1 243 51 52 VAL H H 8.85 . 1 244 51 52 VAL HA H 4.96 . 1 245 51 52 VAL HB H 2.08 . 1 246 51 52 VAL HG1 H .98 . 2 247 51 52 VAL HG2 H 1.01 . 2 248 51 52 VAL N N 127.2 . 1 249 52 53 VAL H H 9.78 . 1 250 52 53 VAL HA H 5.12 . 1 251 52 53 VAL HB H 1.58 . 1 252 52 53 VAL HG1 H .69 . 2 253 52 53 VAL HG2 H .73 . 2 254 52 53 VAL N N 122.4 . 1 255 53 54 SER H H 8.73 . 1 256 53 54 SER N N 110.4 . 1 257 55 56 VAL H H 8.76 . 1 258 55 56 VAL HA H 4.84 . 1 259 55 56 VAL HB H 2.3 . 1 260 55 56 VAL HG1 H .3 . 2 261 55 56 VAL HG2 H 1.02 . 2 262 55 56 VAL N N 122 . 1 263 56 57 ARG H H 7 . 1 264 56 57 ARG HA H 4.85 . 1 265 56 57 ARG HB2 H 1.23 . 1 266 56 57 ARG HB3 H 1.23 . 1 267 56 57 ARG N N 103.6 . 1 268 57 58 GLY H H 8.33 . 1 269 57 58 GLY HA2 H 4.31 . 2 270 57 58 GLY HA3 H 4.42 . 2 271 57 58 GLY N N 114.8 . 1 272 58 59 LYS H H 8.85 . 1 273 58 59 LYS HA H 5.52 . 1 274 58 59 LYS HB2 H 1.58 . 2 275 58 59 LYS HB3 H 1.66 . 2 276 58 59 LYS N N 121.2 . 1 277 59 60 ILE H H 8.79 . 1 278 59 60 ILE HA H 4.08 . 1 279 59 60 ILE HB H 2.39 . 1 280 59 60 ILE HG2 H .68 . 1 281 59 60 ILE N N 121 . 1 282 60 61 LEU H H 9.04 . 1 283 60 61 LEU HA H 4.42 . 1 284 60 61 LEU HB2 H 1.43 . 1 285 60 61 LEU HB3 H 1.43 . 1 286 60 61 LEU N N 130 . 1 287 61 62 ASN H H 7.7 . 1 288 61 62 ASN HA H 4.85 . 1 289 61 62 ASN HB2 H 2.44 . 1 290 61 62 ASN HB3 H 2.44 . 1 291 61 62 ASN N N 113.2 . 1 292 62 63 VAL H H 8.78 . 1 293 62 63 VAL HA H 4.34 . 1 294 62 63 VAL HB H 2.06 . 1 295 62 63 VAL HG1 H .79 . 2 296 62 63 VAL HG2 H .96 . 2 297 62 63 VAL N N 124.2 . 1 298 63 64 PHE H H 8.2 . 1 299 63 64 PHE HA H 4.6 . 1 300 63 64 PHE HB2 H 2.62 . 2 301 63 64 PHE HB3 H 3.22 . 2 302 63 64 PHE HD1 H 7.2 . 1 303 63 64 PHE HD2 H 7.2 . 1 304 63 64 PHE N N 126.6 . 1 305 65 66 THR H H 7.18 . 1 306 65 66 THR HA H 4.07 . 1 307 65 66 THR HB H 4.83 . 1 308 65 66 THR HG2 H 1.22 . 1 309 65 66 THR N N 102.5 . 1 310 66 67 LYS H H 8.37 . 1 311 66 67 LYS HA H 3.49 . 1 312 66 67 LYS HB2 H 2.04 . 1 313 66 67 LYS HB3 H 2.04 . 1 314 66 67 LYS N N 113.3 . 1 315 67 68 HIS H H 6.95 . 1 316 67 68 HIS HA H 3.96 . 1 317 67 68 HIS HB2 H 1.2 . 2 318 67 68 HIS HB3 H 2.87 . 2 319 67 68 HIS HD2 H 5.42 . 1 320 67 68 HIS HE1 H 7.27 . 1 321 67 68 HIS N N 109.5 . 1 322 68 69 ALA H H 6.22 . 1 323 68 69 ALA HA H 5.02 . 1 324 68 69 ALA HB H -.02 . 1 325 68 69 ALA N N 117.6 . 1 326 69 70 ILE H H 8.41 . 1 327 69 70 ILE HA H 4.77 . 1 328 69 70 ILE HB H 1.51 . 1 329 69 70 ILE HG2 H .89 . 1 330 69 70 ILE N N 118.9 . 1 331 70 71 GLY H H 9.31 . 1 332 70 71 GLY HA2 H 3.79 . 2 333 70 71 GLY HA3 H 5.52 . 2 334 70 71 GLY N N 113.2 . 1 335 71 72 LEU H H 9.73 . 1 336 71 72 LEU HA H 5.16 . 1 337 71 72 LEU HB2 H 1.46 . 2 338 71 72 LEU HB3 H 1.47 . 2 339 71 72 LEU HG H 1.52 . 1 340 71 72 LEU HD1 H .67 . 1 341 71 72 LEU HD2 H .67 . 1 342 71 72 LEU N N 124.7 . 1 343 72 73 GLN H H 8.96 . 1 344 72 73 GLN HA H 5.43 . 1 345 72 73 GLN HB2 H 1.86 . 2 346 72 73 GLN HB3 H 1.98 . 2 347 72 73 GLN HG2 H 2.07 . 2 348 72 73 GLN HG3 H 2.45 . 2 349 72 73 GLN N N 120.4 . 1 350 73 74 SER H H 10.07 . 1 351 73 74 SER HA H 4.85 . 1 352 73 74 SER HB2 H 3.86 . 2 353 73 74 SER HB3 H 4.78 . 2 354 73 74 SER N N 126.1 . 1 355 74 75 ASP H H 8.39 . 1 356 74 75 ASP HA H 4.57 . 1 357 74 75 ASP HB2 H 1.85 . 2 358 74 75 ASP HB3 H 2.15 . 2 359 74 75 ASP N N 121.1 . 1 360 75 76 GLY H H 8.14 . 1 361 75 76 GLY HA2 H 3.58 . 2 362 75 76 GLY HA3 H 4.44 . 2 363 75 76 GLY N N 108.2 . 1 364 76 77 GLY H H 8.93 . 1 365 76 77 GLY HA2 H 3.68 . 2 366 76 77 GLY HA3 H 4.15 . 2 367 76 77 GLY N N 107.3 . 1 368 77 78 ARG H H 8.23 . 1 369 77 78 ARG HA H 4.59 . 1 370 77 78 ARG N N 122.1 . 1 371 78 79 GLU H H 8.93 . 1 372 78 79 GLU HA H 5.15 . 1 373 78 79 GLU HB2 H 1.71 . 2 374 78 79 GLU HB3 H 1.87 . 2 375 78 79 GLU HG2 H 2.07 . 2 376 78 79 GLU HG3 H 2.36 . 2 377 78 79 GLU N N 125.2 . 1 378 79 80 ILE H H 8.9 . 1 379 79 80 ILE HA H 5.07 . 1 380 79 80 ILE HB H 1.33 . 1 381 79 80 ILE HG2 H .49 . 1 382 79 80 ILE N N 124.4 . 1 383 80 81 LEU H H 9.56 . 1 384 80 81 LEU HA H 5.2 . 1 385 80 81 LEU HB2 H 1.51 . 2 386 80 81 LEU HB3 H 1.73 . 2 387 80 81 LEU N N 130.3 . 1 388 81 82 ILE H H 8.72 . 1 389 81 82 ILE HA H 4.45 . 1 390 81 82 ILE HB H 1.65 . 1 391 81 82 ILE HG2 H .67 . 1 392 81 82 ILE N N 125 . 1 393 82 83 HIS H H 8.04 . 1 394 82 83 HIS HA H 4.61 . 1 395 82 83 HIS HB2 H 2.32 . 2 396 82 83 HIS HB3 H 2.75 . 2 397 82 83 HIS HD2 H 6.71 . 1 398 82 83 HIS HE1 H 7.87 . 1 399 82 83 HIS N N 128.5 . 1 400 83 84 PHE H H 9.14 . 1 401 83 84 PHE HA H 4.49 . 1 402 83 84 PHE HB2 H 2.44 . 2 403 83 84 PHE HB3 H 3.6 . 2 404 83 84 PHE HD1 H 7.01 . 1 405 83 84 PHE HD2 H 7.01 . 1 406 83 84 PHE N N 127.1 . 1 407 84 85 GLY H H 7.6 . 1 408 84 85 GLY HA2 H 3.35 . 2 409 84 85 GLY HA3 H 3.71 . 2 410 84 85 GLY N N 118.9 . 1 411 85 86 ILE H H 7.18 . 1 412 85 86 ILE HA H 4.68 . 1 413 85 86 ILE HB H 1.89 . 1 414 85 86 ILE HG2 H .99 . 1 415 85 86 ILE N N 113.3 . 1 416 86 87 ASP H H 9.05 . 1 417 86 87 ASP HA H 4.53 . 1 418 86 87 ASP HB2 H 2.71 . 2 419 86 87 ASP HB3 H 3.17 . 2 420 86 87 ASP N N 119.9 . 1 421 87 88 THR H H 7.94 . 1 422 87 88 THR HA H 3.79 . 1 423 87 88 THR HB H 4.04 . 1 424 87 88 THR HG2 H 1.55 . 1 425 87 88 THR N N 107.8 . 1 426 88 89 VAL H H 8.32 . 1 427 88 89 VAL HA H 3.38 . 1 428 88 89 VAL HB H 1.8 . 1 429 88 89 VAL HG1 H .81 . 2 430 88 89 VAL HG2 H .99 . 2 431 88 89 VAL N N 124.5 . 1 432 89 90 SER H H 7.36 . 1 433 89 90 SER HA H 4.16 . 1 434 89 90 SER HB2 H 3.98 . 2 435 89 90 SER HB3 H 4.01 . 2 436 89 90 SER N N 116.4 . 1 437 90 91 LEU H H 7.31 . 1 438 90 91 LEU HA H 4.35 . 1 439 90 91 LEU N N 120.3 . 1 440 91 92 LYS H H 8.12 . 1 441 91 92 LYS HA H 3.74 . 1 442 91 92 LYS N N 114.9 . 1 443 92 93 GLY H H 9.13 . 1 444 92 93 GLY HA2 H 3.86 . 2 445 92 93 GLY HA3 H 4.25 . 2 446 92 93 GLY N N 107 . 1 447 93 94 GLU H H 7.71 . 1 448 93 94 GLU HA H 4.16 . 1 449 93 94 GLU HB2 H 2.08 . 1 450 93 94 GLU HB3 H 2.08 . 1 451 93 94 GLU HG2 H 2.28 . 1 452 93 94 GLU HG3 H 2.28 . 1 453 93 94 GLU N N 123.6 . 1 454 94 95 GLY H H 8.45 . 1 455 94 95 GLY HA2 H 3.54 . 2 456 94 95 GLY HA3 H 4.07 . 2 457 94 95 GLY N N 110.9 . 1 458 95 96 PHE H H 7.72 . 1 459 95 96 PHE HA H 4.7 . 1 460 95 96 PHE HB2 H 2.76 . 2 461 95 96 PHE HB3 H 2.87 . 2 462 95 96 PHE HD1 H 6.87 . 1 463 95 96 PHE HD2 H 6.87 . 1 464 95 96 PHE HE1 H 7.07 . 1 465 95 96 PHE HE2 H 7.07 . 1 466 95 96 PHE HZ H 7 . 1 467 95 96 PHE N N 118.3 . 1 468 96 97 THR H H 8.74 . 1 469 96 97 THR HA H 4.41 . 1 470 96 97 THR HB H 3.91 . 1 471 96 97 THR HG2 H .77 . 1 472 96 97 THR N N 118.2 . 1 473 97 98 SER H H 8.71 . 1 474 97 98 SER HA H 5.15 . 1 475 97 98 SER HB2 H 3.77 . 2 476 97 98 SER HB3 H 3.76 . 2 477 97 98 SER N N 119.3 . 1 478 98 99 PHE H H 8.3 . 1 479 98 99 PHE HA H 4.56 . 1 480 98 99 PHE HB2 H 2.42 . 2 481 98 99 PHE HB3 H 3.47 . 2 482 98 99 PHE HD1 H 7.08 . 1 483 98 99 PHE HD2 H 7.08 . 1 484 98 99 PHE HE1 H 7.23 . 1 485 98 99 PHE HE2 H 7.23 . 1 486 98 99 PHE N N 120.8 . 1 487 99 100 VAL H H 7.61 . 1 488 99 100 VAL HA H 4.9 . 1 489 99 100 VAL HB H 2.28 . 1 490 99 100 VAL HG1 H .83 . 2 491 99 100 VAL HG2 H 1.05 . 2 492 99 100 VAL N N 110.1 . 1 493 100 101 SER H H 8.76 . 1 494 100 101 SER HA H 4.66 . 1 495 100 101 SER HB2 H 3.59 . 2 496 100 101 SER HB3 H 3.81 . 2 497 100 101 SER N N 115.9 . 1 498 101 102 GLU H H 8.79 . 1 499 101 102 GLU HA H 3.43 . 1 500 101 102 GLU HB2 H 1.86 . 2 501 101 102 GLU HB3 H 1.97 . 2 502 101 102 GLU HG2 H 2.13 . 2 503 101 102 GLU HG3 H 2.28 . 2 504 101 102 GLU N N 121.9 . 1 505 102 103 GLY H H 8.66 . 1 506 102 103 GLY HA2 H 3.57 . 2 507 102 103 GLY HA3 H 4.45 . 2 508 102 103 GLY N N 113.7 . 1 509 103 104 ASP H H 7.87 . 1 510 103 104 ASP HA H 4.51 . 1 511 103 104 ASP HB2 H 2.55 . 2 512 103 104 ASP HB3 H 2.73 . 2 513 103 104 ASP N N 121.1 . 1 514 104 105 ARG H H 8.5 . 1 515 104 105 ARG HA H 4.88 . 1 516 104 105 ARG HB2 H 1.83 . 2 517 104 105 ARG HB3 H 2.01 . 2 518 104 105 ARG N N 121 . 1 519 105 106 VAL H H 8.68 . 1 520 105 106 VAL HA H 5.21 . 1 521 105 106 VAL HB H 1.89 . 1 522 105 106 VAL HG1 H .53 . 2 523 105 106 VAL HG2 H .72 . 2 524 105 106 VAL N N 113.6 . 1 525 106 107 GLU H H 7.42 . 1 526 106 107 GLU HA H 4.78 . 1 527 106 107 GLU N N 120.7 . 1 528 107 108 PRO HA H 3.85 . 1 529 107 108 PRO HD2 H 3.36 . 2 530 107 108 PRO HD3 H 3.72 . 2 531 108 109 GLY H H 9.48 . 1 532 108 109 GLY HA2 H 3.09 . 2 533 108 109 GLY HA3 H 4.3 . 2 534 108 109 GLY N N 111.1 . 1 535 109 110 GLN H H 7.93 . 1 536 109 110 GLN HA H 4.09 . 1 537 109 110 GLN HB2 H 1.8 . 1 538 109 110 GLN HB3 H 1.8 . 1 539 109 110 GLN HG2 H 2.26 . 1 540 109 110 GLN HG3 H 2.26 . 1 541 109 110 GLN N N 122.2 . 1 542 110 111 LYS H H 8.75 . 1 543 110 111 LYS HA H 3.82 . 1 544 110 111 LYS N N 127.6 . 1 545 111 112 LEU H H 9.3 . 1 546 111 112 LEU HA H 4.68 . 1 547 111 112 LEU HB2 H 1.58 . 1 548 111 112 LEU HB3 H 1.58 . 1 549 111 112 LEU N N 121.5 . 1 550 112 113 LEU H H 7.79 . 1 551 112 113 LEU HA H 5.56 . 1 552 112 113 LEU HB2 H 1.38 . 2 553 112 113 LEU HB3 H 1.48 . 2 554 112 113 LEU HD1 H .86 . 2 555 112 113 LEU HD2 H .88 . 2 556 112 113 LEU N N 116.9 . 1 557 113 114 GLU H H 9.02 . 1 558 113 114 GLU HA H 4.97 . 1 559 113 114 GLU HB2 H 1.99 . 1 560 113 114 GLU HB3 H 1.99 . 1 561 113 114 GLU HG2 H 2.17 . 1 562 113 114 GLU HG3 H 2.17 . 1 563 113 114 GLU N N 121.3 . 1 564 114 115 VAL H H 8.69 . 1 565 114 115 VAL HA H 4.27 . 1 566 114 115 VAL HB H 1.07 . 1 567 114 115 VAL HG1 H .27 . 2 568 114 115 VAL HG2 H .18 . 2 569 114 115 VAL N N 124.9 . 1 570 115 116 ASP H H 8.45 . 1 571 115 116 ASP HA H 4.58 . 1 572 115 116 ASP HB2 H 2.42 . 2 573 115 116 ASP HB3 H 2.82 . 2 574 115 116 ASP N N 126.1 . 1 575 116 117 LEU H H 8.23 . 1 576 116 117 LEU HA H 3.7 . 1 577 116 117 LEU HB2 H 1.42 . 2 578 116 117 LEU HB3 H 1.89 . 2 579 116 117 LEU HG H 1.74 . 1 580 116 117 LEU HD1 H .73 . 2 581 116 117 LEU HD2 H .8 . 2 582 116 117 LEU N N 125.2 . 1 583 117 118 ASP H H 8.03 . 1 584 117 118 ASP HA H 4.35 . 1 585 117 118 ASP HB2 H 2.58 . 2 586 117 118 ASP HB3 H 2.7 . 2 587 117 118 ASP N N 116.4 . 1 588 118 119 ALA H H 7.21 . 1 589 118 119 ALA HA H 4.19 . 1 590 118 119 ALA HB H 1.34 . 1 591 118 119 ALA N N 119.7 . 1 592 119 120 VAL H H 7.61 . 1 593 119 120 VAL HA H 3.88 . 1 594 119 120 VAL HB H 1.74 . 1 595 119 120 VAL HG1 H .73 . 2 596 119 120 VAL HG2 H .87 . 2 597 119 120 VAL N N 116 . 1 598 120 121 LYS H H 8.43 . 1 599 120 121 LYS HA H 3.95 . 1 600 120 121 LYS N N 118.6 . 1 601 121 122 PRO HD2 H 3.22 . 2 602 121 122 PRO HD3 H 3.69 . 2 603 122 123 ASN H H 7.85 . 1 604 122 123 ASN HA H 4.91 . 1 605 122 123 ASN HB2 H 2.58 . 2 606 122 123 ASN HB3 H 3.08 . 2 607 122 123 ASN N N 112 . 1 608 123 124 VAL H H 7.25 . 1 609 123 124 VAL HA H 5.05 . 1 610 123 124 VAL HB H 2.84 . 1 611 123 124 VAL HG1 H .72 . 2 612 123 124 VAL HG2 H .9 . 2 613 123 124 VAL N N 110.6 . 1 614 124 125 PRO HA H 4.54 . 1 615 124 125 PRO HD2 H 3.87 . 2 616 124 125 PRO HD3 H 4.16 . 2 617 125 126 SER H H 6.67 . 1 618 125 126 SER HA H 4.39 . 1 619 125 126 SER HB2 H 3.04 . 2 620 125 126 SER HB3 H 4.06 . 2 621 125 126 SER N N 105.6 . 1 622 126 127 LEU H H 8.68 . 1 623 126 127 LEU HA H 4.26 . 1 624 126 127 LEU HB2 H 1.52 . 2 625 126 127 LEU HB3 H 1.58 . 2 626 126 127 LEU N N 123.8 . 1 627 127 128 MET H H 8.52 . 1 628 127 128 MET HA H 3.73 . 1 629 127 128 MET N N 120.8 . 1 630 128 129 THR H H 7.95 . 1 631 128 129 THR HA H 4.98 . 1 632 128 129 THR HB H 4.14 . 1 633 128 129 THR HG2 H .88 . 1 634 128 129 THR N N 121.4 . 1 635 129 130 PRO HA H 4.21 . 1 636 129 130 PRO HD2 H 3.46 . 2 637 129 130 PRO HD3 H 4.55 . 2 638 130 131 ILE H H 8.53 . 1 639 130 131 ILE HA H 4.46 . 1 640 130 131 ILE HB H .44 . 1 641 130 131 ILE HG2 H .42 . 1 642 130 131 ILE N N 124.9 . 1 643 131 132 VAL H H 8.8 . 1 644 131 132 VAL HA H 4.59 . 1 645 131 132 VAL HB H 1.89 . 1 646 131 132 VAL HG1 H .71 . 2 647 131 132 VAL HG2 H .86 . 2 648 131 132 VAL N N 120.3 . 1 649 132 133 PHE H H 9.21 . 1 650 132 133 PHE HA H 5.23 . 1 651 132 133 PHE HB2 H 2.98 . 2 652 132 133 PHE HB3 H 3.22 . 2 653 132 133 PHE HD1 H 7.3 . 1 654 132 133 PHE HD2 H 7.3 . 1 655 132 133 PHE HE1 H 6.91 . 1 656 132 133 PHE HE2 H 6.91 . 1 657 132 133 PHE HZ H 6.23 . 1 658 132 133 PHE N N 125.1 . 1 659 133 134 THR H H 8.36 . 1 660 133 134 THR HA H 4.61 . 1 661 133 134 THR HB H 4.59 . 1 662 133 134 THR HG2 H 1.19 . 1 663 133 134 THR N N 113.4 . 1 664 134 135 ASN H H 8.22 . 1 665 134 135 ASN HA H 5.18 . 1 666 134 135 ASN HB2 H 2.65 . 2 667 134 135 ASN HB3 H 3.11 . 2 668 134 135 ASN N N 122.1 . 1 669 135 136 LEU H H 8.46 . 1 670 135 136 LEU HA H 4.18 . 1 671 135 136 LEU HB2 H 1.7 . 2 672 135 136 LEU HB3 H 1.87 . 2 673 135 136 LEU N N 120.3 . 1 674 136 137 ALA H H 8.97 . 1 675 136 137 ALA HA H 4.38 . 1 676 136 137 ALA HB H 1.34 . 1 677 136 137 ALA N N 125.1 . 1 678 137 138 GLU H H 8.52 . 1 679 137 138 GLU HA H 4.04 . 1 680 137 138 GLU N N 121.4 . 1 681 138 139 GLY H H 8.73 . 1 682 138 139 GLY HA2 H 3.68 . 2 683 138 139 GLY HA3 H 4.25 . 2 684 138 139 GLY N N 113.5 . 1 685 139 140 GLU H H 7.81 . 1 686 139 140 GLU HA H 4.83 . 1 687 139 140 GLU HB2 H 1.65 . 2 688 139 140 GLU HB3 H 2.35 . 2 689 139 140 GLU HG2 H 1.97 . 2 690 139 140 GLU HG3 H 2.18 . 2 691 139 140 GLU N N 119.6 . 1 692 140 141 THR H H 8.76 . 1 693 140 141 THR HA H 4.66 . 1 694 140 141 THR HB H 4.08 . 1 695 140 141 THR HG2 H 1.12 . 1 696 140 141 THR N N 114.1 . 1 697 141 142 VAL H H 8.3 . 1 698 141 142 VAL HA H 4.13 . 1 699 141 142 VAL HB H 1.97 . 1 700 141 142 VAL HG1 H .66 . 1 701 141 142 VAL HG2 H .66 . 1 702 141 142 VAL N N 121.9 . 1 703 142 143 SER H H 8.9 . 1 704 142 143 SER HA H 4.8 . 1 705 142 143 SER HB2 H 3.61 . 1 706 142 143 SER HB3 H 3.61 . 1 707 142 143 SER N N 123.3 . 1 708 143 144 ILE H H 8.76 . 1 709 143 144 ILE HA H 4.05 . 1 710 143 144 ILE HB H 1.82 . 1 711 143 144 ILE HG2 H .93 . 1 712 143 144 ILE N N 125.3 . 1 713 144 145 LYS H H 8.34 . 1 714 144 145 LYS HA H 4.35 . 1 715 144 145 LYS N N 125.8 . 1 716 145 146 ALA H H 7.15 . 1 717 145 146 ALA HA H 4.54 . 1 718 145 146 ALA HB H 1.33 . 1 719 145 146 ALA N N 121.4 . 1 720 146 147 SER H H 8.04 . 1 721 146 147 SER HA H 4.43 . 1 722 146 147 SER HB2 H 3.7 . 1 723 146 147 SER HB3 H 3.7 . 1 724 146 147 SER N N 111.2 . 1 725 147 148 GLY H H 8.71 . 1 726 147 148 GLY HA2 H 3.71 . 2 727 147 148 GLY HA3 H 4.1 . 2 728 147 148 GLY N N 111.1 . 1 729 148 149 SER H H 8.33 . 1 730 148 149 SER HA H 4.92 . 1 731 148 149 SER HB2 H 3.76 . 2 732 148 149 SER HB3 H 3.88 . 2 733 148 149 SER N N 120.3 . 1 734 149 150 VAL H H 9.31 . 1 735 149 150 VAL HA H 5.04 . 1 736 149 150 VAL HB H 1.96 . 1 737 149 150 VAL HG1 H .81 . 2 738 149 150 VAL HG2 H .91 . 2 739 149 150 VAL N N 118.1 . 1 740 150 151 ASN H H 8.16 . 1 741 150 151 ASN HA H 5.39 . 1 742 150 151 ASN HB2 H 2.57 . 2 743 150 151 ASN HB3 H 2.68 . 2 744 150 151 ASN N N 119.1 . 1 745 151 152 ARG H H 8.63 . 1 746 151 152 ARG HA H 3.6 . 1 747 151 152 ARG N N 120.7 . 1 748 152 153 GLU H H 9.49 . 1 749 152 153 GLU HA H 3.23 . 1 750 152 153 GLU N N 113.5 . 1 751 153 154 GLN H H 8.01 . 1 752 153 154 GLN HA H 4.12 . 1 753 153 154 GLN HB2 H 1.82 . 1 754 153 154 GLN HB3 H 1.82 . 1 755 153 154 GLN N N 121.7 . 1 756 154 155 GLU H H 8.82 . 1 757 154 155 GLU HA H 4.51 . 1 758 154 155 GLU HB2 H 1.99 . 2 759 154 155 GLU HB3 H 2.11 . 2 760 154 155 GLU HG2 H 2.4 . 2 761 154 155 GLU HG3 H 2.28 . 2 762 154 155 GLU N N 125.6 . 1 763 155 156 ASP H H 8.87 . 1 764 155 156 ASP HA H 4.49 . 1 765 155 156 ASP HB2 H 2.56 . 2 766 155 156 ASP HB3 H 2.96 . 2 767 155 156 ASP N N 117.1 . 1 768 156 157 ILE H H 7.84 . 1 769 156 157 ILE HA H 4.16 . 1 770 156 157 ILE N N 108.2 . 1 771 157 158 VAL H H 7.64 . 1 772 157 158 VAL HA H 4.84 . 1 773 157 158 VAL HB H 1.51 . 1 774 157 158 VAL HG1 H .13 . 2 775 157 158 VAL HG2 H .26 . 2 776 157 158 VAL N N 114.3 . 1 777 158 159 LYS H H 8.67 . 1 778 158 159 LYS HA H 4.5 . 1 779 158 159 LYS HB2 H 1.52 . 2 780 158 159 LYS HB3 H 1.66 . 2 781 158 159 LYS N N 121.8 . 1 782 159 160 ILE H H 8.57 . 1 783 159 160 ILE HA H 4.59 . 1 784 159 160 ILE HB H 1.62 . 1 785 159 160 ILE HG12 H .57 . 2 786 159 160 ILE HG13 H .89 . 2 787 159 160 ILE HG2 H .58 . 1 788 159 160 ILE HD1 H -.07 . 1 789 159 160 ILE N N 124.7 . 1 790 160 161 GLU H H 8.88 . 1 791 160 161 GLU HA H 4.62 . 1 792 160 161 GLU HB2 H 1.76 . 2 793 160 161 GLU HB3 H 2.02 . 2 794 160 161 GLU HG2 H 2.1 . 1 795 160 161 GLU HG3 H 2.1 . 1 796 160 161 GLU N N 128.7 . 1 797 161 162 LYS H H 7.83 . 1 798 161 162 LYS HA H 4.41 . 1 799 161 162 LYS HB2 H 1.67 . 2 800 161 162 LYS HB3 H 1.77 . 2 801 161 162 LYS N N 124.7 . 1 stop_ save_