data_435 #Corrected using PDB structure: 2NVHA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 6 N HA 6.24 5.28 # 15 K HA 3.54 4.28 # 27 A HA 6.15 5.41 #135 G HA 3.37 2.26 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.01 N/A N/A N/A 0.14 0.13 # #bmr435.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr435.str file): #HA CA CB CO N HN #N/A N/A N/A N/A +0.14 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 N/A N/A N/A +/-0.29 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.873 N/A N/A N/A 0.850 0.771 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.139 N/A N/A N/A 1.722 0.284 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Driscoll Paul C. . 2 Clore G. Marius . 3 Marion Dominique . . 4 Wingfield Paul . . 5 Gronenborn Angela M. . stop_ _BMRB_accession_number 435 _BMRB_flat_file_name bmr435.str _Entry_type revision _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _NMR_STAR_version 2.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 665 '15N chemical shifts' 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 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 ; Driscoll, Paul C., Clore, G. Marius, Marion, Dominique, Wingfield, Paul, Gronenborn, Angela M., "Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy," Biochemistry 29, 3542-3556 (1990). ; _Citation_title ; Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy ; _Citation_status published _Citation_type journal _MEDLINE_UI_code ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Driscoll Paul C. . 2 Clore G. Marius . 3 Marion Dominique . . 4 Wingfield Paul . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Page_first 3542 _Page_last 3556 _Year 1990 save_ ################################## # Molecular system description # ################################## save_system_interleukin_1-beta _Saveframe_category molecular_system _Mol_system_name 'interleukin 1-beta' _Abbreviation_common ? loop_ _Mol_system_component_name _Mol_label 'interleukin 1-beta' $interleukin_1-beta stop_ _System_physical_state ? _System_oligomer_state ? _System_paramagnetic ? loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1IOB "Interleukin-1 Beta From Joint X-Ray And Nmr Refinement" . PDB 2I1B "Interleukin-1Beta (IL-1Beta)" . PDB 1ITB "A Chain A, Type-1 Interleukin-1 Receptor Complexed With Interleukin-1 Beta" . PDB 6I1B "Interleukin-1Beta (NMR, Minimized Average Structure)" . PDB 7I1B "Interleukin-1Beta (NMR, 32 Structures)" . PDB 4I1B "Interleukin-1Beta (IL-1Beta)" . PDB 5I1B "Interleukin 1-Beta" . PDB 1I1B "Interleukin-1Beta (IL-1Beta)" . PDB 9ILB "A Chain A, Human Interleukin-1 Beta" . PDB 31BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys 71 Replaced By Ser) (C71S)" . PDB 21BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys 71 Replaced By Ala) (C71A)" . PDB 41BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys 8 Replaced By Ala (C8A)" . PDB 1HIB "Interleukin-1 Beta (Human) Mutant With Thr 9 Replaced By Gly (T9g)" . stop_ save_ ######################## # Monomeric polymers # ######################## save_interleukin_1-beta _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'interleukin 1-beta' _Name_variant des-ala-1-IL-1beta _Abbreviation_common ? ############################## # Polymer residue sequence # ############################## _Residue_count 152 _Mol_residue_sequence ; PVRSLNCTLRDSQQKSLVMS GPYELKALHLQGQDMEQQVV FSMSFVQGEESNDKIPVALG LKEKNLYLSCVLKDDKPTLQ LESVDPKNYPKKKMEKRFVF NKIEINNKLEFESAQFPNWY ISTSQAENMPVFLGGTKGGQ DITDFTMQFVSS ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 VAL 3 ARG 4 SER 5 LEU 6 ASN 7 CYS 8 THR 9 LEU 10 ARG 11 ASP 12 SER 13 GLN 14 GLN 15 LYS 16 SER 17 LEU 18 VAL 19 MET 20 SER 21 GLY 22 PRO 23 TYR 24 GLU 25 LEU 26 LYS 27 ALA 28 LEU 29 HIS 30 LEU 31 GLN 32 GLY 33 GLN 34 ASP 35 MET 36 GLU 37 GLN 38 GLN 39 VAL 40 VAL 41 PHE 42 SER 43 MET 44 SER 45 PHE 46 VAL 47 GLN 48 GLY 49 GLU 50 GLU 51 SER 52 ASN 53 ASP 54 LYS 55 ILE 56 PRO 57 VAL 58 ALA 59 LEU 60 GLY 61 LEU 62 LYS 63 GLU 64 LYS 65 ASN 66 LEU 67 TYR 68 LEU 69 SER 70 CYS 71 VAL 72 LEU 73 LYS 74 ASP 75 ASP 76 LYS 77 PRO 78 THR 79 LEU 80 GLN 81 LEU 82 GLU 83 SER 84 VAL 85 ASP 86 PRO 87 LYS 88 ASN 89 TYR 90 PRO 91 LYS 92 LYS 93 LYS 94 MET 95 GLU 96 LYS 97 ARG 98 PHE 99 VAL 100 PHE 101 ASN 102 LYS 103 ILE 104 GLU 105 ILE 106 ASN 107 ASN 108 LYS 109 LEU 110 GLU 111 PHE 112 GLU 113 SER 114 ALA 115 GLN 116 PHE 117 PRO 118 ASN 119 TRP 120 TYR 121 ILE 122 SER 123 THR 124 SER 125 GLN 126 ALA 127 GLU 128 ASN 129 MET 130 PRO 131 VAL 132 PHE 133 LEU 134 GLY 135 GLY 136 THR 137 LYS 138 GLY 139 GLY 140 GLN 141 ASP 142 ILE 143 THR 144 ASP 145 PHE 146 THR 147 MET 148 GLN 149 PHE 150 VAL 151 SER 152 SER stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-06-24 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 1I1B "Interleukin-1Beta (IL-1Beta)" 99.35 153 100 100 5e-83 PDB 1IOB "Interleukin-1 Beta From Joint X-Ray And NmrRefinement" 99.35 153 100 100 5e-83 PDB 1ITB "A Chain A, Type-1 Interleukin-1 ReceptorComplexed With Interleukin-1 Beta" 99.35 153 100 100 5e-83 PDB 2I1B "Interleukin-1Beta (IL-1Beta)" 99.35 153 100 100 5e-83 PDB 4I1B "Interleukin-1Beta (IL-1Beta)" 99.35 153 100 100 5e-83 PDB 5I1B "Interleukin 1-Beta" 99.35 153 100 100 5e-83 PDB 6I1B "Interleukin-1Beta (NMR, Minimized AverageStructure)" 99.35 153 100 100 5e-83 PDB 7I1B "Interleukin-1Beta (NMR, 32 Structures)" 99.35 153 100 100 5e-83 PDB 9ILB "A Chain A, Human Interleukin-1 Beta" 99.35 153 100 100 5e-83 PDB 1HIB "Interleukin-1 Beta (Human) Mutant With Thr 9Replaced By Gly (T9g)" 99.35 153 99 99 3e-82 PDB 1S0L "A Chain A, Interleukin 1 Beta Mutant F42w" 99.35 153 99 100 2e-82 PDB 21BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys71 Replaced By Ala) (C71A)" 99.35 153 99 99 5e-82 PDB 31BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys71 Replaced By Ser) (C71S)" 99.35 153 99 99 7e-82 PDB 41BI "Interleukin-1Beta (IL-1Beta) (Mutant With Cys8 Replaced By Ala (C8A)" 99.35 153 99 99 5e-82 PDB 1L2H "A Chain A, Crystal Structure Of Interleukin1-Beta F42wW120F MUTANT" 99.35 153 99 100 3e-81 EMBL CAA26372.1 "unnamed protein product [Homo sapiens]" 56.51 269 100 100 5e-83 EMBL CAA28185.1 "prointerleukin-1-beta [Homo sapiens]" 56.51 269 100 100 5e-83 EMBL CAA39567.1 "prointerleukin-1 beta [Homo sapiens]" 56.51 269 100 100 5e-83 EMBL CAG28607.1 "IL1B [Homo sapiens]" 56.51 269 100 100 5e-83 GenBank AAA36106.1 "interleukin 1 precursor polypeptide" 56.51 269 100 100 5e-83 GenBank AAA59135.1 "interleukin 1-beta" 56.51 269 100 100 5e-83 GenBank AAA74137.1 "interleukin 1-beta" 56.51 269 100 100 5e-83 GenBank AAH08678.1 "Interleukin 1, beta, proprotein [Homosapiens]" 56.51 269 100 100 5e-83 GenBank AAM88883.1 "interleukin 1, beta [Homo sapiens]" 56.51 269 100 100 5e-83 PIR ICHU1B "interleukin-1 beta precursor [validated] -human" 56.51 269 100 100 5e-83 PRF 1107273B "interleukin 1beta" 56.51 269 100 100 5e-83 REF NP_000567.1 "interleukin 1, beta proprotein;preinterleukin 1 beta; catabolin [Homo sapiens]" 56.51 269 100 100 5e-83 SWISS-PROT P01584 "IL1B_HUMAN Interleukin-1 beta precursor (IL-1beta) (Catabolin)" 56.51 269 100 100 5e-83 tpe CAD29872.1 "TPA: pro-interleukin-1-beta [Homosapiens]" 56.51 269 100 100 5e-83 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Genus _Species _Strain $interleukin_1-beta human ? Homo sapiens generic stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Genus _Species _Strain $interleukin_1-beta 'not available' Escherichia coli generic stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling ? ? ? ? stop_ save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 . na temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Chem_shift_units _Chem_shift_value DSS H ppm 0 'liquid NH3' N ppm 0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts 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 1-beta' loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 PRO HA H 4.50 . 1 2 1 PRO HD2 H 3.68 . 2 3 1 PRO HD3 H 3.59 . 2 4 2 VAL H H 8.00 . 1 5 2 VAL HA H 4.15 . 1 6 2 VAL HB H 1.93 . 1 7 2 VAL HG1 H 0.83 . 1 8 2 VAL HG2 H 0.83 . 1 9 2 VAL N N 119.24 . 1 10 3 ARG H H 9.00 . 1 11 3 ARG HA H 4.47 . 1 12 3 ARG N N 128.44 . 1 13 4 SER H H 8.28 . 1 14 4 SER N N 118.54 . 1 15 5 LEU H H 9.03 . 1 16 5 LEU HA H 4.78 . 1 17 5 LEU HB2 H 1.82 . 2 18 5 LEU HB3 H 1.81 . 2 19 5 LEU HG H 1.84 . 1 20 5 LEU HD1 H 1.02 . 2 21 5 LEU HD2 H 0.98 . 2 22 5 LEU N N 122.54 . 1 23 6 ASN H H 8.78 . 1 24 6 ASN HA H 6.25 . 1 25 6 ASN HB2 H 2.86 . 2 26 6 ASN HB3 H 2.32 . 2 27 6 ASN N N 121.04 . 1 28 7 CYS H H 9.59 . 1 29 7 CYS HA H 5.76 . 1 30 7 CYS HB2 H 2.96 . 2 31 7 CYS HB3 H 2.86 . 2 32 7 CYS N N 117.94 . 1 33 8 THR H H 8.93 . 1 34 8 THR HA H 5.06 . 1 35 8 THR HB H 4.39 . 1 36 8 THR HG2 H 1.18 . 1 37 8 THR N N 109.64 . 1 38 9 LEU H H 9.41 . 1 39 9 LEU HA H 5.45 . 1 40 9 LEU HB2 H 1.53 . 2 41 9 LEU HB3 H 1.07 . 2 42 9 LEU HG H 1.18 . 1 43 9 LEU HD1 H 0.58 . 2 44 9 LEU HD2 H 0.40 . 2 45 9 LEU N N 120.84 . 1 46 10 ARG H H 8.62 . 1 47 10 ARG HA H 5.28 . 1 48 10 ARG HB2 H 1.66 . 2 49 10 ARG HB3 H 1.60 . 2 50 10 ARG N N 119.74 . 1 51 11 ASP H H 8.71 . 1 52 11 ASP HA H 4.65 . 1 53 11 ASP N N 121.34 . 1 54 12 SER H H 7.42 . 1 55 12 SER HA H 3.99 . 1 56 12 SER HB2 H 3.95 . 2 57 12 SER HB3 H 3.56 . 2 58 12 SER N N 114.54 . 1 59 13 GLN H H 8.02 . 1 60 13 GLN HA H 4.55 . 1 61 13 GLN HB2 H 2.56 . 2 62 13 GLN HB3 H 1.59 . 2 63 13 GLN N N 120.54 . 1 64 14 GLN H H 8.44 . 1 65 14 GLN HA H 3.71 . 1 66 14 GLN HB2 H 2.62 . 1 67 14 GLN HB3 H 2.62 . 1 68 14 GLN N N 111.74 . 1 69 15 LYS H H 8.48 . 1 70 15 LYS HA H 3.55 . 1 71 15 LYS HB2 H 1.97 . 1 72 15 LYS HB3 H 1.97 . 1 73 15 LYS N N 120.34 . 1 74 16 SER H H 8.27 . 1 75 16 SER HA H 4.91 . 1 76 16 SER HB2 H 4.03 . 2 77 16 SER HB3 H 3.76 . 2 78 16 SER N N 119.64 . 1 79 17 LEU H H 8.82 . 1 80 17 LEU HA H 5.38 . 1 81 17 LEU HB2 H 2.15 . 2 82 17 LEU HB3 H 1.40 . 2 83 17 LEU N N 122.54 . 1 84 18 VAL H H 8.80 . 1 85 18 VAL HA H 4.68 . 1 86 18 VAL HB H 2.03 . 1 87 18 VAL HG1 H 0.78 . 2 88 18 VAL HG2 H 0.66 . 2 89 18 VAL N N 115.64 . 1 90 19 MET H H 8.68 . 1 91 19 MET HA H 4.90 . 1 92 19 MET HB2 H 2.19 . 2 93 19 MET HB3 H 1.70 . 2 94 19 MET HG2 H 2.50 . 2 95 19 MET HG3 H 2.36 . 2 96 19 MET N N 121.04 . 1 97 20 SER H H 8.59 . 1 98 20 SER HA H 4.52 . 1 99 20 SER HB2 H 3.60 . 2 100 20 SER HB3 H 3.52 . 2 101 20 SER N N 120.14 . 1 102 21 GLY H H 8.11 . 1 103 21 GLY HA2 H 4.12 . 2 104 21 GLY HA3 H 3.97 . 2 105 21 GLY N N 111.84 . 1 106 22 PRO HA H 4.02 . 1 107 22 PRO HD2 H 3.59 . 2 108 22 PRO HD3 H 3.44 . 2 109 23 TYR H H 8.00 . 1 110 23 TYR HA H 4.78 . 1 111 23 TYR HB2 H 3.54 . 2 112 23 TYR HB3 H 2.76 . 2 113 23 TYR HD1 H 7.09 . 1 114 23 TYR HD2 H 7.09 . 1 115 23 TYR HE1 H 6.78 . 1 116 23 TYR HE2 H 6.78 . 1 117 23 TYR N N 110.74 . 1 118 24 GLU H H 7.20 . 1 119 24 GLU HA H 4.67 . 1 120 24 GLU HB2 H 2.04 . 2 121 24 GLU HB3 H 1.94 . 2 122 24 GLU HG2 H 2.30 . 2 123 24 GLU HG3 H 2.24 . 2 124 24 GLU N N 119.44 . 1 125 25 LEU H H 8.57 . 1 126 25 LEU HA H 5.24 . 1 127 25 LEU HB2 H 1.63 . 1 128 25 LEU HB3 H 1.63 . 1 129 25 LEU N N 123.14 . 1 130 26 LYS H H 9.18 . 1 131 26 LYS HA H 5.14 . 1 132 26 LYS HB2 H 1.48 . 2 133 26 LYS HB3 H 1.43 . 2 134 26 LYS N N 119.94 . 1 135 27 ALA H H 7.62 . 1 136 27 ALA HA H 6.16 . 1 137 27 ALA HB H 1.31 . 1 138 27 ALA N N 119.04 . 1 139 28 LEU H H 9.42 . 1 140 28 LEU HA H 4.87 . 1 141 28 LEU HB2 H 1.95 . 2 142 28 LEU HB3 H 1.58 . 2 143 28 LEU N N 125.74 . 1 144 29 HIS H H 10.19 . 1 145 29 HIS HA H 4.69 . 1 146 29 HIS HB2 H 3.23 . 2 147 29 HIS HB3 H 3.16 . 2 148 29 HIS N N 122.14 . 1 149 30 LEU H H 8.40 . 1 150 30 LEU HA H 4.67 . 1 151 30 LEU HB2 H 1.70 . 2 152 30 LEU HB3 H 1.30 . 2 153 30 LEU N N 126.14 . 1 154 31 GLN H H 8.88 . 1 155 31 GLN HA H 4.53 . 1 156 31 GLN HB2 H 2.19 . 2 157 31 GLN HB3 H 1.98 . 2 158 31 GLN HG2 H 2.31 . 2 159 31 GLN HG3 H 2.25 . 2 160 31 GLN N N 120.34 . 1 161 32 GLY H H 8.72 . 1 162 32 GLY HA2 H 3.99 . 2 163 32 GLY HA3 H 3.77 . 2 164 32 GLY N N 109.64 . 1 165 33 GLN H H 8.83 . 1 166 33 GLN HA H 4.27 . 1 167 33 GLN HB2 H 2.10 . 1 168 33 GLN HB3 H 2.10 . 1 169 33 GLN N N 121.84 . 1 170 34 ASP H H 7.86 . 1 171 34 ASP HA H 4.75 . 1 172 34 ASP HB2 H 2.89 . 2 173 34 ASP HB3 H 2.79 . 2 174 34 ASP N N 119.14 . 1 175 35 MET H H 7.68 . 1 176 35 MET HA H 4.21 . 1 177 35 MET HB2 H 2.05 . 1 178 35 MET HB3 H 2.05 . 1 179 35 MET N N 118.44 . 1 180 36 GLU H H 8.07 . 1 181 36 GLU HA H 4.22 . 1 182 36 GLU HB2 H 2.10 . 2 183 36 GLU HB3 H 2.02 . 2 184 36 GLU N N 117.74 . 1 185 37 GLN H H 7.94 . 1 186 37 GLN HA H 4.21 . 1 187 37 GLN HB2 H 2.23 . 2 188 37 GLN HB3 H 1.97 . 2 189 37 GLN N N 117.14 . 1 190 38 GLN H H 7.53 . 1 191 38 GLN HA H 4.42 . 1 192 38 GLN N N 117.44 . 1 193 39 VAL H H 8.30 . 1 194 39 VAL HA H 3.78 . 1 195 39 VAL HB H 1.58 . 1 196 39 VAL HG1 H 0.62 . 2 197 39 VAL HG2 H 0.19 . 2 198 39 VAL N N 122.84 . 1 199 40 VAL H H 7.69 . 1 200 40 VAL HA H 4.24 . 1 201 40 VAL HB H 1.83 . 1 202 40 VAL HG1 H 0.85 . 1 203 40 VAL HG2 H 0.85 . 1 204 40 VAL N N 124.04 . 1 205 41 PHE H H 9.58 . 1 206 41 PHE HA H 5.04 . 1 207 41 PHE HB2 H 3.07 . 2 208 41 PHE HB3 H 2.57 . 2 209 41 PHE HD1 H 6.90 . 1 210 41 PHE HD2 H 6.90 . 1 211 41 PHE HE1 H 7.00 . 1 212 41 PHE HE2 H 7.00 . 1 213 41 PHE HZ H 6.62 . 1 214 41 PHE N N 127.44 . 1 215 42 SER H H 9.17 . 1 216 42 SER HA H 5.16 . 1 217 42 SER HB2 H 3.61 . 2 218 42 SER HB3 H 3.45 . 2 219 42 SER N N 115.74 . 1 220 43 MET H H 9.57 . 1 221 43 MET HA H 5.30 . 1 222 43 MET HB2 H 2.23 . 1 223 43 MET HB3 H 2.23 . 1 224 43 MET N N 131.44 . 1 225 44 SER H H 8.88 . 1 226 44 SER HA H 5.36 . 1 227 44 SER HB2 H 3.71 . 2 228 44 SER HB3 H 3.58 . 2 229 44 SER N N 121.24 . 1 230 45 PHE H H 8.46 . 1 231 45 PHE HA H 4.77 . 1 232 45 PHE HB2 H 3.37 . 2 233 45 PHE HB3 H 2.98 . 2 234 45 PHE HD1 H 7.23 . 1 235 45 PHE HD2 H 7.23 . 1 236 45 PHE HE1 H 7.13 . 1 237 45 PHE HE2 H 7.13 . 1 238 45 PHE N N 123.34 . 1 239 46 VAL H H 7.45 . 1 240 46 VAL HA H 4.66 . 1 241 46 VAL N N 118.74 . 1 242 47 GLN H H 8.56 . 1 243 47 GLN N N 120.64 . 1 244 48 GLY H H 8.33 . 1 245 48 GLY HA2 H 4.12 . 2 246 48 GLY HA3 H 3.94 . 2 247 48 GLY N N 111.74 . 1 248 49 GLU H H 8.47 . 1 249 49 GLU HA H 4.35 . 1 250 49 GLU HB2 H 2.06 . 2 251 49 GLU HB3 H 1.92 . 2 252 49 GLU N N 121.44 . 1 253 50 GLU H H 8.51 . 1 254 50 GLU HA H 4.50 . 1 255 50 GLU HB2 H 2.09 . 2 256 50 GLU HB3 H 2.01 . 2 257 50 GLU HG2 H 2.34 . 2 258 50 GLU HG3 H 2.27 . 2 259 50 GLU N N 122.74 . 1 260 51 SER H H 8.39 . 1 261 51 SER HA H 4.63 . 1 262 51 SER HB2 H 3.97 . 2 263 51 SER HB3 H 3.88 . 2 264 51 SER N N 116.94 . 1 265 52 ASN H H 8.61 . 1 266 52 ASN HA H 4.60 . 1 267 52 ASN HB2 H 2.90 . 2 268 52 ASN HB3 H 2.83 . 2 269 52 ASN N N 119.84 . 1 270 53 ASP H H 8.53 . 1 271 53 ASP HA H 4.59 . 1 272 53 ASP HB2 H 2.77 . 1 273 53 ASP HB3 H 2.77 . 1 274 53 ASP N N 116.34 . 1 275 54 LYS H H 7.60 . 1 276 54 LYS HA H 4.69 . 1 277 54 LYS HB2 H 1.74 . 2 278 54 LYS HB3 H 1.51 . 2 279 54 LYS N N 118.94 . 1 280 55 ILE H H 8.37 . 1 281 55 ILE HA H 4.86 . 1 282 55 ILE HB H 2.09 . 1 283 55 ILE HG2 H 1.16 . 1 284 55 ILE N N 122.84 . 1 285 56 PRO HA H 5.37 . 1 286 56 PRO HB2 H 2.15 . 2 287 56 PRO HB3 H 1.83 . 2 288 56 PRO HG2 H 1.86 . 1 289 56 PRO HG3 H 1.86 . 1 290 56 PRO HD2 H 4.00 . 2 291 56 PRO HD3 H 3.96 . 2 292 57 VAL H H 10.01 . 1 293 57 VAL HA H 5.64 . 1 294 57 VAL HB H 2.08 . 1 295 57 VAL HG1 H 0.82 . 2 296 57 VAL HG2 H 0.73 . 2 297 57 VAL N N 117.94 . 1 298 58 ALA H H 8.68 . 1 299 58 ALA HA H 5.42 . 1 300 58 ALA HB H 1.51 . 1 301 58 ALA N N 121.04 . 1 302 59 LEU H H 10.53 . 1 303 59 LEU HA H 4.86 . 1 304 59 LEU HB2 H 1.51 . 2 305 59 LEU HB3 H 0.86 . 2 306 59 LEU N N 124.44 . 1 307 60 GLY H H 8.26 . 1 308 60 GLY HA2 H 4.15 . 2 309 60 GLY HA3 H 2.38 . 2 310 60 GLY N N 110.04 . 1 311 61 LEU H H 8.22 . 1 312 61 LEU HA H 4.46 . 1 313 61 LEU HB2 H 1.41 . 2 314 61 LEU HB3 H 1.34 . 2 315 61 LEU N N 121.54 . 1 316 62 LYS H H 8.16 . 1 317 62 LYS HA H 3.84 . 1 318 62 LYS N N 126.44 . 1 319 63 GLU H H 8.90 . 1 320 63 GLU HA H 3.98 . 1 321 63 GLU HB2 H 2.24 . 2 322 63 GLU HB3 H 2.09 . 2 323 63 GLU N N 118.74 . 1 324 64 LYS H H 7.57 . 1 325 64 LYS HA H 4.48 . 1 326 64 LYS HB2 H 1.47 . 1 327 64 LYS HB3 H 1.47 . 1 328 64 LYS N N 115.24 . 1 329 65 ASN H H 8.40 . 1 330 65 ASN HA H 4.41 . 1 331 65 ASN HB2 H 3.14 . 2 332 65 ASN HB3 H 3.01 . 2 333 65 ASN N N 116.34 . 1 334 66 LEU H H 6.82 . 1 335 66 LEU HA H 5.34 . 1 336 66 LEU HB2 H 1.42 . 2 337 66 LEU HB3 H 1.17 . 2 338 66 LEU N N 115.84 . 1 339 67 TYR H H 9.18 . 1 340 67 TYR HA H 4.96 . 1 341 67 TYR HB2 H 3.08 . 2 342 67 TYR HB3 H 2.51 . 2 343 67 TYR HD1 H 6.88 . 1 344 67 TYR HD2 H 6.88 . 1 345 67 TYR HE1 H 6.51 . 1 346 67 TYR HE2 H 6.51 . 1 347 67 TYR N N 121.64 . 1 348 68 LEU H H 8.49 . 1 349 68 LEU HA H 4.84 . 1 350 68 LEU HB2 H 1.96 . 2 351 68 LEU HB3 H 1.66 . 2 352 68 LEU N N 121.94 . 1 353 69 SER H H 9.17 . 1 354 69 SER HA H 5.23 . 1 355 69 SER HB2 H 3.66 . 2 356 69 SER HB3 H 3.28 . 2 357 69 SER N N 115.94 . 1 358 70 CYS H H 8.35 . 1 359 70 CYS HA H 5.53 . 1 360 70 CYS HB2 H 2.86 . 2 361 70 CYS HB3 H 2.46 . 2 362 70 CYS N N 119.64 . 1 363 71 VAL H H 8.80 . 1 364 71 VAL HA H 4.58 . 1 365 71 VAL HB H 1.99 . 1 366 71 VAL HG1 H 0.71 . 2 367 71 VAL HG2 H 0.55 . 2 368 71 VAL N N 117.14 . 1 369 72 LEU H H 8.52 . 1 370 72 LEU HA H 4.17 . 1 371 72 LEU HB2 H 1.48 . 2 372 72 LEU HB3 H 1.36 . 2 373 72 LEU HG H 1.35 . 1 374 72 LEU HD1 H 0.59 . 2 375 72 LEU HD2 H 0.43 . 2 376 72 LEU N N 123.84 . 1 377 73 LYS H H 8.20 . 1 378 73 LYS HA H 4.39 . 1 379 73 LYS HB2 H 1.80 . 2 380 73 LYS HB3 H 1.53 . 2 381 73 LYS N N 126.54 . 1 382 74 ASP H H 9.22 . 1 383 74 ASP HA H 4.15 . 1 384 74 ASP HB2 H 2.81 . 2 385 74 ASP HB3 H 2.66 . 2 386 74 ASP N N 127.64 . 1 387 75 ASP H H 8.46 . 1 388 75 ASP HA H 4.07 . 1 389 75 ASP HB2 H 2.86 . 2 390 75 ASP HB3 H 2.79 . 2 391 75 ASP N N 110.04 . 1 392 76 LYS H H 7.71 . 1 393 76 LYS HA H 4.66 . 1 394 76 LYS HB2 H 1.67 . 2 395 76 LYS HB3 H 1.60 . 2 396 76 LYS N N 119.94 . 1 397 77 PRO HA H 3.19 . 1 398 77 PRO HD2 H 3.07 . 1 399 77 PRO HD3 H 3.07 . 1 400 78 THR H H 8.83 . 1 401 78 THR HA H 4.58 . 1 402 78 THR HB H 3.93 . 1 403 78 THR HG2 H 1.20 . 1 404 78 THR N N 120.14 . 1 405 79 LEU H H 8.83 . 1 406 79 LEU HA H 5.13 . 1 407 79 LEU HB2 H 2.00 . 2 408 79 LEU HB3 H 1.50 . 2 409 79 LEU HG H 1.60 . 1 410 79 LEU HD1 H 1.09 . 2 411 79 LEU HD2 H 0.75 . 2 412 79 LEU N N 127.24 . 1 413 80 GLN H H 9.68 . 1 414 80 GLN HA H 4.98 . 1 415 80 GLN HB2 H 1.96 . 1 416 80 GLN HB3 H 1.96 . 1 417 80 GLN N N 126.44 . 1 418 81 LEU H H 8.44 . 1 419 81 LEU HA H 5.01 . 1 420 81 LEU HB2 H 1.83 . 2 421 81 LEU HB3 H 1.37 . 2 422 81 LEU HG H 1.59 . 1 423 81 LEU HD1 H 0.72 . 2 424 81 LEU HD2 H 0.71 . 2 425 81 LEU N N 122.14 . 1 426 82 GLU H H 9.17 . 1 427 82 GLU HA H 4.63 . 1 428 82 GLU HB2 H 2.10 . 1 429 82 GLU HB3 H 2.10 . 1 430 82 GLU N N 123.94 . 1 431 83 SER H H 8.71 . 1 432 83 SER HA H 5.15 . 1 433 83 SER HB2 H 3.92 . 2 434 83 SER HB3 H 3.90 . 2 435 83 SER N N 121.34 . 1 436 84 VAL H H 7.92 . 1 437 84 VAL HA H 4.59 . 1 438 84 VAL HB H 1.52 . 1 439 84 VAL N N 117.44 . 1 440 85 ASP H H 8.04 . 1 441 85 ASP HA H 4.90 . 1 442 85 ASP HB2 H 2.96 . 2 443 85 ASP HB3 H 2.69 . 2 444 85 ASP N N 122.14 . 1 445 87 LYS H H 8.38 . 1 446 87 LYS HA H 4.20 . 1 447 87 LYS HB2 H 1.80 . 2 448 87 LYS HB3 H 1.73 . 2 449 87 LYS N N 117.24 . 1 450 88 ASN H H 7.78 . 1 451 88 ASN HA H 4.75 . 1 452 88 ASN HB2 H 2.64 . 2 453 88 ASN HB3 H 2.50 . 2 454 88 ASN N N 114.64 . 1 455 89 TYR H H 7.30 . 1 456 89 TYR N N 116.84 . 1 457 90 PRO HA H 4.25 . 1 458 91 LYS H H 7.24 . 1 459 91 LYS HA H 4.41 . 1 460 91 LYS N N 117.44 . 1 461 92 LYS H H 8.29 . 1 462 92 LYS N N 119.44 . 1 463 93 LYS H H 7.80 . 1 464 93 LYS HA H 4.59 . 1 465 93 LYS HB2 H 1.75 . 2 466 93 LYS HB3 H 1.51 . 2 467 93 LYS HG2 H 1.30 . 2 468 93 LYS HG3 H 1.26 . 2 469 93 LYS N N 118.14 . 1 470 94 MET H H 7.64 . 1 471 94 MET HA H 4.23 . 1 472 94 MET N N 122.64 . 1 473 95 GLU H H 9.14 . 1 474 95 GLU HA H 4.09 . 1 475 95 GLU HB2 H 2.23 . 2 476 95 GLU HB3 H 2.08 . 2 477 95 GLU HG2 H 2.72 . 2 478 95 GLU HG3 H 2.44 . 2 479 95 GLU N N 122.84 . 1 480 96 LYS H H 8.23 . 1 481 96 LYS HA H 3.71 . 1 482 96 LYS HB2 H 1.71 . 2 483 96 LYS HB3 H 1.63 . 2 484 96 LYS HG2 H 1.30 . 2 485 96 LYS HG3 H 1.24 . 2 486 96 LYS N N 121.64 . 1 487 97 ARG H H 7.88 . 1 488 97 ARG HA H 3.91 . 1 489 97 ARG HB2 H 1.56 . 2 490 97 ARG HB3 H 1.49 . 2 491 97 ARG N N 114.34 . 1 492 98 PHE H H 7.84 . 1 493 98 PHE HA H 5.16 . 1 494 98 PHE HB2 H 3.69 . 2 495 98 PHE HB3 H 2.87 . 2 496 98 PHE HD1 H 7.51 . 1 497 98 PHE HD2 H 7.51 . 1 498 98 PHE HE1 H 7.04 . 1 499 98 PHE HE2 H 7.04 . 1 500 98 PHE HZ H 6.89 . 1 501 98 PHE N N 116.74 . 1 502 99 VAL H H 7.45 . 1 503 99 VAL HA H 4.36 . 1 504 99 VAL HB H 1.92 . 1 505 99 VAL HG1 H 0.90 . 2 506 99 VAL HG2 H 0.82 . 2 507 99 VAL N N 117.94 . 1 508 100 PHE H H 9.83 . 1 509 100 PHE HA H 5.15 . 1 510 100 PHE HB2 H 2.70 . 2 511 100 PHE HB3 H 2.67 . 2 512 100 PHE HD1 H 6.98 . 1 513 100 PHE HD2 H 6.98 . 1 514 100 PHE HE1 H 7.06 . 1 515 100 PHE HE2 H 7.06 . 1 516 100 PHE HZ H 6.81 . 1 517 100 PHE N N 127.34 . 1 518 101 ASN H H 10.38 . 1 519 101 ASN HA H 5.01 . 1 520 101 ASN HB2 H 2.92 . 2 521 101 ASN HB3 H 2.29 . 2 522 101 ASN N N 121.24 . 1 523 102 LYS H H 9.38 . 1 524 102 LYS HA H 4.64 . 1 525 102 LYS N N 127.84 . 1 526 103 ILE H H 9.23 . 1 527 103 ILE HA H 4.45 . 1 528 103 ILE HB H 1.74 . 1 529 103 ILE HG2 H 0.90 . 1 530 103 ILE N N 133.84 . 1 531 104 GLU H H 8.48 . 1 532 104 GLU HA H 5.14 . 1 533 104 GLU HB2 H 1.94 . 2 534 104 GLU HB3 H 1.73 . 2 535 104 GLU HG2 H 2.14 . 2 536 104 GLU HG3 H 2.05 . 2 537 104 GLU N N 126.94 . 1 538 105 ILE H H 8.67 . 1 539 105 ILE HA H 4.33 . 1 540 105 ILE HB H 1.68 . 1 541 105 ILE HG12 H 1.36 . 2 542 105 ILE HG13 H 1.03 . 2 543 105 ILE HG2 H 0.80 . 1 544 105 ILE HD1 H 0.78 . 1 545 105 ILE N N 125.74 . 1 546 106 ASN H H 9.28 . 1 547 106 ASN HA H 4.27 . 1 548 106 ASN HB2 H 2.99 . 2 549 106 ASN HB3 H 2.72 . 2 550 106 ASN N N 126.54 . 1 551 107 ASN H H 8.81 . 1 552 107 ASN HA H 4.38 . 1 553 107 ASN HB2 H 3.02 . 1 554 107 ASN HB3 H 3.02 . 1 555 107 ASN N N 110.84 . 1 556 108 LYS H H 8.03 . 1 557 108 LYS HA H 4.78 . 1 558 108 LYS HB2 H 1.85 . 2 559 108 LYS HB3 H 1.83 . 2 560 108 LYS N N 120.24 . 1 561 109 LEU H H 9.43 . 1 562 109 LEU HA H 5.42 . 1 563 109 LEU HB2 H 1.36 . 2 564 109 LEU HB3 H 0.94 . 2 565 109 LEU HG H 1.54 . 1 566 109 LEU HD1 H 0.77 . 2 567 109 LEU HD2 H 0.73 . 2 568 109 LEU N N 121.14 . 1 569 110 GLU H H 8.76 . 1 570 110 GLU HA H 5.00 . 1 571 110 GLU HB2 H 1.99 . 1 572 110 GLU HB3 H 1.99 . 1 573 110 GLU N N 117.94 . 1 574 111 PHE H H 10.28 . 1 575 111 PHE HA H 5.23 . 1 576 111 PHE HB2 H 2.54 . 2 577 111 PHE HB3 H 2.36 . 2 578 111 PHE HD1 H 6.62 . 1 579 111 PHE HD2 H 6.62 . 1 580 111 PHE HE1 H 6.65 . 1 581 111 PHE HE2 H 6.65 . 1 582 111 PHE N N 119.64 . 1 583 112 GLU H H 8.82 . 1 584 112 GLU HA H 4.47 . 1 585 112 GLU N N 126.34 . 1 586 113 SER H H 9.14 . 1 587 113 SER HA H 3.90 . 1 588 113 SER HB2 H 4.37 . 2 589 113 SER HB3 H 4.10 . 2 590 113 SER N N 122.04 . 1 591 114 ALA H H 8.12 . 1 592 114 ALA HA H 4.05 . 1 593 114 ALA HB H 1.17 . 1 594 114 ALA N N 128.64 . 1 595 115 GLN H H 7.87 . 1 596 115 GLN HA H 3.61 . 1 597 115 GLN HB2 H 1.42 . 2 598 115 GLN HB3 H 0.98 . 2 599 115 GLN N N 117.04 . 1 600 116 PHE H H 7.38 . 1 601 116 PHE HA H 4.86 . 1 602 116 PHE HB2 H 2.64 . 2 603 116 PHE HB3 H 2.58 . 2 604 116 PHE HD1 H 6.91 . 1 605 116 PHE HD2 H 6.91 . 1 606 116 PHE HE1 H 6.81 . 1 607 116 PHE HE2 H 6.81 . 1 608 116 PHE N N 117.04 . 1 609 117 PRO HA H 4.40 . 1 610 117 PRO HB2 H 2.29 . 1 611 117 PRO HB3 H 2.29 . 1 612 117 PRO HG2 H 3.54 . 2 613 117 PRO HG3 H 3.31 . 2 614 117 PRO HD2 H 2.00 . 2 615 117 PRO HD3 H 1.87 . 2 616 118 ASN H H 10.23 . 1 617 118 ASN HA H 4.04 . 1 618 118 ASN HB2 H 3.37 . 2 619 118 ASN HB3 H 3.03 . 2 620 118 ASN N N 114.24 . 1 621 119 TRP H H 8.11 . 1 622 119 TRP HA H 4.98 . 1 623 119 TRP HB2 H 3.67 . 2 624 119 TRP HB3 H 2.92 . 2 625 119 TRP HD1 H 7.30 . 1 626 119 TRP HE1 H 10.01 . 1 627 119 TRP HE3 H 7.10 . 1 628 119 TRP HZ2 H 7.45 . 1 629 119 TRP HZ3 H 7.21 . 1 630 119 TRP HH2 H 7.21 . 1 631 119 TRP N N 119.84 . 1 632 120 TYR H H 9.40 . 1 633 120 TYR HA H 5.64 . 1 634 120 TYR HB2 H 3.50 . 2 635 120 TYR HB3 H 2.41 . 2 636 120 TYR HD1 H 7.01 . 1 637 120 TYR HD2 H 7.01 . 1 638 120 TYR HE1 H 6.63 . 1 639 120 TYR HE2 H 6.63 . 1 640 120 TYR N N 119.54 . 1 641 121 ILE H H 8.65 . 1 642 121 ILE HA H 3.84 . 1 643 121 ILE HB H 1.62 . 1 644 121 ILE HG2 H 0.41 . 1 645 121 ILE N N 124.74 . 1 646 122 SER H H 8.98 . 1 647 122 SER HA H 5.82 . 1 648 122 SER HB2 H 3.00 . 2 649 122 SER HB3 H 2.06 . 2 650 122 SER N N 122.64 . 1 651 123 THR H H 8.99 . 1 652 123 THR HA H 4.83 . 1 653 123 THR HB H 4.39 . 1 654 123 THR HG2 H 1.16 . 1 655 123 THR N N 110.04 . 1 656 124 SER H H 9.55 . 1 657 124 SER HA H 4.97 . 1 658 124 SER HB2 H 3.98 . 2 659 124 SER HB3 H 3.93 . 2 660 124 SER N N 113.94 . 1 661 125 GLN H H 8.87 . 1 662 125 GLN HA H 3.98 . 1 663 125 GLN HB2 H 2.24 . 2 664 125 GLN HB3 H 2.01 . 2 665 125 GLN HG2 H 2.63 . 2 666 125 GLN HG3 H 2.38 . 2 667 125 GLN N N 122.24 . 1 668 126 ALA H H 8.17 . 1 669 126 ALA HA H 4.38 . 1 670 126 ALA HB H 1.44 . 1 671 126 ALA N N 120.14 . 1 672 127 GLU H H 8.44 . 1 673 127 GLU HA H 4.04 . 1 674 127 GLU HB2 H 2.27 . 2 675 127 GLU HB3 H 1.96 . 2 676 127 GLU N N 117.34 . 1 677 128 ASN H H 8.06 . 1 678 128 ASN HA H 4.18 . 1 679 128 ASN HB2 H 3.31 . 2 680 128 ASN HB3 H 2.55 . 2 681 128 ASN N N 114.24 . 1 682 129 MET H H 8.84 . 1 683 129 MET HA H 5.23 . 1 684 129 MET HB2 H 2.36 . 2 685 129 MET HB3 H 2.15 . 2 686 129 MET N N 117.84 . 1 687 130 PRO HA H 5.20 . 1 688 130 PRO HD2 H 3.94 . 2 689 130 PRO HD3 H 3.78 . 2 690 131 VAL H H 8.01 . 1 691 131 VAL HA H 4.42 . 1 692 131 VAL HB H 1.75 . 1 693 131 VAL HG1 H 0.86 . 1 694 131 VAL HG2 H 0.86 . 1 695 131 VAL N N 125.54 . 1 696 132 PHE H H 8.65 . 1 697 132 PHE HA H 5.27 . 1 698 132 PHE HB2 H 3.30 . 2 699 132 PHE HB3 H 2.97 . 2 700 132 PHE HD1 H 7.31 . 1 701 132 PHE HD2 H 7.31 . 1 702 132 PHE HE1 H 7.23 . 1 703 132 PHE HE2 H 7.23 . 1 704 132 PHE HZ H 7.13 . 1 705 132 PHE N N 124.74 . 1 706 133 LEU H H 8.58 . 1 707 133 LEU HA H 5.21 . 1 708 133 LEU N N 119.84 . 1 709 134 GLY H H 9.34 . 1 710 134 GLY HA2 H 4.92 . 2 711 134 GLY HA3 H 4.02 . 2 712 134 GLY N N 115.04 . 1 713 135 GLY H H 8.75 . 1 714 135 GLY HA2 H 3.84 . 2 715 135 GLY HA3 H 2.93 . 2 716 135 GLY N N 111.34 . 1 717 136 THR H H 7.46 . 1 718 136 THR HA H 4.31 . 1 719 136 THR HB H 3.99 . 1 720 136 THR HG2 H 0.96 . 1 721 136 THR N N 112.24 . 1 722 137 LYS H H 8.37 . 1 723 137 LYS HA H 4.29 . 1 724 137 LYS HB2 H 1.56 . 2 725 137 LYS HB3 H 1.53 . 2 726 137 LYS N N 124.54 . 1 727 138 GLY H H 8.63 . 1 728 138 GLY HA2 H 4.02 . 2 729 138 GLY HA3 H 3.83 . 2 730 138 GLY N N 111.64 . 1 731 139 GLY H H 8.15 . 1 732 139 GLY HA2 H 4.20 . 2 733 139 GLY HA3 H 3.78 . 2 734 139 GLY N N 109.14 . 1 735 140 GLN H H 8.40 . 1 736 140 GLN HA H 4.29 . 1 737 140 GLN HB2 H 2.20 . 2 738 140 GLN HB3 H 2.00 . 2 739 140 GLN N N 119.84 . 1 740 141 ASP H H 7.79 . 1 741 141 ASP HA H 4.93 . 1 742 141 ASP HB2 H 2.82 . 2 743 141 ASP HB3 H 2.57 . 2 744 141 ASP N N 119.74 . 1 745 142 ILE H H 9.18 . 1 746 142 ILE HA H 3.92 . 1 747 142 ILE HB H 2.41 . 1 748 142 ILE HG2 H 0.78 . 1 749 142 ILE N N 125.64 . 1 750 143 THR H H 8.12 . 1 751 143 THR HA H 4.99 . 1 752 143 THR HB H 4.39 . 1 753 143 THR HG2 H 0.96 . 1 754 143 THR N N 111.94 . 1 755 144 ASP H H 7.10 . 1 756 144 ASP HA H 5.58 . 1 757 144 ASP HB2 H 2.54 . 2 758 144 ASP HB3 H 2.42 . 2 759 144 ASP N N 120.74 . 1 760 145 PHE H H 9.55 . 1 761 145 PHE HA H 5.22 . 1 762 145 PHE HB2 H 3.09 . 2 763 145 PHE HB3 H 2.63 . 2 764 145 PHE HD1 H 7.01 . 1 765 145 PHE HD2 H 7.01 . 1 766 145 PHE HE1 H 7.11 . 1 767 145 PHE HE2 H 7.11 . 1 768 145 PHE HZ H 6.81 . 1 769 145 PHE N N 118.14 . 1 770 146 THR H H 9.47 . 1 771 146 THR HA H 4.74 . 1 772 146 THR HB H 4.19 . 1 773 146 THR HG2 H 1.22 . 1 774 146 THR N N 110.14 . 1 775 147 MET H H 8.67 . 1 776 147 MET HA H 5.39 . 1 777 147 MET HB2 H 1.78 . 1 778 147 MET HB3 H 1.78 . 1 779 147 MET N N 121.44 . 1 780 148 GLN H H 8.43 . 1 781 148 GLN HA H 4.63 . 1 782 148 GLN HB2 H 2.07 . 1 783 148 GLN HB3 H 2.07 . 1 784 148 GLN N N 123.84 . 1 785 149 PHE H H 8.72 . 1 786 149 PHE HA H 4.77 . 1 787 149 PHE HB2 H 3.26 . 2 788 149 PHE HB3 H 3.03 . 2 789 149 PHE HD1 H 7.33 . 1 790 149 PHE HD2 H 7.33 . 1 791 149 PHE HE1 H 7.39 . 1 792 149 PHE HE2 H 7.39 . 1 793 149 PHE N N 123.84 . 1 794 150 VAL H H 8.05 . 1 795 150 VAL HA H 4.36 . 1 796 150 VAL HB H 1.84 . 1 797 150 VAL HG1 H 0.95 . 2 798 150 VAL HG2 H 0.90 . 2 799 150 VAL N N 122.74 . 1 800 151 SER H H 8.39 . 1 801 151 SER HA H 4.48 . 1 802 151 SER HB2 H 3.94 . 1 803 151 SER HB3 H 3.94 . 1 804 151 SER N N 119.54 . 1 805 152 SER H H 7.98 . 1 806 152 SER HA H 4.31 . 1 807 152 SER HB2 H 3.89 . 1 808 152 SER HB3 H 3.89 . 1 809 152 SER N N 122.64 . 1 stop_ save_